HEADER TRANSCRIPTION 24-OCT-09 3A9E
TITLE CRYSTAL STRUCTURE OF A MIXED AGONIST-BOUND RAR-ALPHA AND ANTAGONIST-
TITLE 2 BOUND RXR-ALPHA HETERODIMER LIGAND BINDING DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: RETINOID X RECEPTOR ALPHA, NUCLEAR RECEPTOR SUBFAMILY 2
COMPND 6 GROUP B MEMBER 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RETINOIC ACID RECEPTOR ALPHA;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 12 SYNONYM: RAR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP B MEMBER 1;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: 13-MER (LXXLL MOTIF) FROM NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 16 CHAIN: I;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RXRA, NR2B1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RARA, NR1B1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS TRANSCRIPTION, NUCLEUS, RECEPTOR, TRANSCRIPTION REGULATION,
KEYWDS 2 STRUCTURAL GENOMICS, SPINE2-COMPLEXES, STRUCTURAL PROTEOMICS IN
KEYWDS 3 EUROPE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SATO,S.DUCLAUD,C.PELUSO-ILTIS,P.POUSSIN,D.MORAS,N.ROCHEL,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 01-NOV-23 3A9E 1 REMARK
REVDAT 2 30-OCT-13 3A9E 1 JRNL VERSN
REVDAT 1 06-OCT-10 3A9E 0
JRNL AUTH Y.SATO,N.RAMALANJAONA,T.HUET,N.POTIER,J.OSZ,P.ANTONY,
JRNL AUTH 2 C.PELUSO-ILTIS,P.POUSSIN-COURMONTAGNE,E.ENNIFAR,Y.MELY,
JRNL AUTH 3 A.DEJAEGERE,D.MORAS,N.ROCHEL
JRNL TITL THE PHANTOM EFFECT OF THE REXINOID LG100754: STRUCTURAL AND
JRNL TITL 2 FUNCTIONAL INSIGHTS
JRNL REF PLOS ONE V. 5 15119 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 21152046
JRNL DOI 10.1371/JOURNAL.PONE.0015119
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 15179
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.8825 - 4.6862 0.98 3273 165 0.1877 0.2433
REMARK 3 2 4.6862 - 3.7276 0.83 2665 121 0.1802 0.2250
REMARK 3 3 3.7276 - 3.2587 0.72 2261 130 0.2251 0.2820
REMARK 3 4 3.2587 - 2.9618 1.00 3118 170 0.2196 0.2985
REMARK 3 5 2.9618 - 2.7501 1.00 3125 151 0.2276 0.3015
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.27
REMARK 3 B_SOL : 39.73
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.630
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08600
REMARK 3 B22 (A**2) : -1.08600
REMARK 3 B33 (A**2) : 2.17210
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 3833
REMARK 3 ANGLE : 0.542 5188
REMARK 3 CHIRALITY : 0.034 600
REMARK 3 PLANARITY : 0.002 663
REMARK 3 DIHEDRAL : 12.291 1473
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1030 62.1620 7.2991
REMARK 3 T TENSOR
REMARK 3 T11: 0.1329 T22: 0.0319
REMARK 3 T33: 0.1040 T12: 0.0226
REMARK 3 T13: -0.0205 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.2469 L22: 1.4068
REMARK 3 L33: 1.1789 L12: 0.5900
REMARK 3 L13: -0.1421 L23: -0.3309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0839 S12: -0.1236 S13: 0.0012
REMARK 3 S21: 0.0236 S22: -0.0551 S23: -0.1078
REMARK 3 S31: -0.0510 S32: -0.0769 S33: -0.0318
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3A9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000028976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07230
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15407
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.33300
REMARK 200 R SYM FOR SHELL (I) : 0.33300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
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 1DKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM POTASSIUM THIOCYANATE, 20% PEG
