HEADER TRANSCRIPTION REGULATION 18-JUN-03 1PQC
TITLE HUMAN LXR BETA HORMONE RECEPTOR COMPLEXED WITH T0901317
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYSTEROLS RECEPTOR LXR-BETA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, RESIDUES 213-261;
COMPND 5 SYNONYM: LIVER X RECEPTOR BETA, NUCLEAR ORPHAN RECEPTOR LXR-BETA,
COMPND 6 UBIQUITOUSLY-EXPRESSED NUCLEAR RECEPTOR, NUCLEAR RECEPTOR NER;
COMPND 7 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: NR1H2 OR LXRB OR UNR OR NER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS LXRB+T0901317, TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FARNEGARDH,T.BONN,S.SUN,J.LJUNGGREN,H.AHOLA,A.WILHELMSSON,J.-
AUTHOR 2 A.GUSTAFSSON,M.CARLQUIST
REVDAT 6 03-APR-24 1PQC 1 REMARK
REVDAT 5 14-FEB-24 1PQC 1 REMARK SEQADV
REVDAT 4 31-MAR-09 1PQC 1 REVDAT
REVDAT 3 24-FEB-09 1PQC 1 VERSN
REVDAT 2 25-NOV-03 1PQC 1 JRNL
REVDAT 1 09-SEP-03 1PQC 0
JRNL AUTH M.FARNEGARDH,T.BONN,S.SUN,J.LJUNGGREN,H.AHOLA,A.WILHELMSSON,
JRNL AUTH 2 J.-A.GUSTAFSSON,M.CARLQUIST
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF THE LIVER X RECEPTOR BETA
JRNL TITL 2 REVEALS A FLEXIBLE LIGAND-BINDING POCKET THAT CAN
JRNL TITL 3 ACCOMMODATE FUNDAMENTALLY DIFFERENT LIGANDS.
JRNL REF J.BIOL.CHEM. V. 278 38821 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12819202
JRNL DOI 10.1074/JBC.M304842200
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25718
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1381
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1831
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7477
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 1.29000
REMARK 3 B33 (A**2) : -1.30000
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): 0.410
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.305
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.914
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7745 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7177 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10502 ; 1.490 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16631 ; 0.842 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 908 ; 5.804 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1189 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8385 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1612 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1833 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8222 ; 0.224 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 4710 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.180 ; 0.200
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): 20 ; 0.205 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 81 ; 0.243 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.126 ; 0.200
