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HEADER HORMONE 09-FEB-25 9LUO
TITLE CRYO-EM STRUCTURE OF ARABIDOPSIS THALIANA RGA IN COMPLEX WITH GID1A,
TITLE 2 SLY1, AND ASK2 (FOCUSED MAP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELLA PROTEIN RGA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GAI-RELATED SEQUENCE,GRAS FAMILY PROTEIN 10,ATGRAS-10,
COMPND 5 REPRESSOR ON THE GA1-3 MUTANT,RESTORATION OF GROWTH ON AMMONIA
COMPND 6 PROTEIN 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: F-BOX PROTEIN GID2;
COMPND 10 CHAIN: C;
COMPND 11 SYNONYM: PROTEIN SLEEPY 1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: SKP1-LIKE PROTEIN 1B;
COMPND 15 CHAIN: D;
COMPND 16 SYNONYM: SKP1-LIKE 2,UFO-BINDING PROTEIN 2;
COMPND 17 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: RGA, GRS, RGA1, AT2G01570, F2I9.19;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
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: GID2, SLY1, AT4G24210, T22A6.40;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
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: SKP1B, ASK2, UIP2, AT5G42190, MJC20.30;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS GIBBERELLIN, DELLA MOTIF, GRAS DOMAIN, PLANT GROWTH, HORMONE
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.ISLAM,K.PARK,E.KWON,D.Y.KIM
REVDAT 1 09-JUL-25 9LUO 0
JRNL AUTH S.ISLAM,K.PARK,J.XIA,E.KWON,D.Y.KIM
JRNL TITL STRUCTURAL INSIGHTS OF GIBBERELLIN-MEDIATED DELLA PROTEIN
JRNL TITL 2 DEGRADATION.
JRNL REF MOL PLANT 2025
JRNL REFN ESSN 1752-9867
JRNL PMID 40542507
JRNL DOI 10.1016/J.MOLP.2025.06.010
REMARK 2
REMARK 2 RESOLUTION. 3.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX
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) : 3.070
REMARK 3 NUMBER OF PARTICLES : 65737
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 9LUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-FEB-25.
REMARK 100 THE DEPOSITION ID IS D_1300053362.
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 : PARTIAL MODEL OF
REMARK 245 RGA/GID1A/SLY/ASK2
REMARK 245 HETEROTETRAMER
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 : PARTIAL MODEL OF
REMARK 245 RGA/GID1A/SLY/ASK2 HETEROTETRAMER
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 : TFS KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 600.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2700.00
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) : 6000.00
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, C, D
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 LYS A 2
REMARK 465 ARG A 3
REMARK 465 ASP A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 GLN A 7
REMARK 465 PHE A 8
REMARK 465 GLN A 9