REMARK 280 3350, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.66900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.65000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.50350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.65000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.83450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.65000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.50350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.65000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.83450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 55.66900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I
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: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 THR A 228
REMARK 465 SER A 229
REMARK 465 THR A 251
REMARK 465 GLU A 252
REMARK 465 THR A 253
REMARK 465 TYR A 254
REMARK 465 VAL A 255
REMARK 465 GLU A 256
REMARK 465 ALA A 257
REMARK 465 ASN A 258
REMARK 465 MET A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 ASN A 262
REMARK 465 PRO A 263
REMARK 465 SER A 264
REMARK 465 ALA A 462
REMARK 465 PRO A 463
REMARK 465 HIS A 464
REMARK 465 GLN A 465
REMARK 465 ALA A 466
REMARK 465 THR A 467
REMARK 465 MET B 153
REMARK 465 SER B 154
REMARK 465 LYS B 155
REMARK 465 GLU B 156
REMARK 465 SER B 157
REMARK 465 VAL B 158
REMARK 465 ARG B 159
REMARK 465 ASN B 160
REMARK 465 ASP B 161
REMARK 465 ARG B 162
REMARK 465 ASN B 163
REMARK 465 LYS B 164
REMARK 465 LYS B 165
REMARK 465 LYS B 166
REMARK 465 LYS B 167
REMARK 465 GLU B 168
REMARK 465 VAL B 169
REMARK 465 PRO B 170
REMARK 465 LYS B 171
REMARK 465 PRO B 172
REMARK 465 GLU B 173
REMARK 465 CYS B 174
REMARK 465 SER B 175
REMARK 465 GLU B 176
REMARK 465 ASN B 416
REMARK 465 SER B 417
REMARK 465 GLU B 418
REMARK 465 GLY B 419
REMARK 465 LEU B 420
REMARK 465 ASP B 421
REMARK 465 SER I 1482
REMARK 465 SER I 1483
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 233 CD OE1 OE2
REMARK 480 LYS A 239 CE NZ
REMARK 480 GLU A 248 CD OE1 OE2
REMARK 480 LYS A 250 CG CD CE NZ
REMARK 480 SER A 265 OG
REMARK 480 ASN A 267 CG OD1 ND2
REMARK 480 GLN A 275 CD OE1 NE2
REMARK 480 GLU A 286 CD OE1 OE2
REMARK 480 LYS A 289 CG CD CE NZ
REMARK 480 LEU A 299 CD1 CD2
REMARK 480 ARG A 307 NE CZ NH1 NH2
REMARK 480 LYS A 326 CG CD CE NZ
REMARK 480 LEU A 335 CD1 CD2
REMARK 480 LYS A 369 NZ
REMARK 480 LYS A 386 CG CD CE NZ
REMARK 480 LYS A 410 CE NZ
REMARK 480 LYS A 412 CE NZ
REMARK 480 LYS A 422 CE NZ
REMARK 480 LYS A 436 CE NZ
REMARK 480 GLU A 439 CD OE1 OE2
REMARK 480 LYS A 445 CG CD CE NZ
REMARK 480 LEU A 446 CG CD1 CD2
REMARK 480 THR A 450 OG1 CG2
REMARK 480 MET A 457 SD CE
REMARK 480 GLU A 458 CG CD OE1 OE2
REMARK 480 GLU A 461 CD OE1 OE2
REMARK 480 THR B 179 OG1 CG2
REMARK 480 GLU B 183 CD OE1 OE2
REMARK 480 LYS B 190 CD CE NZ
REMARK 480 GLN B 204 CG CD OE1 NE2
REMARK 480 GLU B 215 CG CD OE1 OE2
REMARK 480 GLN B 216 CD OE1 NE2
REMARK 480 ASP B 223 OD1 OD2
REMARK 480 LYS B 227 NZ
REMARK 480 LYS B 234 NZ
REMARK 480 GLU B 241 CD OE1 OE2
REMARK 480 GLU B 320 CD OE1 OE2
REMARK 480 LYS B 390 CD CE NZ
REMARK 480 GLU B 393 CG CD OE1 OE2
REMARK 480 LYS I 1471 CG CD CE NZ
REMARK 480 LYS I 1473 CG CD CE NZ
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 MET A 235 73.64 -156.45
REMARK 500 LEU A 358 -70.30 -111.19
REMARK 500 LEU A 441 42.57 -86.73
REMARK 500 ASP A 449 -106.39 -116.77
REMARK 500 THR A 450 95.20 -160.29
REMARK 500 ILE A 452 18.27 54.84
REMARK 500 PHE B 199 91.91 -160.22
REMARK 500 GLN B 204 40.81 -77.41
REMARK 500 GLU B 215 -72.13 -92.43
REMARK 500 LEU B 220 131.90 -172.03
REMARK 500 ASP B 338 40.27 -95.66
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 754 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE REA B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DKF RELATED DB: PDB
REMARK 900 THE HOMAN RAR-ALPHA LIGAND-BINDING DOMAIN BOUND TO BMS614 AND MOUSE
REMARK 900 RXR-ALPHA LIGAND-BINDING DOMAIN BOUND (F318A) BOUND TO OLEIC ACID.