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): 4613 ; 0.581 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7458 ; 1.145 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3132 ; 1.659 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3044 ; 3.050 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 1PQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MAXFLUX CONFOCAL MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: THYROID HORMONE RECEPTOR BETA LIGAND BINDING
REMARK 200 DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL, PEG 4000, HEPES,
REMARK 280 GLYCEROL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.36100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.00100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.63100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.00100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.36100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.63100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -58.72200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -103.26200
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 GLY A 209
REMARK 465 SER A 210
REMARK 465 HIS A 211
REMARK 465 MET A 212
REMARK 465 GLY A 213
REMARK 465 GLU A 214
REMARK 465 GLY A 215
REMARK 465 GLU A 216
REMARK 465 GLY A 217
REMARK 465 VAL A 218
REMARK 465 GLN A 219
REMARK 465 LEU A 254
REMARK 465 GLY A 255
REMARK 465 ALA A 256
REMARK 465 ASP A 257
REMARK 465 PRO A 258
REMARK 465 GLN A 259
REMARK 465 SER A 260
REMARK 465 VAL A 459
REMARK 465 HIS A 460
REMARK 465 GLU A 461
REMARK 465 GLY B 209
REMARK 465 SER B 210
REMARK 465 HIS B 211
REMARK 465 MET B 212
REMARK 465 GLY B 213
REMARK 465 GLU B 214
REMARK 465 GLY B 215
REMARK 465 GLU B 216
REMARK 465 GLY B 217
REMARK 465 VAL B 218
REMARK 465 GLN B 259
REMARK 465 SER B 260
REMARK 465 VAL B 459
REMARK 465 HIS B 460
REMARK 465 GLU B 461
REMARK 465 GLY C 209
REMARK 465 SER C 210
REMARK 465 HIS C 211
REMARK 465 MET C 212
REMARK 465 GLY C 213
REMARK 465 GLU C 214
REMARK 465 GLY C 215
REMARK 465 GLU C 216
REMARK 465 GLY C 217
REMARK 465 VAL C 218
REMARK 465 GLN C 219
REMARK 465 SER C 244
REMARK 465 ASP C 245
REMARK 465 GLN C 246
REMARK 465 PRO C 247
REMARK 465 GLY C 255
REMARK 465 ALA C 256
REMARK 465 ASP C 257
REMARK 465 PRO C 258
REMARK 465 VAL C 459
REMARK 465 HIS C 460
REMARK 465 GLU C 461
REMARK 465 GLY D 209
REMARK 465 SER D 210
REMARK 465 HIS D 211
REMARK 465 MET D 212
REMARK 465 GLY D 213
REMARK 465 GLU D 214
REMARK 465 GLY D 215
REMARK 465 GLU D 216
REMARK 465 GLY D 217
REMARK 465 VAL D 218
REMARK 465 GLN D 219
REMARK 465 PHE D 243
REMARK 465 SER D 244
REMARK 465 ASP D 245
REMARK 465 GLN D 246
REMARK 465 PRO D 247
REMARK 465 LYS D 248
REMARK 465 PRO D 253
REMARK 465 LEU D 254
REMARK 465 GLY D 255
REMARK 465 ALA D 256
REMARK 465 ASP D 257
REMARK 465 PRO D 258
REMARK 465 GLN D 259
REMARK 465 LEU D 330
REMARK 465 LYS D 331
REMARK 465 ASP D 332
REMARK 465 LEU D 444
REMARK 465 GLN D 445
REMARK 465 ASP D 446
REMARK 465 LYS D 447
REMARK 465 VAL D 459
REMARK 465 HIS D 460
REMARK 465 GLU D 461
