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HEADER HORMONE RECEPTOR 10-SEP-08 2ZSI
TITLE STRUCTURAL BASIS OF GIBBERELLIN(GA4)-INDUCED DELLA
TITLE 2 RECOGNITION BY THE GIBBERELLIN RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE GIBBERELLIN RECEPTOR GID1L1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GID1A, GID1-LIKE PROTEIN 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DELLA PROTEIN GAI;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: DELLA DOMAIN, UNP RESIDUES 11-113;
COMPND 10 SYNONYM: GIBBERELLIC ACID-INSENSITIVE MUTANT PROTEIN,
COMPND 11 RESTORATION OF GROWTH ON AMMONIA PROTEIN 2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 12 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 13 ORGANISM_TAXID: 3702;
SOURCE 14 GENE: GAI;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET47B
KEYWDS PLANT HORMONE RECEPTOR, ALPHA/BETA-HYDROLASE FOLD,
KEYWDS 2 CARBOXYESTERASE FAMILY, GIBBERELLIN SIGNALING PATHWAY,
KEYWDS 3 HYDROLASE, NUCLEUS, RECEPTOR, DEVELOPMENTAL PROTEIN,
KEYWDS 4 PHOSPHOPROTEIN, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 5 REGULATION, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MURASE,Y.HIRANO,T.P.SUN,T.HAKOSHIMA
REVDAT 2 09-DEC-08 2ZSI 1 JRNL VERSN
REVDAT 1 25-NOV-08 2ZSI 0
JRNL AUTH K.MURASE,Y.HIRANO,T.-P.SUN,T.HAKOSHIMA
JRNL TITL GIBBERELLIN-INDUCED DELLA RECOGNITION BY THE
JRNL TITL 2 GIBBERELLIN RECEPTOR GID1
JRNL REF NATURE V. 456 459 2008
JRNL REFN ISSN 0028-0836
JRNL PMID 19037309
JRNL DOI 10.1038/NATURE07519
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 40855
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4118
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 676
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3156
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 267
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : 0.56000
REMARK 3 B33 (A**2) : -1.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.210 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.880 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZSI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB028370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41414
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 13.300
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZSH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.8M LICL2, 26% PEG
REMARK 280 4000, 1MM DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.86850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 40.92600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 40.92600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 97.30275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 40.92600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 40.92600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.43425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 40.92600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.92600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 97.30275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 40.92600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.92600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.43425
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.86850
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 530 LIES ON A SPECIAL POSITION.
