HEADER PROTEIN BINDING 07-FEB-11 3QN1
TITLE CRYSTAL STRUCTURE OF THE PYR1 ABSCISIC ACID RECEPTOR IN COMPLEX WITH
TITLE 2 THE HAB1 TYPE 2C PHOSPHATASE CATALYTIC DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYR1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ABI1-BINDING PROTEIN 6, PROTEIN PYRABACTIN RESISTANCE 1,
COMPND 5 REGULATORY COMPONENTS OF ABA RECEPTOR 11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN PHOSPHATASE 2C 16;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: ATPP2C16, ATP2C-HA, PROTEIN HYPERSENSITIVE TO ABA 1, PROTEIN
COMPND 11 PHOSPHATASE 2C HAB1, PP2C HAB1;
COMPND 12 EC: 3.1.3.16;
COMPND 13 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 GENE: ABIP6, AT4G17870, PYR1, RCAR11, T6K21.50;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM11;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 13 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 14 ORGANISM_TAXID: 3702;
SOURCE 15 GENE: AT1G72770, F28P22.4, HAB1, P2C-HA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS START DOMAIN, BET V DOMAIN, PYR/PYL/RCAR, PP2C, ABSCISIC ACID HORMONE
KEYWDS 2 RECEPTOR, TYPE 2C PROTEIN PHOSPHATASE, PLANT STRESS RESPONSE,
KEYWDS 3 ABIOTIC STRESS, ABSCISIC ACID BINDING, TYPE 2C PROTEIN PHOSPHATASE
KEYWDS 4 BINDING, INTRACELLULAR, NUCLEUS, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BETZ,F.DUPEUX,J.SANTIAGO,J.A.MARQUEZ
REVDAT 3 13-SEP-23 3QN1 1 REMARK SEQADV HETSYN LINK
REVDAT 2 15-JUN-11 3QN1 1 JRNL
REVDAT 1 16-MAR-11 3QN1 0
JRNL AUTH F.DUPEUX,R.ANTONI,K.BETZ,J.SANTIAGO,M.GONZALEZ-GUZMAN,
JRNL AUTH 2 L.RODRIGUEZ,S.RUBIO,S.Y.PARK,S.R.CUTLER,P.L.RODRIGUEZ,
JRNL AUTH 3 J.A.MARQUEZ
JRNL TITL MODULATION OF ABSCISIC ACID SIGNALING IN VIVO BY AN
JRNL TITL 2 ENGINEERED RECEPTOR-INSENSITIVE PROTEIN PHOSPHATASE TYPE 2C
JRNL TITL 3 ALLELE.
JRNL REF PLANT PHYSIOL. V. 156 106 2011
JRNL REFN ISSN 0032-0889
JRNL PMID 21357183
JRNL DOI 10.1104/PP.110.170894
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 46631
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 + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2312
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3399
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 465
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.510
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3760 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5088 ; 1.655 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 468 ; 6.251 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 168 ;29.848 ;23.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 642 ;13.961 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.888 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 576 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2819 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2351 ; 1.128 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3784 ; 1.996 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1409 ; 3.174 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1304 ; 4.898 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3QN1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-09; 03-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5; 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ESRF; ESRF
