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HEADER PLANT PROTEIN 13-JUN-24 8ZWA
TITLE HOPBY INDUCED AT EDS1-PAD4-ADR1 HETEROTRIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISEASE RESISTANCE PROTEIN ADR1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACTIVATED DISEASE RESISTANCE PROTEIN 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ISOFORM 1 OF PROTEIN EDS1;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PAD4;
COMPND 13 CHAIN: C;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: ADR1, AT1G33560, F10C21.19, T1E4.6;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 10 ORGANISM_COMMON: THALE CRESS;
SOURCE 11 ORGANISM_TAXID: 3702;
SOURCE 12 GENE: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 17 ORGANISM_COMMON: THALE CRESS;
SOURCE 18 ORGANISM_TAXID: 3702;
SOURCE 19 GENE: AXX17_AT3G46840, AN1_LOCUS15608;
SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS EFFECTOR-TRIGGERED IMMUNITY (ETI), TNL SIGNALING PATHWAY, EDS1, PAD4,
KEYWDS 2 ADR1, PLANT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR W.Y.XU,Y.ZHANG,H.YU,L.WAN
REVDAT 1 06-NOV-24 8ZWA 0
JRNL AUTH H.YU,W.XU,S.CHEN,X.WU,W.RAO,X.LIU,X.XU,J.CHEN,M.NISHIMURA,
JRNL AUTH 2 Y.ZHANG,L.WAN
JRNL TITL ACTIVATION OF A HELPER NLR BY PLANT AND BACTERIAL TIR IMMUNE
JRNL TITL 2 SIGNALING
JRNL REF SCIENCE 2024
JRNL REFN ESSN 1095-9203
JRNL DOI 10.1126/SCIENCE.ADR3150
REMARK 2
REMARK 2 RESOLUTION. 3.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
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) : 3.480
REMARK 3 NUMBER OF PARTICLES : 107173
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8ZWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 14-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048640.
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 : AT EDS1-PAD4-ADR1 HETEROTRIMER
REMARK 245 BY HOPBY
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.00
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 TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00
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) : 5500.00
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) : 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 ALA A 2
REMARK 465 SER A 3
REMARK 465 PHE A 4
REMARK 465 ILE A 5
REMARK 465 ASP A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 ALA A 9
REMARK 465 GLY A 10
REMARK 465 ASP A 11
REMARK 465 ILE A 12
REMARK 465 THR A 13
REMARK 465 THR A 14
REMARK 465 GLN A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 17
REMARK 465 LYS A 18
REMARK 465 LEU A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 LEU A 22
REMARK 465 VAL A 23
REMARK 465 ALA A 24
REMARK 465 ASN A 25
REMARK 465 THR A 26
REMARK 465 VAL A 27
REMARK 465 TYR A 28
REMARK 465 SER A 29
REMARK 465 CYS A 30
REMARK 465 LYS A 31
REMARK 465 GLY A 32
REMARK 465 ILE A 33
REMARK 465 ALA A 34
REMARK 465 GLU A 35
REMARK 465 ARG A 36
REMARK 465 LEU A 37
REMARK 465 ILE A 38
REMARK 465 THR A 39
REMARK 465 MET A 40
REMARK 465 ILE A 41
REMARK 465 ARG A 42
REMARK 465 ASP A 43
REMARK 465 VAL A 44
REMARK 465 GLN A 45
REMARK 465 PRO A 46
REMARK 465 THR A 47
REMARK 465 ILE A 48
REMARK 465 ARG A 49
REMARK 465 GLU A 50
REMARK 465 ILE A 51
REMARK 465 GLN A 52
REMARK 465 TYR A 53
REMARK 465 SER A 54
REMARK 465 GLY A 55
REMARK 465 ALA A 56
REMARK 465 GLU A 57
REMARK 465 LEU A 58
REMARK 465 SER A 59
REMARK 465 ASN A 60
REMARK 465 HIS A 61
REMARK 465 HIS A 62
REMARK 465 GLN A 63
REMARK 465 THR A 64
REMARK 465 GLN A 65
REMARK 465 LEU A 66
REMARK 465 GLY A 67
REMARK 465 VAL A 68
REMARK 465 PHE A 69
REMARK 465 TYR A 70
REMARK 465 GLU A 71
REMARK 465 ILE A 72
REMARK 465 LEU A 73
REMARK 465 GLU A 74
REMARK 465 LYS A 75
REMARK 465 ALA A 76
REMARK 465 ARG A 77
REMARK 465 LYS A 78
REMARK 465 LEU A 79
REMARK 465 CYS A 80
REMARK 465 GLU A 81
REMARK 465 LYS A 82
REMARK 465 VAL A 83
REMARK 465 LEU A 84
REMARK 465 ARG A 85
REMARK 465 CYS A 86
REMARK 465 ASN A 87
REMARK 465 ARG A 88
REMARK 465 TRP A 89
REMARK 465 ASN A 90
REMARK 465 LEU A 91
REMARK 465 LYS A 92
REMARK 465 HIS A 93
REMARK 465 VAL A 94
REMARK 465 TYR A 95
REMARK 465 HIS A 96
REMARK 465 ALA A 97
REMARK 465 ASN A 98
REMARK 465 LYS A 99
REMARK 465 MET A 100
REMARK 465 LYS A 101
REMARK 465 ASP A 102
REMARK 465 LEU A 103
REMARK 465 GLU A 104
REMARK 465 LYS A 105
REMARK 465 GLN A 106
REMARK 465 ILE A 107
REMARK 465 SER A 108
REMARK 465 ARG A 109