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 -6
REMARK 465 PRO A -5
REMARK 465 GLY A -4
REMARK 465 TYR A -3
REMARK 465 ASN A -2
REMARK 465 GLU A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 ASP A 5
REMARK 465 GLY B 4
REMARK 465 PRO B 5
REMARK 465 GLY B 6
REMARK 465 TYR B 7
REMARK 465 ASN B 8
REMARK 465 GLU B 9
REMARK 465 PRO B 10
REMARK 465 GLN B 11
REMARK 465 ASP B 12
REMARK 465 LYS B 13
REMARK 465 LYS B 14
REMARK 465 THR B 15
REMARK 465 MET B 16
REMARK 465 MET B 17
REMARK 465 MET B 18
REMARK 465 ASN B 19
REMARK 465 GLU B 20
REMARK 465 GLU B 21
REMARK 465 ASP B 22
REMARK 465 ASP B 23
REMARK 465 GLY B 24
REMARK 465 ASN B 25
REMARK 465 GLN B 61
REMARK 465 GLU B 62
REMARK 465 ASP B 63
REMARK 465 ASP B 64
REMARK 465 LEU B 65
REMARK 465 SER B 66
REMARK 465 GLN B 67
REMARK 465 PRO B 93
REMARK 465 PRO B 94
REMARK 465 SER B 95
REMARK 465 SER B 96
REMARK 465 ASN B 97
REMARK 465 ALA B 98
REMARK 465 GLU B 99
REMARK 465 TYR B 100
REMARK 465 ASP B 101
REMARK 465 LEU B 102
REMARK 465 LYS B 103
REMARK 465 ALA B 104
REMARK 465 ILE B 105
REMARK 465 PRO B 106
REMARK 465 GLY B 107
REMARK 465 ASP B 108
REMARK 465 ALA B 109
REMARK 465 ILE B 110
REMARK 465 LEU B 111
REMARK 465 ASN B 112
REMARK 465 GLN B 113
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 LYS A 178 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 PHE A 117 -11.13 75.98
REMARK 500 SER A 120 166.43 69.44
REMARK 500 SER A 191 -131.04 53.23
REMARK 500 PHE A 238 -21.08 76.90
REMARK 500 ALA B 69 -5.31 -145.89
REMARK 500 LEU B 91 -144.29 -88.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 A 345
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZSH RELATED DB: PDB
DBREF 2ZSI A 1 344 UNP Q9MAA7 GI1L1_ARATH 1 344
DBREF 2ZSI B 11 113 UNP Q9LQT8 GAI_ARATH 11 113
SEQADV 2ZSI GLY A -6 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI PRO A -5 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI GLY A -4 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI TYR A -3 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI ASN A -2 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI GLU A -1 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI PRO A 0 UNP Q9MAA7 EXPRESSION TAG
SEQADV 2ZSI GLY B 4 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI PRO B 5 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI GLY B 6 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI TYR B 7 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI ASN B 8 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI GLU B 9 UNP Q9LQT8 EXPRESSION TAG
SEQADV 2ZSI PRO B 10 UNP Q9LQT8 EXPRESSION TAG
SEQRES 1 A 351 GLY PRO GLY TYR ASN GLU PRO MET ALA ALA SER ASP GLU
SEQRES 2 A 351 VAL ASN LEU ILE GLU SER ARG THR VAL VAL PRO LEU ASN
SEQRES 3 A 351 THR TRP VAL LEU ILE SER ASN PHE LYS VAL ALA TYR ASN
SEQRES 4 A 351 ILE LEU ARG ARG PRO ASP GLY THR PHE ASN ARG HIS LEU
SEQRES 5 A 351 ALA GLU TYR LEU ASP ARG LYS VAL THR ALA ASN ALA ASN
SEQRES 6 A 351 PRO VAL ASP GLY VAL PHE SER PHE ASP VAL LEU ILE ASP
SEQRES 7 A 351 ARG ARG ILE ASN LEU LEU SER ARG VAL TYR ARG PRO ALA
SEQRES 8 A 351 TYR ALA ASP GLN GLU GLN PRO PRO SER ILE LEU ASP LEU
SEQRES 9 A 351 GLU LYS PRO VAL ASP GLY ASP ILE VAL PRO VAL ILE LEU
SEQRES 10 A 351 PHE PHE HIS GLY GLY SER PHE ALA HIS SER SER ALA ASN
SEQRES 11 A 351 SER ALA ILE TYR ASP THR LEU CYS ARG ARG LEU VAL GLY
