HEADER TRANSPORT PROTEIN 11-DEC-11 4ABU
TITLE CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 21-144;
COMPND 5 SYNONYM: ATTR, PREALBUMIN, TBPA;
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PMMHA
KEYWDS TRANSPORT PROTEIN, HORMONE, AMYLOIDOSIS INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.TOMAR,T.KHAN,R.R.SINGH,S.MISHRA,S.GUPTA,A.SUROLIA,D.M.SALUNKE
REVDAT 5 20-DEC-23 4ABU 1 REMARK
REVDAT 4 17-JUL-19 4ABU 1 REMARK
REVDAT 3 06-FEB-19 4ABU 1 REMARK
REVDAT 2 30-JAN-19 4ABU 1 REMARK
REVDAT 1 26-SEP-12 4ABU 0
JRNL AUTH D.TOMAR,T.KHAN,R.R.SINGH,S.MISHRA,S.GUPTA,A.SUROLIA,
JRNL AUTH 2 D.M.SALUNKE
JRNL TITL CRYSTALLOGRAPHIC STUDY OF NOVEL TRANSTHYRETIN LIGANDS
JRNL TITL 2 EXHIBITING NEGATIVE-COOPERATIVITY BETWEEN TWO THYROXINE
JRNL TITL 3 BINDING SITES.
JRNL REF PLOS ONE V. 7 43522 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22973437
JRNL DOI 10.1371/JOURNAL.PONE.0043522
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 19121
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1027
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1383
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.09000
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 1.36000
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): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.250
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1854 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2533 ; 2.069 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 228 ; 5.774 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;38.357 ;24.054
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 275 ;16.950 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;17.518 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 285 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1416 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1148 ; 1.580 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1862 ; 2.812 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 706 ; 3.984 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 671 ; 6.140 ; 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 : 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. U VALUES REFINED INDIVIDUALLY. FT1 A 1125 AND FT1 B
REMARK 3 1125 GENERATE CLOSE CONTACTS WITH COPIES RELATED BY A TWO-FOLD
REMARK 3 CRYSTALLOGRAPHIC AXIS. THEIR OCCUPANCIES HAVE THEREFORE BEEN
REMARK 3 DEFINED AS 0.5.
REMARK 4
REMARK 4 4ABU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1290050670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
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 : NI FILTER CMF12 38CU-6
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20168
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 35.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DVQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CHLORIDE, POTASSIUM
REMARK 280 PHOSPHATE, AMMONIUM SULFATE, PH 7.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 42.80000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.80000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.23500
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: 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 -1.000000 0.000000 0.000000 0.00000
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 HOH A2065 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2054 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 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 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 CYS A 10 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 ILE A 107 CG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASN A 124 N - CA - C ANGL. DEV. = 16.4 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 64 69.72 -105.32
REMARK 500 PHE B 64 76.21 -103.30
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 FT1 A 1125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FT1 B 1125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G9K RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH
REMARK 900 HYDROXYLATEDPOLYCHLORINATED BIPHENYL-4-HYDROXY-2',3,3',4 ',5-
REMARK 900 PENTACHLOROBIPHENYL
REMARK 900 RELATED ID: 1DVY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH N-( M-
REMARK 900 TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID
REMARK 900 RELATED ID: 1ETA RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (PREALBUMIN) NATURALLY OCCURRING VARIANT WITH 1:1 MIX