REMARK 465 PHE A 110
REMARK 465 LEU A 111
REMARK 465 ASN A 112
REMARK 465 SER A 113
REMARK 465 GLN A 114
REMARK 465 ILE A 115
REMARK 465 LEU A 116
REMARK 465 LEU A 117
REMARK 465 PHE A 118
REMARK 465 VAL A 119
REMARK 465 LEU A 120
REMARK 465 ALA A 121
REMARK 465 GLU A 122
REMARK 465 VAL A 123
REMARK 465 CYS A 124
REMARK 465 HIS A 125
REMARK 465 LEU A 126
REMARK 465 ARG A 127
REMARK 465 VAL A 128
REMARK 465 ASN A 129
REMARK 465 GLY A 130
REMARK 465 ASP A 131
REMARK 465 ARG A 132
REMARK 465 ILE A 133
REMARK 465 GLU A 134
REMARK 465 ARG A 135
REMARK 465 ASN A 136
REMARK 465 MET A 137
REMARK 465 ASP A 138
REMARK 465 ARG A 139
REMARK 465 LEU A 140
REMARK 465 LEU A 141
REMARK 465 THR A 142
REMARK 465 GLU A 143
REMARK 465 ARG A 144
REMARK 465 ASN A 145
REMARK 465 ASP A 146
REMARK 465 SER A 147
REMARK 465 LEU A 148
REMARK 465 SER A 149
REMARK 465 PHE A 150
REMARK 465 PRO A 151
REMARK 465 GLU A 152
REMARK 465 THR A 153
REMARK 465 MET A 154
REMARK 465 MET A 155
REMARK 465 GLU A 156
REMARK 465 ILE A 157
REMARK 465 GLU A 158
REMARK 465 THR A 159
REMARK 465 VAL A 160
REMARK 465 SER A 161
REMARK 465 ASP A 162
REMARK 465 PRO A 163
REMARK 465 GLU A 164
REMARK 465 ILE A 165
REMARK 465 GLN A 166
REMARK 465 THR A 167
REMARK 465 VAL A 168
REMARK 465 LEU A 169
REMARK 465 GLU A 170
REMARK 465 LEU A 171
REMARK 465 GLY A 172
REMARK 465 LYS A 173
REMARK 465 LYS A 174
REMARK 465 LYS A 175
REMARK 465 VAL A 176
REMARK 465 LYS A 177
REMARK 465 GLU A 178
REMARK 465 MET A 179
REMARK 465 MET A 180
REMARK 465 PHE A 181
REMARK 465 LYS A 182
REMARK 465 PHE A 183
REMARK 465 THR A 184
REMARK 465 ASP A 185
REMARK 465 THR A 186
REMARK 465 HIS A 187
REMARK 465 LEU A 188
REMARK 465 PHE A 189
REMARK 465 GLY A 190
REMARK 465 ILE A 191
REMARK 465 SER A 192
REMARK 465 GLY A 193
REMARK 465 MET A 194
REMARK 465 SER A 195
REMARK 465 GLY A 196
REMARK 465 SER A 197
REMARK 465 GLY A 198
REMARK 465 LYS A 199
REMARK 465 THR A 200
REMARK 465 THR A 201
REMARK 465 LEU A 202
REMARK 465 ALA A 203
REMARK 465 ILE A 204
REMARK 465 GLU A 205
REMARK 465 LEU A 206
REMARK 465 SER A 207
REMARK 465 LYS A 208
REMARK 465 ASP A 209
REMARK 465 ASP A 210
REMARK 465 ASP A 211
REMARK 465 VAL A 212
REMARK 465 ARG A 213
REMARK 465 GLY A 214
REMARK 465 LEU A 215
REMARK 465 PHE A 216
REMARK 465 LYS A 217
REMARK 465 ASN A 218
REMARK 465 LYS A 219
REMARK 465 VAL A 220
REMARK 465 LEU A 221
REMARK 465 PHE A 222
REMARK 465 LEU A 223
REMARK 465 THR A 224
REMARK 465 VAL A 225
REMARK 465 SER A 226
REMARK 465 ARG A 227
REMARK 465 SER A 228
REMARK 465 PRO A 229
REMARK 465 ASN A 230
REMARK 465 PHE A 231
REMARK 465 GLU A 232
REMARK 465 ASN A 233
REMARK 465 LEU A 234
REMARK 465 GLU A 235
REMARK 465 SER A 236
REMARK 465 CYS A 237
REMARK 465 ILE A 238
REMARK 465 ARG A 239
REMARK 465 GLU A 240
REMARK 465 PHE A 241
REMARK 465 LEU A 242
REMARK 465 TYR A 243
REMARK 465 ASP A 244
REMARK 465 GLY A 245
REMARK 465 VAL A 246
REMARK 465 HIS A 247
REMARK 465 GLN A 248
REMARK 465 ARG A 249
REMARK 465 LYS A 250
REMARK 465 LEU A 251
REMARK 465 VAL A 252
REMARK 465 ILE A 253
REMARK 465 LEU A 254
REMARK 465 ASP A 255
REMARK 465 ASP A 256
REMARK 465 VAL A 257
REMARK 465 TRP A 258
REMARK 465 THR A 259
REMARK 465 ARG A 260
REMARK 465 GLU A 261
REMARK 465 SER A 262
REMARK 465 LEU A 263
REMARK 465 ASP A 264
REMARK 465 ARG A 265
REMARK 465 LEU A 266
REMARK 465 MET A 267
REMARK 465 SER A 268
REMARK 465 LYS A 269
REMARK 465 ILE A 270
REMARK 465 ARG A 271
REMARK 465 GLY A 272
REMARK 465 SER A 273
REMARK 465 THR A 274
REMARK 465 THR A 275
REMARK 465 LEU A 276
REMARK 465 VAL A 277
REMARK 465 VAL A 278
REMARK 465 SER A 279
REMARK 465 ARG A 280
REMARK 465 SER A 281
REMARK 465 LYS A 282
REMARK 465 LEU A 283
REMARK 465 ALA A 284
REMARK 465 ASP A 285
REMARK 465 PRO A 286
REMARK 465 ARG A 287
REMARK 465 THR A 288
REMARK 465 THR A 289
REMARK 465 TYR A 290
REMARK 465 ASN A 291
REMARK 465 VAL A 292
REMARK 465 GLU A 293
REMARK 465 LEU A 294
REMARK 465 LEU A 295
REMARK 465 LYS A 296
REMARK 465 LYS A 297
REMARK 465 ASP A 298
REMARK 465 GLU A 299
REMARK 465 ALA A 300
REMARK 465 MET A 301
REMARK 465 SER A 302
REMARK 465 LEU A 303
REMARK 465 LEU A 304
REMARK 465 CYS A 305
REMARK 465 LEU A 306
REMARK 465 CYS A 307
REMARK 465 ALA A 308
REMARK 465 PHE A 309
REMARK 465 GLU A 310
REMARK 465 GLN A 311
REMARK 465 LYS A 312
REMARK 465 SER A 313
REMARK 465 PRO A 314
REMARK 465 PRO A 315
REMARK 465 SER A 316
