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HEADER HORMONE 09-FEB-25 9LUP
TITLE CRYO-EM STRUCTURE OF ARABIDOPSIS THALIANA RGA IN COMPLEX WITH GID1A,
TITLE 2 SLY1, AND ASK2 (COMPOSITE 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: GIBBERELLIN RECEPTOR GID1A;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: ATCXE10,CARBOXYLESTERASE 10,GID1-LIKE PROTEIN 1,PROTEIN GA
COMPND 12 INSENSITIVE DWARF 1A,ATGID1A;
COMPND 13 EC: 3.-.-.-;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: F-BOX PROTEIN GID2;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: PROTEIN SLEEPY 1;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: SKP1-LIKE PROTEIN 1B;
COMPND 22 CHAIN: D;
COMPND 23 SYNONYM: SKP1-LIKE 2,UFO-BINDING PROTEIN 2;
COMPND 24 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: GID1A, CXE10, GID1L1, AT3G05120, T12H1.8;
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: GID2, SLY1, AT4G24210, T22A6.40;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 24 ORGANISM_COMMON: THALE CRESS;
SOURCE 25 ORGANISM_TAXID: 3702;
SOURCE 26 GENE: SKP1B, ASK2, UIP2, AT5G42190, MJC20.30;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 28 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 9LUP 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. 2.80 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) : 2.800
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 9LUP 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_1300053360.
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 : HETEROTETRAMER OF RGA, GID1A,
REMARK 245 SLY1, AND ASK2
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 : HETEROTETRAMER OF THE DELLA
REMARK 245 PROTEIN RGA, GIBBERELLIN RECEPTOR GID1A, F-BOX PROTEIN SLY1, AND
REMARK 245 SKP1-LIKE PROTEIN ASK2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 GLY A 0
REMARK 465 SER 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 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 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 ALA A 585
REMARK 465 ALA A 586
REMARK 465 TYR A 587
REMARK 465 GLY B -1
REMARK 465 SER B 0
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 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: 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 LEU A 470 OG SER A 474 2.10
REMARK 500 OD1 ASP C 48 OG1 THR C 51 2.19
REMARK 500 O LEU A 463 OG1 THR A 467 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 GLN A 77 -148.88 69.95
REMARK 500 ASN A 92 73.60 53.11
REMARK 500 LEU A 237 9.02 58.29
