HEADER TRANSCRIPTION 16-APR-07 2PJL
TITLE CRYSTAL STRUCTURE OF HUMAN ESTROGEN-RELATED RECEPTOR ALPHA IN COMPLEX
TITLE 2 WITH A SYNTHETIC INVERSE AGONIST REVEALS ITS NOVEL MOLECULAR
TITLE 3 MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROID HORMONE RECEPTOR ERR1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: ESTROGEN-RELATED RECEPTOR, ALPHA, ERR- ALPHA, ESTROGEN
COMPND 6 RECEPTOR-LIKE 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESRRA, ERR1, ESRL1, NR3B1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS NUCLEAR HORMONE RECEPTOR, LIGAND BINDING DOMAIN, LIGAND BINDING
KEYWDS 2 POCKET, THREE-LAYERED ALPHA-HELICAL SANDWICH, INVERSE AGONIST, HELIX
KEYWDS 3 12 (H12), COACTIVATOR GROOVE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KALLEN
REVDAT 7 30-AUG-23 2PJL 1 REMARK
REVDAT 6 20-OCT-21 2PJL 1 REMARK SEQADV
REVDAT 5 18-OCT-17 2PJL 1 REMARK
REVDAT 4 13-JUL-11 2PJL 1 VERSN
REVDAT 3 24-FEB-09 2PJL 1 VERSN
REVDAT 2 25-DEC-07 2PJL 1 JRNL
REVDAT 1 12-JUN-07 2PJL 0
JRNL AUTH J.KALLEN,R.LATTMANN,R.BEERLI,A.BLECHSCHMIDT,M.J.BLOMMERS,
JRNL AUTH 2 M.GEISER,J.OTTL,J.M.SCHLAEPPI,A.STRAUSS,B.FOURNIER
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ESTROGEN-RELATED RECEPTOR ALPHA
JRNL TITL 2 IN COMPLEX WITH A SYNTHETIC INVERSE AGONIST REVEALS ITS
JRNL TITL 3 NOVEL MOLECULAR MECHANISM.
JRNL REF J.BIOL.CHEM. V. 282 23231 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17556356
JRNL DOI 10.1074/JBC.M703337200
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 20528
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1056
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1416
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.86000
REMARK 3 B22 (A**2) : 0.86000
REMARK 3 B33 (A**2) : -1.29000
REMARK 3 B12 (A**2) : 0.43000
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): 0.451
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.287
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.255
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3490 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4722 ; 1.127 ; 2.021
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 430 ; 4.433 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;35.015 ;24.028
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 628 ;16.513 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.057 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 564 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2528 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1677 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2409 ; 0.292 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 217 ; 0.175 ; 0.200
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): 56 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.250 ; 0.200
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): 2256 ; 0.489 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3446 ; 0.848 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1423 ; 1.062 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1276 ; 1.685 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
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 2PJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20542
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.24200
REMARK 200 R SYM FOR SHELL (I) : 0.24200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
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 1XB7 WITH H12 REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 12%PEG400, 0.1M HEPES,
REMARK 280 PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.23250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.84705
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.86333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 48.23250
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 27.84705
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.86333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 48.23250
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 27.84705
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.86333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.69409
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 89.72667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 55.69409