REMARK 465 PRO A 317
REMARK 465 PHE A 318
REMARK 465 ASN A 319
REMARK 465 LYS A 320
REMARK 465 TYR A 321
REMARK 465 LEU A 322
REMARK 465 VAL A 323
REMARK 465 LYS A 324
REMARK 465 GLN A 325
REMARK 465 VAL A 326
REMARK 465 VAL A 327
REMARK 465 ASP A 328
REMARK 465 GLU A 329
REMARK 465 CYS A 330
REMARK 465 LYS A 331
REMARK 465 GLY A 332
REMARK 465 LEU A 333
REMARK 465 PRO A 334
REMARK 465 LEU A 335
REMARK 465 SER A 336
REMARK 465 LEU A 337
REMARK 465 LYS A 338
REMARK 465 VAL A 339
REMARK 465 LEU A 340
REMARK 465 GLY A 341
REMARK 465 ALA A 342
REMARK 465 SER A 343
REMARK 465 LEU A 344
REMARK 465 LYS A 345
REMARK 465 ASN A 346
REMARK 465 LYS A 347
REMARK 465 PRO A 348
REMARK 465 GLU A 349
REMARK 465 ARG A 350
REMARK 465 TYR A 351
REMARK 465 TRP A 352
REMARK 465 GLU A 353
REMARK 465 GLY A 354
REMARK 465 VAL A 355
REMARK 465 VAL A 356
REMARK 465 LYS A 357
REMARK 465 ARG A 358
REMARK 465 LEU A 359
REMARK 465 LEU A 360
REMARK 465 ARG A 361
REMARK 465 GLY A 362
REMARK 465 GLU A 363
REMARK 465 ALA A 364
REMARK 465 ALA A 365
REMARK 465 ASP A 366
REMARK 465 GLU A 367
REMARK 465 THR A 368
REMARK 465 HIS A 369
REMARK 465 GLU A 370
REMARK 465 SER A 371
REMARK 465 ARG A 372
REMARK 465 VAL A 373
REMARK 465 MET B 1
REMARK 465 THR B 27
REMARK 465 GLU B 28
REMARK 465 ARG B 29
REMARK 465 ASN B 509
REMARK 465 GLY B 510
REMARK 465 MET B 511
REMARK 465 ILE B 512
REMARK 465 ALA B 513
REMARK 465 GLU B 514
REMARK 465 ASP B 515
REMARK 465 VAL B 516
REMARK 465 PHE B 517
REMARK 465 TRP B 518
REMARK 465 ASN B 519
REMARK 465 LYS B 520
REMARK 465 VAL B 521
REMARK 465 ASN B 522
REMARK 465 GLY B 523
REMARK 465 LEU B 524
REMARK 465 ASN B 525
REMARK 465 LEU B 526
REMARK 465 GLY B 527
REMARK 465 LEU B 528
REMARK 465 GLN B 529
REMARK 465 LEU B 530
REMARK 465 GLU B 531
REMARK 465 GLU B 532
REMARK 465 ILE B 533
REMARK 465 GLN B 534
REMARK 465 GLU B 535
REMARK 465 THR B 536
REMARK 465 LEU B 537
REMARK 465 LYS B 538
REMARK 465 ASN B 539
REMARK 465 SER B 540
REMARK 465 GLY B 541
REMARK 465 SER B 542
REMARK 465 GLU B 543
REMARK 465 CYS B 544
REMARK 465 ASP B 618
REMARK 465 GLU B 619
REMARK 465 ILE B 620
REMARK 465 THR B 621
REMARK 465 ASP B 622
REMARK 465 THR B 623
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 ASP C 3
REMARK 465 CYS C 4
REMARK 465 LEU C 62
REMARK 465 VAL C 63
REMARK 465 GLY C 64
REMARK 465 LEU C 65
REMARK 465 PRO C 66
REMARK 465 GLU C 528
REMARK 465 ILE C 529
REMARK 465 GLU C 530
REMARK 465 MET C 531
REMARK 465 VAL C 532
REMARK 465 VAL C 533
REMARK 465 ASP C 534
REMARK 465 GLU C 535
REMARK 465 SER C 536
REMARK 465 ASP C 537
REMARK 465 ALA C 538
REMARK 465 MET C 539
REMARK 465 GLU C 540
REMARK 465 THR C 541
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 MET A 377 CG SD CE
REMARK 470 LYS A 387 CG CD CE NZ
REMARK 470 MET A 395 CG SD CE
REMARK 470 GLU A 400 CG CD OE1 OE2
REMARK 470 LEU A 406 CG CD1 CD2
REMARK 470 PHE A 427 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 436 CG CD1 CD2
REMARK 470 ILE A 439 CG1 CG2 CD1
REMARK 470 VAL A 440 CG1 CG2
REMARK 470 ASN A 441 CG OD1 ND2
REMARK 470 ARG A 444 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 455 CG1 CG2
REMARK 470 GLN A 459 CG CD OE1 NE2
REMARK 470 ARG A 464 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 468 CG CD1 CD2
REMARK 470 HIS A 469 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 472 CG OD1 ND2
REMARK 470 ARG A 473 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 474 CG1 CG2
REMARK 470 ASP A 475 CG OD1 OD2
REMARK 470 VAL A 476 CG1 CG2
REMARK 470 ASN A 477 CG OD1 ND2
REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 479 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 480 CG CD OE1 OE2
REMARK 470 ARG A 481 CG CD NE CZ NH1 NH2
REMARK 470 THR A 487 OG1 CG2
REMARK 470 VAL A 490 CG1 CG2
REMARK 470 PRO A 492 CG CD
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 494 CG CD OE1 OE2
REMARK 470 TRP A 495 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 495 CZ3 CH2
REMARK 470 GLU A 496 CG CD OE1 OE2
REMARK 470 LYS A 497 CG CD CE NZ
REMARK 470 ASN A 498 CG OD1 ND2
REMARK 470 LYS A 499 CG CD CE NZ
REMARK 470 ASP A 500 CG OD1 OD2
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 PRO A 502 CG CD
REMARK 470 PHE A 503 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 514 CG CD OE1 OE2
REMARK 470 MET A 515 CG SD CE
REMARK 470 ASP A 516 CG OD1 OD2
REMARK 470 GLU A 517 CG CD OE1 OE2
