| content |
HEADER IMMUNE SYSTEM 27-AUG-24 9JBN
TITLE CRYO-EM STRUCTURE OF THE ARABIDOPSIS EDS1-PAD4-ADR1 IMMUNE COMPLEX IN
TITLE 2 THE PRESENCE OF PRIB-AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN EDS1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PAD4;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PROBABLE DISEASE RESISTANCE PROTEIN AT5G04720;
COMPND 12 CHAIN: C;
COMPND 13 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: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 6 EXPRESSION_SYSTEM: NICOTIANA BENTHAMIANA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4100;
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: AXX17_AT3G46840, AN1_LOCUS15608;
SOURCE 13 EXPRESSION_SYSTEM: NICOTIANA BENTHAMIANA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4100;
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: AT5G04720, MUK11.4, T1E3.80;
SOURCE 20 EXPRESSION_SYSTEM: NICOTIANA BENTHAMIANA;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 4100
KEYWDS TIR SIGNALING, EDS1, PAD4, ADR1, PRIB-AMP, CRYO-EM, IMMUNE SYSTEM
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.WANG,J.TAN,X.CUI,S.SONG,C.YAN,T.QI
REVDAT 1 03-SEP-25 9JBN 0
JRNL AUTH H.WANG,J.TAN,X.CUI,S.SONG,C.YAN,T.QI
JRNL TITL SWITCH OF TIR SIGNALING BY A CA2+ SENSOR ACTIVATES ADR1
JRNL TITL 2 RECOGNITION OF PRIB-AMP-BOUND EDS1-PAD4 FOR STOMATAL
JRNL TITL 3 IMMUNITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : 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) : 2.300
REMARK 3 NUMBER OF PARTICLES : 177920
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 9JBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 29-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050820.
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 : EDS1-PAD4-ADR1 COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
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) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 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 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 617
REMARK 465 ASP A 618
REMARK 465 GLU A 619
REMARK 465 ILE A 620
REMARK 465 THR A 621
REMARK 465 ASP A 622
REMARK 465 THR A 623
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 GLU B 526
REMARK 465 ASN B 527
REMARK 465 GLU B 528
REMARK 465 ILE B 529
REMARK 465 GLU B 530
REMARK 465 MET B 531
REMARK 465 VAL B 532
REMARK 465 VAL B 533
REMARK 465 ASP B 534
REMARK 465 GLU B 535
REMARK 465 SER B 536
REMARK 465 ASP B 537
REMARK 465 ALA B 538
REMARK 465 MET B 539
REMARK 465 GLU B 540
REMARK 465 THR B 541
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 ILE C 4
REMARK 465 ILE C 5
REMARK 465 GLY C 6
REMARK 465 GLY C 7
REMARK 465 GLU C 8
REMARK 465 VAL C 9
REMARK 465 VAL C 10
REMARK 465 THR C 11
REMARK 465 GLU C 12
REMARK 465 LEU C 13
REMARK 465 VAL C 14
REMARK 465 ARG C 15
REMARK 465 GLN C 16
REMARK 465 LEU C 17
REMARK 465 TYR C 18
REMARK 465 ALA C 19
REMARK 465 VAL C 20
REMARK 465 SER C 21
REMARK 465 GLN C 22
REMARK 465 LYS C 23
REMARK 465 THR C 24
REMARK 465 LEU C 25
REMARK 465 ARG C 26
REMARK 465 CYS C 27
REMARK 465 ARG C 28
REMARK 465 GLY C 29
REMARK 465 ILE C 30
REMARK 465 ALA C 31
REMARK 465 LYS C 32
REMARK 465 ASN C 33
REMARK 465 LEU C 34
REMARK 465 ALA C 35
REMARK 465 THR C 36
REMARK 465 MET C 37
REMARK 465 ILE C 38
REMARK 465 ASP C 39
REMARK 465 GLY C 40
REMARK 465 LEU C 41
REMARK 465 GLN C 42
REMARK 465 PRO C 43
REMARK 465 THR C 44
REMARK 465 ILE C 45
REMARK 465 LYS C 46
REMARK 465 GLU C 47
REMARK 465 ILE C 48
REMARK 465 GLN C 49
REMARK 465 TYR C 50
REMARK 465 SER C 51
REMARK 465 GLY C 52
REMARK 465 VAL C 53
REMARK 465 GLU C 54
REMARK 465 LEU C 55
