HEADER TRANSCRIPTION 26-AUG-04 1XAP
TITLE STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE RETINOIC ACID RECEPTOR
TITLE 2 BETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: RAR-BETA, RAR-EPSILON, HBV-ACTIVATED PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NUCLEAR RECEPTOR, LIGAND BINDING DOMAIN, RETINOIC ACID RECEPTOR BETA,
KEYWDS 2 TTNPB, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GERMAIN,S.KAMMERER,C.PELUSO-ILTIS,D.TORTOLANI,F.C.ZUSI,J.STARRETT,
AUTHOR 2 P.LAPOINTE,J.P.DARIS,A.MARINIER,A.R.DE LERA,N.ROCHEL,H.GRONEMEYER
REVDAT 6 25-OCT-23 1XAP 1 REMARK SEQADV
REVDAT 5 28-DEC-16 1XAP 1 TITLE VERSN
REVDAT 4 24-FEB-09 1XAP 1 VERSN
REVDAT 3 26-SEP-06 1XAP 1 AUTHOR
REVDAT 2 19-SEP-06 1XAP 1 JRNL AUTHOR
REVDAT 1 16-NOV-04 1XAP 0
JRNL AUTH P.GERMAIN,S.KAMMERER,E.PEREZ,C.PELUSO-ILTIS,D.TORTOLANI,
JRNL AUTH 2 F.C.ZUSI,J.STARRETT,P.LAPOINTE,J.P.DARIS,A.MARINIER,
JRNL AUTH 3 A.R.DE LERA,N.ROCHEL,H.GRONEMEYER
JRNL TITL RATIONAL DESIGN OF RAR-SELECTIVE LIGANDS REVEALED BY RARBETA
JRNL TITL 2 CRYSTAL STRUCTURE
JRNL REF EMBO REP. V. 5 877 2004
JRNL REFN ISSN 1469-221X
JRNL PMID 15319780
JRNL DOI 10.1038/SJ.EMBOR.7400235
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 9.7
REMARK 3 NUMBER OF REFLECTIONS : 14703
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1460
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1831
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.136
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.99
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.753
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14703
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3LBD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM CHLORIDE,
REMARK 280 MAGNESIUM CHLORIDE, MES, PH 5.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
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 23.63800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.14450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.90400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.14450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.63800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.90400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 148
REMARK 465 GLY A 149
REMARK 465 SER A 150
REMARK 465 SER A 151
REMARK 465 HIS A 152
REMARK 465 HIS A 153
REMARK 465 HIS A 154
REMARK 465 HIS A 155
REMARK 465 HIS A 156
REMARK 465 HIS A 157
REMARK 465 SER A 158
REMARK 465 SER A 159
REMARK 465 GLY A 160
REMARK 465 LEU A 161
REMARK 465 VAL A 162
REMARK 465 PRO A 163
REMARK 465 ARG A 164
REMARK 465 GLY A 165
REMARK 465 SER A 166
REMARK 465 HIS A 167
REMARK 465 MET A 168
REMARK 465 GLU A 169
REMARK 465 SER A 170
REMARK 465 TYR A 171
REMARK 465 GLU A 172
REMARK 465 MET A 173
REMARK 465 THR A 174
REMARK 465 SER A 362
REMARK 465 LYS A 363
REMARK 465 PRO A 364
REMARK 465 SER A 410
REMARK 465 GLU A 411
REMARK 465 GLY A 412
REMARK 465 HIS A 413
REMARK 465 GLU A 414
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 GLU A 176 CG CD OE1 OE2
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 NH2 ARG A 360 CB MET A 366 1.02
REMARK 500 NH2 ARG A 360 CG MET A 366 1.92
REMARK 500 CZ ARG A 360 CG MET A 366 2.12
REMARK 500 CZ ARG A 360 CB MET A 366 2.13
REMARK 500 NH2 ARG A 360 CA MET A 366 2.18
REMARK 500 NE ARG A 360 CG MET A 366 2.18
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 ARG A 360 NE - CZ - NH2 ANGL. DEV. = 3.7 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 SER A 206 42.64 37.61
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 TTB A 1
DBREF 1XAP A 169 414 UNP P10826 RARB_HUMAN 176 421
SEQADV 1XAP MET A 148 UNP P10826 EXPRESSION TAG
SEQADV 1XAP GLY A 149 UNP P10826 EXPRESSION TAG