REMARK 470 MET A 518 CG SD CE
REMARK 470 ASN A 519 CG OD1 ND2
REMARK 470 TRP A 520 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 520 CZ3 CH2
REMARK 470 PHE A 521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 523 CG SD CE
REMARK 470 LEU A 531 CG CD1 CD2
REMARK 470 ILE A 532 CG1 CG2 CD1
REMARK 470 TYR A 540 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 542 CG CD1 CD2
REMARK 470 ILE A 546 CG1 CG2 CD1
REMARK 470 MET A 549 CG SD CE
REMARK 470 VAL A 554 CG1 CG2
REMARK 470 HIS A 568 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 572 CG1 CG2 CD1
REMARK 470 PHE A 573 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 575 CG OD1 ND2
REMARK 470 ARG A 586 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 602 CG CD1 CD2
REMARK 470 HIS A 603 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 605 CG1 CG2 CD1
REMARK 470 CYS A 610 SG
REMARK 470 LYS A 613 CG CD CE NZ
REMARK 470 ASN A 614 CG OD1 ND2
REMARK 470 SER A 615 OG
REMARK 470 PHE A 627 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 630 CG CD1 CD2
REMARK 470 LEU A 642 CG CD1 CD2
REMARK 470 ILE A 647 CG1 CG2 CD1
REMARK 470 ARG A 663 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 705 CG OD1 OD2
REMARK 470 ILE A 706 CG1 CG2 CD1
REMARK 470 SER A 714 OG
REMARK 470 LEU A 715 CG CD1 CD2
REMARK 470 PRO A 716 CG CD
REMARK 470 GLU A 717 CG CD OE1 OE2
REMARK 470 LYS A 718 CG CD CE NZ
REMARK 470 PHE A 719 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 727 CG CD CE NZ
REMARK 470 MET A 730 CG SD CE
REMARK 470 LEU A 735 CG CD1 CD2
REMARK 470 LEU A 738 CG CD1 CD2
REMARK 470 VAL A 742 CG1 CG2
REMARK 470 LEU A 748 CG CD1 CD2
REMARK 470 CYS A 753 SG
REMARK 470 TRP A 761 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 761 CZ3 CH2
REMARK 470 MET A 763 CG SD CE
REMARK 470 VAL A 764 CG1 CG2
REMARK 470 VAL A 767 CG1 CG2
REMARK 470 LEU A 771 CG CD1 CD2
REMARK 470 CYS A 772 SG
REMARK 470 ILE A 773 CG1 CG2 CD1
REMARK 470 GLU A 774 CG CD OE1 OE2
REMARK 470 ASP B 12 CG OD1 OD2
REMARK 470 TYR B 25 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 26 CG CD1 CD2
REMARK 470 TYR B 30 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS B 31 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 470 GLU B 33 CG CD OE1 OE2
REMARK 470 LEU B 66 CG CD1 CD2
REMARK 470 ARG B 68 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 100 CG CD NE CZ NH1 NH2
REMARK 470 MET B 109 CG SD CE
REMARK 470 ARG B 112 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 THR B 133 OG1 CG2
REMARK 470 TYR B 140 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2
REMARK 470 SER B 184 OG
REMARK 470 ASP B 187 CG OD1 OD2
REMARK 470 ARG B 191 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 215 CG CD CE NZ
REMARK 470 SER B 216 OG
REMARK 470 SER B 217 OG
REMARK 470 VAL B 218 CG1 CG2
REMARK 470 GLN B 219 CG CD OE1 NE2
REMARK 470 GLU B 252 CG CD OE1 OE2
REMARK 470 GLU B 263 CG CD OE1 OE2
REMARK 470 ARG B 280 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 290 CG1 CG2 CD1
REMARK 470 LEU B 291 CG CD1 CD2
REMARK 470 MET B 293 CG SD CE
REMARK 470 TYR B 296 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 305 CG CD OE1 OE2
REMARK 470 ARG B 312 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 314 CG1 CG2 CD1
REMARK 470 HIS B 317 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 321 CG CD OE1 OE2
REMARK 470 MET B 327 CG SD CE
REMARK 470 LYS B 330 CG CD CE NZ
REMARK 470 ILE B 376 CG1 CG2 CD1
REMARK 470 ILE B 379 CG1 CG2 CD1
REMARK 470 LYS B 411 CG CD CE NZ
REMARK 470 ARG B 425 CG CD NE CZ NH1 NH2
REMARK 470 MET B 439 CG SD CE
REMARK 470 LEU B 457 CG CD1 CD2
REMARK 470 ARG B 460 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 462 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 464 CG CD1 CD2
REMARK 470 LEU B 468 CG CD1 CD2
REMARK 470 ILE B 470 CG1 CG2 CD1
REMARK 470 ARG B 475 CG CD NE CZ NH1 NH2
REMARK 470 MET B 486 CG SD CE
REMARK 470 ILE B 495 CG1 CG2 CD1
REMARK 470 TYR B 504 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 558 CG CD CE NZ
REMARK 470 PRO B 559 CG CD
REMARK 470 TYR B 560 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 561 CG CD OE1 OE2
REMARK 470 GLU B 562 CG CD OE1 OE2
REMARK 470 VAL B 563 CG1 CG2
REMARK 470 LEU B 570 CG CD1 CD2
REMARK 470 GLU B 582 CG CD OE1 OE2
REMARK 470 GLU B 591 CG CD OE1 OE2