REMARK 200 BEAMLINE : ID14-4; BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9395; 1.77120
REMARK 200 MONOCHROMATOR : CHANNEL CUT SI (111); CHANNEL
REMARK 200 CUT SI (111)
REMARK 200 OPTICS : MIRRORS; MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; MARMOSAIC 225
REMARK 200 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47524
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 7.170
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1A6Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25M NACL, 19% PEG 3350, 1MM MNCL2,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. 0.25M
REMARK 280 NACL, 19% PEG 3350, 1MM MNCL2, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 22.92500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.43500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.93000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.43500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.92500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.93000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 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 -1
REMARK 465 ALA A 0
REMARK 465 GLN A 69
REMARK 465 ASN A 70
REMARK 465 SER A 182
REMARK 465 GLY A 183
REMARK 465 ASP A 184
REMARK 465 GLY A 185
REMARK 465 SER A 186
REMARK 465 GLY A 187
REMARK 465 SER A 188
REMARK 465 GLN A 189
REMARK 465 VAL A 190
REMARK 465 THR A 191
REMARK 465 GLY B 175
REMARK 465 ALA B 176
REMARK 465 MET B 177
REMARK 465 GLY B 178
REMARK 465 ARG B 179
REMARK 465 SER B 180
REMARK 465 VAL B 181
REMARK 465 TYR B 182
REMARK 465 GLU B 183
REMARK 465 LEU B 184
REMARK 465 GLY B 222
REMARK 465 ASP B 223
REMARK 465 HIS B 224
REMARK 465 GLU B 225
REMARK 465 GLY B 226
REMARK 465 MET B 227
REMARK 465 SER B 228
REMARK 465 PRO B 229
REMARK 465 SER B 230
REMARK 465 LEU B 231
REMARK 465 ASP B 271
REMARK 465 GLU B 272
REMARK 465 LEU B 273
REMARK 465 CYS B 274
REMARK 465 LYS B 275
REMARK 465 ARG B 276
REMARK 465 ASN B 277
REMARK 465 THR B 278
REMARK 465 GLY B 279
REMARK 465 GLU B 280
REMARK 465 GLY B 281
REMARK 465 ARG B 282
REMARK 465 PRO B 462
REMARK 465 LEU B 463
REMARK 465 ALA B 464
REMARK 465 GLU B 465
REMARK 465 LYS B 506
REMARK 465 PHE B 507
REMARK 465 LYS B 508
REMARK 465 THR B 509
REMARK 465 ARG B 510
REMARK 465 THR B 511
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 GLU A 72 CG CD OE1 OE2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 133 CG OD1 ND2
REMARK 470 ARG A 180 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 214 CG CD CE NZ
REMARK 470 LYS B 218 CG CD CE NZ
