HEADER TRANSPORT PROTEIN 28-MAY-13 4KY2
TITLE TRANSTHYRETIN IN COMPLEX WITH THE FLUORESCENT FOLDING SENSOR (E)-7-
TITLE 2 HYDROXY-3-(4-HYDROXY-3,5-DIMETHYLSTYRYL)-4-METHYL-2H-CHROMEN-2-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATTR, PREALBUMIN, TBPA;
COMPND 5 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: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EPICURIAN GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMMHA
KEYWDS TETRAMER, HORMONE, TRANSPORT PROTEIN, T4, RETINOL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CONNELLY,I.A.WILSON,S.CHOI
REVDAT 3 20-SEP-23 4KY2 1 REMARK
REVDAT 2 05-FEB-14 4KY2 1 JRNL
REVDAT 1 28-AUG-13 4KY2 0
JRNL AUTH N.MYUNG,S.CONNELLY,B.KIM,S.J.PARK,I.A.WILSON,J.W.KELLY,
JRNL AUTH 2 S.CHOI
JRNL TITL BIFUNCTIONAL COUMARIN DERIVATIVES THAT INHIBIT TRANSTHYRETIN
JRNL TITL 2 AMYLOIDOGENESIS AND SERVE AS FLUORESCENT TRANSTHYRETIN
JRNL TITL 3 FOLDING SENSORS.
JRNL REF CHEM.COMMUN.(CAMB.) V. 49 9188 2013
JRNL REFN ISSN 1359-7345
JRNL PMID 23989101
JRNL DOI 10.1039/C3CC44667K
REMARK 2
REMARK 2 RESOLUTION. 1.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 87538
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4383
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) : 1.13
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5012
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 246
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1783
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : 0.34000
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): 0.035
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.033
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.788
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2120 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1415 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2947 ; 1.705 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3503 ; 0.943 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 300 ; 6.209 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;31.425 ;24.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 355 ;14.104 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;19.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 325 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2446 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 442 ; 0.001 ; 0.020
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): 1267 ; 1.874 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 499 ; 0.770 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2099 ; 2.922 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 853 ; 3.374 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 812 ; 5.002 ; 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): 3535 ; 1.594 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 250 ; 7.929 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3447 ; 4.860 ; 3.000
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
REMARK 4
REMARK 4 4KY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000079938.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87639
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.130
REMARK 200 RESOLUTION RANGE LOW (A) : 38.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2FBR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE WT-TTR WAS CONCENTRATED TO 4 MG/ML
REMARK 280 IN 10 MM NAPI, 100 MM KCL, AT PH 7.6 AND CO-CRYSTALLIZED AT ROOM
REMARK 280 TEMPERATURE USING THE VAPOR DIFFUSION SITTING DROP METHOD.
REMARK 280 CRYSTALS WERE GROWN FROM 1.395 M SODIUM CITRATE, 3.5% V/V
REMARK 280 GLYCEROL AT PH 5.5. THE CRYSTALS WERE FROZEN USING A CRYO-
REMARK 280 PROTECTANT SOLUTION OF 1.395 M SODIUM CITRATE, PH 5.5,
REMARK 280 CONTAINING 10% V/V GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298.0K
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 21.39650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.82300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.39650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.82300
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 CAT 1W3 A 201 LIES ON A SPECIAL POSITION.
REMARK 375 CAT 1W3 B 201 LIES ON A SPECIAL POSITION.
REMARK 375 OAF 1W3 B 201 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 PRO B 125
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 CYS A 10 SG
REMARK 470 CYS B 10 SG
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 OD1 ASP A 99 O HOH A 428 1.85
REMARK 500 NH2 ARG B 103 O HOH B 304 2.01
REMARK 500 OE1 GLU A 92 OE1 GLU B 92 2.17
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 1W3 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1W3 B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DVS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH RESVERATROL
REMARK 900 RELATED ID: 3CN0 RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) IN COMPLEX WITH 3,5-DIMETHYL-4-
REMARK 900 HYDROXYSTILBENE
REMARK 900 RELATED ID: 3CN1 RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (TTR) IN COMPLEX WITH 3,5-DIBROMO-4-
REMARK 900 HYDROXYSTILBENE
REMARK 900 RELATED ID: 3CN3 RELATED DB: PDB
REMARK 900 RELATED ID: 3CN4 RELATED DB: PDB
DBREF 4KY2 A 1 127 UNP P02766 TTHY_HUMAN 21 147
DBREF 4KY2 B 1 127 UNP P02766 TTHY_HUMAN 21 147
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 1W3 A 201 24
HET 1W3 B 201 24
HETNAM 1W3 7-HYDROXY-3-[(E)-2-(4-HYDROXY-3,5-DIMETHYLPHENYL)
HETNAM 2 1W3 ETHENYL]-4-METHYL-2H-CHROMEN-2-ONE
HETSYN 1W3 (E)-7-HYDROXY-3-(4-HYDROXY-3,5-DIMETHYLSTYRYL)-4-
HETSYN 2 1W3 METHYL-2H-CHROMEN-2-ONE
FORMUL 3 1W3 2(C20 H18 O4)
FORMUL 5 HOH *250(H2 O)
HELIX 1 1 ASP A 74 LEU A 82 1 9
HELIX 2 2 ASP B 74 LEU B 82 1 9
SHEET 1 A 8 SER A 23 PRO A 24 0
SHEET 2 A 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 A 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 A 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 A 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 A 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 A 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 A 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 B 8 GLU A 54 LEU A 55 0
SHEET 2 B 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 B 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 B 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 B 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 B 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 B 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 B 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 C 8 TRP A 41 LYS A 48 0
SHEET 2 C 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 C 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 C 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 C 8 HIS B 88 ALA B 97 -1 O VAL B 94 N GLU A 89
SHEET 6 C 8 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 7 C 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 C 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
SITE 1 AC1 8 LYS A 15 LEU A 17 GLU A 54 ALA A 108
SITE 2 AC1 8 LEU A 110 SER A 117 HOH A 426 HOH A 427
SITE 1 AC2 5 LYS B 15 LEU B 17 ALA B 108 LEU B 110
SITE 2 AC2 5 SER B 117
CRYST1 42.793 85.646 63.562 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 0.023368 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