REMARK 465 GLY A 10
REMARK 465 ARG A 11
REMARK 465 LEU A 12
REMARK 465 SER A 13
REMARK 465 ASN A 14
REMARK 465 HIS A 15
REMARK 465 GLY A 16
REMARK 465 THR A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 SER A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 ILE A 24
REMARK 465 SER A 25
REMARK 465 LYS A 26
REMARK 465 ASP A 27
REMARK 465 LYS A 28
REMARK 465 MET A 29
REMARK 465 MET A 30
REMARK 465 MET A 31
REMARK 465 VAL A 32
REMARK 465 LYS A 33
REMARK 465 LYS A 34
REMARK 465 GLU A 35
REMARK 465 GLU A 36
REMARK 465 ASP A 37
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 GLY A 40
REMARK 465 ASN A 41
REMARK 465 MET A 42
REMARK 465 ASP A 43
REMARK 465 ASP A 44
REMARK 465 GLU A 45
REMARK 465 LEU A 46
REMARK 465 LEU A 47
REMARK 465 ALA A 48
REMARK 465 VAL A 49
REMARK 465 LEU A 50
REMARK 465 GLY A 51
REMARK 465 TYR A 52
REMARK 465 LYS A 53
REMARK 465 VAL A 54
REMARK 465 ARG A 55
REMARK 465 SER A 56
REMARK 465 SER A 57
REMARK 465 GLU A 58
REMARK 465 MET A 59
REMARK 465 ALA A 60
REMARK 465 GLU A 61
REMARK 465 VAL A 62
REMARK 465 ALA A 63
REMARK 465 LEU A 64
REMARK 465 LYS A 65
REMARK 465 LEU A 66
REMARK 465 GLU A 67
REMARK 465 GLN A 68
REMARK 465 LEU A 69
REMARK 465 GLU A 70
REMARK 465 THR A 71
REMARK 465 MET A 72
REMARK 465 MET A 73
REMARK 465 SER A 74
REMARK 465 ASN A 75
REMARK 465 VAL A 76
REMARK 465 GLN A 77
REMARK 465 GLU A 78
REMARK 465 ASP A 79
REMARK 465 GLY A 80
REMARK 465 LEU A 81
REMARK 465 SER A 82
REMARK 465 HIS A 83
REMARK 465 LEU A 84
REMARK 465 ALA A 85
REMARK 465 THR A 86
REMARK 465 ASP A 87
REMARK 465 THR A 88
REMARK 465 VAL A 89
REMARK 465 HIS A 90
REMARK 465 TYR A 91
REMARK 465 ASN A 92
REMARK 465 PRO A 93
REMARK 465 SER A 94
REMARK 465 GLU A 95
REMARK 465 LEU A 96
REMARK 465 TYR A 97
REMARK 465 SER A 98
REMARK 465 TRP A 99
REMARK 465 LEU A 100
REMARK 465 ASP A 101
REMARK 465 ASN A 102
REMARK 465 MET A 103
REMARK 465 LEU A 104
REMARK 465 SER A 105
REMARK 465 GLU A 106
REMARK 465 LEU A 107
REMARK 465 ASN A 108
REMARK 465 PRO A 109
REMARK 465 PRO A 110
REMARK 465 PRO A 111
REMARK 465 LEU A 112
REMARK 465 PRO A 113
REMARK 465 ALA A 114
REMARK 465 SER A 115
REMARK 465 SER A 116
REMARK 465 ASN A 117
REMARK 465 GLY A 118
REMARK 465 LEU A 119
REMARK 465 ASP A 120
REMARK 465 PRO A 121
REMARK 465 VAL A 122
REMARK 465 LEU A 123
REMARK 465 PRO A 124
REMARK 465 SER A 125
REMARK 465 PRO A 126
REMARK 465 GLU A 127
REMARK 465 ILE A 128
REMARK 465 CYS A 129
REMARK 465 GLY A 130
REMARK 465 PHE A 131
REMARK 465 PRO A 132
REMARK 465 ALA A 133
REMARK 465 SER A 134
REMARK 465 ASP A 135
REMARK 465 TYR A 136
REMARK 465 ASP A 137
REMARK 465 LEU A 138
REMARK 465 LYS A 139
REMARK 465 VAL A 140
REMARK 465 ILE A 141
REMARK 465 PRO A 142
