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HEADER PLANT PROTEIN 08-APR-25 9O4J
TITLE CRYO-EM STRUCTURE OF THE ARABIDOPSIS GA3-GID1A-RGA COMPLEX
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 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GIBBERELLIN RECEPTOR GID1A;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: ATCXE10,CARBOXYLESTERASE 10,GID1-LIKE PROTEIN 1,PROTEIN GA
COMPND 13 INSENSITIVE DWARF 1A,ATGID1A;
COMPND 14 EC: 3.-.-.-;
COMPND 15 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
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: GID1A, CXE10, GID1L1, AT3G05120, T12H1.8;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RGA, GID1A, DELLA, ARABIDOPSIS, PLANT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR P.DAHAL,K.SHARMA,M.BORGNIA,P.ZHOU
REVDAT 1 23-JUL-25 9O4J 0
JRNL AUTH P.DAHAL,Y.WANG,J.HU,J.PARK,K.FORKER,Z.ZHANG,K.SHARMA,
JRNL AUTH 2 M.BORGNIA,T.P.SUN,P.ZHOU
JRNL TITL STRUCTURAL INSIGHTS INTO PROTEOLYSIS-DEPENDENT AND
JRNL TITL 2 -INDEPENDENT SUPPRESSION OF THE MASTER REGULATOR DELLA BY
JRNL TITL 3 GIBBERELLIN RECEPTOR
JRNL REF PROC.NATL.ACAD.SCI.USA 2025
JRNL REFN ESSN 1091-6490
REMARK 2
REMARK 2 RESOLUTION. 3.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC
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) : 3.060
REMARK 3 NUMBER OF PARTICLES : 398856
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 9O4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-25.
REMARK 100 THE DEPOSITION ID IS D_1000294781.
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 : RGA-GID1A-GA3 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 : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 600.00
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) : 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 GLN A 163
REMARK 465 GLN A 164
REMARK 465 LEU A 165
REMARK 465 GLN 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 THR A 584
REMARK 465 ALA A 585
REMARK 465 ALA A 586
REMARK 465 TYR A 587
REMARK 465 GLY A 588
REMARK 465 GLY A 589
REMARK 465 TRP A 590
REMARK 465 SER A 591
REMARK 465 HIS A 592
REMARK 465 PRO A 593
REMARK 465 GLN A 594
REMARK 465 PHE A 595
REMARK 465 GLU A 596
REMARK 465 ARG A 597
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 ASP B 5
REMARK 465 GLU B 6
REMARK 465 VAL B 7
REMARK 465 ASN B 8
REMARK 465 LEU B 9
REMARK 465 GLU B 344
REMARK 465 CYS B 345
REMARK 465 GLY B 346
REMARK 465 GLY B 347
REMARK 465 ASP B 348
REMARK 465 TYR B 349
REMARK 465 LYS B 350
