HEADER TRANSCRIPTION 08-JAN-09 3FS1
TITLE CRYSTAL STRUCTURE OF HNF4A LBD IN COMPLEX WITH THE LIGAND AND THE
TITLE 2 COACTIVATOR PGC-1A FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HNF4A LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: HNF-4-ALPHA, TRANSCRIPTION FACTOR HNF-4, NUCLEAR RECEPTOR
COMPND 6 SUBFAMILY 2 GROUP A MEMBER 1, TRANSCRIPTION FACTOR 14;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PPARGAMMA COACTIVATOR-1A (PGC-1A);
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: PGC-1A LXXLL MOTIFS;
COMPND 12 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: HNF4, HNF4A, NR2A1, TCF14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: PGC-1A;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX
KEYWDS NUCLEAR RECEPTOR, COACTIVATOR, LXXLL MOTIF, MODY, DIABETES,
KEYWDS 2 ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, DIABETES MELLITUS,
KEYWDS 3 DISEASE MUTATION, DNA-BINDING, METAL-BINDING, NUCLEUS,
KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, RECEPTOR, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 5 REGULATION, ZINC, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR G.RHA,G.WU,Y.CHI
REVDAT 4 06-SEP-23 3FS1 1 REMARK
REVDAT 3 01-NOV-17 3FS1 1 REMARK
REVDAT 2 22-DEC-09 3FS1 1 JRNL
REVDAT 1 27-OCT-09 3FS1 0
JRNL AUTH G.B.RHA,G.WU,S.E.SHOELSON,Y.I.CHI
JRNL TITL MULTIPLE BINDING MODES BETWEEN HNF4ALPHA AND THE LXXLL
JRNL TITL 2 MOTIFS OF PGC-1ALPHA LEAD TO FULL ACTIVATION
JRNL REF J.BIOL.CHEM. V. 284 35165 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19846556
JRNL DOI 10.1074/JBC.M109.052506
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 18017
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 + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 922
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1880
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.43000
REMARK 3 B22 (A**2) : 2.43000
REMARK 3 B33 (A**2) : -4.86000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000050970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-08
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18995
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.4000
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) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
REMARK 200 R SYM FOR SHELL (I) : 0.34900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.560
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: PDB ENTRY 1PZL (WITHOUT THE LIGAND AND THE
REMARK 200 PEPTIDE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 2 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 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z+1/2
REMARK 290 8555 -Y,-X,-Z+1/2
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 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 28.66100
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 28.66100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.66100
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 28.66100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 CE3 TRP A 340 CE3 TRP A 340 5655 1.94
REMARK 500 CE3 TRP A 340 CZ3 TRP A 340 5655 2.08
REMARK 500
REMARK 500 REMARK: NULL
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 180 CD GLU A 180 OE1 0.069
REMARK 500 GLU A 180 CD GLU A 180 OE2 0.069
REMARK 500 GLU A 184 CD GLU A 184 OE2 0.068
REMARK 500 ARG A 226 CD ARG A 226 NE -0.124
REMARK 500 GLU A 251 CB GLU A 251 CG -0.340
REMARK 500 ARG A 258 CD ARG A 258 NE -0.165
REMARK 500 GLN A 336 CG GLN A 336 CD 0.151
