HEADER TRANSCRIPTION/RNA/DNA 24-JUN-18 6A5L
TITLE RNA POLYMERASE II ELONGATION COMPLEX STALLED AT SHL(-1) OF THE
TITLE 2 NUCLEOSOME, WITH FOREIGN DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.6;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: DNA-DIRECTED RNA POLYMERASE SUBUNIT RPB;
COMPND 9 EC: 2.7.7.6;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: RNA POLYMERASE II THIRD LARGEST SUBUNIT B44, PART OF
COMPND 12 CENTRAL CORE;
COMPND 13 CHAIN: C;
COMPND 14 SYNONYM: RNA POLYMERASE II THIRD LARGEST SUBUNIT RPB3;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: RNA POLYMERASE II SUBUNIT B32;
COMPND 17 CHAIN: D;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: RNA POLYMERASE SUBUNIT ABC27, COMMON TO RNA POLYMERASES I,
COMPND 20 II, AND III;
COMPND 21 CHAIN: E;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: RNA POLYMERASE SUBUNIT ABC23, COMMON TO RNA POLYMERASES I,
COMPND 24 II, AND III;
COMPND 25 CHAIN: F;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: RNA POLYMERASE II SUBUNIT;
COMPND 28 CHAIN: G;
COMPND 29 SYNONYM: RNA POLYMERASE II SUBUNIT RPB7;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND 32 CHAIN: H;
COMPND 33 SYNONYM: RNA POLYMERASE SUBUNIT ABC14.5, COMMON TO RNA POLYMERASES I,
COMPND 34 II, AND III;
COMPND 35 MOL_ID: 9;
COMPND 36 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT;
COMPND 37 CHAIN: I;
COMPND 38 SYNONYM: DNA-DIRECTED RNA POLYMERASE SUBUNIT, RPB9;
COMPND 39 MOL_ID: 10;
COMPND 40 MOLECULE: RNA POLYMERASE SUBUNIT ABC10-BETA, COMMON TO RNA
COMPND 41 POLYMERASES I, II, AND III;
COMPND 42 CHAIN: J;
COMPND 43 MOL_ID: 11;
COMPND 44 MOLECULE: RNA POLYMERASE II SUBUNIT B12.5;
COMPND 45 CHAIN: K;
COMPND 46 MOL_ID: 12;
COMPND 47 MOLECULE: RNA POLYMERASE SUBUNIT ABC10-ALPHA;
COMPND 48 CHAIN: L;
COMPND 49 MOL_ID: 13;
COMPND 50 MOLECULE: RNA (5'-R(P*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*G)-3');
COMPND 51 CHAIN: P;
COMPND 52 ENGINEERED: YES;
COMPND 53 MOL_ID: 14;
COMPND 54 MOLECULE: DNA (198-MER);
COMPND 55 CHAIN: T;
COMPND 56 ENGINEERED: YES;
COMPND 57 MOL_ID: 15;
COMPND 58 MOLECULE: DNA (198-MER);
COMPND 59 CHAIN: N;
COMPND 60 ENGINEERED: YES;
COMPND 61 MOL_ID: 16;
COMPND 62 MOLECULE: HISTONE H3.3;
COMPND 63 CHAIN: a, e;
COMPND 64 ENGINEERED: YES;
COMPND 65 MOL_ID: 17;
COMPND 66 MOLECULE: HISTONE H4;
COMPND 67 CHAIN: b, f;
COMPND 68 ENGINEERED: YES;
COMPND 69 MOL_ID: 18;
COMPND 70 MOLECULE: HISTONE H2A TYPE 1-B/E;
COMPND 71 CHAIN: c, g;
COMPND 72 SYNONYM: HISTONE H2A.2,HISTONE H2A/A,HISTONE H2A/M;
COMPND 73 ENGINEERED: YES;
COMPND 74 MOL_ID: 19;
COMPND 75 MOLECULE: HISTONE H2B TYPE 1-J;
COMPND 76 CHAIN: d, h;
COMPND 77 SYNONYM: HISTONE H2B.1,HISTONE H2B.R,H2B/R;
COMPND 78 ENGINEERED: YES;
COMPND 79 MOL_ID: 20;
COMPND 80 MOLECULE: DNA (42-MER);
COMPND 81 CHAIN: 0;
COMPND 82 ENGINEERED: YES;
COMPND 83 MOL_ID: 21;
COMPND 84 MOLECULE: DNA (42-MER);
COMPND 85 CHAIN: 1;
COMPND 86 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 3 20864);
SOURCE 4 ORGANISM_COMMON: YEAST;
SOURCE 5 ORGANISM_TAXID: 644223;
SOURCE 6 STRAIN: GS115 / ATCC 20864;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 9 20864);
SOURCE 10 ORGANISM_COMMON: YEAST;
SOURCE 11 ORGANISM_TAXID: 644223;
SOURCE 12 STRAIN: GS115 / ATCC 20864;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 15 20864);
SOURCE 16 ORGANISM_COMMON: YEAST;
SOURCE 17 ORGANISM_TAXID: 644223;
SOURCE 18 STRAIN: GS115 / ATCC 20864;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 21 20864);
SOURCE 22 ORGANISM_COMMON: YEAST;
SOURCE 23 ORGANISM_TAXID: 644223;
SOURCE 24 STRAIN: GS115 / ATCC 20864;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 27 20864);
SOURCE 28 ORGANISM_COMMON: YEAST;
SOURCE 29 ORGANISM_TAXID: 644223;
SOURCE 30 STRAIN: GS115 / ATCC 20864;
SOURCE 31 MOL_ID: 6;
SOURCE 32 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 33 20864);
SOURCE 34 ORGANISM_COMMON: YEAST;
SOURCE 35 ORGANISM_TAXID: 644223;
SOURCE 36 STRAIN: GS115 / ATCC 20864;
SOURCE 37 MOL_ID: 7;
SOURCE 38 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 39 20864);
SOURCE 40 ORGANISM_COMMON: YEAST;
SOURCE 41 ORGANISM_TAXID: 644223;
SOURCE 42 STRAIN: GS115 / ATCC 20864;
SOURCE 43 MOL_ID: 8;
SOURCE 44 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 45 20864);
SOURCE 46 ORGANISM_COMMON: YEAST;
SOURCE 47 ORGANISM_TAXID: 644223;
SOURCE 48 STRAIN: GS115 / ATCC 20864;
SOURCE 49 MOL_ID: 9;
SOURCE 50 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 51 20864);
SOURCE 52 ORGANISM_COMMON: YEAST;
SOURCE 53 ORGANISM_TAXID: 644223;
SOURCE 54 STRAIN: GS115 / ATCC 20864;
SOURCE 55 MOL_ID: 10;
SOURCE 56 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 57 20864);
SOURCE 58 ORGANISM_COMMON: YEAST;
SOURCE 59 ORGANISM_TAXID: 644223;
SOURCE 60 STRAIN: GS115 / ATCC 20864;
SOURCE 61 MOL_ID: 11;
SOURCE 62 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 63 20864);
SOURCE 64 ORGANISM_COMMON: YEAST;
SOURCE 65 ORGANISM_TAXID: 644223;
SOURCE 66 STRAIN: GS115 / ATCC 20864;
SOURCE 67 MOL_ID: 12;
SOURCE 68 ORGANISM_SCIENTIFIC: KOMAGATAELLA PHAFFII (STRAIN GS115 / ATCC
SOURCE 69 20864);
SOURCE 70 ORGANISM_COMMON: YEAST;
SOURCE 71 ORGANISM_TAXID: 644223;
SOURCE 72 STRAIN: GS115 / ATCC 20864;
SOURCE 73 MOL_ID: 13;
SOURCE 74 SYNTHETIC: YES;
SOURCE 75 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 76 ORGANISM_TAXID: 32630;
SOURCE 77 OTHER_DETAILS: PRODUCED BY IN VITRO TRANSCRIPTION;
SOURCE 78 MOL_ID: 14;
SOURCE 79 SYNTHETIC: YES;
SOURCE 80 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 81 ORGANISM_TAXID: 32630;
SOURCE 82 MOL_ID: 15;
SOURCE 83 SYNTHETIC: YES;
SOURCE 84 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 85 ORGANISM_TAXID: 32630;
SOURCE 86 MOL_ID: 16;
SOURCE 87 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 88 ORGANISM_COMMON: HUMAN;
SOURCE 89 ORGANISM_TAXID: 9606;
SOURCE 90 GENE: H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B;
SOURCE 91 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 92 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 93 MOL_ID: 17;
SOURCE 94 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 95 ORGANISM_COMMON: HUMAN;
SOURCE 96 ORGANISM_TAXID: 9606;
SOURCE 97 GENE: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G,
SOURCE 98 H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C,
SOURCE 99 H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E,
SOURCE 100 H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N,
SOURCE 101 H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4;
SOURCE 102 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 103 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 104 MOL_ID: 18;
SOURCE 105 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 106 ORGANISM_COMMON: HUMAN;
SOURCE 107 ORGANISM_TAXID: 9606;
SOURCE 108 GENE: HIST1H2AB, H2AFM, HIST1H2AE, H2AFA;
SOURCE 109 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 110 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 111 MOL_ID: 19;
SOURCE 112 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 113 ORGANISM_COMMON: HUMAN;
SOURCE 114 ORGANISM_TAXID: 9606;
SOURCE 115 GENE: HIST1H2BJ, H2BFR;
SOURCE 116 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 117 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 118 MOL_ID: 20;
SOURCE 119 SYNTHETIC: YES;
SOURCE 120 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 121 ORGANISM_TAXID: 32630;
SOURCE 122 MOL_ID: 21;
SOURCE 123 SYNTHETIC: YES;
SOURCE 124 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 125 ORGANISM_TAXID: 32630
KEYWDS NUCLEOSOME, CHROMATIN, RNA POLYMERASE, TRANSCRIPTION, TRANSCRIPTION-
KEYWDS 2 RNA-DNA COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR T.KUJIRAI,H.EHARA,Y.FUJINO,M.SHIROUZU,S.SEKINE,H.KURUMIZAKA
REVDAT 5 27-MAR-24 6A5L 1 LINK
REVDAT 4 06-NOV-19 6A5L 1 CRYST1
REVDAT 3 14-NOV-18 6A5L 1 JRNL
REVDAT 2 24-OCT-18 6A5L 1 JRNL
REVDAT 1 03-OCT-18 6A5L 0
JRNL AUTH T.KUJIRAI,H.EHARA,Y.FUJINO,M.SHIROUZU,S.I.SEKINE,
JRNL AUTH 2 H.KURUMIZAKA
JRNL TITL STRUCTURAL BASIS OF THE NUCLEOSOME TRANSITION DURING RNA
JRNL TITL 2 POLYMERASE II PASSAGE.
JRNL REF SCIENCE V. 362 595 2018
JRNL REFN ESSN 1095-9203
JRNL PMID 30287617
JRNL DOI 10.1126/SCIENCE.AAU9904
REMARK 2
REMARK 2 RESOLUTION. 5.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SERIALEM, GCTF, UCSF CHIMERA, PHENIX,
REMARK 3 COOT, RELION, RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 5.600
REMARK 3 NUMBER OF PARTICLES : 73183
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6A5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008185.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : RNA POLYMERASE II ELONGATION
REMARK 245 COMPLEX STALLED AT SHL(-1) OF
REMARK 245 THE NUCLEOSOME, WITH FOREIGN DNA
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: 25-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, P, T, N, a, b, c, d,
REMARK 350 AND CHAINS: e, f, g, h, 0, 1
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 154
REMARK 465 ASP A 155
REMARK 465 GLU A 156
REMARK 465 TYR A 157
REMARK 465 SER A 158
REMARK 465 GLU A 159
REMARK 465 GLN A 160
REMARK 465 GLY A 190
REMARK 465 PHE A 191
REMARK 465 SER A 192
REMARK 465 ASP A 193
REMARK 465 THR A 1082
REMARK 465 LEU A 1083
REMARK 465 ASN A 1084
REMARK 465 THR A 1085
REMARK 465 PHE A 1086
REMARK 465 HIS A 1087
REMARK 465 TYR A 1088
REMARK 465 ALA A 1089
REMARK 465 GLY A 1090
REMARK 465 VAL A 1091
REMARK 465 SER A 1092
REMARK 465 SER A 1093
REMARK 465 LYS A 1094
REMARK 465 ILE A 1178
REMARK 465 PRO A 1179
REMARK 465 ASP A 1180
REMARK 465 GLU A 1181
REMARK 465 LYS A 1182
REMARK 465 VAL A 1183
REMARK 465 GLU A 1184
REMARK 465 GLU A 1185
REMARK 465 THR A 1186
REMARK 465 ILE A 1187
REMARK 465 ASP A 1188
REMARK 465 LYS A 1189
REMARK 465 ARG A 1246
REMARK 465 ASP A 1247
REMARK 465 PRO A 1248
REMARK 465 LYS A 1249
REMARK 465 ALA A 1250
REMARK 465 MET A 1251
REMARK 465 ASP A 1252
REMARK 465 GLU A 1253
REMARK 465 GLU A 1254
REMARK 465 LEU A 1255
REMARK 465 GLU A 1256
REMARK 465 ALA A 1257
REMARK 465 ALA A 1458
REMARK 465 ASP A 1459
REMARK 465 TYR A 1460
REMARK 465 ALA A 1461
REMARK 465 PRO A 1462
REMARK 465 THR A 1463
REMARK 465 MET A 1464
REMARK 465 PRO A 1465
REMARK 465 LEU A 1466
REMARK 465 PHE A 1467
REMARK 465 LYS A 1468
REMARK 465 GLY A 1469
REMARK 465 LYS A 1470
REMARK 465 ALA A 1471
REMARK 465 THR A 1472
REMARK 465 GLN A 1473
REMARK 465 GLY A 1474
REMARK 465 SER A 1475
REMARK 465 ALA A 1476
REMARK 465 THR A 1477
REMARK 465 PRO A 1478
REMARK 465 TYR A 1479
REMARK 465 ASP A 1480
REMARK 465 ASN A 1481
REMARK 465 ASN A 1482
REMARK 465 ALA A 1483
REMARK 465 GLN A 1484
REMARK 465 TYR A 1485
REMARK 465 ASP A 1486
REMARK 465 ASP A 1487
REMARK 465 GLU A 1488
REMARK 465 PHE A 1489
REMARK 465 ASN A 1490
REMARK 465 HIS A 1491
REMARK 465 ASP A 1492
REMARK 465 ASP A 1493
REMARK 465 VAL A 1494
REMARK 465 ALA A 1495
REMARK 465 ASP A 1496
REMARK 465 VAL A 1497
REMARK 465 MET A 1498
REMARK 465 PHE A 1499
REMARK 465 SER A 1500
REMARK 465 PRO A 1501
REMARK 465 MET A 1502
REMARK 465 ALA A 1503
REMARK 465 GLU A 1504
REMARK 465 THR A 1505
REMARK 465 GLY A 1506
REMARK 465 SER A 1507
REMARK 465 GLY A 1508
REMARK 465 ASP A 1509
REMARK 465 ASP A 1510
REMARK 465 ARG A 1511
REMARK 465 SER A 1512
REMARK 465 GLY A 1513
REMARK 465 GLY A 1514
REMARK 465 LEU A 1515
REMARK 465 THR A 1516
REMARK 465 GLU A 1517
REMARK 465 TYR A 1518
REMARK 465 ALA A 1519
REMARK 465 GLY A 1520
REMARK 465 ILE A 1521
REMARK 465 GLN A 1522
REMARK 465 SER A 1523
REMARK 465 PRO A 1524
REMARK 465 TYR A 1525
REMARK 465 GLN A 1526
REMARK 465 PRO A 1527
REMARK 465 THR A 1528
REMARK 465 SER A 1529
REMARK 465 PRO A 1530
REMARK 465 GLY A 1531
REMARK 465 LEU A 1532
REMARK 465 SER A 1533
REMARK 465 ALA A 1534
REMARK 465 THR A 1535
REMARK 465 SER A 1536
REMARK 465 PRO A 1537
REMARK 465 GLY A 1538
REMARK 465 PHE A 1539
REMARK 465 ALA A 1540
REMARK 465 PRO A 1541
REMARK 465 THR A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 GLY A 1545
REMARK 465 PHE A 1546
REMARK 465 ALA A 1547
REMARK 465 PRO A 1548
REMARK 465 THR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 ARG A 1552
REMARK 465 TYR A 1553
REMARK 465 SER A 1554
REMARK 465 PRO A 1555
REMARK 465 THR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 GLY A 1559
REMARK 465 TYR A 1560
REMARK 465 SER A 1561
REMARK 465 PRO A 1562
REMARK 465 THR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 SER A 1566
REMARK 465 TYR A 1567
REMARK 465 SER A 1568
REMARK 465 PRO A 1569
REMARK 465 THR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 SER A 1573
REMARK 465 TYR A 1574
REMARK 465 SER A 1575
REMARK 465 PRO A 1576
REMARK 465 THR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 SER A 1580
REMARK 465 TYR A 1581
REMARK 465 SER A 1582
REMARK 465 PRO A 1583
REMARK 465 THR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 SER A 1587
REMARK 465 TYR A 1588
