HEADER SIGNALING PROTEIN/HYDROLASE 01-MAY-16 5JO2
TITLE CRYSTAL STRUCTURE OF ABSCISIC ACID-BOUND ABSCISIC ACID RECEPTOR PYL3
TITLE 2 IN COMPLEX WITH TYPE 2C PROTEIN PHOSPHATASE HAB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYL3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 24-205;
COMPND 5 SYNONYM: PYR1-LIKE PROTEIN 3,REGULATORY COMPONENTS OF ABA RECEPTOR
COMPND 6 13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN PHOSPHATASE 2C 16;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 172-506;
COMPND 12 SYNONYM: ATPP2C16,ATP2C-HA,PROTEIN HYPERSENSITIVE TO ABA 1,PROTEIN
COMPND 13 PHOSPHATASE 2C HAB1,PP2C HAB1;
COMPND 14 EC: 3.1.3.16;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: PYL3, RCAR13, AT1G73000, F3N23.20;
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: MOUSE-EAR CRESS;
SOURCE 11 ORGANISM_TAXID: 3702;
SOURCE 12 GENE: HAB1, P2C-HA, AT1G72770, F28P22.4;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ABA RECEPTOR, PYR/PYL, PYL3, SIGNALING PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.WENG,J.P.NOEL
REVDAT 4 06-MAR-24 5JO2 1 REMARK HETSYN LINK
REVDAT 3 20-NOV-19 5JO2 1 REMARK
REVDAT 2 27-SEP-17 5JO2 1 REMARK
REVDAT 1 07-SEP-16 5JO2 0
JRNL AUTH J.K.WENG,M.YE,B.LI,J.P.NOEL
JRNL TITL CO-EVOLUTION OF HORMONE METABOLISM AND SIGNALING NETWORKS
JRNL TITL 2 EXPANDS PLANT ADAPTIVE PLASTICITY.
JRNL REF CELL V. 166 881 2016
JRNL REFN ISSN 1097-4172
JRNL PMID 27518563
JRNL DOI 10.1016/J.CELL.2016.06.027
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.6
REMARK 3 NUMBER OF REFLECTIONS : 32269
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1616
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 56.2663 - 5.5390 0.96 3252 165 0.1853 0.2055
REMARK 3 2 5.5390 - 4.3970 0.95 3222 169 0.1649 0.2120
REMARK 3 3 4.3970 - 3.8413 0.96 3244 171 0.1746 0.2545
REMARK 3 4 3.8413 - 3.4902 0.96 3223 173 0.1945 0.2340
REMARK 3 5 3.4902 - 3.2400 0.96 3232 170 0.2227 0.2770
REMARK 3 6 3.2400 - 3.0490 0.96 3250 169 0.2490 0.2821
REMARK 3 7 3.0490 - 2.8963 0.95 3213 165 0.2828 0.3679
REMARK 3 8 2.8963 - 2.7702 0.72 2440 118 0.3093 0.2975
REMARK 3 9 2.7702 - 2.6636 0.40 1321 80 0.3460 0.3787
REMARK 3 10 2.6636 - 2.5717 0.43 1451 79 0.3329 0.3257
REMARK 3 11 2.5717 - 2.4913 0.42 1398 85 0.3413 0.4214
REMARK 3 12 2.4913 - 2.4201 0.42 1407 72 0.3484 0.3180
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.003 3840
REMARK 3 ANGLE : 0.776 5193
REMARK 3 CHIRALITY : 0.029 589
REMARK 3 PLANARITY : 0.003 667
REMARK 3 DIHEDRAL : 15.512 1436
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0699 -35.9335 -21.7919
REMARK 3 T TENSOR
REMARK 3 T11: 0.2789 T22: 0.2641
REMARK 3 T33: 0.2400 T12: -0.0249
REMARK 3 T13: -0.0080 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.2896 L22: 1.3537
REMARK 3 L33: 0.6698 L12: 0.3190
REMARK 3 L13: -0.0470 L23: -0.7361
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: -0.1031 S13: 0.0176
REMARK 3 S21: 0.3602 S22: -0.0832 S23: -0.0798