SEQRES 12 A 351 LEU CYS LYS CYS VAL VAL VAL SER VAL ASN TYR ARG ARG
SEQRES 13 A 351 ALA PRO GLU ASN PRO TYR PRO CYS ALA TYR ASP ASP GLY
SEQRES 14 A 351 TRP ILE ALA LEU ASN TRP VAL ASN SER ARG SER TRP LEU
SEQRES 15 A 351 LYS SER LYS LYS ASP SER LYS VAL HIS ILE PHE LEU ALA
SEQRES 16 A 351 GLY ASP SER SER GLY GLY ASN ILE ALA HIS ASN VAL ALA
SEQRES 17 A 351 LEU ARG ALA GLY GLU SER GLY ILE ASP VAL LEU GLY ASN
SEQRES 18 A 351 ILE LEU LEU ASN PRO MET PHE GLY GLY ASN GLU ARG THR
SEQRES 19 A 351 GLU SER GLU LYS SER LEU ASP GLY LYS TYR PHE VAL THR
SEQRES 20 A 351 VAL ARG ASP ARG ASP TRP TYR TRP LYS ALA PHE LEU PRO
SEQRES 21 A 351 GLU GLY GLU ASP ARG GLU HIS PRO ALA CYS ASN PRO PHE
SEQRES 22 A 351 SER PRO ARG GLY LYS SER LEU GLU GLY VAL SER PHE PRO
SEQRES 23 A 351 LYS SER LEU VAL VAL VAL ALA GLY LEU ASP LEU ILE ARG
SEQRES 24 A 351 ASP TRP GLN LEU ALA TYR ALA GLU GLY LEU LYS LYS ALA
SEQRES 25 A 351 GLY GLN GLU VAL LYS LEU MET HIS LEU GLU LYS ALA THR
SEQRES 26 A 351 VAL GLY PHE TYR LEU LEU PRO ASN ASN ASN HIS PHE HIS
SEQRES 27 A 351 ASN VAL MET ASP GLU ILE SER ALA PHE VAL ASN ALA GLU
SEQRES 1 B 110 GLY PRO GLY TYR ASN GLU PRO GLN ASP LYS LYS THR MET
SEQRES 2 B 110 MET MET ASN GLU GLU ASP ASP GLY ASN GLY MET ASP GLU
SEQRES 3 B 110 LEU LEU ALA VAL LEU GLY TYR LYS VAL ARG SER SER GLU
SEQRES 4 B 110 MET ALA ASP VAL ALA GLN LYS LEU GLU GLN LEU GLU VAL
SEQRES 5 B 110 MET MET SER ASN VAL GLN GLU ASP ASP LEU SER GLN LEU
SEQRES 6 B 110 ALA THR GLU THR VAL HIS TYR ASN PRO ALA GLU LEU TYR
SEQRES 7 B 110 THR TRP LEU ASP SER MET LEU THR ASP LEU ASN PRO PRO
SEQRES 8 B 110 SER SER ASN ALA GLU TYR ASP LEU LYS ALA ILE PRO GLY
SEQRES 9 B 110 ASP ALA ILE LEU ASN GLN
HET GA4 A 345 24
HETNAM GA4 GIBBERELLIN A4
FORMUL 3 GA4 C19 H24 O5
FORMUL 4 HOH *267(H2 O)
HELIX 1 1 LEU A 9 THR A 14 1 6
HELIX 2 2 PRO A 17 ARG A 35 1 19
HELIX 3 3 ASN A 42 ASP A 50 1 9
HELIX 4 4 SER A 124 LYS A 139 1 16
HELIX 5 5 PRO A 156 SER A 171 1 16
HELIX 6 6 ARG A 172 LYS A 176 5 5
HELIX 7 7 SER A 192 GLU A 206 1 15
HELIX 8 8 THR A 227 ASP A 234 1 8
HELIX 9 9 THR A 240 LEU A 252 1 13
HELIX 10 10 ILE A 291 ALA A 305 1 15
HELIX 11 11 GLY A 320 LEU A 324 5 5
HELIX 12 12 ASN A 327 ALA A 343 1 17
HELIX 13 13 ASP B 28 VAL B 33 1 6
HELIX 14 14 ARG B 39 SER B 41 5 3
HELIX 15 15 GLU B 42 SER B 58 1 17
HELIX 16 16 GLU B 71 TYR B 75 5 5
HELIX 17 17 GLU B 79 LEU B 91 1 13
SHEET 1 A 8 VAL A 63 ASP A 71 0
SHEET 2 A 8 LEU A 76 PRO A 83 -1 O VAL A 80 N PHE A 66
SHEET 3 A 8 VAL A 141 VAL A 145 -1 O VAL A 142 N TYR A 81
SHEET 4 A 8 PRO A 107 PHE A 112 1 N ILE A 109 O VAL A 141
SHEET 5 A 8 HIS A 184 ASP A 190 1 O PHE A 186 N LEU A 110
SHEET 6 A 8 VAL A 211 LEU A 217 1 O LEU A 212 N ILE A 185
SHEET 7 A 8 LYS A 280 ALA A 286 1 O VAL A 284 N LEU A 216
SHEET 8 A 8 VAL A 309 LEU A 314 1 O MET A 312 N VAL A 285
CISPEP 1 ALA A 150 PRO A 151 0 0.15
CISPEP 2 TYR A 155 PRO A 156 0 0.08
SITE 1 AC1 16 PHE A 27 GLY A 115 SER A 116 ILE A 126
SITE 2 AC1 16 TYR A 127 ASP A 190 SER A 191 VAL A 239
SITE 3 AC1 16 ASP A 243 ARG A 244 TYR A 247 VAL A 319
SITE 4 AC1 16 GLY A 320 TYR A 322 HOH A 348 HOH A 509
CRYST1 81.852 81.852 129.737 90.00 90.00 90.00 P 43 21 2 8
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 0.012217 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007708 0.00000
TER 2686 GLU A 344
TER 3158 ASN B 92
MASTER 345 0 1 17 8 0 4 6 3447 2 24 36
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