REMARK 465 GLY A 143
REMARK 465 ASN A 144
REMARK 465 ALA A 145
REMARK 465 ILE A 146
REMARK 465 TYR A 147
REMARK 465 GLN A 148
REMARK 465 PHE A 149
REMARK 465 PRO A 150
REMARK 465 ALA A 151
REMARK 465 ILE A 152
REMARK 465 ASP A 153
REMARK 465 SER A 154
REMARK 465 SER A 155
REMARK 465 SER A 156
REMARK 465 SER A 157
REMARK 465 SER A 158
REMARK 465 ASN A 159
REMARK 465 ASN A 160
REMARK 465 GLN A 161
REMARK 465 ASN A 162
REMARK 465 LYS A 163
REMARK 465 ARG A 164
REMARK 465 LEU A 165
REMARK 465 LYS A 166
REMARK 465 SER A 167
REMARK 465 CYS A 168
REMARK 465 SER A 169
REMARK 465 SER A 170
REMARK 465 PRO A 171
REMARK 465 ASP A 172
REMARK 465 SER A 173
REMARK 465 MET A 174
REMARK 465 VAL A 175
REMARK 465 THR A 176
REMARK 465 SER A 177
REMARK 465 THR A 178
REMARK 465 SER A 179
REMARK 465 THR A 180
REMARK 465 GLY A 181
REMARK 465 THR A 182
REMARK 465 GLN A 183
REMARK 465 ILE A 184
REMARK 465 GLY A 185
REMARK 465 GLY A 186
REMARK 465 VAL A 187
REMARK 465 ILE A 188
REMARK 465 GLY A 189
REMARK 465 THR A 190
REMARK 465 THR A 191
REMARK 465 VAL A 192
REMARK 465 THR A 193
REMARK 465 THR A 194
REMARK 465 THR A 195
REMARK 465 THR A 196
REMARK 465 THR A 197
REMARK 465 THR A 198
REMARK 465 THR A 199
REMARK 465 THR A 200
REMARK 465 ALA A 201
REMARK 465 ALA A 202
REMARK 465 GLY A 203
REMARK 465 GLU A 204
REMARK 465 SER A 205
REMARK 465 THR A 206
REMARK 465 ARG A 207
REMARK 465 SER A 208
REMARK 465 VAL A 209
REMARK 465 ILE A 210
REMARK 465 LEU A 211
REMARK 465 VAL A 212
REMARK 465 ASP A 213
REMARK 465 SER A 214
REMARK 465 GLN A 215
REMARK 465 GLU A 216
REMARK 465 ASN A 217
REMARK 465 GLY A 218
REMARK 465 VAL A 219
REMARK 465 ARG A 220
REMARK 465 LEU A 221
REMARK 465 VAL A 222
REMARK 465 HIS A 223
REMARK 465 ALA A 224
REMARK 465 LEU A 225
REMARK 465 MET A 226
REMARK 465 ALA A 227
REMARK 465 CYS A 228
REMARK 465 ALA A 229
REMARK 465 GLU A 230
REMARK 465 ALA A 231
REMARK 465 ILE A 232
REMARK 465 GLN A 233
REMARK 465 GLN A 234
REMARK 465 ASN A 235
REMARK 465 ASN A 236
REMARK 465 LEU A 237
REMARK 465 THR A 238
REMARK 465 LEU A 239
REMARK 465 ALA A 240
REMARK 465 GLU A 241
REMARK 465 ALA A 242
REMARK 465 LEU A 243
REMARK 465 VAL A 244
REMARK 465 LYS A 245
REMARK 465 GLN A 246
REMARK 465 ILE A 247
REMARK 465 GLY A 248
REMARK 465 CYS A 249
REMARK 465 LEU A 250
REMARK 465 ALA A 251
REMARK 465 VAL A 252
REMARK 465 SER A 253
REMARK 465 GLN A 254
REMARK 465 ALA A 255
REMARK 465 GLY A 256
REMARK 465 ALA A 257
REMARK 465 MET A 258
REMARK 465 ARG A 259
REMARK 465 LYS A 260
REMARK 465 VAL A 261
REMARK 465 ALA A 262
REMARK 465 THR A 263
REMARK 465 TYR A 264
REMARK 465 PHE A 265
REMARK 465 ALA A 266
REMARK 465 GLU A 267
REMARK 465 ALA A 268
REMARK 465 LEU A 269
REMARK 465 ALA A 270
REMARK 465 ARG A 271