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 ARG A 261 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 219 CG CD OE1 NE2
REMARK 470 ARG B 261 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 330 CG CD1 CD2
REMARK 470 LEU C 254 CG CD1 CD2
REMARK 470 SER D 260 OG
REMARK 470 ARG D 261 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 329 CG CD1 CD2 CE1 CE2 CZ
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 OE2 GLU B 437 O HOH B 50 2.16
REMARK 500 OG SER D 242 OE2 GLU D 281 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 284 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 332 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 338 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 262 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 299 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
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 PHE A 243 36.62 -143.55
REMARK 500 LEU A 293 1.36 -68.24
REMARK 500 GLN A 346 153.85 -48.68
REMARK 500 PHE A 379 53.68 -97.97
REMARK 500 GLU A 388 68.01 -119.84
REMARK 500 GLN A 445 41.40 -96.50
REMARK 500 ASP A 446 42.56 30.91
REMARK 500 LYS A 447 78.69 -110.47
REMARK 500 ASP B 257 -162.09 -79.79
REMARK 500 LYS B 331 -50.34 89.60
REMARK 500 PRO C 253 84.17 -57.30
REMARK 500 THR C 328 76.29 -112.87
REMARK 500 ILE C 409 -74.46 -97.57
REMARK 500 LYS C 410 -74.94 -17.71
REMARK 500 ASP C 414 70.79 -100.25
REMARK 500 ASP C 446 27.13 49.19
REMARK 500 ARG D 241 -34.42 -36.44
REMARK 500 ARG D 261 -87.21 -80.22
REMARK 500 PHE D 379 48.77 -85.92
REMARK 500 GLU D 388 70.51 -116.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS C 248 VAL C 249 -142.90
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 444 A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 444 B 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 444 C 3500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 444 D 4500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PQ9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH THE SAME LIGAND BUT WITH THE LIGAND
REMARK 900 INTACT
REMARK 900 RELATED ID: 1PQ6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH GW3965
DBREF 1PQC A 213 461 UNP P55055 NR1H2_HUMAN 213 461
DBREF 1PQC B 213 461 UNP P55055 NR1H2_HUMAN 213 461
DBREF 1PQC C 213 461 UNP P55055 NR1H2_HUMAN 213 461
DBREF 1PQC D 213 461 UNP P55055 NR1H2_HUMAN 213 461
SEQADV 1PQC GLY A 209 UNP P55055 INSERTION
SEQADV 1PQC SER A 210 UNP P55055 INSERTION
SEQADV 1PQC HIS A 211 UNP P55055 INSERTION
SEQADV 1PQC MET A 212 UNP P55055 INSERTION
SEQADV 1PQC GLY B 209 UNP P55055 INSERTION
SEQADV 1PQC SER B 210 UNP P55055 INSERTION
SEQADV 1PQC HIS B 211 UNP P55055 INSERTION
SEQADV 1PQC MET B 212 UNP P55055 INSERTION
SEQADV 1PQC GLY C 209 UNP P55055 INSERTION
SEQADV 1PQC SER C 210 UNP P55055 INSERTION
SEQADV 1PQC HIS C 211 UNP P55055 INSERTION
SEQADV 1PQC MET C 212 UNP P55055 INSERTION
SEQADV 1PQC GLY D 209 UNP P55055 INSERTION
SEQADV 1PQC SER D 210 UNP P55055 INSERTION