REMARK 3 S31: -0.3037 S32: -0.0699 S33: -0.0003
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 5JO2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
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 : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32269
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 56.251
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1200
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
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MG(NO3)2, 0.1 M TRIS-HCL PH 8.0,
REMARK 280 28% (V/V) PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 22.66500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.60000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 22.66500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.60000
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: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 SER B 172
REMARK 465 ASN B 173
REMARK 465 HIS B 174
REMARK 465 LEU B 175
REMARK 465 VAL B 176
REMARK 465 LYS 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 ASP B 185
REMARK 465 MET B 221
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 THR B 232
REMARK 465 HIS B 233
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 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 158 CG CD CE NZ
REMARK 470 ASP A 159 CG OD1 OD2
REMARK 470 LYS A 160 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 38 NE
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 OE2 GLU A 157 NH2 ARG A 163 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 LEU A 25 124.97 68.63
REMARK 500 ASP A 59 48.04 -88.20
REMARK 500 PRO A 112 42.05 -77.88
REMARK 500 SER A 114 -33.41 -144.63
REMARK 500 LEU A 141 71.41 -103.35
REMARK 500 LYS A 158 -125.17 35.38
REMARK 500 ASP A 159 64.41 -108.30
REMARK 500 LYS A 160 56.85 70.90
REMARK 500 PRO B 188 108.52 -59.88
REMARK 500 ILE B 217 22.79 -67.89
REMARK 500 LYS B 270 -33.89 -30.01
REMARK 500 VAL B 310 36.33 -97.59
REMARK 500 SER B 312 -136.92 -167.80
REMARK 500 ASP B 314 110.86 5.28
REMARK 500 LEU B 317 60.62 -105.08
REMARK 500 TRP B 385 81.80 -157.93
REMARK 500 VAL B 393 -72.48 -111.75
REMARK 500 GLU B 425 -66.68 -90.32
REMARK 500 LEU B 463 62.93 -62.39
REMARK 500 ALA B 464 -80.05 -113.97
REMARK 500 ARG B 466 107.87 -55.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 711 DISTANCE = 8.90 ANGSTROMS
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 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 243 OD1
REMARK 620 2 ASP B 243 OD2 47.6
REMARK 620 3 ASP B 432 OD1 120.1 73.2
REMARK 620 4 ASP B 492 OD2 159.0 151.7 80.7
REMARK 620 5 HOH B 703 O 100.0 89.2 66.5 90.5
REMARK 620 6 HOH B 706 O 83.0 77.2 93.5 93.9 158.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 243 OD1
REMARK 620 2 GLY B 244 O 72.4
REMARK 620 3 HOH B 707 O 74.6 64.2
REMARK 620 N 1 2
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 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JNN RELATED DB: PDB