REMARK 465 SER A 1589
REMARK 465 PRO A 1590
REMARK 465 THR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 SER A 1594
REMARK 465 TYR A 1595
REMARK 465 SER A 1596
REMARK 465 PRO A 1597
REMARK 465 THR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 SER A 1601
REMARK 465 TYR A 1602
REMARK 465 SER A 1603
REMARK 465 PRO A 1604
REMARK 465 THR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 SER A 1608
REMARK 465 TYR A 1609
REMARK 465 SER A 1610
REMARK 465 PRO A 1611
REMARK 465 THR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 SER A 1615
REMARK 465 TYR A 1616
REMARK 465 SER A 1617
REMARK 465 PRO A 1618
REMARK 465 THR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 SER A 1622
REMARK 465 TYR A 1623
REMARK 465 SER A 1624
REMARK 465 PRO A 1625
REMARK 465 THR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 GLN A 1629
REMARK 465 TYR A 1630
REMARK 465 SER A 1631
REMARK 465 PRO A 1632
REMARK 465 THR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 GLN A 1636
REMARK 465 TYR A 1637
REMARK 465 SER A 1638
REMARK 465 PRO A 1639
REMARK 465 THR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 GLN A 1643
REMARK 465 TYR A 1644
REMARK 465 SER A 1645
REMARK 465 PRO A 1646
REMARK 465 THR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 GLN A 1650
REMARK 465 TYR A 1651
REMARK 465 SER A 1652
REMARK 465 PRO A 1653
REMARK 465 THR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 GLN A 1657
REMARK 465 TYR A 1658
REMARK 465 SER A 1659
REMARK 465 PRO A 1660
REMARK 465 THR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 GLN A 1664
REMARK 465 TYR A 1665
REMARK 465 SER A 1666
REMARK 465 PRO A 1667
REMARK 465 THR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 GLN A 1671
REMARK 465 TYR A 1672
REMARK 465 SER A 1673
REMARK 465 PRO A 1674
REMARK 465 THR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 GLN A 1678
REMARK 465 TYR A 1679
REMARK 465 SER A 1680
REMARK 465 PRO A 1681
REMARK 465 THR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 GLN A 1685
REMARK 465 TYR A 1686
REMARK 465 SER A 1687
REMARK 465 PRO A 1688
REMARK 465 THR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 GLN A 1692
REMARK 465 TYR A 1693
REMARK 465 SER A 1694
REMARK 465 PRO A 1695
REMARK 465 THR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 GLN A 1699
REMARK 465 TYR A 1700
REMARK 465 SER A 1701
REMARK 465 PRO A 1702
REMARK 465 THR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 GLN A 1706
REMARK 465 TYR A 1707
REMARK 465 SER A 1708
REMARK 465 PRO A 1709
REMARK 465 THR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLN A 1713
REMARK 465 TYR A 1714
REMARK 465 SER A 1715
REMARK 465 PRO A 1716
REMARK 465 THR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 GLN A 1720
REMARK 465 TYR A 1721
REMARK 465 SER A 1722
REMARK 465 PRO A 1723
REMARK 465 ALA A 1724
REMARK 465 SER A 1725
REMARK 465 PRO A 1726
REMARK 465 GLN A 1727
REMARK 465 TYR A 1728
REMARK 465 SER A 1729
REMARK 465 PRO A 1730
REMARK 465 SER A 1731
REMARK 465 ARG A 1732
REMARK 465 HIS A 1733
REMARK 465 SER A 1734
REMARK 465 PRO A 1735
REMARK 465 ASN A 1736
REMARK 465 GLY A 1737
REMARK 465 GLU A 1738
REMARK 465 SER A 1739
REMARK 465 LYS A 1740
REMARK 465 GLU A 1741
REMARK 465 GLY A 1742
REMARK 465 GLU A 1743
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 TYR B 3
REMARK 465 ASP B 4
REMARK 465 PRO B 5
REMARK 465 TYR B 6
REMARK 465 SER B 7
REMARK 465 ILE B 8
REMARK 465 ASP B 129
REMARK 465 GLU B 130
REMARK 465 GLY B 131
REMARK 465 ASN B 132
REMARK 465 PRO B 133
REMARK 465 ASN B 134
REMARK 465 ALA B 135
REMARK 465 THR B 136
REMARK 465 LEU B 137
REMARK 465 ASP B 138
REMARK 465 TRP B 139
REMARK 465 GLN B 140
REMARK 465 GLN B 141
REMARK 465 VAL B 142
REMARK 465 HIS B 143
REMARK 465 GLU B 144
REMARK 465 PRO B 145
REMARK 465 ILE B 146
REMARK 465 LYS B 147
REMARK 465 ASP B 148
REMARK 465 GLY B 149
REMARK 465 VAL B 150
REMARK 465 GLU B 151
REMARK 465 GLU B 152
REMARK 465 ALA B 663
REMARK 465 MET B 664
REMARK 465 ASN B 665
REMARK 465 ASP B 666
REMARK 465 ASP B 667
REMARK 465 SER B 668
REMARK 465 GLU B 669
REMARK 465 GLU B 670
REMARK 465 GLN B 671
REMARK 465 GLU B 672
REMARK 465 GLN B 673
REMARK 465 ASP B 674
REMARK 465 LEU B 712
REMARK 465 GLU B 713
REMARK 465 GLN B 714
REMARK 465 LYS B 715
REMARK 465 GLU B 716
REMARK 465 ILE B 717
REMARK 465 ASP B 718
REMARK 465 ASP B 921
REMARK 465 THR 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 LYS B 930
REMARK 465 VAL B 1223
REMARK 465 SER B 1224
REMARK 465 MET B 1225
REMARK 465 ARG B 1226
REMARK 465 SER B 1227
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 PRO C 267
REMARK 465 ALA C 268
REMARK 465 ASN C 269
REMARK 465 THR C 270
REMARK 465 THR C 271
REMARK 465 ALA C 272
REMARK 465 TYR C 273
REMARK 465 GLY C 274
REMARK 465 GLY C 275
REMARK 465 ALA C 276
REMARK 465 THR C 277
REMARK 465 ALA C 278
REMARK 465 TYR C 279
REMARK 465 GLY C 280
REMARK 465 GLY C 281
REMARK 465 GLN C 282
REMARK 465 THR C 283
REMARK 465 VAL C 284
REMARK 465 TYR C 285
REMARK 465 GLY C 286
REMARK 465 ARG C 287
REMARK 465 GLU C 288
REMARK 465 THR C 289
REMARK 465 SER C 290
REMARK 465 TYR C 291
REMARK 465 GLY C 292
REMARK 465 GLY C 293
REMARK 465 ASN C 294
REMARK 465 THR C 295
REMARK 465 ASN C 296
REMARK 465 TYR C 297
REMARK 465 GLY C 298
REMARK 465 ASP C 299
REMARK 465 TYR C 300
REMARK 465 ASN C 301
REMARK 465 ALA C 302
REMARK 465 PRO C 303
REMARK 465 TYR C 304
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 ALA D 10
REMARK 465 ARG D 11
REMARK 465 ARG D 12
REMARK 465 ARG D 13
REMARK 465 ARG D 14
REMARK 465 ALA D 15
REMARK 465 LYS D 16
REMARK 465 GLN D 17
REMARK 465 GLN D 18
REMARK 465 VAL D 19
REMARK 465 ASP D 20
REMARK 465 ASP D 21
REMARK 465 ASP D 76
REMARK 465 ILE D 77
REMARK 465 GLU D 78
REMARK 465 SER D 79
REMARK 465 SER D 80
REMARK 465 ASN D 81
REMARK 465 GLY D 82
REMARK 465 GLU D 83
REMARK 465 ASN D 130
REMARK 465 SER D 131
REMARK 465 SER D 132
REMARK 465 ASP D 133
REMARK 465 CYS D 134
REMARK 465 SER D 135
REMARK 465 VAL D 136
REMARK 465 LYS D 186
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 GLU F 3
REMARK 465 ASP F 4
REMARK 465 GLU F 5
REMARK 465 ALA F 6
REMARK 465 PHE F 7
REMARK 465 ASN F 8
REMARK 465 GLU F 9
REMARK 465 GLN F 10
REMARK 465 THR F 11
REMARK 465 GLU F 12
REMARK 465 ASN F 13
REMARK 465 PHE F 14
REMARK 465 GLU F 15
REMARK 465 ASN F 16
REMARK 465 PHE F 17
REMARK 465 GLU F 18
REMARK 465 ASP F 19
REMARK 465 GLU F 20
REMARK 465 HIS F 21
REMARK 465 PHE F 22
REMARK 465 SER F 23
REMARK 465 ASP F 24
REMARK 465 ASP F 25
REMARK 465 ASN F 26
REMARK 465 PHE F 27
REMARK 465 GLU F 28
REMARK 465 ASP F 29
REMARK 465 ARG F 30
REMARK 465 SER F 31
REMARK 465 THR F 32
REMARK 465 GLN F 33
REMARK 465 PRO F 34
REMARK 465 GLU F 35
REMARK 465 ASP F 36
REMARK 465 TYR F 37
REMARK 465 ALA F 38
REMARK 465 VAL F 39
REMARK 465 GLY F 40
REMARK 465 VAL F 41
REMARK 465 THR F 42
REMARK 465 ALA F 43
REMARK 465 ASP F 44
REMARK 465 GLY F 45
REMARK 465 ARG F 46
REMARK 465 GLN F 47
REMARK 465 ILE F 48
REMARK 465 ILE F 49
REMARK 465 ASN F 50
REMARK 465 GLY F 51
REMARK 465 ASP F 52
REMARK 465 GLY F 53
REMARK 465 ILE F 54
REMARK 465 GLN F 55
REMARK 465 GLU F 56
REMARK 465 VAL F 57
REMARK 465 ASN F 58
REMARK 465 GLY F 59
REMARK 465 THR F 60
REMARK 465 ILE F 61
REMARK 465 LYS F 62
REMARK 465 ALA F 63
REMARK 465 HIS F 64
REMARK 465 ARG F 65
REMARK 465 LYS F 66
REMARK 465 ARG F 67
REMARK 465 SER F 68
REMARK 465 ASN F 69
REMARK 465 LYS F 70
REMARK 465 ASN F 155
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 ASP H 66
REMARK 465 GLY H 67
REMARK 465 GLU H 68
REMARK 465 ASP H 69
REMARK 465 GLU H 70
REMARK 465 SER H 71
REMARK 465 ALA H 72
REMARK 465 ASN H 73
REMARK 465 PHE H 74
REMARK 465 SER H 75
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 SER I 114
REMARK 465 GLU I 115
REMARK 465 LYS J 67
REMARK 465 LYS J 68
REMARK 465 ASP J 69
REMARK 465 PHE J 70
REMARK 465 ASP J 71
REMARK 465 SER J 72
REMARK 465 PHE K 114
REMARK 465 SER K 115
REMARK 465 LEU K 116
REMARK 465 ASN K 117
REMARK 465 ASP K 118
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 VAL L 7
REMARK 465 ALA L 8
REMARK 465 PRO L 9
REMARK 465 SER L 10
REMARK 465 GLY L 11
REMARK 465 THR L 12
REMARK 465 ASP L 13
REMARK 465 LEU L 14
REMARK 465 ALA L 15
REMARK 465 ALA L 16
REMARK 465 ALA L 17
REMARK 465 ALA L 18
REMARK 465 SER L 19
REMARK 465 GLY L 20
REMARK 465 VAL L 21
REMARK 465 ALA L 22
REMARK 465 PRO L 23
REMARK 465 ASN L 24
REMARK 465 LYS L 25
REMARK 465 HIS L 26
REMARK 465 TYR L 27
REMARK 465 DG T 54
REMARK 465 DA T 55
REMARK 465 DC T 56
REMARK 465 DA T 57
REMARK 465 DG T 58
REMARK 465 DA T 59
REMARK 465 DA T 60
REMARK 465 DA T 61
REMARK 465 DA T 62
REMARK 465 DA T 63
REMARK 465 DA T 64
REMARK 465 DA T 65
REMARK 465 DC T 66
REMARK 465 DA T 67
REMARK 465 DA T 68
REMARK 465 DC T 69
REMARK 465 DG T 70
REMARK 465 DA T 71
REMARK 465 DA T 72
REMARK 465 DA T 73
REMARK 465 DA T 74
REMARK 465 DC T 75
REMARK 465 DG T 76
REMARK 465 DG T 77
REMARK 465 DC T 78
REMARK 465 DC T 79
REMARK 465 DA T 80
REMARK 465 DC T 81
REMARK 465 DC T 82
REMARK 465 DA T 83
REMARK 465 DC T 84
REMARK 465 DC T 85
REMARK 465 DC T 86
REMARK 465 DA T 87
REMARK 465 DA T 88
REMARK 465 DA T 89
REMARK 465 DC T 90
REMARK 465 DA T 91
REMARK 465 DC T 92
REMARK 465 DA T 93
REMARK 465 DC T 94
REMARK 465 DC T 95
REMARK 465 DA T 96
REMARK 465 DA T 97
REMARK 465 DA T 98
REMARK 465 DC T 99
REMARK 465 DA T 100
REMARK 465 DC T 101
REMARK 465 DA T 102
REMARK 465 DA T 103
REMARK 465 DG T 104
REMARK 465 DA T 105
REMARK 465 DG T 106
REMARK 465 DC T 107
REMARK 465 DT T 108
REMARK 465 DA T 109
REMARK 465 DA T 110
REMARK 465 DT T 111
REMARK 465 DT T 112
REMARK 465 DG T 113
REMARK 465 DA T 114
REMARK 465 DC T 115
REMARK 465 DT T 116
REMARK 465 DG T 117
REMARK 465 DA T 118
REMARK 465 DC T 119
REMARK 465 DG T 120
REMARK 465 DT T 121
REMARK 465 DA T 122
REMARK 465 DA T 123
REMARK 465 DG T 124
REMARK 465 DC T 125
REMARK 465 DG N -125
REMARK 465 DC N -124
REMARK 465 DT N -123
REMARK 465 DT N -122
REMARK 465 DA N -121
REMARK 465 DC N -120
REMARK 465 DG N -119
REMARK 465 DT N -118
REMARK 465 DC N -117
REMARK 465 DA N -116
REMARK 465 DG N -115
REMARK 465 DT N -114
REMARK 465 DC N -113
REMARK 465 DT N -112
REMARK 465 DG N -111
REMARK 465 DG N -110
REMARK 465 DC N -109
REMARK 465 DC N -108
REMARK 465 DA N -107
REMARK 465 DT N -106
REMARK 465 DC N -105
REMARK 465 DT N -104
REMARK 465 DT N -103
REMARK 465 DT N -102
REMARK 465 DG N -101
REMARK 465 DT N -100
REMARK 465 DG N -99
REMARK 465 DT N -98
REMARK 465 DT N -97
REMARK 465 DT N -96
REMARK 465 DG N -95
REMARK 465 DG N -94
REMARK 465 DT N -93
REMARK 465 DG N -92
REMARK 465 DT N -91
REMARK 465 DG N -90
REMARK 465 DT N -89
REMARK 465 DT N -88
REMARK 465 DT N -87
REMARK 465 DG N -86
REMARK 465 DG N -85
REMARK 465 DG N -84
REMARK 465 DT N -83
REMARK 465 DG N -82
REMARK 465 DG N -81
REMARK 465 DT N -80
REMARK 465 DG N -79
REMARK 465 DG N -78
REMARK 465 DC N -77
REMARK 465 DC N -76
REMARK 465 DG N -75
REMARK 465 DT N -74
REMARK 465 DT N -73
REMARK 465 DT N -72
REMARK 465 DT N -71
REMARK 465 DC N -70
REMARK 465 DG N -69
REMARK 465 DT N -68
REMARK 465 DT N -67
REMARK 465 DG N -66
REMARK 465 DT N -65
REMARK 465 DT N -64
REMARK 465 DT N -63
REMARK 465 DT N -62
REMARK 465 DT N -61
REMARK 465 DT N -60
REMARK 465 DT N -59
REMARK 465 DC N -58
REMARK 465 DT N -57
REMARK 465 DG N -56
REMARK 465 DT N -55
REMARK 465 DC N -54
REMARK 465 DT N -41
REMARK 465 DC N -40
REMARK 465 DT N -39
REMARK 465 DT N -38
REMARK 465 DG N -37
REMARK 465 DG N -36
REMARK 465 DG N -35
REMARK 465 DT N -34
REMARK 465 DG N -33
REMARK 465 GLY a -3
REMARK 465 SER a -2
REMARK 465 HIS a -1
REMARK 465 MET a 0
REMARK 465 ALA a 1
REMARK 465 ARG a 2
REMARK 465 THR a 3
REMARK 465 LYS a 4
REMARK 465 GLN a 5
REMARK 465 THR a 6
REMARK 465 ALA a 7
REMARK 465 ARG a 8
REMARK 465 LYS a 9
REMARK 465 SER a 10
REMARK 465 THR a 11
REMARK 465 GLY a 12
REMARK 465 GLY a 13
REMARK 465 LYS a 14
REMARK 465 ALA a 15
REMARK 465 PRO a 16
REMARK 465 ARG a 17
REMARK 465 LYS a 18
REMARK 465 GLN a 19
REMARK 465 LEU a 20
REMARK 465 ALA a 21
REMARK 465 THR a 22
REMARK 465 LYS a 23
REMARK 465 ALA a 24
REMARK 465 ALA a 25
REMARK 465 ARG a 26
REMARK 465 LYS a 27
REMARK 465 SER a 28
REMARK 465 ALA a 29
REMARK 465 PRO a 30
REMARK 465 SER a 31
REMARK 465 THR a 32
REMARK 465 GLY a 33
REMARK 465 GLY a 34
REMARK 465 VAL a 35
REMARK 465 LYS a 36
REMARK 465 LYS a 37
REMARK 465 ALA a 135
REMARK 465 GLY b -3
REMARK 465 SER b -2
REMARK 465 HIS b -1
REMARK 465 MET b 0
REMARK 465 SER b 1
REMARK 465 GLY b 2
REMARK 465 ARG b 3
REMARK 465 GLY b 4
REMARK 465 LYS b 5
REMARK 465 GLY b 6
REMARK 465 GLY b 7
REMARK 465 LYS b 8
REMARK 465 GLY b 9
REMARK 465 LEU b 10
REMARK 465 GLY b 11
REMARK 465 LYS b 12
REMARK 465 GLY b 13
REMARK 465 GLY b 14
REMARK 465 ALA b 15
REMARK 465 LYS b 16
REMARK 465 ARG b 17
REMARK 465 HIS b 18
REMARK 465 ARG b 19
REMARK 465 LYS b 20
REMARK 465 VAL b 21
