Header list of 1wwy.pdb file
Complete list - r 2 2 Bytes
HEADER APOPTOSIS 18-JAN-05 1WWY
TITLE SOLUTION STRUCTURE OF THE DUF1000 DOMAIN OF A THIOREDOXIN-LIKE PROTEIN
TITLE 2 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DUF1000 DOMAIN;
COMPND 5 SYNONYM: 32 KDA THIOREDOXIN-RELATED PROTEIN;
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: TXNL1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, HYPOTHETICAL PROTEIN, REGULATORY PROTEIN,
KEYWDS 2 APOPTOSIS, CANCER, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 3 RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WWY 1 REMARK SEQADV
REVDAT 3 02-JUN-10 1WWY 1 JRNL
REVDAT 2 24-FEB-09 1WWY 1 VERSN
REVDAT 1 18-JUL-05 1WWY 0
JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.INOUE,A.TANAKA,
JRNL AUTH 2 S.SUGANO,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DUF1000 DOMAIN OF THE
JRNL TITL 2 HUMAN THIOREDOXIN-LIKE 1 PROTEIN.
JRNL REF PROTEINS V. 78 2176 2010
JRNL REFN ISSN 0887-3585
JRNL PMID 20455272
JRNL DOI 10.1002/PROT.22719
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), PETER GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024098.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.02MM DUF1000 DOMAIN, 20MM TRIS
REMARK 210 -HCL, 100MM NACL, 1MM D-DTT,
REMARK 210 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.896
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 1 SER A 2 -178.96 60.33
REMARK 500 1 CYS A 47 -65.01 -146.23
REMARK 500 1 ASP A 48 -169.76 -179.44
REMARK 500 1 PRO A 71 -170.84 -69.78
REMARK 500 1 LYS A 78 -76.70 -114.78
REMARK 500 1 ARG A 88 -38.82 -179.66
REMARK 500 1 ASP A 91 -169.62 -102.81
REMARK 500 1 GLN A 102 -76.03 -136.29
REMARK 500 1 ALA A 103 114.81 64.62
REMARK 500 1 ASN A 126 95.21 -160.87
REMARK 500 1 GLN A 135 -63.56 -108.20
REMARK 500 1 GLU A 141 170.41 -51.89
REMARK 500 1 GLN A 157 113.90 -165.03
REMARK 500 1 ASP A 163 -172.40 -178.55
REMARK 500 1 PHE A 164 104.20 62.86
REMARK 500 1 SER A 166 173.70 61.05
REMARK 500 2 TYR A 9 -172.15 -60.82
REMARK 500 2 CYS A 47 -67.78 -156.31
REMARK 500 2 PRO A 71 -170.86 -69.79
REMARK 500 2 LYS A 78 -75.05 -119.98
REMARK 500 2 ARG A 88 -73.53 -171.26
REMARK 500 2 ASP A 91 -169.65 -103.35
REMARK 500 2 GLN A 102 -75.20 -137.66
REMARK 500 2 ALA A 103 117.56 65.22
REMARK 500 2 PHE A 124 31.74 -99.54
REMARK 500 2 GLU A 141 171.63 -52.56
REMARK 500 2 GLN A 157 113.54 -164.21
REMARK 500 2 ALA A 158 -75.76 -136.93
REMARK 500 2 THR A 159 -178.26 -171.23
REMARK 500 2 LYS A 165 104.46 63.18
REMARK 500 2 SER A 166 -176.54 57.61
REMARK 500 2 PRO A 168 -175.91 -69.80
REMARK 500 2 SER A 170 -71.63 -81.17
REMARK 500 3 SER A 2 75.62 58.12
REMARK 500 3 SER A 6 104.03 63.02
REMARK 500 3 CYS A 47 -71.56 -140.43
REMARK 500 3 PRO A 71 -170.90 -69.72
REMARK 500 3 LYS A 78 -75.31 -120.23
