Header list of 1x5e.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 15-MAY-05 1X5E
TITLE THE SOLUTION STRUCTURE OF THE THIOREDOXIN-LIKE DOMAIN OF HUMAN
TITLE 2 THIOREDOXIN-RELATED TRANSMEMBRANE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN DOMAIN CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOREDOXIN LIKE DOMAIN;
COMPND 5 SYNONYM: THIOREDOXIN-RELATED TRANSMEMBRANE 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: TXNDC;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041108-16;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TMX, THIOREDOXIN, TXNDC1, REDOX, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, ELECTRON
KEYWDS 4 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5E 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5E 1 VERSN
REVDAT 1 15-NOV-05 1X5E 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE THIOREDOXIN-LIKE DOMAIN OF
JRNL TITL 2 HUMAN THIOREDOXIN-RELATED TRANSMEMBRANE PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024400.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM THIOREDOXIN LIKE DOMAIN U
REMARK 210 -15N,13C; 20MM D-TRIS HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.926, CYANA 2.0.17
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,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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 GLU A 55 54.97 70.55
REMARK 500 1 THR A 64 -32.49 -131.58
REMARK 500 1 PHE A 104 -26.17 -38.76
REMARK 500 1 ILE A 105 -62.32 -99.35
REMARK 500 1 LYS A 108 32.60 34.53
REMARK 500 1 PRO A 115 -170.06 -69.80
REMARK 500 1 PRO A 123 83.57 -69.74
REMARK 500 1 SER A 125 42.21 -96.44
REMARK 500 2 SER A 2 126.67 -171.93
REMARK 500 2 PHE A 73 34.63 -83.88
REMARK 500 2 ILE A 74 49.90 32.68
REMARK 500 2 GLU A 88 170.91 -56.24
REMARK 500 2 TYR A 92 -70.17 -52.41
REMARK 500 2 ILE A 105 -63.77 -98.09
REMARK 500 2 SER A 117 -70.61 -130.94
REMARK 500 2 SER A 118 37.88 34.16
REMARK 500 2 PRO A 123 99.51 -69.79
REMARK 500 3 SER A 2 98.40 -46.65
REMARK 500 3 ILE A 74 123.98 -29.38
REMARK 500 3 ILE A 75 77.34 -119.05
REMARK 500 3 GLN A 93 74.81 -114.81
REMARK 500 3 SER A 117 152.22 -39.50
REMARK 500 3 SER A 118 135.11 -35.34
REMARK 500 3 SER A 121 117.37 -163.87
REMARK 500 4 SER A 5 134.89 -34.65
REMARK 500 4 GLU A 19 -36.43 -38.57
REMARK 500 4 PRO A 32 2.68 -69.69
REMARK 500 4 ALA A 48 -19.45 -47.59
REMARK 500 4 LEU A 69 -37.76 -39.93
REMARK 500 4 PHE A 73 32.34 -84.65
REMARK 500 4 ILE A 74 38.87 33.86
REMARK 500 4 GLN A 93 68.86 -118.03
REMARK 500 4 ILE A 105 -61.57 -91.57
REMARK 500 4 LYS A 108 42.30 35.17
REMARK 500 4 PRO A 115 -175.60 -69.73
REMARK 500 4 SER A 118 85.05 -63.53
REMARK 500 5 SER A 5 45.67 -97.66
REMARK 500 5 LEU A 69 -34.37 -39.87
REMARK 500 5 GLN A 93 49.40 -107.38
REMARK 500 5 ILE A 105 -60.36 -102.55
REMARK 500 5 LYS A 108 38.44 33.41
REMARK 500 5 SER A 117 -38.70 -130.85
REMARK 500 5 SER A 118 95.62 -50.95
REMARK 500 6 SER A 6 45.20 -88.21
REMARK 500 6 PRO A 32 3.62 -69.79
REMARK 500 6 LYS A 108 40.44 35.45
