HEADER HORMONE, TRANSCRIPTION RECEPTOR 15-MAY-08 3D57
TITLE TR VARIANT D355R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYROID HORMONE RECEPTOR BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR SUBFAMILY 1 GROUP A MEMBER 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: 7068, ERBA2, NR1A2, THR1, THRB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET-1
KEYWDS THYROID HORMONE RECEPTOR, LIGAND BINDING DOMAIN, D355R MUTANT,
KEYWDS 2 HOMODIMER, ALTERNATIVE SPLICING, DEAFNESS, DISEASE MUTATION, DNA-
KEYWDS 3 BINDING, METAL-BINDING, NUCLEUS, POLYMORPHISM, RECEPTOR,
KEYWDS 4 TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-FINGER, HORMONE,
KEYWDS 5 TRANSCRIPTION RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.JOURAVEL
REVDAT 4 30-AUG-23 3D57 1 REMARK
REVDAT 3 20-OCT-21 3D57 1 REMARK SEQADV
REVDAT 2 10-FEB-09 3D57 1 JRNL VERSN
REVDAT 1 14-OCT-08 3D57 0
JRNL AUTH N.JOURAVEL,E.SABLIN,M.TOGASHI,J.D.BAXTER,P.WEBB,
JRNL AUTH 2 R.J.FLETTERICK
JRNL TITL MOLECULAR BASIS FOR DIMER FORMATION OF TRBETA VARIANT D355R.
JRNL REF PROTEINS V. 75 111 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18798561
JRNL DOI 10.1002/PROT.22225
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 25784
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) : 0.210
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 28545
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3917
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 5.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.77300
REMARK 3 B22 (A**2) : 8.55500
REMARK 3 B33 (A**2) : -9.32900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.89900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.197
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 3D57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115891
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28545
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : 0.22000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 1NAX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENE GLYCOL, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 46.48150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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 195
REMARK 465 GLY A 196
REMARK 465 SER A 197
REMARK 465 SER A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 SER A 205
REMARK 465 GLN A 206
REMARK 465 ASP A 207
REMARK 465 PRO A 208
REMARK 465 GLY A 209
REMARK 465 ILE A 255
REMARK 465 VAL A 256
REMARK 465 ASN A 257
REMARK 465 ALA A 258
REMARK 465 PRO A 259
REMARK 465 GLU A 260
REMARK 465 MET B 195
REMARK 465 GLY B 196
REMARK 465 SER B 197
REMARK 465 SER B 198
REMARK 465 HIS B 199
REMARK 465 HIS B 200
REMARK 465 HIS B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 SER B 205
REMARK 465 GLN B 206
REMARK 465 ASP B 207
REMARK 465 PRO B 208
REMARK 465 GLY B 209
REMARK 465 HIS B 210
REMARK 465 VAL B 256
REMARK 465 ASN B 257
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 PRO A 247 CB - CA - C ANGL. DEV. = -13.8 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 LYS A 411 41.98 76.57
REMARK 500 ALA B 253 126.56 -35.62
REMARK 500 GLU B 260 -7.18 73.61
REMARK 500 GLU B 333 -26.61 -141.46
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 4HY A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HY B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
DBREF 3D57 A 209 460 UNP P10828 THB_HUMAN 209 460
