HEADER REPLICATION 10-DEC-19 6TNY
TITLE PROCESSIVE HUMAN POLYMERASE DELTA HOLOENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE DELTA CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DNA POLYMERASE SUBUNIT DELTA P125;
COMPND 5 EC: 2.7.7.7,3.1.11.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA POLYMERASE DELTA SUBUNIT 2;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: DNA POLYMERASE DELTA SUBUNIT P50;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA POLYMERASE DELTA SUBUNIT 3;
COMPND 14 CHAIN: C;
COMPND 15 SYNONYM: DNA POLYMERASE DELTA SUBUNIT C,DNA POLYMERASE DELTA SUBUNIT
COMPND 16 P66,DNA POLYMERASE DELTA SUBUNIT P68;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA POLYMERASE DELTA SUBUNIT 4;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: DNA POLYMERASE DELTA SUBUNIT P12;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;
COMPND 25 CHAIN: E, F, G;
COMPND 26 SYNONYM: PCNA,CYCLIN;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: DNA PRIMER;
COMPND 30 CHAIN: P;
COMPND 31 ENGINEERED: YES;
COMPND 32 MOL_ID: 7;
COMPND 33 MOLECULE: DNA TEMPLATE;
COMPND 34 CHAIN: T;
COMPND 35 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POLD1, POLD;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: POLD2;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: POLD3, KIAA0039;
SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 25 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_COMMON: HUMAN;
SOURCE 31 ORGANISM_TAXID: 9606;
SOURCE 32 GENE: POLD4, POLDS;
SOURCE 33 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 34 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 35 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 37 MOL_ID: 5;
SOURCE 38 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 39 ORGANISM_COMMON: HUMAN;
SOURCE 40 ORGANISM_TAXID: 9606;
SOURCE 41 GENE: PCNA;
SOURCE 42 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 43 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 44 MOL_ID: 6;
SOURCE 45 SYNTHETIC: YES;
SOURCE 46 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 47 ORGANISM_TAXID: 32630;
SOURCE 48 MOL_ID: 7;
SOURCE 49 SYNTHETIC: YES;
SOURCE 50 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 51 ORGANISM_TAXID: 32630
KEYWDS PROTEIN, REPLICATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.LANCEY,S.M.HAMDAN,A.DE BIASIO
REVDAT 2 11-MAR-20 6TNY 1 JRNL
REVDAT 1 18-DEC-19 6TNY 0
JRNL AUTH C.LANCEY,M.TEHSEEN,V.S.RADUCANU,F.RASHID,N.MERINO,T.J.RAGAN,
JRNL AUTH 2 C.G.SAVVA,M.S.ZAHER,A.SHIRBINI,F.J.BLANCO,S.M.HAMDAN,
JRNL AUTH 3 A.DE BIASIO
JRNL TITL STRUCTURE OF THE PROCESSIVE HUMAN POL DELTA HOLOENZYME.
JRNL REF NAT COMMUN V. 11 1109 2020
JRNL REFN ESSN 2041-1723
JRNL PMID 32111820
JRNL DOI 10.1038/S41467-020-14898-6
REMARK 2
REMARK 2 RESOLUTION. 3.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : EPU, CTFFIND, 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 : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
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) : 3.080
REMARK 3 NUMBER OF PARTICLES : 288920
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6TNY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105698.
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 : TOOLBELT; DNA POLYMERASE;
REMARK 245 PROLIFERATING CELL NUCLEAR
REMARK 245 ANTIGEN; DNA PRIMER, TEMPLATE
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 : 5071
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1100.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2300.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 44.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 105000
REMARK 245 CALIBRATED MAGNIFICATION : 57471
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
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: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 114650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, P, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 ARG A 5
REMARK 465 ARG A 6
REMARK 465 PRO A 7
REMARK 465 GLY A 8
REMARK 465 PRO A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 GLY A 12
REMARK 465 VAL A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 LYS A 16
REMARK 465 ARG A 17
REMARK 465 ALA A 18
REMARK 465 ARG A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 LEU A 22
REMARK 465 TRP A 23
REMARK 465 ASP A 24
REMARK 465 ASP A 25
REMARK 465 ASP A 26
REMARK 465 ASP A 27
REMARK 465 ALA A 28
REMARK 465 PRO A 29
REMARK 465 ARG A 30
REMARK 465 PRO A 31
REMARK 465 SER A 32
REMARK 465 GLN A 33
REMARK 465 PHE A 34
REMARK 465 GLU A 35
REMARK 465 GLU A 36
REMARK 465 ASP A 37
REMARK 465 LEU A 38
REMARK 465 ALA A 39
REMARK 465 LEU A 40
REMARK 465 MET A 41
REMARK 465 GLU A 42
REMARK 465 GLU A 43
REMARK 465 MET A 44
REMARK 465 GLU A 45
REMARK 465 ALA A 46
REMARK 465 GLU A 47
REMARK 465 HIS A 48
REMARK 465 ARG A 49
REMARK 465 LEU A 50
REMARK 465 GLN A 51
REMARK 465 GLU A 52
REMARK 465 GLN A 53
REMARK 465 GLU A 54
REMARK 465 GLU A 55
REMARK 465 GLU A 56
REMARK 465 GLU A 57
REMARK 465 LEU A 58
REMARK 465 GLN A 59
REMARK 465 SER A 60
REMARK 465 VAL A 61
REMARK 465 LEU A 62
REMARK 465 GLU A 63
REMARK 465 GLY A 64
REMARK 465 VAL A 65
REMARK 465 ALA A 66
REMARK 465 ASP A 67
REMARK 465 GLY A 68
REMARK 465 GLN A 69
REMARK 465 VAL A 70
REMARK 465 PRO A 71
REMARK 465 PRO A 72
REMARK 465 SER A 73
REMARK 465 ALA A 74
REMARK 465 ILE A 75
REMARK 465 ASP A 76
REMARK 465 PRO A 77
REMARK 465 PRO A 112
REMARK 465 GLY A 113
REMARK 465 GLY A 114
REMARK 465 PRO A 115
REMARK 465 PRO A 116
REMARK 465 PRO A 117
REMARK 465 SER A 118
REMARK 465 ARG A 119
REMARK 465 GLY A 120
REMARK 465 GLN A 485
REMARK 465 LYS A 486
REMARK 465 GLU A 487
REMARK 465 ASP A 488
REMARK 465 VAL A 489
REMARK 465 GLN A 490
REMARK 465 THR A 996
REMARK 465 GLY A 997
REMARK 465 LYS A 998
REMARK 465 VAL A 999
REMARK 465 GLY A 1000
REMARK 465 ARG B 109
REMARK 465 GLU B 110
REMARK 465 VAL B 111
REMARK 465 SER B 112
REMARK 465 GLU B 113
REMARK 465 GLU B 114
REMARK 465 HIS B 115
REMARK 465 ASN B 116
REMARK 465 LEU B 117
REMARK 465 LEU B 118
REMARK 465 PRO B 119
REMARK 465 GLN B 120
REMARK 465 PRO B 121
REMARK 465 PRO B 122
REMARK 465 ARG B 123
REMARK 465 ARG B 255
REMARK 465 ASP B 256
REMARK 465 SER B 257
REMARK 465 ILE B 258
REMARK 465 ASN B 259
