HEADER TRANSCRIPTION/DNA 19-DEC-16 5UAN
TITLE CRYSTAL STRUCTURE OF MULTI-DOMAIN RAR-BETA-RXR-ALPHA HETERODIMER ON
TITLE 2 DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 98-462;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR SUBFAMILY 2 GROUP B MEMBER 1,RETINOID X
COMPND 6 RECEPTOR ALPHA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RETINOIC ACID RECEPTOR BETA;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 98-462;
COMPND 12 SYNONYM: RAR-BETA,HBV-ACTIVATED PROTEIN,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 13 GROUP B MEMBER 2,RAR-EPSILON;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 17 CHAIN: C, D;
COMPND 18 FRAGMENT: UNP RESIDUES 687-696;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: DNA (5'-
COMPND 22 D(*CP*TP*AP*GP*GP*TP*CP*AP*AP*AP*GP*GP*TP*CP*AP*GP*C)-3');
COMPND 23 CHAIN: E;
COMPND 24 ENGINEERED: YES;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: DNA (5'-
COMPND 27 D(*GP*CP*TP*GP*AP*CP*CP*TP*TP*TP*GP*AP*CP*CP*TP*AP*G)-3');
COMPND 28 CHAIN: F;
COMPND 29 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RXRA, NR2B1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: RARB, HAP, NR1B2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 MOL_ID: 4;
SOURCE 21 SYNTHETIC: YES;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 MOL_ID: 5;
SOURCE 26 SYNTHETIC: YES;
SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 28 ORGANISM_COMMON: HUMAN;
SOURCE 29 ORGANISM_TAXID: 9606
KEYWDS NUCLEAR RECEPTORS, TRANSCRIPTION, PROTEIN-DNA COMPLEX, TRANSCRIPTION-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CHANDRA,D.WU,Y.KIM,F.RASTINEJAD
REVDAT 3 04-OCT-23 5UAN 1 REMARK
REVDAT 2 18-APR-18 5UAN 1 JRNL
REVDAT 1 18-OCT-17 5UAN 0
JRNL AUTH V.CHANDRA,D.WU,S.LI,N.POTLURI,Y.KIM,F.RASTINEJAD
JRNL TITL THE QUATERNARY ARCHITECTURE OF RAR BETA-RXR ALPHA
JRNL TITL 2 HETERODIMER FACILITATES DOMAIN-DOMAIN SIGNAL TRANSMISSION.
JRNL REF NAT COMMUN V. 8 868 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29021580
JRNL DOI 10.1038/S41467-017-00981-Y
REMARK 2
REMARK 2 RESOLUTION. 3.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 60.7
REMARK 3 NUMBER OF REFLECTIONS : 13381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1341
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 47.4089 - 7.5480 0.97 1928 218 0.1908 0.2201
REMARK 3 2 7.5480 - 5.9949 0.99 1978 227 0.2439 0.2897
REMARK 3 3 5.9949 - 5.2382 0.93 1813 191 0.2325 0.2635
REMARK 3 4 5.2382 - 4.7597 0.80 1580 193 0.2029 0.2872
REMARK 3 5 4.7597 - 4.4189 0.67 1317 134 0.2084 0.2956
REMARK 3 6 4.4189 - 4.1585 0.54 1093 128 0.2064 0.2696