DBREF 3D57 B 209 460 UNP P10828 THB_HUMAN 209 460
SEQADV 3D57 MET A 195 UNP P10828 EXPRESSION TAG
SEQADV 3D57 GLY A 196 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER A 197 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER A 198 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 199 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 200 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 201 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 202 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 203 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS A 204 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER A 205 UNP P10828 EXPRESSION TAG
SEQADV 3D57 GLN A 206 UNP P10828 EXPRESSION TAG
SEQADV 3D57 ASP A 207 UNP P10828 EXPRESSION TAG
SEQADV 3D57 PRO A 208 UNP P10828 EXPRESSION TAG
SEQADV 3D57 ARG A 355 UNP P10828 ASP 355 ENGINEERED MUTATION
SEQADV 3D57 MET B 195 UNP P10828 EXPRESSION TAG
SEQADV 3D57 GLY B 196 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER B 197 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER B 198 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 199 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 200 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 201 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 202 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 203 UNP P10828 EXPRESSION TAG
SEQADV 3D57 HIS B 204 UNP P10828 EXPRESSION TAG
SEQADV 3D57 SER B 205 UNP P10828 EXPRESSION TAG
SEQADV 3D57 GLN B 206 UNP P10828 EXPRESSION TAG
SEQADV 3D57 ASP B 207 UNP P10828 EXPRESSION TAG
SEQADV 3D57 PRO B 208 UNP P10828 EXPRESSION TAG
SEQADV 3D57 ARG B 355 UNP P10828 ASP 355 ENGINEERED MUTATION
SEQRES 1 A 266 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 266 PRO GLY HIS LYS PRO GLU PRO THR ASP GLU GLU TRP GLU
SEQRES 3 A 266 LEU ILE LYS THR VAL THR GLU ALA HIS VAL ALA THR ASN
SEQRES 4 A 266 ALA GLN GLY SER HIS TRP LYS GLN LYS ARG LYS PHE LEU
SEQRES 5 A 266 PRO GLU ASP ILE GLY GLN ALA PRO ILE VAL ASN ALA PRO
SEQRES 6 A 266 GLU GLY GLY LYS VAL ASP LEU GLU ALA PHE SER HIS PHE
SEQRES 7 A 266 THR LYS ILE ILE THR PRO ALA ILE THR ARG VAL VAL ASP
SEQRES 8 A 266 PHE ALA LYS LYS LEU PRO MET PHE CYS GLU LEU PRO CYS
SEQRES 9 A 266 GLU ASP GLN ILE ILE LEU LEU LYS GLY CYS CYS MET GLU
SEQRES 10 A 266 ILE MET SER LEU ARG ALA ALA VAL ARG TYR ASP PRO GLU
SEQRES 11 A 266 SER GLU THR LEU THR LEU ASN GLY GLU MET ALA VAL THR
SEQRES 12 A 266 ARG GLY GLN LEU LYS ASN GLY GLY LEU GLY VAL VAL SER
SEQRES 13 A 266 ASP ALA ILE PHE ARG LEU GLY MET SER LEU SER SER PHE
SEQRES 14 A 266 ASN LEU ASP ASP THR GLU VAL ALA LEU LEU GLN ALA VAL
SEQRES 15 A 266 LEU LEU MET SER SER ASP ARG PRO GLY LEU ALA CYS VAL
SEQRES 16 A 266 GLU ARG ILE GLU LYS TYR GLN ASP SER PHE LEU LEU ALA
SEQRES 17 A 266 PHE GLU HIS TYR ILE ASN TYR ARG LYS HIS HIS VAL THR
SEQRES 18 A 266 HIS PHE TRP PRO LYS LEU LEU MET LYS VAL THR ASP LEU
SEQRES 19 A 266 ARG MET ILE GLY ALA CYS HIS ALA SER ARG PHE LEU HIS
SEQRES 20 A 266 MET LYS VAL GLU CYS PRO THR GLU LEU PHE PRO PRO LEU
SEQRES 21 A 266 PHE LEU GLU VAL PHE GLU
SEQRES 1 B 266 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 266 PRO GLY HIS LYS PRO GLU PRO THR ASP GLU GLU TRP GLU
SEQRES 3 B 266 LEU ILE LYS THR VAL THR GLU ALA HIS VAL ALA THR ASN
SEQRES 4 B 266 ALA GLN GLY SER HIS TRP LYS GLN LYS ARG LYS PHE LEU
SEQRES 5 B 266 PRO GLU ASP ILE GLY GLN ALA PRO ILE VAL ASN ALA PRO