REMARK 465 ARG A 272
REMARK 465 ILE A 273
REMARK 465 TYR A 274
REMARK 465 ARG A 275
REMARK 465 LEU A 276
REMARK 465 SER A 277
REMARK 465 PRO A 278
REMARK 465 PRO A 279
REMARK 465 GLN A 280
REMARK 465 ASN A 281
REMARK 465 GLN A 282
REMARK 465 ILE A 283
REMARK 465 ASP A 284
REMARK 465 HIS A 285
REMARK 465 CYS A 286
REMARK 465 LEU A 287
REMARK 465 SER A 288
REMARK 465 ASP A 289
REMARK 465 THR A 290
REMARK 465 LEU A 291
REMARK 465 GLN A 292
REMARK 465 MET A 293
REMARK 465 HIS A 294
REMARK 465 PHE A 295
REMARK 465 TYR A 296
REMARK 465 GLU A 297
REMARK 465 THR A 298
REMARK 465 CYS A 299
REMARK 465 PHE A 317
REMARK 465 GLU A 318
REMARK 465 GLY A 319
REMARK 465 LYS A 320
REMARK 465 LYS A 321
REMARK 465 ARG A 322
REMARK 465 VAL A 323
REMARK 465 HIS A 324
REMARK 465 VAL A 325
REMARK 465 ILE A 326
REMARK 465 ASP A 327
REMARK 465 PHE A 328
REMARK 465 PRO A 351
REMARK 465 THR A 352
REMARK 465 PHE A 353
REMARK 465 ARG A 354
REMARK 465 LEU A 355
REMARK 465 THR A 356
REMARK 465 GLY A 357
REMARK 465 ILE A 358
REMARK 465 GLY A 359
REMARK 465 PRO A 360
REMARK 465 PRO A 361
REMARK 465 ALA A 362
REMARK 465 PRO A 363
REMARK 465 ASP A 364
REMARK 465 ASN A 365
REMARK 465 SER A 366
REMARK 465 ASP A 367
REMARK 465 PHE A 387
REMARK 465 GLU A 388
REMARK 465 TYR A 389
REMARK 465 ARG A 390
REMARK 465 GLY A 391
REMARK 465 PHE A 392
REMARK 465 VAL A 393
REMARK 465 ALA A 394
REMARK 465 ASN A 395
REMARK 465 SER A 396
REMARK 465 LEU A 397
REMARK 465 ALA A 398
REMARK 465 ASP A 399
REMARK 465 LEU A 400
REMARK 465 ASP A 401
REMARK 465 ALA A 402
REMARK 465 SER A 403
REMARK 465 MET A 404
REMARK 465 LEU A 405
REMARK 465 GLU A 406
REMARK 465 LEU A 407
REMARK 465 ARG A 408
REMARK 465 PRO A 409
REMARK 465 SER A 410
REMARK 465 ASP A 411
REMARK 465 THR A 412
REMARK 465 GLU A 413
REMARK 465 ALA A 414
REMARK 465 VAL A 415
REMARK 465 ALA A 416
REMARK 465 VAL A 417
REMARK 465 ASN A 418
REMARK 465 SER A 419
REMARK 465 VAL A 420
REMARK 465 PHE A 421
REMARK 465 GLU A 422
REMARK 465 LEU A 423
REMARK 465 HIS A 424
REMARK 465 LYS A 425
REMARK 465 LEU A 426
REMARK 465 LEU A 427
REMARK 465 GLY A 428
REMARK 465 ARG A 429
REMARK 465 PRO A 430
REMARK 465 GLY A 431
REMARK 465 GLY A 432
REMARK 465 ILE A 433
REMARK 465 GLU A 434
REMARK 465 LYS A 435
REMARK 465 VAL A 436
REMARK 465 LEU A 437
REMARK 465 GLY A 438
REMARK 465 VAL A 439
REMARK 465 VAL A 440
REMARK 465 LYS A 441
REMARK 465 GLN A 442
REMARK 465 ILE A 443
REMARK 465 LYS A 444
REMARK 465 PRO A 445
REMARK 465 VAL A 446
REMARK 465 ILE A 447
REMARK 465 PHE A 448
REMARK 465 THR A 449
REMARK 465 VAL A 450
REMARK 465 VAL A 451
REMARK 465 GLU A 452
REMARK 465 GLN A 453
REMARK 465 GLU A 454
REMARK 465 SER A 455
REMARK 465 ASN A 456
REMARK 465 HIS A 457