REMARK 465 LEU b 22
REMARK 465 GLY c -3
REMARK 465 SER c -2
REMARK 465 HIS c -1
REMARK 465 MET c 0
REMARK 465 SER c 1
REMARK 465 GLY c 2
REMARK 465 ARG c 3
REMARK 465 GLY c 4
REMARK 465 LYS c 5
REMARK 465 GLN c 6
REMARK 465 GLY c 7
REMARK 465 GLY c 8
REMARK 465 LYS c 9
REMARK 465 ALA c 10
REMARK 465 ARG c 11
REMARK 465 ALA c 12
REMARK 465 LYS c 13
REMARK 465 ALA c 14
REMARK 465 LYS c 15
REMARK 465 LYS c 119
REMARK 465 THR c 120
REMARK 465 GLU c 121
REMARK 465 SER c 122
REMARK 465 HIS c 123
REMARK 465 HIS c 124
REMARK 465 LYS c 125
REMARK 465 ALA c 126
REMARK 465 LYS c 127
REMARK 465 GLY c 128
REMARK 465 LYS c 129
REMARK 465 GLY d -6
REMARK 465 SER d -5
REMARK 465 HIS d -4
REMARK 465 MET d -3
REMARK 465 PRO d -2
REMARK 465 GLU d -1
REMARK 465 PRO d 0
REMARK 465 ALA d 1
REMARK 465 LYS d 2
REMARK 465 SER d 3
REMARK 465 ALA d 4
REMARK 465 PRO d 5
REMARK 465 ALA d 6
REMARK 465 PRO d 7
REMARK 465 LYS d 8
REMARK 465 LYS d 9
REMARK 465 GLY d 10
REMARK 465 SER d 11
REMARK 465 LYS d 12
REMARK 465 LYS d 13
REMARK 465 ALA d 14
REMARK 465 VAL d 15
REMARK 465 THR d 16
REMARK 465 LYS d 17
REMARK 465 ALA d 18
REMARK 465 GLN d 19
REMARK 465 LYS d 20
REMARK 465 LYS d 21
REMARK 465 ASP d 22
REMARK 465 GLY d 23
REMARK 465 LYS d 24
REMARK 465 LYS d 25
REMARK 465 ARG d 26
REMARK 465 LYS d 27
REMARK 465 GLY e -3
REMARK 465 SER e -2
REMARK 465 HIS e -1
REMARK 465 MET e 0
REMARK 465 ALA e 1
REMARK 465 ARG e 2
REMARK 465 THR e 3
REMARK 465 LYS e 4
REMARK 465 GLN e 5
REMARK 465 THR e 6
REMARK 465 ALA e 7
REMARK 465 ARG e 8
REMARK 465 LYS e 9
REMARK 465 SER e 10
REMARK 465 THR e 11
REMARK 465 GLY e 12
REMARK 465 GLY e 13
REMARK 465 LYS e 14
REMARK 465 ALA e 15
REMARK 465 PRO e 16
REMARK 465 ARG e 17
REMARK 465 LYS e 18
REMARK 465 GLN e 19
REMARK 465 LEU e 20
REMARK 465 ALA e 21
REMARK 465 THR e 22
REMARK 465 LYS e 23
REMARK 465 ALA e 24
REMARK 465 ALA e 25
REMARK 465 ARG e 26
REMARK 465 LYS e 27
REMARK 465 SER e 28
REMARK 465 ALA e 29
REMARK 465 PRO e 30
REMARK 465 SER e 31
REMARK 465 THR e 32
REMARK 465 GLY e 33
REMARK 465 GLY e 34
REMARK 465 VAL e 35
REMARK 465 LYS e 36
REMARK 465 LYS e 37
REMARK 465 PRO e 38
REMARK 465 GLY f -3
REMARK 465 SER f -2
REMARK 465 HIS f -1
REMARK 465 MET f 0
REMARK 465 SER f 1
REMARK 465 GLY f 2
REMARK 465 ARG f 3
REMARK 465 GLY f 4
REMARK 465 LYS f 5
REMARK 465 GLY f 6
REMARK 465 GLY f 7
REMARK 465 LYS f 8
REMARK 465 GLY f 9
REMARK 465 LEU f 10
REMARK 465 GLY f 11
REMARK 465 LYS f 12
REMARK 465 GLY f 13
REMARK 465 GLY f 14
REMARK 465 ALA f 15
REMARK 465 LYS f 16
REMARK 465 ARG f 17
REMARK 465 HIS f 18
REMARK 465 ARG f 19
REMARK 465 LYS f 20
REMARK 465 VAL f 21
REMARK 465 LEU f 22
REMARK 465 ARG f 23
REMARK 465 ASP f 24
REMARK 465 GLY g -3
REMARK 465 SER g -2
REMARK 465 HIS g -1
REMARK 465 MET g 0
REMARK 465 SER g 1
REMARK 465 GLY g 2
REMARK 465 ARG g 3
REMARK 465 GLY g 4
REMARK 465 LYS g 5
REMARK 465 GLN g 6
REMARK 465 GLY g 7
REMARK 465 GLY g 8
REMARK 465 LYS g 9
REMARK 465 ALA g 10
REMARK 465 ARG g 11
REMARK 465 ALA g 12
REMARK 465 LYS g 13
REMARK 465 LYS g 119
REMARK 465 THR g 120
REMARK 465 GLU g 121
REMARK 465 SER g 122
REMARK 465 HIS g 123
REMARK 465 HIS g 124
REMARK 465 LYS g 125
REMARK 465 ALA g 126
REMARK 465 LYS g 127
REMARK 465 GLY g 128
REMARK 465 LYS g 129
REMARK 465 GLY h -6
REMARK 465 SER h -5
REMARK 465 HIS h -4
REMARK 465 MET h -3
REMARK 465 PRO h -2
REMARK 465 GLU h -1
REMARK 465 PRO h 0
REMARK 465 ALA h 1
REMARK 465 LYS h 2
REMARK 465 SER h 3
REMARK 465 ALA h 4
REMARK 465 PRO h 5
REMARK 465 ALA h 6
REMARK 465 PRO h 7
REMARK 465 LYS h 8
REMARK 465 LYS h 9
REMARK 465 GLY h 10
REMARK 465 SER h 11
REMARK 465 LYS h 12
REMARK 465 LYS h 13
REMARK 465 ALA h 14
REMARK 465 VAL h 15
REMARK 465 THR h 16
REMARK 465 LYS h 17
REMARK 465 ALA h 18
REMARK 465 GLN h 19
REMARK 465 LYS h 20
REMARK 465 LYS h 21
REMARK 465 ASP h 22
REMARK 465 GLY h 23
REMARK 465 LYS h 24
REMARK 465 LYS h 25
REMARK 465 ARG h 26
REMARK 465 LYS h 27
REMARK 465 ARG h 28
REMARK 465 SER h 29
REMARK 465 ARG h 30
REMARK 465 LYS h 122
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 OG SER A 467 ND2 ASN K 2 2.02
REMARK 500 N2 DG T 47 O2 DC N -47 2.03
REMARK 500 OG1 THR A 676 OD1 ASN A 737 2.06
REMARK 500 NZ LYS C 185 O GLU C 211 2.08
REMARK 500 OD2 ASP A 854 NH2 ARG A 858 2.09
REMARK 500 OE1 GLU A 1064 OH TYR F 88 2.09
REMARK 500 O PRO A 243 NH1 ARG A 248 2.09
REMARK 500 O ARG B 166 NH2 ARG B 173 2.09
REMARK 500 OG SER B 22 OH TYR B 811 2.11
REMARK 500 O ILE A 887 NH2 ARG A 945 2.11
REMARK 500 O LYS A 1451 OG1 THR A 1454 2.12
REMARK 500 N1 DA T -25 N3 DT N 25 2.12
REMARK 500 OD1 ASP A 610 NE2 GLN A 971 2.12
REMARK 500 N ASP A 891 O SER A 1298 2.13
REMARK 500 OE2 GLU C 179 OG SER C 204 2.13
REMARK 500 N PHE H 117 O LEU H 120 2.14
REMARK 500 O ASP A 982 NH2 ARG A 1041 2.14
REMARK 500 OE2 GLU A 1258 N GLN A 1261 2.15
REMARK 500 O ALA D 143 OG SER D 147 2.15
REMARK 500 N ARG C 148 OE1 GLN C 151 2.16
REMARK 500 NZ LYS E 19 O GLU E 33 2.16
REMARK 500 O GLN B 862 NZ LYS B 914 2.16
REMARK 500 O ALA B 752 OG SER B 771 2.16
REMARK 500 NE ARG B 598 OE1 GLU B 688 2.16
REMARK 500 O GLY A 889 NH2 ARG A 941 2.16
REMARK 500 OD1 ASP A 486 O2' G P 10 2.16
REMARK 500 O LEU J 60 N TYR J 62 2.16
REMARK 500 N GLN B 975 OD2 ASP B 978 2.17
REMARK 500 O PRO B 1197 N ALA B 1200 2.17
REMARK 500 O ASN A 549 N PHE A 552 2.17
REMARK 500 OD2 ASP A 1445 OH TYR F 137 2.17
REMARK 500 OD2 ASP A 1168 NH1 ARG A 1241 2.17
REMARK 500 OG SER C 27 OE1 GLU K 48 2.17
REMARK 500 OG1 THR K 57 O GLN K 76 2.17
REMARK 500 OD2 ASP A 308 NH1 ARG A 327 2.17
REMARK 500 O LEU A 141 OG1 THR A 144 2.18
REMARK 500 NH1 ARG B 1159 OE1 GLN B 1193 2.18
REMARK 500 OG1 THR C 54 N GLU C 152 2.18
REMARK 500 NZ LYS E 160 O GLY E 192 2.18
REMARK 500 ND2 ASN B 72 O SER B 126 2.18
REMARK 500 NH2 ARG I 70 OD1 ASP I 82 2.18
REMARK 500 OE1 GLU A 1153 NH1 ARG A 1196 2.18
REMARK 500 O ALA A 781 NZ LYS A 790 2.19
REMARK 500 O LEU B 681 OG SER B 684 2.19
REMARK 500 O CYS C 91 OG SER C 95 2.19
REMARK 500 OG SER B 233 ND1 HIS B 356 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 G P 10 C1' G P 10 N9 -0.094
REMARK 500 DG T -7 O3' DG T -7 C3' -0.039
REMARK 500 DT T 3 O3' DT T 3 C3' -0.044
REMARK 500 DA T 17 C1' DA T 17 N9 -0.118
REMARK 500 DG T 20 C1' DG T 20 N9 -0.124
REMARK 500 DA T 23 C1' DA T 23 N9 -0.088
REMARK 500 DA T 32 C1' DA T 32 N9 -0.103
REMARK 500 DA T 34 O3' DA T 34 C3' -0.054
REMARK 500 DC T 35 O3' DC T 35 C3' -0.052
REMARK 500 DA T 38 C1' DA T 38 N9 -0.121
REMARK 500 DA T 41 O3' DA T 41 C3' -0.044
REMARK 500 DG N -51 C1' DG N -51 N9 -0.109
REMARK 500 DG N -49 C1' DG N -49 N9 -0.095
REMARK 500 DG N -19 C1' DG N -19 N9 -0.084
REMARK 500 DA N -15 C1' DA N -15 N9 -0.110
REMARK 500 DT 1 -46 O3' DT 1 -46 C3' -0.037
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 LEU A 473 CA - CB - CG ANGL. DEV. = -22.6 DEGREES
REMARK 500 LEU A 926 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU A 962 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU A1316 CA - CB - CG ANGL. DEV. = -14.7 DEGREES
REMARK 500 LEU B 485 CA - CB - CG ANGL. DEV. = -18.1 DEGREES
REMARK 500 GLU B 557 C - N - CA ANGL. DEV. = -21.0 DEGREES
REMARK 500 LEU G 106 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 DG T -68 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT T -59 C3' - C2' - C1' ANGL. DEV. = -5.4 DEGREES
REMARK 500 DT T -59 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG T -30 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT T -26 O4' - C4' - C3' ANGL. DEV. = -2.8 DEGREES
REMARK 500 DC T -8 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC T 10 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA T 17 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG N -51 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT N -16 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DC N 3 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG N 12 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT N 13 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA N 16 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG N 27 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC N 37 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG N 38 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC N 58 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 DT N 66 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT N 67 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DG 0 52 O4' - C4' - C3' ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA 0 55 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DA 0 62 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA 0 64 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT 1 -63 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT 1 -57 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT 1 -55 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DT 1 -34 O4' - C1' - N1 ANGL. DEV. = 2.5 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 ASP A 42 -72.89 -60.98
REMARK 500 GLU A 43 42.95 -145.91
REMARK 500 SER A 44 68.32 63.23
REMARK 500 GLN A 46 84.87 60.86
REMARK 500 ARG A 47 79.52 74.79
REMARK 500 PRO A 48 170.46 -53.58
REMARK 500 ASN A 54 26.49 -143.01
REMARK 500 PRO A 56 4.89 -65.17
REMARK 500 LEU A 114 -10.09 -48.63
REMARK 500 GLU A 117 17.42 -68.56
REMARK 500 ASP A 178 104.37 -163.35
REMARK 500 LYS A 187 52.65 -103.48
REMARK 500 LYS A 188 103.93 -59.77
REMARK 500 LYS A 213 4.74 -65.45
REMARK 500 PRO A 217 -2.54 -56.89
REMARK 500 GLU A 218 -71.31 -78.65
REMARK 500 PHE A 225 -165.41 -72.97
REMARK 500 GLU A 255 0.71 49.94
REMARK 500 THR A 256 -31.87 -137.28
REMARK 500 SER A 285 132.52 -170.42
REMARK 500 PRO A 286 34.01 -81.74
REMARK 500 GLN A 287 -3.12 60.51
REMARK 500 ASP A 306 141.93 -176.02
REMARK 500 LYS A 318 30.01 -81.09
REMARK 500 ALA A 325 -161.27 -72.40
REMARK 500 ASN A 340 -7.59 -148.91
REMARK 500 SER A 349 -168.30 -101.64
REMARK 500 ALA A 350 144.54 -178.49
REMARK 500 THR A 352 -167.50 -179.85
REMARK 500 ASP A 357 87.97 -158.55
REMARK 500 ASN A 359 38.45 -93.91
REMARK 500 GLU A 361 -158.94 -80.73
REMARK 500 ASP A 363 46.90 -91.73
REMARK 500 LEU A 375 -178.22 -63.84
REMARK 500 LYS A 404 -35.43 -135.25
REMARK 500 HIS A 436 -176.74 -67.04
REMARK 500 MET A 438 -164.71 -78.86
REMARK 500 ARG A 447 115.33 -166.30
REMARK 500 HIS A 452 150.35 178.36
REMARK 500 LYS A 453 7.56 -57.08
REMARK 500 SER A 455 5.44 -58.53
REMARK 500 ALA A 458 -172.75 -63.25
REMARK 500 HIS A 459 -155.83 -155.06
REMARK 500 TYR A 466 83.05 63.22
REMARK 500 SER A 467 95.77 -64.94
REMARK 500 ASP A 482 -156.90 -83.19
REMARK 500 PRO A 515 7.51 -60.91
REMARK 500 ASN A 518 40.96 32.20
REMARK 500 GLN A 526 -73.97 -34.30
REMARK 500 VAL A 532 -3.83 -58.37
REMARK 500
REMARK 500 THIS ENTRY HAS 340 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 VAL A 525 GLN A 526 -148.99
REMARK 500 SER B 126 ILE B 127 -149.04
REMARK 500 LEU B 175 ASP B 176 137.66
REMARK 500 ASP C 89 TYR C 90 -147.08
REMARK 500 LEU D 27 LEU D 28 147.70
REMARK 500 ASP G 153 VAL G 154 -149.51
REMARK 500 ASN J 63 PRO J 64 -145.77
REMARK 500 ARG a 42 PRO a 43 -145.09
REMARK 500 ARG a 63 LYS a 64 -143.70
REMARK 500 ARG e 63 LYS e 64 -142.22
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 A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 70 SG
REMARK 620 2 CYS A 77 SG 94.5
REMARK 620 3 HIS A 80 NE2 171.2 76.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107 SG
REMARK 620 2 CYS A 168 N 138.3
REMARK 620 3 CYS A 168 SG 127.0 74.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 482 OD1
REMARK 620 2 ASP A 482 OD2 42.9
REMARK 620 3 ASP A 484 OD1 57.4 70.7
REMARK 620 4 ASP A 484 OD2 87.6 59.5 56.4
REMARK 620 5 G P 10 O3' 109.8 148.8 81.3 115.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163 SG
REMARK 620 2 CYS B1166 SG 109.3
REMARK 620 3 CYS B1182 SG 98.3 93.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 85 SG
REMARK 620 2 CYS C 94 N 161.0
REMARK 620 3 CYS C 94 SG 91.7 88.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 9 OE1
REMARK 620 2 CYS I 32 SG 81.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 75 SG
REMARK 620 2 CYS I 78 SG 87.8
REMARK 620 3 CYS I 103 SG 85.8 135.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 10 SG 90.3
REMARK 620 3 CYS J 44 SG 109.1 83.7
REMARK 620 4 CYS J 45 N 106.1 154.9 73.1
REMARK 620 5 CYS J 45 SG 136.1 82.3 112.9 97.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 50 SG
REMARK 620 2 CYS L 53 SG 117.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-6980 RELATED DB: EMDB
REMARK 900 RNA POLYMERASE II ELONGATION COMPLEX STALLED AT SHL(-1) OF THE
REMARK 900 NUCLEOSOME, WITH FOREIGN DNA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF CHAIN I IS SAME WITH UNP F2QPE6 FROM DIFFERENT
REMARK 999 STRAIN ATCC 76273. THE SEQUENCE OF CHAIN L IS SAME WITH UNP F2QMI1
REMARK 999 FROM DIFFERENT STRAIN ATCC 76273.
