HEADER TRANSFERASE 04-NOV-15 5ELA
TITLE THE STRUCTURE OF DHAR1 FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE DHAR1, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHLORIDE INTRACELLULAR CHANNEL HOMOLOG 1,CLIC HOMOLOG 1,
COMPND 5 GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE 1,MTDHAR;
COMPND 6 EC: 2.5.1.18, 1.8.5.1;
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 GENE: DHAR1, DHAR5, AT1G19570, F14P1.9, F18O14.22;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24-DHAR1
KEYWDS DEHYDROASCOBATE REDUCTASE, GLUTATHIONE S-TRANSFERASE, ARABIDOPSIS
KEYWDS 2 THALIANA, CLIC, CHLORIDE ION CHANNEL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MENAULT,A.W.ROSZAK,A.J.LAPTHORN
REVDAT 2 10-JAN-24 5ELA 1 REMARK
REVDAT 1 16-NOV-16 5ELA 0
JRNL AUTH M.MENAULT,A.W.ROSZAK,A.J.LAPTHORN
JRNL TITL ARABIDOPSIS THALIANA DHAR1 APO STRUCTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.P.DIXON,B.G.DAVIS,R.EDWARDS
REMARK 1 TITL FUNCTIONAL DIVERGENCE IN THE GLUTATHIONE TRANSFERASE
REMARK 1 TITL 2 SUPERFAMILY IN PLANTS. IDENTIFICATION OF TWO CLASSES WITH
REMARK 1 TITL 3 PUTATIVE FUNCTIONS IN REDOX HOMEOSTASIS IN ARABIDOPSIS
REMARK 1 TITL 4 THALIANA.
REMARK 1 REF J. BIOL. CHEM. V. 277 30859 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12077129
REMARK 1 DOI 10.1074/JBC.M202919200
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 14717
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 774
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) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1050
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1662
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.49000
REMARK 3 B22 (A**2) : -1.49000
REMARK 3 B33 (A**2) : 4.83000
REMARK 3 B12 (A**2) : -0.74000
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): 0.202
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.546
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1720 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1630 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2343 ; 1.569 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3790 ; 0.820 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 213 ; 6.386 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;34.458 ;25.352
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 284 ;15.723 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;14.885 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 263 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1902 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 362 ; 0.001 ; 0.020
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): 849 ; 3.050 ; 4.548
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 848 ; 3.018 ; 4.545
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1060 ; 4.327 ; 6.801
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1061 ; 4.337 ; 6.806
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 871 ; 3.687 ; 4.993
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 871 ; 3.687 ; 4.993
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1283 ; 5.578 ; 7.321
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2004 ; 7.960 ;37.435
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2004 ; 7.961 ;37.435
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 : 1
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 213
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7296 16.6123 -7.8888
REMARK 3 T TENSOR
REMARK 3 T11: 0.0515 T22: 0.1943
REMARK 3 T33: 0.0835 T12: -0.0073
REMARK 3 T13: 0.0019 T23: 0.0982
REMARK 3 L TENSOR
REMARK 3 L11: 1.4333 L22: 2.7077
REMARK 3 L33: 1.3565 L12: -0.2287
REMARK 3 L13: 0.3043 L23: 1.5332
REMARK 3 S TENSOR
REMARK 3 S11: 0.1020 S12: -0.0277 S13: -0.0046
REMARK 3 S21: 0.0179 S22: 0.0368 S23: -0.2086
REMARK 3 S31: 0.1465 S32: 0.0224 S33: -0.1388
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 5ELA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215102.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0 -8 .5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15525
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 54.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 18.10
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 19.40
REMARK 200 R MERGE FOR SHELL (I) : 0.63500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5EL8
REMARK 200
REMARK 200 REMARK: HEXAGONAL BIPYRAMIDAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 20 MG/ML, 20% PEG 8000, 0.2
REMARK 280 M NAK PHOSPHATE, 0.1M TRIS, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 177.56667