REMARK 465 ASN A 458
REMARK 465 GLY A 459
REMARK 465 PRO A 460
REMARK 465 VAL A 461
REMARK 465 PHE A 462
REMARK 465 LEU A 463
REMARK 465 ASP A 464
REMARK 465 ARG A 465
REMARK 465 PHE A 466
REMARK 465 THR A 467
REMARK 465 GLU A 468
REMARK 465 SER A 469
REMARK 465 LEU A 470
REMARK 465 HIS A 471
REMARK 465 TYR A 472
REMARK 465 TYR A 473
REMARK 465 SER A 474
REMARK 465 THR A 475
REMARK 465 LEU A 476
REMARK 465 PHE A 477
REMARK 465 ASP A 478
REMARK 465 SER A 479
REMARK 465 LEU A 480
REMARK 465 GLU A 481
REMARK 465 GLY A 482
REMARK 465 VAL A 483
REMARK 465 PRO A 484
REMARK 465 ASN A 485
REMARK 465 SER A 486
REMARK 465 GLN A 487
REMARK 465 ASP A 488
REMARK 465 LYS A 489
REMARK 465 VAL A 490
REMARK 465 MET A 491
REMARK 465 SER A 492
REMARK 465 GLU A 493
REMARK 465 VAL A 494
REMARK 465 TYR A 495
REMARK 465 LEU A 496
REMARK 465 GLY A 497
REMARK 465 LYS A 498
REMARK 465 GLN A 499
REMARK 465 ILE A 500
REMARK 465 CYS A 501
REMARK 465 ASN A 502
REMARK 465 LEU A 503
REMARK 465 VAL A 504
REMARK 465 ALA A 505
REMARK 465 CYS A 506
REMARK 465 GLU A 507
REMARK 465 GLY A 508
REMARK 465 PRO A 509
REMARK 465 ASP A 510
REMARK 465 ARG A 511
REMARK 465 VAL A 512
REMARK 465 GLU A 513
REMARK 465 ARG A 514
REMARK 465 HIS A 515
REMARK 465 GLU A 516
REMARK 465 THR A 517
REMARK 465 LEU A 518
REMARK 465 SER A 519
REMARK 465 GLN A 520
REMARK 465 TRP A 521
REMARK 465 GLY A 522
REMARK 465 ASN A 523
REMARK 465 ARG A 524
REMARK 465 PHE A 525
REMARK 465 GLY A 526
REMARK 465 SER A 527
REMARK 465 SER A 528
REMARK 465 GLY A 529
REMARK 465 LEU A 530
REMARK 465 ALA A 531
REMARK 465 PRO A 532
REMARK 465 ALA A 533
REMARK 465 HIS A 534
REMARK 465 LEU A 535
REMARK 465 SER A 548
REMARK 465 VAL A 549
REMARK 465 PHE A 550
REMARK 465 ASN A 551
REMARK 465 SER A 552
REMARK 465 GLY A 553
REMARK 465 GLN A 554
REMARK 465 GLY A 555
REMARK 465 TYR A 556
REMARK 465 ARG A 557
REMARK 465 VAL A 558
REMARK 465 GLU A 559
REMARK 465 GLU A 560
REMARK 465 SER A 561
REMARK 465 ASN A 562
REMARK 465 GLY A 563
REMARK 465 CYS A 564
REMARK 465 LEU A 565
REMARK 465 MET A 566
REMARK 465 LEU A 567
REMARK 465 GLY A 568
REMARK 465 TRP A 569
REMARK 465 HIS A 570
REMARK 465 THR A 571
REMARK 465 ARG A 572
REMARK 465 PRO A 573
REMARK 465 LEU A 574
REMARK 465 ILE A 575
REMARK 465 THR A 576
REMARK 465 THR A 577
REMARK 465 SER A 578
REMARK 465 ALA A 579
REMARK 465 TRP A 580
REMARK 465 LYS A 581
REMARK 465 LEU A 582
REMARK 465 SER A 583
REMARK 465 THR A 584
REMARK 465 ALA A 585
REMARK 465 ALA A 586
REMARK 465 TYR A 587
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 ARG C 3
REMARK 465 SER C 4
REMARK 465 THR C 5
REMARK 465 THR C 6
REMARK 465 ASP C 7
REMARK 465 SER C 8
REMARK 465 ASP C 9
REMARK 465 LEU C 10
REMARK 465 ALA C 11
