LinkDB: 3D24
Original site: 3D24
Gene (2) KEGG GENES (2) Protein sequence (8) UniProt (2) SWISS-PROT (2) PDBSTR (4) DNA sequence (2) EMBL (2) Protein domain (5) InterPro (4) PROSITE (1) Literature (1) PubMed (1) All databases (18)
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HEADER TRANSCRIPTION 07-MAY-08 3D24
TITLE CRYSTAL STRUCTURE OF LIGAND-BINDING DOMAIN OF ESTROGEN-RELATED
TITLE 2 RECEPTOR ALPHA (ERRALPHA) IN COMPLEX WITH THE PEROXISOME
TITLE 3 PROLIFERATORS-ACTIVATED RECEPTOR COACTIVATOR-1ALPHA BOX3 PEPTIDE
TITLE 4 (PGC-1ALPHA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROID HORMONE RECEPTOR ERR1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN: RESIDUES 278-519;
COMPND 5 SYNONYM: ESTROGEN-RELATED RECEPTOR ALPHA, ERR-ALPHA, ESTROGEN
COMPND 6 RECEPTOR-LIKE 1, NUCLEAR RECEPTOR SUBFAMILY 3 GROUP B MEMBER 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
COMPND 10 COACTIVATOR 1-ALPHA;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: RESIDUES 198-219;
COMPND 13 SYNONYM: PPAR-GAMMA COACTIVATOR 1-ALPHA, PPARGC-1-ALPHA, PGC-1-ALPHA,
COMPND 14 LIGAND EFFECT MODULATOR 6;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: ESRRA, ERR1, ESRL1, NR3B1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: SYNTHETIC PEPTIDE WITH THE SEQUENCE BASED ON THE
SOURCE 12 FRAGMENT (RESIDUES 198-219) OF HUMAN PGC-1-ALPHA, UNIPROT ENTRY
SOURCE 13 Q9UBK2 (PRGC1_HUMAN)
KEYWDS NUCLEAR RECEPTOR, LIGAND BINDING DOMAIN, COACTIVATOR, DNA-BINDING,
KEYWDS 2 METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 3 REGULATION, ZINC, ZINC-FINGER, POLYMORPHISM, RNA-BINDING, STRUCTURAL
KEYWDS 4 GENOMICS, STRUCTURAL PROTEOMICS IN EUROPE, SPINE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MORAS,H.GRESCHIK,R.FLAIG,Y.SATO,N.ROCHEL,STRUCTURAL PROTEOMICS IN
AUTHOR 2 EUROPE (SPINE)
REVDAT 4 30-AUG-23 3D24 1 SEQADV
REVDAT 3 24-FEB-09 3D24 1 VERSN
REVDAT 2 29-JUL-08 3D24 1 JRNL
REVDAT 1 10-JUN-08 3D24 0
JRNL AUTH H.GRESCHIK,M.ALTHAGE,R.FLAIG,Y.SATO,V.CHAVANT,
JRNL AUTH 2 C.PELUSO-ILTIS,L.CHOULIER,P.CRONET,N.ROCHEL,R.SCHULE,
JRNL AUTH 3 P.E.STROMSTEDT,D.MORAS
JRNL TITL COMMUNICATION BETWEEN THE ERR{ALPHA} HOMODIMER INTERFACE AND
JRNL TITL 2 THE PGC-1{ALPHA} BINDING SURFACE VIA THE HELIX 8-9 LOOP.
JRNL REF J.BIOL.CHEM. V. 283 20220 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18441008
JRNL DOI 10.1074/JBC.M801920200
REMARK 2
REMARK 2 RESOLUTION. 2.11 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
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) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 31872
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) : 0.212
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1584
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 : 3518
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.94500
REMARK 3 B22 (A**2) : 2.11900
REMARK 3 B33 (A**2) : 3.82600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.79700
REMARK 3 B23 (A**2) : 0.00000
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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: THE BIJVOET DIFFERENCES WERE USED IN
REMARK 3 PHASING
REMARK 4
REMARK 4 3D24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047495.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : TOROIDAL ZERODUR MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109542
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.23800
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1XB7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 15% PEG 3350,
REMARK 280 0.2 M MG(NO3)2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 59.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.00000
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, 3
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL ASSEMBLY IS A HOMODIMER.
