HEADER NUCLEAR RECEPTOR 21-MAR-01 1H9U
TITLE THE STRUCTURE OF THE HUMAN RETINOID-X-RECEPTOR BETA LIGAND BINDING
TITLE 2 DOMAIN IN COMPLEX WITH THE SPECIFIC SYNTHETIC AGONIST LG100268
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOID X RECEPTOR, BETA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN RESIDUES 299-522;
COMPND 5 SYNONYM: RXRB;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS NUCLEAR RECEPTOR, RXR, TRANSCRIPTION FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.R.SCHWABE,J.D.LOVE,J.T.GOOCH
REVDAT 4 13-DEC-23 1H9U 1 REMARK LINK
REVDAT 3 24-FEB-09 1H9U 1 VERSN
REVDAT 2 22-MAY-02 1H9U 1 JRNL
REVDAT 1 03-APR-02 1H9U 0
JRNL AUTH J.D.LOVE,J.T.GOOCH,S.BENKO,C.LI,L.NAGY,V.K.K.CHATTERJEE,
JRNL AUTH 2 R.M.EVANS,J.W.R.SCHWABE
JRNL TITL THE STRUCTURAL BASIS FOR THE SPECIFICITY OF RETINOID-X
JRNL TITL 2 RECEPTOR-SELECTIVE AGONISTS: NEW INSIGHTS INTO THE ROLE OF
JRNL TITL 3 HELIX H12
JRNL REF J.BIOL.CHEM. V. 277 11385 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11782480
JRNL DOI 10.1074/JBC.M110869200
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2064073.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 29621
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 SET) : 0.273
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2929
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4461
REMARK 3 BIN R VALUE (WORKING SET) : 0.3540
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 483
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6220
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.68000
REMARK 3 B22 (A**2) : -13.83000
REMARK 3 B33 (A**2) : 11.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 19.66000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.710 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.670 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 52.24
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : LG2.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : LG2.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1290005953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.60
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) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29713
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 38.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1LBD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.60
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 61.94300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.44100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.94300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 53.44100
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 300 REMARK: CRYSTAL. THE RETINOID X RECEPTOR IS ACTIVE
REMARK 300 AS DIMERIC
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
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 BIOMT1 2 -1.000000 0.000000 0.000000 -38.51649