REMARK 3 7 4.1585 - 3.9503 0.45 892 94 0.2309 0.2829
REMARK 3 8 3.9503 - 3.7785 0.33 669 67 0.2312 0.2627
REMARK 3 9 3.7785 - 3.6330 0.23 457 54 0.2680 0.3162
REMARK 3 10 3.6330 - 3.5077 0.16 313 35 0.3054 0.3477
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.003 5745
REMARK 3 ANGLE : 0.546 7848
REMARK 3 CHIRALITY : 0.037 882
REMARK 3 PLANARITY : 0.003 881
REMARK 3 DIHEDRAL : 14.372 3394
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): -9.6616 20.0592 -31.9392
REMARK 3 T TENSOR
REMARK 3 T11: 0.0417 T22: 0.2190
REMARK 3 T33: 0.2954 T12: 0.1826
REMARK 3 T13: -0.0296 T23: -0.1120
REMARK 3 L TENSOR
REMARK 3 L11: 1.4051 L22: 1.6757
REMARK 3 L33: 1.9401 L12: -0.1855
REMARK 3 L13: 0.3545 L23: -0.7645
REMARK 3 S TENSOR
REMARK 3 S11: -0.5157 S12: -0.0691 S13: -0.0527
REMARK 3 S21: 0.4562 S22: 0.4112 S23: -0.2450
REMARK 3 S31: -0.1285 S32: -0.0068 S33: 0.0636
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 5UAN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225577.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9550
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 52.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.43100
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: PHASER
REMARK 200 STARTING MODEL: 1DSZ, 1XDK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, PEG300, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.70150
REMARK 290 SMTRY3 2 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 98
REMARK 465 ASN A 99
REMARK 465 PRO A 100
REMARK 465 VAL A 101
REMARK 465 SER A 102
REMARK 465 SER A 103
REMARK 465 SER A 104
REMARK 465 GLU A 105
REMARK 465 ASP A 106
REMARK 465 ILE A 107
REMARK 465 LYS A 108
REMARK 465 PRO A 109
REMARK 465 PRO A 110
REMARK 465 LEU A 111
REMARK 465 GLY A 112
REMARK 465 LEU A 113
REMARK 465 ASN A 114
REMARK 465 GLY A 115
REMARK 465 VAL A 116
REMARK 465 LEU A 117
REMARK 465 LYS A 118
REMARK 465 VAL A 119
REMARK 465 PRO A 120
REMARK 465 ALA A 121
REMARK 465 HIS A 122
REMARK 465 PRO A 123
REMARK 465 SER A 124
REMARK 465 GLY A 125
REMARK 465 ASN A 126
REMARK 465 MET A 127
REMARK 465 ALA A 128
REMARK 465 SER A 129
REMARK 465 PHE A 130
REMARK 465 THR A 131
REMARK 465 LYS A 132
REMARK 465 LEU A 167
REMARK 465 THR A 168
REMARK 465 TYR A 169
REMARK 465 THR A 170
REMARK 465 CYS A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 ASN A 174
REMARK 465 LYS A 175
REMARK 465 ASP A 176
REMARK 465 ARG A 186
REMARK 465 GLN A 210
REMARK 465 ARG A 211
REMARK 465 GLY A 212
REMARK 465 LYS A 213
REMARK 465 ASP A 214
REMARK 465 ARG A 215
REMARK 465 ASN A 216