REMARK 465 LYS B 260
REMARK 465 ALA B 261
REMARK 465 LYS B 262
REMARK 465 TYR B 263
REMARK 465 LEU B 264
REMARK 465 THR B 265
REMARK 465 LYS B 266
REMARK 465 LYS B 267
REMARK 465 THR B 268
REMARK 465 GLN B 269
REMARK 465 ALA B 270
REMARK 465 GLY B 463
REMARK 465 GLY B 464
REMARK 465 LEU B 465
REMARK 465 GLY B 466
REMARK 465 LEU B 467
REMARK 465 GLY B 468
REMARK 465 PRO B 469
REMARK 465 MET C -7
REMARK 465 TRP C -6
REMARK 465 SER C -5
REMARK 465 HIS C -4
REMARK 465 PRO C -3
REMARK 465 GLN C -2
REMARK 465 PHE C -1
REMARK 465 GLU C 0
REMARK 465 LYS C 1
REMARK 465 PRO C 145
REMARK 465 ALA C 146
REMARK 465 GLU C 147
REMARK 465 SER C 148
REMARK 465 SER C 149
REMARK 465 SER C 150
REMARK 465 SER C 151
REMARK 465 SER C 152
REMARK 465 LYS C 153
REMARK 465 LYS C 154
REMARK 465 PHE C 155
REMARK 465 GLU C 156
REMARK 465 GLN C 157
REMARK 465 SER C 158
REMARK 465 HIS C 159
REMARK 465 LEU C 160
REMARK 465 HIS C 161
REMARK 465 MET C 162
REMARK 465 SER C 163
REMARK 465 SER C 164
REMARK 465 GLU C 165
REMARK 465 THR C 166
REMARK 465 GLN C 167
REMARK 465 ALA C 168
REMARK 465 ASN C 169
REMARK 465 ASN C 170
REMARK 465 GLU C 171
REMARK 465 LEU C 172
REMARK 465 THR C 173
REMARK 465 THR C 174
REMARK 465 ASN C 175
REMARK 465 GLY C 176
REMARK 465 HIS C 177
REMARK 465 GLY C 178
REMARK 465 PRO C 179
REMARK 465 PRO C 180
REMARK 465 ALA C 181
REMARK 465 SER C 182
REMARK 465 LYS C 183
REMARK 465 GLN C 184
REMARK 465 VAL C 185
REMARK 465 SER C 186
REMARK 465 GLN C 187
REMARK 465 GLN C 188
REMARK 465 PRO C 189
REMARK 465 LYS C 190
REMARK 465 GLY C 191
REMARK 465 ILE C 192
REMARK 465 MET C 193
REMARK 465 GLY C 194
REMARK 465 MET C 195
REMARK 465 PHE C 196
REMARK 465 ALA C 197
REMARK 465 SER C 198
REMARK 465 LYS C 199
REMARK 465 ALA C 200
REMARK 465 ALA C 201
REMARK 465 ALA C 202
REMARK 465 LYS C 203
REMARK 465 THR C 204
REMARK 465 GLN C 205
REMARK 465 GLU C 206
REMARK 465 THR C 207
REMARK 465 ASN C 208
REMARK 465 LYS C 209
REMARK 465 GLU C 210
REMARK 465 THR C 211
REMARK 465 LYS C 212
REMARK 465 THR C 213
REMARK 465 GLU C 214
REMARK 465 ALA C 215
REMARK 465 LYS C 216
REMARK 465 GLU C 217
REMARK 465 VAL C 218
REMARK 465 THR C 219
REMARK 465 ASN C 220
REMARK 465 ALA C 221
REMARK 465 SER C 222
REMARK 465 ALA C 223
REMARK 465 ALA C 224
REMARK 465 GLY C 225
REMARK 465 ASN C 226
REMARK 465 LYS C 227
REMARK 465 ALA C 228
REMARK 465 PRO C 229
REMARK 465 GLY C 230
REMARK 465 LYS C 231
REMARK 465 GLY C 232
REMARK 465 ASN C 233
REMARK 465 MET C 234
REMARK 465 MET C 235
REMARK 465 SER C 236
REMARK 465 ASN C 237
REMARK 465 PHE C 238
REMARK 465 PHE C 239
REMARK 465 GLY C 240
REMARK 465 LYS C 241
REMARK 465 ALA C 242
REMARK 465 ALA C 243
REMARK 465 MET C 244
REMARK 465 ASN C 245
REMARK 465 LYS C 246
REMARK 465 PHE C 247
REMARK 465 LYS C 248
REMARK 465 VAL C 249
REMARK 465 ASN C 250
REMARK 465 LEU C 251
REMARK 465 ASP C 252
REMARK 465 SER C 253
REMARK 465 GLU C 254
REMARK 465 GLN C 255
REMARK 465 ALA C 256
REMARK 465 VAL C 257
REMARK 465 LYS C 258
REMARK 465 GLU C 259
REMARK 465 GLU C 260
REMARK 465 LYS C 261
REMARK 465 ILE C 262
REMARK 465 VAL C 263
REMARK 465 GLU C 264
REMARK 465 GLN C 265
REMARK 465 PRO C 266
REMARK 465 THR C 267
REMARK 465 VAL C 268
REMARK 465 SER C 269
REMARK 465 VAL C 270
REMARK 465 THR C 271
REMARK 465 GLU C 272
REMARK 465 PRO C 273
REMARK 465 LYS C 274
REMARK 465 LEU C 275
REMARK 465 ALA C 276
REMARK 465 THR C 277
REMARK 465 PRO C 278
REMARK 465 ALA C 279
REMARK 465 GLY C 280
REMARK 465 LEU C 281
REMARK 465 LYS C 282
REMARK 465 LYS C 283
REMARK 465 SER C 284
REMARK 465 SER C 285
REMARK 465 LYS C 286
REMARK 465 LYS C 287
REMARK 465 ALA C 288
REMARK 465 GLU C 289
REMARK 465 PRO C 290
REMARK 465 VAL C 291
REMARK 465 LYS C 292
REMARK 465 VAL C 293
REMARK 465 LEU C 294
REMARK 465 GLN C 295
REMARK 465 LYS C 296
REMARK 465 GLU C 297
REMARK 465 LYS C 298
REMARK 465 LYS C 299
REMARK 465 ARG C 300
REMARK 465 GLY C 301
REMARK 465 LYS C 302
REMARK 465 ARG C 303
REMARK 465 VAL C 304
REMARK 465 ALA C 305
REMARK 465 LEU C 306
REMARK 465 SER C 307
REMARK 465 ASP C 308
REMARK 465 ASP C 309
REMARK 465 GLU C 310
REMARK 465 THR C 311
REMARK 465 LYS C 312
REMARK 465 GLU C 313
REMARK 465 THR C 314
REMARK 465 GLU C 315
REMARK 465 ASN C 316
REMARK 465 MET C 317
REMARK 465 ARG C 318
REMARK 465 LYS C 319
REMARK 465 LYS C 320
REMARK 465 ARG C 321
REMARK 465 ARG C 322
REMARK 465 ARG C 323
REMARK 465 ILE C 324
REMARK 465 LYS C 325
REMARK 465 LEU C 326
REMARK 465 PRO C 327
REMARK 465 GLU C 328
REMARK 465 SER C 329
REMARK 465 ASP C 330
REMARK 465 SER C 331
REMARK 465 SER C 332
REMARK 465 GLU C 333
REMARK 465 ASP C 334
REMARK 465 GLU C 335
REMARK 465 VAL C 336
REMARK 465 PHE C 337
REMARK 465 PRO C 338
REMARK 465 ASP C 339
REMARK 465 SER C 340
REMARK 465 PRO C 341
REMARK 465 GLY C 342
REMARK 465 ALA C 343
REMARK 465 TYR C 344
REMARK 465 GLU C 345
REMARK 465 ALA C 346
REMARK 465 GLU C 347
REMARK 465 SER C 348
REMARK 465 PRO C 349
REMARK 465 SER C 350
REMARK 465 PRO C 351
REMARK 465 PRO C 352
REMARK 465 PRO C 353
REMARK 465 PRO C 354
REMARK 465 PRO C 355
REMARK 465 SER C 356
REMARK 465 PRO C 357
REMARK 465 PRO C 358
REMARK 465 LEU C 359
REMARK 465 GLU C 360
REMARK 465 PRO C 361
REMARK 465 VAL C 362
REMARK 465 PRO C 363
REMARK 465 LYS C 364
REMARK 465 THR C 365
REMARK 465 GLU C 366
REMARK 465 PRO C 367
REMARK 465 GLU C 368
REMARK 465 PRO C 369
REMARK 465 PRO C 370
REMARK 465 SER C 371
REMARK 465 VAL C 372
REMARK 465 LYS C 373
REMARK 465 SER C 374
REMARK 465 SER C 375
REMARK 465 SER C 376
REMARK 465 GLY C 377
REMARK 465 GLU C 378
REMARK 465 ASN C 379
REMARK 465 LYS C 380
REMARK 465 ARG C 381
REMARK 465 LYS C 382
REMARK 465 ARG C 383
REMARK 465 LYS C 384
REMARK 465 ARG C 385
REMARK 465 VAL C 386
REMARK 465 LEU C 387
REMARK 465 LYS C 388
REMARK 465 SER C 389
REMARK 465 LYS C 390
REMARK 465 THR C 391
REMARK 465 TYR C 392
REMARK 465 LEU C 393
REMARK 465 ASP C 394
REMARK 465 GLY C 395
REMARK 465 GLU C 396
REMARK 465 GLY C 397
REMARK 465 CYS C 398
REMARK 465 ILE C 399
REMARK 465 VAL C 400
REMARK 465 THR C 401
REMARK 465 GLU C 402
REMARK 465 LYS C 403
REMARK 465 VAL C 404
REMARK 465 TYR C 405
REMARK 465 GLU C 406
REMARK 465 SER C 407
REMARK 465 GLU C 408
REMARK 465 SER C 409
REMARK 465 CYS C 410
REMARK 465 THR C 411
REMARK 465 ASP C 412
REMARK 465 SER C 413
REMARK 465 GLU C 414
REMARK 465 GLU C 415
REMARK 465 GLU C 416