SEQADV 1PQC HIS D 211 UNP P55055 INSERTION
SEQADV 1PQC MET D 212 UNP P55055 INSERTION
SEQRES 1 A 253 GLY SER HIS MET GLY GLU GLY GLU GLY VAL GLN LEU THR
SEQRES 2 A 253 ALA ALA GLN GLU LEU MET ILE GLN GLN LEU VAL ALA ALA
SEQRES 3 A 253 GLN LEU GLN CYS ASN LYS ARG SER PHE SER ASP GLN PRO
SEQRES 4 A 253 LYS VAL THR PRO TRP PRO LEU GLY ALA ASP PRO GLN SER
SEQRES 5 A 253 ARG ASP ALA ARG GLN GLN ARG PHE ALA HIS PHE THR GLU
SEQRES 6 A 253 LEU ALA ILE ILE SER VAL GLN GLU ILE VAL ASP PHE ALA
SEQRES 7 A 253 LYS GLN VAL PRO GLY PHE LEU GLN LEU GLY ARG GLU ASP
SEQRES 8 A 253 GLN ILE ALA LEU LEU LYS ALA SER THR ILE GLU ILE MET
SEQRES 9 A 253 LEU LEU GLU THR ALA ARG ARG TYR ASN HIS GLU THR GLU
SEQRES 10 A 253 CYS ILE THR PHE LEU LYS ASP PHE THR TYR SER LYS ASP
SEQRES 11 A 253 ASP PHE HIS ARG ALA GLY LEU GLN VAL GLU PHE ILE ASN
SEQRES 12 A 253 PRO ILE PHE GLU PHE SER ARG ALA MET ARG ARG LEU GLY
SEQRES 13 A 253 LEU ASP ASP ALA GLU TYR ALA LEU LEU ILE ALA ILE ASN
SEQRES 14 A 253 ILE PHE SER ALA ASP ARG PRO ASN VAL GLN GLU PRO GLY
SEQRES 15 A 253 ARG VAL GLU ALA LEU GLN GLN PRO TYR VAL GLU ALA LEU
SEQRES 16 A 253 LEU SER TYR THR ARG ILE LYS ARG PRO GLN ASP GLN LEU
SEQRES 17 A 253 ARG PHE PRO ARG MET LEU MET LYS LEU VAL SER LEU ARG
SEQRES 18 A 253 THR LEU SER SER VAL HIS SER GLU GLN VAL PHE ALA LEU
SEQRES 19 A 253 ARG LEU GLN ASP LYS LYS LEU PRO PRO LEU LEU SER GLU
SEQRES 20 A 253 ILE TRP ASP VAL HIS GLU
SEQRES 1 B 253 GLY SER HIS MET GLY GLU GLY GLU GLY VAL GLN LEU THR
SEQRES 2 B 253 ALA ALA GLN GLU LEU MET ILE GLN GLN LEU VAL ALA ALA
SEQRES 3 B 253 GLN LEU GLN CYS ASN LYS ARG SER PHE SER ASP GLN PRO
SEQRES 4 B 253 LYS VAL THR PRO TRP PRO LEU GLY ALA ASP PRO GLN SER
SEQRES 5 B 253 ARG ASP ALA ARG GLN GLN ARG PHE ALA HIS PHE THR GLU
SEQRES 6 B 253 LEU ALA ILE ILE SER VAL GLN GLU ILE VAL ASP PHE ALA
SEQRES 7 B 253 LYS GLN VAL PRO GLY PHE LEU GLN LEU GLY ARG GLU ASP
SEQRES 8 B 253 GLN ILE ALA LEU LEU LYS ALA SER THR ILE GLU ILE MET
SEQRES 9 B 253 LEU LEU GLU THR ALA ARG ARG TYR ASN HIS GLU THR GLU
SEQRES 10 B 253 CYS ILE THR PHE LEU LYS ASP PHE THR TYR SER LYS ASP
SEQRES 11 B 253 ASP PHE HIS ARG ALA GLY LEU GLN VAL GLU PHE ILE ASN
SEQRES 12 B 253 PRO ILE PHE GLU PHE SER ARG ALA MET ARG ARG LEU GLY
SEQRES 13 B 253 LEU ASP ASP ALA GLU TYR ALA LEU LEU ILE ALA ILE ASN
SEQRES 14 B 253 ILE PHE SER ALA ASP ARG PRO ASN VAL GLN GLU PRO GLY
SEQRES 15 B 253 ARG VAL GLU ALA LEU GLN GLN PRO TYR VAL GLU ALA LEU
SEQRES 16 B 253 LEU SER TYR THR ARG ILE LYS ARG PRO GLN ASP GLN LEU
SEQRES 17 B 253 ARG PHE PRO ARG MET LEU MET LYS LEU VAL SER LEU ARG
SEQRES 18 B 253 THR LEU SER SER VAL HIS SER GLU GLN VAL PHE ALA LEU
SEQRES 19 B 253 ARG LEU GLN ASP LYS LYS LEU PRO PRO LEU LEU SER GLU
SEQRES 20 B 253 ILE TRP ASP VAL HIS GLU
SEQRES 1 C 253 GLY SER HIS MET GLY GLU GLY GLU GLY VAL GLN LEU THR
SEQRES 2 C 253 ALA ALA GLN GLU LEU MET ILE GLN GLN LEU VAL ALA ALA
SEQRES 3 C 253 GLN LEU GLN CYS ASN LYS ARG SER PHE SER ASP GLN PRO