REMARK 465 THR C 56
REMARK 465 PRO C 57
REMARK 465 HIS C 58
REMARK 465 ARG C 59
REMARK 465 GLN C 60
REMARK 465 ALA C 61
REMARK 465 GLN C 62
REMARK 465 LEU C 63
REMARK 465 ARG C 64
REMARK 465 MET C 65
REMARK 465 PHE C 66
REMARK 465 SER C 67
REMARK 465 GLU C 68
REMARK 465 THR C 69
REMARK 465 LEU C 70
REMARK 465 ASP C 71
REMARK 465 LYS C 72
REMARK 465 CYS C 73
REMARK 465 ARG C 74
REMARK 465 LYS C 75
REMARK 465 LEU C 76
REMARK 465 THR C 77
REMARK 465 GLU C 78
REMARK 465 LYS C 79
REMARK 465 VAL C 80
REMARK 465 LEU C 81
REMARK 465 LYS C 82
REMARK 465 SER C 83
REMARK 465 SER C 84
REMARK 465 ARG C 85
REMARK 465 TRP C 86
REMARK 465 ASN C 87
REMARK 465 MET C 88
REMARK 465 VAL C 89
REMARK 465 ARG C 90
REMARK 465 GLN C 91
REMARK 465 LEU C 92
REMARK 465 LEU C 93
REMARK 465 HIS C 94
REMARK 465 VAL C 95
REMARK 465 ARG C 96
REMARK 465 LYS C 97
REMARK 465 MET C 98
REMARK 465 GLU C 99
REMARK 465 ASN C 100
REMARK 465 LEU C 101
REMARK 465 GLN C 102
REMARK 465 SER C 103
REMARK 465 LYS C 104
REMARK 465 VAL C 105
REMARK 465 SER C 106
REMARK 465 SER C 107
REMARK 465 PHE C 108
REMARK 465 LEU C 109
REMARK 465 ASN C 110
REMARK 465 GLY C 111
REMARK 465 GLN C 112
REMARK 465 LEU C 113
REMARK 465 LEU C 114
REMARK 465 VAL C 115
REMARK 465 HIS C 116
REMARK 465 VAL C 117
REMARK 465 LEU C 118
REMARK 465 ALA C 119
REMARK 465 ASP C 120
REMARK 465 VAL C 121
REMARK 465 HIS C 122
REMARK 465 HIS C 123
REMARK 465 VAL C 124
REMARK 465 ARG C 125
REMARK 465 ALA C 126
REMARK 465 ASP C 127
REMARK 465 SER C 128
REMARK 465 GLU C 129
REMARK 465 PHE C 130
REMARK 465 ARG C 131
REMARK 465 PHE C 132
REMARK 465 ASP C 133
REMARK 465 ARG C 134
REMARK 465 ILE C 135
REMARK 465 ASP C 136
REMARK 465 ARG C 137
REMARK 465 LYS C 138
REMARK 465 VAL C 139
REMARK 465 ASP C 140
REMARK 465 SER C 141
REMARK 465 LEU C 142
REMARK 465 ASN C 143
REMARK 465 GLU C 144
REMARK 465 LYS C 145
REMARK 465 LEU C 146
REMARK 465 GLY C 147
REMARK 465 SER C 148
REMARK 465 MET C 149
REMARK 465 LYS C 150
REMARK 465 LEU C 151
REMARK 465 ARG C 152
REMARK 465 GLY C 153
REMARK 465 SER C 154
REMARK 465 GLU C 155
REMARK 465 SER C 156
REMARK 465 LEU C 157
REMARK 465 ARG C 158
REMARK 465 GLU C 159
REMARK 465 ALA C 160
REMARK 465 LEU C 161
REMARK 465 LYS C 162
REMARK 465 THR C 163
REMARK 465 ALA C 164
REMARK 465 GLU C 165
REMARK 465 ALA C 166
REMARK 465 THR C 167
REMARK 465 VAL C 168
REMARK 465 GLU C 169
REMARK 465 MET C 170
REMARK 465 VAL C 171
REMARK 465 THR C 172
REMARK 465 THR C 173
REMARK 465 ASP C 174
REMARK 465 GLY C 175
REMARK 465 ALA C 176
REMARK 465 ASP C 177
REMARK 465 LEU C 178
REMARK 465 GLY C 179
REMARK 465 VAL C 180
REMARK 465 GLY C 181
REMARK 465 LEU C 182
REMARK 465 ASP C 183
REMARK 465 LEU C 184
REMARK 465 GLY C 185
REMARK 465 LYS C 186
REMARK 465 ARG C 187
REMARK 465 LYS C 188
REMARK 465 VAL C 189
REMARK 465 LYS C 190
REMARK 465 GLU C 191
REMARK 465 MET C 192
REMARK 465 LEU C 193
REMARK 465 PHE C 194
REMARK 465 LYS C 195
REMARK 465 SER C 196
REMARK 465 ILE C 197
REMARK 465 ASP C 198
REMARK 465 GLY C 199
REMARK 465 GLU C 200
REMARK 465 ARG C 201
REMARK 465 LEU C 202
REMARK 465 ILE C 203
REMARK 465 GLY C 204
REMARK 465 ILE C 205
REMARK 465 SER C 206
REMARK 465 GLY C 207
REMARK 465 MET C 208
REMARK 465 SER C 209
REMARK 465 GLY C 210
REMARK 465 SER C 211
REMARK 465 GLY C 212
REMARK 465 LYS C 213
REMARK 465 THR C 214
REMARK 465 THR C 215
REMARK 465 LEU C 216
REMARK 465 ALA C 217
REMARK 465 LYS C 218
REMARK 465 GLU C 219
REMARK 465 LEU C 220
REMARK 465 ALA C 221
REMARK 465 ARG C 222
REMARK 465 ASP C 223
REMARK 465 GLU C 224
REMARK 465 GLU C 225
REMARK 465 VAL C 226
REMARK 465 ARG C 227
REMARK 465 GLY C 228
REMARK 465 HIS C 229
REMARK 465 PHE C 230
