HEADER DNA BINDING PROTEIN 22-JUN-18 6A59
TITLE STRUCTURE OF HISTONE DEMETHYLASE REF6 AT 1.8A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE REF6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IG GAMMA-1 CHAIN C REGION;
COMPND 5 SYNONYM: JUMONJI DOMAIN-CONTAINING PROTEIN 12,LYSINE-SPECIFIC HISTONE
COMPND 6 DEMETHYLASE REF6,PROTEIN RELATIVE OF EARLY FLOWERING 6;
COMPND 7 EC: 1.14.11.-;
COMPND 8 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: REF6, JMJ12, PKDM9A, AT3G48430, T29H11_50;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, HISTONE DEMETHYLASE REF6, DNA, ZINC FINGER, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.TIAN,Z.CHEN
REVDAT 3 22-NOV-23 6A59 1 REMARK
REVDAT 2 08-JUL-20 6A59 1 JRNL
REVDAT 1 26-JUN-19 6A59 0
JRNL AUTH Z.TIAN,X.LI,M.LI,W.WU,M.ZHANG,C.TANG,Z.LI,Y.LIU,Z.CHEN,
JRNL AUTH 2 M.YANG,L.MA,C.CABA,Y.TONG,H.M.LAM,S.DAI,Z.CHEN
JRNL TITL CRYSTAL STRUCTURES OF REF6 AND ITS COMPLEX WITH DNA REVEAL
JRNL TITL 2 DIVERSE RECOGNITION MECHANISMS.
JRNL REF CELL DISCOV V. 6 17 2020
JRNL REFN ESSN 2056-5968
JRNL PMID 32257379
JRNL DOI 10.1038/S41421-020-0150-6
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 14748
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 826
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1063
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 927
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
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): 0.174
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.486
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 964 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 897 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1293 ; 0.959 ; 1.905
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2065 ; 0.801 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 115 ; 4.720 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 46 ;22.519 ;21.087
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 173 ;12.141 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;11.910 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 126 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1080 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 262 ; 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): 457 ; 1.320 ; 3.957
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 456 ; 1.319 ; 3.947
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 570 ; 1.595 ; 5.916
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 571 ; 1.594 ; 5.928
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 507 ; 1.013 ; 4.138
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 507 ; 1.011 ; 4.138
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 723 ; 1.176 ; 6.134
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1121 ; 2.581 ;31.647
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1104 ; 2.336 ;31.447
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1861 ; 0.567 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 45 ;20.603 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1887 ; 4.961 ; 5.000
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 : 1.20
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 6A59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1300008176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL18U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15648
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 63.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
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) : 0.46000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL2MAP
REMARK 200 STARTING MODEL: 6A58
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 21.76650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 10.88325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.64975
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 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 GLY A 1221
REMARK 465 SER A 1222
REMARK 465 VAL A 1223
REMARK 465 GLU A 1224
REMARK 465 GLU A 1225