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.3 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 171
REMARK 465 ARG A 172
REMARK 465 SER A 173
REMARK 465 HIS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 HIS A 177
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 GLY A 180
REMARK 465 PRO A 181
REMARK 465 GLY A 182
REMARK 465 LEU A 183
REMARK 465 VAL A 184
REMARK 465 PRO A 185
REMARK 465 ARG A 186
REMARK 465 GLY A 187
REMARK 465 SER A 188
REMARK 465 LYS A 189
REMARK 465 THR A 190
REMARK 465 ALA A 191
REMARK 465 ALA A 192
REMARK 465 PRO A 193
REMARK 465 PRO A 213
REMARK 465 ASP A 214
REMARK 465 PRO A 215
REMARK 465 ALA A 216
REMARK 465 GLY A 217
REMARK 465 PRO A 218
REMARK 465 ASP A 219
REMARK 465 GLY A 220
REMARK 465 HIS A 221
REMARK 465 LEU A 222
REMARK 465 ARG A 366
REMARK 465 ALA A 367
REMARK 465 GLY A 368
REMARK 465 PRO A 369
REMARK 465 GLY A 370
REMARK 465 GLY A 371
REMARK 465 GLY A 372
REMARK 465 ALA A 373
REMARK 465 MET A 421
REMARK 465 MET A 422
REMARK 465 ASP A 423
REMARK 465 GLN B 198
REMARK 465 GLN B 199
REMARK 465 GLN B 200
REMARK 465 LYS B 201
REMARK 465 PRO B 202
REMARK 465 GLN B 203
REMARK 465 ARG B 204
REMARK 465 ASP B 218
REMARK 465 ASP B 219
REMARK 465 MET C 171
REMARK 465 ARG C 172
REMARK 465 SER C 173
REMARK 465 HIS C 174
REMARK 465 HIS C 175
REMARK 465 HIS C 176
REMARK 465 HIS C 177
REMARK 465 HIS C 178
REMARK 465 HIS C 179
REMARK 465 GLY C 180
REMARK 465 PRO C 181
REMARK 465 GLY C 182
REMARK 465 LEU C 183
REMARK 465 VAL C 184
REMARK 465 PRO C 185
REMARK 465 ARG C 186
REMARK 465 GLY C 187
REMARK 465 SER C 188
REMARK 465 LYS C 189
REMARK 465 THR C 190
REMARK 465 ALA C 191
REMARK 465 ASP C 214
REMARK 465 PRO C 215
REMARK 465 ALA C 216
REMARK 465 GLY C 217
REMARK 465 PRO C 218
REMARK 465 ASP C 219
REMARK 465 GLY C 220
REMARK 465 HIS C 221
REMARK 465 LEU C 222
REMARK 465 GLY C 368
REMARK 465 PRO C 369
REMARK 465 GLY C 370
REMARK 465 GLY C 371
REMARK 465 GLY C 372
REMARK 465 ALA C 373
REMARK 465 GLU C 374
REMARK 465 GLN D 198
REMARK 465 GLN D 199
REMARK 465 GLN D 200
REMARK 465 LYS D 201
REMARK 465 PRO D 202
REMARK 465 GLN D 203
REMARK 465 ARG D 204
REMARK 465 ASP D 219
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 ALA C 192 CB
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 O HOH C 529 O HOH C 529 2657 2.01
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 PRO A 206 159.07 -48.04
REMARK 500 ALA A 224 -70.42 -111.18
REMARK 500 ALA A 300 3.03 -66.50
REMARK 500 ASP A 344 72.46 -101.15
REMARK 500 ALA A 364 5.09 -63.40
REMARK 500 HIS A 411 172.42 -53.84
REMARK 500 PRO B 206 99.64 -64.17
REMARK 500 CYS B 207 24.29 -157.83
REMARK 500 THR B 215 52.49 -114.49
REMARK 500 THR B 216 -157.56 -141.98
REMARK 500 PRO C 193 -179.21 -59.83
REMARK 500 VAL C 194 -1.75 -141.68
REMARK 500 MET C 212 -117.49 -119.05
REMARK 500 ALA C 224 -91.63 -37.63
REMARK 500 LEU C 290 86.46 -156.60
REMARK 500 CYS D 207 18.28 -146.81
REMARK 500 ASN D 217 66.77 -63.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IGBMC-0062-000 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 1XB7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ERRALPHA LBD IN COMPLEX WITH A PGC-1ALPHA
REMARK 900 PEPTIDE AT 2.5 A RESOLUTION
DBREF 3D24 A 192 423 UNP P11474 ERR1_HUMAN 288 519