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 88.78333
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 133.17500
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 44.39167
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 221.95833
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 177.56667
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 88.78333
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 44.39167
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 133.17500
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 221.95833
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 TOTAL BURIED SURFACE AREA: 270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 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 MET A 1
REMARK 465 VAL A 214
REMARK 465 GLU A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
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 68 CG CD CE NZ
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 O HOH A 451 O HOH A 475 2.04
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 ALA A 13 67.90 -161.07
REMARK 500 ASP A 66 -126.51 54.79
REMARK 500 ASP A 72 104.45 82.91
REMARK 500 SER A 112 135.01 -37.96
REMARK 500 SER A 115 -8.46 -45.12
REMARK 500 PHE A 177 64.85 -114.01
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 GOL A 301
DBREF 5ELA A 1 213 UNP Q9FWR4 DHAR1_ARATH 1 213
SEQADV 5ELA VAL A 214 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA GLU A 215 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 216 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 217 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 218 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 219 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 220 UNP Q9FWR4 EXPRESSION TAG
SEQADV 5ELA HIS A 221 UNP Q9FWR4 EXPRESSION TAG
SEQRES 1 A 221 MET ALA LEU GLU ILE CYS VAL LYS ALA ALA VAL GLY ALA
SEQRES 2 A 221 PRO ASP HIS LEU GLY ASP OCS PRO PHE SER GLN ARG ALA
SEQRES 3 A 221 LEU LEU THR LEU GLU GLU LYS SER LEU THR TYR LYS ILE
SEQRES 4 A 221 HIS LEU ILE ASN LEU SER ASP LYS PRO GLN TRP PHE LEU
SEQRES 5 A 221 ASP ILE SER PRO GLN GLY LYS VAL PRO VAL LEU LYS ILE
SEQRES 6 A 221 ASP ASP LYS TRP VAL THR ASP SER ASP VAL ILE VAL GLY
SEQRES 7 A 221 ILE LEU GLU GLU LYS TYR PRO ASP PRO PRO LEU LYS THR
SEQRES 8 A 221 PRO ALA GLU PHE ALA SER VAL GLY SER ASN ILE PHE GLY
SEQRES 9 A 221 THR PHE GLY THR PHE LEU LYS SER LYS ASP SER ASN ASP
SEQRES 10 A 221 GLY SER GLU HIS ALA LEU LEU VAL GLU LEU GLU ALA LEU
SEQRES 11 A 221 GLU ASN HIS LEU LYS SER HIS ASP GLY PRO PHE ILE ALA
SEQRES 12 A 221 GLY GLU ARG VAL SER ALA VAL ASP LEU SER LEU ALA PRO
SEQRES 13 A 221 LYS LEU TYR HIS LEU GLN VAL ALA LEU GLY HIS PHE LYS
SEQRES 14 A 221 SER TRP SER VAL PRO GLU SER PHE PRO HIS VAL HIS ASN
SEQRES 15 A 221 TYR MET LYS THR LEU PHE SER LEU ASP SER PHE GLU LYS
SEQRES 16 A 221 THR LYS THR GLU GLU LYS TYR VAL ILE SER GLY TRP ALA
SEQRES 17 A 221 PRO LYS VAL ASN PRO VAL GLU HIS HIS HIS HIS HIS HIS
MODRES 5ELA OCS A 20 CYS MODIFIED RESIDUE
HET OCS A 20 9
HET GOL A 301 6
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 OCS C3 H7 N O5 S
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *89(H2 O)
HELIX 1 AA1 OCS A 20 LYS A 33 1 14
HELIX 2 AA2 PRO A 48 SER A 55 1 8
HELIX 3 AA3 ASP A 72 TYR A 84 1 13
HELIX 4 AA4 PRO A 92 ALA A 96 5 5
HELIX 5 AA5 ASN A 101 SER A 112 1 12
HELIX 6 AA6 GLY A 118 HIS A 137 1 20
HELIX 7 AA7 SER A 148 SER A 170 1 23
HELIX 8 AA8 PHE A 177 SER A 189 1 13
HELIX 9 AA9 LEU A 190 LYS A 197 1 8
HELIX 10 AB1 GLU A 199 ALA A 208 1 10
HELIX 11 AB2 PRO A 209 VAL A 211 5 3
SHEET 1 AA1 3 ALA A 13 LEU A 17 0
SHEET 2 AA1 3 LEU A 3 ALA A 10 -1 N ALA A 10 O HIS A 16
SHEET 3 AA1 3 TYR A 37 ILE A 42 1 O ILE A 42 N VAL A 7
SHEET 1 AA2 4 ALA A 13 LEU A 17 0
SHEET 2 AA2 4 LEU A 3 ALA A 10 -1 N ALA A 10 O HIS A 16
SHEET 3 AA2 4 VAL A 62 ILE A 65 -1 O LYS A 64 N GLU A 4
SHEET 4 AA2 4 LYS A 68 THR A 71 -1 O VAL A 70 N LEU A 63
LINK C ASP A 19 N OCS A 20 1555 1555 1.32
LINK C OCS A 20 N PRO A 21 1555 1555 1.34
CISPEP 1 VAL A 60 PRO A 61 0 -2.62
CISPEP 2 ASP A 86 PRO A 87 0 -4.35
CISPEP 3 GLY A 139 PRO A 140 0 5.55
SITE 1 AC1 7 LYS A 8 ASP A 19 PRO A 21 PHE A 103
SITE 2 AC1 7 GLY A 206 TRP A 207 LYS A 210
CRYST1 63.690 63.690 266.350 90.00 90.00 120.00 P 65 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 0.015701 0.009065 0.000000 0.00000
SCALE2 0.000000 0.018130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003754 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
