HEADER METAL BINDING PROTEIN 16-APR-06 2GP3
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC CORE DOMAIN OF JMJD2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: JMJD2A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T2
KEYWDS BETA BARREL, ZINC FINGER, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.CHEN,J.ZANG,J.WHETSTINE,X.HONG,F.DAVRAZOU,T.G.KUTATELADZE,
AUTHOR 2 M.SIMPSON,S.DAI,J.HAGMAN,Y.SHI,G.ZHANG
REVDAT 5 14-FEB-24 2GP3 1 REMARK LINK
REVDAT 4 27-NOV-13 2GP3 1 HET HETATM HETNAM REMARK
REVDAT 4 2 1 VERSN
REVDAT 3 13-OCT-09 2GP3 1 TITLE
REVDAT 2 20-MAY-08 2GP3 1 JRNL VERSN
REVDAT 1 23-MAY-06 2GP3 0
JRNL AUTH Z.CHEN,J.ZANG,J.WHETSTINE,X.HONG,F.DAVRAZOU,T.G.KUTATELADZE,
JRNL AUTH 2 M.SIMPSON,Q.MAO,C.H.PAN,S.DAI,J.HAGMAN,K.HANSEN,Y.SHI,
JRNL AUTH 3 G.ZHANG
JRNL TITL STRUCTURAL INSIGHTS INTO HISTONE DEMETHYLATION BY JMJD2
JRNL TITL 2 FAMILY MEMBERS
JRNL REF CELL(CAMBRIDGE,MASS.) V. 125 691 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16677698
JRNL DOI 10.1016/J.CELL.2006.04.024
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1360
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3401
REMARK 3 BIN FREE R VALUE : 0.3422
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 38
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5653
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 103
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.390
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 0.9793, 0.9600
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33706
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
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 (%) : 92.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 50.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 200 MM MGCL2, 100 MM
REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,-Z
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 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 50.43350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.77000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.43350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.77000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 LEU B 8
REMARK 465 ASN B 9
REMARK 465 GLU B 349
REMARK 465 ALA B 350
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 ASN A 9 N SER A 11 2.07
REMARK 500 O SER A 3 N SER A 5 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR A 76 O THR B 126 4545 2.19
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 PRO A 10 C - N - CA ANGL. DEV. = 9.6 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 GLU A 4 27.72 -32.73
REMARK 500 GLU A 6 34.15 -54.05
REMARK 500 ASN A 9 136.55 -36.78
REMARK 500 PRO A 10 43.32 -27.11
REMARK 500 ALA A 12 56.47 23.12
REMARK 500 LYS A 51 -50.10 -28.05
REMARK 500 GLU A 52 31.72 -75.71
REMARK 500 ILE A 62 -22.81 -165.86
REMARK 500 ASP A 63 -5.38 -56.58
REMARK 500 SER A 79 71.82 34.92
REMARK 500 LYS A 89 -135.97 -74.74
REMARK 500 ALA A 91 131.92 -15.51
REMARK 500 ASP A 104 -7.65 -48.21
REMARK 500 SER A 112 -77.51 -80.23
REMARK 500 PRO A 129 104.81 -42.56
REMARK 500 LYS A 182 -2.91 74.67
REMARK 500 MET A 192 16.98 55.33
REMARK 500 ALA A 236 53.03 -143.61
REMARK 500 ASP A 337 103.50 -31.13
REMARK 500 ASN A 338 44.27 -104.60
REMARK 500 THR A 347 -66.35 -24.93
REMARK 500 LYS B 51 -48.25 -29.66