DBREF 3D24 B 198 219 UNP Q9UBK2 PRGC1_HUMAN 198 219
DBREF 3D24 C 192 423 UNP P11474 ERR1_HUMAN 288 519
DBREF 3D24 D 198 219 UNP Q9UBK2 PRGC1_HUMAN 198 219
SEQADV 3D24 MET A 171 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ARG A 172 UNP P11474 EXPRESSION TAG
SEQADV 3D24 SER A 173 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 174 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 175 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 176 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 177 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 178 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS A 179 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY A 180 UNP P11474 EXPRESSION TAG
SEQADV 3D24 PRO A 181 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY A 182 UNP P11474 EXPRESSION TAG
SEQADV 3D24 LEU A 183 UNP P11474 EXPRESSION TAG
SEQADV 3D24 VAL A 184 UNP P11474 EXPRESSION TAG
SEQADV 3D24 PRO A 185 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ARG A 186 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY A 187 UNP P11474 EXPRESSION TAG
SEQADV 3D24 SER A 188 UNP P11474 EXPRESSION TAG
SEQADV 3D24 LYS A 189 UNP P11474 EXPRESSION TAG
SEQADV 3D24 THR A 190 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ALA A 191 UNP P11474 EXPRESSION TAG
SEQADV 3D24 MET C 171 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ARG C 172 UNP P11474 EXPRESSION TAG
SEQADV 3D24 SER C 173 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 174 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 175 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 176 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 177 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 178 UNP P11474 EXPRESSION TAG
SEQADV 3D24 HIS C 179 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY C 180 UNP P11474 EXPRESSION TAG
SEQADV 3D24 PRO C 181 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY C 182 UNP P11474 EXPRESSION TAG
SEQADV 3D24 LEU C 183 UNP P11474 EXPRESSION TAG
SEQADV 3D24 VAL C 184 UNP P11474 EXPRESSION TAG
SEQADV 3D24 PRO C 185 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ARG C 186 UNP P11474 EXPRESSION TAG
SEQADV 3D24 GLY C 187 UNP P11474 EXPRESSION TAG
SEQADV 3D24 SER C 188 UNP P11474 EXPRESSION TAG
SEQADV 3D24 LYS C 189 UNP P11474 EXPRESSION TAG
SEQADV 3D24 THR C 190 UNP P11474 EXPRESSION TAG
SEQADV 3D24 ALA C 191 UNP P11474 EXPRESSION TAG
SEQRES 1 A 253 MET ARG SER HIS HIS HIS HIS HIS HIS GLY PRO GLY LEU
SEQRES 2 A 253 VAL PRO ARG GLY SER LYS THR ALA ALA PRO VAL ASN ALA
SEQRES 3 A 253 LEU VAL SER HIS LEU LEU VAL VAL GLU PRO GLU LYS LEU
SEQRES 4 A 253 TYR ALA MET PRO ASP PRO ALA GLY PRO ASP GLY HIS LEU
SEQRES 5 A 253 PRO ALA VAL ALA THR LEU CYS ASP LEU PHE ASP ARG GLU
SEQRES 6 A 253 ILE VAL VAL THR ILE SER TRP ALA LYS SER ILE PRO GLY
SEQRES 7 A 253 PHE SER SER LEU SER LEU SER ASP GLN MET SER VAL LEU
SEQRES 8 A 253 GLN SER VAL TRP MET GLU VAL LEU VAL LEU GLY VAL ALA
SEQRES 9 A 253 GLN ARG SER LEU PRO LEU GLN ASP GLU LEU ALA PHE ALA
SEQRES 10 A 253 GLU ASP LEU VAL LEU ASP GLU GLU GLY ALA ARG ALA ALA
SEQRES 11 A 253 GLY LEU GLY GLU LEU GLY ALA ALA LEU LEU GLN LEU VAL
SEQRES 12 A 253 ARG ARG LEU GLN ALA LEU ARG LEU GLU ARG GLU GLU TYR
SEQRES 13 A 253 VAL LEU LEU LYS ALA LEU ALA LEU ALA ASN SER ASP SER