REMARK 900 OF VAL AND MET AT POSITION 30 COMPLEXED WITH THYROXINE (3,5,3',5'-
REMARK 900 TETRAIODO-L-THYRONINE)
REMARK 900 RELATED ID: 2B9A RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH DIFLUNISALANALOGUES -
REMARK 900 TTR.3',5'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1TTR RELATED DB: PDB
REMARK 900 TRANSTHYRETIN - V/122/I CARDIOMYOPATHIC MUTANT
REMARK 900 RELATED ID: 4AC2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-7
REMARK 900 RELATED ID: 1III RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C -DATA
REMARK 900 COLLECTED AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 1DVT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH
REMARK 900 FLURBIPROFEN
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: 1IJN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR C10A/ Y114C
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: 1TT6 RELATED DB: PDB
REMARK 900 THE ORTHORHOMBIC CRYSTAL STRUCTURE OF TRANSTHYRETIN INCOMPLEX WITH
REMARK 900 DIETHYLSTILBESTROL
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: 2B77 RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH DIFLUNISALANALOGUES -
REMARK 900 TTR.2',4'-DICHLORO-4-HYDROXY-1,1'-BIPHENYL-3- CARBOXYLIC ACID
REMARK 900 RELATED ID: 1TLM RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH MILRINONE
REMARK 900 RELATED ID: 1F41 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION
REMARK 900 RELATED ID: 1TYR RELATED DB: PDB
REMARK 900 TRANSTHYRETIN COMPLEX WITH RETINOIC ACID
REMARK 900 RELATED ID: 1E5A RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW
REMARK 900 MODE OF BINDING
REMARK 900 RELATED ID: 4ACT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-17
REMARK 900 RELATED ID: 2PAB RELATED DB: PDB
REMARK 900 PREALBUMIN (HUMAN PLASMA)
REMARK 900 RELATED ID: 1SOK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT A108Y/ L110ESOLVED IN
REMARK 900 SPACE GROUP P21212
REMARK 900 RELATED ID: 2WQA RELATED DB: PDB
REMARK 900 COMPLEX OF TTR AND RBP4 AND OLEIC ACID
REMARK 900 RELATED ID: 1E4H RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW
REMARK 900 MODE OF BINDING
REMARK 900 RELATED ID: 2ROX RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH THYROXINE (T4)
REMARK 900 RELATED ID: 2B15 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF 2,4-DINITROPHENOL IN COMPLEX WITHHUMAN
REMARK 900 TRANSTHYRETIN
REMARK 900 RELATED ID: 1FHN RELATED DB: PDB
REMARK 900 TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS
REMARK 900 RELATED ID: 1FH2 RELATED DB: PDB
REMARK 900 TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS
REMARK 900 RELATED ID: 1G1O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETINMUTANT
REMARK 900 TTR G53S/E54D/L55S
REMARK 900 RELATED ID: 4ABQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-1
REMARK 900 RELATED ID: 2B16 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF 2,4-DINITROPHENOL IN COMPLEX WITHTHE
REMARK 900 AMYLOIDOGENIC VARIANT TRANSTHYRETIN TYR78PHE
REMARK 900 RELATED ID: 2F8I RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH BENZOXAZOLE
REMARK 900 RELATED ID: 1IIK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C -DATA
REMARK 900 COLLECTED AT CRYO TEMPERATURE
REMARK 900 RELATED ID: 1TTA RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (FORMERLY PREALBUMIN)
REMARK 900 RELATED ID: 1BMZ RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (PREALBUMIN)
REMARK 900 RELATED ID: 2B14 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF 2,4-DINITROPHENOL IN COMPLEX WITHTHE
REMARK 900 AMYLOIDOGENIC VARIANT TRANSTHYRETIN LEU 55 PRO
REMARK 900 RELATED ID: 1DVS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH RESVERATROL
REMARK 900 RELATED ID: 1Z7J RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3,3',5,5'-
REMARK 900 TETRAIODOTHYROACETIC ACID (T4AC)
REMARK 900 RELATED ID: 1GKO RELATED DB: PDB
REMARK 900 AN ENGINEERED TRANSTHYRETIN MONOMER THAT IS NON- AMYLOIDOGENIC -
REMARK 900 UNLESS PARTIALLY DENATURED
REMARK 900 RELATED ID: 2FLM RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH BIVALANT AMYLOIDINHIBITOR
REMARK 900 (6 CARBON LINKER)
REMARK 900 RELATED ID: 2FBR RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH BIVALANT AMYLOIDINHIBITOR
REMARK 900 (4 CORBON LINKER)
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: 1DVU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH
REMARK 900 DIBENZOFURAN- 4,6-DICARBOXYLIC ACID
REMARK 900 RELATED ID: 1BZ8 RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (DEL VAL122)
REMARK 900 RELATED ID: 1TTB RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH ALA 109 REPLACED BY
REMARK 900 THR (A109T)
REMARK 900 RELATED ID: 1THC RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5 '-DIBROMO-
REMARK 900 2',4,4',6-TETRA-HYDROXYAURONE
REMARK 900 RELATED ID: 1DVZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH O-
REMARK 900 TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID
REMARK 900 RELATED ID: 1QWH RELATED DB: PDB
REMARK 900 A COVALENT DIMER OF TRANSTHYRETIN THAT AFFECTS THE AMYLOIDPATHWAY
REMARK 900 RELATED ID: 1DVQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN
REMARK 900 RELATED ID: 1THA RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3,3 '-DIIODO-L-
REMARK 900 THYRONINE
REMARK 900 RELATED ID: 1QAB RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HUMAN RETINOL BINDING PROTEIN WITH ITSCARRIER
REMARK 900 PROTEIN TRANSTHYRETIN REVEALS INTERACTION WITH THECARBOXY TERMINUS
REMARK 900 OF RBP
REMARK 900 RELATED ID: 1Y1D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITHIODODIFLUNISAL
REMARK 900 RELATED ID: 1F86 RELATED DB: PDB
REMARK 900 TRANSTHYRETIN THR119MET PROTEIN STABILISATION
REMARK 900 RELATED ID: 1U21 RELATED DB: PDB
REMARK 900 TRANSTHYRETIN WITH TETHERED INHIBITOR ON ONE MONOMER.
REMARK 900 RELATED ID: 1SOQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT A108Y/ L110ESOLVED IN
REMARK 900 SPACE GROUP C2
REMARK 900 RELATED ID: 2F7I RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH DIFLUNISALANALOGUES - TTR.
REMARK 900 2',6'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1X7S RELATED DB: PDB
REMARK 900 THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE AMYLOIDOGENICVARIANT
REMARK 900 TTR TYR78PHE
REMARK 900 RELATED ID: 4ABV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-3
REMARK 900 RELATED ID: 1ZCR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN WITH BOUND IODIDE
REMARK 900 RELATED ID: 1ICT RELATED DB: PDB
REMARK 900 MONOCLINIC FORM OF HUMAN TRANSTHYRETIN COMPLEXED WITHTHYROXINE (T4)
REMARK 900 RELATED ID: 1TTC RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH VAL 30 REPLACED BY
REMARK 900 MET (V30M)
REMARK 900 RELATED ID: 1DVX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC
REMARK 900 RELATED ID: 1BM7 RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (PREALBUMIN) COMPLEX WITH FLUFENAMIC ACID (2-
REMARK 900 [[3-(TRIFLUOROMETHYL)PHENYL]AMINO] BENZOIC ACID )
REMARK 900 RELATED ID: 2ROY RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5 '-DINITRO-
REMARK 900 N-ACETYL-L-THYRONINE
REMARK 900 RELATED ID: 1TZ8 RELATED DB: PDB
REMARK 900 THE MONOCLINIC CRYSTAL STRUTURE OF TRANSTHYRETIN IN COMPLEXWITH
REMARK 900 DIETHYLSTILBESTROL
REMARK 900 RELATED ID: 1ETB RELATED DB: PDB
REMARK 900 TRANSTHYRETIN (PREALBUMIN) MUTANT WITH ALA 109 REPLACED BY THR
REMARK 900 (A109T) COMPLEXED WITH THYROXINE (3,5,3',5'- TETRAIODO-L-THYRONINE)
REMARK 900 RELATED ID: 1RLB RELATED DB: PDB
REMARK 900 RETINOL BINDING PROTEIN COMPLEXED WITH TRANSTHYRETIN 1RLB 3
REMARK 900 RELATED ID: 5TTR RELATED DB: PDB
REMARK 900 LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1F64 RELATED DB: PDB
REMARK 900 LEU55PRO TTR-IDOX THEORETICAL MODEL
REMARK 900 RELATED ID: 2G5U RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH
REMARK 900 HYDROXYLATEDPOLYCHLORINATED BIPHENYL-4,4'-DIHYDROXY-3,3', 5,5'-
REMARK 900 TETRACHLOROBIPHENYL
REMARK 900 RELATED ID: 2GAB RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) COMPLEXED WITH
REMARK 900 HYDROXYLATEDPOLYCHLORINATED BIPHENYL-4-HYDROXY-3,3',5,4 '-
REMARK 900 TETRACHLOROBIPHENYL
REMARK 900 RELATED ID: 4AC4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-18
REMARK 900 RELATED ID: 1X7T RELATED DB: PDB
REMARK 900 STRUCTURE OF TTR R104H: A NON-AMYLOIDOGENIC VARIANT WITHPROTECTIVE
REMARK 900 CLINICAL EFFECTS
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: 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: 1ZD6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN WITH BOUND CHLORIDE
REMARK 900 RELATED ID: 4ABW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH LIGAND C-6
REMARK 900 RELATED ID: 4ANK RELATED DB: PDB
REMARK 900 CRYSTALLOGRAPHIC STUDY OF NOVEL TRANSTHYRETIN LIGANDS EXHIBITING
REMARK 900 NEGATIVE-COOPERATIVITY BETWEEN TWO T4 BINDING SITES.