REMARK 500 ASN A 331 -106.80 52.05
REMARK 500 HIS A 384 61.48 61.26
REMARK 500 LYS A 444 61.54 61.83
REMARK 500 HIS A 570 -115.14 56.77
REMARK 500 LEU A 574 -50.29 -120.90
REMARK 500 GLU B 98 53.29 -94.53
REMARK 500 SER B 120 174.45 63.86
REMARK 500 PRO B 156 50.10 -98.46
REMARK 500 SER B 191 -119.35 52.66
REMARK 500 PHE B 238 -3.52 64.47
REMARK 500 PRO B 253 -178.30 -66.11
REMARK 500 LEU B 273 32.45 -98.94
REMARK 500 PRO B 325 57.37 -90.60
REMARK 500 TRP C 80 -62.01 -94.35
REMARK 500 THR D 140 159.81 -48.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 9LUN RELATED DB: PDB
REMARK 900 RELATED ID: 9LUO RELATED DB: PDB
REMARK 900 RELATED ID: 9LUM RELATED DB: PDB
REMARK 900 RELATED ID: EMD-63401 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF ARABIDOPSIS THALIANA RGA IN COMPLEX WITH GID1A,
REMARK 900 SLY1, AND ASK2 (COMPOSITE MAP)
REMARK 900 RELATED ID: EMD-63398 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-63399 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-63400 RELATED DB: EMDB
DBREF 9LUP A 2 587 UNP Q9SLH3 RGA_ARATH 2 587
DBREF 9LUP B 1 345 UNP Q9MAA7 GID1A_ARATH 1 345
DBREF 9LUP C 1 151 UNP Q9STX3 GID2_ARATH 1 151
DBREF 9LUP D 1 171 UNP Q9FHW7 SKP1B_ARATH 1 171
SEQADV 9LUP GLY A 0 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9LUP SER A 1 UNP Q9SLH3 EXPRESSION TAG
SEQADV 9LUP GLY B -1 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9LUP SER B 0 UNP Q9MAA7 EXPRESSION TAG
SEQADV 9LUP GLY C -1 UNP Q9STX3 EXPRESSION TAG
SEQADV 9LUP SER C 0 UNP Q9STX3 EXPRESSION TAG
SEQADV 9LUP GLY D -1 UNP Q9FHW7 EXPRESSION TAG
SEQADV 9LUP SER D 0 UNP Q9FHW7 EXPRESSION TAG
SEQRES 1 A 588 GLY SER LYS ARG ASP HIS HIS GLN PHE GLN GLY ARG LEU
SEQRES 2 A 588 SER ASN HIS GLY THR SER SER SER SER SER SER ILE SER
SEQRES 3 A 588 LYS ASP LYS MET MET MET VAL LYS LYS GLU GLU ASP GLY
SEQRES 4 A 588 GLY GLY ASN MET ASP ASP GLU LEU LEU ALA VAL LEU GLY
SEQRES 5 A 588 TYR LYS VAL ARG SER SER GLU MET ALA GLU VAL ALA LEU
SEQRES 6 A 588 LYS LEU GLU GLN LEU GLU THR MET MET SER ASN VAL GLN
SEQRES 7 A 588 GLU ASP GLY LEU SER HIS LEU ALA THR ASP THR VAL HIS
SEQRES 8 A 588 TYR ASN PRO SER GLU LEU TYR SER TRP LEU ASP ASN MET
SEQRES 9 A 588 LEU SER GLU LEU ASN PRO PRO PRO LEU PRO ALA SER SER
SEQRES 10 A 588 ASN GLY LEU ASP PRO VAL LEU PRO SER PRO GLU ILE CYS
SEQRES 11 A 588 GLY PHE PRO ALA SER ASP TYR ASP LEU LYS VAL ILE PRO
SEQRES 12 A 588 GLY ASN ALA ILE TYR GLN PHE PRO ALA ILE ASP SER SER
SEQRES 13 A 588 SER SER SER ASN ASN GLN ASN LYS ARG LEU LYS SER CYS