REMARK 500 GLU B 52 33.07 -77.22
REMARK 500 ILE B 62 -23.09 -169.16
REMARK 500 ASP B 63 -1.51 -56.40
REMARK 500 SER B 79 69.30 35.21
REMARK 500 LYS B 89 -135.97 -77.04
REMARK 500 ALA B 91 133.39 -17.39
REMARK 500 ASP B 104 -6.03 -47.90
REMARK 500 SER B 112 -76.57 -79.64
REMARK 500 PRO B 129 109.06 -42.29
REMARK 500 VAL B 171 -60.09 -99.57
REMARK 500 LYS B 182 -2.28 74.52
REMARK 500 MET B 192 19.30 55.64
REMARK 500 ALA B 236 56.00 -144.05
REMARK 500 THR B 344 -19.95 102.95
REMARK 500 LEU B 345 -84.10 -3.55
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 A 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE1 112.2
REMARK 620 3 HIS A 276 NE2 97.7 79.5
REMARK 620 4 HOH A 521 O 96.2 151.3 102.3
REMARK 620 5 HOH A 529 O 111.3 88.1 150.9 76.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 106.0
REMARK 620 3 CYS A 306 SG 115.5 115.9
REMARK 620 4 CYS A 308 SG 113.5 90.8 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 B 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE1 110.2
REMARK 620 3 HIS B 276 NE2 93.8 77.4
REMARK 620 4 HOH B 532 O 107.9 141.8 96.9
REMARK 620 5 HOH B 535 O 100.2 93.4 165.2 83.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 107.2
REMARK 620 3 CYS B 306 SG 126.0 112.4
REMARK 620 4 CYS B 308 SG 110.4 83.7 109.1
REMARK 620 N 1 2 3
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 402
DBREF 2GP3 A 2 350 UNP O75164 JHD3A_HUMAN 2 350
DBREF 2GP3 B 2 350 UNP O75164 JHD3A_HUMAN 2 350
SEQRES 1 A 349 ALA SER GLU SER GLU THR LEU ASN PRO SER ALA ARG ILE
SEQRES 2 A 349 MET THR PHE TYR PRO THR MET GLU GLU PHE ARG ASN PHE
SEQRES 3 A 349 SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY ALA HIS
SEQRES 4 A 349 ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP
SEQRES 5 A 349 LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP LEU VAL
SEQRES 6 A 349 ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY GLN SER
SEQRES 7 A 349 GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS ALA MET
SEQRES 8 A 349 THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER ASP LYS
SEQRES 9 A 349 TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU LEU GLU
SEQRES 10 A 349 ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO PRO ILE
SEQRES 11 A 349 TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU LYS HIS
SEQRES 12 A 349 VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR ILE LEU
SEQRES 13 A 349 ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE GLU GLY
SEQRES 14 A 349 VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS THR
SEQRES 15 A 349 SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR SER
SEQRES 16 A 349 ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER TRP TYR
SEQRES 17 A 349 SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU
SEQRES 18 A 349 ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER CYS GLU
SEQRES 19 A 349 ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER PRO LEU
SEQRES 20 A 349 MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS VAL THR
SEQRES 21 A 349 GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO TYR GLY
SEQRES 22 A 349 TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU
SEQRES 23 A 349 SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU TYR GLY
SEQRES 24 A 349 LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP MET VAL