DBREF 6A5L A 1 1743 UNP C4R4Y0 C4R4Y0_KOMPG 1 1743
DBREF 6A5L B 1 1227 UNP C4QZQ7 C4QZQ7_KOMPG 1 1227
DBREF 6A5L C 1 304 UNP C4R7L2 C4R7L2_KOMPG 1 304
DBREF 6A5L D 1 186 UNP C4R2U9 C4R2U9_KOMPG 1 186
DBREF 6A5L E 1 214 UNP C4R3P8 C4R3P8_KOMPG 1 214
DBREF 6A5L F 1 155 UNP C4R1V1 C4R1V1_KOMPG 1 155
DBREF 6A5L G 1 171 UNP C4R9A1 C4R9A1_KOMPG 1 171
DBREF 6A5L H 1 145 UNP C4R273 C4R273_KOMPG 1 145
DBREF 6A5L I 1 115 UNP F2QPE6 F2QPE6_KOMPC 1 115
DBREF 6A5L J 1 72 UNP C4R009 C4R009_KOMPG 1 72
DBREF 6A5L K 1 118 UNP C4R3Z5 C4R3Z5_KOMPG 1 118
DBREF 6A5L L 1 72 UNP F2QMI1 F2QMI1_KOMPC 1 72
DBREF 6A5L P 0 10 PDB 6A5L 6A5L 0 10
DBREF 6A5L T -72 125 PDB 6A5L 6A5L -72 125
DBREF 6A5L N -125 72 PDB 6A5L 6A5L -125 72
DBREF 6A5L a 0 135 UNP P84243 H33_HUMAN 1 136
DBREF 6A5L b 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 6A5L c 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 6A5L d -3 122 UNP P06899 H2B1J_HUMAN 1 126
DBREF 6A5L e 0 135 UNP P84243 H33_HUMAN 1 136
DBREF 6A5L f 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 6A5L g 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 6A5L h -3 122 UNP P06899 H2B1J_HUMAN 1 126
DBREF 6A5L 0 25 66 PDB 6A5L 6A5L 25 66
DBREF 6A5L 1 -66 -25 PDB 6A5L 6A5L -66 -25
SEQADV 6A5L GLY a -3 UNP P84243 EXPRESSION TAG
SEQADV 6A5L SER a -2 UNP P84243 EXPRESSION TAG
SEQADV 6A5L HIS a -1 UNP P84243 EXPRESSION TAG
SEQADV 6A5L GLY b -3 UNP P62805 EXPRESSION TAG
SEQADV 6A5L SER b -2 UNP P62805 EXPRESSION TAG
SEQADV 6A5L HIS b -1 UNP P62805 EXPRESSION TAG
SEQADV 6A5L GLY c -3 UNP P04908 EXPRESSION TAG
SEQADV 6A5L SER c -2 UNP P04908 EXPRESSION TAG
SEQADV 6A5L HIS c -1 UNP P04908 EXPRESSION TAG
SEQADV 6A5L GLY d -6 UNP P06899 EXPRESSION TAG
SEQADV 6A5L SER d -5 UNP P06899 EXPRESSION TAG
SEQADV 6A5L HIS d -4 UNP P06899 EXPRESSION TAG
SEQADV 6A5L GLY e -3 UNP P84243 EXPRESSION TAG
SEQADV 6A5L SER e -2 UNP P84243 EXPRESSION TAG
SEQADV 6A5L HIS e -1 UNP P84243 EXPRESSION TAG
SEQADV 6A5L GLY f -3 UNP P62805 EXPRESSION TAG
SEQADV 6A5L SER f -2 UNP P62805 EXPRESSION TAG
SEQADV 6A5L HIS f -1 UNP P62805 EXPRESSION TAG
SEQADV 6A5L GLY g -3 UNP P04908 EXPRESSION TAG
SEQADV 6A5L SER g -2 UNP P04908 EXPRESSION TAG
SEQADV 6A5L HIS g -1 UNP P04908 EXPRESSION TAG
SEQADV 6A5L GLY h -6 UNP P06899 EXPRESSION TAG
SEQADV 6A5L SER h -5 UNP P06899 EXPRESSION TAG
SEQADV 6A5L HIS h -4 UNP P06899 EXPRESSION TAG
SEQRES 1 A 1743 MET SER GLN PHE PRO TYR SER SER ALA PRO LEU ARG SER
SEQRES 2 A 1743 VAL LYS GLU VAL GLN PHE GLY LEU LEU SER PRO GLU GLU
SEQRES 3 A 1743 ILE ARG ALA ILE SER VAL VAL LYS ILE GLU TYR PRO GLU
SEQRES 4 A 1743 ILE MET ASP GLU SER ARG GLN ARG PRO ARG GLU GLY GLY
SEQRES 5 A 1743 LEU ASN ASP PRO LYS LEU GLY SER ILE ASP ARG ASN PHE
SEQRES 6 A 1743 LYS CYS GLN THR CYS GLY GLU GLY MET ALA GLU CYS PRO
SEQRES 7 A 1743 GLY HIS PHE GLY HIS MET GLU LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1743 HIS ILE GLY PHE ILE PRO LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1743 CYS ILE CYS MET ASN CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1743 THR ASN PRO THR MET ALA GLN ALA ILE ARG ILE ARG ASP
SEQRES 11 A 1743 PRO LYS LYS ARG PHE ASN ALA VAL TRP GLN LEU CYS LYS
SEQRES 12 A 1743 THR LYS MET VAL CYS GLU ALA ASP ALA PRO VAL ASP GLU
SEQRES 13 A 1743 TYR SER GLU GLN LYS VAL VAL SER ARG GLY GLY CYS GLY
SEQRES 14 A 1743 ASN THR GLN PRO VAL VAL ARG LYS ASP GLY MET LYS LEU
SEQRES 15 A 1743 TRP GLY THR TRP LYS LYS SER GLY PHE SER ASP ARG ASP
SEQRES 16 A 1743 ALA GLN PRO GLU ARG LYS LEU LEU THR PRO GLY GLU ILE
SEQRES 17 A 1743 LEU ASN VAL PHE LYS HIS ILE SER PRO GLU ASP CYS PHE
SEQRES 18 A 1743 ARG LEU GLY PHE ASN GLU ASP TYR ALA ARG PRO GLU TRP
SEQRES 19 A 1743 MET ILE ILE THR VAL LEU PRO VAL PRO PRO PRO GLN VAL
SEQRES 20 A 1743 ARG PRO SER ILE ALA MET ASP GLU THR THR GLN GLY GLN
SEQRES 21 A 1743 ASP ASP LEU THR HIS LYS LEU SER ASP ILE LEU LYS ALA
SEQRES 22 A 1743 ASN ILE ASN VAL GLN LYS LEU GLU MET ASP GLY SER PRO
SEQRES 23 A 1743 GLN HIS ILE ILE ASN GLU VAL GLU GLN LEU LEU GLN PHE
SEQRES 24 A 1743 HIS VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN
SEQRES 25 A 1743 PRO GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS ALA
SEQRES 26 A 1743 ILE ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG LEU ARG
SEQRES 27 A 1743 GLY ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG
SEQRES 28 A 1743 THR VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN
SEQRES 29 A 1743 VAL GLY VAL PRO ILE SER ILE ALA LYS THR LEU SER TYR
SEQRES 30 A 1743 PRO GLU THR VAL THR GLN TYR ASN ILE HIS ARG LEU THR
SEQRES 31 A 1743 GLU TYR VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA
SEQRES 32 A 1743 LYS TYR VAL ILE ARG ASP ASN GLY ASP ARG ILE ASP LEU
SEQRES 33 A 1743 ARG TYR HIS LYS ARG ALA GLY ASP ILE VAL LEU GLN TYR
SEQRES 34 A 1743 GLY TRP LYS VAL GLU ARG HIS LEU MET ASP ASP ASP PRO
SEQRES 35 A 1743 VAL LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER
SEQRES 36 A 1743 MET MET ALA HIS ARG VAL LYS VAL MET PRO TYR SER THR
SEQRES 37 A 1743 PHE ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA
SEQRES 38 A 1743 ASP PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN
SEQRES 39 A 1743 SER GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA
SEQRES 40 A 1743 VAL PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO
SEQRES 41 A 1743 VAL MET GLY ILE VAL GLN ASP THR LEU CYS GLY VAL ARG
SEQRES 42 A 1743 LYS MET THR LEU ARG ASP THR PHE ILE GLU TYR GLU GLN
SEQRES 43 A 1743 VAL MET ASN MET LEU PHE TRP VAL PRO SER TRP ASP GLY
SEQRES 44 A 1743 VAL VAL PRO GLN PRO ALA ILE LEU LYS PRO LYS PRO LEU
SEQRES 45 A 1743 TRP THR GLY LYS GLN LEU LEU SER ILE ALA ILE PRO SER
SEQRES 46 A 1743 GLY ILE HIS LEU GLN ARG THR ASP GLY GLY ASN SER LEU
SEQRES 47 A 1743 LEU SER PRO LYS ASP ASN GLY MET LEU ILE VAL ASP GLY
SEQRES 48 A 1743 LYS VAL MET PHE GLY VAL VAL ASP LYS LYS THR VAL GLY
SEQRES 49 A 1743 SER GLY GLY GLY GLY LEU ILE HIS THR VAL MET ARG GLU
SEQRES 50 A 1743 LYS GLY PRO LYS ILE CYS ALA GLU LEU PHE GLY ASN ILE
SEQRES 51 A 1743 GLN LYS VAL VAL ASN TYR TRP LEU LEU HIS ASN GLY PHE
SEQRES 52 A 1743 SER ILE GLY ILE GLY ASP ALA ILE ALA ASP ALA SER THR
SEQRES 53 A 1743 MET LYS GLU ILE THR HIS ALA ILE SER SER ALA LYS GLU
SEQRES 54 A 1743 GLN VAL GLN GLU ILE ILE TYR LYS ALA GLN HIS ASN GLU
SEQRES 55 A 1743 LEU GLU LEU LYS PRO GLY MET THR LEU ARG GLU SER PHE
SEQRES 56 A 1743 GLU GLY GLU VAL SER ARG THR LEU ASN ASP ALA ARG ASP
SEQRES 57 A 1743 SER ALA GLY ARG SER ALA GLU MET ASN LEU LYS ASP LEU
SEQRES 58 A 1743 ASN ASN VAL LYS GLN MET VAL SER ALA GLY SER LYS GLY
SEQRES 59 A 1743 SER PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY
SEQRES 60 A 1743 GLN GLN MET VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE
SEQRES 61 A 1743 ALA ASP ARG SER LEU PRO HIS PHE THR LYS ASP ASP PHE
SEQRES 62 A 1743 SER PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU
SEQRES 63 A 1743 ARG GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET
SEQRES 64 A 1743 ALA GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR
SEQRES 65 A 1743 ALA GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA
SEQRES 66 A 1743 LEU GLU ASP ILE MET VAL HIS TYR ASP GLY THR THR ARG
SEQRES 67 A 1743 ASN SER LEU GLY ASP ILE ILE GLN PHE LEU TYR GLY GLU
SEQRES 68 A 1743 ASP GLY LEU ASP GLY THR GLN VAL GLU ARG GLN THR ILE
SEQRES 69 A 1743 ASP THR ILE PRO GLY SER ASP LYS ALA PHE HIS LYS ARG
SEQRES 70 A 1743 TYR TYR VAL ASP LEU MET ASP GLU LYS ASN SER ILE LYS
SEQRES 71 A 1743 PRO ASP VAL ILE GLU TYR ALA ALA ASP ILE LEU GLY ASP
SEQRES 72 A 1743 VAL GLU LEU GLN LYS GLU LEU ASN SER GLU TYR GLU GLN
SEQRES 73 A 1743 LEU VAL SER ASP ARG LYS PHE LEU ARG GLU ILE VAL PHE
SEQRES 74 A 1743 VAL ASN GLY ASP HIS ASN TRP PRO LEU PRO VAL ASN LEU
SEQRES 75 A 1743 ARG ARG ILE ILE GLN ASN ALA GLN GLN ILE PHE HIS LEU
SEQRES 76 A 1743 ASP ARG ALA LYS ALA SER ASP LEU THR ILE PRO GLU ILE
SEQRES 77 A 1743 ILE HIS GLY VAL ARG ASP LEU CYS LYS LYS LEU PHE VAL
SEQRES 78 A 1743 LEU ARG GLY GLU ASN GLU LEU ILE LYS GLU ALA GLN GLN
SEQRES 79 A 1743 ASN ALA THR SER LEU PHE GLN CYS LEU VAL ARG ALA ARG
SEQRES 80 A 1743 LEU ALA THR ARG ARG ILE LEU GLU GLU PHE ARG LEU ASN
SEQRES 81 A 1743 ARG ASP ALA PHE GLU TRP VAL LEU GLY THR ILE GLU ALA
SEQRES 82 A 1743 GLN PHE GLN ARG SER LEU VAL HIS PRO GLY GLU MET VAL
SEQRES 83 A 1743 GLY VAL ILE ALA ALA GLN SER ILE GLY GLU PRO ALA THR
SEQRES 84 A 1743 GLN MET THR LEU ASN THR PHE HIS TYR ALA GLY VAL SER
SEQRES 85 A 1743 SER LYS ASN VAL THR LEU GLY VAL PRO ARG LEU LYS GLU
SEQRES 86 A 1743 ILE LEU ASN VAL ALA LYS ASN ILE LYS THR PRO ALA LEU
SEQRES 87 A 1743 THR VAL TYR LEU ASP ARG GLU ILE ALA LEU ASP ILE GLU
SEQRES 88 A 1743 LYS ALA LYS VAL ILE GLN SER SER ILE GLU TYR THR THR
SEQRES 89 A 1743 LEU LYS ASN VAL THR SER ALA THR GLU ILE TYR TYR ASP
SEQRES 90 A 1743 PRO ASP PRO THR SER THR VAL ILE GLU GLU ASP PHE ASP
SEQRES 91 A 1743 THR VAL GLU ALA TYR PHE SER ILE PRO ASP GLU LYS VAL
SEQRES 92 A 1743 GLU GLU THR ILE ASP LYS GLN SER PRO TRP LEU LEU ARG
SEQRES 93 A 1743 LEU GLU LEU ASP ARG ALA ARG MET LEU ASP LYS GLN LEU
SEQRES 94 A 1743 THR MET ASN GLN VAL ALA ASP LYS ILE SER GLU VAL PHE
SEQRES 95 A 1743 SER ASP ASP LEU PHE VAL MET TRP SER GLU ASP ASN ALA
SEQRES 96 A 1743 ASP LYS LEU ILE ILE ARG CYS ARG VAL ILE ARG ASP PRO
SEQRES 97 A 1743 LYS ALA MET ASP GLU GLU LEU GLU ALA GLU GLU ASP GLN
SEQRES 98 A 1743 MET LEU LYS ARG ILE GLU ALA HIS MET LEU ASP LEU ILE
SEQRES 99 A 1743 ALA LEU ARG GLY ILE PRO GLY ILE SER LYS VAL TYR MET
SEQRES 100 A 1743 VAL LYS HIS LYS VAL SER VAL PRO ASP GLU SER GLY GLU
SEQRES 101 A 1743 TYR LYS ASN GLU GLU LEU TRP ALA LEU GLU THR ASP GLY
SEQRES 102 A 1743 ILE ASN LEU ALA GLU VAL MET ALA VAL PRO GLY VAL ASP
SEQRES 103 A 1743 SER SER ARG THR TYR SER ASN SER PHE VAL GLU ILE LEU
SEQRES 104 A 1743 SER VAL LEU GLY ILE GLU ALA THR ARG SER SER LEU TYR
SEQRES 105 A 1743 LYS GLU ILE LEU ASN VAL ILE ALA PHE ASP GLY SER TYR
SEQRES 106 A 1743 VAL ASN TYR ARG HIS MET ALA LEU LEU VAL ASP VAL MET
SEQRES 107 A 1743 THR SER ARG GLY TYR LEU MET ALA ILE THR ARG HIS GLY
SEQRES 108 A 1743 ILE ASN ARG ALA ASP THR GLY ALA LEU MET ARG CYS SER