SEQRES 14 A 588 SER SER PRO ASP SER MET VAL THR SER THR SER THR GLY
SEQRES 15 A 588 THR GLN ILE GLY GLY VAL ILE GLY THR THR VAL THR THR
SEQRES 16 A 588 THR THR THR THR THR THR ALA ALA GLY GLU SER THR ARG
SEQRES 17 A 588 SER VAL ILE LEU VAL ASP SER GLN GLU ASN GLY VAL ARG
SEQRES 18 A 588 LEU VAL HIS ALA LEU MET ALA CYS ALA GLU ALA ILE GLN
SEQRES 19 A 588 GLN ASN ASN LEU THR LEU ALA GLU ALA LEU VAL LYS GLN
SEQRES 20 A 588 ILE GLY CYS LEU ALA VAL SER GLN ALA GLY ALA MET ARG
SEQRES 21 A 588 LYS VAL ALA THR TYR PHE ALA GLU ALA LEU ALA ARG ARG
SEQRES 22 A 588 ILE TYR ARG LEU SER PRO PRO GLN ASN GLN ILE ASP HIS
SEQRES 23 A 588 CYS LEU SER ASP THR LEU GLN MET HIS PHE TYR GLU THR
SEQRES 24 A 588 CYS PRO TYR LEU LYS PHE ALA HIS PHE THR ALA ASN GLN
SEQRES 25 A 588 ALA ILE LEU GLU ALA PHE GLU GLY LYS LYS ARG VAL HIS
SEQRES 26 A 588 VAL ILE ASP PHE SER MET ASN GLN GLY LEU GLN TRP PRO
SEQRES 27 A 588 ALA LEU MET GLN ALA LEU ALA LEU ARG GLU GLY GLY PRO
SEQRES 28 A 588 PRO THR PHE ARG LEU THR GLY ILE GLY PRO PRO ALA PRO
SEQRES 29 A 588 ASP ASN SER ASP HIS LEU HIS GLU VAL GLY CYS LYS LEU
SEQRES 30 A 588 ALA GLN LEU ALA GLU ALA ILE HIS VAL GLU PHE GLU TYR
SEQRES 31 A 588 ARG GLY PHE VAL ALA ASN SER LEU ALA ASP LEU ASP ALA
SEQRES 32 A 588 SER MET LEU GLU LEU ARG PRO SER ASP THR GLU ALA VAL
SEQRES 33 A 588 ALA VAL ASN SER VAL PHE GLU LEU HIS LYS LEU LEU GLY
SEQRES 34 A 588 ARG PRO GLY GLY ILE GLU LYS VAL LEU GLY VAL VAL LYS
SEQRES 35 A 588 GLN ILE LYS PRO VAL ILE PHE THR VAL VAL GLU GLN GLU
SEQRES 36 A 588 SER ASN HIS ASN GLY PRO VAL PHE LEU ASP ARG PHE THR
SEQRES 37 A 588 GLU SER LEU HIS TYR TYR SER THR LEU PHE ASP SER LEU
SEQRES 38 A 588 GLU GLY VAL PRO ASN SER GLN ASP LYS VAL MET SER GLU
SEQRES 39 A 588 VAL TYR LEU GLY LYS GLN ILE CYS ASN LEU VAL ALA CYS
SEQRES 40 A 588 GLU GLY PRO ASP ARG VAL GLU ARG HIS GLU THR LEU SER
SEQRES 41 A 588 GLN TRP GLY ASN ARG PHE GLY SER SER GLY LEU ALA PRO
SEQRES 42 A 588 ALA HIS LEU GLY SER ASN ALA PHE LYS GLN ALA SER MET
SEQRES 43 A 588 LEU LEU SER VAL PHE ASN SER GLY GLN GLY TYR ARG VAL
SEQRES 44 A 588 GLU GLU SER ASN GLY CYS LEU MET LEU GLY TRP HIS THR
SEQRES 45 A 588 ARG PRO LEU ILE THR THR SER ALA TRP LYS LEU SER THR
SEQRES 46 A 588 ALA ALA TYR
SEQRES 1 B 347 GLY SER MET ALA ALA SER ASP GLU VAL ASN LEU ILE GLU
SEQRES 2 B 347 SER ARG THR VAL VAL PRO LEU ASN THR TRP VAL LEU ILE
SEQRES 3 B 347 SER ASN PHE LYS VAL ALA TYR ASN ILE LEU ARG ARG PRO
SEQRES 4 B 347 ASP GLY THR PHE ASN ARG HIS LEU ALA GLU TYR LEU ASP
SEQRES 5 B 347 ARG LYS VAL THR ALA ASN ALA ASN PRO VAL ASP GLY VAL