REMARK 465 LEU C 417
REMARK 465 ASN C 418
REMARK 465 MET C 419
REMARK 465 LYS C 420
REMARK 465 THR C 421
REMARK 465 SER C 422
REMARK 465 SER C 423
REMARK 465 VAL C 424
REMARK 465 HIS C 425
REMARK 465 ARG C 426
REMARK 465 PRO C 427
REMARK 465 PRO C 428
REMARK 465 ALA C 429
REMARK 465 MET C 430
REMARK 465 THR C 431
REMARK 465 VAL C 432
REMARK 465 LYS C 433
REMARK 465 LYS C 434
REMARK 465 GLU C 435
REMARK 465 PRO C 436
REMARK 465 ARG C 437
REMARK 465 GLU C 438
REMARK 465 GLU C 439
REMARK 465 ARG C 440
REMARK 465 LYS C 441
REMARK 465 GLY C 442
REMARK 465 PRO C 443
REMARK 465 LYS C 444
REMARK 465 LYS C 445
REMARK 465 GLY C 446
REMARK 465 THR C 447
REMARK 465 ALA C 448
REMARK 465 ALA C 449
REMARK 465 LEU C 450
REMARK 465 GLY C 451
REMARK 465 LYS C 452
REMARK 465 ALA C 453
REMARK 465 ASN C 454
REMARK 465 ARG C 455
REMARK 465 GLN C 456
REMARK 465 VAL C 457
REMARK 465 SER C 458
REMARK 465 ILE C 459
REMARK 465 THR C 460
REMARK 465 GLY C 461
REMARK 465 PHE C 462
REMARK 465 PHE C 463
REMARK 465 GLN C 464
REMARK 465 ARG C 465
REMARK 465 LYS C 466
REMARK 465 MET D -29
REMARK 465 HIS D -28
REMARK 465 HIS D -27
REMARK 465 HIS D -26
REMARK 465 HIS D -25
REMARK 465 HIS D -24
REMARK 465 HIS D -23
REMARK 465 SER D -22
REMARK 465 ARG D -21
REMARK 465 ALA D -20
REMARK 465 TRP D -19
REMARK 465 ARG D -18
REMARK 465 HIS D -17
REMARK 465 PRO D -16
REMARK 465 GLN D -15
REMARK 465 PHE D -14
REMARK 465 GLY D -13
REMARK 465 GLY D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 GLU D -5
REMARK 465 ASN D -4
REMARK 465 LEU D -3
REMARK 465 TYR D -2
REMARK 465 PHE D -1
REMARK 465 GLN D 0
REMARK 465 SER D 1
REMARK 465 GLY D 2
REMARK 465 ARG D 3
REMARK 465 LYS D 4
REMARK 465 ARG D 5
REMARK 465 LEU D 6
REMARK 465 ILE D 7
REMARK 465 THR D 8
REMARK 465 ASP D 9
REMARK 465 SER D 10
REMARK 465 TYR D 11
REMARK 465 PRO D 12
REMARK 465 VAL D 13
REMARK 465 VAL D 14
REMARK 465 LYS D 15
REMARK 465 ARG D 16
REMARK 465 ARG D 17
REMARK 465 GLU D 18
REMARK 465 GLY D 19
REMARK 465 PRO D 20
REMARK 465 ALA D 21
REMARK 465 GLY D 22
REMARK 465 HIS D 23
REMARK 465 SER D 24
REMARK 465 LYS D 25
REMARK 465 GLY D 26
REMARK 465 GLU D 27
REMARK 465 LEU D 28
REMARK 465 ALA D 29
REMARK 465 PRO D 30
REMARK 465 GLU D 31
REMARK 465 LEU D 32
REMARK 465 GLY D 33
REMARK 465 GLU D 34
REMARK 465 GLU D 35
REMARK 465 PRO D 36
REMARK 465 GLN D 37
REMARK 465 PRO D 38
REMARK 465 ARG D 39
REMARK 465 ASP D 40
REMARK 465 GLU D 41
REMARK 465 GLY E -2
REMARK 465 PRO E -1
REMARK 465 HIS E 0
REMARK 465 ASN E 187
REMARK 465 VAL E 188
REMARK 465 ASP E 189
REMARK 465 LYS E 190
REMARK 465 GLU E 256
REMARK 465 ASP E 257
REMARK 465 GLU E 258
REMARK 465 GLU E 259
REMARK 465 GLY E 260
REMARK 465 SER E 261
REMARK 465 GLY F -2
REMARK 465 PRO F -1
REMARK 465 HIS F 0
REMARK 465 GLN F 108
REMARK 465 SER F 186
REMARK 465 ASN F 187
REMARK 465 VAL F 188
REMARK 465 ASP F 189
REMARK 465 LYS F 190
REMARK 465 GLU F 256
REMARK 465 ASP F 257
REMARK 465 GLU F 258
REMARK 465 GLU F 259
REMARK 465 GLY F 260
REMARK 465 SER F 261
REMARK 465 GLY G -2
REMARK 465 PRO G -1
REMARK 465 HIS G 0
REMARK 465 ASN G 187
REMARK 465 VAL G 188
REMARK 465 ASP G 189
REMARK 465 LYS G 190
REMARK 465 GLU G 191
REMARK 465 GLU G 192
REMARK 465 GLU G 256
REMARK 465 ASP G 257
REMARK 465 GLU G 258
REMARK 465 GLU G 259
REMARK 465 GLY G 260
REMARK 465 SER G 261
REMARK 465 DA P 1
REMARK 465 DG P 2
REMARK 465 DC T -12
REMARK 465 DT T -11
REMARK 465 DG T -10
REMARK 465 DC T -9
REMARK 465 DA T -8
REMARK 465 DC T -7
REMARK 465 DG T -6
REMARK 465 DA T -5
REMARK 465 DA T -4
REMARK 465 DC T 24
REMARK 465 DT T 25
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A1007 CG CD CE NZ
REMARK 470 ARG A1008 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1009 CG CD NE CZ NH1 NH2
REMARK 470 THR A1017 OG1 CG2
REMARK 470 VAL A1018 CG1 CG2
REMARK 470 SER A1020 OG
REMARK 470 VAL A1025 CG1 CG2
REMARK 470 GLU A1027 CG CD OE1 OE2
REMARK 470 PHE A1028 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 251 OG
REMARK 470 THR B 252 OG1 CG2
REMARK 470 GLN B 253 CG CD OE1 NE2
REMARK 470 SER B 254 OG
REMARK 470 ASN E 107 CG OD1 ND2
REMARK 470 GLN E 108 CG CD OE1 NE2
REMARK 470 ASN F 107 CG OD1 ND2
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 OE1 GLN B 308 ND2 ASN B 330 1.83
REMARK 500 CG1 VAL A 861 NE ARG A 985 1.94
REMARK 500 O GLN B 308 CG2 THR B 329 2.13
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 DT P 22 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG P 24 C3' - O3' - P ANGL. DEV. = 8.3 DEGREES
REMARK 500 DOC P 25 O3' - P - O5' ANGL. DEV. = 13.7 DEGREES
REMARK 500 DOC P 25 O3' - P - OP2 ANGL. DEV. = -20.3 DEGREES
REMARK 500 DOC P 25 O3' - P - OP1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 DA T 4 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT T 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT T 15 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT T 21 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DT T 21 O4' - C1' - N1 ANGL. DEV. = 3.5 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 ALA A 86 34.92 -143.07
REMARK 500 ALA A 189 179.91 72.08
REMARK 500 ARG A 218 46.48 -92.71
REMARK 500 ALA A 246 60.06 60.70
REMARK 500 PRO A 329 6.72 -69.64
REMARK 500 CYS A 360 -168.55 -126.20
REMARK 500 PRO A 419 43.33 -80.89
REMARK 500 ASN A 615 60.85 60.24
REMARK 500 ASP A 635 18.68 48.86
REMARK 500 LEU A 711 86.77 -157.89
REMARK 500 LEU A 714 -19.06 -49.49
REMARK 500 THR A 756 -13.15 60.74
REMARK 500 ASP A 757 -14.64 -140.40
REMARK 500 PRO A 789 42.63 -86.26
REMARK 500 GLU A 795 -32.91 -131.59
REMARK 500 ARG A 823 -174.20 -170.47
REMARK 500 ASN A 836 -168.94 -126.23
REMARK 500 PRO A 912 41.03 -89.79
REMARK 500 SER A 949 64.79 60.11
REMARK 500 HIS A1021 159.62 91.67
REMARK 500 CYS A1029 46.25 -108.47
REMARK 500 ARG A1032 82.97 -67.16
REMARK 500 GLU A1040 -15.78 100.14
REMARK 500 THR A1072 42.01 -106.97
REMARK 500 TYR A1080 -6.90 64.64
REMARK 500 LEU B 14 57.48 -96.67
REMARK 500 ALA B 30 4.21 -64.53
REMARK 500 PHE B 46 -158.50 -81.95
REMARK 500 SER B 47 42.28 70.18
REMARK 500 LEU B 103 -5.65 74.89
REMARK 500 ASP B 180 -176.02 78.64
REMARK 500 PRO B 301 73.63 -69.58
REMARK 500 VAL B 328 -155.75 -116.68
REMARK 500 THR B 329 -156.33 -121.55
REMARK 500 ASN B 330 -93.11 -74.84
REMARK 500 ASP B 380 -31.88 -136.98
REMARK 500 CYS B 404 -167.44 -124.82