REMARK 465 LYS A 1226
REMARK 465 GLU A 1227
REMARK 465 GLU A 1228
REMARK 465 GLU A 1229
REMARK 465 GLU A 1230
REMARK 465 GLU A 1231
REMARK 465 GLU A 1232
REMARK 465 GLU A 1233
REMARK 465 GLU A 1234
REMARK 465 ASN A 1235
REMARK 465 GLU A 1236
REMARK 465 GLU A 1237
REMARK 465 GLU A 1238
REMARK 465 GLU A 1239
REMARK 465 VAL A 1354
REMARK 465 LYS A 1355
REMARK 465 LYS A 1356
REMARK 465 THR A 1357
REMARK 465 ASN A 1358
REMARK 465 LYS A 1359
REMARK 465 ARG A 1360
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 A1330 CG CD OE1 OE2
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 CYS A1273 -61.58 -90.21
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 A1594 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A1595 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH A1596 DISTANCE = 8.64 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 ZN A1401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1245 SG
REMARK 620 2 CYS A1250 SG 113.8
REMARK 620 3 HIS A1263 NE2 112.4 108.3
REMARK 620 4 HIS A1280 NE2 133.7 81.8 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1268 SG
REMARK 620 2 CYS A1273 SG 116.6
REMARK 620 3 HIS A1290 NE2 126.1 98.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1298 SG
REMARK 620 2 CYS A1303 SG 119.1
REMARK 620 3 HIS A1316 NE2 126.5 97.1
REMARK 620 4 HIS A1320 NE2 121.1 97.1 88.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1328 SG
REMARK 620 2 CYS A1333 SG 112.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6A58 RELATED DB: PDB
REMARK 900 RELATED ID: 6A57 RELATED DB: PDB
DBREF 6A59 A 1223 1360 UNP Q9STM3 REF6_ARATH 1223 1360
SEQADV 6A59 GLY A 1221 UNP Q9STM3 EXPRESSION TAG
SEQADV 6A59 SER A 1222 UNP Q9STM3 EXPRESSION TAG
SEQRES 1 A 140 GLY SER VAL GLU GLU LYS GLU GLU GLU GLU GLU GLU GLU
SEQRES 2 A 140 GLU ASN GLU GLU GLU GLU CYS ALA ALA TYR GLN CYS ASN
SEQRES 3 A 140 MET GLU GLY CYS THR MET SER PHE SER SER GLU LYS GLN
SEQRES 4 A 140 LEU MET LEU HIS LYS ARG ASN ILE CYS PRO ILE LYS GLY
SEQRES 5 A 140 CYS GLY LYS ASN PHE PHE SER HIS LYS TYR LEU VAL GLN
SEQRES 6 A 140 HIS GLN ARG VAL HIS SER ASP ASP ARG PRO LEU LYS CYS
SEQRES 7 A 140 PRO TRP LYS GLY CYS LYS MET THR PHE LYS TRP ALA TRP
SEQRES 8 A 140 SER ARG THR GLU HIS ILE ARG VAL HIS THR GLY ALA ARG
SEQRES 9 A 140 PRO TYR VAL CYS ALA GLU PRO ASP CYS GLY GLN THR PHE
SEQRES 10 A 140 ARG PHE VAL SER ASP PHE SER ARG HIS LYS ARG LYS THR
SEQRES 11 A 140 GLY HIS SER VAL LYS LYS THR ASN LYS ARG
HET ZN A1401 1
HET ZN A1402 1
HET ZN A1403 1
HET ZN A1404 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 HOH *96(H2 O)
HELIX 1 AA1 SER A 1256 ARG A 1265 1 10
HELIX 2 AA2 SER A 1279 SER A 1291 1 13
HELIX 3 AA3 TRP A 1309 GLY A 1322 1 14
HELIX 4 AA4 PHE A 1339 THR A 1350 1 12
SHEET 1 AA1 2 TYR A1243 GLN A1244 0
SHEET 2 AA1 2 SER A1253 PHE A1254 -1 O PHE A1254 N TYR A1243
SHEET 1 AA2 2 LEU A1296 LYS A1297 0
SHEET 2 AA2 2 THR A1306 PHE A1307 -1 O PHE A1307 N LEU A1296
SHEET 1 AA3 2 TYR A1326 VAL A1327 0
SHEET 2 AA3 2 THR A1336 PHE A1337 -1 O PHE A1337 N TYR A1326
LINK SG CYS A1245 ZN ZN A1401 1555 1555 2.30
LINK SG CYS A1250 ZN ZN A1401 1555 1555 2.24
LINK NE2 HIS A1263 ZN ZN A1401 1555 1555 2.36
LINK SG CYS A1268 ZN ZN A1402 1555 1555 2.18
LINK SG CYS A1273 ZN ZN A1402 1555 1555 2.29
LINK NE2 HIS A1280 ZN ZN A1401 1555 1555 2.59
LINK NE2 HIS A1290 ZN ZN A1402 1555 1555 2.64
LINK SG CYS A1298 ZN ZN A1403 1555 1555 2.19
LINK SG CYS A1303 ZN ZN A1403 1555 1555 2.25
LINK NE2 HIS A1316 ZN ZN A1403 1555 1555 2.63
LINK NE2 HIS A1320 ZN ZN A1403 1555 1555 2.47
LINK SG CYS A1328 ZN ZN A1404 1555 1555 2.25
LINK SG CYS A1333 ZN ZN A1404 1555 1555 2.43
SITE 1 AC1 4 CYS A1245 CYS A1250 HIS A1263 HIS A1280
SITE 1 AC2 4 CYS A1268 CYS A1273 HIS A1286 HIS A1290
SITE 1 AC3 4 CYS A1298 CYS A1303 HIS A1316 HIS A1320
SITE 1 AC4 4 CYS A1328 CYS A1333 HIS A1346 HIS A1352
CRYST1 63.445 63.445 43.533 90.00 90.00 90.00 P 41 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 0.015762 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022971 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