SEQRES 6 B 347 PHE SER PHE ASP VAL LEU ILE ASP ARG ARG ILE ASN LEU
SEQRES 7 B 347 LEU SER ARG VAL TYR ARG PRO ALA TYR ALA ASP GLN GLU
SEQRES 8 B 347 GLN PRO PRO SER ILE LEU ASP LEU GLU LYS PRO VAL ASP
SEQRES 9 B 347 GLY ASP ILE VAL PRO VAL ILE LEU PHE PHE HIS GLY GLY
SEQRES 10 B 347 SER PHE ALA HIS SER SER ALA ASN SER ALA ILE TYR ASP
SEQRES 11 B 347 THR LEU CYS ARG ARG LEU VAL GLY LEU CYS LYS CYS VAL
SEQRES 12 B 347 VAL VAL SER VAL ASN TYR ARG ARG ALA PRO GLU ASN PRO
SEQRES 13 B 347 TYR PRO CYS ALA TYR ASP ASP GLY TRP ILE ALA LEU ASN
SEQRES 14 B 347 TRP VAL ASN SER ARG SER TRP LEU LYS SER LYS LYS ASP
SEQRES 15 B 347 SER LYS VAL HIS ILE PHE LEU ALA GLY ASP SER SER GLY
SEQRES 16 B 347 GLY ASN ILE ALA HIS ASN VAL ALA LEU ARG ALA GLY GLU
SEQRES 17 B 347 SER GLY ILE ASP VAL LEU GLY ASN ILE LEU LEU ASN PRO
SEQRES 18 B 347 MET PHE GLY GLY ASN GLU ARG THR GLU SER GLU LYS SER
SEQRES 19 B 347 LEU ASP GLY LYS TYR PHE VAL THR VAL ARG ASP ARG ASP
SEQRES 20 B 347 TRP TYR TRP LYS ALA PHE LEU PRO GLU GLY GLU ASP ARG
SEQRES 21 B 347 GLU HIS PRO ALA CYS ASN PRO PHE SER PRO ARG GLY LYS
SEQRES 22 B 347 SER LEU GLU GLY VAL SER PHE PRO LYS SER LEU VAL VAL
SEQRES 23 B 347 VAL ALA GLY LEU ASP LEU ILE ARG ASP TRP GLN LEU ALA
SEQRES 24 B 347 TYR ALA GLU GLY LEU LYS LYS ALA GLY GLN GLU VAL LYS
SEQRES 25 B 347 LEU MET HIS LEU GLU LYS ALA THR VAL GLY PHE TYR LEU
SEQRES 26 B 347 LEU PRO ASN ASN ASN HIS PHE HIS ASN VAL MET ASP GLU
SEQRES 27 B 347 ILE SER ALA PHE VAL ASN ALA GLU CYS
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
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 5 GA3 C19 H22 O6
HELIX 1 AA1 ASP A 44 VAL A 49 1 6
HELIX 2 AA2 GLU A 58 ASP A 87 1 30
HELIX 3 AA3 GLU A 95 ASN A 108 1 14
HELIX 4 AA4 GLN A 215 GLN A 234 1 20
HELIX 5 AA5 THR A 238 GLN A 254 1 17
HELIX 6 AA6 GLY A 256 TYR A 274 1 19
HELIX 7 AA7 SER A 288 PHE A 295 1 8
HELIX 8 AA8 PRO A 300 PHE A 317 1 18
HELIX 9 AA9 GLN A 335 LEU A 345 1 11
HELIX 10 AB1 ASP A 364 ILE A 383 1 20
HELIX 11 AB2 SER A 396 LEU A 400 5 5
HELIX 12 AB3 ASP A 401 GLU A 406 5 6
HELIX 13 AB4 GLU A 422 LEU A 427 5 6
HELIX 14 AB5 GLY A 431 LYS A 444 1 14
HELIX 15 AB6 VAL A 461 LEU A 480 1 20
HELIX 16 AB7 SER A 486 ALA A 505 1 20
HELIX 17 AB8 GLU A 507 ARG A 511 5 5
HELIX 18 AB9 THR A 517 GLY A 529 1 13
HELIX 19 AC1 GLY A 536 PHE A 550 1 15
HELIX 20 AC2 PRO B 17 LEU B 34 1 18
HELIX 21 AC3 ASN B 42 ASP B 50 1 9
HELIX 22 AC4 ILE B 126 LYS B 139 1 14
HELIX 23 AC5 PRO B 156 ASN B 170 1 15
HELIX 24 AC6 SER B 171 LYS B 176 5 6