REMARK 465 GLY C 12
REMARK 465 ASP C 13
REMARK 465 ALA C 14
REMARK 465 HIS C 15
REMARK 465 ASN C 16
REMARK 465 GLU C 17
REMARK 465 THR C 18
REMARK 465 ASN C 19
REMARK 465 LYS C 20
REMARK 465 LYS C 21
REMARK 465 MET C 22
REMARK 465 LYS C 23
REMARK 465 SER C 24
REMARK 465 THR C 25
REMARK 465 GLU C 26
REMARK 465 GLU C 27
REMARK 465 GLU C 28
REMARK 465 GLU C 29
REMARK 465 ILE C 30
REMARK 465 PHE C 142
REMARK 465 THR C 143
REMARK 465 LYS C 144
REMARK 465 ARG C 145
REMARK 465 PRO C 146
REMARK 465 LEU C 147
REMARK 465 PRO C 148
REMARK 465 GLU C 149
REMARK 465 SER C 150
REMARK 465 LYS C 151
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 THR D 3
REMARK 465 VAL D 4
REMARK 465 ARG D 5
REMARK 465 ILE D 34
REMARK 465 GLU D 35
REMARK 465 ASP D 36
REMARK 465 ASP D 37
REMARK 465 CYS D 38
REMARK 465 THR D 39
REMARK 465 ASP D 40
REMARK 465 ASN D 41
REMARK 465 GLY D 42
REMARK 465 LYS D 69
REMARK 465 SER D 70
REMARK 465 GLU D 71
REMARK 465 THR D 72
REMARK 465 THR D 73
REMARK 465 ALA D 74
REMARK 465 ASP D 75
REMARK 465 ALA D 76
REMARK 465 ALA D 77
REMARK 465 ALA D 78
REMARK 465 ALA D 79
REMARK 465 THR D 80
REMARK 465 THR D 81
REMARK 465 THR D 82
REMARK 465 THR D 83
REMARK 465 THR D 84
REMARK 465 VAL D 85
REMARK 465 ALA D 86
REMARK 465 SER D 87
REMARK 465 GLU D 171
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO C 114 CG PRO C 114 CD -0.461
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO C 114 N - CA - CB ANGL. DEV. = -7.5 DEGREES
REMARK 500 PRO C 114 CA - CB - CG ANGL. DEV. = -33.5 DEGREES
REMARK 500 PRO C 114 N - CD - CG ANGL. DEV. = -30.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 330 18.60 -141.53
REMARK 500 GLN A 332 -6.76 67.35
REMARK 500 TRP C 80 -61.85 -93.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-63400 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF ARABIDOPSIS THALIANA RGA IN COMPLEX WITH GID1A,
REMARK 900 SLY1, AND ASK2 (FOCUSED MAP)
DBREF 9LUO A 1 587 UNP Q9SLH3 RGA_ARATH 1 587
DBREF 9LUO C 1 151 UNP Q9STX3 GID2_ARATH 1 151
DBREF 9LUO D 1 171 UNP Q9FHW7 SKP1B_ARATH 1 171
SEQADV 9LUO GLY C -1 UNP Q9STX3 EXPRESSION TAG
SEQADV 9LUO SER C 0 UNP Q9STX3 EXPRESSION TAG
SEQADV 9LUO GLY D -1 UNP Q9FHW7 EXPRESSION TAG
SEQADV 9LUO SER D 0 UNP Q9FHW7 EXPRESSION TAG
SEQRES 1 A 587 MET LYS ARG ASP HIS HIS GLN PHE GLN GLY ARG LEU SER
SEQRES 2 A 587 ASN HIS GLY THR SER SER SER SER SER SER ILE SER LYS
SEQRES 3 A 587 ASP LYS MET MET MET VAL LYS LYS GLU GLU ASP GLY GLY
SEQRES 4 A 587 GLY ASN MET ASP ASP GLU LEU LEU ALA VAL LEU GLY TYR
SEQRES 5 A 587 LYS VAL ARG SER SER GLU MET ALA GLU VAL ALA LEU LYS
SEQRES 6 A 587 LEU GLU GLN LEU GLU THR MET MET SER ASN VAL GLN GLU
SEQRES 7 A 587 ASP GLY LEU SER HIS LEU ALA THR ASP THR VAL HIS TYR