REMARK 465 GLY C 231
REMARK 465 ASN C 232
REMARK 465 LYS C 233
REMARK 465 VAL C 234
REMARK 465 LEU C 235
REMARK 465 PHE C 236
REMARK 465 LEU C 237
REMARK 465 THR C 238
REMARK 465 VAL C 239
REMARK 465 SER C 240
REMARK 465 GLN C 241
REMARK 465 SER C 242
REMARK 465 PRO C 243
REMARK 465 ASN C 244
REMARK 465 LEU C 245
REMARK 465 GLU C 246
REMARK 465 GLU C 247
REMARK 465 LEU C 248
REMARK 465 ARG C 249
REMARK 465 ALA C 250
REMARK 465 HIS C 251
REMARK 465 ILE C 252
REMARK 465 TRP C 253
REMARK 465 GLY C 254
REMARK 465 PHE C 255
REMARK 465 LEU C 256
REMARK 465 THR C 257
REMARK 465 SER C 258
REMARK 465 TYR C 259
REMARK 465 GLU C 260
REMARK 465 ALA C 261
REMARK 465 GLY C 262
REMARK 465 VAL C 263
REMARK 465 GLY C 264
REMARK 465 ALA C 265
REMARK 465 THR C 266
REMARK 465 LEU C 267
REMARK 465 PRO C 268
REMARK 465 GLU C 269
REMARK 465 SER C 270
REMARK 465 ARG C 271
REMARK 465 LYS C 272
REMARK 465 LEU C 273
REMARK 465 VAL C 274
REMARK 465 ILE C 275
REMARK 465 LEU C 276
REMARK 465 ASP C 277
REMARK 465 ASP C 278
REMARK 465 VAL C 279
REMARK 465 TRP C 280
REMARK 465 THR C 281
REMARK 465 ARG C 282
REMARK 465 GLU C 283
REMARK 465 SER C 284
REMARK 465 LEU C 285
REMARK 465 ASP C 286
REMARK 465 GLN C 287
REMARK 465 LEU C 288
REMARK 465 MET C 289
REMARK 465 PHE C 290
REMARK 465 GLU C 291
REMARK 465 ASN C 292
REMARK 465 ILE C 293
REMARK 465 PRO C 294
REMARK 465 GLY C 295
REMARK 465 THR C 296
REMARK 465 THR C 297
REMARK 465 THR C 298
REMARK 465 LEU C 299
REMARK 465 VAL C 300
REMARK 465 VAL C 301
REMARK 465 SER C 302
REMARK 465 ARG C 303
REMARK 465 SER C 304
REMARK 465 LYS C 305
REMARK 465 LEU C 306
REMARK 465 ALA C 307
REMARK 465 ASP C 308
REMARK 465 SER C 309
REMARK 465 ARG C 310
REMARK 465 VAL C 311
REMARK 465 THR C 312
REMARK 465 TYR C 313
REMARK 465 ASP C 314
REMARK 465 VAL C 315
REMARK 465 GLU C 316
REMARK 465 LEU C 317
REMARK 465 LEU C 318
REMARK 465 ASN C 319
REMARK 465 GLU C 320
REMARK 465 HIS C 321
REMARK 465 GLU C 322
REMARK 465 ALA C 323
REMARK 465 THR C 324
REMARK 465 ALA C 325
REMARK 465 LEU C 326
REMARK 465 PHE C 327
REMARK 465 CYS C 328
REMARK 465 LEU C 329
REMARK 465 SER C 330
REMARK 465 VAL C 331
REMARK 465 PHE C 332
REMARK 465 ASN C 333
REMARK 465 GLN C 334
REMARK 465 LYS C 335
REMARK 465 LEU C 336
REMARK 465 VAL C 337
REMARK 465 PRO C 338
REMARK 465 SER C 339
REMARK 465 GLY C 340
REMARK 465 PHE C 341
REMARK 465 SER C 342
REMARK 465 GLN C 343
REMARK 465 SER C 344
REMARK 465 LEU C 345
REMARK 465 VAL C 346
REMARK 465 LYS C 347
REMARK 465 GLN C 348
REMARK 465 VAL C 349
REMARK 465 VAL C 350
REMARK 465 GLY C 351
REMARK 465 GLU C 352
REMARK 465 CYS C 353
REMARK 465 LYS C 354
REMARK 465 GLY C 355
REMARK 465 LEU C 356
REMARK 465 PRO C 357
REMARK 465 LEU C 358
REMARK 465 SER C 359
REMARK 465 LEU C 360
REMARK 465 LYS C 361
REMARK 465 VAL C 362
REMARK 465 ILE C 363
REMARK 465 GLY C 364
REMARK 465 ALA C 365
REMARK 465 SER C 366
REMARK 465 LEU C 367
REMARK 465 LYS C 368
REMARK 465 GLU C 369
REMARK 465 ARG C 370
REMARK 465 PRO C 371
REMARK 465 GLU C 372
REMARK 465 LYS C 373
REMARK 465 TYR C 374
REMARK 465 TRP C 375
REMARK 465 GLU C 376
REMARK 465 GLY C 377
REMARK 465 ALA C 378
REMARK 465 VAL C 379
REMARK 465 GLU C 380
REMARK 465 ARG C 381
REMARK 465 LEU C 382
REMARK 465 SER C 383
REMARK 465 ARG C 384
REMARK 465 GLY C 385
REMARK 465 GLU C 386
REMARK 465 PRO C 387
REMARK 465 ALA C 388
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 O HOH A 801 O HOH A 874 1.87
REMARK 500 O LEU A 160 O HOH A 801 1.88
REMARK 500 O HOH A 864 O HOH A 932 1.90
REMARK 500 OE1 GLU A 49 O HOH A 802 1.92
REMARK 500 OE1 GLN A 23 O HOH A 803 1.93
REMARK 500 O HOH A 894 O HOH A 943 1.94
REMARK 500 O HOH A 886 O HOH A 952 1.94