REMARK 465 GLU A 217
REMARK 465 ASN A 218
REMARK 465 GLU A 219
REMARK 465 VAL A 220
REMARK 465 GLU A 221
REMARK 465 SER A 222
REMARK 465 THR A 223
REMARK 465 SER A 224
REMARK 465 SER A 225
REMARK 465 PRO A 244
REMARK 465 LYS A 245
REMARK 465 THR A 246
REMARK 465 GLU A 247
REMARK 465 THR A 248
REMARK 465 TYR A 249
REMARK 465 VAL A 250
REMARK 465 GLU A 251
REMARK 465 ALA A 252
REMARK 465 ASN A 253
REMARK 465 MET A 254
REMARK 465 GLY A 255
REMARK 465 LEU A 256
REMARK 465 ASN A 257
REMARK 465 PRO A 258
REMARK 465 SER A 259
REMARK 465 SER A 260
REMARK 465 PRO A 261
REMARK 465 ASN A 262
REMARK 465 ASP A 263
REMARK 465 PRO A 458
REMARK 465 HIS A 459
REMARK 465 GLN A 460
REMARK 465 MET A 461
REMARK 465 THR A 462
REMARK 465 MET B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 SER B 55
REMARK 465 HIS B 56
REMARK 465 HIS B 57
REMARK 465 HIS B 58
REMARK 465 HIS B 59
REMARK 465 HIS B 60
REMARK 465 HIS B 61
REMARK 465 SER B 62
REMARK 465 SER B 63
REMARK 465 GLY B 64
REMARK 465 LEU B 65
REMARK 465 VAL B 66
REMARK 465 PRO B 67
REMARK 465 ARG B 68
REMARK 465 GLY B 69
REMARK 465 SER B 70
REMARK 465 HIS B 71
REMARK 465 MET B 72
REMARK 465 PRO B 73
REMARK 465 PRO B 74
REMARK 465 PRO B 75
REMARK 465 ARG B 76
REMARK 465 VAL B 77
REMARK 465 TYR B 78
REMARK 465 LYS B 79
REMARK 465 ASN B 153
REMARK 465 ASP B 154
REMARK 465 ARG B 155
REMARK 465 ASN B 156
REMARK 465 LYS B 157
REMARK 465 LYS B 158
REMARK 465 LYS B 159
REMARK 465 LYS B 160
REMARK 465 GLU B 161
REMARK 465 THR B 162
REMARK 465 SER B 163
REMARK 465 LYS B 164
REMARK 465 GLN B 165
REMARK 465 GLU B 166
REMARK 465 CYS B 167
REMARK 465 THR B 168
REMARK 465 GLU B 169
REMARK 465 SER B 170
REMARK 465 TYR B 171
REMARK 465 GLU B 172
REMARK 465 MET B 173
REMARK 465 ASN B 409
REMARK 465 SER B 410
REMARK 465 GLU B 411
REMARK 465 GLY B 412
REMARK 465 HIS B 413
REMARK 465 GLU B 414
REMARK 465 PRO B 415
REMARK 465 LEU B 416
REMARK 465 THR B 417
REMARK 465 PRO B 418
REMARK 465 SER B 419
REMARK 465 SER B 420
REMARK 465 SER B 421
REMARK 465 GLY B 422
REMARK 465 ASN B 423
REMARK 465 THR B 424
REMARK 465 ALA B 425
REMARK 465 GLU B 426
REMARK 465 HIS B 427
REMARK 465 SER B 428
REMARK 465 PRO B 429
REMARK 465 SER B 430
REMARK 465 ILE B 431
REMARK 465 SER B 432
REMARK 465 PRO B 433
REMARK 465 SER B 434
REMARK 465 SER B 435
REMARK 465 VAL B 436
REMARK 465 GLU B 437
REMARK 465 ASN B 438
REMARK 465 SER B 439
REMARK 465 GLY B 440
REMARK 465 VAL B 441
REMARK 465 SER B 442
REMARK 465 GLN B 443
REMARK 465 SER B 444
REMARK 465 PRO B 445
REMARK 465 LEU B 446
REMARK 465 VAL B 447
REMARK 465 GLN B 448
REMARK 465 ASP D 696