SEQRES 8 A 587 ASN PRO SER GLU LEU TYR SER TRP LEU ASP ASN MET LEU
SEQRES 9 A 587 SER GLU LEU ASN PRO PRO PRO LEU PRO ALA SER SER ASN
SEQRES 10 A 587 GLY LEU ASP PRO VAL LEU PRO SER PRO GLU ILE CYS GLY
SEQRES 11 A 587 PHE PRO ALA SER ASP TYR ASP LEU LYS VAL ILE PRO GLY
SEQRES 12 A 587 ASN ALA ILE TYR GLN PHE PRO ALA ILE ASP SER SER SER
SEQRES 13 A 587 SER SER ASN ASN GLN ASN LYS ARG LEU LYS SER CYS SER
SEQRES 14 A 587 SER PRO ASP SER MET VAL THR SER THR SER THR GLY THR
SEQRES 15 A 587 GLN ILE GLY GLY VAL ILE GLY THR THR VAL THR THR THR
SEQRES 16 A 587 THR THR THR THR THR ALA ALA GLY GLU SER THR ARG SER
SEQRES 17 A 587 VAL ILE LEU VAL ASP SER GLN GLU ASN GLY VAL ARG LEU
SEQRES 18 A 587 VAL HIS ALA LEU MET ALA CYS ALA GLU ALA ILE GLN GLN
SEQRES 19 A 587 ASN ASN LEU THR LEU ALA GLU ALA LEU VAL LYS GLN ILE
SEQRES 20 A 587 GLY CYS LEU ALA VAL SER GLN ALA GLY ALA MET ARG LYS
SEQRES 21 A 587 VAL ALA THR TYR PHE ALA GLU ALA LEU ALA ARG ARG ILE
SEQRES 22 A 587 TYR ARG LEU SER PRO PRO GLN ASN GLN ILE ASP HIS CYS
SEQRES 23 A 587 LEU SER ASP THR LEU GLN MET HIS PHE TYR GLU THR CYS
SEQRES 24 A 587 PRO TYR LEU LYS PHE ALA HIS PHE THR ALA ASN GLN ALA
SEQRES 25 A 587 ILE LEU GLU ALA PHE GLU GLY LYS LYS ARG VAL HIS VAL
SEQRES 26 A 587 ILE ASP PHE SER MET ASN GLN GLY LEU GLN TRP PRO ALA
SEQRES 27 A 587 LEU MET GLN ALA LEU ALA LEU ARG GLU GLY GLY PRO PRO
SEQRES 28 A 587 THR PHE ARG LEU THR GLY ILE GLY PRO PRO ALA PRO ASP
SEQRES 29 A 587 ASN SER ASP HIS LEU HIS GLU VAL GLY CYS LYS LEU ALA
SEQRES 30 A 587 GLN LEU ALA GLU ALA ILE HIS VAL GLU PHE GLU TYR ARG
SEQRES 31 A 587 GLY PHE VAL ALA ASN SER LEU ALA ASP LEU ASP ALA SER
SEQRES 32 A 587 MET LEU GLU LEU ARG PRO SER ASP THR GLU ALA VAL ALA
SEQRES 33 A 587 VAL ASN SER VAL PHE GLU LEU HIS LYS LEU LEU GLY ARG
SEQRES 34 A 587 PRO GLY GLY ILE GLU LYS VAL LEU GLY VAL VAL LYS GLN
SEQRES 35 A 587 ILE LYS PRO VAL ILE PHE THR VAL VAL GLU GLN GLU SER
SEQRES 36 A 587 ASN HIS ASN GLY PRO VAL PHE LEU ASP ARG PHE THR GLU
SEQRES 37 A 587 SER LEU HIS TYR TYR SER THR LEU PHE ASP SER LEU GLU
SEQRES 38 A 587 GLY VAL PRO ASN SER GLN ASP LYS VAL MET SER GLU VAL
SEQRES 39 A 587 TYR LEU GLY LYS GLN ILE CYS ASN LEU VAL ALA CYS GLU
SEQRES 40 A 587 GLY PRO ASP ARG VAL GLU ARG HIS GLU THR LEU SER GLN
SEQRES 41 A 587 TRP GLY ASN ARG PHE GLY SER SER GLY LEU ALA PRO ALA
SEQRES 42 A 587 HIS LEU GLY SER ASN ALA PHE LYS GLN ALA SER MET LEU
SEQRES 43 A 587 LEU SER VAL PHE ASN SER GLY GLN GLY TYR ARG VAL GLU
SEQRES 44 A 587 GLU SER ASN GLY CYS LEU MET LEU GLY TRP HIS THR ARG
SEQRES 45 A 587 PRO LEU ILE THR THR SER ALA TRP LYS LEU SER THR ALA
SEQRES 46 A 587 ALA TYR
SEQRES 1 C 153 GLY SER MET LYS ARG SER THR THR ASP SER ASP LEU ALA