DBREF 4ABU A 1 124 UNP P02766 TTHY_HUMAN 21 144
DBREF 4ABU B 1 124 UNP P02766 TTHY_HUMAN 21 144
SEQRES 1 A 124 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 124 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 124 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 124 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 124 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 A 124 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 124 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 124 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 124 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 A 124 THR THR ALA VAL VAL THR ASN
SEQRES 1 B 124 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 124 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 124 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 124 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 124 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 B 124 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 124 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 124 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 124 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 B 124 THR THR ALA VAL VAL THR ASN
HET FT1 A1125 18
HET FT1 B1125 18
HETNAM FT1 4-(2,4-DICHLOROPHENOXY)-3-HYDROXYBENZALDEHYDE
FORMUL 3 FT1 2(C13 H8 CL2 O3)
FORMUL 5 HOH *126(H2 O)
HELIX 1 1 ASP A 74 LEU A 82 1 9
HELIX 2 2 ASP B 74 ALA B 81 1 8
SHEET 1 AA 2 SER A 23 PRO A 24 0
SHEET 2 AA 2 LEU A 12 ASP A 18 -1 O ASP A 18 N SER A 23
SHEET 1 AB 2 GLU A 54 LEU A 55 0
SHEET 2 AB 2 LEU A 12 ASP A 18 -1 O VAL A 14 N LEU A 55
SHEET 1 BA 2 SER B 23 PRO B 24 0
SHEET 2 BA 2 LEU B 12 ASP B 18 -1 O ASP B 18 N SER B 23
SHEET 1 BB 2 GLU B 54 LEU B 55 0
SHEET 2 BB 2 LEU B 12 ASP B 18 -1 O VAL B 14 N LEU B 55
SHEET 1 AC 8 TRP A 41 LYS A 48 0
SHEET 2 AC 8 ALA A 29 LYS A 35 -1 O VAL A 30 N GLY A 47
SHEET 3 AC 8 GLY A 67 ILE A 73 -1 O ILE A 68 N LYS A 35
SHEET 4 AC 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 AC 8 HIS B 88 ALA B 97 -1 N GLU B 89 O VAL A 94
SHEET 6 AC 8 GLY B 67 ILE B 73 -1 O GLY B 67 N ALA B 97
SHEET 7 AC 8 ALA B 29 LYS B 35 -1 O HIS B 31 N GLU B 72
SHEET 8 AC 8 TRP B 41 LYS B 48 -1 O GLU B 42 N ARG B 34
SITE 1 AC1 7 LYS A 15 LEU A 17 ALA A 108 LEU A 110
SITE 2 AC1 7 SER A 117 THR A 118 THR A 119
SITE 1 AC2 6 LYS B 15 LEU B 17 ALA B 108 SER B 117
SITE 2 AC2 6 THR B 119 VAL B 121
CRYST1 85.600 42.470 63.870 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 0.011682 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015657 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