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 OG SER B 280 O1 REA B 503 2.19
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 GLN A 183 25.78 -143.82
REMARK 500 TYR A 189 -71.45 -61.79
REMARK 500 GLU A 207 -162.80 -76.23
REMARK 500 ASN A 227 -153.90 -77.03
REMARK 500 GLU A 228 14.09 -140.19
REMARK 500 LYS A 321 -74.53 -86.13
REMARK 500 ARG A 334 -137.91 69.23
REMARK 500 ALA A 340 40.86 -93.46
REMARK 500 LEU A 353 -62.43 -123.88
REMARK 500 TYR A 408 76.48 -119.60
REMARK 500 ARG B 119 -144.51 -126.07
REMARK 500 CYS B 123 109.05 -43.09
REMARK 500 ASN B 126 -146.11 -147.90
REMARK 500 ASN B 131 -124.91 62.63
REMARK 500 ARG B 132 -57.81 71.66
REMARK 500 PHE B 192 96.62 -164.58
REMARK 500 ASP B 208 -80.04 -90.18
REMARK 500 LEU B 213 140.69 -172.02
REMARK 500 PRO B 364 31.90 -82.16
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 135 SG
REMARK 620 2 CYS A 138 SG 108.7
REMARK 620 3 CYS A 152 SG 116.6 102.0
REMARK 620 4 CYS A 155 SG 117.3 109.3 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 177 SG
REMARK 620 2 CYS A 187 SG 108.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 81 SG
REMARK 620 2 CYS B 84 SG 112.5
REMARK 620 3 CYS B 98 SG 108.7 103.2
REMARK 620 4 CYS B 101 SG 124.6 101.8 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 117 SG
REMARK 620 2 CYS B 123 SG 165.5
REMARK 620 3 CYS B 133 SG 99.0 89.2
REMARK 620 4 CYS B 136 SG 84.1 95.4 147.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9CR A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue REA B 503
DBREF 5UAN A 98 462 UNP P19793 RXRA_HUMAN 98 462
DBREF 5UAN B 73 448 UNP P10826 RARB_HUMAN 80 455
DBREF 5UAN C 687 696 UNP E7EWM1 E7EWM1_HUMAN 687 696
DBREF 5UAN D 687 696 UNP E7EWM1 E7EWM1_HUMAN 687 696
DBREF 5UAN E 1 17 PDB 5UAN 5UAN 1 17
DBREF 5UAN F 1 17 PDB 5UAN 5UAN 1 17
SEQADV 5UAN MET B 52 UNP P10826 INITIATING METHIONINE
SEQADV 5UAN GLY B 53 UNP P10826 EXPRESSION TAG
SEQADV 5UAN SER B 54 UNP P10826 EXPRESSION TAG
SEQADV 5UAN SER B 55 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 56 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 57 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 58 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 59 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 60 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 61 UNP P10826 EXPRESSION TAG
SEQADV 5UAN SER B 62 UNP P10826 EXPRESSION TAG
SEQADV 5UAN SER B 63 UNP P10826 EXPRESSION TAG
SEQADV 5UAN GLY B 64 UNP P10826 EXPRESSION TAG
SEQADV 5UAN LEU B 65 UNP P10826 EXPRESSION TAG
SEQADV 5UAN VAL B 66 UNP P10826 EXPRESSION TAG