REMARK 470 HIS B 233 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 406 CG CD CE NZ
REMARK 470 ARG B 422 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 468 CG CD CE NZ
REMARK 470 GLN B 504 CG CD OE1 NE2
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 PRO A 88 49.86 -83.04
REMARK 500 ARG A 104 60.26 62.88
REMARK 500 GLU A 132 -138.95 74.64
REMARK 500 TRP B 385 85.80 -156.96
REMARK 500 ALA B 395 31.59 -88.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 1 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 16 O
REMARK 620 2 HOH B 24 O 171.6
REMARK 620 3 ASP B 243 OD2 82.5 97.6
REMARK 620 4 ASP B 432 OD1 104.6 83.8 90.2
REMARK 620 5 ASP B 492 OD2 88.7 92.5 166.7 82.3
REMARK 620 6 HOH B 669 O 88.9 82.9 104.2 161.5 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 2 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 11 O
REMARK 620 2 HOH B 33 O 91.1
REMARK 620 3 HOH B 125 O 160.0 99.1
REMARK 620 4 ASP B 243 OD1 78.0 168.0 92.7
REMARK 620 5 GLY B 244 O 103.8 85.5 94.1 92.0
REMARK 620 6 HOH B 669 O 80.8 95.5 81.2 88.0 175.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 3 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 89 O
REMARK 620 2 ASP B 346 OD2 169.0
REMARK 620 3 ASP B 432 OD2 90.8 100.2
REMARK 620 4 HOH B 575 O 82.4 94.8 107.3
REMARK 620 5 HOH B 647 O 107.8 72.3 88.2 161.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A8S A 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K90 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DIMERIC ABSCISIC ACID RECEPTOR PYR1
REMARK 900 RELATED ID: 3K3K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DIMERIC ABSCISIC ACID RECEPTOR PYR1
REMARK 900 RELATED ID: 3NMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HAB1 PHOSPHATASE CATALYTIC DOMAIN IN
REMARK 900 COMPLEX WITH THE ABSICSIC ACID RECEPTOR PYL2
REMARK 900 RELATED ID: 3NJO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYR1 IN COMPLEX WITH PYRABACTIN
DBREF 3QN1 A 3 191 UNP O49686 PYR1_ARATH 3 191
DBREF 3QN1 B 178 511 UNP Q9CAJ0 P2C16_ARATH 178 511
SEQADV 3QN1 GLY A -1 UNP O49686 EXPRESSION TAG
SEQADV 3QN1 ALA A 0 UNP O49686 EXPRESSION TAG
SEQADV 3QN1 MET A 1 UNP O49686 EXPRESSION TAG
SEQADV 3QN1 ALA A 2 UNP O49686 EXPRESSION TAG
SEQADV 3QN1 GLY B 175 UNP Q9CAJ0 EXPRESSION TAG
SEQADV 3QN1 ALA B 176 UNP Q9CAJ0 EXPRESSION TAG
SEQADV 3QN1 MET B 177 UNP Q9CAJ0 EXPRESSION TAG
SEQRES 1 A 193 GLY ALA MET ALA SER GLU LEU THR PRO GLU GLU ARG SER
SEQRES 2 A 193 GLU LEU LYS ASN SER ILE ALA GLU PHE HIS THR TYR GLN
SEQRES 3 A 193 LEU ASP PRO GLY SER CYS SER SER LEU HIS ALA GLN ARG
SEQRES 4 A 193 ILE HIS ALA PRO PRO GLU LEU VAL TRP SER ILE VAL ARG
SEQRES 5 A 193 ARG PHE ASP LYS PRO GLN THR TYR LYS HIS PHE ILE LYS
SEQRES 6 A 193 SER CYS SER VAL GLU GLN ASN PHE GLU MET ARG VAL GLY
SEQRES 7 A 193 CYS THR ARG ASP VAL ILE VAL ILE SER GLY LEU PRO ALA
SEQRES 8 A 193 ASN THR SER THR GLU ARG LEU ASP ILE LEU ASP ASP GLU