SEQRES 109 A 1743 PHE GLU GLU THR VAL GLU ILE LEU PHE GLU ALA GLY ALA
SEQRES 110 A 1743 ALA ALA GLU LEU ASP ASP CYS ARG GLY VAL SER GLU ASN
SEQRES 111 A 1743 VAL MET LEU GLY GLN LEU ALA PRO MET GLY THR GLY ALA
SEQRES 112 A 1743 PHE ASP VAL MET ILE ASP GLU LYS LEU LEU THR SER LEU
SEQRES 113 A 1743 PRO ALA ASP TYR ALA PRO THR MET PRO LEU PHE LYS GLY
SEQRES 114 A 1743 LYS ALA THR GLN GLY SER ALA THR PRO TYR ASP ASN ASN
SEQRES 115 A 1743 ALA GLN TYR ASP ASP GLU PHE ASN HIS ASP ASP VAL ALA
SEQRES 116 A 1743 ASP VAL MET PHE SER PRO MET ALA GLU THR GLY SER GLY
SEQRES 117 A 1743 ASP ASP ARG SER GLY GLY LEU THR GLU TYR ALA GLY ILE
SEQRES 118 A 1743 GLN SER PRO TYR GLN PRO THR SER PRO GLY LEU SER ALA
SEQRES 119 A 1743 THR SER PRO GLY PHE ALA PRO THR SER PRO GLY PHE ALA
SEQRES 120 A 1743 PRO THR SER PRO ARG TYR SER PRO THR SER PRO GLY TYR
SEQRES 121 A 1743 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 122 A 1743 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 123 A 1743 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 124 A 1743 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 125 A 1743 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 126 A 1743 THR SER PRO GLN TYR SER PRO THR SER PRO GLN TYR SER
SEQRES 127 A 1743 PRO THR SER PRO GLN TYR SER PRO THR SER PRO GLN TYR
SEQRES 128 A 1743 SER PRO THR SER PRO GLN TYR SER PRO THR SER PRO GLN
SEQRES 129 A 1743 TYR SER PRO THR SER PRO GLN TYR SER PRO THR SER PRO
SEQRES 130 A 1743 GLN TYR SER PRO THR SER PRO GLN TYR SER PRO THR SER
SEQRES 131 A 1743 PRO GLN TYR SER PRO THR SER PRO GLN TYR SER PRO THR
SEQRES 132 A 1743 SER PRO GLN TYR SER PRO THR SER PRO GLN TYR SER PRO
SEQRES 133 A 1743 THR SER PRO GLN TYR SER PRO ALA SER PRO GLN TYR SER
SEQRES 134 A 1743 PRO SER ARG HIS SER PRO ASN GLY GLU SER LYS GLU GLY
SEQRES 135 A 1743 GLU
SEQRES 1 B 1227 MET SER TYR ASP PRO TYR SER ILE ASP ASP THR ILE THR
SEQRES 2 B 1227 THR GLU ASP CYS TRP THR VAL ILE SER ALA PHE PHE GLU
SEQRES 3 B 1227 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASP
SEQRES 4 B 1227 GLU PHE MET GLU THR SER ILE GLN ASP LEU VAL TRP GLU
SEQRES 5 B 1227 GLU PRO ARG LEU ILE LEU ASP GLN PRO ALA GLN HIS THR
SEQRES 6 B 1227 ASN GLU LYS ASP ASN ILE ASN LYS ARG TYR GLU ILE ARG
SEQRES 7 B 1227 PHE GLY LYS ILE TYR LEU SER ARG PRO THR MET THR GLU
SEQRES 8 B 1227 ALA ASP GLY THR THR HIS ALA MET PHE PRO GLN GLU ALA
SEQRES 9 B 1227 ARG LEU ARG ASN LEU THR TYR SER SER PRO VAL TYR LEU
SEQRES 10 B 1227 ASP MET GLU LYS SER MET PHE THR SER ILE ASP ASP GLU
SEQRES 11 B 1227 GLY ASN PRO ASN ALA THR LEU ASP TRP GLN GLN VAL HIS
SEQRES 12 B 1227 GLU PRO ILE LYS ASP GLY VAL GLU GLU GLY ASN LYS VAL
SEQRES 13 B 1227 HIS ILE GLY LYS VAL PRO ILE MET LEU ARG SER LYS PHE
SEQRES 14 B 1227 CYS SER LEU ARG THR LEU ASP GLU VAL ASP LEU TYR LYS
SEQRES 15 B 1227 MET LYS GLU CYS PRO TYR ASP MET GLY GLY TYR PHE VAL
SEQRES 16 B 1227 ILE ASN GLY SER GLU LYS VAL LEU ILE ALA GLN GLU ARG
SEQRES 17 B 1227 SER ALA ALA ASN ILE VAL GLN VAL PHE LYS LYS ALA ALA
SEQRES 18 B 1227 PRO SER PRO ILE SER HIS VAL ALA GLU ILE ARG SER ALA
SEQRES 19 B 1227 LEU GLU LYS GLY SER ARG LEU ILE SER THR MET GLN ILE
SEQRES 20 B 1227 LYS LEU TYR GLY ARG GLU ASP LYS GLY THR GLY ARG THR
SEQRES 21 B 1227 ILE LYS ALA THR LEU PRO TYR VAL LYS GLN ASP ILE PRO
SEQRES 22 B 1227 ILE VAL ILE VAL PHE ARG ALA LEU GLY VAL VAL PRO ASP
SEQRES 23 B 1227 GLY GLU ILE LEU GLN HIS ILE CYS TYR ASP GLU ASN ASP
SEQRES 24 B 1227 TRP GLN MET LEU GLU MET LEU LYS PRO CYS ILE GLU GLU
SEQRES 25 B 1227 GLY PHE VAL ILE GLN ASP LYS GLU VAL ALA LEU ASP PHE
SEQRES 26 B 1227 ILE GLY ARG ARG GLY SER ALA ALA LEU GLY ILE ARG ARG
SEQRES 27 B 1227 GLU LYS ARG ILE GLN TYR ALA LYS ASP ILE LEU GLN LYS
SEQRES 28 B 1227 GLU LEU LEU PRO HIS ILE THR GLN GLU GLU GLY PHE GLU
SEQRES 29 B 1227 THR ARG LYS THR PHE PHE LEU GLY TYR MET VAL ASN ARG
SEQRES 30 B 1227 LEU LEU LEU CYS ALA LEU GLU ARG LYS ASP GLN ASP ASP
SEQRES 31 B 1227 ARG ASP HIS PHE GLY LYS LYS ARG LEU ASP LEU ALA GLY
SEQRES 32 B 1227 PRO LEU LEU ALA ASN LEU PHE ARG ILE LEU PHE ARG LYS
SEQRES 33 B 1227 LEU THR ARG GLU ILE TYR ARG TYR MET GLN ARG CYS ILE
SEQRES 34 B 1227 GLU THR ASP ARG ASP PHE ASN LEU ASN LEU ALA VAL LYS
SEQRES 35 B 1227 SER THR THR ILE THR SER GLY LEU LYS TYR SER LEU ALA
SEQRES 36 B 1227 THR GLY ASN TRP GLY GLU GLN LYS LYS ALA MET SER SER
SEQRES 37 B 1227 ARG ALA GLY VAL SER GLN VAL LEU ASN ARG TYR THR TYR
SEQRES 38 B 1227 SER SER THR LEU SER HIS LEU ARG ARG THR ASN THR PRO
SEQRES 39 B 1227 ILE GLY ARG ASP GLY LYS LEU ALA LYS PRO ARG GLN LEU
SEQRES 40 B 1227 HIS ASN THR HIS TRP GLY LEU VAL CYS PRO ALA GLU THR
SEQRES 41 B 1227 PRO GLU GLY GLN ALA CYS GLY LEU VAL LYS ASN LEU SER
SEQRES 42 B 1227 LEU LEU SER GLY ILE SER ILE GLY SER PRO SER GLU PRO
SEQRES 43 B 1227 ILE ILE ASN PHE LEU GLU GLU TRP GLY MET GLU PRO LEU
SEQRES 44 B 1227 GLU ASP TYR ASP PRO ALA GLN HIS THR LYS SER THR ARG
SEQRES 45 B 1227 ILE PHE VAL ASN GLY VAL TRP THR GLY ILE HIS ARG ASP
SEQRES 46 B 1227 PRO SER MET LEU VAL SER THR MET ARG ASP LEU ARG ARG
SEQRES 47 B 1227 SER GLY ALA ILE SER PRO GLU VAL SER ILE ILE ARG ASP
SEQRES 48 B 1227 ILE ARG GLU ARG GLU PHE LYS ILE PHE THR ASP VAL GLY
SEQRES 49 B 1227 ARG VAL TYR ARG PRO LEU PHE ILE VAL GLU ASP ASP GLU
SEQRES 50 B 1227 SER LYS ASP ASN LYS GLY GLU LEU ARG ILE THR LYS GLU
SEQRES 51 B 1227 HIS ILE ARG LYS ILE GLN GLN GLY TYR ASP ASP ASP ALA
SEQRES 52 B 1227 MET ASN ASP ASP SER GLU GLU GLN GLU GLN ASP VAL TYR
SEQRES 53 B 1227 GLY TRP SER SER LEU VAL THR SER GLY VAL ILE GLU TYR
SEQRES 54 B 1227 VAL ASP GLY GLU GLU GLU GLU THR ILE MET ILE ALA MET
SEQRES 55 B 1227 THR PRO GLU ASP LEU GLN THR ARG SER LEU GLU GLN LYS
SEQRES 56 B 1227 GLU ILE ASP LEU ASN ASP THR ALA LYS ARG ILE LYS PRO
SEQRES 57 B 1227 GLU MET SER THR SER SER HIS HIS THR PHE THR HIS CYS
SEQRES 58 B 1227 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1227 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1227 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1227 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1227 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU ALA LYS THR
SEQRES 63 B 1227 GLN ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1227 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1227 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1227 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1227 TYR MET ASP GLN GLU LYS ARG PHE GLY ILE SER ILE VAL
SEQRES 68 B 1227 GLU GLU PHE GLU LYS PRO THR ARG ALA THR THR LEU ARG
SEQRES 69 B 1227 LEU LYS HIS GLY THR TYR GLU LYS LEU ASP GLU ASP GLY
SEQRES 70 B 1227 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY ASP ASP ILE
SEQRES 71 B 1227 ILE ILE GLY LYS THR THR PRO ILE PRO PRO ASP THR GLU
SEQRES 72 B 1227 GLU LEU GLY GLN ARG THR LYS TYR HIS THR LYS ARG ASP
SEQRES 73 B 1227 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1227 ASP GLN VAL LEU LEU THR THR ASN GLN GLU GLY LEU LYS
SEQRES 75 B 1227 PHE VAL LYS VAL ARG MET ARG THR THR LYS VAL PRO GLN
SEQRES 76 B 1227 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1227 THR ILE GLY VAL THR TYR ARG HIS GLU ASP MET PRO PHE
SEQRES 78 B 1227 SER ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1227 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1227 GLU CYS LEU LEU SER LYS VAL GLY SER ILE ARG GLY TYR
SEQRES 81 B 1227 GLU GLY ASP ALA THR PRO PHE THR ASP LEU THR VAL ASP
SEQRES 82 B 1227 ALA VAL SER ASN LEU LEU ARG ASP ASN GLY TYR GLN SER
SEQRES 83 B 1227 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1227 LYS LEU MET ALA GLN VAL PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1227 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1227 ARG ALA ARG GLY PRO VAL GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1227 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1227 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1227 GLY PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1227 PHE ARG VAL HIS VAL CYS GLY ILE CYS GLY LEU MET SER
SEQRES 91 B 1227 VAL ILE ALA ASN LEU LYS LYS ASN GLN PHE GLU CYS ARG
SEQRES 92 B 1227 SER CYS LYS ASN LYS THR ASN ILE TYR GLN LEU HIS ILE
SEQRES 93 B 1227 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1227 MET ASN ILE ALA PRO ARG LEU TYR THR GLU ARG SER GLY
SEQRES 95 B 1227 VAL SER MET ARG SER
SEQRES 1 C 304 MET SER LYS GLU PRO LYS VAL ASN ILE ILE ASN ALA GLN
SEQRES 2 C 304 ASP ASP GLU VAL GLU LEU MET LEU SER ASP VAL ASN LEU
SEQRES 3 C 304 SER LEU ALA ASN SER LEU ARG ARG THR MET LEU ALA GLU
SEQRES 4 C 304 VAL PRO THR LEU ALA ILE ASP LEU VAL GLU ILE LYS MET
SEQRES 5 C 304 ASN THR SER VAL LEU ALA ASP GLU PHE ILE SER HIS ARG
SEQRES 6 C 304 LEU GLY LEU ILE PRO LEU VAL SER GLU ASP VAL GLU GLU
SEQRES 7 C 304 MET LYS TYR SER ARG ASP CYS THR CYS GLU ASP TYR CYS
SEQRES 8 C 304 ASP GLU CYS SER VAL VAL LEU GLU LEU SER ALA ARG HIS
SEQRES 9 C 304 GLU GLY GLU GLU GLY THR THR ASP VAL TYR SER SER SER
SEQRES 10 C 304 LEU ILE LYS VAL SER GLY PRO GLY ASN LEU ASN VAL GLY
SEQRES 11 C 304 GLU PRO VAL ARG ARG ASP ASP TYR ASP GLN GLY ILE LEU
SEQRES 12 C 304 LEU CYS LYS LEU ARG ASN HIS GLN GLU LEU ASN ILE ARG
SEQRES 13 C 304 CYS ILE ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES 14 C 304 TRP SER PRO CYS SER ALA ILE ALA PHE GLU TYR ASP PRO
SEQRES 15 C 304 HIS ASN LYS LEU LYS HIS THR ASP PHE TRP PHE GLU VAL
SEQRES 16 C 304 ASP ALA LYS LYS GLU TRP PRO ASP SER LYS TYR ALA THR
SEQRES 17 C 304 TRP GLU GLU PRO PRO LYS PRO GLY GLU VAL PHE ASP TYR
SEQRES 18 C 304 LYS ALA LYS PRO ASN ARG PHE TYR MET THR VAL GLU THR
SEQRES 19 C 304 THR GLY SER LEU LYS ALA ASN GLN VAL PHE SER ARG GLY
SEQRES 20 C 304 ILE LYS THR LEU GLN GLU LYS LEU ALA ASN VAL LEU PHE
SEQRES 21 C 304 GLU LEU GLU ASN SER ARG PRO ALA ASN THR THR ALA TYR
SEQRES 22 C 304 GLY GLY ALA THR ALA TYR GLY GLY GLN THR VAL TYR GLY
SEQRES 23 C 304 ARG GLU THR SER TYR GLY GLY ASN THR ASN TYR GLY ASP
SEQRES 24 C 304 TYR ASN ALA PRO TYR
SEQRES 1 D 186 MET ASN VAL SER THR SER THR VAL GLY ALA ARG ARG ARG
SEQRES 2 D 186 ARG ALA LYS GLN GLN VAL ASP ASP GLU GLU ASN ALA THR
SEQRES 3 D 186 LEU LEU ARG LEU GLY PRO GLU PHE ALA LEU LYS GLN TYR
SEQRES 4 D 186 ASP HIS ASP GLY ASN GLU HIS ASP LEU ILE ALA LEU SER
