HEADER TRANSPORT PROTEIN 04-JUL-00 1E4H
TITLE STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW
TITLE 2 MODE OF BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PREALBUMIN, ATTR, TBPA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PLASMA
KEYWDS TRANSPORT PROTEIN, TRANSPORT(THYROXINE), ENVIRONMENTAL POLLUTANTS,
KEYWDS 2 BROMOPHENOLS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GHOSH,I.A.T.M.MEERTS,A.COOK,A.BERGMAN,A.BROUWER,L.N.JOHNSON
REVDAT 6 13-DEC-23 1E4H 1 REMARK
REVDAT 5 05-JUL-17 1E4H 1 REMARK
REVDAT 4 21-SEP-11 1E4H 1 HEADER COMPND KEYWDS REMARK
REVDAT 4 2 1 HETSYN FORMUL VERSN
REVDAT 3 01-SEP-09 1E4H 1 HEADER KEYWDS REMARK SITE
REVDAT 3 2 1 MASTER
REVDAT 2 24-FEB-09 1E4H 1 VERSN
REVDAT 1 29-AUG-00 1E4H 0
JRNL AUTH M.GHOSH,I.A.T.M.MEERTS,A.COOK,A.BERGMAN,A.BROUWER,
JRNL AUTH 2 L.N.JOHNSON
JRNL TITL STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS
JRNL TITL 2 : A NEW MODE OF BINDING
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 1085 2000
JRNL REFN ISSN 0907-4449
JRNL PMID 10957627
JRNL DOI 10.1107/S0907444900008568
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.DE LA PAZ,J.M.BURRIDGE,S.J.OATLEY,C.C.F.BLAKE
REMARK 1 TITL MULTIPLE MODES OF BINDING OF THYROID HORMONES AND OTHER
REMARK 1 TITL 2 IODOTHYRONINES TO HUMAN PLASMA TRANSTHYRETIN
REMARK 1 EDIT C.R.BEDDLE
REMARK 1 REF THE DESIGN OF DRUGS TO 119 1992
REMARK 1 REF 2 MACROMOLECULAR TARGETS
REMARK 1 PUBL JOHN WILEY & SONS LTD
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.C.F.BLAKE,M.J.GEISOW,S.J.OATLEY,C.RERAT,B.RERAT
REMARK 1 TITL STRUCTURE OF PREALBUMIN.SECONDARY,TERTIARY AND QUATERNARY
REMARK 1 TITL 2 INTERACTIONS DETERMINED BY FOURIER REFINEMRNT AND THYROXINE
REMARK 1 TITL 3 BINDING
REMARK 1 REF J.MOL.BIOL. V. 88 339 1978
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.C.F.BLAKE,S.J.OATLEY
REMARK 1 TITL PROTEIN-DNA AND PROTEIN-HORMONE INTERACTIONS IN PREALBUMIN :
REMARK 1 TITL 2 A MODEL OF THE THYROID HORMONE NUCLEAR RECEPTOR ?
REMARK 1 REF NATURE V. 268 115 1977
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 201845
REMARK 1 DOI 10.1038/268115A0
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 0.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22132
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) : 0.193
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1133
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4138
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 246
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 : 1760
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.70
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) : 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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.300
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : PBP_HALF.PAR
REMARK 3 PARAMETER FILE 4 : GOL.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : PBP_HALF.TOP
REMARK 3 TOPOLOGY FILE 4 : GOL.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE PENTABROMOPHENOL MOLECULE IS
REMARK 3 LOCATED RIGHT ON THE CRYSTALLOGRAPHIC Z AXIS. HALF THE MOLECULE
REMARK 3 WAS INCLUDED IN THE REFINEMENT WHILE THE OTHER HALF WAS
REMARK 3 GENERATED BY THE SYMMETRY OPERATION. WATER MOLECULES W302, W28,
REMARK 3 W350 ALSO LOCATED ON THE SAME SYMMETRY AXIS WERE KEPT FIXED IN
REMARK 3 POSITION DURING THE REFINEMENT. THERE WAS NO OBSERVABLE DENSITY
REMARK 3 FOR THE RESIDUES 1-9, AS WELL AS FOR 126- 127 OF BOTH THE
REMARK 3 CHAINS. THIS COORDINATE SET COMPRISES TWO CHAINS REPRESENTING
REMARK 3 TWO CHEMICALLY EQUIVALENT, BUT CRYSTALLOGRAPHICALLY DISTINCT,
REMARK 3 ENTITIES. THE OTHER HALF OF THE COMPLETE TETRAMER CAN BE
REMARK 3 GENERATED FROM THIS DIMER BY THE APPLICATION OF THE
REMARK 3 CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY ALONG Z THROUGH THE ORIGIN OF
REMARK 3 THE COORDINATE SYSTEM.
REMARK 4
REMARK 4 1E4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290004932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22174
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
REMARK 200 R SYM FOR SHELL (I) : 0.27900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1TTA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.70000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.2 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 BIOMT1 2 -1.000000 0.000000 0.000000 86.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 BR3 PBR A 998 LIES ON A SPECIAL POSITION.
REMARK 375 O1 PBR A 998 LIES ON A SPECIAL POSITION.
REMARK 375 C3 PBR A 998 LIES ON A SPECIAL POSITION.
REMARK 375 C6 PBR A 998 LIES ON A SPECIAL POSITION.
REMARK 375 BR3 PBR B 999 LIES ON A SPECIAL POSITION.
REMARK 375 O1 PBR B 999 LIES ON A SPECIAL POSITION.
REMARK 375 C3 PBR B 999 LIES ON A SPECIAL POSITION.
