HEADER SIGNALING PROTEIN 29-SEP-10 3P0U
TITLE CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF HUMAN TESTICULAR
TITLE 2 RECEPTOR 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 2 GROUP C MEMBER 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: ORPHAN NUCLEAR RECEPTOR TR4, TESTICULAR RECEPTOR 4, ORPHAN
COMPND 6 NUCLEAR RECEPTOR TAK1;
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: NR2C2, TAK1, TR4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGAND BINDING DOMAIN, ORPHAN NUCLEAR RECEPTOR, TESTICULAR RECEPTOR
KEYWDS 2 4, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,K.M.SUINO-POWELL,Y.XU,C.-W.CHAN,S.W.KRUSE,R.REYNOLDS,
AUTHOR 2 J.D.ENGEL,H.E.XU
REVDAT 4 21-FEB-24 3P0U 1 SEQADV
REVDAT 3 09-FEB-11 3P0U 1 JRNL
REVDAT 2 24-NOV-10 3P0U 1 JRNL
REVDAT 1 10-NOV-10 3P0U 0
JRNL AUTH X.E.ZHOU,K.M.SUINO-POWELL,Y.XU,C.W.CHAN,O.TANABE,S.W.KRUSE,
JRNL AUTH 2 R.REYNOLDS,J.D.ENGEL,H.E.XU
JRNL TITL THE ORPHAN NUCLEAR RECEPTOR TR4 IS A VITAMIN A-ACTIVATED
JRNL TITL 2 NUCLEAR RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 286 2877 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21068381
JRNL DOI 10.1074/JBC.M110.168740
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15825
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) : 0.260
REMARK 3 R VALUE (WORKING SET) : 0.258
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1228
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1146
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.4320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3485
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.20000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -7.36000
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): 0.419
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.337
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.216
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3557 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2369 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4827 ; 1.418 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5801 ; 0.967 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 432 ; 4.672 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;43.281 ;24.323
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 622 ;20.006 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;19.626 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 561 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3864 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 696 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2190 ; 1.742 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 868 ; 0.557 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3552 ; 3.198 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1367 ; 2.319 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1275 ; 3.800 ; 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): 5926 ; 1.544 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 73 ;16.676 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5854 ;10.779 ; 5.000
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 : BABINET MODEL WITH 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 3P0U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-08
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 : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17576
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 92.7
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M HEPES, 25% W/V
REMARK 280 PEG 3,350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 70.48150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 92.43150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 70.48150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 92.43150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.48150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 92.43150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 70.48150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.43150