REMARK 470 PHE B 595 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 596 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 602 CG CD1 CD2
REMARK 470 MET B 617 CG SD CE
REMARK 470 THR C 8 OG1 CG2
REMARK 470 THR C 19 OG1 CG2
REMARK 470 VAL C 54 CG1 CG2
REMARK 470 MET C 56 CG SD CE
REMARK 470 GLN C 58 CG CD OE1 NE2
REMARK 470 VAL C 67 CG1 CG2
REMARK 470 PHE C 73 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO C 81 CG CD
REMARK 470 MET C 84 CG SD CE
REMARK 470 ASP C 86 CG OD1 OD2
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 LYS C 110 CG CD CE NZ
REMARK 470 VAL C 113 CG1 CG2
REMARK 470 LEU C 129 CG CD1 CD2
REMARK 470 CYS C 144 SG
REMARK 470 ILE C 145 CG1 CG2 CD1
REMARK 470 THR C 146 OG1 CG2
REMARK 470 PHE C 147 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 157 CG CD1 CD2
REMARK 470 HIS C 168 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 173 CG1 CG2
REMARK 470 LEU C 195 CG CD1 CD2
REMARK 470 ARG C 212 CG CD NE CZ NH1 NH2
REMARK 470 MET C 214 CG SD CE
REMARK 470 PHE C 243 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 244 CG CD1 CD2
REMARK 470 ARG C 247 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 282 CG1 CG2
REMARK 470 SER C 385 OG
REMARK 470 LYS C 402 CG CD CE NZ
REMARK 470 LYS C 407 CG CD CE NZ
REMARK 470 ILE C 424 CG1 CG2 CD1
REMARK 470 GLN C 428 CG CD OE1 NE2
REMARK 470 ARG C 439 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 468 CG CD OE1 OE2
REMARK 470 TYR C 488 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL C 498 CG1 CG2
REMARK 470 VAL C 502 CG1 CG2
REMARK 470 LYS C 503 CG CD CE NZ
REMARK 470 ASN C 506 CG OD1 ND2
REMARK 470 SER C 507 OG
REMARK 470 LYS C 517 CG CD CE NZ
REMARK 470 MET C 523 CG SD CE
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 LYS A 486 -11.68 74.74
REMARK 500 VAL A 490 107.79 -57.82
REMARK 500 LYS A 497 26.94 46.01
REMARK 500 ASN A 519 -165.95 72.40
REMARK 500 SER A 536 -149.11 -153.23
REMARK 500 SER A 537 -135.62 53.57
REMARK 500 LEU A 592 55.92 -93.21
REMARK 500 LEU A 644 11.47 -145.61
REMARK 500 TYR A 683 -31.74 -130.23
REMARK 500 CYS A 685 82.12 -160.53
REMARK 500 GLU B 34 81.35 -66.75
REMARK 500 LYS B 79 -7.99 72.61
REMARK 500 SER B 123 -124.53 52.69
REMARK 500 CYS B 547 36.45 -98.04
REMARK 500 GLU C 7 85.23 -68.12
REMARK 500 PRO C 74 3.88 -65.39
REMARK 500 SER C 118 -118.28 54.09
REMARK 500 ASN C 369 51.79 70.71
REMARK 500 LYS C 379 -63.05 61.97
REMARK 500 HIS C 411 -160.21 58.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 389 0.08 SIDE CHAIN
REMARK 500 ARG C 5 0.08 SIDE CHAIN
REMARK 500 ARG C 339 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-60521 RELATED DB: EMDB
REMARK 900 AT EDS1-PAD4-ADR1 HETEROTRIMER BY HOPBY
DBREF 8ZWA A 1 787 UNP Q9FW44 ADR1_ARATH 1 787
DBREF 8ZWA B 1 623 UNP Q9SU72 EDS1C_ARATH 1 623
DBREF1 8ZWA C 1 541 UNP A0A178V847_ARATH
DBREF2 8ZWA C A0A178V847 1 541
SEQRES 1 A 787 MET ALA SER PHE ILE ASP LEU PHE ALA GLY ASP ILE THR
SEQRES 2 A 787 THR GLN LEU LEU LYS LEU LEU ALA LEU VAL ALA ASN THR
SEQRES 3 A 787 VAL TYR SER CYS LYS GLY ILE ALA GLU ARG LEU ILE THR
SEQRES 4 A 787 MET ILE ARG ASP VAL GLN PRO THR ILE ARG GLU ILE GLN
SEQRES 5 A 787 TYR SER GLY ALA GLU LEU SER ASN HIS HIS GLN THR GLN
SEQRES 6 A 787 LEU GLY VAL PHE TYR GLU ILE LEU GLU LYS ALA ARG LYS
SEQRES 7 A 787 LEU CYS GLU LYS VAL LEU ARG CYS ASN ARG TRP ASN LEU
SEQRES 8 A 787 LYS HIS VAL TYR HIS ALA ASN LYS MET LYS ASP LEU GLU
SEQRES 9 A 787 LYS GLN ILE SER ARG PHE LEU ASN SER GLN ILE LEU LEU
SEQRES 10 A 787 PHE VAL LEU ALA GLU VAL CYS HIS LEU ARG VAL ASN GLY
SEQRES 11 A 787 ASP ARG ILE GLU ARG ASN MET ASP ARG LEU LEU THR GLU
SEQRES 12 A 787 ARG ASN ASP SER LEU SER PHE PRO GLU THR MET MET GLU
SEQRES 13 A 787 ILE GLU THR VAL SER ASP PRO GLU ILE GLN THR VAL LEU
SEQRES 14 A 787 GLU LEU GLY LYS LYS LYS VAL LYS GLU MET MET PHE LYS
SEQRES 15 A 787 PHE THR ASP THR HIS LEU PHE GLY ILE SER GLY MET SER
SEQRES 16 A 787 GLY SER GLY LYS THR THR LEU ALA ILE GLU LEU SER LYS
SEQRES 17 A 787 ASP ASP ASP VAL ARG GLY LEU PHE LYS ASN LYS VAL LEU
SEQRES 18 A 787 PHE LEU THR VAL SER ARG SER PRO ASN PHE GLU ASN LEU
SEQRES 19 A 787 GLU SER CYS ILE ARG GLU PHE LEU TYR ASP GLY VAL HIS
SEQRES 20 A 787 GLN ARG LYS LEU VAL ILE LEU ASP ASP VAL TRP THR ARG
SEQRES 21 A 787 GLU SER LEU ASP ARG LEU MET SER LYS ILE ARG GLY SER
SEQRES 22 A 787 THR THR LEU VAL VAL SER ARG SER LYS LEU ALA ASP PRO
SEQRES 23 A 787 ARG THR THR TYR ASN VAL GLU LEU LEU LYS LYS ASP GLU
