HEADER TRANSCRIPTION 08-JAN-14 4OC7
TITLE RETINOIC ACID RECEPTOR ALPHA IN COMPLEX WITH (E)-3-(3'-ALLYL-6-
TITLE 2 HYDROXY-[1,1'-BIPHENYL]-3-YL)ACRYLIC ACID AND A FRAGMENT OF THE
TITLE 3 COACTIVATOR TIF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 223-462);
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: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: NUCLEAR RECEPTOR INTERACTION MOTIF 2 (RESIDUES 686-698);
COMPND 12 SYNONYM: NCOA-2, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75, BHLHE75,
COMPND 13 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2, HTIF2;
COMPND 14 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: NR2B1, RXRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS LIGAND BINDING DOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEYSEN,M.SCHEEPSTRA,L.BRUNSVELD,L.G.MILROY,C.OTTMANN
REVDAT 4 28-FEB-24 4OC7 1 REMARK
REVDAT 3 17-AUG-22 4OC7 1 REMARK SEQADV
REVDAT 2 22-NOV-17 4OC7 1 REMARK
REVDAT 1 08-OCT-14 4OC7 0
JRNL AUTH M.SCHEEPSTRA,L.NIETO,A.K.HIRSCH,S.FUCHS,S.LEYSEN,C.V.LAM,
JRNL AUTH 2 L.IN HET PANHUIS,C.A.VAN BOECKEL,H.WIENK,R.BOELENS,
JRNL AUTH 3 C.OTTMANN,L.G.MILROY,L.BRUNSVELD
JRNL TITL A NATURAL-PRODUCT SWITCH FOR A DYNAMIC PROTEIN INTERFACE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 53 6443 2014
JRNL REFN ISSN 1433-7851
JRNL PMID 24821627
JRNL DOI 10.1002/ANIE.201403773
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 9256
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670
REMARK 3 FREE R VALUE TEST SET COUNT : 432
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 47.7766 - 3.6053 1.00 3095 144 0.1636 0.1999
REMARK 3 2 3.6053 - 2.8617 1.00 2916 146 0.2622 0.3043
REMARK 3 3 2.8617 - 2.5000 0.98 2813 142 0.2857 0.3919
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.10
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 : 0.004 1826
REMARK 3 ANGLE : 0.750 2467
REMARK 3 CHIRALITY : 0.030 281
REMARK 3 PLANARITY : 0.003 314
REMARK 3 DIHEDRAL : 15.450 692
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4OC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9327
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 47.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA HEPES PH 7.5, 20% PEG 2000
REMARK 280 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 55.03750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.77700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.77700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.55625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.77700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.77700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.51875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.77700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.77700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 82.55625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.77700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.77700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.51875
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 55.03750
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 67.55400
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -67.55400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 220.15000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 209
REMARK 465 SER A 210
REMARK 465 HIS A 211
REMARK 465 MET A 212
REMARK 465 THR A 213
REMARK 465 SER A 214
REMARK 465 SER A 215
REMARK 465 ALA A 216
REMARK 465 ASN A 217
REMARK 465 GLU A 218
REMARK 465 GLY A 219
REMARK 465 SER A 220
REMARK 465 HIS A 221
REMARK 465 MET A 222
REMARK 465 THR A 223
REMARK 465 SER A 224
REMARK 465 SER A 225
REMARK 465 ALA A 226
REMARK 465 ASN A 227
REMARK 465 GLU A 228
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 HIS A 459
REMARK 465 GLN A 460
REMARK 465 MET A 461
REMARK 465 THR A 462
REMARK 465 LYS B 471
REMARK 465 SER B 482
REMARK 465 SER B 483
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 HIS A 288 -0.01 71.18
REMARK 500 ASP A 322 59.67 29.48
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 2QO A 501
DBREF 4OC7 A 223 462 UNP P19793 RXRA_HUMAN 223 462
DBREF 4OC7 B 471 483 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 4OC7 GLY A 209 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 SER A 210 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 HIS A 211 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 MET A 212 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 THR A 213 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 SER A 214 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 SER A 215 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 ALA A 216 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 ASN A 217 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 GLU A 218 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 GLY A 219 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 SER A 220 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 HIS A 221 UNP P19793 EXPRESSION TAG
SEQADV 4OC7 MET A 222 UNP P19793 EXPRESSION TAG
SEQRES 1 A 254 GLY SER HIS MET THR SER SER ALA ASN GLU GLY SER HIS
SEQRES 2 A 254 MET THR SER SER ALA ASN GLU ASP MET PRO VAL GLU ARG
SEQRES 3 A 254 ILE LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU
SEQRES 4 A 254 THR TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER
SEQRES 5 A 254 PRO ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP
SEQRES 6 A 254 LYS GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE
SEQRES 7 A 254 PRO HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE
SEQRES 8 A 254 LEU LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER
SEQRES 9 A 254 PHE SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU
SEQRES 10 A 254 LEU ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS
SEQRES 11 A 254 SER ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR
SEQRES 12 A 254 GLU LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS
SEQRES 13 A 254 THR GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN
SEQRES 14 A 254 PRO ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU
SEQRES 15 A 254 ALA LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR
SEQRES 16 A 254 CYS LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA
SEQRES 17 A 254 LYS LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY
SEQRES 18 A 254 LEU LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE
SEQRES 19 A 254 GLY ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU
SEQRES 20 A 254 GLU ALA PRO HIS GLN MET THR
SEQRES 1 B 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET 2QO A 501 21
HETNAM 2QO (2E)-3-[6-HYDROXY-3'-(PROP-2-EN-1-YL)BIPHENYL-3-
HETNAM 2 2QO YL]PROP-2-ENOIC ACID
HETSYN 2QO (E)-3-(3'-ALLYL-6-HYDROXY-[1,1'-BIPHENYL]-3-YL)ACRYLIC
HETSYN 2 2QO ACID
FORMUL 3 2QO C18 H16 O3
FORMUL 4 HOH *6(H2 O)
HELIX 1 1 PRO A 231 VAL A 242 1 12
HELIX 2 2 ASP A 263 ARG A 285 1 23
HELIX 3 3 PRO A 293 SER A 317 1 25
HELIX 4 4 ARG A 334 SER A 339 1 6
HELIX 5 5 VAL A 342 LEU A 353 1 12
HELIX 6 6 LEU A 353 GLN A 361 1 9
HELIX 7 7 ASP A 363 PHE A 376 1 14
HELIX 8 8 ASN A 385 TYR A 408 1 24
HELIX 9 9 GLY A 413 LEU A 420 1 8
HELIX 10 10 ARG A 421 GLY A 443 1 23
HELIX 11 11 ASP A 448 LEU A 455 1 8
HELIX 12 12 LYS B 473 ASP B 481 1 9
SHEET 1 A 2 GLY A 323 LEU A 325 0
SHEET 2 A 2 HIS A 331 HIS A 333 -1 O VAL A 332 N ILE A 324
SITE 1 AC1 10 ILE A 268 ALA A 271 GLN A 275 ASN A 306
SITE 2 AC1 10 PHE A 313 ARG A 316 ILE A 324 LEU A 326
SITE 3 AC1 10 ALA A 327 CYS A 432
CRYST1 67.554 67.554 110.075 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 0.014803 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009085 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
