HEADER TRANSPORT PROTEIN 30-MAY-14 4TLT
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 29-147;
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 GENE: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS HUMAN TRANSTHYRETIN, AMYLOID, TRANSTHYRETIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SAELICES,D.CASCIO,M.SAWAYA,D.S.EISENBERG
REVDAT 4 27-DEC-23 4TLT 1 JRNL REMARK LINK
REVDAT 3 09-DEC-15 4TLT 1 JRNL
REVDAT 2 28-OCT-15 4TLT 1 JRNL
REVDAT 1 21-OCT-15 4TLT 0
JRNL AUTH L.SAELICES,L.M.JOHNSON,W.Y.LIANG,M.R.SAWAYA,D.CASCIO,
JRNL AUTH 2 P.RUCHALA,J.WHITELEGGE,L.JIANG,R.RIEK,D.S.EISENBERG
JRNL TITL UNCOVERING THE MECHANISM OF AGGREGATION OF HUMAN
JRNL TITL 2 TRANSTHYRETIN.
JRNL REF J.BIOL.CHEM. V. 290 28932 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26459562
JRNL DOI 10.1074/JBC.M115.659912
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 24511
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1241
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.78
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2884
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2304
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2750
REMARK 3 BIN R VALUE (WORKING SET) : 0.2286
REMARK 3 BIN FREE R VALUE : 0.2671
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.65
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
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 : 1784
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.25300
REMARK 3 B22 (A**2) : -1.24270
REMARK 3 B33 (A**2) : -1.01030
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.229
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.112
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.109
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.112
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.109
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1852 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2535 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 604 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 36 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 274 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1852 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 248 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2084 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.73
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.48
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7103 13.0093 68.9756
REMARK 3 T TENSOR
REMARK 3 T11: -0.0199 T22: -0.0119
REMARK 3 T33: -0.0221 T12: -0.0062
REMARK 3 T13: -0.0058 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.6477 L22: 0.8459
REMARK 3 L33: 0.5982 L12: 0.3982
REMARK 3 L13: -0.1141 L23: -0.0432
REMARK 3 S TENSOR
REMARK 3 S11: -0.0954 S12: 0.0045 S13: 0.0551
REMARK 3 S21: -0.1016 S22: 0.0346 S23: 0.0282
REMARK 3 S31: 0.0059 S32: 0.0163 S33: 0.0608
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9864 12.2274 88.5669
REMARK 3 T TENSOR
REMARK 3 T11: -0.0406 T22: 0.0067
REMARK 3 T33: -0.0338 T12: 0.0139
REMARK 3 T13: -0.0123 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 1.0129 L22: 1.1683
REMARK 3 L33: 0.7825 L12: -0.3102
REMARK 3 L13: -0.4114 L23: 0.6833
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: -0.0165 S13: 0.1150
REMARK 3 S21: 0.1181 S22: -0.0587 S23: 0.0365
REMARK 3 S31: 0.0406 S32: -0.1311 S33: 0.1041
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TLT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG-1000, 0.1M IMIDAZOLE,
REMARK 280 0.2M CALCIUM ACETATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 20.62000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.62000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.12000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 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 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 LYS A 9
REMARK 465 PRO A 125
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 LYS B 9
REMARK 465 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 HIS B 133
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 44 -50.15 -123.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 66 OE1
REMARK 620 2 ASP A 99 O 97.0
REMARK 620 3 ASP A 99 OD1 90.3 67.8
REMARK 620 4 HOH A 301 O 147.2 55.9 94.6
REMARK 620 5 HOH A 304 O 154.4 108.3 95.9 57.0
REMARK 620 6 HOH A 309 O 82.3 144.2 147.7 108.5 79.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 58 O
REMARK 620 2 GLU B 66 OE1 57.3
REMARK 620 3 GLU B 66 OE2 51.1 6.2
REMARK 620 4 HOH B 302 O 52.9 5.0 2.6
REMARK 620 5 HOH B 303 O 54.4 8.2 8.5 9.9
REMARK 620 6 HOH B 305 O 60.5 6.6 11.2 11.0 6.5
REMARK 620 7 HOH B 307 O 49.9 8.2 3.9 6.3 6.0 10.9
REMARK 620 8 HOH B 315 O 55.0 4.6 5.7 6.4 3.8 5.8 5.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TKW RELATED DB: PDB
REMARK 900 RELATED ID: 4TL4 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL5 RELATED DB: PDB
REMARK 900 RELATED ID: 4TLK RELATED DB: PDB
REMARK 900 RELATED ID: 4TLS RELATED DB: PDB
REMARK 900 RELATED ID: 4TLU RELATED DB: PDB
REMARK 900 RELATED ID: 4TM9 RELATED DB: PDB
REMARK 900 RELATED ID: 4TNE RELATED DB: PDB
REMARK 900 RELATED ID: 4TNF RELATED DB: PDB
REMARK 900 RELATED ID: 4TNG RELATED DB: PDB
DBREF 4TLT A 9 127 UNP P02766 TTHY_HUMAN 29 147
DBREF 4TLT B 9 127 UNP P02766 TTHY_HUMAN 29 147