REMARK 465 ASP B 351
REMARK 465 ASP B 352
REMARK 465 ASP B 353
REMARK 465 ASP B 354
REMARK 465 LYS B 355
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 42 CG SD CE
REMARK 470 SER A 56 OG
REMARK 470 SER A 74 OG
REMARK 470 GLN A 77 CG CD OE1 NE2
REMARK 470 GLU A 78 CG CD OE1 OE2
REMARK 470 ASP A 79 CG OD1 OD2
REMARK 470 SER A 205 OG
REMARK 470 THR A 206 OG1 CG2
REMARK 470 SER A 214 OG
REMARK 470 GLN A 215 CG CD OE1 NE2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 ASN A 217 CG OD1 ND2
REMARK 470 CYS A 249 SG
REMARK 470 SER A 253 OG
REMARK 470 LEU A 276 CG CD1 CD2
REMARK 470 SER A 277 OG
REMARK 470 GLN A 280 CG CD OE1 NE2
REMARK 470 ASN A 281 CG OD1 ND2
REMARK 470 GLN A 282 CG CD OE1 NE2
REMARK 470 ASP A 284 CG OD1 OD2
REMARK 470 HIS A 285 CG ND1 CD2 CE1 NE2
REMARK 470 CYS A 286 SG
REMARK 470 LEU A 287 CG CD1 CD2
REMARK 470 SER A 288 OG
REMARK 470 ASP A 289 CG OD1 OD2
REMARK 470 THR A 290 OG1 CG2
REMARK 470 MET A 293 CG SD CE
REMARK 470 GLU A 297 CG CD OE1 OE2
REMARK 470 GLU A 347 CG CD OE1 OE2
REMARK 470 ASP A 364 CG OD1 OD2
REMARK 470 ASN A 365 CG OD1 ND2
REMARK 470 SER A 366 OG
REMARK 470 ASP A 367 CG OD1 OD2
REMARK 470 LEU A 379 CG CD1 CD2
REMARK 470 GLU A 381 CG CD OE1 OE2
REMARK 470 ILE A 383 CG1 CG2 CD1
REMARK 470 HIS A 384 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 385 CG1 CG2
REMARK 470 GLU A 386 CG CD OE1 OE2
REMARK 470 GLU A 406 CG CD OE1 OE2
REMARK 470 SER A 410 OG
REMARK 470 ASP A 411 CG OD1 OD2
REMARK 470 ASP A 464 CG OD1 OD2
REMARK 470 MET A 545 SD CE
REMARK 470 ASN A 551 CG OD1 ND2
REMARK 470 SER A 552 OG
REMARK 470 GLN A 554 CG CD OE1 NE2
REMARK 470 LYS A 581 CG CD CE NZ
REMARK 470 SER A 583 OG
REMARK 470 ILE B 10 CG1 CG2 CD1
REMARK 470 GLU B 11 CG CD OE1 OE2
REMARK 470 ASP B 87 CG OD1 OD2
REMARK 470 GLN B 88 CG CD OE1 NE2
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 GLN B 90 CG CD OE1 NE2
REMARK 470 LYS B 178 CG CD CE NZ
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 ASP B 210 CG OD1 OD2
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 GLU B 274 CG CD OE1 OE2
REMARK 470 VAL B 276 CG1 CG2
REMARK 470 LYS B 316 CG CD CE NZ
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 ASN A 92 71.45 51.53
REMARK 500 LEU A 276 -89.57 -116.32
REMARK 500 PRO A 279 52.78 -91.37
REMARK 500 GLN A 280 36.78 -145.07
REMARK 500 ILE A 283 -150.90 -128.18
REMARK 500 ASP A 284 -155.61 -122.84
REMARK 500 ASP A 289 -60.62 -154.72
REMARK 500 ASN A 331 -116.21 46.50
REMARK 500 SER A 561 116.41 -160.09