SEQADV 1XAP SER A 150 UNP P10826 EXPRESSION TAG
SEQADV 1XAP SER A 151 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 152 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 153 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 154 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 155 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 156 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 157 UNP P10826 EXPRESSION TAG
SEQADV 1XAP SER A 158 UNP P10826 EXPRESSION TAG
SEQADV 1XAP SER A 159 UNP P10826 EXPRESSION TAG
SEQADV 1XAP GLY A 160 UNP P10826 EXPRESSION TAG
SEQADV 1XAP LEU A 161 UNP P10826 EXPRESSION TAG
SEQADV 1XAP VAL A 162 UNP P10826 EXPRESSION TAG
SEQADV 1XAP PRO A 163 UNP P10826 EXPRESSION TAG
SEQADV 1XAP ARG A 164 UNP P10826 EXPRESSION TAG
SEQADV 1XAP GLY A 165 UNP P10826 EXPRESSION TAG
SEQADV 1XAP SER A 166 UNP P10826 EXPRESSION TAG
SEQADV 1XAP HIS A 167 UNP P10826 EXPRESSION TAG
SEQADV 1XAP MET A 168 UNP P10826 EXPRESSION TAG
SEQRES 1 A 267 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 267 LEU VAL PRO ARG GLY SER HIS MET GLU SER TYR GLU MET
SEQRES 3 A 267 THR ALA GLU LEU ASP ASP LEU THR GLU LYS ILE ARG LYS
SEQRES 4 A 267 ALA HIS GLN GLU THR PHE PRO SER LEU CYS GLN LEU GLY
SEQRES 5 A 267 LYS TYR THR THR ASN SER SER ALA ASP HIS ARG VAL ARG
SEQRES 6 A 267 LEU ASP LEU GLY LEU TRP ASP LYS PHE SER GLU LEU ALA
SEQRES 7 A 267 THR LYS CYS ILE ILE LYS ILE VAL GLU PHE ALA LYS ARG
SEQRES 8 A 267 LEU PRO GLY PHE THR GLY LEU THR ILE ALA ASP GLN ILE
SEQRES 9 A 267 THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU
SEQRES 10 A 267 ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET
SEQRES 11 A 267 THR PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET
SEQRES 12 A 267 HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE
SEQRES 13 A 267 THR PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP
SEQRES 14 A 267 THR GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS
SEQRES 15 A 267 GLY ASP ARG GLN ASP LEU GLU GLU PRO THR LYS VAL ASP
SEQRES 16 A 267 LYS LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS ILE TYR
SEQRES 17 A 267 ILE ARG LYS ARG ARG PRO SER LYS PRO HIS MET PHE PRO
SEQRES 18 A 267 LYS ILE LEU MET LYS ILE THR ASP LEU ARG SER ILE SER
SEQRES 19 A 267 ALA LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU
SEQRES 20 A 267 ILE PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU
SEQRES 21 A 267 GLU ASN SER GLU GLY HIS GLU
HET TTB A 1 26
HETNAM TTB 4-[(1E)-2-(5,5,8,8-TETRAMETHYL-5,6,7,8-
HETNAM 2 TTB TETRAHYDRONAPHTHALEN-2-YL)PROP-1-ENYL]BENZOIC ACID
HETSYN TTB TTNPB
FORMUL 2 TTB C24 H28 O2
FORMUL 3 HOH *115(H2 O)
HELIX 1 1 ALA A 175 PHE A 192 1 18
HELIX 2 2 SER A 194 LEU A 198 5 5
HELIX 3 3 ASP A 214 LEU A 239 1 26
HELIX 4 4 GLY A 241 LEU A 245 5 5
HELIX 5 5 THR A 246 THR A 268 1 23
HELIX 6 6 ARG A 287 GLY A 294 1 8
HELIX 7 7 PHE A 295 PRO A 297 5 3
HELIX 8 8 LEU A 298 LEU A 310 1 13
HELIX 9 9 PRO A 311 GLU A 313 5 3
HELIX 10 10 ASP A 315 ILE A 328 1 14
HELIX 11 11 GLU A 337 ARG A 360 1 24
HELIX 12 12 HIS A 365 LYS A 383 1 19
HELIX 13 13 LYS A 383 ILE A 395 1 13
HELIX 14 14 PRO A 400 GLU A 408 1 9
SHEET 1 A 3 TYR A 270 THR A 271 0
SHEET 2 A 3 THR A 276 THR A 278 -1 O THR A 276 N THR A 271
SHEET 3 A 3 THR A 284 ASN A 286 -1 O LEU A 285 N MET A 277
SITE 1 AC1 9 HOH A 11 PHE A 221 LEU A 224 ALA A 225
SITE 2 AC1 9 LEU A 262 ARG A 269 PHE A 279 SER A 280
SITE 3 AC1 9 VAL A 388
CRYST1 47.276 57.808 90.289 90.00 90.00 90.00 P 21 21 21 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 0.021152 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017299 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011076 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