REMARK 500 6 SER A 118 92.45 -45.07
REMARK 500 6 PRO A 123 -176.79 -69.78
REMARK 500 7 SER A 3 113.93 -171.92
REMARK 500 7 GLU A 19 -35.85 -39.47
REMARK 500
REMARK 500 THIS ENTRY HAS 152 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002022397.1 RELATED DB: TARGETDB
DBREF 1X5E A 8 120 UNP Q9H3N1 TXND1_HUMAN 30 142
SEQADV 1X5E GLY A 1 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 2 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 3 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E GLY A 4 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 5 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 6 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E GLY A 7 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 121 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E GLY A 122 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E PRO A 123 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 124 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E SER A 125 UNP Q9H3N1 CLONING ARTIFACT
SEQADV 1X5E GLY A 126 UNP Q9H3N1 CLONING ARTIFACT
SEQRES 1 A 126 GLY SER SER GLY SER SER GLY ASN VAL ARG VAL ILE THR
SEQRES 2 A 126 ASP GLU ASN TRP ARG GLU LEU LEU GLU GLY ASP TRP MET
SEQRES 3 A 126 ILE GLU PHE TYR ALA PRO TRP CYS PRO ALA CYS GLN ASN
SEQRES 4 A 126 LEU GLN PRO GLU TRP GLU SER PHE ALA GLU TRP GLY GLU
SEQRES 5 A 126 ASP LEU GLU VAL ASN ILE ALA LYS VAL ASP VAL THR GLU
SEQRES 6 A 126 GLN PRO GLY LEU SER GLY ARG PHE ILE ILE ASN ALA LEU
SEQRES 7 A 126 PRO THR ILE TYR HIS CYS LYS ASP GLY GLU PHE ARG ARG
SEQRES 8 A 126 TYR GLN GLY PRO ARG THR LYS LYS ASP PHE ILE ASN PHE
SEQRES 9 A 126 ILE SER ASP LYS GLU TRP LYS SER ILE GLU PRO VAL SER
SEQRES 10 A 126 SER TRP PHE SER GLY PRO SER SER GLY
HELIX 1 1 ASN A 16 LEU A 21 1 6
HELIX 2 2 CYS A 34 GLU A 52 1 19
HELIX 3 3 ASP A 53 GLU A 55 5 3
HELIX 4 4 GLN A 66 PHE A 73 1 8
HELIX 5 5 THR A 97 ASP A 107 1 11
HELIX 6 6 LYS A 108 ILE A 113 5 6
SHEET 1 A 6 VAL A 9 VAL A 11 0
SHEET 2 A 6 ASN A 57 ASP A 62 1 O ILE A 58 N ARG A 10
SHEET 3 A 6 ASP A 24 TYR A 30 1 N MET A 26 O ALA A 59
SHEET 4 A 6 THR A 80 LYS A 85 -1 O THR A 80 N PHE A 29
SHEET 5 A 6 GLU A 88 ARG A 91 -1 O GLU A 88 N LYS A 85
SHEET 6 A 6 PRO A 115 VAL A 116 -1 O VAL A 116 N PHE A 89
CISPEP 1 LEU A 78 PRO A 79 1 -0.20
CISPEP 2 LEU A 78 PRO A 79 2 -0.11
CISPEP 3 LEU A 78 PRO A 79 3 -0.16
CISPEP 4 LEU A 78 PRO A 79 4 -0.15
CISPEP 5 LEU A 78 PRO A 79 5 -0.14
CISPEP 6 LEU A 78 PRO A 79 6 -0.12
CISPEP 7 LEU A 78 PRO A 79 7 -0.13
CISPEP 8 LEU A 78 PRO A 79 8 -0.17
CISPEP 9 LEU A 78 PRO A 79 9 -0.14
CISPEP 10 LEU A 78 PRO A 79 10 -0.12
CISPEP 11 LEU A 78 PRO A 79 11 -0.14
CISPEP 12 LEU A 78 PRO A 79 12 -0.11
CISPEP 13 LEU A 78 PRO A 79 13 -0.10
CISPEP 14 LEU A 78 PRO A 79 14 -0.08
CISPEP 15 LEU A 78 PRO A 79 15 -0.12
CISPEP 16 LEU A 78 PRO A 79 16 -0.16
CISPEP 17 LEU A 78 PRO A 79 17 -0.15
CISPEP 18 LEU A 78 PRO A 79 18 -0.19
CISPEP 19 LEU A 78 PRO A 79 19 -0.03
CISPEP 20 LEU A 78 PRO A 79 20 -0.08
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