REMARK 500 HIS A 570 -108.20 54.83
REMARK 500 ASP B 87 52.28 -109.75
REMARK 500 SER B 93 -143.30 -119.19
REMARK 500 GLU B 98 33.81 -83.31
REMARK 500 ALA B 118 -48.05 -155.04
REMARK 500 SER B 120 -176.98 62.31
REMARK 500 LYS B 178 30.16 -93.72
REMARK 500 SER B 191 -114.07 59.78
REMARK 500 PHE B 266 57.58 -95.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-70103 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE ARABIDOPSIS GA3-GID1A-RGA COMPLEX
DBREF 9O4J A 1 587 UNP Q9SLH3 RGA_ARATH 1 587
DBREF 9O4J B 1 345 UNP Q9MAA7 GID1A_ARATH 1 345
SEQADV 9O4J GLN A 163 UNP Q9SLH3 LYS 163 ENGINEERED MUTATION
SEQADV 9O4J GLN A 164 UNP Q9SLH3 ARG 164 ENGINEERED MUTATION
SEQADV 9O4J GLN A 166 UNP Q9SLH3 LYS 166 ENGINEERED MUTATION
SEQADV 9O4J GLY A 588 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J GLY A 589 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J TRP A 590 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J SER A 591 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J HIS A 592 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J PRO A 593 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J GLN A 594 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J PHE A 595 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J GLU A 596 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J ARG A 597 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9O4J GLY B 346 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J GLY B 347 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J ASP B 348 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J TYR B 349 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J LYS B 350 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J ASP B 351 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J ASP B 352 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J ASP B 353 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J ASP B 354 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9O4J LYS B 355 UNP Q9MAA7 EXPRESSION TAG
SEQRES 1 A 597 MET LYS ARG ASP HIS HIS GLN PHE GLN GLY ARG LEU SER
SEQRES 2 A 597 ASN HIS GLY THR SER SER SER SER SER SER ILE SER LYS
SEQRES 3 A 597 ASP LYS MET MET MET VAL LYS LYS GLU GLU ASP GLY GLY
SEQRES 4 A 597 GLY ASN MET ASP ASP GLU LEU LEU ALA VAL LEU GLY TYR
SEQRES 5 A 597 LYS VAL ARG SER SER GLU MET ALA GLU VAL ALA LEU LYS
SEQRES 6 A 597 LEU GLU GLN LEU GLU THR MET MET SER ASN VAL GLN GLU
SEQRES 7 A 597 ASP GLY LEU SER HIS LEU ALA THR ASP THR VAL HIS TYR