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 254.33272
REMARK 400
REMARK 400 COMPOUND
REMARK 400 BINDS TO 9-CIS RETINOIC ACID (9C-RA). INVOLVED IN
REMARK 400 RETINOIC ACID RESPONSE PATHWAY. THE C-TERMINAL DOMAIN
REMARK 400 IS INVOLVED IN STEROID-BINDING.
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 GLU A 312
REMARK 465 GLN A 313
REMARK 465 LYS A 314
REMARK 465 SER A 315
REMARK 465 ASP A 316
REMARK 465 GLN A 317
REMARK 465 GLY A 318
REMARK 465 VAL A 319
REMARK 465 GLU A 320
REMARK 465 GLY A 321
REMARK 465 PRO A 322
REMARK 465 GLY A 323
REMARK 465 GLY A 324
REMARK 465 THR A 325
REMARK 465 GLY A 326
REMARK 465 GLY A 327
REMARK 465 SER A 328
REMARK 465 GLY A 329
REMARK 465 SER A 330
REMARK 465 SER A 331
REMARK 465 PRO A 332
REMARK 465 ASN A 333
REMARK 465 ASP A 334
REMARK 465 GLU B 312
REMARK 465 GLN B 313
REMARK 465 LYS B 314
REMARK 465 SER B 315
REMARK 465 ASP B 316
REMARK 465 GLN B 317
REMARK 465 GLY B 318
REMARK 465 VAL B 319
REMARK 465 GLU B 320
REMARK 465 GLY B 321
REMARK 465 PRO B 322
REMARK 465 GLY B 323
REMARK 465 GLY B 324
REMARK 465 THR B 325
REMARK 465 GLY B 326
REMARK 465 GLY B 327
REMARK 465 SER B 328
REMARK 465 GLY B 329
REMARK 465 SER B 330
REMARK 465 SER B 331
REMARK 465 PRO B 332
REMARK 465 ASN B 333
REMARK 465 ASP B 334
REMARK 465 GLU C 312
REMARK 465 GLN C 313
REMARK 465 LYS C 314
REMARK 465 SER C 315
REMARK 465 ASP C 316
REMARK 465 GLN C 317
REMARK 465 GLY C 318
REMARK 465 VAL C 319
REMARK 465 GLU C 320
REMARK 465 GLY C 321
REMARK 465 PRO C 322
REMARK 465 GLY C 323
REMARK 465 GLY C 324
REMARK 465 THR C 325
REMARK 465 GLY C 326
REMARK 465 GLY C 327
REMARK 465 SER C 328
REMARK 465 GLY C 329
REMARK 465 SER C 330
REMARK 465 SER C 331
REMARK 465 PRO C 332
REMARK 465 ASN C 333
REMARK 465 ASP C 334
REMARK 465 GLU D 312
REMARK 465 GLN D 313
REMARK 465 LYS D 314
REMARK 465 SER D 315
REMARK 465 ASP D 316
REMARK 465 GLN D 317
REMARK 465 GLY D 318
REMARK 465 VAL D 319
REMARK 465 GLU D 320
REMARK 465 GLY D 321
REMARK 465 PRO D 322
REMARK 465 GLY D 323
REMARK 465 GLY D 324
REMARK 465 THR D 325
REMARK 465 GLY D 326
REMARK 465 GLY D 327
REMARK 465 SER D 328
REMARK 465 GLY D 329
REMARK 465 SER D 330
REMARK 465 SER D 331
REMARK 465 PRO D 332
REMARK 465 ASN D 333
REMARK 465 ASP D 334
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 LYS A 355 CB CG CD CE NZ
REMARK 470 GLU A 459 CG CD OE1 OE2
REMARK 470 GLN A 483 CB CG CD OE1 NE2
REMARK 470 LYS A 511 CG CD CE NZ
REMARK 470 ILE A 518 CG1 CG2 CD1
REMARK 470 ASP A 519 CG OD1 OD2
REMARK 470 THR A 520 OG1 CG2
REMARK 470 PHE A 521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 522 CG CD1 CD2
REMARK 470 LYS B 355 CB CG CD CE NZ
REMARK 470 GLU B 459 CG CD OE1 OE2
REMARK 470 GLN B 477 CB CG CD OE1 NE2
REMARK 470 GLU B 481 CG CD OE1 OE2
REMARK 470 GLN B 483 CG CD OE1 NE2
REMARK 470 LYS B 511 CB CG CD CE NZ
REMARK 470 ILE B 518 CB CG1 CG2 CD1