SEQADV 5UAN PRO B 67 UNP P10826 EXPRESSION TAG
SEQADV 5UAN ARG B 68 UNP P10826 EXPRESSION TAG
SEQADV 5UAN GLY B 69 UNP P10826 EXPRESSION TAG
SEQADV 5UAN SER B 70 UNP P10826 EXPRESSION TAG
SEQADV 5UAN HIS B 71 UNP P10826 EXPRESSION TAG
SEQADV 5UAN MET B 72 UNP P10826 EXPRESSION TAG
SEQRES 1 A 365 MET ASN PRO VAL SER SER SER GLU ASP ILE LYS PRO PRO
SEQRES 2 A 365 LEU GLY LEU ASN GLY VAL LEU LYS VAL PRO ALA HIS PRO
SEQRES 3 A 365 SER GLY ASN MET ALA SER PHE THR LYS HIS ILE CYS ALA
SEQRES 4 A 365 ILE CYS GLY ASP ARG SER SER GLY LYS HIS TYR GLY VAL
SEQRES 5 A 365 TYR SER CYS GLU GLY CYS LYS GLY PHE PHE LYS ARG THR
SEQRES 6 A 365 VAL ARG LYS ASP LEU THR TYR THR CYS ARG ASP ASN LYS
SEQRES 7 A 365 ASP CYS LEU ILE ASP LYS ARG GLN ARG ASN ARG CYS GLN
SEQRES 8 A 365 TYR CYS ARG TYR GLN LYS CYS LEU ALA MET GLY MET LYS
SEQRES 9 A 365 ARG GLU ALA VAL GLN GLU GLU ARG GLN ARG GLY LYS ASP
SEQRES 10 A 365 ARG ASN GLU ASN GLU VAL GLU SER THR SER SER ALA ASN
SEQRES 11 A 365 GLU ASP MET PRO VAL GLU ARG ILE LEU GLU ALA GLU LEU
SEQRES 12 A 365 ALA VAL GLU PRO LYS THR GLU THR TYR VAL GLU ALA ASN
SEQRES 13 A 365 MET GLY LEU ASN PRO SER SER PRO ASN ASP PRO VAL THR
SEQRES 14 A 365 ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU PHE THR LEU
SEQRES 15 A 365 VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE SER GLU LEU
SEQRES 16 A 365 PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG ALA GLY TRP
SEQRES 17 A 365 ASN GLU LEU LEU ILE ALA SER PHE SER HIS ARG SER ILE
SEQRES 18 A 365 ALA VAL LYS ASP GLY ILE LEU LEU ALA THR GLY LEU HIS
SEQRES 19 A 365 VAL HIS ARG ASN SER ALA HIS SER ALA GLY VAL GLY ALA
SEQRES 20 A 365 ILE PHE ASP ARG VAL LEU THR GLU LEU VAL SER LYS MET
SEQRES 21 A 365 ARG ASP MET GLN MET ASP LYS THR GLU LEU GLY CYS LEU
SEQRES 22 A 365 ARG ALA ILE VAL LEU PHE ASN PRO ASP SER LYS GLY LEU
SEQRES 23 A 365 SER ASN PRO ALA GLU VAL GLU ALA LEU ARG GLU LYS VAL
SEQRES 24 A 365 TYR ALA SER LEU GLU ALA TYR CYS LYS HIS LYS TYR PRO
SEQRES 25 A 365 GLU GLN PRO GLY ARG PHE ALA LYS LEU LEU LEU ARG LEU
SEQRES 26 A 365 PRO ALA LEU ARG SER ILE GLY LEU LYS CYS LEU GLU HIS
SEQRES 27 A 365 LEU PHE PHE PHE LYS LEU ILE GLY ASP THR PRO ILE ASP
SEQRES 28 A 365 THR PHE LEU MET GLU MET LEU GLU ALA PRO HIS GLN MET
SEQRES 29 A 365 THR
SEQRES 1 B 397 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 397 LEU VAL PRO ARG GLY SER HIS MET PRO PRO PRO ARG VAL
SEQRES 3 B 397 TYR LYS PRO CYS PHE VAL CYS GLN ASP LYS SER SER GLY
SEQRES 4 B 397 TYR HIS TYR GLY VAL SER ALA CYS GLU GLY CYS LYS GLY
SEQRES 5 B 397 PHE PHE ARG ARG SER ILE GLN LYS ASN MET ILE TYR THR
