HEADER OXIDOREDUCTASE 11-MAY-05 2BRT
TITLE ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH
TITLE 2 NARINGENIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCOANTHOCYANIDIN DIOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LDOX, LEUCOCYANIDIN OXYGENASE, ANS, LEUCOANTHOCYANIDIN
COMPND 5 HYDROXYLASE, ANTHOCYANIDIN SYNTHASE;
COMPND 6 EC: 1.14.11.19;
COMPND 7 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-24A
KEYWDS OXIDOREDUCTASE, DIOXYGENASE, FLAVONOID BIOSYNTHESIS, IRON, METAL-
KEYWDS 2 BINDING, VITAMIN C
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TURNBULL,I.J.CLIFTON,R.W.D.WELFORD,C.J.SCHOFIELD
REVDAT 5 13-DEC-23 2BRT 1 REMARK LINK
REVDAT 4 13-JUL-11 2BRT 1 VERSN
REVDAT 3 22-DEC-09 2BRT 1 VERSN
REVDAT 2 24-FEB-09 2BRT 1 VERSN
REVDAT 1 29-AUG-06 2BRT 0
JRNL AUTH R.W.D.WELFORD,I.J.CLIFTON,J.J.TURNBULL,S.C.WILSON,
JRNL AUTH 2 C.J.SCHOFIELD
JRNL TITL STRUCTURAL AND MECHANISTIC STUDIES ON ANTHOCYANIDIN SYNTHASE
JRNL TITL 2 CATALYSED OXIDATION OF FLAVANONE SUBSTRATES: THE EFFECT OF
JRNL TITL 3 C-2 STEREOCHEMISTRY ON PRODUCT SELECTIVITY AND MECHANISM
JRNL REF ORG.BIOMOL.CHEM. V. 3 3117 2005
JRNL REFN ISSN 1477-0520
JRNL PMID 16106293
JRNL DOI 10.1039/B507153D
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 17793
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.200
REMARK 3 FREE R VALUE TEST SET COUNT : 785
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1293
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2685
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 42.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : 2.31000
REMARK 3 B33 (A**2) : -1.77000
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): 0.312
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.239
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.922
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2778 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2489 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3772 ; 1.887 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5800 ; 0.913 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 347 ; 7.457 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;37.807 ;25.210
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;16.659 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.978 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 413 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3097 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 519 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 629 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2529 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1329 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1586 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 145 ; 0.194 ; 0.200
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): 6 ; 0.314 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 23 ; 0.183 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.169 ; 0.200
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): 1789 ; 0.850 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2791 ; 1.316 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1140 ; 2.240 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 981 ; 3.245 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1600 34.9777 39.8590
REMARK 3 T TENSOR
REMARK 3 T11: -0.0047 T22: -0.1218