REMARK 500 ASP B 460 34.07 -93.99
REMARK 500 SER C 53 -6.30 71.58
REMARK 500 GLN C 69 -64.85 -91.54
REMARK 500 ARG C 81 -167.30 -77.22
REMARK 500 GLU D 43 -8.72 73.62
REMARK 500 GLU D 79 53.36 152.88
REMARK 500 PRO D 82 46.59 -84.82
REMARK 500 GLU D 83 -30.89 -130.89
REMARK 500 GLN D 98 49.89 -94.11
REMARK 500 LEU D 104 -150.12 -80.01
REMARK 500 TYR D 105 92.01 66.20
REMARK 500 PRO D 106 3.46 -54.54
REMARK 500 ALA E 218 32.27 -91.41
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1012 SG
REMARK 620 2 CYS A1015 SG 111.7
REMARK 620 3 CYS A1026 SG 112.7 108.8
REMARK 620 4 CYS A1029 SG 92.4 121.0 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1202 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1058 SG
REMARK 620 2 SF4 A1202 S1 123.5
REMARK 620 3 SF4 A1202 S2 109.9 103.6
REMARK 620 4 SF4 A1202 S4 108.7 105.8 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1202 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1061 SG
REMARK 620 2 SF4 A1202 S1 119.5
REMARK 620 3 SF4 A1202 S2 101.5 104.0
REMARK 620 4 SF4 A1202 S3 121.7 103.4 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1202 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1071 SG
REMARK 620 2 SF4 A1202 S2 102.2
REMARK 620 3 SF4 A1202 S3 104.8 104.2
REMARK 620 4 SF4 A1202 S4 134.5 104.2 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1202 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1076 SG
REMARK 620 2 SF4 A1202 S1 116.7
REMARK 620 3 SF4 A1202 S3 74.9 102.9
REMARK 620 4 SF4 A1202 S4 137.1 105.6 103.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TTP A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DG P 24 and DOC P
REMARK 800 25
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-10080 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-10081 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-10082 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-10539 RELATED DB: EMDB
REMARK 900 PROCESSIVE HUMAN POLYMERASE DELTA HOLOENZYME
DBREF 6TNY A 1 1107 UNP P28340 DPOD1_HUMAN 1 1107
DBREF 6TNY B 1 469 UNP P49005 DPOD2_HUMAN 1 469
DBREF 6TNY C 2 466 UNP Q15054 DPOD3_HUMAN 2 466
DBREF 6TNY D 2 107 UNP Q9HCU8 DPOD4_HUMAN 2 107
DBREF 6TNY E 1 261 UNP P12004 PCNA_HUMAN 1 261
DBREF 6TNY F 1 261 UNP P12004 PCNA_HUMAN 1 261
DBREF 6TNY G 1 261 UNP P12004 PCNA_HUMAN 1 261
DBREF 6TNY P 1 25 PDB 6TNY 6TNY 1 25
DBREF 6TNY T -12 25 PDB 6TNY 6TNY -12 25
SEQADV 6TNY MET C -7 UNP Q15054 INITIATING METHIONINE
SEQADV 6TNY TRP C -6 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY SER C -5 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY HIS C -4 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY PRO C -3 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY GLN C -2 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY PHE C -1 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY GLU C 0 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY LYS C 1 UNP Q15054 EXPRESSION TAG
SEQADV 6TNY MET D -29 UNP Q9HCU8 INITIATING METHIONINE
SEQADV 6TNY HIS D -28 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -27 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -26 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -25 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -24 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -23 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY SER D -22 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY ARG D -21 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY ALA D -20 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY TRP D -19 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY ARG D -18 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -17 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY PRO D -16 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLN D -15 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY PHE D -14 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLY D -13 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLY D -12 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -11 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -10 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -9 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -8 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -7 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY HIS D -6 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLU D -5 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY ASN D -4 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY LEU D -3 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY TYR D -2 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY PHE D -1 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLN D 0 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY SER D 1 UNP Q9HCU8 EXPRESSION TAG
SEQADV 6TNY GLY E -2 UNP P12004 EXPRESSION TAG
SEQADV 6TNY PRO E -1 UNP P12004 EXPRESSION TAG
SEQADV 6TNY HIS E 0 UNP P12004 EXPRESSION TAG
SEQADV 6TNY GLY F -2 UNP P12004 EXPRESSION TAG
SEQADV 6TNY PRO F -1 UNP P12004 EXPRESSION TAG
SEQADV 6TNY HIS F 0 UNP P12004 EXPRESSION TAG
SEQADV 6TNY GLY G -2 UNP P12004 EXPRESSION TAG
SEQADV 6TNY PRO G -1 UNP P12004 EXPRESSION TAG
SEQADV 6TNY HIS G 0 UNP P12004 EXPRESSION TAG
SEQRES 1 A 1107 MET ASP GLY LYS ARG ARG PRO GLY PRO GLY PRO GLY VAL
SEQRES 2 A 1107 PRO PRO LYS ARG ALA ARG GLY GLY LEU TRP ASP ASP ASP
SEQRES 3 A 1107 ASP ALA PRO ARG PRO SER GLN PHE GLU GLU ASP LEU ALA
SEQRES 4 A 1107 LEU MET GLU GLU MET GLU ALA GLU HIS ARG LEU GLN GLU
SEQRES 5 A 1107 GLN GLU GLU GLU GLU LEU GLN SER VAL LEU GLU GLY VAL
SEQRES 6 A 1107 ALA ASP GLY GLN VAL PRO PRO SER ALA ILE ASP PRO ARG
SEQRES 7 A 1107 TRP LEU ARG PRO THR PRO PRO ALA LEU ASP PRO GLN THR
SEQRES 8 A 1107 GLU PRO LEU ILE PHE GLN GLN LEU GLU ILE ASP HIS TYR
SEQRES 9 A 1107 VAL GLY PRO ALA GLN PRO VAL PRO GLY GLY PRO PRO PRO
SEQRES 10 A 1107 SER ARG GLY SER VAL PRO VAL LEU ARG ALA PHE GLY VAL
SEQRES 11 A 1107 THR ASP GLU GLY PHE SER VAL CYS CYS HIS ILE HIS GLY
SEQRES 12 A 1107 PHE ALA PRO TYR PHE TYR THR PRO ALA PRO PRO GLY PHE
SEQRES 13 A 1107 GLY PRO GLU HIS MET GLY ASP LEU GLN ARG GLU LEU ASN
SEQRES 14 A 1107 LEU ALA ILE SER ARG ASP SER ARG GLY GLY ARG GLU LEU
SEQRES 15 A 1107 THR GLY PRO ALA VAL LEU ALA VAL GLU LEU CYS SER ARG