SEQRES 4 C 253 LYS VAL THR PRO TRP PRO LEU GLY ALA ASP PRO GLN SER
SEQRES 5 C 253 ARG ASP ALA ARG GLN GLN ARG PHE ALA HIS PHE THR GLU
SEQRES 6 C 253 LEU ALA ILE ILE SER VAL GLN GLU ILE VAL ASP PHE ALA
SEQRES 7 C 253 LYS GLN VAL PRO GLY PHE LEU GLN LEU GLY ARG GLU ASP
SEQRES 8 C 253 GLN ILE ALA LEU LEU LYS ALA SER THR ILE GLU ILE MET
SEQRES 9 C 253 LEU LEU GLU THR ALA ARG ARG TYR ASN HIS GLU THR GLU
SEQRES 10 C 253 CYS ILE THR PHE LEU LYS ASP PHE THR TYR SER LYS ASP
SEQRES 11 C 253 ASP PHE HIS ARG ALA GLY LEU GLN VAL GLU PHE ILE ASN
SEQRES 12 C 253 PRO ILE PHE GLU PHE SER ARG ALA MET ARG ARG LEU GLY
SEQRES 13 C 253 LEU ASP ASP ALA GLU TYR ALA LEU LEU ILE ALA ILE ASN
SEQRES 14 C 253 ILE PHE SER ALA ASP ARG PRO ASN VAL GLN GLU PRO GLY
SEQRES 15 C 253 ARG VAL GLU ALA LEU GLN GLN PRO TYR VAL GLU ALA LEU
SEQRES 16 C 253 LEU SER TYR THR ARG ILE LYS ARG PRO GLN ASP GLN LEU
SEQRES 17 C 253 ARG PHE PRO ARG MET LEU MET LYS LEU VAL SER LEU ARG
SEQRES 18 C 253 THR LEU SER SER VAL HIS SER GLU GLN VAL PHE ALA LEU
SEQRES 19 C 253 ARG LEU GLN ASP LYS LYS LEU PRO PRO LEU LEU SER GLU
SEQRES 20 C 253 ILE TRP ASP VAL HIS GLU
SEQRES 1 D 253 GLY SER HIS MET GLY GLU GLY GLU GLY VAL GLN LEU THR
SEQRES 2 D 253 ALA ALA GLN GLU LEU MET ILE GLN GLN LEU VAL ALA ALA
SEQRES 3 D 253 GLN LEU GLN CYS ASN LYS ARG SER PHE SER ASP GLN PRO
SEQRES 4 D 253 LYS VAL THR PRO TRP PRO LEU GLY ALA ASP PRO GLN SER
SEQRES 5 D 253 ARG ASP ALA ARG GLN GLN ARG PHE ALA HIS PHE THR GLU
SEQRES 6 D 253 LEU ALA ILE ILE SER VAL GLN GLU ILE VAL ASP PHE ALA
SEQRES 7 D 253 LYS GLN VAL PRO GLY PHE LEU GLN LEU GLY ARG GLU ASP
SEQRES 8 D 253 GLN ILE ALA LEU LEU LYS ALA SER THR ILE GLU ILE MET
SEQRES 9 D 253 LEU LEU GLU THR ALA ARG ARG TYR ASN HIS GLU THR GLU
SEQRES 10 D 253 CYS ILE THR PHE LEU LYS ASP PHE THR TYR SER LYS ASP
SEQRES 11 D 253 ASP PHE HIS ARG ALA GLY LEU GLN VAL GLU PHE ILE ASN
SEQRES 12 D 253 PRO ILE PHE GLU PHE SER ARG ALA MET ARG ARG LEU GLY
SEQRES 13 D 253 LEU ASP ASP ALA GLU TYR ALA LEU LEU ILE ALA ILE ASN
SEQRES 14 D 253 ILE PHE SER ALA ASP ARG PRO ASN VAL GLN GLU PRO GLY
SEQRES 15 D 253 ARG VAL GLU ALA LEU GLN GLN PRO TYR VAL GLU ALA LEU
SEQRES 16 D 253 LEU SER TYR THR ARG ILE LYS ARG PRO GLN ASP GLN LEU
SEQRES 17 D 253 ARG PHE PRO ARG MET LEU MET LYS LEU VAL SER LEU ARG
SEQRES 18 D 253 THR LEU SER SER VAL HIS SER GLU GLN VAL PHE ALA LEU
SEQRES 19 D 253 ARG LEU GLN ASP LYS LYS LEU PRO PRO LEU LEU SER GLU
SEQRES 20 D 253 ILE TRP ASP VAL HIS GLU
HET 444 A1500 31
HET 444 B2500 31
HET 444 C3500 31
HET 444 D4500 31
HETNAM 444 N-(2,2,2-TRIFLUOROETHYL)-N-{4-[2,2,2-TRIFLUORO-1-
HETNAM 2 444 HYDROXY-1-(TRIFLUOROMETHYL)
HETNAM 3 444 ETHYL]PHENYL}BENZENESULFONAMIDE
FORMUL 5 444 4(C17 H12 F9 N O3 S)
FORMUL 9 HOH *181(H2 O)
HELIX 1 1 THR A 221 SER A 244 1 24
HELIX 2 2 ARG A 261 LYS A 287 1 27
HELIX 3 3 GLY A 291 LEU A 295 5 5
HELIX 4 4 GLY A 296 ARG A 319 1 24
HELIX 5 5 LYS A 337 ALA A 343 1 7
HELIX 6 6 GLN A 346 GLY A 364 1 19
