Header list of 1wmj.pdb file
Complete list - r 2 2 Bytes
HEADER OXIDOREDUCTASE 09-JUL-04 1WMJ
TITLE SOLUTION STRUCTURE OF THIOREDOXIN TYPE H FROM ORYZA SATIVA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN H-TYPE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRX-H, PHLOEM SAP 13 KDA PROTEIN-1;
COMPND 5 EC: 1.8.4.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 4530;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST32A
KEYWDS STRUCTURAL GENOMICS, PROGRAM FOR RICE GENOME RESEARCH, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.KUMETA,H.OGURA,K.AKAGI,E.KATOH,F.INAGAKI
REVDAT 3 02-MAR-22 1WMJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WMJ 1 VERSN
REVDAT 1 25-OCT-05 1WMJ 0
JRNL AUTH H.KUMETA,H.OGURA,K.AKAGI,E.KATOH,F.INAGAKI
JRNL TITL SOLUTION STRUCTURE OF THIOREDOXIN TYPE H FROM ORYZA SATIVA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.06
REMARK 3 AUTHORS : WELCH (VNMR), GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WMJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023745.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.77MM U-13C,15N;20MM TRIS-HCL
REMARK 210 PH 7.4; 100MM NACL; 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 23, SPARKY 3.110, CYANA
REMARK 210 1.06
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -7
REMARK 465 PRO A -6
REMARK 465 MET A -5
REMARK 465 ALA A -4
REMARK 465 ALA A -3
REMARK 465 GLU A -2
REMARK 465 GLU A -1
REMARK 465 GLY A 0
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 ALA A 3 39.28 33.58
REMARK 500 1 GLU A 4 93.08 60.40
REMARK 500 1 GLU A 5 -155.93 -92.47
REMARK 500 1 VAL A 8 95.49 -52.95
REMARK 500 1 ILE A 9 168.29 -43.39
REMARK 500 1 CYS A 11 159.93 -47.48
REMARK 500 1 HIS A 12 36.29 -165.26
REMARK 500 1 ASN A 13 26.90 -178.77
REMARK 500 1 LYS A 14 -69.11 64.90
REMARK 500 1 PHE A 35 -164.24 -61.73
REMARK 500 1 THR A 36 136.02 161.71
REMARK 500 1 SER A 38 -34.36 -167.06
REMARK 500 1 CYS A 40 -59.00 77.78
REMARK 500 1 CYS A 43 31.27 35.02
REMARK 500 1 ARG A 44 -48.92 -158.43
REMARK 500 1 PRO A 48 4.23 -69.74
REMARK 500 1 PHE A 50 -71.92 -63.16
REMARK 500 1 PHE A 62 152.86 58.31
REMARK 500 1 LEU A 63 149.07 170.48
REMARK 500 1 VAL A 67 34.29 -82.56
REMARK 500 1 LYS A 71 -34.57 -32.67
REMARK 500 1 GLU A 72 -28.86 -36.13
REMARK 500 1 ASN A 78 72.36 72.75
REMARK 500 1 GLU A 80 -70.34 86.22
REMARK 500 1 ALA A 81 97.75 169.11
REMARK 500 1 MET A 82 168.69 174.93
REMARK 500 1 PRO A 83 36.31 -69.82
REMARK 500 1 PHE A 85 40.41 -81.78
REMARK 500 1 LEU A 86 142.11 -33.12
REMARK 500 1 ASP A 90 -6.98 81.49
REMARK 500 1 ALA A 92 -86.36 -145.67
REMARK 500 1 GLU A 93 103.64 -177.60
REMARK 500 1 ASP A 95 179.85 159.18
REMARK 500 1 VAL A 97 -95.31 -141.44
REMARK 500 1 VAL A 98 144.57 159.32
REMARK 500 1 ALA A 100 14.22 -155.50
REMARK 500 1 LEU A 105 -75.53 -78.72
REMARK 500 1 GLN A 106 -18.33 -48.86
REMARK 500 1 ALA A 115 14.80 54.92
REMARK 500 1 THR A 116 -32.50 -133.95
REMARK 500 1 ALA A 117 86.03 53.39
REMARK 500 1 SER A 119 89.89 -158.84
REMARK 500 1 ALA A 120 168.64 56.29
REMARK 500 1 SER A 121 -45.72 -136.11
REMARK 500 2 ALA A 2 -99.78 51.82
REMARK 500 2 ALA A 3 69.88 72.14
REMARK 500 2 GLU A 4 98.18 50.50
REMARK 500 2 GLU A 5 -153.24 -103.73
REMARK 500 2 VAL A 8 94.68 -50.89
REMARK 500 2 ILE A 9 167.31 -42.36
REMARK 500
REMARK 500 THIS ENTRY HAS 840 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EP7 RELATED DB: PDB
REMARK 900 A SAME PROTEIN FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 1ERT RELATED DB: PDB
REMARK 900 A SAME PROTEIN FROM HUMAN (REDUCED FORM)
REMARK 900 RELATED ID: 1ERU RELATED DB: PDB
REMARK 900 A SAME PROTEIN FROM HUMAN (OXIDIZED FORM)
REMARK 900 RELATED ID: 1SRX RELATED DB: PDB
REMARK 900 A SAME PROTEIN FROM E. COLI
DBREF 1WMJ A 1 122 UNP Q42443 TRXH_ORYSA 1 122
SEQADV 1WMJ GLY A -7 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ PRO A -6 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ MET A -5 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ ALA A -4 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ ALA A -3 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ GLU A -2 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ GLU A -1 UNP Q42443 CLONING ARTIFACT
SEQADV 1WMJ GLY A 0 UNP Q42443 CLONING ARTIFACT
SEQRES 1 A 130 GLY PRO MET ALA ALA GLU GLU GLY MET ALA ALA GLU GLU
SEQRES 2 A 130 GLY VAL VAL ILE ALA CYS HIS ASN LYS ASP GLU PHE ASP
SEQRES 3 A 130 ALA GLN MET THR LYS ALA LYS GLU ALA GLY LYS VAL VAL
SEQRES 4 A 130 ILE ILE ASP PHE THR ALA SER TRP CYS GLY PRO CYS ARG
SEQRES 5 A 130 PHE ILE ALA PRO VAL PHE ALA GLU TYR ALA LYS LYS PHE
SEQRES 6 A 130 PRO GLY ALA VAL PHE LEU LYS VAL ASP VAL ASP GLU LEU
SEQRES 7 A 130 LYS GLU VAL ALA GLU LYS TYR ASN VAL GLU ALA MET PRO
SEQRES 8 A 130 THR PHE LEU PHE ILE LYS ASP GLY ALA GLU ALA ASP LYS
SEQRES 9 A 130 VAL VAL GLY ALA ARG LYS ASP ASP LEU GLN ASN THR ILE
SEQRES 10 A 130 VAL LYS HIS VAL GLY ALA THR ALA ALA SER ALA SER ALA
HELIX 1 1 LYS A 14 GLU A 26 1 13
HELIX 2 2 ILE A 46 PHE A 57 1 12
HELIX 3 3 LEU A 70 GLU A 72 5 3
HELIX 4 4 VAL A 73 ASN A 78 1 6
HELIX 5 5 ASP A 104 VAL A 113 1 10
SHEET 1 A 2 ILE A 33 ASP A 34 0
SHEET 2 A 2 LEU A 63 LYS A 64 1 O LEU A 63 N ASP A 34
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