Header list of 1wfs.pdb file
Complete list - c 21 2 Bytes
HEADER PROTEIN BINDING 26-MAY-04 1WFS
TITLE SOLUTION STRUCTURE OF GLIA MATURATION FACTOR-GAMMA FROM MUS MUSCULUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLIA MATURATION FACTOR GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COFILIN-ADF-DOMAIN;
COMPND 5 SYNONYM: GMF-GAMMA, MGMF-GAMMA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 2310057N07;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030324-83;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ACTIN BINDING PROTEIN, CYTOSKELETON, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
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 5 21-DEC-22 1WFS 1 SEQADV
REVDAT 4 02-MAR-22 1WFS 1 REMARK SEQADV
REVDAT 3 02-FEB-10 1WFS 1 JRNL
REVDAT 2 24-FEB-09 1WFS 1 VERSN
REVDAT 1 26-NOV-04 1WFS 0
JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.SATO,M.INOUE,
JRNL AUTH 2 S.WATANABE,Y.HAYASHIZAKI,A.TANAKA,T.KIGAWA,S.YOKOYAMA
JRNL TITL NMR SOLUTION STRUCTURES OF ACTIN DEPOLYMERIZING FACTOR
JRNL TITL 2 HOMOLOGY DOMAINS.
JRNL REF PROTEIN SCI. V. 18 2384 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19768801
JRNL DOI 10.1002/PRO.248
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.26
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023531.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.21MM COFILIN U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL;
REMARK 210 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW
REMARK 210 5.0.14, KUJIRA 0.899
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 10 138.91 -174.32
REMARK 500 1 VAL A 12 44.82 -96.83
REMARK 500 1 VAL A 13 139.37 -38.73
REMARK 500 1 ASP A 17 140.29 -35.44
REMARK 500 1 LYS A 31 33.67 -91.69
REMARK 500 1 THR A 33 26.26 -148.19
REMARK 500 1 GLN A 47 48.55 33.98
REMARK 500 1 PRO A 68 -165.41 -69.78
REMARK 500 1 ARG A 70 43.60 -155.23
REMARK 500 1 HIS A 83 -79.94 -104.24
REMARK 500 1 ASP A 84 -52.83 166.38
REMARK 500 1 PRO A 91 96.89 -69.80
REMARK 500 1 THR A 131 148.61 179.68
REMARK 500 1 LEU A 135 84.68 -61.36
REMARK 500 1 GLU A 137 -39.65 -39.48
REMARK 500 1 ALA A 145 -72.52 -37.95
REMARK 500 1 SER A 146 76.08 -172.43
REMARK 500 1 PRO A 148 -168.69 -69.77
REMARK 500 1 SER A 150 166.89 57.70
REMARK 500 2 SER A 2 -50.30 -121.10
REMARK 500 2 SER A 3 -56.96 -174.91
REMARK 500 2 SER A 5 -64.05 -134.10
REMARK 500 2 SER A 6 -55.90 79.21
REMARK 500 2 ASP A 9 86.83 -155.56
REMARK 500 2 VAL A 12 44.65 -105.27
REMARK 500 2 VAL A 13 153.13 -37.88
REMARK 500 2 ASP A 17 139.92 -33.26
REMARK 500 2 THR A 33 26.54 -151.57
REMARK 500 2 GLN A 47 43.57 37.67
REMARK 500 2 PRO A 68 -169.10 -69.72
REMARK 500 2 ARG A 70 50.39 -149.18
REMARK 500 2 HIS A 83 -86.62 -103.24
REMARK 500 2 ASP A 84 -39.93 172.19
REMARK 500 2 PRO A 91 95.83 -69.73
REMARK 500 2 PRO A 99 -163.45 -69.77
REMARK 500 2 GLU A 122 41.95 74.66