REMARK 470 THR B 520 OG1 CG2
REMARK 470 PHE B 521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 522 CG CD1 CD2
REMARK 470 ASP C 302 CG OD1 OD2
REMARK 470 ARG C 303 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 306 CG CD OE1 OE2
REMARK 470 ARG C 392 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU C 481 CB CG CD OE1 OE2
REMARK 470 GLN C 483 CB CG CD OE1 NE2
REMARK 470 LYS C 511 CB CG CD CE NZ
REMARK 470 THR C 520 OG1 CG2
REMARK 470 LEU C 522 CG CD1 CD2
REMARK 470 ASP D 302 CB CG OD1 OD2
REMARK 470 LEU D 305 CG CD1 CD2
REMARK 470 ARG D 392 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS D 452 CG CD CE NZ
REMARK 470 GLN D 477 CB CG CD OE1 NE2
REMARK 470 LYS D 478 CB CG CD CE NZ
REMARK 470 GLU D 481 CB CG CD OE1 OE2
REMARK 470 GLN D 483 CB CG CD OE1 NE2
REMARK 470 THR D 520 OG1 CG2
REMARK 470 LEU D 522 CG CD1 CD2
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 358 -71.08 -12.38
REMARK 500 ASP A 393 59.07 34.38
REMARK 500 ARG A 405 -36.47 -35.84
REMARK 500 LEU A 491 4.43 -68.39
REMARK 500 ASP A 515 29.56 45.52
REMARK 500 PHE A 521 -87.84 -45.78
REMARK 500 PRO B 358 -72.15 -11.47
REMARK 500 ASP B 393 58.25 35.44
REMARK 500 ARG B 405 -37.24 -34.37
REMARK 500 LEU B 491 3.82 -69.30
REMARK 500 PRO C 358 -73.33 -10.89
REMARK 500 ASP C 393 57.62 34.56
REMARK 500 ARG C 405 -36.17 -34.95
REMARK 500 PRO D 358 -72.15 -12.07
REMARK 500 ASP D 393 58.29 34.50
REMARK 500 ARG D 405 -36.05 -34.66
REMARK 500 LEU D 491 2.94 -69.75
REMARK 500 ASP D 515 27.98 47.48
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 NI A 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL A 3 CL
REMARK 620 2 HIS A 404 NE2 94.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL B 3 CL
REMARK 620 2 HIS B 402 ND1 116.5
REMARK 620 3 HIS B 404 NE2 86.3 127.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 402 ND1
REMARK 620 2 HIS C 404 NE2 124.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 402 ND1
REMARK 620 2 HIS D 404 NE2 126.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG2 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG2 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG2 C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG2 D 1
DBREF 1H9U A 299 522 UNP P28702 RXRB_HUMAN 299 522
DBREF 1H9U B 299 522 UNP P28702 RXRB_HUMAN 299 522
DBREF 1H9U C 299 522 UNP P28702 RXRB_HUMAN 299 522
DBREF 1H9U D 299 522 UNP P28702 RXRB_HUMAN 299 522
SEQRES 1 A 224 MET PRO VAL ASP ARG ILE LEU GLU ALA GLU LEU ALA VAL
SEQRES 2 A 224 GLU GLN LYS SER ASP GLN GLY VAL GLU GLY PRO GLY GLY
SEQRES 3 A 224 THR GLY GLY SER GLY SER SER PRO ASN ASP PRO VAL THR
SEQRES 4 A 224 ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU PHE THR LEU
SEQRES 5 A 224 VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE SER SER LEU
SEQRES 6 A 224 PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG ALA GLY TRP
SEQRES 7 A 224 ASN GLU LEU LEU ILE ALA SER PHE SER HIS ARG SER ILE