SEQRES 24 A 787 ALA MET SER LEU LEU CYS LEU CYS ALA PHE GLU GLN LYS
SEQRES 25 A 787 SER PRO PRO SER PRO PHE ASN LYS TYR LEU VAL LYS GLN
SEQRES 26 A 787 VAL VAL ASP GLU CYS LYS GLY LEU PRO LEU SER LEU LYS
SEQRES 27 A 787 VAL LEU GLY ALA SER LEU LYS ASN LYS PRO GLU ARG TYR
SEQRES 28 A 787 TRP GLU GLY VAL VAL LYS ARG LEU LEU ARG GLY GLU ALA
SEQRES 29 A 787 ALA ASP GLU THR HIS GLU SER ARG VAL PHE ALA HIS MET
SEQRES 30 A 787 GLU GLU SER LEU GLU ASN LEU ASP PRO LYS ILE ARG ASP
SEQRES 31 A 787 CYS PHE LEU ASP MET GLY ALA PHE PRO GLU ASP LYS LYS
SEQRES 32 A 787 ILE PRO LEU ASP LEU LEU THR SER VAL TRP VAL GLU ARG
SEQRES 33 A 787 HIS ASP ILE ASP GLU GLU THR ALA PHE SER PHE VAL LEU
SEQRES 34 A 787 ARG LEU ALA ASP LYS ASN LEU LEU THR ILE VAL ASN ASN
SEQRES 35 A 787 PRO ARG PHE GLY ASP VAL HIS ILE GLY TYR TYR ASP VAL
SEQRES 36 A 787 PHE VAL THR GLN HIS ASP VAL LEU ARG ASP LEU ALA LEU
SEQRES 37 A 787 HIS MET SER ASN ARG VAL ASP VAL ASN ARG ARG GLU ARG
SEQRES 38 A 787 LEU LEU MET PRO LYS THR GLU PRO VAL LEU PRO ARG GLU
SEQRES 39 A 787 TRP GLU LYS ASN LYS ASP GLU PRO PHE ASP ALA LYS ILE
SEQRES 40 A 787 VAL SER LEU HIS THR GLY GLU MET ASP GLU MET ASN TRP
SEQRES 41 A 787 PHE ASP MET ASP LEU PRO LYS ALA GLU VAL LEU ILE LEU
SEQRES 42 A 787 ASN PHE SER SER ASP ASN TYR VAL LEU PRO PRO PHE ILE
SEQRES 43 A 787 GLY LYS MET SER ARG LEU ARG VAL LEU VAL ILE ILE ASN
SEQRES 44 A 787 ASN GLY MET SER PRO ALA ARG LEU HIS GLY PHE SER ILE
SEQRES 45 A 787 PHE ALA ASN LEU ALA LYS LEU ARG SER LEU TRP LEU LYS
SEQRES 46 A 787 ARG VAL HIS VAL PRO GLU LEU THR SER CYS THR ILE PRO
SEQRES 47 A 787 LEU LYS ASN LEU HIS LYS ILE HIS LEU ILE PHE CYS LYS
SEQRES 48 A 787 VAL LYS ASN SER PHE VAL GLN THR SER PHE ASP ILE SER
SEQRES 49 A 787 LYS ILE PHE PRO SER LEU SER ASP LEU THR ILE ASP HIS
SEQRES 50 A 787 CYS ASP ASP LEU LEU GLU LEU LYS SER ILE PHE GLY ILE
SEQRES 51 A 787 THR SER LEU ASN SER LEU SER ILE THR ASN CYS PRO ARG
SEQRES 52 A 787 ILE LEU GLU LEU PRO LYS ASN LEU SER ASN VAL GLN SER
SEQRES 53 A 787 LEU GLU ARG LEU ARG LEU TYR ALA CYS PRO GLU LEU ILE
SEQRES 54 A 787 SER LEU PRO VAL GLU VAL CYS GLU LEU PRO CYS LEU LYS
SEQRES 55 A 787 TYR VAL ASP ILE SER GLN CYS VAL SER LEU VAL SER LEU
SEQRES 56 A 787 PRO GLU LYS PHE GLY LYS LEU GLY SER LEU GLU LYS ILE
SEQRES 57 A 787 ASP MET ARG GLU CYS SER LEU LEU GLY LEU PRO SER SER
SEQRES 58 A 787 VAL ALA ALA LEU VAL SER LEU ARG HIS VAL ILE CYS ASP
SEQRES 59 A 787 GLU GLU THR SER SER MET TRP GLU MET VAL LYS LYS VAL
SEQRES 60 A 787 VAL PRO GLU LEU CYS ILE GLU VAL ALA LYS LYS CYS PHE
SEQRES 61 A 787 THR VAL ASP TRP LEU ASP ASP
SEQRES 1 B 623 MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 2 B 623 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 3 B 623 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 4 B 623 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 5 B 623 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 6 B 623 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 7 B 623 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 8 B 623 ASN LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN
SEQRES 9 B 623 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 10 B 623 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 11 B 623 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 12 B 623 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 13 B 623 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 14 B 623 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 15 B 623 VAL SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA
SEQRES 16 B 623 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 17 B 623 ALA GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER
SEQRES 18 B 623 GLU GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG
SEQRES 19 B 623 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 20 B 623 THR GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER
SEQRES 21 B 623 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 22 B 623 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 23 B 623 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN
SEQRES 24 B 623 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 25 B 623 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 26 B 623 SER MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 27 B 623 ASN SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER
SEQRES 28 B 623 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 29 B 623 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 30 B 623 VAL ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 31 B 623 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 32 B 623 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 33 B 623 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 34 B 623 GLY VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS
SEQRES 35 B 623 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 36 B 623 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 37 B 623 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 38 B 623 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 39 B 623 ILE TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS
SEQRES 40 B 623 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 41 B 623 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 42 B 623 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 43 B 623 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 44 B 623 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 45 B 623 MET LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP
SEQRES 46 B 623 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 47 B 623 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 48 B 623 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR
SEQRES 1 C 541 MET ASP ASP CYS ARG PHE GLU THR SER GLU LEU GLN ALA
SEQRES 2 C 541 SER VAL MET ILE SER THR PRO LEU PHE THR ASP SER TRP
SEQRES 3 C 541 SER SER CYS ASN THR ALA ASN CYS ASN GLY SER ILE LYS
SEQRES 4 C 541 ILE HIS ASP ILE ALA GLY ILE THR TYR VAL ALA ILE PRO
SEQRES 5 C 541 ALA VAL SER MET ILE GLN LEU GLY ASN LEU VAL GLY LEU
SEQRES 6 C 541 PRO VAL THR GLY ASP VAL LEU PHE PRO GLY LEU SER SER
SEQRES 7 C 541 ASP GLU PRO LEU PRO MET VAL ASP ALA ALA ILE LEU LYS
SEQRES 8 C 541 LEU PHE LEU GLN LEU LYS ILE LYS GLU GLY LEU GLU LEU
SEQRES 9 C 541 GLU LEU LEU GLY LYS LYS LEU VAL VAL ILE THR GLY HIS
SEQRES 10 C 541 SER THR GLY GLY ALA LEU ALA ALA PHE THR ALA LEU TRP
SEQRES 11 C 541 LEU LEU SER GLN SER SER PRO PRO SER PHE ARG VAL PHE
SEQRES 12 C 541 CYS ILE THR PHE GLY SER PRO LEU LEU GLY ASN GLN SER
SEQRES 13 C 541 LEU SER THR SER ILE SER ARG SER ARG LEU ALA HIS ASN
SEQRES 14 C 541 PHE CYS HIS VAL VAL SER ILE HIS ASP LEU VAL PRO ARG
SEQRES 15 C 541 SER SER ASN GLU GLN PHE TRP PRO PHE GLY THR TYR LEU
SEQRES 16 C 541 PHE CYS SER ASP LYS GLY GLY VAL CYS LEU ASP ASN ALA
SEQRES 17 C 541 GLY SER VAL ARG LEU MET PHE ASN ILE LEU ASN THR THR
SEQRES 18 C 541 ALA THR GLN ASN THR GLU GLU HIS GLN ARG TYR GLY HIS
SEQRES 19 C 541 TYR VAL PHE THR LEU SER HIS MET PHE LEU LYS SER ARG
SEQRES 20 C 541 SER PHE LEU GLY GLY SER ILE PRO ASP ASN SER TYR GLN
SEQRES 21 C 541 ALA GLY VAL ALA LEU ALA VAL GLU ALA LEU GLY PHE SER
SEQRES 22 C 541 ASN ASP ASP THR SER GLY VAL LEU VAL LYS GLU CYS ILE
SEQRES 23 C 541 GLU THR ALA THR ARG ILE VAL ARG ALA PRO ILE LEU ARG
SEQRES 24 C 541 SER ALA GLU LEU ALA ASN GLU LEU ALA SER VAL LEU PRO
SEQRES 25 C 541 ALA ARG LEU GLU ILE GLN TRP TYR LYS ASP ARG CYS ASP
SEQRES 26 C 541 ALA SER GLU GLU GLN LEU GLY TYR TYR ASP PHE PHE LYS
SEQRES 27 C 541 ARG TYR SER LEU LYS ARG ASP PHE LYS VAL ASN MET SER
SEQRES 28 C 541 ARG ILE ARG LEU ALA LYS PHE TRP ASP THR VAL ILE LYS
SEQRES 29 C 541 MET VAL GLU THR ASN GLU LEU PRO PHE ASP PHE HIS LEU
SEQRES 30 C 541 GLY LYS LYS TRP ILE TYR ALA SER GLN PHE TYR GLN LEU
SEQRES 31 C 541 LEU ALA GLU PRO LEU ASP ILE ALA ASN PHE TYR LYS ASN
SEQRES 32 C 541 ARG ASP ILE LYS THR GLY GLY HIS TYR LEU GLU GLY ASN
SEQRES 33 C 541 ARG PRO LYS ARG TYR GLU VAL ILE ASP LYS TRP GLN LYS
SEQRES 34 C 541 GLY VAL LYS VAL PRO GLU GLU CYS VAL ARG SER ARG TYR
SEQRES 35 C 541 ALA SER THR THR GLN ASP THR CYS PHE TRP ALA LYS LEU
SEQRES 36 C 541 GLU GLN ALA LYS GLU TRP LEU ASP GLU ALA ARG LYS GLU
SEQRES 37 C 541 SER SER ASP PRO GLN ARG ARG SER LEU LEU ARG GLU LYS
SEQRES 38 C 541 ILE VAL PRO PHE GLU SER TYR ALA ASN THR LEU VAL THR
SEQRES 39 C 541 LYS LYS GLU VAL SER LEU ASP VAL LYS ALA LYS ASN SER
SEQRES 40 C 541 SER TYR SER VAL TRP GLU ALA ASN LEU LYS GLU PHE LYS
SEQRES 41 C 541 CYS LYS MET GLY TYR GLU ASN GLU ILE GLU MET VAL VAL
SEQRES 42 C 541 ASP GLU SER ASP ALA MET GLU THR
HET RIA B 701 36
HETNAM RIA 2'-O-[(5'-PHOSPHO)RIBOSYL]ADENOSINE-5'-MONOPHOSPHATE
FORMUL 4 RIA C15 H23 N5 O14 P2
HELIX 1 AA1 PHE A 374 LEU A 384 1 11