REMARK 900 RELATED ID: 1XDK RELATED DB: PDB
REMARK 900 THE MOUSE RAR-BETA LIGAND-BINDING DOMAIN BOUND TO 9-CIS RETINOIC
REMARK 900 ACID AND MOUSE RXR-ALPHA LIGAND-BINDING DOMAIN BOUND BOUND TO 9-CIS
REMARK 900 RETINOIC ACID COMPLEXED WITH THE PEPTIDES OF TRAP220.
DBREF 3A9E A 228 467 UNP P28700 RXRA_MOUSE 228 467
DBREF 3A9E B 153 421 UNP P10276 RARA_HUMAN 153 421
DBREF 3A9E I 1471 1483 UNP Q15596 NCOA2_HUMAN 686 698
SEQRES 1 A 240 THR SER SER ALA ASN GLU ASP MET PRO VAL GLU LYS ILE
SEQRES 2 A 240 LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR
SEQRES 3 A 240 TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO
SEQRES 4 A 240 ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS
SEQRES 5 A 240 GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO
SEQRES 6 A 240 HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU
SEQRES 7 A 240 LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE
SEQRES 8 A 240 SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU
SEQRES 9 A 240 ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER
SEQRES 10 A 240 ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU
SEQRES 11 A 240 LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR
SEQRES 12 A 240 GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO
SEQRES 13 A 240 ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA
SEQRES 14 A 240 LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS
SEQRES 15 A 240 LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS
SEQRES 16 A 240 LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU
SEQRES 17 A 240 LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY
SEQRES 18 A 240 ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU
SEQRES 19 A 240 ALA PRO HIS GLN ALA THR
SEQRES 1 B 269 MET SER LYS GLU SER VAL ARG ASN ASP ARG ASN LYS LYS
SEQRES 2 B 269 LYS LYS GLU VAL PRO LYS PRO GLU CYS SER GLU SER TYR
SEQRES 3 B 269 THR LEU THR PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL
SEQRES 4 B 269 ARG LYS ALA HIS GLN GLU THR PHE PRO ALA LEU CYS GLN
SEQRES 5 B 269 LEU GLY LYS TYR THR THR ASN ASN SER SER GLU GLN ARG
SEQRES 6 B 269 VAL SER LEU ASP ILE ASP LEU TRP ASP LYS PHE SER GLU
SEQRES 7 B 269 LEU SER THR LYS CYS ILE ILE LYS THR VAL GLU PHE ALA
SEQRES 8 B 269 LYS GLN LEU PRO GLY PHE THR THR LEU THR ILE ALA ASP
SEQRES 9 B 269 GLN ILE THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU
SEQRES 10 B 269 ILE LEU ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP
SEQRES 11 B 269 THR MET THR PHE SER ASP GLY LEU THR LEU ASN ARG THR
SEQRES 12 B 269 GLN MET HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU
SEQRES 13 B 269 VAL PHE ALA PHE ALA ASN GLN LEU LEU PRO LEU GLU MET
SEQRES 14 B 269 ASP ASP ALA GLU THR GLY LEU LEU SER ALA ILE CYS LEU
SEQRES 15 B 269 ILE CYS GLY ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG
SEQRES 16 B 269 VAL ASP MET LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS
SEQRES 17 B 269 VAL TYR VAL ARG LYS ARG ARG PRO SER ARG PRO HIS MET
SEQRES 18 B 269 PHE PRO LYS MET LEU MET LYS ILE THR ASP LEU ARG SER
SEQRES 19 B 269 ILE SER ALA LYS GLY ALA GLU ARG VAL ILE THR LEU LYS
SEQRES 20 B 269 MET GLU ILE PRO GLY SER MET PRO PRO LEU ILE GLN GLU
SEQRES 21 B 269 MET LEU GLU ASN SER GLU GLY LEU ASP
SEQRES 1 I 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET 754 A 1 29
HET REA B 1 22
HETNAM 754 (2E,4E,6Z)-3-METHYL-7-(5,5,8,8-TETRAMETHYL-3-PROPOXY-5,
HETNAM 2 754 6,7,8-TETRAHYDRONAPHTHALEN-2-YL)OCTA-2,4,6-TRIENOIC
HETNAM 3 754 ACID
HETNAM REA RETINOIC ACID
FORMUL 4 754 C26 H36 O3
FORMUL 5 REA C20 H28 O2
FORMUL 6 HOH *115(H2 O)
HELIX 1 1 PRO A 236 VAL A 247 1 12
HELIX 2 2 ASP A 268 ARG A 290 1 23
HELIX 3 3 PRO A 298 SER A 322 1 25
HELIX 4 4 ARG A 339 ALA A 345 1 7
HELIX 5 5 VAL A 347 LEU A 358 1 12
HELIX 6 6 LEU A 358 MET A 365 1 8
HELIX 7 7 ASP A 368 PHE A 381 1 14
HELIX 8 8 ASN A 390 TYR A 413 1 24
HELIX 9 9 GLY A 418 LEU A 425 1 8
HELIX 10 10 ARG A 426 LEU A 441 1 16
HELIX 11 11 LEU A 441 LEU A 446 1 6
HELIX 12 12 THR A 450 ILE A 452 5 3
HELIX 13 13 ASP A 453 GLU A 461 1 9
HELIX 14 14 THR B 181 PHE B 199 1 19
HELIX 15 15 ASP B 221 GLN B 245 1 25
HELIX 16 16 THR B 253 CYS B 274 1 22
HELIX 17 17 ARG B 294 GLY B 301 1 8
HELIX 18 18 PHE B 302 PRO B 304 5 3
HELIX 19 19 LEU B 305 LEU B 317 1 13
HELIX 20 20 PRO B 318 GLU B 320 5 3
HELIX 21 21 ASP B 322 ILE B 335 1 14
HELIX 22 22 GLN B 344 ARG B 367 1 24
HELIX 23 23 HIS B 372 ILE B 402 1 31
HELIX 24 24 PRO B 407 GLU B 415 1 9
HELIX 25 25 HIS I 1472 ASP I 1481 1 10
SHEET 1 A 2 GLY A 328 LEU A 330 0
SHEET 2 A 2 HIS A 336 HIS A 338 -1 O VAL A 337 N ILE A 329
SHEET 1 B 3 TYR B 277 THR B 278 0
SHEET 2 B 3 THR B 283 THR B 285 -1 O THR B 283 N THR B 278
SHEET 3 B 3 THR B 291 ASN B 293 -1 O LEU B 292 N MET B 284
SITE 1 AC1 11 ILE A 273 ALA A 276 GLN A 280 TRP A 310
SITE 2 AC1 11 PHE A 318 ARG A 321 LEU A 331 ALA A 332
SITE 3 AC1 11 ILE A 350 CYS A 437 LEU A 441
SITE 1 AC2 9 HOH B 40 PHE B 228 CYS B 235 LEU B 269
SITE 2 AC2 9 ARG B 276 PHE B 286 SER B 287 VAL B 395
SITE 3 AC2 9 LEU B 398
CRYST1 105.300 105.300 111.338 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009497 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008982 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