SEQRES 8 A 224 ASP VAL ARG ASP GLY ILE LEU LEU ALA THR GLY LEU HIS
SEQRES 9 A 224 VAL HIS ARG ASN SER ALA HIS SER ALA GLY VAL GLY ALA
SEQRES 10 A 224 ILE PHE ASP ARG VAL LEU THR GLU LEU VAL SER LYS MET
SEQRES 11 A 224 ARG ASP MET ARG MET ASP LYS THR GLU LEU GLY CYS LEU
SEQRES 12 A 224 ARG ALA ILE ILE LEU PHE ASN PRO ASP ALA LYS GLY LEU
SEQRES 13 A 224 SER ASN PRO SER GLU VAL GLU VAL LEU ARG GLU LYS VAL
SEQRES 14 A 224 TYR ALA SER LEU GLU THR TYR CYS LYS GLN LYS TYR PRO
SEQRES 15 A 224 GLU GLN GLN GLY ARG PHE ALA LYS LEU LEU LEU ARG LEU
SEQRES 16 A 224 PRO ALA LEU ARG SER ILE GLY LEU LYS CYS LEU GLU HIS
SEQRES 17 A 224 LEU PHE PHE PHE LYS LEU ILE GLY ASP THR PRO ILE ASP
SEQRES 18 A 224 THR PHE LEU
SEQRES 1 B 224 MET PRO VAL ASP ARG ILE LEU GLU ALA GLU LEU ALA VAL
SEQRES 2 B 224 GLU GLN LYS SER ASP GLN GLY VAL GLU GLY PRO GLY GLY
SEQRES 3 B 224 THR GLY GLY SER GLY SER SER PRO ASN ASP PRO VAL THR
SEQRES 4 B 224 ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU PHE THR LEU
SEQRES 5 B 224 VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE SER SER LEU
SEQRES 6 B 224 PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG ALA GLY TRP
SEQRES 7 B 224 ASN GLU LEU LEU ILE ALA SER PHE SER HIS ARG SER ILE
SEQRES 8 B 224 ASP VAL ARG ASP GLY ILE LEU LEU ALA THR GLY LEU HIS
SEQRES 9 B 224 VAL HIS ARG ASN SER ALA HIS SER ALA GLY VAL GLY ALA
SEQRES 10 B 224 ILE PHE ASP ARG VAL LEU THR GLU LEU VAL SER LYS MET
SEQRES 11 B 224 ARG ASP MET ARG MET ASP LYS THR GLU LEU GLY CYS LEU
SEQRES 12 B 224 ARG ALA ILE ILE LEU PHE ASN PRO ASP ALA LYS GLY LEU
SEQRES 13 B 224 SER ASN PRO SER GLU VAL GLU VAL LEU ARG GLU LYS VAL
SEQRES 14 B 224 TYR ALA SER LEU GLU THR TYR CYS LYS GLN LYS TYR PRO
SEQRES 15 B 224 GLU GLN GLN GLY ARG PHE ALA LYS LEU LEU LEU ARG LEU
SEQRES 16 B 224 PRO ALA LEU ARG SER ILE GLY LEU LYS CYS LEU GLU HIS
SEQRES 17 B 224 LEU PHE PHE PHE LYS LEU ILE GLY ASP THR PRO ILE ASP
SEQRES 18 B 224 THR PHE LEU
SEQRES 1 C 224 MET PRO VAL ASP ARG ILE LEU GLU ALA GLU LEU ALA VAL
SEQRES 2 C 224 GLU GLN LYS SER ASP GLN GLY VAL GLU GLY PRO GLY GLY
SEQRES 3 C 224 THR GLY GLY SER GLY SER SER PRO ASN ASP PRO VAL THR
SEQRES 4 C 224 ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU PHE THR LEU
SEQRES 5 C 224 VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE SER SER LEU
SEQRES 6 C 224 PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG ALA GLY TRP
SEQRES 7 C 224 ASN GLU LEU LEU ILE ALA SER PHE SER HIS ARG SER ILE
SEQRES 8 C 224 ASP VAL ARG ASP GLY ILE LEU LEU ALA THR GLY LEU HIS
SEQRES 9 C 224 VAL HIS ARG ASN SER ALA HIS SER ALA GLY VAL GLY ALA
SEQRES 10 C 224 ILE PHE ASP ARG VAL LEU THR GLU LEU VAL SER LYS MET
SEQRES 11 C 224 ARG ASP MET ARG MET ASP LYS THR GLU LEU GLY CYS LEU
SEQRES 12 C 224 ARG ALA ILE ILE LEU PHE ASN PRO ASP ALA LYS GLY LEU
SEQRES 13 C 224 SER ASN PRO SER GLU VAL GLU VAL LEU ARG GLU LYS VAL