HELIX 2 AA2 ASP A 385 GLY A 396 1 12
HELIX 3 AA3 PRO A 405 ASP A 418 1 14
HELIX 4 AA4 ASP A 420 LYS A 434 1 15
HELIX 5 AA5 ASN A 442 ASP A 447 5 6
HELIX 6 AA6 HIS A 460 SER A 471 1 12
HELIX 7 AA7 SER A 471 VAL A 476 1 6
HELIX 8 AA8 MET A 484 GLU A 488 5 5
HELIX 9 AA9 TRP A 495 LYS A 499 5 5
HELIX 10 AB1 PRO A 544 MET A 549 1 6
HELIX 11 AB2 PHE A 570 ASN A 575 1 6
HELIX 12 AB3 ASP A 622 PHE A 627 1 6
HELIX 13 AB4 LEU A 644 ILE A 650 1 7
HELIX 14 AB5 PRO A 692 LEU A 698 5 7
HELIX 15 AB6 PRO A 739 LEU A 745 1 7
HELIX 16 AB7 THR A 757 VAL A 768 1 12
HELIX 17 AB8 VAL A 782 ASP A 786 5 5
HELIX 18 AB9 PHE B 3 GLY B 8 1 6
HELIX 19 AC1 ASN B 10 LEU B 26 1 17
HELIX 20 AC2 SER B 48 PHE B 53 1 6
HELIX 21 AC3 ASN B 86 ASP B 98 1 13
HELIX 22 AC4 SER B 102 SER B 113 1 12
HELIX 23 AC5 SER B 123 PHE B 141 1 19
HELIX 24 AC6 ASP B 163 GLU B 173 1 11
HELIX 25 AC7 TRP B 175 ARG B 177 5 3
HELIX 26 AC8 ARG B 196 GLU B 202 1 7
HELIX 27 AC9 THR B 203 ASP B 212 1 10
HELIX 28 AD1 SER B 221 THR B 248 1 28
HELIX 29 AD2 ALA B 251 LEU B 262 1 12
HELIX 30 AD3 ASN B 286 SER B 298 1 13
HELIX 31 AD4 LEU B 308 HIS B 317 1 10
HELIX 32 AD5 SER B 319 SER B 326 1 8
HELIX 33 AD6 ILE B 341 GLY B 349 1 9
HELIX 34 AD7 SER B 351 GLN B 381 1 31
HELIX 35 AD8 GLN B 381 GLU B 394 1 14
HELIX 36 AD9 GLU B 394 HIS B 402 1 9
HELIX 37 AE1 GLY B 405 VAL B 412 1 8
HELIX 38 AE2 GLU B 415 LYS B 441 1 27
HELIX 39 AE3 ASP B 451 HIS B 476 1 26
HELIX 40 AE4 LEU B 477 ASP B 481 5 5
HELIX 41 AE5 PRO B 491 LYS B 507 1 17
HELIX 42 AE6 CYS B 547 LYS B 556 1 10
HELIX 43 AE7 TYR B 560 GLY B 581 1 22
HELIX 44 AE8 ASP B 584 PHE B 589 1 6
HELIX 45 AE9 SER B 593 LEU B 602 1 10
HELIX 46 AF1 PRO B 603 SER B 610 1 8
HELIX 47 AF2 LEU B 612 MET B 617 1 6
HELIX 48 AF3 THR C 8 THR C 19 1 12
HELIX 49 AF4 THR C 19 GLY C 36 1 18
HELIX 50 AF5 ASP C 86 LEU C 96 1 11
HELIX 51 AF6 LYS C 97 LEU C 106 1 10
HELIX 52 AF7 SER C 118 SER C 133 1 16
HELIX 53 AF8 ASN C 154 SER C 164 1 11
HELIX 54 AF9 ASN C 207 THR C 221 1 15
HELIX 55 AG1 GLU C 227 HIS C 241 1 15
HELIX 56 AG2 ASN C 257 LEU C 270 1 14
HELIX 57 AG3 ASP C 276 THR C 290 1 15
HELIX 58 AG4 ALA C 295 SER C 327 1 33
HELIX 59 AG5 GLY C 332 ARG C 339 1 8
HELIX 60 AG6 LEU C 342 ASN C 369 1 28
HELIX 61 AG7 PRO C 372 GLY C 378 5 7
HELIX 62 AG8 LYS C 379 ARG C 404 1 26
HELIX 63 AG9 PRO C 418 GLY C 430 1 13
HELIX 64 AH1 CYS C 450 GLU C 468 1 19
HELIX 65 AH2 ASP C 471 LYS C 495 1 25
HELIX 66 AH3 SER C 507 GLY C 524 1 18
SHEET 1 AA1 2 THR A 438 ILE A 439 0
SHEET 2 AA1 2 VAL A 457 THR A 458 -1 O THR A 458 N THR A 438
SHEET 1 AA211 SER A 509 HIS A 511 0
SHEET 2 AA211 ILE A 532 PHE A 535 1 O ASN A 534 N LEU A 510
SHEET 3 AA211 VAL A 554 ASN A 559 1 O ILE A 558 N PHE A 535
SHEET 4 AA211 SER A 581 LYS A 585 1 O TRP A 583 N ILE A 557
SHEET 5 AA211 LYS A 604 ILE A 608 1 O HIS A 606 N LEU A 584
SHEET 6 AA211 ASP A 632 ASP A 636 1 O THR A 634 N LEU A 607
SHEET 7 AA211 SER A 655 THR A 659 1 O SER A 657 N ILE A 635
SHEET 8 AA211 ARG A 679 LEU A 682 1 O ARG A 679 N LEU A 656
SHEET 9 AA211 TYR A 703 ILE A 706 1 O ASP A 705 N LEU A 682
SHEET 10 AA211 LYS A 727 ASP A 729 1 O ASP A 729 N VAL A 704
SHEET 11 AA211 ARG A 749 ILE A 752 1 O ILE A 752 N ILE A 728
SHEET 1 AA3 2 TYR A 540 VAL A 541 0
SHEET 2 AA3 2 LEU A 567 HIS A 568 1 O HIS A 568 N TYR A 540
SHEET 1 AA4 8 HIS B 31 ALA B 35 0
SHEET 2 AA4 8 VAL B 38 ALA B 42 -1 O ALA B 42 N HIS B 31
SHEET 3 AA4 8 GLN B 116 HIS B 122 1 O THR B 120 N PHE B 41
SHEET 4 AA4 8 ARG B 152 PHE B 156 1 O ARG B 152 N PHE B 119
SHEET 5 AA4 8 PHE B 179 SER B 184 1 O PHE B 182 N THR B 155
SHEET 6 AA4 8 THR B 272 SER B 276 1 O VAL B 274 N ASN B 181
SHEET 7 AA4 8 ARG B 280 ALA B 283 -1 O VAL B 282 N PHE B 275
SHEET 8 AA4 8 LEU B 331 HIS B 334 1 O LEU B 331 N LEU B 281
SHEET 1 AA5 2 ILE B 64 LYS B 65 0
SHEET 2 AA5 2 THR B 84 VAL B 85 -1 O VAL B 85 N ILE B 64
SHEET 1 AA6 4 LYS C 39 ILE C 43 0
SHEET 2 AA6 4 ILE C 46 ALA C 50 -1 O ILE C 46 N ILE C 43
SHEET 3 AA6 4 LEU C 111 THR C 115 1 O VAL C 113 N THR C 47
SHEET 4 AA6 4 ARG C 141 CYS C 144 1 O PHE C 143 N ILE C 114
SHEET 1 AA7 3 CYS C 171 SER C 175 0
SHEET 2 AA7 3 THR C 193 CYS C 197 1 O LEU C 195 N VAL C 174
SHEET 3 AA7 3 GLY C 202 LEU C 205 -1 O LEU C 205 N TYR C 194
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
TER 2970 ASP A 787
TER 7387 MET B 617
TER 11362 ASN C 527
MASTER 818 0 1 66 32 0 0 611395 3 36 151
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