SEQRES 2 C 153 GLY ASP ALA HIS ASN GLU THR ASN LYS LYS MET LYS SER
SEQRES 3 C 153 THR GLU GLU GLU GLU ILE GLY PHE SER ASN LEU ASP GLU
SEQRES 4 C 153 ASN LEU VAL TYR GLU VAL LEU LYS HIS VAL ASP ALA LYS
SEQRES 5 C 153 THR LEU ALA MET SER SER CYS VAL SER LYS ILE TRP HIS
SEQRES 6 C 153 LYS THR ALA GLN ASP GLU ARG LEU TRP GLU LEU ILE CYS
SEQRES 7 C 153 THR ARG HIS TRP THR ASN ILE GLY CYS GLY GLN ASN GLN
SEQRES 8 C 153 LEU ARG SER VAL VAL LEU ALA LEU GLY GLY PHE ARG ARG
SEQRES 9 C 153 LEU HIS SER LEU TYR LEU TRP PRO LEU SER LYS PRO ASN
SEQRES 10 C 153 PRO ARG ALA ARG PHE GLY LYS ASP GLU LEU LYS LEU THR
SEQRES 11 C 153 LEU SER LEU LEU SER ILE ARG TYR TYR GLU LYS MET SER
SEQRES 12 C 153 PHE THR LYS ARG PRO LEU PRO GLU SER LYS
SEQRES 1 D 173 GLY SER MET SER THR VAL ARG LYS ILE THR LEU LYS SER
SEQRES 2 D 173 SER ASP GLY GLU ASN PHE GLU ILE ASP GLU ALA VAL ALA
SEQRES 3 D 173 LEU GLU SER GLN THR ILE LYS HIS MET ILE GLU ASP ASP
SEQRES 4 D 173 CYS THR ASP ASN GLY ILE PRO LEU PRO ASN VAL THR SER
SEQRES 5 D 173 LYS ILE LEU SER LYS VAL ILE GLU TYR CYS LYS ARG HIS
SEQRES 6 D 173 VAL GLU ALA ALA GLU LYS SER GLU THR THR ALA ASP ALA
SEQRES 7 D 173 ALA ALA ALA THR THR THR THR THR VAL ALA SER GLY SER
SEQRES 8 D 173 SER ASP GLU ASP LEU LYS THR TRP ASP SER GLU PHE ILE
SEQRES 9 D 173 LYS VAL ASP GLN GLY THR LEU PHE ASP LEU ILE LEU ALA
SEQRES 10 D 173 ALA ASN TYR LEU ASN ILE LYS GLY LEU LEU ASP LEU THR
SEQRES 11 D 173 CYS GLN THR VAL ALA ASP MET ILE LYS GLY LYS THR PRO
SEQRES 12 D 173 GLU GLU ILE ARG LYS THR PHE ASN ILE LYS ASN ASP PHE
SEQRES 13 D 173 THR PRO GLU GLU GLU GLU GLU VAL ARG ARG GLU ASN GLN
SEQRES 14 D 173 TRP ALA PHE GLU
HELIX 1 AA1 PRO A 300 ALA A 316 1 17
HELIX 2 AA2 MET A 330 LEU A 334 5 5
HELIX 3 AA3 GLN A 335 LEU A 345 1 11
HELIX 4 AA4 LEU A 369 ILE A 383 1 15
HELIX 5 AA5 SER A 537 LEU A 547 1 11
HELIX 6 AA6 GLY C 31 LEU C 35 5 5
HELIX 7 AA7 ASP C 36 LYS C 45 1 10
HELIX 8 AA8 ASP C 48 SER C 56 1 9
HELIX 9 AA9 SER C 59 GLN C 67 1 9
HELIX 10 AB1 ASP C 68 HIS C 79 1 12
HELIX 11 AB2 GLY C 86 LEU C 97 1 12
HELIX 12 AB3 GLY C 99 TYR C 107 1 9
HELIX 13 AB4 TYR C 107 LYS C 113 1 7
HELIX 14 AB5 LYS C 122 SER C 141 1 20
HELIX 15 AB6 ASP D 20 LEU D 25 1 6
HELIX 16 AB7 SER D 27 MET D 33 1 7
HELIX 17 AB8 THR D 49 GLU D 68 1 20
HELIX 18 AB9 SER D 89 LYS D 103 1 15
HELIX 19 AC1 ASP D 105 ASN D 120 1 16
HELIX 20 AC2 ILE D 121 LYS D 137 1 17
HELIX 21 AC3 THR D 140 PHE D 148 1 9
HELIX 22 AC4 THR D 155 ASN D 166 1 12
SHEET 1 AA1 2 ILE D 7 LYS D 10 0
SHEET 2 AA1 2 ASN D 16 ILE D 19 -1 O PHE D 17 N LEU D 9
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 535 LEU A 547
TER 1443 SER C 141
TER 2543 PHE D 170
MASTER 764 0 0 22 2 0 0 6 2540 3 0 72
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