SEQRES 14 C 224 TYR ALA SER LEU GLU THR TYR CYS LYS GLN LYS TYR PRO
SEQRES 15 C 224 GLU GLN GLN GLY ARG PHE ALA LYS LEU LEU LEU ARG LEU
SEQRES 16 C 224 PRO ALA LEU ARG SER ILE GLY LEU LYS CYS LEU GLU HIS
SEQRES 17 C 224 LEU PHE PHE PHE LYS LEU ILE GLY ASP THR PRO ILE ASP
SEQRES 18 C 224 THR PHE LEU
SEQRES 1 D 224 MET PRO VAL ASP ARG ILE LEU GLU ALA GLU LEU ALA VAL
SEQRES 2 D 224 GLU GLN LYS SER ASP GLN GLY VAL GLU GLY PRO GLY GLY
SEQRES 3 D 224 THR GLY GLY SER GLY SER SER PRO ASN ASP PRO VAL THR
SEQRES 4 D 224 ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU PHE THR LEU
SEQRES 5 D 224 VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE SER SER LEU
SEQRES 6 D 224 PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG ALA GLY TRP
SEQRES 7 D 224 ASN GLU LEU LEU ILE ALA SER PHE SER HIS ARG SER ILE
SEQRES 8 D 224 ASP VAL ARG ASP GLY ILE LEU LEU ALA THR GLY LEU HIS
SEQRES 9 D 224 VAL HIS ARG ASN SER ALA HIS SER ALA GLY VAL GLY ALA
SEQRES 10 D 224 ILE PHE ASP ARG VAL LEU THR GLU LEU VAL SER LYS MET
SEQRES 11 D 224 ARG ASP MET ARG MET ASP LYS THR GLU LEU GLY CYS LEU
SEQRES 12 D 224 ARG ALA ILE ILE LEU PHE ASN PRO ASP ALA LYS GLY LEU
SEQRES 13 D 224 SER ASN PRO SER GLU VAL GLU VAL LEU ARG GLU LYS VAL
SEQRES 14 D 224 TYR ALA SER LEU GLU THR TYR CYS LYS GLN LYS TYR PRO
SEQRES 15 D 224 GLU GLN GLN GLY ARG PHE ALA LYS LEU LEU LEU ARG LEU
SEQRES 16 D 224 PRO ALA LEU ARG SER ILE GLY LEU LYS CYS LEU GLU HIS
SEQRES 17 D 224 LEU PHE PHE PHE LYS LEU ILE GLY ASP THR PRO ILE ASP
SEQRES 18 D 224 THR PHE LEU
HET LG2 A 1 27
HET NI A 2 1
HET CL A 3 1
HET LG2 B 1 27
HET NI B 2 1
HET CL B 3 1
HET LG2 C 1 27
HET NI C 2 1
HET LG2 D 1 27
HET NI D 2 1
HETNAM LG2 6-[1-(3,5,5,8,8-PENTAMETHYL-5,6,7,8-
HETNAM 2 LG2 TETRAHYDRONAPHTHALEN-2-YL)CYCLOPROPYL]PYRIDINE-3-
HETNAM 3 LG2 CARBOXYLIC ACID
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
FORMUL 5 LG2 4(C24 H29 N O2)
FORMUL 6 NI 4(NI 2+)
FORMUL 7 CL 2(CL 1-)
FORMUL 15 HOH *4(H2 O)
HELIX 1 1 PRO A 300 ALA A 310 1 11
HELIX 2 2 PRO A 335 PHE A 348 1 14
HELIX 3 3 THR A 349 ARG A 356 1 8
HELIX 4 4 HIS A 359 LEU A 363 5 5
HELIX 5 5 PRO A 364 SER A 388 1 25
HELIX 6 6 ARG A 405 GLY A 412 1 8
HELIX 7 7 VAL A 413 LEU A 424 1 12
HELIX 8 8 LEU A 424 ARG A 432 1 9
HELIX 9 9 ASP A 434 PHE A 447 1 14
HELIX 10 10 ASN A 456 TYR A 479 1 24
HELIX 11 11 GLY A 484 LEU A 491 1 8
HELIX 12 12 ARG A 492 GLY A 514 1 23
HELIX 13 13 THR A 516 LEU A 522 1 7
HELIX 14 14 PRO B 300 ALA B 310 1 11
HELIX 15 15 PRO B 335 PHE B 348 1 14
HELIX 16 16 THR B 349 ARG B 356 1 8
HELIX 17 17 HIS B 359 LEU B 363 5 5
HELIX 18 18 PRO B 364 SER B 388 1 25
HELIX 19 19 ARG B 405 GLY B 412 1 8
HELIX 20 20 VAL B 413 LEU B 424 1 12
HELIX 21 21 LEU B 424 ARG B 432 1 9
HELIX 22 22 ASP B 434 PHE B 447 1 14
HELIX 23 23 ASN B 456 TYR B 479 1 24
HELIX 24 24 GLY B 484 LEU B 491 1 8
HELIX 25 25 ARG B 492 GLY B 514 1 23
HELIX 26 26 THR B 516 LEU B 522 1 7
HELIX 27 27 PRO C 300 ALA C 310 1 11