SEQRES 5 D 186 LEU SER GLU SER ARG LEU LEU ILE ARG GLU ALA LEU LYS
SEQRES 6 D 186 ALA ARG SER ARG ALA ARG ASN GLY GLY VAL ASP ILE GLU
SEQRES 7 D 186 SER SER ASN GLY GLU ILE ASP ASP ASP GLU LEU ALA LYS
SEQRES 8 D 186 VAL THR SER GLY ALA VAL ALA ASN GLY VAL VAL LYS LYS
SEQRES 9 D 186 THR LEU ASP TYR LEU ASN THR PHE ALA ARG PHE LYS ASP
SEQRES 10 D 186 GLU GLU THR CYS THR ALA VAL ASP GLN LEU LEU HIS ASN
SEQRES 11 D 186 SER SER ASP CYS SER VAL LEU HIS PRO PHE GLU ILE ALA
SEQRES 12 D 186 GLN LEU SER SER LEU GLY CYS GLU ASP VAL ASP GLU ALA
SEQRES 13 D 186 ILE THR LEU ILE PRO SER LEU ALA ALA LYS LYS GLU VAL
SEQRES 14 D 186 ASN LEU GLN ARG ILE LEU ASP GLU LEU ASN ARG LEU GLU
SEQRES 15 D 186 ASP PRO TYR LYS
SEQRES 1 E 214 MET GLU ASP ASN ASN ARG ILE ILE SER ARG LEU TRP ARG
SEQRES 2 E 214 SER PHE ARG THR VAL LYS GLU MET ALA ALA ASP ARG GLY
SEQRES 3 E 214 TYR PHE ILE SER GLN GLU GLU MET ASP GLN SER LEU GLU
SEQRES 4 E 214 GLU PHE ARG SER LYS ILE CYS ASP SER MET GLY ASN PRO
SEQRES 5 E 214 GLN ARG LYS LEU MET SER PHE LEU ALA ASN PRO THR PRO
SEQRES 6 E 214 GLU ALA LEU GLU LYS TYR SER ASP LEU GLY THR LEU TRP
SEQRES 7 E 214 VAL GLU PHE CYS ASP GLU PRO SER VAL GLY ILE LYS THR
SEQRES 8 E 214 MET ARG ASN PHE CYS LEU ARG ILE GLN GLU LYS ASN PHE
SEQRES 9 E 214 SER THR GLY ILE PHE ILE TYR GLN ASN ASN ILE THR PRO
SEQRES 10 E 214 SER ALA ASN LYS MET ILE PRO THR VAL SER PRO ALA ILE
SEQRES 11 E 214 ILE GLU THR PHE GLN GLU SER ASP LEU VAL VAL ASN ILE
SEQRES 12 E 214 THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU SER
SEQRES 13 E 214 ASP GLY GLU LYS SER GLN LEU LEU GLN ARG TYR LYS LEU
SEQRES 14 E 214 LYS GLU SER GLN LEU PRO ARG ILE GLN ARG GLU ASP PRO
SEQRES 15 E 214 VAL ALA ARG TYR LEU GLY LEU LYS ARG GLY GLN VAL VAL
SEQRES 16 E 214 LYS ILE ILE ARG ARG SER GLU THR SER GLY ARG TYR ALA
SEQRES 17 E 214 SER TYR ARG ILE CYS LEU
SEQRES 1 F 155 MET SER GLU ASP GLU ALA PHE ASN GLU GLN THR GLU ASN
SEQRES 2 F 155 PHE GLU ASN PHE GLU ASP GLU HIS PHE SER ASP ASP ASN
SEQRES 3 F 155 PHE GLU ASP ARG SER THR GLN PRO GLU ASP TYR ALA VAL
SEQRES 4 F 155 GLY VAL THR ALA ASP GLY ARG GLN ILE ILE ASN GLY ASP
SEQRES 5 F 155 GLY ILE GLN GLU VAL ASN GLY THR ILE LYS ALA HIS ARG
SEQRES 6 F 155 LYS ARG SER ASN LYS GLU LEU ALA ILE LEU LYS GLU GLU
SEQRES 7 F 155 ARG THR THR THR PRO TYR LEU 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 LEU VAL ASP ILE GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU GLN ILE ALA MET LYS GLU LEU SER GLN ARG LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER TYR
SEQRES 12 F 155 GLU ASP TRP GLY CYS ASP GLU LEU ILE VAL ASP ASN
SEQRES 1 G 171 MET PHE PHE LEU LYS ASP LEU SER LEU ILE LEU THR LEU
SEQRES 2 G 171 HIS PRO SER TYR PHE GLY PRO GLN MET ASN GLN TYR LEU
SEQRES 3 G 171 ARG GLU LYS LEU LEU THR ASP VAL GLU GLY THR CYS THR
SEQRES 4 G 171 GLY GLN PHE GLY TYR ILE VAL THR VAL LEU ASP GLY MET
SEQRES 5 G 171 ASN ILE ASP VAL GLY LYS GLY ARG ILE ILE PRO GLY SER
SEQRES 6 G 171 GLY SER ALA GLU PHE GLU VAL LYS TYR ARG ALA VAL VAL
SEQRES 7 G 171 TRP LYS PRO PHE LYS GLY GLU VAL VAL ASP ALA ILE VAL
SEQRES 8 G 171 SER ASN VAL SER PRO ILE GLY PHE PHE ALA ASP VAL GLY
SEQRES 9 G 171 PRO LEU ASN VAL PHE VAL SER THR ARG LEU ILE PRO ASP
SEQRES 10 G 171 ASN LEU VAL TYR ASN PRO SER ASN SER PRO PRO ALA TYR
SEQRES 11 G 171 MET SER ASN ASP GLU LEU ILE THR LYS GLY SER LYS VAL
SEQRES 12 G 171 ARG LEU LYS VAL VAL GLY THR ARG THR ASP VAL ASN GLU
SEQRES 13 G 171 ILE TYR ALA ILE GLY SER ILE LYS GLU ASP PHE LEU GLY
SEQRES 14 G 171 ALA ILE
SEQRES 1 H 145 MET SER SER ALA LEU PHE ASP ASP ILE PHE THR VAL GLN
SEQRES 2 H 145 THR VAL ASP ASN GLY ARG TYR ASN LYS VAL SER ARG ILE
SEQRES 3 H 145 ILE GLY ILE SER THR THR ASN SER ALA ILE LYS LEU THR
SEQRES 4 H 145 LEU ASP ILE ASN ASN GLU MET PHE PRO VAL SER GLN ASP
SEQRES 5 H 145 ASP SER LEU THR VAL THR LEU ALA ASN SER LEU SER LEU
SEQRES 6 H 145 ASP GLY GLU ASP GLU SER ALA ASN PHE SER LYS SER TRP
SEQRES 7 H 145 ARG PRO PRO LYS PRO THR ASP LYS SER LEU ALA ASP ASP
SEQRES 8 H 145 TYR ASP TYR VAL MET PHE GLY THR VAL TYR LYS PHE GLU
SEQRES 9 H 145 GLU GLY ASP GLU ASP LYS ILE LYS VAL TYR VAL SER PHE
SEQRES 10 H 145 GLY GLY LEU LEU MET CYS LEU GLU GLY GLY TYR LYS SER
SEQRES 11 H 145 LEU ALA SER LEU LYS GLN ASP ASN LEU TYR ILE LEU ILE
SEQRES 12 H 145 ARG ARG
SEQRES 1 I 115 MET ALA SER PHE ARG PHE CYS LEU GLU CYS ASN ASN MET
SEQRES 2 I 115 LEU TYR PRO LYS GLU ASP LYS GLU ASN GLN ARG LEU LEU
SEQRES 3 I 115 TYR SER CYS ARG ASN CYS ASP TYR THR GLU LEU ALA GLU
SEQRES 4 I 115 ASP PRO LYS VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 115 GLY GLU THR ALA GLY ILE VAL ASP ASP ILE GLY GLN ASP
SEQRES 6 I 115 PRO THR LEU PRO ARG SER ASP LYS GLU CYS PRO GLU CYS
SEQRES 7 I 115 HIS SER ARG ASP CYS VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 115 ARG LYS ASP THR ASN MET THR LEU PHE TYR VAL CYS LEU
SEQRES 9 I 115 ASN CYS LYS LYS THR PHE ARG ASP GLU SER GLU
SEQRES 1 J 72 MET ILE ILE PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 72 VAL GLY ASP LYS TRP ASP ALA TYR LEU ARG LEU LEU GLU
SEQRES 3 J 72 GLU GLY LYS GLN GLU GLY ASP ALA LEU ASP GLU LEU LYS
SEQRES 4 J 72 LEU LYS ARG TYR CYS CYS ARG ARG MET VAL LEU THR HIS
SEQRES 5 J 72 VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO LEU
SEQRES 6 J 72 GLU LYS LYS ASP PHE ASP SER
SEQRES 1 K 118 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE ILE LEU PRO
SEQRES 2 K 118 ASP ASP VAL PRO LYS LEU LYS ILE THR PRO ASP SER ARG
SEQRES 3 K 118 VAL PRO ASN CYS ILE ILE ILE LYS PHE GLU ARG GLU ASP
SEQRES 4 K 118 HIS THR LEU ALA ASN LEU LEU ARG GLU GLU LEU ALA LEU
SEQRES 5 K 118 TYR PRO ASP VAL THR PHE VAL ALA TYR LYS VAL GLU HIS
SEQRES 6 K 118 PRO LEU PHE ALA ASN PHE VAL MET ARG LEU GLN THR GLU
SEQRES 7 K 118 GLU GLY THR ARG PRO LYS GLN ALA LEU GLU ARG ALA CYS
SEQRES 8 K 118 ALA SER ILE ILE ASN LYS LEU LYS THR LEU ASP HIS LYS
SEQRES 9 K 118 PHE ASN GLU GLU TRP ASN ILE LYS ASN PHE SER LEU ASN
SEQRES 10 K 118 ASP
SEQRES 1 L 72 MET SER ARG GLU GLY PHE VAL ALA PRO SER GLY THR ASP
SEQRES 2 L 72 LEU ALA ALA ALA ALA SER GLY VAL ALA PRO ASN LYS HIS
SEQRES 3 L 72 TYR GLY VAL LYS TYR THR CYS GLY ALA CYS ALA HIS ASN
SEQRES 4 L 72 PHE SER LEU ASN LYS SER ASP PRO VAL ARG CYS LYS GLU
SEQRES 5 L 72 CYS GLY HIS ARG VAL ILE TYR LYS ALA ARG THR LYS ARG
SEQRES 6 L 72 MET ILE GLN PHE ASP ALA ARG
SEQRES 1 P 11 G G U G U C U U G G G
SEQRES 1 T 198 DA DT DC DA DG DA DA DT DC DC DC DG DG
SEQRES 2 T 198 DT DG DC DC DG DA DG DG DC DC DG DC DT
SEQRES 3 T 198 DC DA DA DT DT DG DG DT DC DG DT DA DG
SEQRES 4 T 198 DA DC DA DG DC DT DC DT DA DG DC DA DC
SEQRES 5 T 198 DC DG DC DT DT DA DA DA DC DG DC DA DC
SEQRES 6 T 198 DG DT DA DC DG DC DG DC DT DG DT DC DC
SEQRES 7 T 198 DC DC DC DG DC DG DT DT DT DT DA DA DC
SEQRES 8 T 198 DC DG DC DC DA DA DG DG DG DG DA DT DT
SEQRES 9 T 198 DA DC DA DC DC DC DA DA DG DA DC DA DC
SEQRES 10 T 198 DC DA DG DG DC DA DC DG DA DG DA DC DA
SEQRES 11 T 198 DG DA DA DA DA DA DA DA DC DA DA DC DG
SEQRES 12 T 198 DA DA DA DA DC DG DG DC DC DA DC DC DA
SEQRES 13 T 198 DC DC DC DA DA DA DC DA DC DA DC DC DA
SEQRES 14 T 198 DA DA DC DA DC DA DA DG DA DG DC DT DA
SEQRES 15 T 198 DA DT DT DG DA DC DT DG DA DC DG DT DA
SEQRES 16 T 198 DA DG DC
SEQRES 1 N 198 DG DC DT DT DA DC DG DT DC DA DG DT DC
SEQRES 2 N 198 DT DG DG DC DC DA DT DC DT DT DT DG DT
SEQRES 3 N 198 DG DT DT DT DG DG DT DG DT DG DT DT DT
SEQRES 4 N 198 DG DG DG DT DG DG DT DG DG DC DC DG DT
SEQRES 5 N 198 DT DT DT DC DG DT DT DG DT DT DT DT DT
SEQRES 6 N 198 DT DT DC DT DG DT DC DT DC DG DT DG DC
SEQRES 7 N 198 DC DT DG DG DT DG DT DC DT DT DG DG DG
SEQRES 8 N 198 DT DG DT DA DA DT DC DC DC DC DT DT DG
SEQRES 9 N 198 DG DC DG DG DT DT DA DA DA DA DC DG DC
SEQRES 10 N 198 DG DG DG DG DG DA DC DA DG DC DG DC DG
SEQRES 11 N 198 DT DA DC DG DT DG DC DG DT DT DT DA DA
SEQRES 12 N 198 DG DC DG DG DT DG DC DT DA DG DA DG DC
SEQRES 13 N 198 DT DG DT DC DT DA DC DG DA DC DC DA DA
SEQRES 14 N 198 DT DT DG DA DG DC DG DG DC DC DT DC DG
SEQRES 15 N 198 DG DC DA DC DC DG DG DG DA DT DT DC DT
SEQRES 16 N 198 DG DA DT
SEQRES 1 a 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 a 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 a 139 LYS ALA ALA ARG LYS SER ALA PRO SER THR GLY GLY VAL
SEQRES 4 a 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 a 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 a 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 a 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER ALA
SEQRES 8 a 139 ALA ILE GLY ALA LEU GLN GLU ALA SER GLU ALA TYR LEU
SEQRES 9 a 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 a 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 a 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 b 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 b 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 b 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 b 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 b 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 b 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 b 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 b 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 b 106 GLY GLY
SEQRES 1 c 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 c 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 c 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 c 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 c 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 c 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 c 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 c 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 c 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 c 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 c 133 LYS GLY LYS
SEQRES 1 d 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 d 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 d 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 d 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 d 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 d 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 d 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 d 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 d 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 d 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 e 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 e 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 e 139 LYS ALA ALA ARG LYS SER ALA PRO SER THR GLY GLY VAL