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 89.72667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 55.69409
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 89.72667
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER AS IN THE ASYMMETRIC UNIT
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 273
REMARK 465 SER A 274
REMARK 465 SER A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 PRO A 309
REMARK 465 ASP A 310
REMARK 465 PRO A 311
REMARK 465 ALA A 312
REMARK 465 GLY A 313
REMARK 465 PRO A 314
REMARK 465 ASP A 315
REMARK 465 GLY A 316
REMARK 465 HIS A 317
REMARK 465 ARG A 462
REMARK 465 ALA A 463
REMARK 465 GLY A 464
REMARK 465 PRO A 465
REMARK 465 GLY A 466
REMARK 465 GLY A 467
REMARK 465 GLY A 468
REMARK 465 ALA A 469
REMARK 465 GLU A 470
REMARK 465 MET A 518
REMARK 465 ASP A 519
REMARK 465 GLY B 273
REMARK 465 SER B 274
REMARK 465 SER B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 PRO B 309
REMARK 465 ASP B 310
REMARK 465 PRO B 311
REMARK 465 ALA B 312
REMARK 465 GLY B 313
REMARK 465 PRO B 314
REMARK 465 ASP B 315
REMARK 465 GLY B 316
REMARK 465 HIS B 317
REMARK 465 ARG B 462
REMARK 465 ALA B 463
REMARK 465 GLY B 464
REMARK 465 PRO B 465
REMARK 465 GLY B 466
REMARK 465 GLY B 467
REMARK 465 GLY B 468
REMARK 465 ALA B 469
REMARK 465 GLU B 470
REMARK 465 MET B 518
REMARK 465 ASP B 519
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 B 375 21.84 -78.12
REMARK 500 ALA B 414 6.43 -69.01
REMARK 500 ALA B 460 -71.02 -72.20
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 047 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 047 B 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XB7 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF APO ERRALPHA LBD IN COMPLEX WITH A PGC-1ALPHA
REMARK 900 PEPTIDE AT 2.5A RESOLUTION
DBREF 2PJL A 289 519 UNP P11474 ERR1_HUMAN 289 519
DBREF 2PJL B 289 519 UNP P11474 ERR1_HUMAN 289 519
SEQADV 2PJL GLY A 273 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER A 274 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER A 275 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 276 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 277 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 278 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 279 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 280 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS A 281 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL LEU A 282 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLU A 283 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL VAL A 284 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL LEU A 285 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL PHE A 286 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLN A 287 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLY A 288 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER A 325 UNP P11474 CYS 325 ENGINEERED MUTATION
SEQADV 2PJL GLY B 273 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER B 274 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER B 275 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 276 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 277 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 278 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 279 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 280 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL HIS B 281 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL LEU B 282 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLU B 283 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL VAL B 284 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL LEU B 285 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL PHE B 286 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLN B 287 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL GLY B 288 UNP P11474 CLONING ARTIFACT
SEQADV 2PJL SER B 325 UNP P11474 CYS 325 ENGINEERED MUTATION
SEQRES 1 A 247 GLY SER SER HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU
SEQRES 2 A 247 PHE GLN GLY PRO VAL ASN ALA LEU VAL SER HIS LEU LEU
SEQRES 3 A 247 VAL VAL GLU PRO GLU LYS LEU TYR ALA MET PRO ASP PRO