SEQRES 8 A 597 ASN PRO SER GLU LEU TYR SER TRP LEU ASP ASN MET LEU
SEQRES 9 A 597 SER GLU LEU ASN PRO PRO PRO LEU PRO ALA SER SER ASN
SEQRES 10 A 597 GLY LEU ASP PRO VAL LEU PRO SER PRO GLU ILE CYS GLY
SEQRES 11 A 597 PHE PRO ALA SER ASP TYR ASP LEU LYS VAL ILE PRO GLY
SEQRES 12 A 597 ASN ALA ILE TYR GLN PHE PRO ALA ILE ASP SER SER SER
SEQRES 13 A 597 SER SER ASN ASN GLN ASN GLN GLN LEU GLN SER CYS SER
SEQRES 14 A 597 SER PRO ASP SER MET VAL THR SER THR SER THR GLY THR
SEQRES 15 A 597 GLN ILE GLY GLY VAL ILE GLY THR THR VAL THR THR THR
SEQRES 16 A 597 THR THR THR THR THR ALA ALA GLY GLU SER THR ARG SER
SEQRES 17 A 597 VAL ILE LEU VAL ASP SER GLN GLU ASN GLY VAL ARG LEU
SEQRES 18 A 597 VAL HIS ALA LEU MET ALA CYS ALA GLU ALA ILE GLN GLN
SEQRES 19 A 597 ASN ASN LEU THR LEU ALA GLU ALA LEU VAL LYS GLN ILE
SEQRES 20 A 597 GLY CYS LEU ALA VAL SER GLN ALA GLY ALA MET ARG LYS
SEQRES 21 A 597 VAL ALA THR TYR PHE ALA GLU ALA LEU ALA ARG ARG ILE
SEQRES 22 A 597 TYR ARG LEU SER PRO PRO GLN ASN GLN ILE ASP HIS CYS
SEQRES 23 A 597 LEU SER ASP THR LEU GLN MET HIS PHE TYR GLU THR CYS
SEQRES 24 A 597 PRO TYR LEU LYS PHE ALA HIS PHE THR ALA ASN GLN ALA
SEQRES 25 A 597 ILE LEU GLU ALA PHE GLU GLY LYS LYS ARG VAL HIS VAL
SEQRES 26 A 597 ILE ASP PHE SER MET ASN GLN GLY LEU GLN TRP PRO ALA
SEQRES 27 A 597 LEU MET GLN ALA LEU ALA LEU ARG GLU GLY GLY PRO PRO
SEQRES 28 A 597 THR PHE ARG LEU THR GLY ILE GLY PRO PRO ALA PRO ASP
SEQRES 29 A 597 ASN SER ASP HIS LEU HIS GLU VAL GLY CYS LYS LEU ALA
SEQRES 30 A 597 GLN LEU ALA GLU ALA ILE HIS VAL GLU PHE GLU TYR ARG
SEQRES 31 A 597 GLY PHE VAL ALA ASN SER LEU ALA ASP LEU ASP ALA SER
SEQRES 32 A 597 MET LEU GLU LEU ARG PRO SER ASP THR GLU ALA VAL ALA
SEQRES 33 A 597 VAL ASN SER VAL PHE GLU LEU HIS LYS LEU LEU GLY ARG
SEQRES 34 A 597 PRO GLY GLY ILE GLU LYS VAL LEU GLY VAL VAL LYS GLN
SEQRES 35 A 597 ILE LYS PRO VAL ILE PHE THR VAL VAL GLU GLN GLU SER
SEQRES 36 A 597 ASN HIS ASN GLY PRO VAL PHE LEU ASP ARG PHE THR GLU
SEQRES 37 A 597 SER LEU HIS TYR TYR SER THR LEU PHE ASP SER LEU GLU
SEQRES 38 A 597 GLY VAL PRO ASN SER GLN ASP LYS VAL MET SER GLU VAL
SEQRES 39 A 597 TYR LEU GLY LYS GLN ILE CYS ASN LEU VAL ALA CYS GLU
SEQRES 40 A 597 GLY PRO ASP ARG VAL GLU ARG HIS GLU THR LEU SER GLN
SEQRES 41 A 597 TRP GLY ASN ARG PHE GLY SER SER GLY LEU ALA PRO ALA
SEQRES 42 A 597 HIS LEU GLY SER ASN ALA PHE LYS GLN ALA SER MET LEU
SEQRES 43 A 597 LEU SER VAL PHE ASN SER GLY GLN GLY TYR ARG VAL GLU
SEQRES 44 A 597 GLU SER ASN GLY CYS LEU MET LEU GLY TRP HIS THR ARG