REMARK 500 OD1 ASN A 414 O HOH A 804 1.99
REMARK 500 O2' AMP A 701 O4 RP5 A 702 1.99
REMARK 500 O HOH B 676 O HOH B 682 1.99
REMARK 500 OG SER A 46 OD2 ASP A 51 2.00
REMARK 500 OD1 ASP C 655 OG SER C 679 2.00
REMARK 500 O HOH A 937 O HOH B 631 2.00
REMARK 500 O HOH A 902 O HOH A 956 2.00
REMARK 500 OE1 GLU A 449 O HOH A 805 2.01
REMARK 500 O HOH B 628 O HOH B 664 2.01
REMARK 500 O GLY A 8 O HOH A 806 2.03
REMARK 500 O HOH B 638 O HOH B 657 2.04
REMARK 500 OE1 GLU A 554 O HOH A 807 2.04
REMARK 500 OD2 ASP B 448 OH TYR B 488 2.04
REMARK 500 O HOH A 906 O HOH A 945 2.05
REMARK 500 OD2 ASP A 12 O HOH A 808 2.05
REMARK 500 O HOH B 673 O HOH B 692 2.07
REMARK 500 OE1 GLN B 447 O HOH B 601 2.07
REMARK 500 O TRP B 189 O HOH B 602 2.07
REMARK 500 O HOH A 830 O HOH A 888 2.07
REMARK 500 OD2 ASP B 24 O HOH B 603 2.09
REMARK 500 O HOH A 919 O HOH A 962 2.11
REMARK 500 NZ LYS A 440 O HOH A 809 2.13
REMARK 500 O PRO A 72 NH1 ARG A 75 2.13
REMARK 500 NH1 ARG B 182 O HOH B 604 2.15
REMARK 500 O ASP A 446 O HOH A 810 2.16
REMARK 500 OE2 GLU A 571 OG SER A 610 2.19
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 ARG A 29 -14.34 75.62
REMARK 500 TYR A 30 164.15 178.42
REMARK 500 SER A 102 9.41 81.18
REMARK 500 SER A 123 -132.35 68.73
REMARK 500 ASN A 144 86.16 -151.15
REMARK 500 PRO A 145 2.60 -66.63
REMARK 500 VAL A 161 -51.33 -125.62
REMARK 500 THR A 277 -169.37 -126.57
REMARK 500 LEU A 537 40.18 -103.92
REMARK 500 PHE B 73 66.45 -117.14
REMARK 500 SER B 118 -126.25 70.09
REMARK 500 ARG B 294 77.04 62.09
REMARK 500 ALA B 295 125.11 -35.72
REMARK 500 GLU B 414 57.16 -93.04
REMARK 500 VAL B 431 140.90 63.83
REMARK 500 PRO C 422 172.35 -59.65
REMARK 500 ASN C 636 -131.01 56.51
REMARK 500 PHE C 650 78.00 -111.54
REMARK 500 ALA C 708 30.54 73.76
REMARK 500 SER C 758 50.70 -97.45
REMARK 500 SER C 805 133.91 113.91
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 C 510 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-61320 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE ARABIDOPSIS EDS1-PAD4-ADR1 IMMUNE COMPLEX
REMARK 900 IN THE PRESENCE OF PRIB-AMP
DBREF 9JBN A 1 623 UNP Q9SU72 EDS1C_ARATH 1 623
DBREF1 9JBN B 1 541 UNP A0A178V847_ARATH
DBREF2 9JBN B A0A178V847 1 541
DBREF 9JBN C 1 811 UNP Q9LZ25 DRL30_ARATH 1 811
SEQRES 1 A 623 MET ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 2 A 623 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 3 A 623 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 4 A 623 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 5 A 623 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 6 A 623 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 7 A 623 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 8 A 623 ASN LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN
SEQRES 9 A 623 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 10 A 623 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 11 A 623 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 12 A 623 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 13 A 623 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 14 A 623 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 15 A 623 VAL SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA
SEQRES 16 A 623 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 17 A 623 ALA GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER
SEQRES 18 A 623 GLU GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG
SEQRES 19 A 623 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 20 A 623 THR GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER
SEQRES 21 A 623 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 22 A 623 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 23 A 623 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN
SEQRES 24 A 623 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 25 A 623 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 26 A 623 SER MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 27 A 623 ASN SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER
SEQRES 28 A 623 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 29 A 623 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 30 A 623 VAL ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 31 A 623 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 32 A 623 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 33 A 623 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 34 A 623 GLY VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS
SEQRES 35 A 623 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 36 A 623 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 37 A 623 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 38 A 623 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 39 A 623 ILE TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS
SEQRES 40 A 623 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 41 A 623 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 42 A 623 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 43 A 623 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 44 A 623 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 45 A 623 MET LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP
SEQRES 46 A 623 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 47 A 623 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 48 A 623 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR
SEQRES 1 B 541 MET ASP ASP CYS ARG PHE GLU THR SER GLU LEU GLN ALA
SEQRES 2 B 541 SER VAL MET ILE SER THR PRO LEU PHE THR ASP SER TRP
SEQRES 3 B 541 SER SER CYS ASN THR ALA ASN CYS ASN GLY SER ILE LYS
SEQRES 4 B 541 ILE HIS ASP ILE ALA GLY ILE THR TYR VAL ALA ILE PRO
SEQRES 5 B 541 ALA VAL SER MET ILE GLN LEU GLY ASN LEU VAL GLY LEU
SEQRES 6 B 541 PRO VAL THR GLY ASP VAL LEU PHE PRO GLY LEU SER SER
SEQRES 7 B 541 ASP GLU PRO LEU PRO MET VAL ASP ALA ALA ILE LEU LYS
SEQRES 8 B 541 LEU PHE LEU GLN LEU LYS ILE LYS GLU GLY LEU GLU LEU
SEQRES 9 B 541 GLU LEU LEU GLY LYS LYS LEU VAL VAL ILE THR GLY HIS
SEQRES 10 B 541 SER THR GLY GLY ALA LEU ALA ALA PHE THR ALA LEU TRP
SEQRES 11 B 541 LEU LEU SER GLN SER SER PRO PRO SER PHE ARG VAL PHE
SEQRES 12 B 541 CYS ILE THR PHE GLY SER PRO LEU LEU GLY ASN GLN SER
SEQRES 13 B 541 LEU SER THR SER ILE SER ARG SER ARG LEU ALA HIS ASN
SEQRES 14 B 541 PHE CYS HIS VAL VAL SER ILE HIS ASP LEU VAL PRO ARG
SEQRES 15 B 541 SER SER ASN GLU GLN PHE TRP PRO PHE GLY THR TYR LEU
SEQRES 16 B 541 PHE CYS SER ASP LYS GLY GLY VAL CYS LEU ASP ASN ALA
SEQRES 17 B 541 GLY SER VAL ARG LEU MET PHE ASN ILE LEU ASN THR THR
SEQRES 18 B 541 ALA THR GLN ASN THR GLU GLU HIS GLN ARG TYR GLY HIS
SEQRES 19 B 541 TYR VAL PHE THR LEU SER HIS MET PHE LEU LYS SER ARG
SEQRES 20 B 541 SER PHE LEU GLY GLY SER ILE PRO ASP ASN SER TYR GLN
SEQRES 21 B 541 ALA GLY VAL ALA LEU ALA VAL GLU ALA LEU GLY PHE SER
SEQRES 22 B 541 ASN ASP ASP THR SER GLY VAL LEU VAL LYS GLU CYS ILE
SEQRES 23 B 541 GLU THR ALA THR ARG ILE VAL ARG ALA PRO ILE LEU ARG
SEQRES 24 B 541 SER ALA GLU LEU ALA ASN GLU LEU ALA SER VAL LEU PRO
SEQRES 25 B 541 ALA ARG LEU GLU ILE GLN TRP TYR LYS ASP ARG CYS ASP
SEQRES 26 B 541 ALA SER GLU GLU GLN LEU GLY TYR TYR ASP PHE PHE LYS
SEQRES 27 B 541 ARG TYR SER LEU LYS ARG ASP PHE LYS VAL ASN MET SER