SEQRES 16 A 1107 GLU SER MET PHE GLY TYR HIS GLY HIS GLY PRO SER PRO
SEQRES 17 A 1107 PHE LEU ARG ILE THR VAL ALA LEU PRO ARG LEU VAL ALA
SEQRES 18 A 1107 PRO ALA ARG ARG LEU LEU GLU GLN GLY ILE ARG VAL ALA
SEQRES 19 A 1107 GLY LEU GLY THR PRO SER PHE ALA PRO TYR GLU ALA ASN
SEQRES 20 A 1107 VAL ASP PHE GLU ILE ARG PHE MET VAL ASP THR ASP ILE
SEQRES 21 A 1107 VAL GLY CYS ASN TRP LEU GLU LEU PRO ALA GLY LYS TYR
SEQRES 22 A 1107 ALA LEU ARG LEU LYS GLU LYS ALA THR GLN CYS GLN LEU
SEQRES 23 A 1107 GLU ALA ASP VAL LEU TRP SER ASP VAL VAL SER HIS PRO
SEQRES 24 A 1107 PRO GLU GLY PRO TRP GLN ARG ILE ALA PRO LEU ARG VAL
SEQRES 25 A 1107 LEU SER PHE ASP ILE GLU CYS ALA GLY ARG LYS GLY ILE
SEQRES 26 A 1107 PHE PRO GLU PRO GLU ARG ASP PRO VAL ILE GLN ILE CYS
SEQRES 27 A 1107 SER LEU GLY LEU ARG TRP GLY GLU PRO GLU PRO PHE LEU
SEQRES 28 A 1107 ARG LEU ALA LEU THR LEU ARG PRO CYS ALA PRO ILE LEU
SEQRES 29 A 1107 GLY ALA LYS VAL GLN SER TYR GLU LYS GLU GLU ASP LEU
SEQRES 30 A 1107 LEU GLN ALA TRP SER THR PHE ILE ARG ILE MET ASP PRO
SEQRES 31 A 1107 ASP VAL ILE THR GLY TYR ASN ILE GLN ASN PHE ASP LEU
SEQRES 32 A 1107 PRO TYR LEU ILE SER ARG ALA GLN THR LEU LYS VAL GLN
SEQRES 33 A 1107 THR PHE PRO PHE LEU GLY ARG VAL ALA GLY LEU CYS SER
SEQRES 34 A 1107 ASN ILE ARG ASP SER SER PHE GLN SER LYS GLN THR GLY
SEQRES 35 A 1107 ARG ARG ASP THR LYS VAL VAL SER MET VAL GLY ARG VAL
SEQRES 36 A 1107 GLN MET ASP MET LEU GLN VAL LEU LEU ARG GLU TYR LYS
SEQRES 37 A 1107 LEU ARG SER TYR THR LEU ASN ALA VAL SER PHE HIS PHE
SEQRES 38 A 1107 LEU GLY GLU GLN LYS GLU ASP VAL GLN HIS SER ILE ILE
SEQRES 39 A 1107 THR ASP LEU GLN ASN GLY ASN ASP GLN THR ARG ARG ARG
SEQRES 40 A 1107 LEU ALA VAL TYR CYS LEU LYS ASP ALA TYR LEU PRO LEU
SEQRES 41 A 1107 ARG LEU LEU GLU ARG LEU MET VAL LEU VAL ASN ALA VAL
SEQRES 42 A 1107 GLU MET ALA ARG VAL THR GLY VAL PRO LEU SER TYR LEU
SEQRES 43 A 1107 LEU SER ARG GLY GLN GLN VAL LYS VAL VAL SER GLN LEU
SEQRES 44 A 1107 LEU ARG GLN ALA MET HIS GLU GLY LEU LEU MET PRO VAL
SEQRES 45 A 1107 VAL LYS SER GLU GLY GLY GLU ASP TYR THR GLY ALA THR
SEQRES 46 A 1107 VAL ILE GLU PRO LEU LYS GLY TYR TYR ASP VAL PRO ILE
SEQRES 47 A 1107 ALA THR LEU ASP PHE SER SER LEU TYR PRO SER ILE MET
SEQRES 48 A 1107 MET ALA HIS ASN LEU CYS TYR THR THR LEU LEU ARG PRO
SEQRES 49 A 1107 GLY THR ALA GLN LYS LEU GLY LEU THR GLU ASP GLN PHE
SEQRES 50 A 1107 ILE ARG THR PRO THR GLY ASP GLU PHE VAL LYS THR SER
SEQRES 51 A 1107 VAL ARG LYS GLY LEU LEU PRO GLN ILE LEU GLU ASN LEU
SEQRES 52 A 1107 LEU SER ALA ARG LYS ARG ALA LYS ALA GLU LEU ALA LYS
SEQRES 53 A 1107 GLU THR ASP PRO LEU ARG ARG GLN VAL LEU ASP GLY ARG
SEQRES 54 A 1107 GLN LEU ALA LEU LYS VAL SER ALA ASN SER VAL TYR GLY
SEQRES 55 A 1107 PHE THR GLY ALA GLN VAL GLY LYS LEU PRO CYS LEU GLU
SEQRES 56 A 1107 ILE SER GLN SER VAL THR GLY PHE GLY ARG GLN MET ILE
SEQRES 57 A 1107 GLU LYS THR LYS GLN LEU VAL GLU SER LYS TYR THR VAL
SEQRES 58 A 1107 GLU ASN GLY TYR SER THR SER ALA LYS VAL VAL TYR GLY
SEQRES 59 A 1107 ASP THR ASP SER VAL MET CYS ARG PHE GLY VAL SER SER
SEQRES 60 A 1107 VAL ALA GLU ALA MET ALA LEU GLY ARG GLU ALA ALA ASP
SEQRES 61 A 1107 TRP VAL SER GLY HIS PHE PRO SER PRO ILE ARG LEU GLU
SEQRES 62 A 1107 PHE GLU LYS VAL TYR PHE PRO TYR LEU LEU ILE SER LYS
SEQRES 63 A 1107 LYS ARG TYR ALA GLY LEU LEU PHE SER SER ARG PRO ASP
SEQRES 64 A 1107 ALA HIS ASP ARG MET ASP CYS LYS GLY LEU GLU ALA VAL
SEQRES 65 A 1107 ARG ARG ASP ASN CYS PRO LEU VAL ALA ASN LEU VAL THR
SEQRES 66 A 1107 ALA SER LEU ARG ARG LEU LEU ILE ASP ARG ASP PRO GLU
SEQRES 67 A 1107 GLY ALA VAL ALA HIS ALA GLN ASP VAL ILE SER ASP LEU
SEQRES 68 A 1107 LEU CYS ASN ARG ILE ASP ILE SER GLN LEU VAL ILE THR
SEQRES 69 A 1107 LYS GLU LEU THR ARG ALA ALA SER ASP TYR ALA GLY LYS
SEQRES 70 A 1107 GLN ALA HIS VAL GLU LEU ALA GLU ARG MET ARG LYS ARG
SEQRES 71 A 1107 ASP PRO GLY SER ALA PRO SER LEU GLY ASP ARG VAL PRO
SEQRES 72 A 1107 TYR VAL ILE ILE SER ALA ALA LYS GLY VAL ALA ALA TYR
SEQRES 73 A 1107 MET LYS SER GLU ASP PRO LEU PHE VAL LEU GLU HIS SER
SEQRES 74 A 1107 LEU PRO ILE ASP THR GLN TYR TYR LEU GLU GLN GLN LEU
SEQRES 75 A 1107 ALA LYS PRO LEU LEU ARG ILE PHE GLU PRO ILE LEU GLY
SEQRES 76 A 1107 GLU GLY ARG ALA GLU ALA VAL LEU LEU ARG GLY ASP HIS
SEQRES 77 A 1107 THR ARG CYS LYS THR VAL LEU THR GLY LYS VAL GLY GLY
SEQRES 78 A 1107 LEU LEU ALA PHE ALA LYS ARG ARG ASN CYS CYS ILE GLY
SEQRES 79 A 1107 CYS ARG THR VAL LEU SER HIS GLN GLY ALA VAL CYS GLU
SEQRES 80 A 1107 PHE CYS GLN PRO ARG GLU SER GLU LEU TYR GLN LYS GLU
SEQRES 81 A 1107 VAL SER HIS LEU ASN ALA LEU GLU GLU ARG PHE SER ARG
SEQRES 82 A 1107 LEU TRP THR GLN CYS GLN ARG CYS GLN GLY SER LEU HIS
SEQRES 83 A 1107 GLU ASP VAL ILE CYS THR SER ARG ASP CYS PRO ILE PHE
SEQRES 84 A 1107 TYR MET ARG LYS LYS VAL ARG LYS ASP LEU GLU ASP GLN
SEQRES 85 A 1107 GLU GLN LEU LEU ARG ARG PHE GLY PRO PRO GLY PRO GLU
SEQRES 86 A 1107 ALA TRP
SEQRES 1 B 469 MET PHE SER GLU GLN ALA ALA GLN ARG ALA HIS THR LEU
SEQRES 2 B 469 LEU SER PRO PRO SER ALA ASN ASN ALA THR PHE ALA ARG
SEQRES 3 B 469 VAL PRO VAL ALA THR TYR THR ASN SER SER GLN PRO PHE
SEQRES 4 B 469 ARG LEU GLY GLU ARG SER PHE SER ARG GLN TYR ALA HIS
SEQRES 5 B 469 ILE TYR ALA THR ARG LEU ILE GLN MET ARG PRO PHE LEU
SEQRES 6 B 469 GLU ASN ARG ALA GLN GLN HIS TRP GLY SER GLY VAL GLY
SEQRES 7 B 469 VAL LYS LYS LEU CYS GLU LEU GLN PRO GLU GLU LYS CYS
SEQRES 8 B 469 CYS VAL VAL GLY THR LEU PHE LYS ALA MET PRO LEU GLN
SEQRES 9 B 469 PRO SER ILE LEU ARG GLU VAL SER GLU GLU HIS ASN LEU
SEQRES 10 B 469 LEU PRO GLN PRO PRO ARG SER LYS TYR ILE HIS PRO ASP
SEQRES 11 B 469 ASP GLU LEU VAL LEU GLU ASP GLU LEU GLN ARG ILE LYS
SEQRES 12 B 469 LEU LYS GLY THR ILE ASP VAL SER LYS LEU VAL THR GLY
SEQRES 13 B 469 THR VAL LEU ALA VAL PHE GLY SER VAL ARG ASP ASP GLY
SEQRES 14 B 469 LYS PHE LEU VAL GLU ASP TYR CYS PHE ALA ASP LEU ALA
SEQRES 15 B 469 PRO GLN LYS PRO ALA PRO PRO LEU ASP THR ASP ARG PHE
SEQRES 16 B 469 VAL LEU LEU VAL SER GLY LEU GLY LEU GLY GLY GLY GLY
SEQRES 17 B 469 GLY GLU SER LEU LEU GLY THR GLN LEU LEU VAL ASP VAL
SEQRES 18 B 469 VAL THR GLY GLN LEU GLY ASP GLU GLY GLU GLN CYS SER
SEQRES 19 B 469 ALA ALA HIS VAL SER ARG VAL ILE LEU ALA GLY ASN LEU
SEQRES 20 B 469 LEU SER HIS SER THR GLN SER ARG ASP SER ILE ASN LYS
SEQRES 21 B 469 ALA LYS TYR LEU THR LYS LYS THR GLN ALA ALA SER VAL