SEQRES 9 A 193 ARG ARG VAL THR GLY PHE SER ILE ILE GLY GLY GLU HIS
SEQRES 10 A 193 ARG LEU THR ASN TYR LYS SER VAL THR THR VAL HIS ARG
SEQRES 11 A 193 PHE GLU LYS GLU ASN ARG ILE TRP THR VAL VAL LEU GLU
SEQRES 12 A 193 SER TYR VAL VAL ASP MET PRO GLU GLY ASN SER GLU ASP
SEQRES 13 A 193 ASP THR ARG MET PHE ALA ASP THR VAL VAL LYS LEU ASN
SEQRES 14 A 193 LEU GLN LYS LEU ALA THR VAL ALA GLU ALA MET ALA ARG
SEQRES 15 A 193 ASN SER GLY ASP GLY SER GLY SER GLN VAL THR
SEQRES 1 B 337 GLY ALA MET GLY ARG SER VAL TYR GLU LEU ASP CYS ILE
SEQRES 2 B 337 PRO LEU TRP GLY THR VAL SER ILE GLN GLY ASN ARG SER
SEQRES 3 B 337 GLU MET GLU ASP ALA PHE ALA VAL SER PRO HIS PHE LEU
SEQRES 4 B 337 LYS LEU PRO ILE LYS MET LEU MET GLY ASP HIS GLU GLY
SEQRES 5 B 337 MET SER PRO SER LEU THR HIS LEU THR GLY HIS PHE PHE
SEQRES 6 B 337 GLY VAL TYR ASP GLY HIS GLY GLY HIS LYS VAL ALA ASP
SEQRES 7 B 337 TYR CYS ARG ASP ARG LEU HIS PHE ALA LEU ALA GLU GLU
SEQRES 8 B 337 ILE GLU ARG ILE LYS ASP GLU LEU CYS LYS ARG ASN THR
SEQRES 9 B 337 GLY GLU GLY ARG GLN VAL GLN TRP ASP LYS VAL PHE THR
SEQRES 10 B 337 SER CYS PHE LEU THR VAL ASP GLY GLU ILE GLU GLY LYS
SEQRES 11 B 337 ILE GLY ARG ALA VAL VAL GLY SER SER ASP LYS VAL LEU
SEQRES 12 B 337 GLU ALA VAL ALA SER GLU THR VAL GLY SER THR ALA VAL
SEQRES 13 B 337 VAL ALA LEU VAL CYS SER SER HIS ILE VAL VAL SER ASN
SEQRES 14 B 337 CYS GLY ASP SER ARG ALA VAL LEU PHE ARG GLY LYS GLU
SEQRES 15 B 337 ALA MET PRO LEU SER VAL ASP HIS LYS PRO ASP ARG GLU
SEQRES 16 B 337 ASP GLU TYR ALA ARG ILE GLU ASN ALA GLY GLY LYS VAL
SEQRES 17 B 337 ILE GLN TRP GLN GLY ALA ARG VAL PHE GLY VAL LEU ALA
SEQRES 18 B 337 MET SER ARG SER ILE GLY ASP ARG TYR LEU LYS PRO TYR
SEQRES 19 B 337 VAL ILE PRO GLU PRO GLU VAL THR PHE MET PRO ARG SER
SEQRES 20 B 337 ARG GLU ASP GLU CYS LEU ILE LEU ALA SER ASP GLY LEU
SEQRES 21 B 337 TRP ASP VAL MET ASN ASN GLN GLU VAL CYS GLU ILE ALA
SEQRES 22 B 337 ARG ARG ARG ILE LEU MET TRP HIS LYS LYS ASN GLY ALA
SEQRES 23 B 337 PRO PRO LEU ALA GLU ARG GLY LYS GLY ILE ASP PRO ALA
SEQRES 24 B 337 CYS GLN ALA ALA ALA ASP TYR LEU SER MET LEU ALA LEU
SEQRES 25 B 337 GLN LYS GLY SER LYS ASP ASN ILE SER ILE ILE VAL ILE
SEQRES 26 B 337 ASP LEU LYS ALA GLN ARG LYS PHE LYS THR ARG THR
HET A8S A 192 19
HET MN B 1 1
HET MN B 2 1
HET MN B 3 1
HETNAM A8S (2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-
HETNAM 2 A8S OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC ACID
HETNAM MN MANGANESE (II) ION
HETSYN A8S (+)-ABSCISIC ACID; (2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-
HETSYN 2 A8S TRIMETHYL-4-OXO-2-CYCLOHEXEN-1-YL]-3-METHYL-2,4-
HETSYN 3 A8S PENTADIENOIC ACID
FORMUL 3 A8S C15 H20 O4
FORMUL 4 MN 3(MN 2+)
FORMUL 7 HOH *465(H2 O)
HELIX 1 1 THR A 6 HIS A 21 1 16
HELIX 2 2 PRO A 41 ARG A 50 1 10
HELIX 3 3 LYS A 54 TYR A 58 5 5
HELIX 4 4 SER A 152 ASN A 181 1 30
HELIX 5 5 LYS B 218 LEU B 220 5 3
HELIX 6 6 HIS B 248 ILE B 269 1 22