REMARK 500 3 ARG A 88 -73.22 -171.29
REMARK 500 3 ASP A 91 -169.67 -102.92
REMARK 500 3 GLN A 102 -74.83 -140.21
REMARK 500 3 ALA A 103 117.93 65.32
REMARK 500 3 GLU A 141 171.01 -52.29
REMARK 500 3 ALA A 158 -174.29 -171.84
REMARK 500 3 LYS A 165 99.33 60.45
REMARK 500 3 SER A 169 94.14 58.97
REMARK 500 4 SER A 2 -177.18 58.25
REMARK 500 4 SER A 3 106.47 -173.82
REMARK 500 4 SER A 5 -68.82 -162.19
REMARK 500 4 CYS A 47 -69.46 -169.16
REMARK 500
REMARK 500 THIS ENTRY HAS 356 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003443.1 RELATED DB: TARGETDB
DBREF 1WWY A 8 165 UNP O43396 TXNL1_HUMAN 122 279
SEQADV 1WWY GLY A 1 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 2 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 3 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY GLY A 4 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 5 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 6 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY GLY A 7 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 166 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY GLY A 167 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY PRO A 168 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 169 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY SER A 170 UNP O43396 CLONING ARTIFACT
SEQADV 1WWY GLY A 171 UNP O43396 CLONING ARTIFACT
SEQRES 1 A 171 GLY SER SER GLY SER SER GLY GLY TYR MET ASP LEU MET
SEQRES 2 A 171 PRO PHE ILE ASN LYS ALA GLY CYS GLU CYS LEU ASN GLU
SEQRES 3 A 171 SER ASP GLU HIS GLY PHE ASP ASN CYS LEU ARG LYS ASP
SEQRES 4 A 171 THR THR PHE LEU GLU SER ASP CYS ASP GLU GLN LEU LEU
SEQRES 5 A 171 ILE THR VAL ALA PHE ASN GLN PRO VAL LYS LEU TYR SER
SEQRES 6 A 171 MET LYS PHE GLN GLY PRO ASP ASN GLY GLN GLY PRO LYS
SEQRES 7 A 171 TYR VAL LYS ILE PHE ILE ASN LEU PRO ARG SER MET ASP
SEQRES 8 A 171 PHE GLU GLU ALA GLU ARG SER GLU PRO THR GLN ALA LEU
SEQRES 9 A 171 GLU LEU THR GLU ASP ASP ILE LYS GLU ASP GLY ILE VAL
SEQRES 10 A 171 PRO LEU ARG TYR VAL LYS PHE GLN ASN VAL ASN SER VAL
SEQRES 11 A 171 THR ILE PHE VAL GLN SER ASN GLN GLY GLU GLU GLU THR
SEQRES 12 A 171 THR ARG ILE SER TYR PHE THR PHE ILE GLY THR PRO VAL
SEQRES 13 A 171 GLN ALA THR ASN MET ASN ASP PHE LYS SER GLY PRO SER
SEQRES 14 A 171 SER GLY
HELIX 1 1 LEU A 12 ILE A 16 5 5
HELIX 2 2 GLU A 93 SER A 98 1 6
SHEET 1 A 3 GLU A 22 LEU A 24 0
SHEET 2 A 3 LEU A 52 PHE A 68 -1 O THR A 54 N GLU A 22
SHEET 3 A 3 VAL A 117 PRO A 118 -1 O VAL A 117 N MET A 66
SHEET 1 B 5 LEU A 104 GLU A 105 0
SHEET 2 B 5 TYR A 79 ILE A 84 -1 N VAL A 80 O LEU A 104
SHEET 3 B 5 VAL A 127 VAL A 134 -1 O THR A 131 N PHE A 83
SHEET 4 B 5 LEU A 52 PHE A 68 -1 N ILE A 53 O ILE A 132
SHEET 5 B 5 PHE A 149 PRO A 155 -1 O ILE A 152 N SER A 65
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes