HEADER HORMONE RECEPTOR 16-JUN-10 3NJ1
TITLE X-RAY CRYSTAL STRUCTURE OF THE PYL2(V114I)-PYRABACTIN A COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYL2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PYR1-LIKE PROTEIN 2, REGULATORY COMPONENTS OF ABA RECEPTOR
COMPND 5 14;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 STRAIN: COLUMBIA;
SOURCE 6 GENE: AT2G26040, PYL2, RCAR14, T19L18.15;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS START, ABA, PYR/PYL/RCAR, PLANT HORMONE, STRUCTURAL GENOMICS, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, PSI, CENTER FOR EUKARYOTIC STRUCTURAL
KEYWDS 3 GENOMICS, CESG, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR F.C.PETERSON,E.S.BURGIE,C.A.BINGMAN,B.F.VOLKMAN,G.N.PHILLIPS JR.,
AUTHOR 2 S.R.CUTLER,D.R.JENSEN,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS
AUTHOR 3 (CESG)
REVDAT 7 06-SEP-23 3NJ1 1 REMARK SEQADV
REVDAT 6 08-NOV-17 3NJ1 1 REMARK
REVDAT 5 16-MAR-11 3NJ1 1 TITLE
REVDAT 4 15-SEP-10 3NJ1 1 JRNL
REVDAT 3 01-SEP-10 3NJ1 1 HETATM
REVDAT 2 25-AUG-10 3NJ1 1 JRNL
REVDAT 1 18-AUG-10 3NJ1 0
JRNL AUTH F.C.PETERSON,E.S.BURGIE,S.Y.PARK,D.R.JENSEN,J.J.WEINER,
JRNL AUTH 2 C.A.BINGMAN,C.E.CHANG,S.R.CUTLER,G.N.PHILLIPS,B.F.VOLKMAN
JRNL TITL STRUCTURAL BASIS FOR SELECTIVE ACTIVATION OF ABA RECEPTORS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 1109 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20729860
JRNL DOI 10.1038/NSMB.1898
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.140
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 18358
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.890
REMARK 3 FREE R VALUE TEST SET COUNT : 1816
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 30.4316 - 4.5757 0.99 1502 167 0.1892 0.1901
REMARK 3 2 4.5757 - 3.6338 0.99 1368 152 0.1597 0.1938
REMARK 3 3 3.6338 - 3.1750 0.99 1359 150 0.1847 0.2012
REMARK 3 4 3.1750 - 2.8850 0.99 1336 148 0.2136 0.2170
REMARK 3 5 2.8850 - 2.6783 0.98 1296 144 0.2060 0.2498
REMARK 3 6 2.6783 - 2.5205 0.98 1330 146 0.2027 0.2297
REMARK 3 7 2.5205 - 2.3943 0.98 1278 139 0.2030 0.2492
REMARK 3 8 2.3943 - 2.2901 0.98 1287 142 0.2020 0.2398
REMARK 3 9 2.2901 - 2.2020 0.95 1234 139 0.1875 0.2334
REMARK 3 10 2.2020 - 2.1260 0.95 1252 135 0.1857 0.2214
REMARK 3 11 2.1260 - 2.0596 0.93 1201 135 0.1955 0.2571
REMARK 3 12 2.0596 - 2.0007 0.88 1153 122 0.2176 0.2567
REMARK 3 13 2.0007 - 1.9480 0.73 946 97 0.2504 0.2902
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 39.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.017 1594
REMARK 3 ANGLE : 1.263 2174
REMARK 3 CHIRALITY : 0.101 245
REMARK 3 PLANARITY : 0.006 280
REMARK 3 DIHEDRAL : 19.211 596
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8011 25.5497 9.0924
REMARK 3 T TENSOR
REMARK 3 T11: 0.0803 T22: 0.1485
REMARK 3 T33: 0.1187 T12: 0.0229
REMARK 3 T13: -0.0253 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.6041 L22: 1.1602
REMARK 3 L33: 1.2041 L12: -0.3715
REMARK 3 L13: -0.2759 L23: 0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: -0.1138 S13: -0.0887
REMARK 3 S21: 0.0996 S22: 0.0548 S23: -0.0839
REMARK 3 S31: 0.0711 S32: 0.1574 S33: -0.0539
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : 300 MM CCD
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19119
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 16.30
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 2.2.0
REMARK 200 STARTING MODEL: 3NJ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION 2 UL- 20 MM TRIS, PH
REMARK 280 7.5, PRECIPITANT SOLUTION 2 UL- 220 MM AMMONIUM CITRATE AND 19.5%
REMARK 280 (W/V) PEG-3350, CRYOPROTECTANT- 20% (V/V) GLYCEROL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.00067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 148.00133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.00100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 185.00167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.00033
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.00067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 148.00133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 185.00167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 111.00100
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.00033
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: 2190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 0.500000 0.866025 0.000000 -30.87700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 53.48053
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 37.00033
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 264 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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 PRO A 5
REMARK 465 ALA A 6
REMARK 465 VAL A 7
REMARK 465 GLU A 190
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 ASP A 31 126.83 -174.60
REMARK 500 ARG A 69 149.20 -170.70
REMARK 500 ALA A 93 150.61 -49.18
REMARK 500 ASP A 137 -65.20 87.85
REMARK 500 SER A 183 -13.39 -146.98
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 PYV A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P2M A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 191
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NJ0 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE PY12-PYRABACTIN A COMPLEX
REMARK 900 RELATED ID: 3NJO RELATED DB: PDB
REMARK 900 RELATED ID: AT2G26040.1 RELATED DB: TARGETDB
REMARK 900 RELATED ID: GO.10139 RELATED DB: TARGETDB
DBREF 3NJ1 A 1 190 UNP O80992 PYL2_ARATH 1 190
SEQADV 3NJ1 GLY A -2 UNP O80992 EXPRESSION TAG
SEQADV 3NJ1 SER A -1 UNP O80992 EXPRESSION TAG
SEQADV 3NJ1 HIS A 0 UNP O80992 EXPRESSION TAG
SEQADV 3NJ1 ILE A 114 UNP O80992 VAL 114 ENGINEERED MUTATION
SEQRES 1 A 193 GLY SER HIS MET SER SER SER PRO ALA VAL LYS GLY LEU
SEQRES 2 A 193 THR ASP GLU GLU GLN LYS THR LEU GLU PRO VAL ILE LYS
SEQRES 3 A 193 THR TYR HIS GLN PHE GLU PRO ASP PRO THR THR CYS THR
SEQRES 4 A 193 SER LEU ILE THR GLN ARG ILE HIS ALA PRO ALA SER VAL
SEQRES 5 A 193 VAL TRP PRO LEU ILE ARG ARG PHE ASP ASN PRO GLU ARG
SEQRES 6 A 193 TYR LYS HIS PHE VAL LYS ARG CYS ARG LEU ILE SER GLY
SEQRES 7 A 193 ASP GLY ASP VAL GLY SER VAL ARG GLU VAL THR VAL ILE
SEQRES 8 A 193 SER GLY LEU PRO ALA SER THR SER THR GLU ARG LEU GLU
SEQRES 9 A 193 PHE VAL ASP ASP ASP HIS ARG VAL LEU SER PHE ARG ILE
SEQRES 10 A 193 VAL GLY GLY GLU HIS ARG LEU LYS ASN TYR LYS SER VAL
SEQRES 11 A 193 THR SER VAL ASN GLU PHE LEU ASN GLN ASP SER GLY LYS
SEQRES 12 A 193 VAL TYR THR VAL VAL LEU GLU SER TYR THR VAL ASP ILE
SEQRES 13 A 193 PRO GLU GLY ASN THR GLU GLU ASP THR LYS MET PHE VAL
SEQRES 14 A 193 ASP THR VAL VAL LYS LEU ASN LEU GLN LYS LEU GLY VAL
SEQRES 15 A 193 ALA ALA THR SER ALA PRO MET HIS ASP ASP GLU
HET PYV A 300 22
HET P2M A 301 21
HET GOL A 191 6
HETNAM PYV 4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE
HETNAM P2M N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE
HETNAM GOL GLYCEROL
HETSYN PYV PYRABACTIN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 PYV C16 H13 BR N2 O2 S
FORMUL 3 P2M C16 H14 N2 O2 S
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *112(H2 O)
HELIX 1 1 THR A 11 HIS A 26 1 16
HELIX 2 2 PRO A 46 ARG A 56 1 11
HELIX 3 3 ASN A 59 TYR A 63 5 5
HELIX 4 4 THR A 158 ALA A 184 1 27
SHEET 1 A 7 THR A 34 ILE A 43 0
SHEET 2 A 7 VAL A 141 ASP A 152 -1 O THR A 143 N ILE A 43
SHEET 3 A 7 LYS A 125 LEU A 134 -1 N ASN A 131 O VAL A 144
SHEET 4 A 7 VAL A 109 GLY A 117 -1 N LEU A 110 O THR A 128
SHEET 5 A 7 SER A 94 ASP A 104 -1 N THR A 97 O VAL A 115
SHEET 6 A 7 VAL A 82 VAL A 87 -1 N ARG A 83 O GLU A 98
SHEET 7 A 7 VAL A 67 SER A 74 -1 N ARG A 69 O THR A 86
CISPEP 1 LEU A 91 PRO A 92 0 0.27
SITE 1 AC1 13 LYS A 64 HIS A 65 PHE A 66 VAL A 85
SITE 2 AC1 13 VAL A 87 SER A 96 GLU A 98 HIS A 119
SITE 3 AC1 13 LEU A 121 TYR A 124 VAL A 169 HOH A 197
SITE 4 AC1 13 HOH A 249
SITE 1 AC2 12 LYS A 64 HIS A 65 VAL A 85 VAL A 87
SITE 2 AC2 12 SER A 96 GLU A 98 HIS A 119 LEU A 121
SITE 3 AC2 12 TYR A 124 VAL A 169 HOH A 197 HOH A 249
SITE 1 AC3 4 VAL A 103 ASP A 104 ASP A 105 ASP A 106
CRYST1 61.754 61.754 222.002 90.00 90.00 120.00 P 61 2 2 12
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 0.016193 0.009349 0.000000 0.00000
SCALE2 0.000000 0.018698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004504 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