REMARK 3 T33: -0.2709 T12: 0.1409
REMARK 3 T13: -0.0907 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 5.7523 L22: 3.8752
REMARK 3 L33: 5.9026 L12: -0.4875
REMARK 3 L13: -1.8878 L23: -1.3383
REMARK 3 S TENSOR
REMARK 3 S11: 0.1949 S12: -0.2940 S13: 0.5323
REMARK 3 S21: 0.0530 S22: -0.0413 S23: 0.0307
REMARK 3 S31: -1.0184 S32: -0.7256 S33: -0.1536
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0972 16.3827 38.3985
REMARK 3 T TENSOR
REMARK 3 T11: -0.2054 T22: -0.2400
REMARK 3 T33: -0.2135 T12: -0.0259
REMARK 3 T13: -0.0028 T23: 0.0694
REMARK 3 L TENSOR
REMARK 3 L11: 3.6105 L22: 5.8946
REMARK 3 L33: 4.5007 L12: 1.1331
REMARK 3 L13: 0.9141 L23: -0.1623
REMARK 3 S TENSOR
REMARK 3 S11: -0.2385 S12: -0.3203 S13: -0.4672
REMARK 3 S21: -0.2970 S22: -0.1390 S23: -0.2534
REMARK 3 S31: 0.5481 S32: -0.3307 S33: 0.3775
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3200 28.9304 37.2102
REMARK 3 T TENSOR
REMARK 3 T11: -0.2324 T22: -0.0679
REMARK 3 T33: -0.2791 T12: 0.1618
REMARK 3 T13: 0.0157 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 3.1089 L22: 2.1244
REMARK 3 L33: 6.8648 L12: -0.5538
REMARK 3 L13: -0.6388 L23: -0.6509
REMARK 3 S TENSOR
REMARK 3 S11: 0.2160 S12: -0.2270 S13: 0.0308
REMARK 3 S21: 0.0542 S22: -0.1587 S23: 0.1190
REMARK 3 S31: -0.7118 S32: -1.3794 S33: -0.0573
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 301 A 347
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4350 29.9891 20.7473
REMARK 3 T TENSOR
REMARK 3 T11: -0.0059 T22: 0.2449
REMARK 3 T33: -0.2100 T12: 0.3687
REMARK 3 T13: -0.0164 T23: -0.0812
REMARK 3 L TENSOR
REMARK 3 L11: 5.1316 L22: 1.8752
REMARK 3 L33: 13.0308 L12: -1.9415
REMARK 3 L13: 0.7983 L23: -0.5018
REMARK 3 S TENSOR
REMARK 3 S11: 0.3661 S12: 0.9092 S13: 0.1070
REMARK 3 S21: -0.5982 S22: -0.5251 S23: -0.1473
REMARK 3 S31: -0.9808 S32: -2.0977 S33: 0.1590
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2BRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1290021606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18607
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GP4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG 2000 MONOMETHYLETHER,
REMARK 280 50MM MES, 200MM AMMONIUM ACETATE, 2MM FESO4, 10MM POTASSIUM
REMARK 280 ALPHA-KETOGLUTARATE, 10MM SODIUM ASCORBATE, 2.5MM RACEMIC
REMARK 280 NARINGENIN IN 10% (V/V) MEOH, PH 6.50
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 28.40350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.24650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.15450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.24650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.40350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.15450
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 LEU A 350
REMARK 465 VAL A 351
REMARK 465 SER A 352
REMARK 465 GLU A 353
REMARK 465 LYS A 354
REMARK 465 ASN A 355
REMARK 465 ASP A 356
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 12 CE NZ
REMARK 470 ILE A 16 CG1 CG2 CD1
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 LYS A 26 NZ
REMARK 470 LEU A 37 CG CD1 CD2
REMARK 470 LYS A 40 CE NZ
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 ASP A 59 CG OD1 OD2
REMARK 470 GLU A 60 CB CG CD OE1 OE2
REMARK 470 LYS A 61 CB CG CD CE NZ
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 LYS A 72 CD CE NZ
REMARK 470 LYS A 112 CD CE NZ
REMARK 470 GLU A 167 CD OE1 OE2