HELIX 7 7 ASP A 366 PHE A 379 1 14
HELIX 8 8 GLU A 388 ARG A 411 1 24
HELIX 9 9 LEU A 416 LEU A 444 1 29
HELIX 10 10 PRO A 450 ASP A 458 1 9
HELIX 11 11 THR B 221 ASN B 239 1 19
HELIX 12 12 ASN B 239 ASP B 245 1 7
HELIX 13 13 ARG B 261 VAL B 289 1 29
HELIX 14 14 GLY B 291 LEU B 295 5 5
HELIX 15 15 GLY B 296 ARG B 319 1 24
HELIX 16 16 LYS B 337 ALA B 343 1 7
HELIX 17 17 GLN B 346 GLY B 364 1 19
HELIX 18 18 ASP B 366 PHE B 379 1 14
HELIX 19 19 GLU B 388 ARG B 411 1 24
HELIX 20 20 LEU B 416 LEU B 444 1 29
HELIX 21 21 PRO B 450 ASP B 458 1 9
HELIX 22 22 THR C 221 ASN C 239 1 19
HELIX 23 23 SER C 260 GLN C 288 1 29
HELIX 24 24 GLY C 291 LEU C 295 5 5
HELIX 25 25 GLY C 296 ARG C 319 1 24
HELIX 26 26 SER C 336 ALA C 343 1 8
HELIX 27 27 GLN C 346 GLY C 364 1 19
HELIX 28 28 ASP C 366 PHE C 379 1 14
HELIX 29 29 GLU C 388 ARG C 411 1 24
HELIX 30 30 LEU C 416 LEU C 444 1 29
HELIX 31 31 PRO C 450 ASP C 458 1 9
HELIX 32 32 THR D 221 SER D 242 1 22
HELIX 33 33 SER D 260 VAL D 289 1 30
HELIX 34 34 GLY D 291 LEU D 295 5 5
HELIX 35 35 GLY D 296 ARG D 319 1 24
HELIX 36 36 SER D 336 ALA D 343 1 8
HELIX 37 37 GLN D 346 GLY D 364 1 19
HELIX 38 38 ASP D 366 PHE D 379 1 14
HELIX 39 39 GLU D 388 ARG D 411 1 24
HELIX 40 40 LEU D 416 ARG D 443 1 28
HELIX 41 41 PRO D 450 ASP D 458 1 9
SHEET 1 A 3 TYR A 320 ASN A 321 0
SHEET 2 A 3 CYS A 326 LEU A 330 -1 O CYS A 326 N ASN A 321
SHEET 3 A 3 PHE A 333 SER A 336 -1 O PHE A 333 N LEU A 330
SHEET 1 B 3 TYR B 320 ASN B 321 0
SHEET 2 B 3 CYS B 326 PHE B 329 -1 O CYS B 326 N ASN B 321
SHEET 3 B 3 PHE B 333 SER B 336 -1 O TYR B 335 N ILE B 327
SHEET 1 C 3 TYR C 320 ASN C 321 0
SHEET 2 C 3 CYS C 326 LEU C 330 -1 O CYS C 326 N ASN C 321
SHEET 3 C 3 PHE C 333 TYR C 335 -1 O TYR C 335 N ILE C 327
SHEET 1 D 2 TYR D 320 ASN D 321 0
SHEET 2 D 2 CYS D 326 ILE D 327 -1 O CYS D 326 N ASN D 321
SITE 1 AC1 15 PHE A 271 THR A 272 ALA A 275 MET A 312
SITE 2 AC1 15 THR A 316 PHE A 329 LEU A 345 PHE A 349
SITE 3 AC1 15 ILE A 353 HIS A 435 GLN A 438 LEU A 442
SITE 4 AC1 15 LEU A 449 LEU A 453 TRP A 457
SITE 1 AC2 17 PHE B 268 PHE B 271 ALA B 275 MET B 312
SITE 2 AC2 17 LEU B 313 THR B 316 PHE B 329 LEU B 345
SITE 3 AC2 17 PHE B 349 ILE B 353 HIS B 435 GLN B 438
SITE 4 AC2 17 VAL B 439 LEU B 442 LEU B 449 LEU B 453
SITE 5 AC2 17 TRP B 457
SITE 1 AC3 16 PHE C 268 PHE C 271 LEU C 274 ALA C 275
SITE 2 AC3 16 MET C 312 LEU C 313 THR C 316 LEU C 345
SITE 3 AC3 16 PHE C 349 ILE C 353 HIS C 435 GLN C 438
SITE 4 AC3 16 LEU C 442 LEU C 449 LEU C 453 TRP C 457
SITE 1 AC4 16 PHE D 268 PHE D 271 LEU D 274 ALA D 275
SITE 2 AC4 16 ILE D 309 MET D 312 LEU D 313 THR D 316
SITE 3 AC4 16 TYR D 335 LEU D 345 PHE D 349 ILE D 353
SITE 4 AC4 16 HIS D 435 GLN D 438 LEU D 449 TRP D 457
CRYST1 58.722 103.262 176.002 90.00 90.00 90.00 P 21 21 21 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 0.017029 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005682 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