SEQRES 4 e 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 e 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 e 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 e 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER ALA
SEQRES 8 e 139 ALA ILE GLY ALA LEU GLN GLU ALA SER GLU ALA TYR LEU
SEQRES 9 e 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 e 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 e 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 f 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 f 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 f 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 f 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 f 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 f 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 f 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 f 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 f 106 GLY GLY
SEQRES 1 g 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 g 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 g 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 g 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 g 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 g 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 g 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 g 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 g 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 g 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 g 133 LYS GLY LYS
SEQRES 1 h 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 h 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 h 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 h 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 h 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 h 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 h 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 h 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 h 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 h 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 0 42 DG DG DG DG DA DT DT DA DC DA DC DC DC
SEQRES 2 0 42 DA DA DG DA DC DA DC DC DA DG DG DC DA
SEQRES 3 0 42 DC DG DA DG DA DC DA DG DA DA DA DA DA
SEQRES 4 0 42 DA DA DC
SEQRES 1 1 42 DG DT DT DT DT DT DT DT DC DT DG DT DC
SEQRES 2 1 42 DT DC DG DT DG DC DC DT DG DG DT DG DT
SEQRES 3 1 42 DC DT DT DG DG DG DT DG DT DA DA DT DC
SEQRES 4 1 42 DC DC DC
HET ZN A1801 1
HET ZN A1802 1
HET MG A1803 1
HET ZN B1301 1
HET ZN C 401 1
HET ZN I 201 1
HET ZN I 202 1
HET ZN J 101 1
HET ZN L 101 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 26 ZN 8(ZN 2+)
FORMUL 28 MG MG 2+
HELIX 1 AA1 SER A 23 SER A 31 1 9
HELIX 2 AA2 PHE A 95 ILE A 106 1 12
HELIX 3 AA3 ASN A 119 ILE A 126 1 8
HELIX 4 AA4 ASP A 130 LYS A 143 1 14
HELIX 5 AA5 THR A 204 LYS A 213 1 10
HELIX 6 AA6 SER A 216 LEU A 223 1 8
HELIX 7 AA7 PRO A 244 ARG A 248 5 5
HELIX 8 AA8 ASP A 261 LYS A 279 1 19
HELIX 9 AA9 LEU A 280 ASP A 283 5 4
HELIX 10 AB1 HIS A 288 ASP A 306 1 19
HELIX 11 AB2 PRO A 368 LEU A 375 1 8
HELIX 12 AB3 ASN A 385 GLY A 396 1 12
HELIX 13 AB4 ARG A 421 ILE A 425 5 5
HELIX 14 AB5 SER A 495 CYS A 506 1 12
HELIX 15 AB6 ALA A 507 GLN A 511 5 5
HELIX 16 AB7 VAL A 525 MET A 535 1 11
HELIX 17 AB8 GLU A 543 LEU A 551 1 9
HELIX 18 AB9 THR A 574 ILE A 583 1 10
HELIX 19 AC1 ASP A 619 GLY A 624 1 6
HELIX 20 AC2 GLY A 629 GLY A 639 1 11
HELIX 21 AC3 GLY A 639 GLY A 662 1 24
HELIX 22 AC4 GLY A 666 ILE A 671 5 6
HELIX 23 AC5 ASP A 673 GLN A 699 1 27
HELIX 24 AC6 THR A 710 LEU A 738 1 29
HELIX 25 AC7 ASN A 742 GLY A 751 1 10
HELIX 26 AC8 SER A 755 SER A 763 1 9
HELIX 27 AC9 SER A 804 GLY A 808 5 5
HELIX 28 AD1 THR A 810 GLU A 847 1 38
HELIX 29 AD2 LEU A 868 ASP A 872 5 5
HELIX 30 AD3 SER A 890 TYR A 899 1 10
HELIX 31 AD4 LYS A 910 ILE A 914 5 5
HELIX 32 AD5 VAL A 924 ILE A 947 1 24
HELIX 33 AD6 ASN A 961 PHE A 973 1 13
HELIX 34 AD7 THR A 984 CYS A 996 1 13
HELIX 35 AD8 ASN A 1006 THR A 1017 1 12
HELIX 36 AD9 THR A 1017 LEU A 1028 1 12
HELIX 37 AE1 ALA A 1029 GLU A 1036 1 8
HELIX 38 AE2 ARG A 1041 SER A 1058 1 18
HELIX 39 AE3 MET A 1065 GLN A 1080 1 16
HELIX 40 AE4 GLY A 1099 ASN A 1108 1 10
HELIX 41 AE5 ASP A 1123 LEU A 1128 1 6
HELIX 42 AE6 ILE A 1130 GLU A 1141 1 12
HELIX 43 AE7 ASP A 1168 SER A 1177 1 10
HELIX 44 AE8 ASP A 1200 LYS A 1207 1 8
HELIX 45 AE9 THR A 1210 PHE A 1222 1 13
HELIX 46 AF1 GLU A 1259 ILE A 1274 1 16
HELIX 47 AF2 ASN A 1315 MET A 1320 1 6
HELIX 48 AF3 PHE A 1335 GLY A 1343 1 9
HELIX 49 AF4 ILE A 1344 ALA A 1360 1 17
HELIX 50 AF5 ASN A 1367 MET A 1378 1 12
HELIX 51 AF6 THR A 1388 ARG A 1394 1 7
HELIX 52 AF7 ALA A 1399 SER A 1404 1 6
HELIX 53 AF8 GLU A 1407 ALA A 1417 1 11
HELIX 54 AF9 GLY A 1426 LEU A 1433 1 8
HELIX 55 AG1 MET A 1439 GLY A 1442 5 4
HELIX 56 AG2 ASP A 1449 LEU A 1456 1 8
HELIX 57 AG3 THR B 13 LYS B 28 1 16
HELIX 58 AG4 VAL B 31 SER B 45 1 15
HELIX 59 AG5 ILE B 46 TRP B 51 1 6
HELIX 60 AG6 PHE B 100 ARG B 107 1 8
HELIX 61 AG7 ASP B 176 MET B 183 1 8
HELIX 62 AG8 ILE B 274 LEU B 281 1 8
HELIX 63 AG9 PRO B 285 CYS B 294 1 10
HELIX 64 AH1 ASP B 299 PHE B 314 1 16
HELIX 65 AH2 ASP B 318 ARG B 328 1 11
HELIX 66 AH3 ARG B 337 LEU B 349 1 13
HELIX 67 AH4 PHE B 363 LEU B 383 1 21
HELIX 68 AH5 HIS B 393 GLY B 395 5 3
HELIX 69 AH6 LEU B 401 ILE B 429 1 29
HELIX 70 AH7 SER B 443 THR B 456 1 14
HELIX 71 AH8 GLU B 461 ALA B 465 5 5
HELIX 72 AH9 THR B 480 HIS B 487 1 8
HELIX 73 AI1 PRO B 543 GLU B 553 1 11
HELIX 74 AI2 GLU B 560 TYR B 562 5 3
HELIX 75 AI3 PRO B 586 GLY B 600 1 15
HELIX 76 AI4 THR B 648 GLY B 658 1 11
HELIX 77 AI5 GLY B 677 GLY B 685 1 9
HELIX 78 AI6 GLU B 693 THR B 697 5 5
HELIX 79 AI7 THR B 703 LEU B 707 5 5
HELIX 80 AI8 HIS B 744 LEU B 749 5 6
HELIX 81 AI9 GLN B 763 ALA B 772 1 10
HELIX 82 AJ1 MET B 773 ALA B 777 5 5
HELIX 83 AJ2 GLN B 843 ARG B 848 1 6
HELIX 84 AJ3 ASN B 1013 ILE B 1017 5 5
HELIX 85 AJ4 THR B 1022 GLY B 1039 1 18
HELIX 86 AJ5 VAL B 1052 ASN B 1062 1 11
HELIX 87 AJ6 MET B 1098 LYS B 1102 5 5
HELIX 88 AJ7 GLY B 1131 HIS B 1141 1 11
HELIX 89 AJ8 ALA B 1143 MET B 1152 1 10
HELIX 90 AJ9 TYR B 1198 MET B 1210 1 13
HELIX 91 AK1 ASN C 25 ALA C 38 1 14
HELIX 92 AK2 ALA C 58 GLY C 67 1 10
HELIX 93 AK3 ASP C 75 MET C 79 5 5
HELIX 94 AK4 TYR C 81 CYS C 85 5 5
HELIX 95 AK5 ASP C 196 TRP C 201 1 6
HELIX 96 AK6 LYS C 239 ARG C 266 1 28
HELIX 97 AK7 SER D 52 GLY D 73 1 22
HELIX 98 AK8 GLU D 88 THR D 93 5 6
HELIX 99 AK9 GLY D 95 THR D 111 1 17
HELIX 100 AL1 GLU D 118 LEU D 128 1 11
HELIX 101 AL2 HIS D 138 SER D 146 1 9
HELIX 102 AL3 ASP D 152 ILE D 160 1 9
HELIX 103 AL4 PRO D 161 ALA D 164 5 4
HELIX 104 AL5 ASN D 170 GLU D 182 1 13
HELIX 105 AL6 ASP E 3 ARG E 25 1 23
HELIX 106 AL7 SER E 30 ASP E 35 1 6
HELIX 107 AL8 LEU E 38 ILE E 45 1 8
HELIX 108 AL9 GLN E 53 SER E 58 5 6
HELIX 109 AM1 THR E 64 TYR E 71 1 8
HELIX 110 AM2 GLY E 88 LYS E 102 1 15
HELIX 111 AM3 THR E 116 LYS E 121 1 6
HELIX 112 AM4 MET E 122 SER E 127 5 6
HELIX 113 AM5 SER E 137 LEU E 139 5 3
HELIX 114 AM6 ASN E 142 HIS E 146 5 5
HELIX 115 AM7 SER E 156 LYS E 168 1 13
HELIX 116 AM8 ASP E 181 LEU E 187 1 7
HELIX 117 AM9 THR F 86 MET F 103 1 18
HELIX 118 AN1 ASP F 116 ARG F 128 1 13
HELIX 119 AN2 HIS G 14 PHE G 18 5 5
HELIX 120 AN3 GLN G 21 GLU G 35 1 15
HELIX 121 AN4 ASP G 50 ILE G 54 5 5
HELIX 122 AN5 ARG G 113 ILE G 115 5 3
HELIX 123 AN6 LEU H 88 TYR H 92 5 5
HELIX 124 AN7 GLY H 127 ALA H 132 1 6
HELIX 125 AN8 SER H 133 LYS H 135 5 3
HELIX 126 AN9 LYS J 17 GLU J 26 1 10
HELIX 127 AO1 GLN J 30 LEU J 38 1 9
HELIX 128 AO2 ARG J 42 THR J 51 1 10
HELIX 129 AO3 ILE J 56 ARG J 61 1 6
HELIX 130 AO4 ASP K 39 ALA K 51 1 13
HELIX 131 AO5 ARG K 82 ASN K 113 1 32
HELIX 132 AO6 GLY a 44 SER a 57 1 14
HELIX 133 AO7 ARG a 63 GLN a 76 1 14
HELIX 134 AO8 GLN a 85 ALA a 114 1 30
HELIX 135 AO9 MET a 120 ARG a 131 1 12
HELIX 136 AP1 ASP b 24 ILE b 29 5 6
HELIX 137 AP2 THR b 30 GLY b 41 1 12
HELIX 138 AP3 ILE b 50 LYS b 77 1 28
HELIX 139 AP4 THR b 82 GLY b 94 1 13
HELIX 140 AP5 ARG c 17 ALA c 21 1 5
HELIX 141 AP6 PRO c 26 LYS c 36 1 11
HELIX 142 AP7 GLY c 46 LYS c 74 1 29
HELIX 143 AP8 ILE c 79 ASP c 90 1 12
HELIX 144 AP9 ASP c 90 LEU c 97 1 8
HELIX 145 AQ1 GLN c 112 LEU c 116 5 5
HELIX 146 AQ2 TYR d 34 HIS d 46 1 13
HELIX 147 AQ3 SER d 52 TYR d 80 1 29
HELIX 148 AQ4 THR d 87 LEU d 99 1 13
HELIX 149 AQ5 PRO d 100 ALA d 121 1 22
HELIX 150 AQ6 GLY e 44 GLN e 55 1 12
HELIX 151 AQ7 ARG e 63 GLN e 76 1 14
HELIX 152 AQ8 GLN e 85 ALA e 114 1 30
HELIX 153 AQ9 MET e 120 GLY e 132 1 13
HELIX 154 AR1 ASN f 25 ILE f 29 5 5
HELIX 155 AR2 THR f 30 GLY f 42 1 13
HELIX 156 AR3 LEU f 49 LYS f 77 1 29
HELIX 157 AR4 THR f 82 GLN f 93 1 12
HELIX 158 AR5 THR g 16 GLY g 22 1 7
HELIX 159 AR6 PRO g 26 LYS g 36 1 11
HELIX 160 AR7 ALA g 45 ASP g 72 1 28
HELIX 161 AR8 ILE g 79 ASP g 90 1 12
HELIX 162 AR9 GLU g 91 LEU g 97 1 7
HELIX 163 AS1 TYR h 34 HIS h 46 1 13
HELIX 164 AS2 SER h 52 LYS h 82 1 31
HELIX 165 AS3 THR h 87 LEU h 99 1 13
HELIX 166 AS4 PRO h 100 ALA h 121 1 22
SHEET 1 AA1 3 LEU A1421 ASP A1422 0
SHEET 2 AA1 3 GLU A 16 GLN A 18 -1 N VAL A 17 O ASP A1422
SHEET 3 AA1 3 ARG B1215 TYR B1217 -1 O TYR B1217 N GLU A 16
SHEET 1 AA2 2 GLY A 82 HIS A 83 0
SHEET 2 AA2 2 PRO A 241 VAL A 242 -1 O VAL A 242 N GLY A 82
SHEET 1 AA3 2 VAL A 90 PHE A 91 0
SHEET 2 AA3 2 ILE A 236 ILE A 237 -1 O ILE A 237 N VAL A 90
SHEET 1 AA4 3 VAL A 174 ASP A 178 0
SHEET 2 AA4 3 LYS A 181 THR A 185 -1 O TRP A 183 N ARG A 176
SHEET 3 AA4 3 LYS A 201 LEU A 202 -1 O LYS A 201 N GLY A 184
SHEET 1 AA5 2 ILE A 251 ALA A 252 0
SHEET 2 AA5 2 GLN A 258 GLY A 259 -1 O GLY A 259 N ILE A 251
SHEET 1 AA6 2 ARG A 345 VAL A 346 0
SHEET 2 AA6 2 LEU B1128 ARG B1129 -1 O LEU B1128 N VAL A 346
SHEET 1 AA7 2 ILE A 354 GLY A 356 0
SHEET 2 AA7 2 PHE A 469 LEU A 471 1 O PHE A 469 N SER A 355