HELIX 28 28 PRO C 335 PHE C 348 1 14
HELIX 29 29 THR C 349 ARG C 356 1 8
HELIX 30 30 HIS C 359 LEU C 363 5 5
HELIX 31 31 PRO C 364 SER C 388 1 25
HELIX 32 32 ARG C 405 GLY C 412 1 8
HELIX 33 33 VAL C 413 LEU C 424 1 12
HELIX 34 34 LEU C 424 ARG C 432 1 9
HELIX 35 35 ASP C 434 PHE C 447 1 14
HELIX 36 36 ASN C 456 TYR C 479 1 24
HELIX 37 37 GLY C 484 LEU C 491 1 8
HELIX 38 38 ARG C 492 GLY C 514 1 23
HELIX 39 39 THR C 516 LEU C 522 1 7
HELIX 40 40 PRO D 300 ALA D 310 1 11
HELIX 41 41 PRO D 335 PHE D 348 1 14
HELIX 42 42 THR D 349 ARG D 356 1 8
HELIX 43 43 HIS D 359 LEU D 363 5 5
HELIX 44 44 PRO D 364 SER D 388 1 25
HELIX 45 45 ARG D 405 ALA D 411 1 7
HELIX 46 46 VAL D 413 LEU D 424 1 12
HELIX 47 47 LEU D 424 ARG D 432 1 9
HELIX 48 48 ASP D 434 PHE D 447 1 14
HELIX 49 49 ASN D 456 TYR D 479 1 24
HELIX 50 50 GLY D 484 LEU D 491 1 8
HELIX 51 51 ARG D 492 GLY D 514 1 23
HELIX 52 52 THR D 516 PHE D 521 1 6
SHEET 1 AA 2 GLY A 394 LEU A 396 0
SHEET 2 AA 2 HIS A 402 HIS A 404 -1 O VAL A 403 N ILE A 395
SHEET 1 BA 2 GLY B 394 LEU B 396 0
SHEET 2 BA 2 HIS B 402 HIS B 404 -1 O VAL B 403 N ILE B 395
SHEET 1 CA 2 GLY C 394 LEU C 396 0
SHEET 2 CA 2 HIS C 402 HIS C 404 -1 O VAL C 403 N ILE C 395
SHEET 1 DA 2 GLY D 394 LEU D 396 0
SHEET 2 DA 2 HIS D 402 HIS D 404 -1 O VAL D 403 N ILE D 395
LINK NI NI A 2 CL CL A 3 1555 1555 1.98
LINK NI NI A 2 NE2 HIS A 404 1555 1555 2.18
LINK NI NI B 2 CL CL B 3 1555 1555 2.06
LINK NI NI B 2 ND1 HIS B 402 1555 1555 2.56
LINK NI NI B 2 NE2 HIS B 404 1555 1555 2.26
LINK NI NI C 2 ND1 HIS C 402 1555 1555 2.62
LINK NI NI C 2 NE2 HIS C 404 1555 1555 2.30
LINK NI NI D 2 ND1 HIS D 402 1555 1555 2.62
LINK NI NI D 2 NE2 HIS D 404 1555 1555 2.26
SITE 1 AC1 3 CL A 3 HIS A 402 HIS A 404
SITE 1 AC2 2 NI A 2 HIS A 404
SITE 1 AC3 3 CL B 3 HIS B 402 HIS B 404
SITE 1 AC4 2 NI B 2 HIS B 404
SITE 1 AC5 2 HIS C 402 HIS C 404
SITE 1 AC6 2 HIS D 402 HIS D 404
SITE 1 AC7 15 ILE A 339 ALA A 342 ALA A 343 GLN A 346
SITE 2 AC7 15 TRP A 376 LEU A 380 ILE A 381 PHE A 384
SITE 3 AC7 15 ARG A 387 LEU A 397 ALA A 398 ILE A 416
SITE 4 AC7 15 CYS A 503 HIS A 506 HOH A2001
SITE 1 AC8 13 ILE B 339 ALA B 342 ALA B 343 GLN B 346
SITE 2 AC8 13 LEU B 380 ILE B 381 PHE B 384 ARG B 387
SITE 3 AC8 13 LEU B 397 ALA B 398 ILE B 416 CYS B 503
SITE 4 AC8 13 HIS B 506
SITE 1 AC9 13 ILE C 339 ALA C 342 ALA C 343 GLN C 346
SITE 2 AC9 13 TRP C 376 LEU C 380 ILE C 381 ARG C 387
SITE 3 AC9 13 LEU C 397 ALA C 398 CYS C 503 HIS C 506
SITE 4 AC9 13 HOH C2001
SITE 1 BC1 14 ILE D 339 ALA D 342 ALA D 343 GLN D 346
SITE 2 BC1 14 TRP D 376 LEU D 380 ILE D 381 PHE D 384
SITE 3 BC1 14 ARG D 387 LEU D 397 ALA D 398 ILE D 416
SITE 4 BC1 14 CYS D 503 HIS D 506
CRYST1 123.886 106.882 100.587 90.00 122.56 90.00 C 1 2 1 16
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 0.008072 0.000000 0.005154 0.00000
SCALE2 0.000000 0.009356 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