SEQRES 45 A 597 PRO LEU ILE THR THR SER ALA TRP LYS LEU SER THR ALA
SEQRES 46 A 597 ALA TYR GLY GLY TRP SER HIS PRO GLN PHE GLU ARG
SEQRES 1 B 355 MET ALA ALA SER ASP GLU VAL ASN LEU ILE GLU SER ARG
SEQRES 2 B 355 THR VAL VAL PRO LEU ASN THR TRP VAL LEU ILE SER ASN
SEQRES 3 B 355 PHE LYS VAL ALA TYR ASN ILE LEU ARG ARG PRO ASP GLY
SEQRES 4 B 355 THR PHE ASN ARG HIS LEU ALA GLU TYR LEU ASP ARG LYS
SEQRES 5 B 355 VAL THR ALA ASN ALA ASN PRO VAL ASP GLY VAL PHE SER
SEQRES 6 B 355 PHE ASP VAL LEU ILE ASP ARG ARG ILE ASN LEU LEU SER
SEQRES 7 B 355 ARG VAL TYR ARG PRO ALA TYR ALA ASP GLN GLU GLN PRO
SEQRES 8 B 355 PRO SER ILE LEU ASP LEU GLU LYS PRO VAL ASP GLY ASP
SEQRES 9 B 355 ILE VAL PRO VAL ILE LEU PHE PHE HIS GLY GLY SER PHE
SEQRES 10 B 355 ALA HIS SER SER ALA ASN SER ALA ILE TYR ASP THR LEU
SEQRES 11 B 355 CYS ARG ARG LEU VAL GLY LEU CYS LYS CYS VAL VAL VAL
SEQRES 12 B 355 SER VAL ASN TYR ARG ARG ALA PRO GLU ASN PRO TYR PRO
SEQRES 13 B 355 CYS ALA TYR ASP ASP GLY TRP ILE ALA LEU ASN TRP VAL
SEQRES 14 B 355 ASN SER ARG SER TRP LEU LYS SER LYS LYS ASP SER LYS
SEQRES 15 B 355 VAL HIS ILE PHE LEU ALA GLY ASP SER SER GLY GLY ASN
SEQRES 16 B 355 ILE ALA HIS ASN VAL ALA LEU ARG ALA GLY GLU SER GLY
SEQRES 17 B 355 ILE ASP VAL LEU GLY ASN ILE LEU LEU ASN PRO MET PHE
SEQRES 18 B 355 GLY GLY ASN GLU ARG THR GLU SER GLU LYS SER LEU ASP
SEQRES 19 B 355 GLY LYS TYR PHE VAL THR VAL ARG ASP ARG ASP TRP TYR
SEQRES 20 B 355 TRP LYS ALA PHE LEU PRO GLU GLY GLU ASP ARG GLU HIS
SEQRES 21 B 355 PRO ALA CYS ASN PRO PHE SER PRO ARG GLY LYS SER LEU
SEQRES 22 B 355 GLU GLY VAL SER PHE PRO LYS SER LEU VAL VAL VAL ALA
SEQRES 23 B 355 GLY LEU ASP LEU ILE ARG ASP TRP GLN LEU ALA TYR ALA
SEQRES 24 B 355 GLU GLY LEU LYS LYS ALA GLY GLN GLU VAL LYS LEU MET
SEQRES 25 B 355 HIS LEU GLU LYS ALA THR VAL GLY PHE TYR LEU LEU PRO
SEQRES 26 B 355 ASN ASN ASN HIS PHE HIS ASN VAL MET ASP GLU ILE SER
SEQRES 27 B 355 ALA PHE VAL ASN ALA GLU CYS GLY GLY ASP TYR LYS ASP
SEQRES 28 B 355 ASP ASP ASP LYS
HET GA3 B 401 25
HETNAM GA3 GIBBERELLIN A3
HETSYN GA3 (1S,2S,4AR,4BR,7S,9AS,10S,10AR)-2,7-DIHYDROXY-1-METHYL-
HETSYN 2 GA3 8-METHYLIDENE-13-OXO-1,2,4B,5,6,7,8,9,10,10A-
HETSYN 3 GA3 DECAHYDRO-4A,1-(EPO XYMETHANO)-7,9A-
HETSYN 4 GA3 METHANOBENZO[A]AZULENE-10-CARBOXYLIC ACID
FORMUL 3 GA3 C19 H22 O6
HELIX 1 AA1 ASP A 44 GLY A 51 1 8
HELIX 2 AA2 ARG A 55 SER A 57 5 3
HELIX 3 AA3 GLU A 58 VAL A 76 1 19
HELIX 4 AA4 ASP A 79 ASP A 87 1 9
HELIX 5 AA5 GLU A 95 ASN A 108 1 14
HELIX 6 AA6 ASN A 217 GLN A 234 1 18