SEQRES 28 B 541 ARG ILE ARG LEU ALA LYS PHE TRP ASP THR VAL ILE LYS
SEQRES 29 B 541 MET VAL GLU THR ASN GLU LEU PRO PHE ASP PHE HIS LEU
SEQRES 30 B 541 GLY LYS LYS TRP ILE TYR ALA SER GLN PHE TYR GLN LEU
SEQRES 31 B 541 LEU ALA GLU PRO LEU ASP ILE ALA ASN PHE TYR LYS ASN
SEQRES 32 B 541 ARG ASP ILE LYS THR GLY GLY HIS TYR LEU GLU GLY ASN
SEQRES 33 B 541 ARG PRO LYS ARG TYR GLU VAL ILE ASP LYS TRP GLN LYS
SEQRES 34 B 541 GLY VAL LYS VAL PRO GLU GLU CYS VAL ARG SER ARG TYR
SEQRES 35 B 541 ALA SER THR THR GLN ASP THR CYS PHE TRP ALA LYS LEU
SEQRES 36 B 541 GLU GLN ALA LYS GLU TRP LEU ASP GLU ALA ARG LYS GLU
SEQRES 37 B 541 SER SER ASP PRO GLN ARG ARG SER LEU LEU ARG GLU LYS
SEQRES 38 B 541 ILE VAL PRO PHE GLU SER TYR ALA ASN THR LEU VAL THR
SEQRES 39 B 541 LYS LYS GLU VAL SER LEU ASP VAL LYS ALA LYS ASN SER
SEQRES 40 B 541 SER TYR SER VAL TRP GLU ALA ASN LEU LYS GLU PHE LYS
SEQRES 41 B 541 CYS LYS MET GLY TYR GLU ASN GLU ILE GLU MET VAL VAL
SEQRES 42 B 541 ASP GLU SER ASP ALA MET GLU THR
SEQRES 1 C 811 MET ALA ASP ILE ILE GLY GLY GLU VAL VAL THR GLU LEU
SEQRES 2 C 811 VAL ARG GLN LEU TYR ALA VAL SER GLN LYS THR LEU ARG
SEQRES 3 C 811 CYS ARG GLY ILE ALA LYS ASN LEU ALA THR MET ILE ASP
SEQRES 4 C 811 GLY LEU GLN PRO THR ILE LYS GLU ILE GLN TYR SER GLY
SEQRES 5 C 811 VAL GLU LEU THR PRO HIS ARG GLN ALA GLN LEU ARG MET
SEQRES 6 C 811 PHE SER GLU THR LEU ASP LYS CYS ARG LYS LEU THR GLU
SEQRES 7 C 811 LYS VAL LEU LYS SER SER ARG TRP ASN MET VAL ARG GLN
SEQRES 8 C 811 LEU LEU HIS VAL ARG LYS MET GLU ASN LEU GLN SER LYS
SEQRES 9 C 811 VAL SER SER PHE LEU ASN GLY GLN LEU LEU VAL HIS VAL
SEQRES 10 C 811 LEU ALA ASP VAL HIS HIS VAL ARG ALA ASP SER GLU PHE
SEQRES 11 C 811 ARG PHE ASP ARG ILE ASP ARG LYS VAL ASP SER LEU ASN
SEQRES 12 C 811 GLU LYS LEU GLY SER MET LYS LEU ARG GLY SER GLU SER
SEQRES 13 C 811 LEU ARG GLU ALA LEU LYS THR ALA GLU ALA THR VAL GLU
SEQRES 14 C 811 MET VAL THR THR ASP GLY ALA ASP LEU GLY VAL GLY LEU
SEQRES 15 C 811 ASP LEU GLY LYS ARG LYS VAL LYS GLU MET LEU PHE LYS
SEQRES 16 C 811 SER ILE ASP GLY GLU ARG LEU ILE GLY ILE SER GLY MET
SEQRES 17 C 811 SER GLY SER GLY LYS THR THR LEU ALA LYS GLU LEU ALA
SEQRES 18 C 811 ARG ASP GLU GLU VAL ARG GLY HIS PHE GLY ASN LYS VAL
SEQRES 19 C 811 LEU PHE LEU THR VAL SER GLN SER PRO ASN LEU GLU GLU
SEQRES 20 C 811 LEU ARG ALA HIS ILE TRP GLY PHE LEU THR SER TYR GLU
SEQRES 21 C 811 ALA GLY VAL GLY ALA THR LEU PRO GLU SER ARG LYS LEU
SEQRES 22 C 811 VAL ILE LEU ASP ASP VAL TRP THR ARG GLU SER LEU ASP
SEQRES 23 C 811 GLN LEU MET PHE GLU ASN ILE PRO GLY THR THR THR LEU
SEQRES 24 C 811 VAL VAL SER ARG SER LYS LEU ALA ASP SER ARG VAL THR
SEQRES 25 C 811 TYR ASP VAL GLU LEU LEU ASN GLU HIS GLU ALA THR ALA
SEQRES 26 C 811 LEU PHE CYS LEU SER VAL PHE ASN GLN LYS LEU VAL PRO
SEQRES 27 C 811 SER GLY PHE SER GLN SER LEU VAL LYS GLN VAL VAL GLY
SEQRES 28 C 811 GLU CYS LYS GLY LEU PRO LEU SER LEU LYS VAL ILE GLY
SEQRES 29 C 811 ALA SER LEU LYS GLU ARG PRO GLU LYS TYR TRP GLU GLY
SEQRES 30 C 811 ALA VAL GLU ARG LEU SER ARG GLY GLU PRO ALA ASP GLU
SEQRES 31 C 811 THR HIS GLU SER ARG VAL PHE ALA GLN ILE GLU ALA THR
SEQRES 32 C 811 LEU GLU ASN LEU ASP PRO LYS THR ARG ASP CYS PHE LEU
SEQRES 33 C 811 VAL LEU GLY ALA PHE PRO GLU ASP LYS LYS ILE PRO LEU
SEQRES 34 C 811 ASP VAL LEU ILE ASN VAL LEU VAL GLU LEU HIS ASP LEU
SEQRES 35 C 811 GLU ASP ALA THR ALA PHE ALA VAL ILE VAL ASP LEU ALA
SEQRES 36 C 811 ASN ARG ASN LEU LEU THR LEU VAL LYS ASP PRO ARG PHE
SEQRES 37 C 811 GLY HIS MET TYR THR SER TYR TYR ASP ILE PHE VAL THR
SEQRES 38 C 811 GLN HIS ASP VAL LEU ARG ASP VAL ALA LEU ARG LEU SER
SEQRES 39 C 811 ASN HIS GLY LYS VAL ASN ASN ARG GLU ARG LEU LEU MET