HELIX 25 AC7 SER B 192 SER B 207 1 16
HELIX 26 AC8 THR B 227 LEU B 233 1 7
HELIX 27 AC9 THR B 240 LEU B 252 1 13
HELIX 28 AD1 ILE B 291 LYS B 304 1 14
HELIX 29 AD2 GLY B 320 LEU B 324 5 5
HELIX 30 AD3 ASN B 327 ASN B 342 1 16
HELIX 31 AD4 GLY C 31 LEU C 35 5 5
HELIX 32 AD5 ASP C 36 LYS C 45 1 10
HELIX 33 AD6 ASP C 48 SER C 56 1 9
HELIX 34 AD7 SER C 59 GLN C 67 1 9
HELIX 35 AD8 ASP C 68 HIS C 79 1 12
HELIX 36 AD9 GLY C 86 LEU C 97 1 12
HELIX 37 AE1 GLY C 99 TYR C 107 1 9
HELIX 38 AE2 TYR C 107 LYS C 113 1 7
HELIX 39 AE3 LYS C 122 SER C 141 1 20
HELIX 40 AE4 ASP D 20 LEU D 25 1 6
HELIX 41 AE5 SER D 27 MET D 33 1 7
HELIX 42 AE6 THR D 49 GLU D 68 1 20
HELIX 43 AE7 SER D 89 LYS D 103 1 15
HELIX 44 AE8 ASP D 105 ASN D 120 1 16
HELIX 45 AE9 ILE D 121 LYS D 137 1 17
HELIX 46 AF1 THR D 140 PHE D 148 1 9
HELIX 47 AF2 THR D 155 ASN D 166 1 12
SHEET 1 AA1 9 ILE A 210 LEU A 211 0
SHEET 2 AA1 9 VAL B 63 LEU B 69 1 O ASP B 67 N LEU A 211
SHEET 3 AA1 9 LEU B 77 PRO B 83 -1 O SER B 78 N VAL B 68
SHEET 4 AA1 9 VAL B 141 ASN B 146 -1 O VAL B 142 N TYR B 81
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 ASP B 190 1 O ALA B 188 N LEU B 110
SHEET 7 AA1 9 GLY B 213 LEU B 217 1 O ILE B 215 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 MET B 312 N VAL B 283
SHEET 1 AA2 7 PHE A 387 ARG A 390 0
SHEET 2 AA2 7 THR A 352 GLY A 357 1 N LEU A 355 O GLU A 388
SHEET 3 AA2 7 ARG A 322 ASP A 327 1 N VAL A 323 O THR A 352
SHEET 4 AA2 7 ALA A 414 VAL A 420 1 O ALA A 414 N ARG A 322
SHEET 5 AA2 7 ILE A 447 GLN A 453 1 O ILE A 447 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 ALA A 533 -1 N ALA A 531 O LYS A 581
SHEET 1 AA3 8 PHE A 387 ARG A 390 0
SHEET 2 AA3 8 THR A 352 GLY A 357 1 N LEU A 355 O GLU A 388
SHEET 3 AA3 8 ARG A 322 ASP A 327 1 N VAL A 323 O THR A 352
SHEET 4 AA3 8 ALA A 414 VAL A 420 1 O ALA A 414 N ARG A 322
SHEET 5 AA3 8 ILE A 447 GLN A 453 1 O ILE A 447 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 CYS A 564 TRP A 569 -1 N LEU A 565 O THR A 577
SHEET 8 AA3 8 TYR A 556 SER A 561 -1 N ARG A 557 O GLY A 568
SHEET 1 AA4 2 ARG B 35 ARG B 36 0
SHEET 2 AA4 2 THR B 40 PHE B 41 -1 O THR B 40 N ARG B 36
SHEET 1 AA5 2 ILE D 7 LYS D 10 0
SHEET 2 AA5 2 ASN D 16 ILE D 19 -1 O PHE D 17 N LEU D 9
CISPEP 1 ALA B 150 PRO B 151 0 4.43
CISPEP 2 TYR B 155 PRO B 156 0 -1.22
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 3404 THR A 584
TER 6052 ALA B 343
TER 6960 SER C 141
TER 8060 PHE D 170
MASTER 403 0 1 47 28 0 0 6 8081 4 25 99
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