SEQRES 6 B 397 CYS HIS ARG ASP LYS ASN CYS VAL ILE ASN LYS VAL THR
SEQRES 7 B 397 ARG ASN ARG CYS GLN TYR CYS ARG LEU GLN LYS CYS PHE
SEQRES 8 B 397 GLU VAL GLY MET SER LYS GLU SER VAL ARG ASN ASP ARG
SEQRES 9 B 397 ASN LYS LYS LYS LYS GLU THR SER LYS GLN GLU CYS THR
SEQRES 10 B 397 GLU SER TYR GLU MET THR ALA GLU LEU ASP ASP LEU THR
SEQRES 11 B 397 GLU LYS ILE ARG LYS ALA HIS GLN GLU THR PHE PRO SER
SEQRES 12 B 397 LEU CYS GLN LEU GLY LYS TYR THR THR ASN SER SER ALA
SEQRES 13 B 397 ASP HIS ARG VAL ARG LEU ASP LEU GLY LEU TRP ASP LYS
SEQRES 14 B 397 PHE SER GLU LEU ALA THR LYS CYS ILE ILE LYS ILE VAL
SEQRES 15 B 397 GLU PHE ALA LYS ARG LEU PRO GLY PHE THR GLY LEU THR
SEQRES 16 B 397 ILE ALA ASP GLN ILE THR LEU LEU LYS ALA ALA CYS LEU
SEQRES 17 B 397 ASP ILE LEU ILE LEU ARG ILE CYS THR ARG TYR THR PRO
SEQRES 18 B 397 GLU GLN ASP THR MET THR PHE SER ASP GLY LEU THR LEU
SEQRES 19 B 397 ASN ARG THR GLN MET HIS ASN ALA GLY PHE GLY PRO LEU
SEQRES 20 B 397 THR ASP LEU VAL PHE THR PHE ALA ASN GLN LEU LEU PRO
SEQRES 21 B 397 LEU GLU MET ASP ASP THR GLU THR GLY LEU LEU SER ALA
SEQRES 22 B 397 ILE CYS LEU ILE CYS GLY ASP ARG GLN ASP LEU GLU GLU
SEQRES 23 B 397 PRO THR LYS VAL ASP LYS LEU GLN GLU PRO LEU LEU GLU
SEQRES 24 B 397 ALA LEU LYS ILE TYR ILE ARG LYS ARG ARG PRO SER LYS
SEQRES 25 B 397 PRO HIS MET PHE PRO LYS ILE LEU MET LYS ILE THR ASP
SEQRES 26 B 397 LEU ARG SER ILE SER ALA LYS GLY ALA GLU ARG VAL ILE
SEQRES 27 B 397 THR LEU LYS MET GLU ILE PRO GLY SER MET PRO PRO LEU
SEQRES 28 B 397 ILE GLN GLU MET LEU GLU ASN SER GLU GLY HIS GLU PRO
SEQRES 29 B 397 LEU THR PRO SER SER SER GLY ASN THR ALA GLU HIS SER
SEQRES 30 B 397 PRO SER ILE SER PRO SER SER VAL GLU ASN SER GLY VAL
SEQRES 31 B 397 SER GLN SER PRO LEU VAL GLN
SEQRES 1 C 10 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP
SEQRES 1 D 10 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP
SEQRES 1 E 17 DC DT DA DG DG DT DC DA DA DA DG DG DT
SEQRES 2 E 17 DC DA DG DC
SEQRES 1 F 17 DG DC DT DG DA DC DC DT DT DT DG DA DC
SEQRES 2 F 17 DC DT DA DG
HET ZN A 501 1
HET ZN A 502 1
HET 9CR A 503 22
HET ZN B 501 1
HET ZN B 502 1
HET REA B 503 22
HETNAM ZN ZINC ION
HETNAM 9CR (9CIS)-RETINOIC ACID
HETNAM REA RETINOIC ACID
FORMUL 7 ZN 4(ZN 2+)
FORMUL 9 9CR C20 H28 O2
FORMUL 12 REA C20 H28 O2
HELIX 1 AA1 CYS A 152 ASP A 166 1 15
HELIX 2 AA2 GLN A 188 GLY A 199 1 12
HELIX 3 AA3 LYS A 201 VAL A 205 5 5
HELIX 4 AA4 PRO A 231 GLU A 243 1 13
HELIX 5 AA5 VAL A 265 LYS A 284 1 20
HELIX 6 AA6 PRO A 293 GLY A 304 1 12
HELIX 7 AA7 GLY A 304 SER A 317 1 14
HELIX 8 AA8 ARG A 334 HIS A 338 1 5
HELIX 9 AA9 VAL A 342 LEU A 353 1 12