HELIX 7 AA7 ASN A 236 SER A 253 1 18
HELIX 8 AA8 GLY A 256 TYR A 274 1 19
HELIX 9 AA9 LEU A 291 CYS A 299 1 9
HELIX 10 AB1 PRO A 300 ALA A 316 1 17
HELIX 11 AB2 GLN A 335 LEU A 345 1 11
HELIX 12 AB3 ASP A 367 ALA A 380 1 14
HELIX 13 AB4 LEU A 423 GLY A 428 5 6
HELIX 14 AB5 GLY A 431 LYS A 444 1 14
HELIX 15 AB6 VAL A 461 SER A 479 1 19
HELIX 16 AB7 SER A 486 CYS A 506 1 21
HELIX 17 AB8 THR A 517 SER A 527 1 11
HELIX 18 AB9 GLY A 536 SER A 548 1 13
HELIX 19 AC1 VAL A 549 GLN A 554 5 6
HELIX 20 AC2 GLU B 11 VAL B 15 5 5
HELIX 21 AC3 PRO B 17 ARG B 35 1 19
HELIX 22 AC4 ASN B 42 ASP B 50 1 9
HELIX 23 AC5 SER B 124 LYS B 139 1 16
HELIX 24 AC6 PRO B 156 ARG B 172 1 17
HELIX 25 AC7 SER B 192 GLY B 205 1 14
HELIX 26 AC8 THR B 227 LEU B 233 1 7
HELIX 27 AC9 VAL B 241 LEU B 252 1 12
HELIX 28 AD1 ARG B 292 GLY B 306 1 15
HELIX 29 AD2 ASN B 327 ASN B 342 1 16
SHEET 1 AA1 9 ILE A 210 VAL A 212 0
SHEET 2 AA1 9 VAL B 63 ASP B 71 1 O ASP B 67 N LEU A 211
SHEET 3 AA1 9 LEU B 76 PRO B 83 -1 O VAL B 80 N PHE B 66
SHEET 4 AA1 9 VAL B 141 ASN B 146 -1 O SER B 144 N ARG B 79
SHEET 5 AA1 9 PRO B 107 PHE B 112 1 N ILE B 109 O VAL B 141
SHEET 6 AA1 9 HIS B 184 SER B 191 1 O PHE B 186 N LEU B 110
SHEET 7 AA1 9 GLY B 213 PRO B 219 1 O GLY B 213 N LEU B 187
SHEET 8 AA1 9 LYS B 280 ALA B 286 1 O LEU B 282 N LEU B 216
SHEET 9 AA1 9 VAL B 309 LEU B 314 1 O LEU B 314 N VAL B 285
SHEET 1 AA2 7 PHE A 387 GLU A 388 0
SHEET 2 AA2 7 THR A 352 GLY A 359 1 N LEU A 355 O GLU A 388
SHEET 3 AA2 7 ARG A 322 ASP A 327 1 N VAL A 325 O THR A 356
SHEET 4 AA2 7 ALA A 414 VAL A 420 1 O ALA A 416 N ILE A 326
SHEET 5 AA2 7 ILE A 447 GLN A 453 1 O THR A 449 N VAL A 417
SHEET 6 AA2 7 ARG A 572 LEU A 582 -1 O SER A 578 N VAL A 450
SHEET 7 AA2 7 LEU A 530 PRO A 532 -1 N ALA A 531 O LYS A 581
SHEET 1 AA3 8 GLY A 391 VAL A 393 0
SHEET 2 AA3 8 THR A 352 GLY A 359 1 N GLY A 359 O PHE A 392
SHEET 3 AA3 8 ARG A 322 ASP A 327 1 N VAL A 325 O THR A 356
SHEET 4 AA3 8 ALA A 414 VAL A 420 1 O ALA A 416 N ILE A 326
SHEET 5 AA3 8 ILE A 447 GLN A 453 1 O THR A 449 N VAL A 417
SHEET 6 AA3 8 ARG A 572 LEU A 582 -1 O SER A 578 N VAL A 450
SHEET 7 AA3 8 LEU A 565 TRP A 569 -1 N LEU A 567 O ILE A 575
SHEET 8 AA3 8 TYR A 556 GLU A 560 -1 N ARG A 557 O GLY A 568
CISPEP 1 ALA B 150 PRO B 151 0 4.87
CISPEP 2 TYR B 155 PRO B 156 0 -7.65
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 3342 SER A 583
TER 5935 ALA B 343
MASTER 381 0 1 29 24 0 0 6 5958 2 25 74
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