SEQRES 40 C 811 PRO LYS ARG GLU SER MET LEU PRO ARG GLU TRP GLU ARG
SEQRES 41 C 811 ASN ASN ASP GLU PRO TYR LYS ALA ARG VAL VAL SER ILE
SEQRES 42 C 811 HIS THR GLY GLU MET THR GLN MET ASP TRP PHE ASP MET
SEQRES 43 C 811 GLU LEU PRO LYS ALA GLU VAL LEU ILE LEU HIS PHE SER
SEQRES 44 C 811 SER ASP LYS TYR VAL LEU PRO PRO PHE ILE ALA LYS MET
SEQRES 45 C 811 GLY LYS LEU THR ALA LEU VAL ILE ILE ASN ASN GLY MET
SEQRES 46 C 811 SER PRO ALA ARG LEU HIS ASP PHE SER ILE PHE THR ASN
SEQRES 47 C 811 LEU ALA LYS LEU LYS SER LEU TRP LEU GLN ARG VAL HIS
SEQRES 48 C 811 VAL PRO GLU LEU SER SER SER THR VAL PRO LEU GLN ASN
SEQRES 49 C 811 LEU HIS LYS LEU SER LEU ILE PHE CYS LYS ILE ASN THR
SEQRES 50 C 811 SER LEU ASP GLN THR GLU LEU ASP ILE ALA GLN ILE PHE
SEQRES 51 C 811 PRO LYS LEU SER ASP LEU THR ILE ASP HIS CYS ASP ASP
SEQRES 52 C 811 LEU LEU GLU LEU PRO SER THR ILE CYS GLY ILE THR SER
SEQRES 53 C 811 LEU ASN SER ILE SER ILE THR ASN CYS PRO ARG ILE LYS
SEQRES 54 C 811 GLU LEU PRO LYS ASN LEU SER LYS LEU LYS ALA LEU GLN
SEQRES 55 C 811 LEU LEU ARG LEU TYR ALA CYS HIS GLU LEU ASN SER LEU
SEQRES 56 C 811 PRO VAL GLU ILE CYS GLU LEU PRO ARG LEU LYS TYR VAL
SEQRES 57 C 811 ASP ILE SER GLN CYS VAL SER LEU SER SER LEU PRO GLU
SEQRES 58 C 811 LYS ILE GLY LYS VAL LYS THR LEU GLU LYS ILE ASP THR
SEQRES 59 C 811 ARG GLU CYS SER LEU SER SER ILE PRO ASN SER VAL VAL
SEQRES 60 C 811 LEU LEU THR SER LEU ARG HIS VAL ILE CYS ASP ARG GLU
SEQRES 61 C 811 ALA LEU TRP MET TRP GLU LYS VAL GLN LYS ALA VAL ALA
SEQRES 62 C 811 GLY LEU ARG VAL GLU ALA ALA GLU LYS SER PHE SER ARG
SEQRES 63 C 811 ASP TRP LEU ASP ASP
HET AMP A 701 34
HET RP5 A 702 21
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM RP5 5-O-PHOSPHONO-BETA-D-RIBOFURANOSE
HETSYN RP5 [(2R,3S,4S,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-
HETSYN 2 RP5 YL]METHYL DIHYDROGEN PHOSPHATE; 5-O-PHOSPHONO-BETA-D-
HETSYN 3 RP5 RIBOSE; 5-O-PHOSPHONO-D-RIBOSE; 5-O-PHOSPHONO-RIBOSE
FORMUL 4 AMP C10 H14 N5 O7 P
FORMUL 5 RP5 C5 H11 O8 P
FORMUL 6 HOH *274(H2 O)
HELIX 1 AA1 MET A 1 GLY A 8 1 8
HELIX 2 AA2 ASN A 10 ALA A 24 1 15
HELIX 3 AA3 SER A 48 PHE A 52 5 5
HELIX 4 AA4 GLU A 87 ILE A 97 1 11
HELIX 5 AA5 ASP A 98 THR A 101 5 4
HELIX 6 AA6 SER A 102 SER A 113 1 12
HELIX 7 AA7 SER A 123 TYR A 140 1 18
HELIX 8 AA8 ASP A 163 GLU A 173 1 11
HELIX 9 AA9 TRP A 175 ARG A 177 5 3
HELIX 10 AB1 ILE A 188 MET A 193 1 6
HELIX 11 AB2 ARG A 196 GLU A 201 1 6
HELIX 12 AB3 THR A 203 ASP A 212 1 10
HELIX 13 AB4 SER A 221 THR A 248 1 28
HELIX 14 AB5 ALA A 251 SER A 260 1 10
HELIX 15 AB6 ASN A 286 THR A 297 1 12
HELIX 16 AB7 GLN A 304 SER A 307 5 4
HELIX 17 AB8 LEU A 308 ASP A 316 1 9
HELIX 18 AB9 SER A 319 MET A 327 1 9
HELIX 19 AC1 GLY A 328 LYS A 330 5 3
HELIX 20 AC2 ILE A 341 LEU A 348 1 8
HELIX 21 AC3 SER A 351 GLU A 380 1 30
HELIX 22 AC4 GLN A 381 GLU A 394 1 14
HELIX 23 AC5 GLU A 394 HIS A 402 1 9
HELIX 24 AC6 GLY A 405 SER A 413 1 9
HELIX 25 AC7 GLU A 415 LYS A 441 1 27
HELIX 26 AC8 GLU A 447 GLY A 450 5 4
HELIX 27 AC9 ASP A 451 HIS A 476 1 26
HELIX 28 AD1 LYS A 478 GLY A 483 1 6
HELIX 29 AD2 PRO A 484 GLY A 489 1 6
HELIX 30 AD3 PRO A 491 LYS A 507 1 17
HELIX 31 AD4 PRO A 508 GLY A 510 5 3
HELIX 32 AD5 ILE A 512 GLY A 523 1 12
HELIX 33 AD6 GLN A 529 LEU A 537 1 9
HELIX 34 AD7 CYS A 544 SER A 546 5 3
HELIX 35 AD8 CYS A 547 LYS A 556 1 10
HELIX 36 AD9 PRO A 559 ASP A 580 1 22
HELIX 37 AE1 SER A 593 ILE A 600 1 8
HELIX 38 AE2 PRO A 603 HIS A 609 1 7
HELIX 39 AE3 THR B 8 SER B 18 1 11
HELIX 40 AE4 THR B 19 GLY B 36 1 18
HELIX 41 AE5 ALA B 87 LYS B 97 1 11
HELIX 42 AE6 LYS B 97 LEU B 106 1 10
HELIX 43 AE7 SER B 118 SER B 133 1 16
HELIX 44 AE8 ASN B 154 SER B 164 1 11
HELIX 45 AE9 LEU B 166 HIS B 168 5 3