HELIX 10 AB1 LEU A 353 GLN A 361 1 9
HELIX 11 AB2 ASP A 363 PHE A 376 1 14
HELIX 12 AB3 ASN A 385 TYR A 408 1 24
HELIX 13 AB4 GLY A 413 LEU A 420 1 8
HELIX 14 AB5 LEU A 420 GLY A 443 1 24
HELIX 15 AB6 ASP A 448 GLU A 456 1 9
HELIX 16 AB7 CYS B 98 LYS B 111 1 14
HELIX 17 AB8 CYS B 133 GLY B 145 1 13
HELIX 18 AB9 ALA B 175 THR B 191 1 17
HELIX 19 AC1 SER B 194 LEU B 198 5 5
HELIX 20 AC2 ASP B 214 ARG B 238 1 25
HELIX 21 AC3 THR B 246 THR B 268 1 23
HELIX 22 AC4 ARG B 287 GLY B 294 1 8
HELIX 23 AC5 PRO B 297 LEU B 310 1 14
HELIX 24 AC6 ASP B 315 ILE B 328 1 14
HELIX 25 AC7 GLU B 337 ARG B 360 1 24
HELIX 26 AC8 HIS B 365 ILE B 395 1 31
HELIX 27 AC9 PRO B 400 GLU B 408 1 9
HELIX 28 AD1 LYS C 688 LEU C 694 1 7
HELIX 29 AD2 LYS D 688 GLN D 695 1 8
SHEET 1 AA1 2 GLY A 144 HIS A 146 0
SHEET 2 AA1 2 VAL A 149 SER A 151 -1 O VAL A 149 N HIS A 146
SHEET 1 AA2 2 GLY A 323 LEU A 325 0
SHEET 2 AA2 2 HIS A 331 HIS A 333 -1 O VAL A 332 N ILE A 324
SHEET 1 AA3 2 TYR B 91 HIS B 92 0
SHEET 2 AA3 2 VAL B 95 SER B 96 -1 O VAL B 95 N HIS B 92
SHEET 1 AA4 3 TYR B 270 THR B 271 0
SHEET 2 AA4 3 THR B 276 THR B 278 -1 O THR B 276 N THR B 271
SHEET 3 AA4 3 THR B 284 ASN B 286 -1 O LEU B 285 N MET B 277
LINK SG CYS A 135 ZN ZN A 501 1555 1555 2.34
LINK SG CYS A 138 ZN ZN A 501 1555 1555 2.32
LINK SG CYS A 152 ZN ZN A 501 1555 1555 2.32
LINK SG CYS A 155 ZN ZN A 501 1555 1555 2.33
LINK SG CYS A 177 ZN ZN A 502 1555 1555 2.34
LINK SG CYS A 187 ZN ZN A 502 1555 1555 2.31
LINK SG CYS B 81 ZN ZN B 501 1555 1555 2.34
LINK SG CYS B 84 ZN ZN B 501 1555 1555 2.29
LINK SG CYS B 98 ZN ZN B 501 1555 1555 2.30
LINK SG CYS B 101 ZN ZN B 501 1555 1555 2.29
LINK SG CYS B 117 ZN ZN B 502 1555 1555 2.29
LINK SG CYS B 123 ZN ZN B 502 1555 1555 2.34
LINK SG CYS B 133 ZN ZN B 502 1555 1555 2.32
LINK SG CYS B 136 ZN ZN B 502 1555 1555 2.26
SITE 1 AC1 4 CYS A 135 CYS A 138 CYS A 152 CYS A 155
SITE 1 AC2 3 CYS A 177 CYS A 187 CYS A 190
SITE 1 AC3 12 ILE A 268 ALA A 271 ALA A 272 GLN A 275
SITE 2 AC3 12 TRP A 305 LEU A 309 PHE A 313 ARG A 316
SITE 3 AC3 12 LEU A 325 LEU A 326 ALA A 327 CYS A 432
SITE 1 AC4 4 CYS B 81 CYS B 84 CYS B 98 CYS B 101
SITE 1 AC5 4 CYS B 117 CYS B 123 CYS B 133 CYS B 136
SITE 1 AC6 8 ALA B 225 CYS B 228 LEU B 262 ILE B 263
SITE 2 AC6 8 ILE B 266 PHE B 279 SER B 280 GLY B 294
CRYST1 52.470 77.403 112.113 90.00 90.37 90.00 P 1 21 1 4
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 0.019059 0.000000 0.000123 0.00000
SCALE2 0.000000 0.012919 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008920 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