REMARK 500 2 THR A 131 144.62 179.74
REMARK 500 2 LEU A 135 82.63 -60.26
REMARK 500 2 ALA A 145 178.33 -52.13
REMARK 500 2 SER A 146 43.36 -100.42
REMARK 500 2 PRO A 148 -174.85 -69.72
REMARK 500 3 SER A 3 123.07 66.41
REMARK 500 3 SER A 5 121.00 -35.83
REMARK 500 3 SER A 6 -52.72 -147.82
REMARK 500 3 SER A 8 83.93 63.70
REMARK 500 3 ASP A 9 76.05 -173.09
REMARK 500 3 SER A 10 174.16 51.90
REMARK 500 3 VAL A 12 44.52 -103.50
REMARK 500 3 ASP A 17 140.47 -33.16
REMARK 500 3 LYS A 31 30.30 -85.84
REMARK 500
REMARK 500 THIS ENTRY HAS 419 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK001005899.1 RELATED DB: TARGETDB
DBREF 1WFS A 8 145 UNP Q9ERL7 GMFG_MOUSE 2 139
SEQADV 1WFS GLY A 1 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 2 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 3 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS GLY A 4 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 5 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 6 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS GLY A 7 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 146 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS GLY A 147 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS PRO A 148 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 149 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS SER A 150 UNP Q9ERL7 CLONING ARTIFACT
SEQADV 1WFS GLY A 151 UNP Q9ERL7 CLONING ARTIFACT
SEQRES 1 A 151 GLY SER SER GLY SER SER GLY SER ASP SER LEU VAL VAL
SEQRES 2 A 151 CYS GLU VAL ASP PRO GLU LEU LYS GLU THR LEU ARG LYS
SEQRES 3 A 151 PHE ARG PHE ARG LYS GLU THR ASN ASN ALA ALA ILE ILE
SEQRES 4 A 151 MET LYS VAL ASP LYS ASP ARG GLN MET VAL VAL LEU GLU
SEQRES 5 A 151 ASP GLU LEU GLN ASN ILE SER PRO GLU GLU LEU LYS LEU
SEQRES 6 A 151 GLU LEU PRO GLU ARG GLN PRO ARG PHE VAL VAL TYR SER
SEQRES 7 A 151 TYR LYS TYR VAL HIS ASP ASP GLY ARG VAL SER TYR PRO
SEQRES 8 A 151 LEU CYS PHE ILE PHE SER SER PRO VAL GLY CYS LYS PRO
SEQRES 9 A 151 GLU GLN GLN MET MET TYR ALA GLY SER LYS ASN ARG LEU
SEQRES 10 A 151 VAL GLN THR ALA GLU LEU THR LYS VAL PHE GLU ILE ARG
SEQRES 11 A 151 THR THR ASP ASP LEU THR GLU THR TRP LEU LYS GLU LYS
SEQRES 12 A 151 LEU ALA SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 17 ARG A 28 1 12
HELIX 2 2 GLU A 61 LEU A 67 1 7
HELIX 3 3 LYS A 103 GLU A 122 1 20
HELIX 4 4 THR A 131 LEU A 135 5 5
HELIX 5 5 THR A 136 GLY A 147 1 12
SHEET 1 A 6 GLU A 15 VAL A 16 0
SHEET 2 A 6 MET A 48 GLN A 56 1 O VAL A 49 N GLU A 15
SHEET 3 A 6 ALA A 36 ASP A 43 -1 N ALA A 37 O LEU A 55
SHEET 4 A 6 ARG A 73 SER A 78 -1 O PHE A 74 N MET A 40
SHEET 5 A 6 LEU A 92 SER A 97 -1 O ILE A 95 N VAL A 75
SHEET 6 A 6 VAL A 126 ILE A 129 1 O PHE A 127 N PHE A 94
SHEET 1 B 2 TYR A 81 VAL A 82 0
SHEET 2 B 2 VAL A 88 SER A 89 -1 O SER A 89 N TYR A 81
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 - c 21 2 Bytes