SEQRES 25 A 349 LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE GLN PRO
SEQRES 26 A 349 GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP ASN THR
SEQRES 27 A 349 VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 1 B 349 ALA SER GLU SER GLU THR LEU ASN PRO SER ALA ARG ILE
SEQRES 2 B 349 MET THR PHE TYR PRO THR MET GLU GLU PHE ARG ASN PHE
SEQRES 3 B 349 SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY ALA HIS
SEQRES 4 B 349 ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP
SEQRES 5 B 349 LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP LEU VAL
SEQRES 6 B 349 ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY GLN SER
SEQRES 7 B 349 GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS ALA MET
SEQRES 8 B 349 THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER ASP LYS
SEQRES 9 B 349 TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU LEU GLU
SEQRES 10 B 349 ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO PRO ILE
SEQRES 11 B 349 TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU LYS HIS
SEQRES 12 B 349 VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR ILE LEU
SEQRES 13 B 349 ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE GLU GLY
SEQRES 14 B 349 VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS THR
SEQRES 15 B 349 SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR SER
SEQRES 16 B 349 ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER TRP TYR
SEQRES 17 B 349 SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU
SEQRES 18 B 349 ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER CYS GLU
SEQRES 19 B 349 ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER PRO LEU
SEQRES 20 B 349 MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS VAL THR
SEQRES 21 B 349 GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO TYR GLY
SEQRES 22 B 349 TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU
SEQRES 23 B 349 SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU TYR GLY
SEQRES 24 B 349 LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP MET VAL
SEQRES 25 B 349 LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE GLN PRO
SEQRES 26 B 349 GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP ASN THR
SEQRES 27 B 349 VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
HET ZN A 401 1
HET FE2 A 402 1
HET ZN B 401 1
HET FE2 B 402 1
HETNAM ZN ZINC ION
HETNAM FE2 FE (II) ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 FE2 2(FE 2+)
FORMUL 7 HOH *103(H2 O)
HELIX 1 1 SER A 5 ASN A 9 5 5
HELIX 2 2 THR A 20 ASN A 26 1 7
HELIX 3 3 ASN A 26 GLN A 37 1 12
HELIX 4 4 GLY A 38 ALA A 42 5 5
HELIX 5 5 VAL A 94 SER A 103 1 10
HELIX 6 6 GLU A 113 LEU A 125 1 13
HELIX 7 7 LEU A 157 GLY A 165 1 9
HELIX 8 8 GLU A 190 LEU A 194 5 5
HELIX 9 9 PRO A 212 GLU A 214 5 3
HELIX 10 10 HIS A 215 PHE A 227 1 13
HELIX 11 11 PHE A 227 CYS A 234 1 8
HELIX 12 12 ALA A 236 LYS A 241 5 6
HELIX 13 13 SER A 246 TYR A 253 1 8
HELIX 14 14 ARG A 295 ALA A 303 1 9
HELIX 15 15 MET A 317 GLN A 325 1 9
HELIX 16 16 ARG A 328 ALA A 334 1 7
HELIX 17 17 THR B 20 ASN B 26 1 7
HELIX 18 18 ASN B 26 GLN B 37 1 12
HELIX 19 19 GLY B 38 ALA B 42 5 5
HELIX 20 20 VAL B 94 SER B 103 1 10
HELIX 21 21 GLU B 113 LEU B 125 1 13
HELIX 22 22 LEU B 157 GLY B 165 1 9
HELIX 23 23 GLU B 190 LEU B 194 5 5
HELIX 24 24 PRO B 212 GLU B 214 5 3