SEQRES 6 B 266 GLU GLY GLY LYS VAL ASP LEU GLU ALA PHE SER HIS PHE
SEQRES 7 B 266 THR LYS ILE ILE THR PRO ALA ILE THR ARG VAL VAL ASP
SEQRES 8 B 266 PHE ALA LYS LYS LEU PRO MET PHE CYS GLU LEU PRO CYS
SEQRES 9 B 266 GLU ASP GLN ILE ILE LEU LEU LYS GLY CYS CYS MET GLU
SEQRES 10 B 266 ILE MET SER LEU ARG ALA ALA VAL ARG TYR ASP PRO GLU
SEQRES 11 B 266 SER GLU THR LEU THR LEU ASN GLY GLU MET ALA VAL THR
SEQRES 12 B 266 ARG GLY GLN LEU LYS ASN GLY GLY LEU GLY VAL VAL SER
SEQRES 13 B 266 ASP ALA ILE PHE ARG LEU GLY MET SER LEU SER SER PHE
SEQRES 14 B 266 ASN LEU ASP ASP THR GLU VAL ALA LEU LEU GLN ALA VAL
SEQRES 15 B 266 LEU LEU MET SER SER ASP ARG PRO GLY LEU ALA CYS VAL
SEQRES 16 B 266 GLU ARG ILE GLU LYS TYR GLN ASP SER PHE LEU LEU ALA
SEQRES 17 B 266 PHE GLU HIS TYR ILE ASN TYR ARG LYS HIS HIS VAL THR
SEQRES 18 B 266 HIS PHE TRP PRO LYS LEU LEU MET LYS VAL THR ASP LEU
SEQRES 19 B 266 ARG MET ILE GLY ALA CYS HIS ALA SER ARG PHE LEU HIS
SEQRES 20 B 266 MET LYS VAL GLU CYS PRO THR GLU LEU PHE PRO PRO LEU
SEQRES 21 B 266 PHE LEU GLU VAL PHE GLU
HET 4HY A 500 21
HET 4HY B 500 21
HET SO4 B 501 5
HETNAM 4HY [4-(4-HYDROXY-3-IODO-PHENOXY)-3,5-DIIODO-PHENYL]-ACETIC
HETNAM 2 4HY ACID
HETNAM SO4 SULFATE ION
FORMUL 3 4HY 2(C14 H9 I3 O4)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *105(H2 O)
HELIX 1 1 THR A 215 THR A 232 1 18
HELIX 2 2 ASP A 265 LYS A 274 1 10
HELIX 3 3 ILE A 275 LYS A 289 1 15
HELIX 4 4 LEU A 290 GLU A 295 1 6
HELIX 5 5 PRO A 297 VAL A 319 1 23
HELIX 6 6 ARG A 338 GLY A 344 1 7
HELIX 7 7 VAL A 348 SER A 361 1 14
HELIX 8 8 SER A 362 ASN A 364 5 3
HELIX 9 9 ASP A 366 MET A 379 1 14
HELIX 10 10 CYS A 388 LYS A 411 1 24
HELIX 11 11 HIS A 416 CYS A 446 1 31
HELIX 12 12 PRO A 447 PHE A 451 5 5
HELIX 13 13 PRO A 452 PHE A 459 1 8
HELIX 14 14 THR B 215 THR B 232 1 18
HELIX 15 15 HIS B 238 ARG B 243 1 6
HELIX 16 16 ASP B 265 LYS B 274 1 10
HELIX 17 17 ILE B 275 LYS B 289 1 15
HELIX 18 18 LEU B 290 GLU B 295 1 6
HELIX 19 19 PRO B 297 VAL B 319 1 23
HELIX 20 20 THR B 337 GLY B 344 1 8
HELIX 21 21 GLY B 347 SER B 361 1 15
HELIX 22 22 SER B 362 ASN B 364 5 3
HELIX 23 23 ASP B 366 MET B 379 1 14
HELIX 24 24 CYS B 388 LYS B 411 1 24
HELIX 25 25 HIS B 416 CYS B 446 1 31
HELIX 26 26 PRO B 447 PHE B 451 5 5
HELIX 27 27 PRO B 452 GLU B 460 1 9
SHEET 1 A 4 LYS A 244 PHE A 245 0
SHEET 2 A 4 MET A 334 THR A 337 1 O ALA A 335 N LYS A 244
SHEET 3 A 4 THR A 327 LEU A 330 -1 N LEU A 330 O MET A 334
SHEET 4 A 4 TYR A 321 ASP A 322 -1 N ASP A 322 O THR A 327
SHEET 1 B 4 LYS B 244 PHE B 245 0
SHEET 2 B 4 MET B 334 VAL B 336 1 O ALA B 335 N LYS B 244
SHEET 3 B 4 THR B 327 LEU B 330 -1 N LEU B 330 O MET B 334
SHEET 4 B 4 TYR B 321 ASP B 322 -1 N ASP B 322 O THR B 327
SITE 1 AC1 11 PHE A 272 MET A 313 ALA A 317 ARG A 320
SITE 2 AC1 11 LEU A 330 ASN A 331 LEU A 346 ILE A 353
SITE 3 AC1 11 HIS A 435 MET A 442 PHE A 455
SITE 1 AC2 14 PHE B 272 ILE B 276 MET B 313 ALA B 317
SITE 2 AC2 14 ARG B 320 LEU B 330 ASN B 331 GLY B 344
SITE 3 AC2 14 LEU B 346 ILE B 353 HIS B 435 MET B 442
SITE 4 AC2 14 PHE B 455 HOH B 541
SITE 1 AC3 7 ASN A 364 HIS A 412 HIS A 413 ASN B 364
SITE 2 AC3 7 HIS B 412 HIS B 413 HOH B 546
CRYST1 55.557 92.963 58.808 90.00 110.02 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 0.018000 0.000000 0.006558 0.00000
SCALE2 0.000000 0.010757 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018098 0.00000
(ATOM LINES ARE NOT SHOWN.)
END