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 92.43150
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 92.43150
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 92.43150
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 92.43150
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 70.48150
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 70.48150
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 70.48150
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 64.73950
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 70.48150
REMARK 290 SMTRY3 16 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 ILE A 466
REMARK 465 HIS A 469
REMARK 465 LEU A 470
REMARK 465 GLN A 471
REMARK 465 ILE A 474
REMARK 465 GLN A 475
REMARK 465 GLU A 476
REMARK 465 ASP A 477
REMARK 465 LYS A 478
REMARK 465 LEU A 479
REMARK 465 SER A 480
REMARK 465 GLY A 481
REMARK 465 ASP A 482
REMARK 465 GLU A 602
REMARK 465 THR A 603
REMARK 465 ALA A 604
REMARK 465 GLU A 605
REMARK 465 TYR A 606
REMARK 465 ASN A 607
REMARK 465 GLY A 608
REMARK 465 GLN A 609
REMARK 465 ILE A 610
REMARK 465 THR A 611
REMARK 465 GLY A 612
REMARK 465 ALA A 613
REMARK 465 SER A 614
REMARK 465 LEU A 615
REMARK 465 ALA B 465
REMARK 465 ILE B 466
REMARK 465 VAL B 467
REMARK 465 ASN B 468
REMARK 465 HIS B 469
REMARK 465 LEU B 470
REMARK 465 GLN B 471
REMARK 465 ASN B 472
REMARK 465 SER B 473
REMARK 465 ILE B 474
REMARK 465 GLN B 475
REMARK 465 GLU B 476
REMARK 465 ASP B 477
REMARK 465 LYS B 478
REMARK 465 LEU B 479
REMARK 465 SER B 480
REMARK 465 GLY B 481
REMARK 465 LYS B 600
REMARK 465 MET B 601
REMARK 465 GLU B 602
REMARK 465 THR B 603
REMARK 465 ALA B 604
REMARK 465 GLU B 605
REMARK 465 TYR B 606
REMARK 465 ASN B 607
REMARK 465 GLY B 608
REMARK 465 GLN B 609
REMARK 465 ILE B 610
REMARK 465 THR B 611
REMARK 465 GLY B 612
REMARK 465 ALA B 613
REMARK 465 SER B 614
REMARK 465 LEU B 615
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 THR A 530 O HOH A 5 2.16
REMARK 500 O SER A 529 O HOH A 5 2.17
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 ASP A 368 89.41 -168.93
REMARK 500 VAL A 376 -73.99 -113.80
REMARK 500 PRO A 379 93.95 -62.76
REMARK 500 ASP A 383 -84.56 -114.91
REMARK 500 HIS A 385 -96.34 -69.77
REMARK 500 THR A 387 -100.01 -96.80
REMARK 500 LEU A 390 -8.43 -51.62
REMARK 500 MET A 392 88.21 -158.01
REMARK 500 PRO A 397 -99.71 -69.92
REMARK 500 GLU A 398 -152.86 -102.34
REMARK 500 TYR A 399 -154.08 -89.32
REMARK 500 LEU A 400 141.06 -7.20
REMARK 500 ASN A 401 52.09 -58.71
REMARK 500 VAL A 402 -144.14 -70.27
REMARK 500 CYS A 441 24.53 -150.99
REMARK 500 MET A 457 90.72 -46.82
REMARK 500 SER A 460 46.73 -84.58
REMARK 500 ILE A 462 74.67 -107.90
REMARK 500 ILE A 484 43.07 -102.25
REMARK 500 PHE A 520 58.92 -98.44
REMARK 500 THR A 530 -111.21 -102.21
REMARK 500 ALA A 550 -70.73 -78.23
REMARK 500 LEU A 571 -13.60 -48.17
REMARK 500 THR A 583 -45.11 -139.72
REMARK 500 SER A 590 97.58 70.41
REMARK 500 ASP B 368 97.07 179.41
REMARK 500 PRO B 372 -175.17 -63.46
REMARK 500 ILE B 373 40.24 -78.89
REMARK 500 ILE B 374 -125.64 -152.66
REMARK 500 VAL B 376 175.38 -51.32
REMARK 500 THR B 384 146.39 -178.81
REMARK 500 HIS B 385 76.63 -158.53
REMARK 500 VAL B 386 151.54 -28.95
REMARK 500 PRO B 397 -139.38 -55.76
REMARK 500 GLU B 398 -32.30 -148.44
REMARK 500 TYR B 399 -167.87 -79.33
REMARK 500 VAL B 402 -140.17 -88.12
REMARK 500 HIS B 403 31.23 -94.01
REMARK 500 LEU B 429 31.54 -74.71
REMARK 500 THR B 435 29.34 -76.51
REMARK 500 SER B 436 -36.43 -133.37
REMARK 500 ALA B 451 30.06 -79.50
REMARK 500 GLN B 455 -169.73 -108.56
REMARK 500 VAL B 456 -148.99 -107.79
REMARK 500 THR B 461 98.81 -46.18
REMARK 500 LEU B 463 151.94 -0.48
REMARK 500 ASP B 505 89.93 46.53
REMARK 500 TYR B 509 67.00 -101.57
REMARK 500 THR B 528 -87.19 -92.83
REMARK 500 VAL B 548 -67.24 -93.57
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3P0U A 367 615 UNP P49116 NR2C2_HUMAN 348 596
DBREF 3P0U B 367 615 UNP P49116 NR2C2_HUMAN 348 596