SEQRES 22 B 469 GLU ALA VAL LYS MET LEU ASP GLU ILE LEU LEU GLN LEU
SEQRES 23 B 469 SER ALA SER VAL PRO VAL ASP VAL MET PRO GLY GLU PHE
SEQRES 24 B 469 ASP PRO THR ASN TYR THR LEU PRO GLN GLN PRO LEU HIS
SEQRES 25 B 469 PRO CYS MET PHE PRO LEU ALA THR ALA TYR SER THR LEU
SEQRES 26 B 469 GLN LEU VAL THR ASN PRO TYR GLN ALA THR ILE ASP GLY
SEQRES 27 B 469 VAL ARG PHE LEU GLY THR SER GLY GLN ASN VAL SER ASP
SEQRES 28 B 469 ILE PHE ARG TYR SER SER MET GLU ASP HIS LEU GLU ILE
SEQRES 29 B 469 LEU GLU TRP THR LEU ARG VAL ARG HIS ILE SER PRO THR
SEQRES 30 B 469 ALA PRO ASP THR LEU GLY CYS TYR PRO PHE TYR LYS THR
SEQRES 31 B 469 ASP PRO PHE ILE PHE PRO GLU CYS PRO HIS VAL TYR PHE
SEQRES 32 B 469 CYS GLY ASN THR PRO SER PHE GLY SER LYS ILE ILE ARG
SEQRES 33 B 469 GLY PRO GLU ASP GLN THR VAL LEU LEU VAL THR VAL PRO
SEQRES 34 B 469 ASP PHE SER ALA THR GLN THR ALA CYS LEU VAL ASN LEU
SEQRES 35 B 469 ARG SER LEU ALA CYS GLN PRO ILE SER PHE SER GLY PHE
SEQRES 36 B 469 GLY ALA GLU ASP ASP ASP LEU GLY GLY LEU GLY LEU GLY
SEQRES 37 B 469 PRO
SEQRES 1 C 474 MET TRP SER HIS PRO GLN PHE GLU LYS ALA ASP GLN LEU
SEQRES 2 C 474 TYR LEU GLU ASN ILE ASP GLU PHE VAL THR ASP GLN ASN
SEQRES 3 C 474 LYS ILE VAL THR TYR LYS TRP LEU SER TYR THR LEU GLY
SEQRES 4 C 474 VAL HIS VAL ASN GLN ALA LYS GLN MET LEU TYR ASP TYR
SEQRES 5 C 474 VAL GLU ARG LYS ARG LYS GLU ASN SER GLY ALA GLN LEU
SEQRES 6 C 474 HIS VAL THR TYR LEU VAL SER GLY SER LEU ILE GLN ASN
SEQRES 7 C 474 GLY HIS SER CYS HIS LYS VAL ALA VAL VAL ARG GLU ASP
SEQRES 8 C 474 LYS LEU GLU ALA VAL LYS SER LYS LEU ALA VAL THR ALA
SEQRES 9 C 474 SER ILE HIS VAL TYR SER ILE GLN LYS ALA MET LEU LYS
SEQRES 10 C 474 ASP SER GLY PRO LEU PHE ASN THR ASP TYR ASP ILE LEU
SEQRES 11 C 474 LYS SER ASN LEU GLN ASN CYS SER LYS PHE SER ALA ILE
SEQRES 12 C 474 GLN CYS ALA ALA ALA VAL PRO ARG ALA PRO ALA GLU SER
SEQRES 13 C 474 SER SER SER SER LYS LYS PHE GLU GLN SER HIS LEU HIS
SEQRES 14 C 474 MET SER SER GLU THR GLN ALA ASN ASN GLU LEU THR THR
SEQRES 15 C 474 ASN GLY HIS GLY PRO PRO ALA SER LYS GLN VAL SER GLN
SEQRES 16 C 474 GLN PRO LYS GLY ILE MET GLY MET PHE ALA SER LYS ALA
SEQRES 17 C 474 ALA ALA LYS THR GLN GLU THR ASN LYS GLU THR LYS THR
SEQRES 18 C 474 GLU ALA LYS GLU VAL THR ASN ALA SER ALA ALA GLY ASN
SEQRES 19 C 474 LYS ALA PRO GLY LYS GLY ASN MET MET SER ASN PHE PHE
SEQRES 20 C 474 GLY LYS ALA ALA MET ASN LYS PHE LYS VAL ASN LEU ASP
SEQRES 21 C 474 SER GLU GLN ALA VAL LYS GLU GLU LYS ILE VAL GLU GLN
SEQRES 22 C 474 PRO THR VAL SER VAL THR GLU PRO LYS LEU ALA THR PRO
SEQRES 23 C 474 ALA GLY LEU LYS LYS SER SER LYS LYS ALA GLU PRO VAL
SEQRES 24 C 474 LYS VAL LEU GLN LYS GLU LYS LYS ARG GLY LYS ARG VAL
SEQRES 25 C 474 ALA LEU SER ASP ASP GLU THR LYS GLU THR GLU ASN MET
SEQRES 26 C 474 ARG LYS LYS ARG ARG ARG ILE LYS LEU PRO GLU SER ASP
SEQRES 27 C 474 SER SER GLU ASP GLU VAL PHE PRO ASP SER PRO GLY ALA
SEQRES 28 C 474 TYR GLU ALA GLU SER PRO SER PRO PRO PRO PRO PRO SER
SEQRES 29 C 474 PRO PRO LEU GLU PRO VAL PRO LYS THR GLU PRO GLU PRO
SEQRES 30 C 474 PRO SER VAL LYS SER SER SER GLY GLU ASN LYS ARG LYS
SEQRES 31 C 474 ARG LYS ARG VAL LEU LYS SER LYS THR TYR LEU ASP GLY
SEQRES 32 C 474 GLU GLY CYS ILE VAL THR GLU LYS VAL TYR GLU SER GLU
SEQRES 33 C 474 SER CYS THR ASP SER GLU GLU GLU LEU ASN MET LYS THR
SEQRES 34 C 474 SER SER VAL HIS ARG PRO PRO ALA MET THR VAL LYS LYS
SEQRES 35 C 474 GLU PRO ARG GLU GLU ARG LYS GLY PRO LYS LYS GLY THR
SEQRES 36 C 474 ALA ALA LEU GLY LYS ALA ASN ARG GLN VAL SER ILE THR
SEQRES 37 C 474 GLY PHE PHE GLN ARG LYS
SEQRES 1 D 137 MET HIS HIS HIS HIS HIS HIS SER ARG ALA TRP ARG HIS
SEQRES 2 D 137 PRO GLN PHE GLY GLY HIS HIS HIS HIS HIS HIS GLU ASN
SEQRES 3 D 137 LEU TYR PHE GLN SER GLY ARG LYS ARG LEU ILE THR ASP
SEQRES 4 D 137 SER TYR PRO VAL VAL LYS ARG ARG GLU GLY PRO ALA GLY
SEQRES 5 D 137 HIS SER LYS GLY GLU LEU ALA PRO GLU LEU GLY GLU GLU
SEQRES 6 D 137 PRO GLN PRO ARG ASP GLU GLU GLU ALA GLU LEU GLU LEU
SEQRES 7 D 137 LEU ARG GLN PHE ASP LEU ALA TRP GLN TYR GLY PRO CYS
SEQRES 8 D 137 THR GLY ILE THR ARG LEU GLN ARG TRP CYS ARG ALA LYS
SEQRES 9 D 137 GLN MET GLY LEU GLU PRO PRO PRO GLU VAL TRP GLN VAL
SEQRES 10 D 137 LEU LYS THR HIS PRO GLY ASP PRO ARG PHE GLN CYS SER
SEQRES 11 D 137 LEU TRP HIS LEU TYR PRO LEU
SEQRES 1 E 264 GLY PRO HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER
SEQRES 2 E 264 ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE
SEQRES 3 E 264 ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN
SEQRES 4 E 264 LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN
SEQRES 5 E 264 LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS
SEQRES 6 E 264 ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET
SEQRES 7 E 264 SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE
SEQRES 8 E 264 THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU
SEQRES 9 E 264 VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR
SEQRES 10 E 264 GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY
SEQRES 11 E 264 ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO
SEQRES 12 E 264 SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS
SEQRES 13 E 264 ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY
SEQRES 14 E 264 VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN
SEQRES 15 E 264 ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU
SEQRES 16 E 264 GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU
SEQRES 17 E 264 THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA
SEQRES 18 E 264 THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA
SEQRES 19 E 264 ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET
SEQRES 20 E 264 GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP
SEQRES 21 E 264 GLU GLU GLY SER
SEQRES 1 F 264 GLY PRO HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER
SEQRES 2 F 264 ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE
SEQRES 3 F 264 ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN
SEQRES 4 F 264 LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN
SEQRES 5 F 264 LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS
SEQRES 6 F 264 ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET
SEQRES 7 F 264 SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE
SEQRES 8 F 264 THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU
SEQRES 9 F 264 VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR
SEQRES 10 F 264 GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY
SEQRES 11 F 264 ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO
SEQRES 12 F 264 SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS
SEQRES 13 F 264 ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY
SEQRES 14 F 264 VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN
SEQRES 15 F 264 ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU
SEQRES 16 F 264 GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU
SEQRES 17 F 264 THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA
SEQRES 18 F 264 THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA
SEQRES 19 F 264 ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET
SEQRES 20 F 264 GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP
SEQRES 21 F 264 GLU GLU GLY SER
SEQRES 1 G 264 GLY PRO HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER
SEQRES 2 G 264 ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE
SEQRES 3 G 264 ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN
SEQRES 4 G 264 LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN
SEQRES 5 G 264 LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS
SEQRES 6 G 264 ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET
SEQRES 7 G 264 SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE
SEQRES 8 G 264 THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU
SEQRES 9 G 264 VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR
SEQRES 10 G 264 GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY
SEQRES 11 G 264 ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO
SEQRES 12 G 264 SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS
SEQRES 13 G 264 ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY
SEQRES 14 G 264 VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN
SEQRES 15 G 264 ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU
SEQRES 16 G 264 GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU
SEQRES 17 G 264 THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA
SEQRES 18 G 264 THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA
SEQRES 19 G 264 ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET
SEQRES 20 G 264 GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP
SEQRES 21 G 264 GLU GLU GLY SER
SEQRES 1 P 25 DA DG DC DT DA DT DG DA DC DC DA DT DG
SEQRES 2 P 25 DA DT DT DA DC DG DA DA DT DT DG DOC
SEQRES 1 T 38 DC DT DG DC DA DC DG DA DA DT DT DA DA
SEQRES 2 T 38 DG DC DA DA DT DT DC DG DT DA DA DT DC
SEQRES 3 T 38 DA DT DG DG DT DC DA DT DA DG DC DT
HET DOC P 25 18
HET ZN A1201 1
HET SF4 A1202 8
HET TTP A1203 29
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM TTP THYMIDINE-5'-TRIPHOSPHATE
FORMUL 8 DOC C9 H14 N3 O6 P
FORMUL 10 ZN ZN 2+
FORMUL 11 SF4 FE4 S4
FORMUL 12 TTP C10 H17 N2 O14 P3
HELIX 1 AA1 HIS A 160 ASN A 169 1 10
HELIX 2 AA2 SER A 173 ARG A 177 5 5
HELIX 3 AA3 LEU A 216 ARG A 218 5 3
HELIX 4 AA4 LEU A 219 GLU A 228 1 10
HELIX 5 AA5 ASP A 249 ASP A 259 1 11
HELIX 6 AA6 GLU A 301 ARG A 306 5 6
HELIX 7 AA7 LYS A 373 ASP A 389 1 17
HELIX 8 AA8 PHE A 401 LEU A 413 1 13
HELIX 9 AA9 MET A 459 TYR A 467 1 9
HELIX 10 AB1 THR A 473 LEU A 482 1 10
HELIX 11 AB2 ILE A 493 ASN A 499 1 7
HELIX 12 AB3 ASN A 501 LEU A 526 1 26
HELIX 13 AB4 MET A 527 GLY A 540 1 14
HELIX 14 AB5 SER A 544 SER A 548 5 5
HELIX 15 AB6 GLN A 551 MET A 564 1 14
HELIX 16 AB7 SER A 605 HIS A 614 1 10
HELIX 17 AB8 CYS A 617 THR A 619 5 3
HELIX 18 AB9 LEU A 655 ALA A 675 1 21
HELIX 19 AC1 ASP A 679 GLY A 705 1 27
HELIX 20 AC2 CYS A 713 TYR A 739 1 27
HELIX 21 AC3 SER A 767 SER A 783 1 17
HELIX 22 AC4 CYS A 837 ILE A 853 1 17
HELIX 23 AC5 ASP A 856 CYS A 873 1 18
HELIX 24 AC6 GLN A 898 ARG A 906 1 9
HELIX 25 AC7 ASP A 941 SER A 949 1 9
HELIX 26 AC8 ASP A 953 GLN A 960 1 8
HELIX 27 AC9 LEU A 962 GLU A 971 1 10
HELIX 28 AD1 GLU A 976 ARG A 990 1 15
HELIX 29 AD2 GLY A 1001 PHE A 1005 5 5
HELIX 30 AD3 GLU A 1033 THR A 1056 1 24
HELIX 31 AD4 THR A 1056 GLY A 1063 1 8
HELIX 32 AD5 PRO A 1077 LEU A 1096 1 20
HELIX 33 AD6 GLU B 4 GLN B 8 5 5
HELIX 34 AD7 SER B 36 ARG B 40 5 5
HELIX 35 AD8 TYR B 50 GLY B 74 1 25
HELIX 36 AD9 GLY B 209 THR B 223 1 15
HELIX 37 AE1 ASP B 228 ALA B 236 1 9
HELIX 38 AE2 SER B 272 ALA B 288 1 17
HELIX 39 AE3 HIS B 312 PHE B 316 5 5
HELIX 40 AE4 LEU B 318 TYR B 322 5 5
HELIX 41 AE5 GLN B 347 TYR B 355 1 9
HELIX 42 AE6 ASP B 360 VAL B 371 1 12
HELIX 43 AE7 ASP C 3 THR C 15 1 13
HELIX 44 AE8 LYS C 24 LEU C 30 1 7
HELIX 45 AE9 HIS C 33 ASN C 52 1 20
HELIX 46 AF1 LYS C 84 LEU C 92 1 9
HELIX 47 AF2 GLY C 112 SER C 124 1 13
HELIX 48 AF3 ALA D 44 ASP D 53 1 10
HELIX 49 AF4 THR D 65 GLY D 77 1 13
HELIX 50 AF5 GLY E 9 ALA E 18 1 10
HELIX 51 AF6 GLU E 55 PHE E 57 5 3
HELIX 52 AF7 LEU E 72 LYS E 80 1 9
HELIX 53 AF8 SER E 141 HIS E 153 1 13
HELIX 54 AF9 LEU E 209 THR E 216 1 8
HELIX 55 AG1 LYS E 217 SER E 222 5 6
HELIX 56 AG2 GLN F 8 LYS F 20 1 13
HELIX 57 AG3 LEU F 72 LEU F 79 1 8
HELIX 58 AG4 SER F 141 SER F 152 1 12
HELIX 59 AG5 LEU F 209 THR F 216 1 8
HELIX 60 AG6 LYS F 217 SER F 222 5 6
HELIX 61 AG7 GLN G 8 LYS G 20 1 13
HELIX 62 AG8 LEU G 72 LEU G 79 1 8
HELIX 63 AG9 SER G 141 GLY G 155 1 15
HELIX 64 AH1 LEU G 209 THR G 216 1 8
HELIX 65 AH2 LYS G 217 SER G 222 5 6
SHEET 1 AA1 6 LEU A 286 LEU A 291 0
SHEET 2 AA1 6 SER A 136 HIS A 142 1 N HIS A 140 O VAL A 290
SHEET 3 AA1 6 PRO A 123 THR A 131 -1 N LEU A 125 O ILE A 141
SHEET 4 AA1 6 LEU A 94 VAL A 105 -1 N TYR A 104 O VAL A 124
SHEET 5 AA1 6 TRP A 265 LEU A 268 -1 O LEU A 266 N PHE A 96
SHEET 6 AA1 6 VAL A 296 HIS A 298 -1 O HIS A 298 N TRP A 265
SHEET 1 AA2 3 TYR A 147 PRO A 151 0
SHEET 2 AA2 3 SER A 207 THR A 213 -1 O LEU A 210 N THR A 150
SHEET 3 AA2 3 LEU A 192 ARG A 195 -1 N CYS A 193 O PHE A 209
SHEET 1 AA3 6 LYS A 367 SER A 370 0
SHEET 2 AA3 6 LEU A 351 THR A 356 1 N THR A 356 O GLN A 369
SHEET 3 AA3 6 VAL A 334 ARG A 343 -1 N ILE A 337 O LEU A 355
SHEET 4 AA3 6 ARG A 311 CYS A 319 -1 N VAL A 312 O LEU A 342
SHEET 5 AA3 6 VAL A 392 GLY A 395 1 O THR A 394 N LEU A 313
SHEET 6 AA3 6 VAL A 455 ASP A 458 1 O MET A 457 N ILE A 393
SHEET 1 AA4 2 ILE A 431 SER A 438 0
SHEET 2 AA4 2 GLY A 442 VAL A 449 -1 O ARG A 444 N PHE A 436