HELIX 7 7 GLN B 283 GLY B 303 1 21
HELIX 8 8 ARG B 368 ALA B 378 1 11
HELIX 9 9 ARG B 403 LYS B 406 5 4
HELIX 10 10 SER B 431 ASP B 436 1 6
HELIX 11 11 ASN B 439 GLY B 459 1 21
HELIX 12 12 ASP B 471 LYS B 488 1 18
SHEET 1 A 7 SER A 29 ILE A 38 0
SHEET 2 A 7 ARG A 134 ASP A 146 -1 O THR A 137 N ILE A 38
SHEET 3 A 7 LYS A 121 LYS A 131 -1 N THR A 125 O LEU A 140
SHEET 4 A 7 VAL A 105 GLY A 112 -1 N THR A 106 O THR A 124
SHEET 5 A 7 THR A 91 ASP A 100 -1 N ASP A 100 O VAL A 105
SHEET 6 A 7 THR A 78 VAL A 83 -1 N VAL A 81 O SER A 92
SHEET 7 A 7 ILE A 62 SER A 66 -1 N SER A 66 O ASP A 80
SHEET 1 B 5 TRP B 190 ILE B 195 0
SHEET 2 B 5 ILE B 494 ASP B 500 -1 O ILE B 494 N ILE B 195
SHEET 3 B 5 ASP B 424 ALA B 430 -1 N LEU B 429 O ILE B 497
SHEET 4 B 5 ARG B 348 ARG B 353 -1 N PHE B 352 O GLU B 425
SHEET 5 B 5 GLU B 356 PRO B 359 -1 O MET B 358 N LEU B 351
SHEET 1 C 4 ASP B 204 PRO B 216 0
SHEET 2 C 4 HIS B 233 HIS B 245 -1 O TYR B 242 N ALA B 205
SHEET 3 C 4 GLY B 326 SER B 327 -1 O GLY B 326 N HIS B 245
SHEET 4 C 4 ILE B 400 GLY B 401 -1 O ILE B 400 N SER B 327
SHEET 1 D 5 ASP B 204 PRO B 216 0
SHEET 2 D 5 HIS B 233 HIS B 245 -1 O TYR B 242 N ALA B 205
SHEET 3 D 5 ALA B 329 VAL B 334 -1 O ALA B 332 N PHE B 239
SHEET 4 D 5 HIS B 338 CYS B 344 -1 O CYS B 344 N ALA B 329
SHEET 5 D 5 GLU B 414 PRO B 419 -1 O MET B 418 N ILE B 339
SHEET 1 E 2 VAL B 382 GLN B 384 0
SHEET 2 E 2 ALA B 388 VAL B 390 -1 O ARG B 389 N ILE B 383
LINK MN MN B 1 O HOH B 16 1555 1555 2.29
LINK MN MN B 1 O HOH B 24 1555 1555 2.22
LINK MN MN B 1 OD2 ASP B 243 1555 1555 2.15
LINK MN MN B 1 OD1 ASP B 432 1555 1555 2.19
LINK MN MN B 1 OD2 ASP B 492 1555 1555 2.24
LINK MN MN B 1 O HOH B 669 1555 1555 2.33
LINK MN MN B 2 O HOH B 11 1555 1555 2.26
LINK MN MN B 2 O HOH B 33 1555 1555 2.34
LINK MN MN B 2 O HOH B 125 1555 1555 2.37
LINK MN MN B 2 OD1 ASP B 243 1555 1555 2.19
LINK MN MN B 2 O GLY B 244 1555 1555 2.24
LINK MN MN B 2 O HOH B 669 1555 1555 2.20
LINK MN MN B 3 O HOH B 89 1555 1555 2.30
LINK MN MN B 3 OD2 ASP B 346 1555 1555 2.51
LINK MN MN B 3 OD2 ASP B 432 1555 1555 2.23
LINK MN MN B 3 O HOH B 575 1555 1555 2.30
LINK MN MN B 3 O HOH B 647 1555 1555 2.35
CISPEP 1 LYS B 406 PRO B 407 0 6.98
SITE 1 AC1 14 LYS A 59 PHE A 61 VAL A 83 ALA A 89
SITE 2 AC1 14 PHE A 108 ILE A 110 TYR A 120 PHE A 159
SITE 3 AC1 14 VAL A 163 HOH A 197 HOH A 205 HOH A 234
SITE 4 AC1 14 HOH A 266 HOH A 293
SITE 1 AC2 6 HOH B 16 HOH B 24 ASP B 243 ASP B 432
SITE 2 AC2 6 ASP B 492 HOH B 669
SITE 1 AC3 6 HOH B 11 HOH B 33 HOH B 125 ASP B 243
SITE 2 AC3 6 GLY B 244 HOH B 669
SITE 1 AC4 6 HOH B 89 ASP B 346 LYS B 365 ASP B 432
SITE 2 AC4 6 HOH B 575 HOH B 647
CRYST1 45.850 65.860 170.870 90.00 90.00 90.00 P 21 21 21 4
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 0.021810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015184 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005852 0.00000
(ATOM LINES ARE NOT SHOWN.)
END