HEADER TRANSCRIPTION/DNA 21-FEB-08 3CBB
TITLE CRYSTAL STRUCTURE OF HEPATOCYTE NUCLEAR FACTOR 4ALPHA IN COMPLEX WITH
TITLE 2 DNA: DIABETES GENE PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA PROMOTER ELEMENT DNA;
COMPND 3 CHAIN: C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA PROMOTER ELEMENT DNA;
COMPND 7 CHAIN: D;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA, DNA BINDING DOMAIN;
COMPND 11 CHAIN: A, B;
COMPND 12 FRAGMENT: DNA BINDING DOMAIN;
COMPND 13 SYNONYM: HNF-4-ALPHA; TRANSCRIPTION FACTOR HNF-4; NUCLEAR RECEPTOR
COMPND 14 SUBFAMILY 2 GROUP A MEMBER 1; TRANSCRIPTION FACTOR 14;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: HNF4A, HNF4, NR2A1, TCF14;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET41A
KEYWDS ZINC FINGER, PROTEIN-DNA COMPLEX, DIABETES, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.LU,G.B.RHA,M.MELIKISHVILI,B.C.ADKINS,M.G.FRIED,Y.I.CHI
REVDAT 5 21-FEB-24 3CBB 1 REMARK
REVDAT 4 25-OCT-17 3CBB 1 REMARK
REVDAT 3 22-DEC-09 3CBB 1 JRNL
REVDAT 2 24-FEB-09 3CBB 1 VERSN
REVDAT 1 07-OCT-08 3CBB 0
JRNL AUTH P.LU,G.B.RHA,M.MELIKISHVILI,G.WU,B.C.ADKINS,M.G.FRIED,
JRNL AUTH 2 Y.I.CHI
JRNL TITL STRUCTURAL BASIS OF NATURAL PROMOTER RECOGNITION BY A UNIQUE
JRNL TITL 2 NUCLEAR RECEPTOR, HNF4ALPHA. DIABETES GENE PRODUCT.
JRNL REF J.BIOL.CHEM. V. 283 33685 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18829458
JRNL DOI 10.1074/JBC.M806213200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.LU,J.LIU,M.MELIKISHVILI,M.G.FRIED,Y.-I.CHI
REMARK 1 TITL CRYSTALLIZATION OF HEPATOCYTE NUCLEAR FACTOR 4ALPHA
REMARK 1 TITL 2 (HNF4ALPHA) IN COMPLEX WITH THE HNF1ALPHA PROMOTER ELEMENT
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 16841
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 811
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 1230
REMARK 3 NUCLEIC ACID ATOMS : 855
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 157
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.17
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.031
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.150
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 3CBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92017
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200 HIGH-RESOLUTION DOUBLE-CRYSTAL
REMARK 200 SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17094
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30400
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 4000, 80MM MAGNESIUM ACETATE,
REMARK 280 50MM SODIUM CITRATE, PH 4.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 60.81400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.71250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.81400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 17.71250
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 ARG A 125
REMARK 465 ASP A 126
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 NE ARG A 76 O HOH A 1020 2.18
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 TYR A 85 -170.69 64.25
REMARK 500 PHE A 89 -128.05 -116.74
REMARK 500 GLN A 92 44.27 -142.50
REMARK 500 TYR B 63 18.64 56.12
REMARK 500 PHE B 89 -135.02 -94.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DG C 5 0.07 SIDE CHAIN
REMARK 500 DG C 12 0.08 SIDE CHAIN
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 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 CYS A 54 SG 111.7
REMARK 620 3 CYS A 68 SG 113.6 103.3