REMARK 375 C6 PBR B 999 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2077 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2005 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2067 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 9
REMARK 465 LYS B 126
REMARK 465 GLU B 127
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 62 CG CD OE1 OE2
REMARK 470 ASP B 38 CG OD1 OD2
REMARK 470 ASP B 39 CG OD1 OD2
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 ARG B 103 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 125 CG CD
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBR A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBR B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 990
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TTA RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (FORMERLY PREALBUMIN)
REMARK 900 RELATED ID: 2PAB RELATED DB: PDB
REMARK 900 RELATED ID: 1THC RELATED DB: PDB
REMARK 900 RELATED ID: 1THA RELATED DB: PDB
REMARK 900 RELATED ID: 1TLM RELATED DB: PDB
REMARK 900 RELATED ID: 1TTB RELATED DB: PDB
REMARK 900 RELATED ID: 1TTC RELATED DB: PDB
REMARK 900 RELATED ID: 1ETA RELATED DB: PDB
REMARK 900 RELATED ID: 1ETB RELATED DB: PDB
REMARK 900 RELATED ID: 1RLB RELATED DB: PDB
REMARK 900 RELATED ID: 1TYR RELATED DB: PDB
REMARK 900 RELATED ID: 1BM7 RELATED DB: PDB
REMARK 900 RELATED ID: 1BMZ RELATED DB: PDB
REMARK 900 RELATED ID: 1QAB RELATED DB: PDB
REMARK 900 RELATED ID: 2TRH RELATED DB: PDB
REMARK 900 TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS
REMARK 900 AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
REMARK 900 RELATED ID: 2TRY RELATED DB: PDB
REMARK 900 TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS
REMARK 900 AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
REMARK 900 RELATED ID: 2ROX RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH THYROXINE (T4)
REMARK 900 RELATED ID: 2ROY RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5'-DINITRO-N-
REMARK 900 ACETYL-L-THYRONINE
REMARK 900 RELATED ID: 1TTR RELATED DB: PDB
REMARK 900 TRANSTHYRETIN - V/122/I CARDIOMYOPATHIC MUTANT
REMARK 900 RELATED ID: 1TSH RELATED DB: PDB
REMARK 900 TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS
REMARK 900 AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
REMARK 900 RELATED ID: 1E3F RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW
REMARK 900 MODE OF BINDING
REMARK 900 RELATED ID: 1BZD RELATED DB: PDB
REMARK 900 TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS
REMARK 900 AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
REMARK 900 RELATED ID: 1BZE RELATED DB: PDB
REMARK 900 TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS
REMARK 900 AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
REMARK 900 RELATED ID: 1BZ8 RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (DEL VAL122)
REMARK 900 RELATED ID: 5TTR RELATED DB: PDB
REMARK 900 LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1E5A RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW
REMARK 900 MODE OF BINDING
DBREF 1E4H A 1 127 UNP P02766 TTHY_HUMAN 21 147
DBREF 1E4H B 1 127 UNP P02766 TTHY_HUMAN 21 147
SEQADV 1E4H GLU A 63 UNP P02766 GLN 63 CONFLICT
SEQRES 1 A 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 A 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 A 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
SEQRES 1 B 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 B 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 B 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
HET GOL A 990 6
HET PBR A 998 12
HET GOL B 990 6
HET PBR B 999 12
HETNAM GOL GLYCEROL
HETNAM PBR PENTABROMOPHENOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 PBR 2(C6 H BR5 O)
FORMUL 7 HOH *152(H2 O)
HELIX 1 1 ASP A 74 LEU A 82 1 9
HELIX 2 2 ASP B 74 GLY B 83 1 10
SHEET 1 A 3 LEU A 12 ASP A 18 0
SHEET 2 A 3 ARG A 103 SER A 112 1 N TYR A 105 O MET A 13
SHEET 3 A 3 SER A 115 ASN A 124 -1 N THR A 123 O ARG A 104
SHEET 1 B 4 ALA A 91 ALA A 97 0
SHEET 2 B 4 GLY A 67 ILE A 73 -1 N ILE A 73 O ALA A 91
SHEET 3 B 4 ALA A 29 LYS A 35 -1 N PHE A 33 O LYS A 70
SHEET 4 B 4 TRP A 41 LYS A 48 -1 N GLY A 47 O VAL A 30
SHEET 1 C 3 LEU B 12 ASP B 18 0
SHEET 2 C 3 ARG B 104 SER B 112 1 N TYR B 105 O MET B 13
SHEET 3 C 3 SER B 115 THR B 123 -1 N THR B 123 O ARG B 104
SHEET 1 D 4 ALA B 91 ALA B 97 0
SHEET 2 D 4 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 3 D 4 ALA B 29 LYS B 35 -1 N PHE B 33 O LYS B 70
SHEET 4 D 4 TRP B 41 LYS B 48 -1 N GLY B 47 O VAL B 30
SITE 1 AC1 6 HOH A2084 LYS B 15 LEU B 17 ALA B 108
SITE 2 AC1 6 THR B 119 HOH B2058
SITE 1 AC2 2 LYS A 15 THR A 119
SITE 1 AC3 3 TRP A 41 LYS A 70 GLU A 72
SITE 1 AC4 11 LEU A 110 SER A 117 HOH A2077 LEU B 110
SITE 2 AC4 11 LEU B 111 SER B 112 SER B 115 TYR B 116
SITE 3 AC4 11 SER B 117 HOH B2067 HOH B2068
CRYST1 43.000 85.400 64.400 90.00 90.00 90.00 P 21 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 0.023256 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015528 0.00000
MTRIX1 1 -0.993100 -0.117300 0.008200 85.51800 1
MTRIX2 1 -0.117400 0.993100 -0.000500 4.83600 1
MTRIX3 1 -0.008100 -0.001400 -1.000000 32.58500 1
(ATOM LINES ARE NOT SHOWN.)
END