SEQRES 14 A 253 VAL HIS ILE GLU ASP ALA GLU ALA VAL GLU GLN LEU ARG
SEQRES 15 A 253 GLU ALA LEU HIS GLU ALA LEU LEU GLU TYR GLU ALA GLY
SEQRES 16 A 253 ARG ALA GLY PRO GLY GLY GLY ALA GLU ARG ARG ARG ALA
SEQRES 17 A 253 GLY ARG LEU LEU LEU THR LEU PRO LEU LEU ARG GLN THR
SEQRES 18 A 253 ALA GLY LYS VAL LEU ALA HIS PHE TYR GLY VAL LYS LEU
SEQRES 19 A 253 GLU GLY LYS VAL PRO MET HIS LYS LEU PHE LEU GLU MET
SEQRES 20 A 253 LEU GLU ALA MET MET ASP
SEQRES 1 B 22 GLN GLN GLN LYS PRO GLN ARG ARG PRO CYS SER GLU LEU
SEQRES 2 B 22 LEU LYS TYR LEU THR THR ASN ASP ASP
SEQRES 1 C 253 MET ARG SER HIS HIS HIS HIS HIS HIS GLY PRO GLY LEU
SEQRES 2 C 253 VAL PRO ARG GLY SER LYS THR ALA ALA PRO VAL ASN ALA
SEQRES 3 C 253 LEU VAL SER HIS LEU LEU VAL VAL GLU PRO GLU LYS LEU
SEQRES 4 C 253 TYR ALA MET PRO ASP PRO ALA GLY PRO ASP GLY HIS LEU
SEQRES 5 C 253 PRO ALA VAL ALA THR LEU CYS ASP LEU PHE ASP ARG GLU
SEQRES 6 C 253 ILE VAL VAL THR ILE SER TRP ALA LYS SER ILE PRO GLY
SEQRES 7 C 253 PHE SER SER LEU SER LEU SER ASP GLN MET SER VAL LEU
SEQRES 8 C 253 GLN SER VAL TRP MET GLU VAL LEU VAL LEU GLY VAL ALA
SEQRES 9 C 253 GLN ARG SER LEU PRO LEU GLN ASP GLU LEU ALA PHE ALA
SEQRES 10 C 253 GLU ASP LEU VAL LEU ASP GLU GLU GLY ALA ARG ALA ALA
SEQRES 11 C 253 GLY LEU GLY GLU LEU GLY ALA ALA LEU LEU GLN LEU VAL
SEQRES 12 C 253 ARG ARG LEU GLN ALA LEU ARG LEU GLU ARG GLU GLU TYR
SEQRES 13 C 253 VAL LEU LEU LYS ALA LEU ALA LEU ALA ASN SER ASP SER
SEQRES 14 C 253 VAL HIS ILE GLU ASP ALA GLU ALA VAL GLU GLN LEU ARG
SEQRES 15 C 253 GLU ALA LEU HIS GLU ALA LEU LEU GLU TYR GLU ALA GLY
SEQRES 16 C 253 ARG ALA GLY PRO GLY GLY GLY ALA GLU ARG ARG ARG ALA
SEQRES 17 C 253 GLY ARG LEU LEU LEU THR LEU PRO LEU LEU ARG GLN THR
SEQRES 18 C 253 ALA GLY LYS VAL LEU ALA HIS PHE TYR GLY VAL LYS LEU
SEQRES 19 C 253 GLU GLY LYS VAL PRO MET HIS LYS LEU PHE LEU GLU MET
SEQRES 20 C 253 LEU GLU ALA MET MET ASP
SEQRES 1 D 22 GLN GLN GLN LYS PRO GLN ARG ARG PRO CYS SER GLU LEU
SEQRES 2 D 22 LEU LYS TYR LEU THR THR ASN ASP ASP
FORMUL 5 HOH *272(H2 O)
HELIX 1 1 ASN A 195 VAL A 204 1 10
HELIX 2 2 ALA A 224 ILE A 246 1 23
HELIX 3 3 SER A 253 LEU A 278 1 26
HELIX 4 4 GLU A 294 ALA A 300 1 7
HELIX 5 5 GLU A 304 ALA A 318 1 15
HELIX 6 6 GLU A 322 ASN A 336 1 15
HELIX 7 7 ASP A 344 ALA A 364 1 21
HELIX 8 8 GLU A 374 LEU A 383 1 10
HELIX 9 9 THR A 384 GLU A 405 1 22
HELIX 10 10 HIS A 411 ALA A 420 1 10
HELIX 11 11 CYS B 207 THR B 215 1 9
HELIX 12 12 ASN C 195 VAL C 204 1 10
HELIX 13 13 PRO C 223 SER C 245 1 23
HELIX 14 14 SER C 253 LEU C 278 1 26
HELIX 15 15 GLU C 294 GLY C 301 1 8
HELIX 16 16 GLU C 304 ARG C 320 1 17
HELIX 17 17 GLU C 322 ASN C 336 1 15
HELIX 18 18 ASP C 344 ALA C 364 1 21
HELIX 19 19 ARG C 376 LEU C 383 1 8
HELIX 20 20 THR C 384 GLU C 405 1 22
HELIX 21 21 HIS C 411 MET C 421 1 11
HELIX 22 22 CYS D 207 THR D 215 1 9
SHEET 1 A 2 GLU A 283 ALA A 287 0
SHEET 2 A 2 LEU A 290 ASP A 293 -1 O LEU A 290 N ALA A 287
SHEET 1 B 2 GLU C 283 ALA C 287 0
SHEET 2 B 2 LEU C 290 ASP C 293 -1 O LEU C 292 N LEU C 284
CISPEP 1 MET C 212 PRO C 213 0 -0.20
CRYST1 119.400 56.000 96.200 90.00 106.40 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 0.008375 0.000000 0.002465 0.00000
SCALE2 0.000000 0.017857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END