REMARK 900 RELATED ID: 5JO1 RELATED DB: PDB
DBREF 5JO2 A 24 205 UNP Q9SSM7 PYL3_ARATH 24 205
DBREF 5JO2 B 172 506 UNP Q9CAJ0 P2C16_ARATH 172 506
SEQRES 1 A 182 GLY LEU THR LYS ASP GLU PHE SER THR LEU ASP SER ILE
SEQRES 2 A 182 ILE ARG THR HIS HIS THR PHE PRO ARG SER PRO ASN THR
SEQRES 3 A 182 CYS THR SER LEU ILE ALA HIS ARG VAL ASP ALA PRO ALA
SEQRES 4 A 182 HIS ALA ILE TRP ARG PHE VAL ARG ASP PHE ALA ASN PRO
SEQRES 5 A 182 ASN LYS TYR LYS HIS PHE ILE LYS SER CYS THR ILE ARG
SEQRES 6 A 182 VAL ASN GLY ASN GLY ILE LYS GLU ILE LYS VAL GLY THR
SEQRES 7 A 182 ILE ARG GLU VAL SER VAL VAL SER GLY LEU PRO ALA SER
SEQRES 8 A 182 THR SER VAL GLU ILE LEU GLU VAL LEU ASP GLU GLU LYS
SEQRES 9 A 182 ARG ILE LEU SER PHE ARG VAL LEU GLY GLY GLU HIS ARG
SEQRES 10 A 182 LEU ASN ASN TYR ARG SER VAL THR SER VAL ASN GLU PHE
SEQRES 11 A 182 VAL VAL LEU GLU LYS ASP LYS LYS LYS ARG VAL TYR SER
SEQRES 12 A 182 VAL VAL LEU GLU SER TYR ILE VAL ASP ILE PRO GLN GLY
SEQRES 13 A 182 ASN THR GLU GLU ASP THR ARG MET PHE VAL ASP THR VAL
SEQRES 14 A 182 VAL LYS SER ASN LEU GLN ASN LEU ALA VAL ILE SER THR
SEQRES 1 B 335 SER ASN HIS LEU VAL LYS GLY ARG SER VAL TYR GLU LEU
SEQRES 2 B 335 ASP CYS ILE PRO LEU TRP GLY THR VAL SER ILE GLN GLY
SEQRES 3 B 335 ASN ARG SER GLU MET GLU ASP ALA PHE ALA VAL SER PRO
SEQRES 4 B 335 HIS PHE LEU LYS LEU PRO ILE LYS MET LEU MET GLY ASP
SEQRES 5 B 335 HIS GLU GLY MET SER PRO SER LEU THR HIS LEU THR GLY
SEQRES 6 B 335 HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY GLY HIS LYS
SEQRES 7 B 335 VAL ALA ASP TYR CYS ARG ASP ARG LEU HIS PHE ALA LEU
SEQRES 8 B 335 ALA GLU GLU ILE GLU ARG ILE LYS ASP GLU LEU CYS LYS
SEQRES 9 B 335 ARG ASN THR GLY GLU GLY ARG GLN VAL GLN TRP ASP LYS
SEQRES 10 B 335 VAL PHE THR SER CYS PHE LEU THR VAL ASP GLY GLU ILE
SEQRES 11 B 335 GLU GLY LYS ILE GLY ARG ALA VAL VAL GLY SER SER ASP
SEQRES 12 B 335 LYS VAL LEU GLU ALA VAL ALA SER GLU THR VAL GLY SER
SEQRES 13 B 335 THR ALA VAL VAL ALA LEU VAL CYS SER SER HIS ILE VAL
SEQRES 14 B 335 VAL SER ASN CYS GLY ASP SER ARG ALA VAL LEU PHE ARG
SEQRES 15 B 335 GLY LYS GLU ALA MET PRO LEU SER VAL ASP HIS LYS PRO
SEQRES 16 B 335 ASP ARG GLU ASP GLU TYR ALA ARG ILE GLU ASN ALA GLY
SEQRES 17 B 335 GLY LYS VAL ILE GLN TRP GLN GLY ALA ARG VAL PHE GLY
SEQRES 18 B 335 VAL LEU ALA MET SER ARG SER ILE GLY ASP ARG TYR LEU
SEQRES 19 B 335 LYS PRO TYR VAL ILE PRO GLU PRO GLU VAL THR PHE MET
SEQRES 20 B 335 PRO ARG SER ARG GLU ASP GLU CYS LEU ILE LEU ALA SER
SEQRES 21 B 335 ASP GLY LEU TRP ASP VAL MET ASN ASN GLN GLU VAL CYS
SEQRES 22 B 335 GLU ILE ALA ARG ARG ARG ILE LEU MET TRP HIS LYS LYS
SEQRES 23 B 335 ASN GLY ALA PRO PRO LEU ALA GLU ARG GLY LYS GLY ILE
SEQRES 24 B 335 ASP PRO ALA CYS GLN ALA ALA ALA ASP TYR LEU SER MET
SEQRES 25 B 335 LEU ALA LEU GLN LYS GLY SER LYS ASP ASN ILE SER ILE
SEQRES 26 B 335 ILE VAL ILE ASP LEU LYS ALA GLN ARG LYS
HET A8S A 800 19
HET MG B 601 1