SEQADV 4TLT HIS A 128 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS A 129 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS A 130 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS A 131 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS A 132 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS A 133 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 128 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 129 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 130 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 131 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 132 UNP P02766 EXPRESSION TAG
SEQADV 4TLT HIS B 133 UNP P02766 EXPRESSION TAG
SEQRES 1 A 125 LYS OCS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL ARG
SEQRES 2 A 125 GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE ARG
SEQRES 3 A 125 LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER GLY
SEQRES 4 A 125 LYS THR SER GLU SER GLY GLU LEU HIS GLY LEU THR THR
SEQRES 5 A 125 GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU ILE
SEQRES 6 A 125 ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER PRO
SEQRES 7 A 125 PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN ASP
SEQRES 8 A 125 SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU SER
SEQRES 9 A 125 PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN PRO
SEQRES 10 A 125 LYS GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 125 LYS OCS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL ARG
SEQRES 2 B 125 GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE ARG
SEQRES 3 B 125 LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER GLY
SEQRES 4 B 125 LYS THR SER GLU SER GLY GLU LEU HIS GLY LEU THR THR
SEQRES 5 B 125 GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU ILE
SEQRES 6 B 125 ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER PRO
SEQRES 7 B 125 PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN ASP
SEQRES 8 B 125 SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU SER
SEQRES 9 B 125 PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN PRO
SEQRES 10 B 125 LYS GLU HIS HIS HIS HIS HIS HIS
MODRES 4TLT OCS A 10 CYS MODIFIED RESIDUE
MODRES 4TLT OCS B 10 CYS MODIFIED RESIDUE
HET OCS A 10 9
HET OCS B 10 9
HET MG A 201 1
HET MG B 201 1
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM MG MAGNESIUM ION
FORMUL 1 OCS 2(C3 H7 N O5 S)
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *69(H2 O)
HELIX 1 AA1 ASP A 74 LEU A 82 1 9
HELIX 2 AA2 ASP B 74 LEU B 82 1 9
SHEET 1 AA1 8 SER A 23 PRO A 24 0
SHEET 2 AA1 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 AA1 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA1 8 SER A 115 THR A 123 -1 O SER A 117 N LEU A 110
SHEET 5 AA1 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N SER B 112 O SER B 115
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 GLU A 54 LEU A 55 0
SHEET 2 AA2 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 AA2 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA2 8 SER A 115 THR A 123 -1 O SER A 117 N LEU A 110
SHEET 5 AA2 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 AA2 8 ARG B 104 SER B 112 -1 N SER B 112 O SER B 115
SHEET 7 AA2 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA2 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 AA3 8 TRP A 41 LYS A 48 0
SHEET 2 AA3 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA3 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA3 8 HIS A 88 ALA A 97 -1 O ALA A 97 N GLY A 67
SHEET 5 AA3 8 HIS B 88 ALA B 97 -1 O GLU B 89 N VAL A 94
SHEET 6 AA3 8 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 7 AA3 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 AA3 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
LINK C OCS A 10 N PRO A 11 1555 1555 1.34
LINK C OCS B 10 N PRO B 11 1555 1555 1.34
LINK OE1 GLU A 66 MG MG A 201 1555 1555 2.45
LINK O ASP A 99 MG MG A 201 1555 1555 2.70
LINK OD1 ASP A 99 MG MG A 201 1555 1555 2.31
LINK MG MG A 201 O HOH A 301 1555 1555 2.24
LINK MG MG A 201 O HOH A 304 1555 4557 2.36
LINK MG MG A 201 O HOH A 309 1555 1555 2.50
LINK O LEU B 58 MG MG B 201 1555 4558 2.39
LINK OE1 GLU B 66 MG MG B 201 1555 1555 2.28
LINK OE2 GLU B 66 MG MG B 201 1555 1555 2.84
LINK MG MG B 201 O HOH B 302 1555 4458 2.16
LINK MG MG B 201 O HOH B 303 1555 1555 2.55
LINK MG MG B 201 O HOH B 305 1555 4458 2.33
LINK MG MG B 201 O HOH B 307 1555 1555 2.52
LINK MG MG B 201 O HOH B 315 1555 4458 2.39
SITE 1 AC1 5 GLU A 66 ASP A 99 HOH A 301 HOH A 304
SITE 2 AC1 5 HOH A 309
SITE 1 AC2 3 GLU B 66 HOH B 303 HOH B 307
CRYST1 41.240 84.240 63.080 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 0.024248 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015853 0.00000
HETATM 1 N OCS A 10 7.636 10.676 55.127 1.00 45.70 N
ANISOU 1 N OCS A 10 6268 5799 5297 -564 351 259 N
HETATM 2 CA OCS A 10 6.817 11.002 56.293 1.00 44.50 C
ANISOU 2 CA OCS A 10 6065 5648 5195 -509 277 278 C
HETATM 3 CB OCS A 10 5.644 10.101 56.504 1.00 49.75 C
ANISOU 3 CB OCS A 10 6743 6304 5855 -500 255 267 C
HETATM 4 SG OCS A 10 4.217 11.154 56.689 1.00 54.74 S
ANISOU 4 SG OCS A 10 7370 6938 6490 -506 135 304 S
HETATM 5 C OCS A 10 7.636 10.842 57.559 1.00 38.73 C
ANISOU 5 C OCS A 10 5257 4923 4534 -437 305 271 C
HETATM 6 O OCS A 10 7.759 9.734 58.084 1.00 38.60 O
ANISOU 6 O OCS A 10 5222 4902 4544 -397 351 250 O
HETATM 7 OD1 OCS A 10 3.559 11.142 55.396 1.00 55.29 O
ANISOU 7 OD1 OCS A 10 7511 7006 6492 -580 108 313 O
HETATM 8 OD2 OCS A 10 4.632 12.642 56.758 1.00 55.13 O
ANISOU 8 OD2 OCS A 10 7401 6990 6555 -508 90 335 O
HETATM 9 OD3 OCS A 10 3.470 10.932 57.843 1.00 55.40 O
ANISOU 9 OD3 OCS A 10 7405 7022 6624 -450 103 303 O
(ATOM LINES ARE NOT SHOWN.)
END