REMARK 620 4 CYS A 71 SG 110.3 112.7 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 87 SG
REMARK 620 2 CYS A 93 SG 97.7
REMARK 620 3 CYS A 103 SG 116.3 116.0
REMARK 620 4 CYS A 106 SG 116.2 100.8 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 51 SG
REMARK 620 2 CYS B 54 SG 110.3
REMARK 620 3 CYS B 68 SG 114.5 107.2
REMARK 620 4 CYS B 71 SG 107.2 112.7 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 87 SG
REMARK 620 2 CYS B 93 SG 103.2
REMARK 620 3 CYS B 103 SG 107.4 115.8
REMARK 620 4 CYS B 106 SG 113.3 108.0 109.2
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2002
DBREF 3CBB A 49 126 UNP P41235 HNF4A_HUMAN 58 135
DBREF 3CBB B 49 126 UNP P41235 HNF4A_HUMAN 58 135
DBREF 3CBB C 1 21 PDB 3CBB 3CBB 1 21
DBREF 3CBB D 1 21 PDB 3CBB 3CBB 1 21
SEQRES 1 C 21 DT DG DA DA DG DT DC DC DA DA DA DG DT
SEQRES 2 C 21 DT DC DA DG DT DC DC DC
SEQRES 1 D 21 DA DG DG DG DA DC DT DG DA DA DC DT DT
SEQRES 2 D 21 DT DG DG DA DC DT DT DC
SEQRES 1 A 78 ALA LEU CYS ALA ILE CYS GLY ASP ARG ALA THR GLY LYS
SEQRES 2 A 78 HIS TYR GLY ALA SER SER CYS ASP GLY CYS LYS GLY PHE
SEQRES 3 A 78 PHE ARG ARG SER VAL ARG LYS ASN HIS MET TYR SER CYS
SEQRES 4 A 78 ARG PHE SER ARG GLN CYS VAL VAL ASP LYS ASP LYS ARG
SEQRES 5 A 78 ASN GLN CYS ARG TYR CYS ARG LEU LYS LYS CYS PHE ARG
SEQRES 6 A 78 ALA GLY MET LYS LYS GLU ALA VAL GLN ASN GLU ARG ASP
SEQRES 1 B 78 ALA LEU CYS ALA ILE CYS GLY ASP ARG ALA THR GLY LYS
SEQRES 2 B 78 HIS TYR GLY ALA SER SER CYS ASP GLY CYS LYS GLY PHE
SEQRES 3 B 78 PHE ARG ARG SER VAL ARG LYS ASN HIS MET TYR SER CYS
SEQRES 4 B 78 ARG PHE SER ARG GLN CYS VAL VAL ASP LYS ASP LYS ARG
SEQRES 5 B 78 ASN GLN CYS ARG TYR CYS ARG LEU LYS LYS CYS PHE ARG
SEQRES 6 B 78 ALA GLY MET LYS LYS GLU ALA VAL GLN ASN GLU ARG ASP
HET ZN A1001 1
HET ZN A1002 1
HET ZN B2001 1
HET ZN B2002 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 HOH *157(H2 O)
HELIX 1 1 CYS A 68 LYS A 81 1 14
HELIX 2 2 CYS A 103 GLY A 115 1 13
HELIX 3 3 LYS A 117 VAL A 121 5 5
HELIX 4 4 CYS B 68 LYS B 81 1 14
HELIX 5 5 CYS B 103 ALA B 114 1 12
HELIX 6 6 LYS B 117 VAL B 121 5 5
SHEET 1 A 2 LYS A 61 HIS A 62 0
SHEET 2 A 2 ALA A 65 SER A 66 -1 O ALA A 65 N HIS A 62
SHEET 1 B 2 LYS B 61 HIS B 62 0
SHEET 2 B 2 ALA B 65 SER B 66 -1 O ALA B 65 N HIS B 62
LINK SG CYS A 51 ZN ZN A1001 1555 1555 2.46
LINK SG CYS A 54 ZN ZN A1001 1555 1555 2.34
LINK SG CYS A 68 ZN ZN A1001 1555 1555 2.38
LINK SG CYS A 71 ZN ZN A1001 1555 1555 2.34
LINK SG CYS A 87 ZN ZN A1002 1555 1555 2.49
LINK SG CYS A 93 ZN ZN A1002 1555 1555 2.49
LINK SG CYS A 103 ZN ZN A1002 1555 1555 2.44
LINK SG CYS A 106 ZN ZN A1002 1555 1555 2.49
LINK SG CYS B 51 ZN ZN B2001 1555 1555 2.41
LINK SG CYS B 54 ZN ZN B2001 1555 1555 2.36
LINK SG CYS B 68 ZN ZN B2001 1555 1555 2.41
LINK SG CYS B 71 ZN ZN B2001 1555 1555 2.40
LINK SG CYS B 87 ZN ZN B2002 1555 1555 2.51
LINK SG CYS B 93 ZN ZN B2002 1555 1555 2.43
LINK SG CYS B 103 ZN ZN B2002 1555 1555 2.38
LINK SG CYS B 106 ZN ZN B2002 1555 1555 2.42
SITE 1 AC1 4 CYS A 51 CYS A 54 CYS A 68 CYS A 71
SITE 1 AC2 4 CYS A 87 CYS A 93 CYS A 103 CYS A 106
SITE 1 AC3 4 CYS B 51 CYS B 54 CYS B 68 CYS B 71
SITE 1 AC4 4 CYS B 87 CYS B 93 CYS B 103 CYS B 106
CRYST1 121.628 35.425 70.985 90.00 119.36 90.00 C 1 2 1 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 0.008222 0.000000 0.004625 0.00000
SCALE2 0.000000 0.028229 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016164 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