SEQADV 3P0U ALA A 539 UNP P49116 LYS 520 ENGINEERED MUTATION
SEQADV 3P0U ALA A 550 UNP P49116 LYS 531 ENGINEERED MUTATION
SEQADV 3P0U ALA B 539 UNP P49116 LYS 520 ENGINEERED MUTATION
SEQADV 3P0U ALA B 550 UNP P49116 LYS 531 ENGINEERED MUTATION
SEQRES 1 A 249 ARG ASP GLN SER THR PRO ILE ILE GLU VAL GLU GLY PRO
SEQRES 2 A 249 LEU LEU SER ASP THR HIS VAL THR PHE LYS LEU THR MET
SEQRES 3 A 249 PRO SER PRO MET PRO GLU TYR LEU ASN VAL HIS TYR ILE
SEQRES 4 A 249 CYS GLU SER ALA SER ARG LEU LEU PHE LEU SER MET HIS
SEQRES 5 A 249 TRP ALA ARG SER ILE PRO ALA PHE GLN ALA LEU GLY GLN
SEQRES 6 A 249 ASP CYS ASN THR SER LEU VAL ARG ALA CYS TRP ASN GLU
SEQRES 7 A 249 LEU PHE THR LEU GLY LEU ALA GLN CYS ALA GLN VAL MET
SEQRES 8 A 249 SER LEU SER THR ILE LEU ALA ALA ILE VAL ASN HIS LEU
SEQRES 9 A 249 GLN ASN SER ILE GLN GLU ASP LYS LEU SER GLY ASP ARG
SEQRES 10 A 249 ILE LYS GLN VAL MET GLU HIS ILE TRP LYS LEU GLN GLU
SEQRES 11 A 249 PHE CYS ASN SER MET ALA LYS LEU ASP ILE ASP GLY TYR
SEQRES 12 A 249 GLU TYR ALA TYR LEU LYS ALA ILE VAL LEU PHE SER PRO
SEQRES 13 A 249 ASP HIS PRO GLY LEU THR SER THR SER GLN ILE GLU LYS
SEQRES 14 A 249 PHE GLN GLU ALA ALA GLN MET GLU LEU GLN ASP TYR VAL
SEQRES 15 A 249 GLN ALA THR TYR SER GLU ASP THR TYR ARG LEU ALA ARG
SEQRES 16 A 249 ILE LEU VAL ARG LEU PRO ALA LEU ARG LEU MET SER SER
SEQRES 17 A 249 ASN ILE THR GLU GLU LEU PHE PHE THR GLY LEU ILE GLY
SEQRES 18 A 249 ASN VAL SER ILE ASP SER ILE ILE PRO TYR ILE LEU LYS
SEQRES 19 A 249 MET GLU THR ALA GLU TYR ASN GLY GLN ILE THR GLY ALA
SEQRES 20 A 249 SER LEU
SEQRES 1 B 249 ARG ASP GLN SER THR PRO ILE ILE GLU VAL GLU GLY PRO
SEQRES 2 B 249 LEU LEU SER ASP THR HIS VAL THR PHE LYS LEU THR MET
SEQRES 3 B 249 PRO SER PRO MET PRO GLU TYR LEU ASN VAL HIS TYR ILE
SEQRES 4 B 249 CYS GLU SER ALA SER ARG LEU LEU PHE LEU SER MET HIS
SEQRES 5 B 249 TRP ALA ARG SER ILE PRO ALA PHE GLN ALA LEU GLY GLN
SEQRES 6 B 249 ASP CYS ASN THR SER LEU VAL ARG ALA CYS TRP ASN GLU
SEQRES 7 B 249 LEU PHE THR LEU GLY LEU ALA GLN CYS ALA GLN VAL MET
SEQRES 8 B 249 SER LEU SER THR ILE LEU ALA ALA ILE VAL ASN HIS LEU
SEQRES 9 B 249 GLN ASN SER ILE GLN GLU ASP LYS LEU SER GLY ASP ARG
SEQRES 10 B 249 ILE LYS GLN VAL MET GLU HIS ILE TRP LYS LEU GLN GLU
SEQRES 11 B 249 PHE CYS ASN SER MET ALA LYS LEU ASP ILE ASP GLY TYR
SEQRES 12 B 249 GLU TYR ALA TYR LEU LYS ALA ILE VAL LEU PHE SER PRO
SEQRES 13 B 249 ASP HIS PRO GLY LEU THR SER THR SER GLN ILE GLU LYS
SEQRES 14 B 249 PHE GLN GLU ALA ALA GLN MET GLU LEU GLN ASP TYR VAL
SEQRES 15 B 249 GLN ALA THR TYR SER GLU ASP THR TYR ARG LEU ALA ARG
SEQRES 16 B 249 ILE LEU VAL ARG LEU PRO ALA LEU ARG LEU MET SER SER
SEQRES 17 B 249 ASN ILE THR GLU GLU LEU PHE PHE THR GLY LEU ILE GLY
SEQRES 18 B 249 ASN VAL SER ILE ASP SER ILE ILE PRO TYR ILE LEU LYS
SEQRES 19 B 249 MET GLU THR ALA GLU TYR ASN GLY GLN ILE THR GLY ALA
SEQRES 20 B 249 SER LEU
FORMUL 3 HOH *73(H2 O)
HELIX 1 1 TYR A 404 SER A 422 1 19
HELIX 2 2 PHE A 426 LEU A 429 5 4
HELIX 3 3 GLY A 430 ALA A 440 1 11
HELIX 4 4 CYS A 441 CYS A 453 1 13
HELIX 5 5 GLN A 486 LEU A 504 1 19
HELIX 6 6 ASP A 507 PHE A 520 1 14
HELIX 7 7 THR A 530 TYR A 552 1 23
HELIX 8 8 TYR A 557 VAL A 564 1 8
HELIX 9 9 ARG A 565 LEU A 571 1 7
HELIX 10 10 SER A 573 PHE A 582 1 10
HELIX 11 11 LEU A 585 SER A 590 1 6
HELIX 12 12 SER A 590 LEU A 599 1 10
HELIX 13 13 VAL B 386 THR B 391 5 6
HELIX 14 14 TYR B 404 ILE B 423 1 20
HELIX 15 15 ILE B 423 LEU B 429 1 7
HELIX 16 16 CYS B 433 VAL B 438 1 6
HELIX 17 17 CYS B 441 ALA B 451 1 11
HELIX 18 18 GLN B 486 LEU B 504 1 19
HELIX 19 19 TYR B 509 PHE B 520 1 12
HELIX 20 20 SER B 529 GLN B 549 1 21
HELIX 21 21 TYR B 557 VAL B 564 1 8
HELIX 22 22 ARG B 565 ARG B 570 1 6
HELIX 23 23 SER B 573 PHE B 581 1 9
HELIX 24 24 SER B 590 ILE B 595 1 6
CRYST1 129.479 140.963 184.863 90.00 90.00 90.00 F 2 2 2 32
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 0.007723 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007094 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END