REMARK 470 LEU A 205 CG CD1 CD2
REMARK 470 GLU A 206 CG CD OE1 OE2
REMARK 470 LYS A 256 CD CE NZ
REMARK 470 LYS A 261 NZ
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 LYS A 284 CE NZ
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 LYS A 296 CD CE NZ
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 VAL A 321 CG1 CG2
REMARK 470 VAL A 323 CG1 CG2
REMARK 470 LEU A 342 CG CD1 CD2
REMARK 470 LYS A 345 CE NZ
REMARK 470 GLU A 346 CG CD OE1 OE2
REMARK 470 GLN A 347 CG CD OE1 NE2
REMARK 470 GLU A 349 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 68 CD GLU A 68 OE1 0.262
REMARK 500 GLU A 68 CD GLU A 68 OE2 0.238
REMARK 500 LEU A 193 C LEU A 193 O 0.135
REMARK 500 GLU A 194 CD GLU A 194 OE1 0.172
REMARK 500 GLU A 194 CD GLU A 194 OE2 0.117
REMARK 500 GLU A 254 CD GLU A 254 OE2 0.102
REMARK 500 GLU A 319 CD GLU A 319 OE1 0.149
REMARK 500 GLU A 319 CD GLU A 319 OE2 0.177
REMARK 500 MET A 320 C MET A 320 O 0.138
REMARK 500 GLU A 324 CD GLU A 324 OE1 0.495
REMARK 500 GLU A 324 CD GLU A 324 OE2 0.361
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 68 OE1 - CD - OE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLU A 324 OE1 - CD - OE2 ANGL. DEV. = 14.2 DEGREES
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 LYS A 53 -55.09 -27.87
REMARK 500 ASP A 76 -60.96 -97.63
REMARK 500 SER A 236 171.63 -59.26
REMARK 500 ASN A 244 31.79 -91.62
REMARK 500 GLU A 254 64.47 25.40
REMARK 500 LYS A 311 -47.58 124.83
REMARK 500 SER A 325 83.11 -155.51
REMARK 500 GLN A 347 53.07 160.63
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 FE2 A1350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 232 NE2
REMARK 620 2 ASP A 234 OD2 92.9
REMARK 620 3 HIS A 288 NE2 84.3 93.9
REMARK 620 4 AKG A1351 O2 93.3 100.1 166.0
REMARK 620 5 AKG A1351 O5 88.7 176.7 89.2 76.9
REMARK 620 6 HOH A2094 O 177.0 87.2 92.6 89.6 91.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAR A 1352
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GP4 RELATED DB: PDB
REMARK 900 ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA (SELENOMETHIONINE
REMARK 900 SUBSTITUTED)
REMARK 900 RELATED ID: 1GP5 RELATED DB: PDB
REMARK 900 ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH
REMARK 900 TRANS-DIHYDROQUERCETIN
REMARK 900 RELATED ID: 1GP6 RELATED DB: PDB
REMARK 900 ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH
REMARK 900 TRANS-DIHYDROQUERCETIN (WITH 30 MIN EXPOSURE TO O2)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 350-356 DISORDERED
DBREF 2BRT A 2 356 UNP Q96323 LDOX_ARATH 2 356
SEQRES 1 A 355 VAL ALA VAL GLU ARG VAL GLU SER LEU ALA LYS SER GLY
SEQRES 2 A 355 ILE ILE SER ILE PRO LYS GLU TYR ILE ARG PRO LYS GLU
SEQRES 3 A 355 GLU LEU GLU SER ILE ASN ASP VAL PHE LEU GLU GLU LYS
SEQRES 4 A 355 LYS GLU ASP GLY PRO GLN VAL PRO THR ILE ASP LEU LYS
SEQRES 5 A 355 ASN ILE GLU SER ASP ASP GLU LYS ILE ARG GLU ASN CYS
SEQRES 6 A 355 ILE GLU GLU LEU LYS LYS ALA SER LEU ASP TRP GLY VAL
SEQRES 7 A 355 MET HIS LEU ILE ASN HIS GLY ILE PRO ALA ASP LEU MET
SEQRES 8 A 355 GLU ARG VAL LYS LYS ALA GLY GLU GLU PHE PHE SER LEU
SEQRES 9 A 355 SER VAL GLU GLU LYS GLU LYS TYR ALA ASN ASP GLN ALA
SEQRES 10 A 355 THR GLY LYS ILE GLN GLY TYR GLY SER LYS LEU ALA ASN
SEQRES 11 A 355 ASN ALA SER GLY GLN LEU GLU TRP GLU ASP TYR PHE PHE
SEQRES 12 A 355 HIS LEU ALA TYR PRO GLU GLU LYS ARG ASP LEU SER ILE
SEQRES 13 A 355 TRP PRO LYS THR PRO SER ASP TYR ILE GLU ALA THR SER