HELIX 46 AF1 LEU B 179 SER B 183 5 5
HELIX 47 AF2 ASN B 207 THR B 221 1 15
HELIX 48 AF3 ASN B 225 GLN B 230 5 6
HELIX 49 AF4 ARG B 231 MET B 242 1 12
HELIX 50 AF5 PHE B 243 LYS B 245 5 3
HELIX 51 AF6 ASN B 257 LEU B 270 1 14
HELIX 52 AF7 ASP B 276 THR B 290 1 15
HELIX 53 AF8 ALA B 295 ALA B 326 1 32
HELIX 54 AF9 GLY B 332 TYR B 340 1 9
HELIX 55 AG1 LEU B 342 THR B 368 1 27
HELIX 56 AG2 ASP B 374 LEU B 377 5 4
HELIX 57 AG3 GLY B 378 ASN B 403 1 26
HELIX 58 AG4 PRO B 418 GLN B 428 1 11
HELIX 59 AG5 CYS B 450 LYS B 467 1 18
HELIX 60 AG6 ASP B 471 LYS B 495 1 25
HELIX 61 AG7 SER B 499 ALA B 504 5 6
HELIX 62 AG8 SER B 507 GLY B 524 1 18
HELIX 63 AG9 GLU C 390 GLU C 405 1 16
HELIX 64 AH1 ASP C 408 LEU C 418 1 11
HELIX 65 AH2 GLY C 419 PHE C 421 5 3
HELIX 66 AH3 LEU C 429 ASP C 441 1 13
HELIX 67 AH4 GLU C 443 ARG C 457 1 15
HELIX 68 AH5 HIS C 483 ASN C 495 1 13
HELIX 69 AH6 PRO C 515 ASN C 521 1 7
HELIX 70 AH7 THR C 539 TRP C 543 5 5
HELIX 71 AH8 PRO C 566 MET C 572 5 7
HELIX 72 AH9 ASP C 592 LEU C 599 5 8
HELIX 73 AI1 ASP C 645 PHE C 650 1 6
HELIX 74 AI2 PRO C 668 ILE C 674 5 7
HELIX 75 AI3 ASN C 694 LEU C 698 5 5
HELIX 76 AI4 PRO C 716 LEU C 722 5 7
HELIX 77 AI5 LYS C 742 VAL C 746 5 5
HELIX 78 AI6 PRO C 763 LEU C 769 5 7
HELIX 79 AI7 ASP C 778 MET C 784 5 7
HELIX 80 AI8 TRP C 785 VAL C 792 1 8
HELIX 81 AI9 ARG C 806 ASP C 810 5 5
SHEET 1 AA1 8 HIS A 31 ALA A 35 0
SHEET 2 AA1 8 VAL A 38 PHE A 43 -1 O ALA A 42 N HIS A 31
SHEET 3 AA1 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 41
SHEET 4 AA1 8 ARG A 152 PHE A 156 1 O ARG A 152 N PHE A 119
SHEET 5 AA1 8 PHE A 179 SER A 184 1 O PHE A 182 N THR A 155
SHEET 6 AA1 8 THR A 272 SER A 276 1 O VAL A 274 N ASN A 181
SHEET 7 AA1 8 ARG A 280 VAL A 284 -1 O VAL A 282 N PHE A 275
SHEET 8 AA1 8 LEU A 331 HIS A 334 1 O LEU A 331 N LEU A 281
SHEET 1 AA2 2 GLU A 63 LYS A 65 0
SHEET 2 AA2 2 THR A 84 ASN A 86 -1 O VAL A 85 N ILE A 64
SHEET 1 AA3 7 LYS B 39 ILE B 43 0
SHEET 2 AA3 7 ILE B 46 ILE B 51 -1 O TYR B 48 N HIS B 41
SHEET 3 AA3 7 LEU B 111 HIS B 117 1 O VAL B 113 N VAL B 49
SHEET 4 AA3 7 ARG B 141 PHE B 147 1 O PHE B 143 N ILE B 114
SHEET 5 AA3 7 PHE B 170 SER B 175 1 O VAL B 173 N THR B 146
SHEET 6 AA3 7 THR B 193 CYS B 197 1 O LEU B 195 N HIS B 172
SHEET 7 AA3 7 GLY B 202 LEU B 205 -1 O LEU B 205 N TYR B 194
SHEET 1 AA4 2 LEU B 62 GLY B 64 0
SHEET 2 AA4 2 MET B 84 ASP B 86 -1 O VAL B 85 N VAL B 63
SHEET 1 AA5 3 ILE C 427 PRO C 428 0
SHEET 2 AA5 3 PHE C 479 THR C 481 -1 O VAL C 480 N ILE C 427
SHEET 3 AA5 3 THR C 461 LEU C 462 -1 N THR C 461 O THR C 481
SHEET 1 AA613 ARG C 504 LEU C 506 0
SHEET 2 AA613 VAL C 530 HIS C 534 1 O VAL C 530 N LEU C 505
SHEET 3 AA613 VAL C 553 PHE C 558 1 O ILE C 555 N VAL C 531
SHEET 4 AA613 ALA C 577 ASN C 582 1 O ILE C 581 N LEU C 556
SHEET 5 AA613 SER C 604 GLN C 608 1 O TRP C 606 N ILE C 580
SHEET 6 AA613 LYS C 627 ILE C 631 1 O ILE C 631 N LEU C 607
SHEET 7 AA613 ASP C 655 ASP C 659 1 O ASP C 659 N LEU C 630
SHEET 8 AA613 SER C 679 THR C 683 1 O SER C 681 N ILE C 658
SHEET 9 AA613 LEU C 703 ARG C 705 1 O ARG C 705 N ILE C 680
SHEET 10 AA613 TYR C 727 ASP C 729 1 O ASP C 729 N LEU C 704
SHEET 11 AA613 LYS C 751 ASP C 753 1 O ASP C 753 N VAL C 728
SHEET 12 AA613 HIS C 774 CYS C 777 1 O ILE C 776 N ILE C 752
SHEET 13 AA613 ARG C 796 ALA C 799 1 O GLU C 798 N VAL C 775
SHEET 1 AA7 2 LYS C 562 VAL C 564 0
SHEET 2 AA7 2 ARG C 589 HIS C 591 1 O ARG C 589 N TYR C 563
LINK O2' AMP A 701 C1 RP5 A 702 1555 1555 1.39
CISPEP 1 GLU B 80 PRO B 81 0 0.49
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 9917 MET A 616
TER 18187 TYR B 525
TER 25051 ASP C 811
MASTER 614 0 2 81 37 0 0 612842 3 55 153
END |