SHEET 1 AA8 2 VAL A 365 VAL A 367 0
SHEET 2 AA8 2 VAL A 461 VAL A 463 1 O LYS A 462 N VAL A 365
SHEET 1 AA9 4 TYR A 377 THR A 380 0
SHEET 2 AA9 4 LYS A 432 ARG A 435 -1 O ARG A 435 N TYR A 377
SHEET 3 AA9 4 ALA A 403 ILE A 407 -1 N ILE A 407 O LYS A 432
SHEET 4 AA9 4 ARG A 413 ASP A 415 -1 O ILE A 414 N VAL A 406
SHEET 1 AB1 2 VAL A 513 SER A 514 0
SHEET 2 AB1 2 LYS A 519 PRO A 520 -1 O LYS A 519 N SER A 514
SHEET 1 AB2 3 HIS A 588 ARG A 591 0
SHEET 2 AB2 3 MET A 606 VAL A 609 -1 O MET A 606 N ARG A 591
SHEET 3 AB2 3 LYS A 612 PHE A 615 -1 O LYS A 612 N VAL A 609
SHEET 1 AB3 2 GLY A 767 GLN A 768 0
SHEET 2 AB3 2 PHE A 800 VAL A 801 -1 O VAL A 801 N GLY A 767
SHEET 1 AB4 2 MET A 850 VAL A 851 0
SHEET 2 AB4 2 THR A 857 ARG A 858 -1 O ARG A 858 N MET A 850
SHEET 1 AB5 2 GLU A 880 THR A 883 0
SHEET 2 AB5 2 ASN A 955 LEU A 958 -1 O TRP A 956 N GLN A 882
SHEET 1 AB6 4 VAL A1285 VAL A1288 0
SHEET 2 AB6 4 ALA A1308 ASP A1312 -1 O GLU A1310 N TYR A1286
SHEET 3 AB6 4 ALA A1117 VAL A1120 -1 N VAL A1120 O LEU A1309
SHEET 4 AB6 4 TYR A1331 SER A1332 -1 O TYR A1331 N THR A1119
SHEET 1 AB7 2 THR A1143 THR A1144 0
SHEET 2 AB7 2 ALA A1275 ARG A1277 -1 O LEU A1276 N THR A1143
SHEET 1 AB8 5 LEU A1226 TRP A1230 0
SHEET 2 AB8 5 LEU A1238 VAL A1244 -1 O ARG A1241 N MET A1229
SHEET 3 AB8 5 TRP A1193 LEU A1199 -1 N LEU A1195 O CYS A1242
SHEET 4 AB8 5 THR A1149 TYR A1156 -1 N SER A1150 O GLU A1198
SHEET 5 AB8 5 TYR I 44 GLU I 47 -1 O TYR I 44 N ILE A1154
SHEET 1 AB9 2 VAL A1292 PRO A1295 0
SHEET 2 AB9 2 TYR A1301 GLU A1304 -1 O LYS A1302 N VAL A1294
SHEET 1 AC1 6 TYR F 143 GLY F 147 0
SHEET 2 AC1 6 VAL F 133 TYR F 137 -1 N ILE F 134 O TRP F 146
SHEET 3 AC1 6 PHE A1444 ILE A1448 -1 N MET A1447 O VAL F 133
SHEET 4 AC1 6 GLY G 59 ILE G 61 -1 O ILE G 61 N VAL A1446
SHEET 5 AC1 6 ALA G 68 TRP G 79 -1 O GLU G 69 N ARG G 60
SHEET 6 AC1 6 PHE G 2 LEU G 13 -1 N PHE G 3 O VAL G 78
SHEET 1 AC2 7 TYR F 143 GLY F 147 0
SHEET 2 AC2 7 VAL F 133 TYR F 137 -1 N ILE F 134 O TRP F 146
SHEET 3 AC2 7 PHE A1444 ILE A1448 -1 N MET A1447 O VAL F 133
SHEET 4 AC2 7 GLY G 59 ILE G 61 -1 O ILE G 61 N VAL A1446
SHEET 5 AC2 7 ALA G 68 TRP G 79 -1 O GLU G 69 N ARG G 60
SHEET 6 AC2 7 GLY G 43 VAL G 48 -1 N TYR G 44 O TRP G 79
SHEET 7 AC2 7 CYS G 38 THR G 39 -1 N THR G 39 O GLY G 43
SHEET 1 AC3 4 ARG B 55 GLN B 60 0
SHEET 2 AC3 4 LYS B 73 LEU B 84 -1 O LYS B 73 N GLN B 60
SHEET 3 AC3 4 SER B 113 PHE B 124 -1 O GLU B 120 N ARG B 78
SHEET 4 AC3 4 LYS B 155 VAL B 161 -1 O VAL B 156 N LEU B 117
SHEET 1 AC4 2 MET B 89 THR B 90 0
SHEET 2 AC4 2 THR B 96 HIS B 97 -1 O HIS B 97 N MET B 89
SHEET 1 AC5 3 PHE B 194 ILE B 196 0
SHEET 2 AC5 3 SER B 199 LEU B 203 -1 O LYS B 201 N PHE B 194
SHEET 3 AC5 3 SER B 473 GLN B 474 -1 O GLN B 474 N VAL B 202
SHEET 1 AC6 2 GLN B 206 SER B 209 0
SHEET 2 AC6 2 LYS B 397 ASP B 400 -1 O ASP B 400 N GLN B 206
SHEET 1 AC7 5 GLN B 215 PHE B 217 0
SHEET 2 AC7 5 ILE B 225 GLU B 230 -1 O VAL B 228 N PHE B 217
SHEET 3 AC7 5 GLN B 246 TYR B 250 -1 O LEU B 249 N SER B 226
SHEET 4 AC7 5 ILE B 261 THR B 264 -1 O LYS B 262 N LYS B 248
SHEET 5 AC7 5 ILE B 272 PRO B 273 -1 O ILE B 272 N ALA B 263
SHEET 1 AC8 2 ALA B 234 LEU B 235 0
SHEET 2 AC8 2 ARG B 240 LEU B 241 -1 O ARG B 240 N LEU B 235
SHEET 1 AC9 3 GLY B 537 ILE B 538 0
SHEET 2 AC9 3 VAL B 626 PHE B 631 -1 O TYR B 627 N GLY B 537
SHEET 3 AC9 3 ILE B 687 ASP B 691 -1 O VAL B 690 N ARG B 628
SHEET 1 AD1 5 GLU B 557 PRO B 558 0
SHEET 2 AD1 5 GLY B 581 HIS B 583 -1 O ILE B 582 N GLU B 557
SHEET 3 AD1 5 THR B 571 ILE B 573 -1 N THR B 571 O HIS B 583
SHEET 4 AD1 5 GLU B 616 PHE B 620 1 O PHE B 617 N ARG B 572
SHEET 5 AD1 5 SER B 607 ASP B 611 -1 N ILE B 609 O LYS B 618
SHEET 1 AD2 2 ILE B 700 ALA B 701 0
SHEET 2 AD2 2 HIS B 740 CYS B 741 1 O HIS B 740 N ALA B 701
SHEET 1 AD3 2 GLN B 821 VAL B 825 0
SHEET 2 AD3 2 GLY B1088 TYR B1092 -1 O THR B1090 N ALA B 823
SHEET 1 AD4 3 MET B 839 ASN B 842 0
SHEET 2 AD4 3 GLY B 988 TYR B 994 1 O GLY B 991 N MET B 839
SHEET 3 AD4 3 LYS B 979 PHE B 980 -1 N PHE B 980 O GLY B 988
SHEET 1 AD5 4 SER B 853 ASP B 861 0
SHEET 2 AD5 4 LYS B 962 LYS B 972 -1 O MET B 968 N ARG B 857
SHEET 3 AD5 4 GLY B 947 VAL B 949 -1 N ILE B 948 O ARG B 969
SHEET 4 AD5 4 ARG B 904 VAL B 905 -1 N VAL B 905 O GLY B 947
SHEET 1 AD6 5 SER B 853 ASP B 861 0
SHEET 2 AD6 5 LYS B 962 LYS B 972 -1 O MET B 968 N ARG B 857
SHEET 3 AD6 5 LEU B 953 THR B 956 -1 N THR B 955 O PHE B 963
SHEET 4 AD6 5 ILE L 58 LYS L 60 -1 O ILE L 58 N LEU B 954
SHEET 5 AD6 5 TYR L 31 CYS L 33 -1 N THR L 32 O TYR L 59
SHEET 1 AD7 2 ARG B 865 GLY B 867 0
SHEET 2 AD7 2 ILE B 870 VAL B 871 -1 O ILE B 870 N GLY B 867
SHEET 1 AD8 4 GLU B 873 PHE B 874 0
SHEET 2 AD8 4 LYS B 914 PRO B 917 -1 O THR B 915 N GLU B 873
SHEET 3 AD8 4 LYS B 934 ASP B 936 -1 O ARG B 935 N THR B 916
SHEET 4 AD8 4 THR B 882 LEU B 883 1 N LEU B 883 O LYS B 934
SHEET 1 AD9 2 ALA B1157 PHE B1158 0
SHEET 2 AD9 2 ILE B1196 PRO B1197 -1 O ILE B1196 N PHE B1158
SHEET 1 AE1 2 HIS B1161 CYS B1163 0
SHEET 2 AE1 2 ILE B1191 GLN B1193 -1 O TYR B1192 N VAL B1162
SHEET 1 AE2 4 ILE C 9 ALA C 12 0
SHEET 2 AE2 4 VAL C 17 LEU C 19 -1 O GLU C 18 N ASN C 11
SHEET 3 AE2 4 MET C 230 VAL C 232 -1 O MET C 230 N LEU C 19
SHEET 4 AE2 4 ALA C 177 PHE C 178 -1 N ALA C 177 O THR C 231
SHEET 1 AE3 4 THR C 42 ASN C 53 0
SHEET 2 AE3 4 LEU C 153 GLY C 162 -1 O ASN C 154 N MET C 52
SHEET 3 AE3 4 LEU C 98 LEU C 100 -1 N LEU C 100 O ILE C 155
SHEET 4 AE3 4 ILE C 119 LYS C 120 -1 O ILE C 119 N GLU C 99
SHEET 1 AE4 2 THR C 111 TYR C 114 0
SHEET 2 AE4 2 LEU C 143 LEU C 147 -1 O LEU C 147 N THR C 111
SHEET 1 AE5 2 LYS D 37 TYR D 39 0
SHEET 2 AE5 2 GLU D 45 ASP D 47 -1 O HIS D 46 N GLN D 38
SHEET 1 AE6 5 TYR E 27 PHE E 28 0
SHEET 2 AE6 5 PHE E 59 PRO E 63 -1 O ASN E 62 N PHE E 28
SHEET 3 AE6 5 LEU E 77 GLU E 80 -1 O LEU E 77 N ALA E 61
SHEET 4 AE6 5 THR E 106 TYR E 111 1 O ILE E 108 N GLU E 80
SHEET 5 AE6 5 THR E 133 GLN E 135 1 N PHE E 134 O TYR E 111
SHEET 1 AE7 2 SER E 86 VAL E 87 0
SHEET 2 AE7 2 ASN E 114 ILE E 115 1 O ASN E 114 N VAL E 87
SHEET 1 AE8 3 ARG E 176 ILE E 177 0
SHEET 2 AE8 3 GLY E 205 CYS E 213 1 O ILE E 212 N ILE E 177
SHEET 3 AE8 3 VAL E 194 SER E 201 -1 N ARG E 199 O TYR E 207
SHEET 1 AE9 5 LEU G 106 SER G 111 0
SHEET 2 AE9 5 GLY G 98 VAL G 103 -1 N ALA G 101 O VAL G 108
SHEET 3 AE9 5 VAL G 86 SER G 95 -1 N ILE G 90 O ASP G 102
SHEET 4 AE9 5 VAL G 143 ASP G 153 -1 O LEU G 145 N VAL G 87
SHEET 5 AE9 5 GLU G 156 SER G 162 -1 O GLU G 156 N ASP G 153
SHEET 1 AF1 3 VAL G 120 ASN G 122 0
SHEET 2 AF1 3 ALA G 129 MET G 131 -1 O MET G 131 N VAL G 120
SHEET 3 AF1 3 LEU G 136 THR G 138 -1 O ILE G 137 N TYR G 130
SHEET 1 AF2 7 SER H 54 VAL H 57 0
SHEET 2 AF2 7 ASP H 8 ASP H 16 -1 N PHE H 10 O LEU H 55
SHEET 3 AF2 7 VAL H 23 SER H 30 -1 O ILE H 27 N GLN H 13
SHEET 4 AF2 7 LYS H 37 ASN H 43 -1 O LEU H 40 N ILE H 26
SHEET 5 AF2 7 MET H 122 LEU H 124 -1 O CYS H 123 N THR H 39
SHEET 6 AF2 7 ILE H 111 SER H 116 -1 N VAL H 113 O LEU H 124
SHEET 7 AF2 7 THR H 99 GLU H 105 -1 N TYR H 101 O TYR H 114
SHEET 1 AF3 2 TYR H 94 MET H 96 0
SHEET 2 AF3 2 ILE H 141 ILE H 143 -1 O ILE H 143 N TYR H 94
SHEET 1 AF4 3 TYR I 15 ASP I 19 0
SHEET 2 AF4 3 ARG I 24 SER I 28 -1 O SER I 28 N TYR I 15
SHEET 3 AF4 3 THR I 35 LEU I 37 -1 O GLU I 36 N TYR I 27
SHEET 1 AF5 3 ARG I 70 SER I 71 0
SHEET 2 AF5 3 CYS I 83 VAL I 84 -1 O CYS I 83 N SER I 71
SHEET 3 AF5 3 VAL I 102 CYS I 103 -1 O VAL I 102 N VAL I 84
SHEET 1 AF6 4 LEU K 19 PRO K 23 0
SHEET 2 AF6 4 ILE K 31 PHE K 35 -1 O LYS K 34 N LYS K 20
SHEET 3 AF6 4 VAL K 72 THR K 77 -1 O MET K 73 N ILE K 33
SHEET 4 AF6 4 VAL K 56 LYS K 62 -1 N PHE K 58 O GLN K 76
SHEET 1 AF7 2 ARG a 83 PHE a 84 0
SHEET 2 AF7 2 THR b 80 VAL b 81 1 O VAL b 81 N ARG a 83
SHEET 1 AF8 2 ARG c 77 ILE c 78 0
SHEET 2 AF8 2 GLY d 50 ILE d 51 1 O GLY d 50 N ILE c 78
SHEET 1 AF9 2 ARG e 83 PHE e 84 0
SHEET 2 AF9 2 THR f 80 VAL f 81 1 O VAL f 81 N ARG e 83
SHEET 1 AG1 2 ARG g 42 VAL g 43 0
SHEET 2 AG1 2 THR h 85 ILE h 86 1 O ILE h 86 N ARG g 42
SHEET 1 AG2 2 ARG g 77 ILE g 78 0
SHEET 2 AG2 2 GLY h 50 ILE h 51 1 O GLY h 50 N ILE g 78
LINK SG CYS A 70 ZN ZN A1801 1555 1555 2.31
LINK SG CYS A 77 ZN ZN A1801 1555 1555 2.24
LINK NE2 HIS A 80 ZN ZN A1801 1555 1555 2.06
LINK SG CYS A 107 ZN ZN A1802 1555 1555 2.74
LINK N CYS A 168 ZN ZN A1802 1555 1555 2.10
LINK SG CYS A 168 ZN ZN A1802 1555 1555 2.93
LINK OD1 ASP A 482 MG MG A1803 1555 1555 2.95
LINK OD2 ASP A 482 MG MG A1803 1555 1555 3.00
LINK OD1 ASP A 484 MG MG A1803 1555 1555 2.32
LINK OD2 ASP A 484 MG MG A1803 1555 1555 2.26
LINK MG MG A1803 O3' G P 10 1555 1555 1.82
LINK SG CYS B1163 ZN ZN B1301 1555 1555 2.44
LINK SG CYS B1166 ZN ZN B1301 1555 1555 2.27
LINK SG CYS B1182 ZN ZN B1301 1555 1555 2.28
LINK SG CYS C 85 ZN ZN C 401 1555 1555 2.49
LINK N CYS C 94 ZN ZN C 401 1555 1555 2.07
LINK SG CYS C 94 ZN ZN C 401 1555 1555 2.51
LINK OE1 GLU I 9 ZN ZN I 202 1555 1555 2.46
LINK SG CYS I 32 ZN ZN I 202 1555 1555 2.33
LINK SG CYS I 75 ZN ZN I 201 1555 1555 2.48
LINK SG CYS I 78 ZN ZN I 201 1555 1555 2.64
LINK SG CYS I 103 ZN ZN I 201 1555 1555 2.54
LINK SG CYS J 7 ZN ZN J 101 1555 1555 2.12
LINK SG CYS J 10 ZN ZN J 101 1555 1555 2.64
LINK SG CYS J 44 ZN ZN J 101 1555 1555 2.20
LINK N CYS J 45 ZN ZN J 101 1555 1555 1.96
LINK SG CYS J 45 ZN ZN J 101 1555 1555 2.20
LINK SG CYS L 50 ZN ZN L 101 1555 1555 2.38
LINK SG CYS L 53 ZN ZN L 101 1555 1555 2.52
CISPEP 1 HIS A 400 PRO A 401 0 4.41
CISPEP 2 GLN A 448 PRO A 449 0 -5.64
CISPEP 3 LYS A 568 PRO A 569 0 10.41
CISPEP 4 GLY C 125 ASN C 126 0 -1.01
CISPEP 5 SER E 127 PRO E 128 0 -3.05
CISPEP 6 SER G 126 PRO G 127 0 -2.24
SITE 1 AC1 4 CYS A 67 CYS A 70 CYS A 77 HIS A 80
SITE 1 AC2 4 CYS A 107 ASN A 109 GLY A 167 CYS A 168
SITE 1 AC3 4 ASP A 482 ASP A 484 ASP A 486 G P 10
SITE 1 AC4 4 CYS B1163 CYS B1166 CYS B1182 CYS B1185
SITE 1 AC5 4 CYS C 85 CYS C 91 GLU C 93 CYS C 94
SITE 1 AC6 4 CYS I 75 CYS I 78 CYS I 103 ASN I 105
SITE 1 AC7 3 GLU I 9 CYS I 10 CYS I 32
SITE 1 AC8 4 CYS J 7 CYS J 10 CYS J 44 CYS J 45
SITE 1 AC9 5 CYS L 33 CYS L 36 CYS L 50 GLU L 52
SITE 2 AC9 5 CYS L 53
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END