HET MG B 602 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 MG MAGNESIUM 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 MG 2(MG 2+)
FORMUL 6 HOH *19(H2 O)
HELIX 1 AA1 THR A 26 HIS A 41 1 16
HELIX 2 AA2 PRO A 61 ARG A 70 1 10
HELIX 3 AA3 ASN A 74 TYR A 78 5 5
HELIX 4 AA4 THR A 181 SER A 204 1 24
HELIX 5 AA5 VAL B 250 LEU B 258 1 9
HELIX 6 AA6 HIS B 259 GLU B 267 1 9
HELIX 7 AA7 GLN B 283 GLY B 303 1 21
HELIX 8 AA8 ARG B 368 ALA B 378 1 11
HELIX 9 AA9 ARG B 403 LYS B 406 5 4
HELIX 10 AB1 SER B 431 ASP B 436 1 6
HELIX 11 AB2 ASN B 439 GLY B 459 1 21
HELIX 12 AB3 ASP B 471 LYS B 488 1 18
SHEET 1 AA1 7 THR A 49 VAL A 58 0
SHEET 2 AA1 7 LYS A 161 ASP A 175 -1 O VAL A 168 N HIS A 56
SHEET 3 AA1 7 ARG A 145 GLU A 157 -1 N PHE A 153 O TYR A 165
SHEET 4 AA1 7 ILE A 129 GLY A 136 -1 N LEU A 130 O THR A 148
SHEET 5 AA1 7 THR A 115 ASP A 124 -1 N VAL A 117 O LEU A 135
SHEET 6 AA1 7 ILE A 102 VAL A 107 -1 N VAL A 105 O SER A 116
SHEET 7 AA1 7 ILE A 82 ILE A 87 -1 N LYS A 83 O SER A 106
SHEET 1 AA2 5 TRP B 190 ILE B 195 0
SHEET 2 AA2 5 ILE B 494 ASP B 500 -1 O ILE B 496 N VAL B 193
SHEET 3 AA2 5 ASP B 424 ALA B 430 -1 N LEU B 429 O ILE B 497
SHEET 4 AA2 5 ARG B 348 ARG B 353 -1 N PHE B 352 O GLU B 425
SHEET 5 AA2 5 GLU B 356 PRO B 359 -1 O MET B 358 N LEU B 351
SHEET 1 AA3 4 ASP B 204 LYS B 214 0
SHEET 2 AA3 4 THR B 235 HIS B 245 -1 O TYR B 242 N ALA B 205
SHEET 3 AA3 4 GLY B 326 SER B 327 -1 O GLY B 326 N HIS B 245
SHEET 4 AA3 4 ILE B 400 GLY B 401 -1 O ILE B 400 N SER B 327
SHEET 1 AA4 5 ASP B 204 LYS B 214 0
SHEET 2 AA4 5 THR B 235 HIS B 245 -1 O TYR B 242 N ALA B 205
SHEET 3 AA4 5 ALA B 329 VAL B 334 -1 O ALA B 332 N PHE B 239
SHEET 4 AA4 5 HIS B 338 CYS B 344 -1 O SER B 342 N VAL B 331
SHEET 5 AA4 5 GLU B 414 PRO B 419 -1 O MET B 418 N ILE B 339
SHEET 1 AA5 2 ARG B 307 ALA B 308 0
SHEET 2 AA5 2 LYS B 315 VAL B 316 -1 O VAL B 316 N ARG B 307
SHEET 1 AA6 2 VAL B 382 GLN B 384 0
SHEET 2 AA6 2 ALA B 388 VAL B 390 -1 O ARG B 389 N ILE B 383
LINK OD1 ASP B 243 MG MG B 601 1555 1555 2.96
LINK OD2 ASP B 243 MG MG B 601 1555 1555 2.14
LINK OD1 ASP B 243 MG MG B 602 1555 1555 2.26
LINK O GLY B 244 MG MG B 602 1555 1555 2.74
LINK OD1 ASP B 432 MG MG B 601 1555 1555 2.55
LINK OD2 ASP B 492 MG MG B 601 1555 1555 2.03
LINK MG MG B 601 O HOH B 703 1555 1555 2.13
LINK MG MG B 601 O HOH B 706 1555 1555 2.13
LINK MG MG B 602 O HOH B 707 1555 1555 2.11
CISPEP 1 LYS B 406 PRO B 407 0 -0.40
SITE 1 AC1 14 LYS A 79 PHE A 81 VAL A 107 ALA A 113
SITE 2 AC1 14 SER A 116 PHE A 132 HIS A 139 TYR A 144
SITE 3 AC1 14 GLU A 170 PHE A 188 VAL A 192 ASN A 196
SITE 4 AC1 14 HOH A 902 HOH A 903
SITE 1 AC2 6 ASP B 243 ASP B 432 ASP B 492 MG B 602
SITE 2 AC2 6 HOH B 703 HOH B 706
SITE 1 AC3 4 ASP B 243 GLY B 244 MG B 601 HOH B 707
CRYST1 45.330 75.310 169.200 90.00 90.00 90.00 P 21 2 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 0.022060 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013278 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