SEQRES 14 A 355 GLU TYR ALA LYS CYS LEU ARG LEU LEU ALA THR LYS VAL
SEQRES 15 A 355 PHE LYS ALA LEU SER VAL GLY LEU GLY LEU GLU PRO ASP
SEQRES 16 A 355 ARG LEU GLU LYS GLU VAL GLY GLY LEU GLU GLU LEU LEU
SEQRES 17 A 355 LEU GLN MET LYS ILE ASN TYR TYR PRO LYS CYS PRO GLN
SEQRES 18 A 355 PRO GLU LEU ALA LEU GLY VAL GLU ALA HIS THR ASP VAL
SEQRES 19 A 355 SER ALA LEU THR PHE ILE LEU HIS ASN MET VAL PRO GLY
SEQRES 20 A 355 LEU GLN LEU PHE TYR GLU GLY LYS TRP VAL THR ALA LYS
SEQRES 21 A 355 CYS VAL PRO ASP SER ILE VAL MET HIS ILE GLY ASP THR
SEQRES 22 A 355 LEU GLU ILE LEU SER ASN GLY LYS TYR LYS SER ILE LEU
SEQRES 23 A 355 HIS ARG GLY LEU VAL ASN LYS GLU LYS VAL ARG ILE SER
SEQRES 24 A 355 TRP ALA VAL PHE CYS GLU PRO PRO LYS ASP LYS ILE VAL
SEQRES 25 A 355 LEU LYS PRO LEU PRO GLU MET VAL SER VAL GLU SER PRO
SEQRES 26 A 355 ALA LYS PHE PRO PRO ARG THR PHE ALA GLN HIS ILE GLU
SEQRES 27 A 355 HIS LYS LEU PHE GLY LYS GLU GLN GLU GLU LEU VAL SER
SEQRES 28 A 355 GLU LYS ASN ASP
HET FE2 A1350 1
HET AKG A1351 10
HET NAR A1352 20
HETNAM FE2 FE (II) ION
HETNAM AKG 2-OXOGLUTARIC ACID
HETNAM NAR NARINGENIN
FORMUL 2 FE2 FE 2+
FORMUL 3 AKG C5 H6 O5
FORMUL 4 NAR C15 H12 O5
FORMUL 5 HOH *128(H2 O)
HELIX 1 1 ARG A 6 SER A 13 1 8
HELIX 2 2 PRO A 19 ILE A 23 5 5
HELIX 3 3 PRO A 25 GLU A 30 1 6
HELIX 4 4 ASP A 34 GLU A 39 1 6
HELIX 5 5 ASP A 59 TRP A 77 1 19
HELIX 6 6 PRO A 88 SER A 104 1 17
HELIX 7 7 SER A 106 GLU A 111 1 6
HELIX 8 8 GLN A 117 GLY A 120 5 4
HELIX 9 9 PRO A 149 ARG A 153 5 5
HELIX 10 10 ASP A 154 TRP A 158 5 5
HELIX 11 11 ASP A 164 GLY A 192 1 29
HELIX 12 12 ASP A 196 GLY A 203 1 8
HELIX 13 13 GLY A 203 LEU A 208 1 6
HELIX 14 14 GLN A 222 ALA A 226 5 5
HELIX 15 15 GLY A 272 SER A 279 1 8
HELIX 16 16 LEU A 317 VAL A 321 5 5
HELIX 17 17 PHE A 334 GLU A 346 1 13
SHEET 1 AA 8 THR A 49 ASP A 51 0
SHEET 2 AA 8 VAL A 79 ILE A 83 1 O HIS A 81 N ILE A 50
SHEET 3 AA 8 ILE A 267 ILE A 271 -1 O ILE A 267 N LEU A 82
SHEET 4 AA 8 LEU A 238 HIS A 243 -1 O THR A 239 N HIS A 270
SHEET 5 AA 8 ARG A 298 GLU A 306 -1 O TRP A 301 N LEU A 242
SHEET 6 AA 8 LEU A 209 TYR A 217 -1 O LEU A 209 N GLU A 306
SHEET 7 AA 8 ASP A 141 TYR A 148 -1 O ASP A 141 N TYR A 216
SHEET 8 AA 8 GLY A 124 SER A 127 -1 O GLY A 124 N PHE A 144
SHEET 1 AB 4 VAL A 229 HIS A 232 0
SHEET 2 AB 4 HIS A 288 GLY A 290 -1 O HIS A 288 N HIS A 232
SHEET 3 AB 4 LEU A 249 TYR A 253 -1 O GLN A 250 N ARG A 289
SHEET 4 AB 4 LYS A 256 THR A 259 -1 O LYS A 256 N TYR A 253
SHEET 1 AC 2 VAL A 313 LEU A 314 0
SHEET 2 AC 2 ARG A 332 THR A 333 -1 O ARG A 332 N LEU A 314
LINK NE2 HIS A 232 FE FE2 A1350 1555 1555 2.31
LINK OD2 ASP A 234 FE FE2 A1350 1555 1555 2.15
LINK NE2 HIS A 288 FE FE2 A1350 1555 1555 2.29
LINK FE FE2 A1350 O2 AKG A1351 1555 1555 2.12
LINK FE FE2 A1350 O5 AKG A1351 1555 1555 2.15
LINK FE FE2 A1350 O HOH A2094 1555 1555 2.24
CISPEP 1 TYR A 148 PRO A 149 0 3.48
CISPEP 2 THR A 161 PRO A 162 0 3.95
SITE 1 AC1 5 HIS A 232 ASP A 234 HIS A 288 AKG A1351
SITE 2 AC1 5 HOH A2094
SITE 1 AC2 11 ASN A 215 TYR A 217 HIS A 232 ASP A 234
SITE 2 AC2 11 HIS A 288 ARG A 298 SER A 300 PHE A 304
SITE 3 AC2 11 FE2 A1350 NAR A1352 HOH A2094
SITE 1 AC3 10 TYR A 142 ASP A 234 VAL A 235 SER A 236
SITE 2 AC3 10 PHE A 304 GLU A 306 PHE A 334 AKG A1351
SITE 3 AC3 10 HOH A2085 HOH A2128
CRYST1 56.807 62.309 102.493 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 0.017603 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