HELIX 25 25 HIS B 215 PHE B 227 1 13
HELIX 26 26 PHE B 227 CYS B 234 1 8
HELIX 27 27 ALA B 236 LYS B 241 5 6
HELIX 28 28 SER B 246 TYR B 253 1 8
HELIX 29 29 ARG B 295 ALA B 303 1 9
HELIX 30 30 MET B 317 GLN B 325 1 9
HELIX 31 31 ARG B 328 ALA B 334 1 7
SHEET 1 A10 MET A 15 PHE A 17 0
SHEET 2 A10 LEU A 44 VAL A 47 1 O LYS A 46 N MET A 15
SHEET 3 A10 PHE A 267 THR A 270 -1 O PHE A 267 N VAL A 47
SHEET 4 A10 TYR A 195 GLY A 203 -1 N ASN A 198 O MET A 268
SHEET 5 A10 ASN A 284 PHE A 291 -1 O GLU A 287 N TYR A 199
SHEET 6 A10 TYR A 175 PHE A 178 -1 N TYR A 177 O ALA A 286
SHEET 7 A10 ILE A 131 ASN A 137 -1 N GLY A 133 O PHE A 178
SHEET 8 A10 ILE A 71 GLN A 78 -1 N ILE A 71 O TYR A 132
SHEET 9 A10 LEU A 81 GLN A 88 -1 O TYR A 85 N LEU A 74
SHEET 10 A10 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 B 2 VAL A 66 ILE A 67 0
SHEET 2 B 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 C 4 SER A 184 HIS A 188 0
SHEET 2 C 4 TYR A 275 ASN A 280 -1 O GLY A 278 N PHE A 185
SHEET 3 C 4 LYS A 206 VAL A 211 -1 N TYR A 209 O ALA A 277
SHEET 4 C 4 ASP A 258 GLN A 262 -1 O VAL A 260 N TRP A 208
SHEET 1 D10 MET B 15 PHE B 17 0
SHEET 2 D10 LEU B 44 VAL B 47 1 O LYS B 46 N MET B 15
SHEET 3 D10 PHE B 267 THR B 270 -1 O ILE B 269 N ALA B 45
SHEET 4 D10 TYR B 195 GLY B 203 -1 N SER B 196 O THR B 270
SHEET 5 D10 ASN B 284 PHE B 291 -1 O GLU B 287 N TYR B 199
SHEET 6 D10 TYR B 175 PHE B 178 -1 N TYR B 177 O ALA B 286
SHEET 7 D10 ILE B 131 ASN B 137 -1 N GLY B 133 O PHE B 178
SHEET 8 D10 ILE B 71 GLN B 78 -1 N ILE B 71 O TYR B 132
SHEET 9 D10 LEU B 81 GLN B 88 -1 O TYR B 85 N LEU B 74
SHEET 10 D10 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 E 2 VAL B 66 ILE B 67 0
SHEET 2 E 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 F 4 SER B 184 HIS B 188 0
SHEET 2 F 4 TYR B 275 ASN B 280 -1 O GLY B 278 N PHE B 185
SHEET 3 F 4 LYS B 206 VAL B 211 -1 N TYR B 209 O ALA B 277
SHEET 4 F 4 ASP B 258 GLN B 262 -1 O VAL B 260 N TRP B 208
LINK NE2 HIS A 188 FE FE2 A 402 1555 1555 2.24
LINK OE1 GLU A 190 FE FE2 A 402 1555 1555 2.09
LINK SG CYS A 234 ZN ZN A 401 1555 1555 2.34
LINK NE2 HIS A 240 ZN ZN A 401 1555 1555 2.09
LINK NE2 HIS A 276 FE FE2 A 402 1555 1555 2.15
LINK SG CYS A 306 ZN ZN A 401 1555 1555 2.18
LINK SG CYS A 308 ZN ZN A 401 1555 1555 2.38
LINK FE FE2 A 402 O HOH A 521 1555 1555 2.49
LINK FE FE2 A 402 O HOH A 529 1555 1555 2.67
LINK NE2 HIS B 188 FE FE2 B 402 1555 1555 2.20
LINK OE1 GLU B 190 FE FE2 B 402 1555 1555 2.13
LINK SG CYS B 234 ZN ZN B 401 1555 1555 2.22
LINK NE2 HIS B 240 ZN ZN B 401 1555 1555 2.22
LINK NE2 HIS B 276 FE FE2 B 402 1555 1555 2.26
LINK SG CYS B 306 ZN ZN B 401 1555 1555 2.26
LINK SG CYS B 308 ZN ZN B 401 1555 1555 2.43
LINK FE FE2 B 402 O HOH B 532 1555 1555 2.34
LINK FE FE2 B 402 O HOH B 535 1555 1555 2.47
SITE 1 AC1 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC2 5 HIS A 188 GLU A 190 HIS A 276 HOH A 521
SITE 2 AC2 5 HOH A 529
SITE 1 AC3 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC4 5 HIS B 188 GLU B 190 HIS B 276 HOH B 532
SITE 2 AC4 5 HOH B 535
CRYST1 100.867 149.540 56.815 90.00 90.00 90.00 P 21 21 2 8
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 0.009914 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006687 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017601 0.00000
(ATOM LINES ARE NOT SHOWN.)
END