SEQRES 4 A 247 ALA GLY PRO ASP GLY HIS LEU PRO ALA VAL ALA THR LEU
SEQRES 5 A 247 SER ASP LEU PHE ASP ARG GLU ILE VAL VAL THR ILE SER
SEQRES 6 A 247 TRP ALA LYS SER ILE PRO GLY PHE SER SER LEU SER LEU
SEQRES 7 A 247 SER ASP GLN MET SER VAL LEU GLN SER VAL TRP MET GLU
SEQRES 8 A 247 VAL LEU VAL LEU GLY VAL ALA GLN ARG SER LEU PRO LEU
SEQRES 9 A 247 GLN ASP GLU LEU ALA PHE ALA GLU ASP LEU VAL LEU ASP
SEQRES 10 A 247 GLU GLU GLY ALA ARG ALA ALA GLY LEU GLY GLU LEU GLY
SEQRES 11 A 247 ALA ALA LEU LEU GLN LEU VAL ARG ARG LEU GLN ALA LEU
SEQRES 12 A 247 ARG LEU GLU ARG GLU GLU TYR VAL LEU LEU LYS ALA LEU
SEQRES 13 A 247 ALA LEU ALA ASN SER ASP SER VAL HIS ILE GLU ASP ALA
SEQRES 14 A 247 GLU ALA VAL GLU GLN LEU ARG GLU ALA LEU HIS GLU ALA
SEQRES 15 A 247 LEU LEU GLU TYR GLU ALA GLY ARG ALA GLY PRO GLY GLY
SEQRES 16 A 247 GLY ALA GLU ARG ARG ARG ALA GLY ARG LEU LEU LEU THR
SEQRES 17 A 247 LEU PRO LEU LEU ARG GLN THR ALA GLY LYS VAL LEU ALA
SEQRES 18 A 247 HIS PHE TYR GLY VAL LYS LEU GLU GLY LYS VAL PRO MET
SEQRES 19 A 247 HIS LYS LEU PHE LEU GLU MET LEU GLU ALA MET MET ASP
SEQRES 1 B 247 GLY SER SER HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU
SEQRES 2 B 247 PHE GLN GLY PRO VAL ASN ALA LEU VAL SER HIS LEU LEU
SEQRES 3 B 247 VAL VAL GLU PRO GLU LYS LEU TYR ALA MET PRO ASP PRO
SEQRES 4 B 247 ALA GLY PRO ASP GLY HIS LEU PRO ALA VAL ALA THR LEU
SEQRES 5 B 247 SER ASP LEU PHE ASP ARG GLU ILE VAL VAL THR ILE SER
SEQRES 6 B 247 TRP ALA LYS SER ILE PRO GLY PHE SER SER LEU SER LEU
SEQRES 7 B 247 SER ASP GLN MET SER VAL LEU GLN SER VAL TRP MET GLU
SEQRES 8 B 247 VAL LEU VAL LEU GLY VAL ALA GLN ARG SER LEU PRO LEU
SEQRES 9 B 247 GLN ASP GLU LEU ALA PHE ALA GLU ASP LEU VAL LEU ASP
SEQRES 10 B 247 GLU GLU GLY ALA ARG ALA ALA GLY LEU GLY GLU LEU GLY
SEQRES 11 B 247 ALA ALA LEU LEU GLN LEU VAL ARG ARG LEU GLN ALA LEU
SEQRES 12 B 247 ARG LEU GLU ARG GLU GLU TYR VAL LEU LEU LYS ALA LEU
SEQRES 13 B 247 ALA LEU ALA ASN SER ASP SER VAL HIS ILE GLU ASP ALA
SEQRES 14 B 247 GLU ALA VAL GLU GLN LEU ARG GLU ALA LEU HIS GLU ALA
SEQRES 15 B 247 LEU LEU GLU TYR GLU ALA GLY ARG ALA GLY PRO GLY GLY
SEQRES 16 B 247 GLY ALA GLU ARG ARG ARG ALA GLY ARG LEU LEU LEU THR
SEQRES 17 B 247 LEU PRO LEU LEU ARG GLN THR ALA GLY LYS VAL LEU ALA
SEQRES 18 B 247 HIS PHE TYR GLY VAL LYS LEU GLU GLY LYS VAL PRO MET
SEQRES 19 B 247 HIS LYS LEU PHE LEU GLU MET LEU GLU ALA MET MET ASP
HET 047 A 600 25
HET 047 B 700 25
HETNAM 047 1-CYCLOHEXYL-N-{[1-(4-METHYLPHENYL)-1H-INDOL-3-
HETNAM 2 047 YL]METHYL}METHANAMINE
FORMUL 3 047 2(C23 H28 N2)
FORMUL 5 HOH *236(H2 O)
HELIX 1 1 GLU A 283 GLY A 288 1 6
HELIX 2 2 PRO A 289 VAL A 300 1 12
HELIX 3 3 ALA A 320 LYS A 340 1 21
HELIX 4 4 GLY A 344 LEU A 348 5 5
HELIX 5 5 SER A 349 ARG A 372 1 24
HELIX 6 6 GLU A 390 ALA A 396 1 7
HELIX 7 7 GLU A 400 ALA A 414 1 15
HELIX 8 8 GLU A 418 ASN A 432 1 15
HELIX 9 9 ASP A 440 GLY A 461 1 22
HELIX 10 10 ARG A 471 LEU A 479 1 9
HELIX 11 11 THR A 480 LYS A 499 1 20
HELIX 12 12 LEU A 500 LYS A 503 5 4
HELIX 13 13 VAL A 504 ALA A 516 1 13
HELIX 14 14 GLU B 283 GLY B 288 1 6
HELIX 15 15 PRO B 289 VAL B 300 1 12
HELIX 16 16 ALA B 320 LYS B 340 1 21
HELIX 17 17 GLY B 344 LEU B 348 5 5
HELIX 18 18 SER B 349 ARG B 372 1 24
HELIX 19 19 ASP B 389 ALA B 396 1 8
HELIX 20 20 GLU B 400 ALA B 414 1 15
HELIX 21 21 GLU B 418 ASN B 432 1 15
HELIX 22 22 ASP B 440 GLY B 461 1 22
HELIX 23 23 ARG B 471 LEU B 479 1 9
HELIX 24 24 THR B 480 LYS B 499 1 20
HELIX 25 25 LEU B 500 LYS B 503 5 4
HELIX 26 26 VAL B 504 MET B 517 1 14
SHEET 1 A 2 GLU A 379 ALA A 383 0
SHEET 2 A 2 LEU A 386 ASP A 389 -1 O LEU A 388 N LEU A 380
SHEET 1 B 2 LEU B 380 ALA B 383 0
SHEET 2 B 2 LEU B 386 LEU B 388 -1 O LEU B 388 N LEU B 380
SITE 1 AC1 7 HOH A 5 VAL A 321 LEU A 324 GLU A 331
SITE 2 AC1 7 PHE A 382 GLY A 397 PHE A 495
SITE 1 AC2 10 HOH B 11 LEU B 324 PHE B 328 GLU B 331
SITE 2 AC2 10 PHE B 382 LEU B 386 GLY B 397 LEU B 398
SITE 3 AC2 10 PHE B 495 LEU B 500
CRYST1 96.465 96.465 134.590 90.00 90.00 120.00 H 3 18
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 0.010366 0.005985 0.000000 0.00000
SCALE2 0.000000 0.011970 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007430 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