SHEET 1 AA5 5 GLY A 592 TYR A 594 0
SHEET 2 AA5 5 LEU A 792 SER A 805 -1 O TYR A 801 N TYR A 594
SHEET 3 AA5 5 ILE A 598 PHE A 603 -1 N ILE A 598 O TYR A 798
SHEET 4 AA5 5 SER A 758 ARG A 762 -1 O CYS A 761 N ALA A 599
SHEET 5 AA5 5 LYS A 750 GLY A 754 -1 N TYR A 753 O MET A 760
SHEET 1 AA6 4 GLY A 592 TYR A 594 0
SHEET 2 AA6 4 LEU A 792 SER A 805 -1 O TYR A 801 N TYR A 594
SHEET 3 AA6 4 ARG A 808 PHE A 814 -1 O ALA A 810 N LEU A 802
SHEET 4 AA6 4 MET A 824 LYS A 827 -1 O ASP A 825 N GLY A 811
SHEET 1 AA7 3 LEU A 621 LEU A 622 0
SHEET 2 AA7 3 GLU A 645 VAL A 647 -1 O GLU A 645 N LEU A 622
SHEET 3 AA7 3 PHE A 637 ARG A 639 -1 N ILE A 638 O PHE A 646
SHEET 1 AA8 3 ILE A 883 GLU A 886 0
SHEET 2 AA8 3 ARG A 921 ILE A 926 -1 O TYR A 924 N ILE A 883
SHEET 3 AA8 3 SER A 939 GLU A 940 -1 O GLU A 940 N VAL A 925
SHEET 1 AA9 2 LYS A 992 THR A 993 0
SHEET 2 AA9 2 ASP F 120 LEU F 121 1 O ASP F 120 N THR A 993
SHEET 1 AB1 6 ARG B 141 LYS B 143 0
SHEET 2 AB1 6 GLU B 132 GLU B 136 -1 N LEU B 135 O ILE B 142
SHEET 3 AB1 6 CYS B 91 ALA B 100 -1 N THR B 96 O GLU B 136
SHEET 4 AB1 6 VAL B 158 VAL B 165 -1 O GLY B 163 N CYS B 91
SHEET 5 AB1 6 PHE B 171 CYS B 177 -1 O GLU B 174 N PHE B 162
SHEET 6 AB1 6 LYS B 145 GLY B 146 1 N LYS B 145 O PHE B 171
SHEET 1 AB210 LEU B 325 LEU B 327 0
SHEET 2 AB210 VAL B 292 MET B 295 1 N VAL B 294 O GLN B 326
SHEET 3 AB210 VAL B 238 ALA B 244 1 N LEU B 243 O ASP B 293
SHEET 4 AB210 PHE B 195 VAL B 199 1 N PHE B 195 O SER B 239
SHEET 5 AB210 THR B 436 ASN B 441 -1 O VAL B 440 N VAL B 196
SHEET 6 AB210 CYS B 447 GLY B 454 -1 O GLN B 448 N LEU B 439
SHEET 7 AB210 SER C 73 VAL C 80 1 O HIS C 75 N SER B 451
SHEET 8 AB210 HIS C 58 ILE C 68 -1 N VAL C 63 O ALA C 78
SHEET 9 AB210 SER C 97 GLN C 104 -1 O TYR C 101 N THR C 60
SHEET 10 AB210 VAL C 21 THR C 22 -1 N VAL C 21 O ILE C 103
SHEET 1 AB3 5 TYR B 332 ILE B 336 0
SHEET 2 AB3 5 VAL B 339 GLY B 343 -1 O GLY B 343 N TYR B 332
SHEET 3 AB3 5 VAL B 401 PHE B 403 1 O VAL B 401 N ARG B 340
SHEET 4 AB3 5 THR B 422 THR B 427 1 O LEU B 424 N TYR B 402
SHEET 5 AB3 5 GLY B 411 ARG B 416 -1 N GLY B 411 O THR B 427
SHEET 1 AB4 5 TYR E 60 ARG E 61 0
SHEET 2 AB4 5 PHE E 2 LEU E 6 -1 N GLU E 3 O ARG E 61
SHEET 3 AB4 5 ILE E 87 ALA E 92 -1 O LEU E 90 N ALA E 4
SHEET 4 AB4 5 THR E 98 GLU E 104 -1 O VAL E 102 N THR E 89
SHEET 5 AB4 5 SER E 112 LYS E 117 -1 O TYR E 114 N LEU E 101
SHEET 1 AB5 9 LEU E 66 ASN E 71 0
SHEET 2 AB5 9 GLU E 25 SER E 31 -1 N ALA E 26 O VAL E 70
SHEET 3 AB5 9 GLY E 34 MET E 40 -1 O ASN E 36 N ASP E 29
SHEET 4 AB5 9 SER E 46 ARG E 53 -1 O VAL E 48 N SER E 39
SHEET 5 AB5 9 GLY E 245 LEU E 251 -1 O LYS E 248 N GLN E 49
SHEET 6 AB5 9 LEU E 235 ILE E 241 -1 N TYR E 239 O LEU E 247
SHEET 7 AB5 9 THR E 224 MET E 229 -1 N THR E 226 O GLU E 238
SHEET 8 AB5 9 CYS E 135 PRO E 140 -1 N MET E 139 O VAL E 225
SHEET 9 AB5 9 THR E 196 MET E 199 -1 O GLU E 198 N VAL E 136
SHEET 1 AB6 4 GLY E 178 SER E 183 0
SHEET 2 AB6 4 GLY E 166 ALA E 171 -1 N PHE E 169 O ILE E 180
SHEET 3 AB6 4 ALA E 157 CYS E 162 -1 N VAL E 159 O SER E 170
SHEET 4 AB6 4 VAL E 203 ALA E 208 -1 O LEU E 205 N ILE E 160
SHEET 1 AB7 9 THR F 59 CYS F 62 0
SHEET 2 AB7 9 PHE F 2 LEU F 6 -1 N GLU F 3 O ARG F 61
SHEET 3 AB7 9 ILE F 87 ALA F 92 -1 O ALA F 92 N PHE F 2
SHEET 4 AB7 9 THR F 98 GLU F 104 -1 O ALA F 100 N ARG F 91
SHEET 5 AB7 9 LYS F 110 LYS F 117 -1 O TYR F 114 N LEU F 101
SHEET 6 AB7 9 GLY G 176 SER G 183 -1 O ASN G 177 N GLU F 115
SHEET 7 AB7 9 GLY G 166 GLY G 173 -1 N ALA G 171 O GLY G 178
SHEET 8 AB7 9 ALA G 157 CYS G 162 -1 N VAL G 159 O SER G 170
SHEET 9 AB7 9 GLN G 204 ALA G 208 -1 O PHE G 207 N VAL G 158
SHEET 1 AB8 9 MET F 68 ASN F 71 0
SHEET 2 AB8 9 GLU F 25 ILE F 30 -1 N ALA F 26 O VAL F 70
SHEET 3 AB8 9 GLY F 34 MET F 40 -1 O ASN F 36 N ASP F 29
SHEET 4 AB8 9 LEU F 47 ARG F 53 -1 O VAL F 48 N SER F 39
SHEET 5 AB8 9 GLY F 245 LEU F 251 -1 O LYS F 248 N GLN F 49
SHEET 6 AB8 9 LEU F 235 ILE F 241 -1 N ILE F 241 O GLY F 245
SHEET 7 AB8 9 THR F 224 MET F 229 -1 N THR F 226 O GLU F 238
SHEET 8 AB8 9 CYS F 135 PRO F 140 -1 N VAL F 137 O LEU F 227
SHEET 9 AB8 9 THR F 196 MET F 199 -1 O GLU F 198 N VAL F 136
SHEET 1 AB9 4 GLY F 178 SER F 183 0
SHEET 2 AB9 4 GLY F 166 ALA F 171 -1 N PHE F 169 O ILE F 180
SHEET 3 AB9 4 ALA F 157 CYS F 162 -1 N VAL F 159 O SER F 170
SHEET 4 AB9 4 VAL F 203 ALA F 208 -1 O PHE F 207 N VAL F 158
SHEET 1 AC1 5 THR G 59 CYS G 62 0
SHEET 2 AC1 5 PHE G 2 LEU G 6 -1 N GLU G 3 O ARG G 61
SHEET 3 AC1 5 ILE G 87 ALA G 92 -1 O ILE G 88 N LEU G 6
SHEET 4 AC1 5 THR G 98 GLU G 104 -1 O ALA G 100 N ARG G 91
SHEET 5 AC1 5 VAL G 111 LYS G 117 -1 O TYR G 114 N LEU G 101
SHEET 1 AC2 9 LEU G 66 ASN G 71 0
SHEET 2 AC2 9 GLU G 25 ILE G 30 -1 N ILE G 30 O LEU G 66
SHEET 3 AC2 9 GLY G 34 MET G 40 -1 O ASN G 36 N ASP G 29
SHEET 4 AC2 9 LEU G 47 ARG G 53 -1 O VAL G 48 N SER G 39
SHEET 5 AC2 9 GLY G 245 LEU G 251 -1 O LYS G 248 N GLN G 49
SHEET 6 AC2 9 LEU G 235 ILE G 241 -1 N LEU G 235 O LEU G 251
SHEET 7 AC2 9 THR G 224 MET G 229 -1 N THR G 226 O GLU G 238
SHEET 8 AC2 9 CYS G 135 PRO G 140 -1 N VAL G 137 O LEU G 227
SHEET 9 AC2 9 THR G 196 MET G 199 -1 O GLU G 198 N VAL G 136
LINK SG CYS A1012 ZN ZN A1201 1555 1555 2.47
LINK SG CYS A1015 ZN ZN A1201 1555 1555 2.25
LINK SG CYS A1026 ZN ZN A1201 1555 1555 2.53
LINK SG CYS A1029 ZN ZN A1201 1555 1555 2.11
LINK SG CYS A1058 FE3 SF4 A1202 1555 1555 2.27
LINK SG CYS A1061 FE4 SF4 A1202 1555 1555 2.38
LINK SG CYS A1071 FE1 SF4 A1202 1555 1555 2.25
LINK SG CYS A1076 FE2 SF4 A1202 1555 1555 2.25
LINK O3' DG P 24 P DOC P 25 1555 1555 1.56
CISPEP 1 SER A 240 PHE A 241 0 6.20
CISPEP 2 GLU A 576 GLY A 577 0 -3.44
CISPEP 3 GLN A 628 LYS A 629 0 3.82
CISPEP 4 SER A 788 PRO A 789 0 6.02
CISPEP 5 PHE A 799 PRO A 800 0 3.21
CISPEP 6 ALA B 378 PRO B 379 0 -4.51
SITE 1 AC1 4 CYS A1012 CYS A1015 CYS A1026 CYS A1029
SITE 1 AC2 6 CYS A1058 CYS A1061 CYS A1071 CYS A1076
SITE 2 AC2 6 ILE A1078 PHE A1079
SITE 1 AC3 12 PHE A 603 SER A 604 SER A 605 LEU A 606
SITE 2 AC3 12 TYR A 607 ARG A 667 LYS A 694 ASN A 698
SITE 3 AC3 12 ASP A 757 DOC P 25 DA T 0 DG T 1
SITE 1 AC4 11 ASP A 755 THR A 756 ASP A 757 TYR A 809
SITE 2 AC4 11 LYS A 827 GLY A 828 TTP A1203 DT P 23
SITE 3 AC4 11 DG T 1 DC T 2 DA T 3
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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