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 ASP A 166 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 177 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 226 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 GLU A 251 CA - CB - CG ANGL. DEV. = 23.4 DEGREES
REMARK 500 GLU A 251 CB - CG - CD ANGL. DEV. = -23.9 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 273 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 274 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 287 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 295 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 303 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 303 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU A 310 CB - CG - CD2 ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP A 320 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 340 CA - CB - CG ANGL. DEV. = -11.9 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 ARG A 154 27.00 -78.93
REMARK 500 HIS A 214 33.69 -143.95
REMARK 500 ASP A 239 2.65 83.04
REMARK 500 ALA A 250 -132.30 46.15
REMARK 500 TYR A 319 -80.15 -104.33
REMARK 500 SER A 321 -38.93 -141.90
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 ARG A 226 0.07 SIDE CHAIN
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 MYR A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HNF4A LBD IN COMPLEX WITH THE LIGAND AND THE
REMARK 900 COACTIVATOR SRC-1 PEPTIDE
DBREF 3FS1 A 139 368 UNP P41235 HNF4A_HUMAN 148 377
DBREF 3FS1 B 8 16 PDB 3FS1 3FS1 8 16
SEQRES 1 A 230 SER LEU PRO SER ILE ASN ALA LEU LEU GLN ALA GLU VAL
SEQRES 2 A 230 LEU SER ARG GLN ILE THR SER PRO VAL SER GLY ILE ASN
SEQRES 3 A 230 GLY ASP ILE ARG ALA LYS LYS ILE ALA SER ILE ALA ASP
SEQRES 4 A 230 VAL CYS GLU SER MET LYS GLU GLN LEU LEU VAL LEU VAL
SEQRES 5 A 230 GLU TRP ALA LYS TYR ILE PRO ALA PHE CYS GLU LEU PRO
SEQRES 6 A 230 LEU ASP ASP GLN VAL ALA LEU LEU ARG ALA HIS ALA GLY
SEQRES 7 A 230 GLU HIS LEU LEU LEU GLY ALA THR LYS ARG SER MET VAL
SEQRES 8 A 230 PHE LYS ASP VAL LEU LEU LEU GLY ASN ASP TYR ILE VAL
SEQRES 9 A 230 PRO ARG HIS CYS PRO GLU LEU ALA GLU MET SER ARG VAL
SEQRES 10 A 230 SER ILE ARG ILE LEU ASP GLU LEU VAL LEU PRO PHE GLN
SEQRES 11 A 230 GLU LEU GLN ILE ASP ASP ASN GLU TYR ALA TYR LEU LYS
SEQRES 12 A 230 ALA ILE ILE PHE PHE ASP PRO ASP ALA LYS GLY LEU SER
SEQRES 13 A 230 ASP PRO GLY LYS ILE LYS ARG LEU ARG SER GLN VAL GLN
SEQRES 14 A 230 VAL SER LEU GLU ASP TYR ILE ASN ASP ARG GLN TYR ASP
SEQRES 15 A 230 SER ARG GLY ARG PHE GLY GLU LEU LEU LEU LEU LEU PRO
SEQRES 16 A 230 THR LEU GLN SER ILE THR TRP GLN MET ILE GLU GLN ILE
SEQRES 17 A 230 GLN PHE ILE LYS LEU PHE GLY MET ALA LYS ILE ASP ASN
SEQRES 18 A 230 LEU LEU GLN GLU MET LEU LEU GLY GLY
SEQRES 1 B 9 ALA ALA LEU ALA ALA LEU LEU ALA ALA
HET MYR A 500 16
HETNAM MYR MYRISTIC ACID
FORMUL 3 MYR C14 H28 O2
FORMUL 4 HOH *77(H2 O)
HELIX 1 1 SER A 142 ARG A 154 1 13
HELIX 2 2 ASP A 166 LYS A 170 5 5
HELIX 3 3 SER A 174 TYR A 195 1 22
HELIX 4 4 ILE A 196 GLU A 201 1 6
HELIX 5 5 PRO A 203 HIS A 214 1 12
HELIX 6 6 HIS A 214 MET A 228 1 15
HELIX 7 7 CYS A 246 GLU A 251 5 6
HELIX 8 8 MET A 252 LEU A 263 1 12
HELIX 9 9 LEU A 263 GLN A 271 1 9
HELIX 10 10 ASP A 273 PHE A 286 1 14
HELIX 11 11 ASP A 295 ASP A 316 1 22
HELIX 12 12 GLY A 323 LEU A 330 1 8
HELIX 13 13 LEU A 331 PHE A 352 1 22
HELIX 14 14 ASP A 358 LEU A 366 1 9
SHEET 1 A 2 VAL A 233 LEU A 235 0
SHEET 2 A 2 ILE A 241 PRO A 243 -1 O VAL A 242 N LEU A 234
SITE 1 AC1 9 HOH A 21 SER A 181 GLN A 185 ALA A 223
SITE 2 AC1 9 ARG A 226 LEU A 236 GLY A 237 MET A 252
SITE 3 AC1 9 ILE A 346
CRYST1 113.049 113.049 57.322 90.00 90.00 90.00 P 42 2 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 0.008846 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
