Header list of 1v6f.pdb file
Complete list - r 2 2 Bytes
HEADER HORMONE/GROWTH FACTOR 29-NOV-03 1V6F
TITLE SOLUTION STRUCTURE OF GLIA MATURATION FACTOR-BETA FROM MUS MUSCULUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLIA MATURATION FACTOR, BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COFILIN-ADF DOMIAN;
COMPND 5 SYNONYM: MGMF-BETA;
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 3110001H22;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030324-81;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ACTIN BINDING PROTEIN, CYTOSKELETON, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, HORMONE-
KEYWDS 3 GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,T.TOMIZAWA,N.KOBAYASHI,N.TOCHIO,
AUTHOR 2 M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 4 02-MAR-22 1V6F 1 REMARK SEQADV
REVDAT 3 02-FEB-10 1V6F 1 JRNL
REVDAT 2 24-FEB-09 1V6F 1 VERSN
REVDAT 1 29-MAY-04 1V6F 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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), PETER GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006264.
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 : 1.16MM COFILIN, 20MM PHOSPHATE
REMARK 210 BUFFER NA, 100MM NACL, 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 : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW
REMARK 210 5.0.14, KUJIRA 0.861
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 PHE A 29 32.28 -93.79
REMARK 500 1 ARG A 47 37.24 32.14
REMARK 500 1 ARG A 70 -36.42 -131.06
REMARK 500 1 LEU A 135 95.66 -58.43
REMARK 500 2 GLU A 9 81.94 -67.44
REMARK 500 2 HIS A 34 -177.26 -66.36
REMARK 500 2 ASP A 45 -70.60 -82.80
REMARK 500 2 ASP A 85 -37.74 -37.12
REMARK 500 2 LEU A 135 84.50 -56.34
REMARK 500 2 SER A 146 108.16 -161.83
REMARK 500 3 PHE A 29 35.02 -94.94
REMARK 500 3 HIS A 34 179.34 -55.88
REMARK 500 3 ARG A 47 37.46 32.21
REMARK 500 3 GLU A 53 149.28 -176.07
REMARK 500 3 LEU A 135 94.57 -59.67
REMARK 500 4 PHE A 29 35.60 -98.47
REMARK 500 4 ARG A 47 41.70 32.24
REMARK 500 4 VAL A 118 -19.76 -49.61
REMARK 500 4 LEU A 135 98.01 -55.23
REMARK 500 4 PRO A 148 4.38 -69.75
REMARK 500 5 SER A 5 172.38 -58.15
REMARK 500 5 GLU A 9 45.09 -82.81
REMARK 500 5 PHE A 29 33.64 -96.70
REMARK 500 5 LYS A 31 37.42 -92.92
REMARK 500 5 ASN A 131 137.56 -171.53
REMARK 500 5 LEU A 135 92.72 -60.95
REMARK 500 6 PHE A 29 35.82 -96.94
REMARK 500 6 LYS A 31 41.72 -88.20
REMARK 500 6 ASP A 43 -175.57 -59.37
REMARK 500 6 LEU A 135 94.96 -50.04
REMARK 500 7 LEU A 11 170.38 -58.16
REMARK 500 7 PHE A 29 34.70 -96.79
REMARK 500 7 LYS A 31 32.62 -89.32
REMARK 500 7 HIS A 34 178.30 -54.74
REMARK 500 7 ARG A 47 38.33 32.40
REMARK 500 7 LEU A 135 89.59 -56.73
REMARK 500 7 SER A 146 43.81 -80.43
REMARK 500 8 SER A 3 115.79 -160.98
REMARK 500 8 SER A 10 149.70 -174.76
REMARK 500 8 PHE A 29 35.39 -95.31
REMARK 500 8 LYS A 31 37.67 -89.20
REMARK 500 8 HIS A 34 178.37 -55.47
REMARK 500 8 LEU A 135 96.98 -53.02
REMARK 500 8 SER A 146 39.24 -90.79
REMARK 500 8 PRO A 148 96.24 -69.71
REMARK 500 8 SER A 149 -19.85 -49.76
REMARK 500 9 PHE A 29 36.57 -97.89
REMARK 500 9 LYS A 31 35.87 -84.42
REMARK 500 9 HIS A 34 -177.08 -58.24
REMARK 500 9 ARG A 47 43.51 31.76
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK001003312.1 RELATED DB: TARGETDB
DBREF 1V6F A 8 145 GB 12851526 BAB29076 2 139
SEQADV 1V6F GLY A 1 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 2 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 3 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F GLY A 4 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 5 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 6 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F GLY A 7 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 146 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F GLY A 147 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F PRO A 148 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 149 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F SER A 150 GB 12851526 CLONING ARTIFACT
SEQADV 1V6F GLY A 151 GB 12851526 CLONING ARTIFACT
SEQRES 1 A 151 GLY SER SER GLY SER SER GLY SER GLU SER LEU VAL VAL
SEQRES 2 A 151 CYS ASP VAL ALA GLU ASP LEU VAL GLU LYS LEU ARG LYS
SEQRES 3 A 151 PHE ARG PHE ARG LYS GLU THR HIS ASN ALA ALA ILE ILE
SEQRES 4 A 151 MET LYS ILE ASP LYS ASP GLU ARG LEU VAL VAL LEU ASP
SEQRES 5 A 151 GLU GLU LEU GLU GLY VAL SER PRO ASP GLU LEU LYS ASP
SEQRES 6 A 151 GLU LEU PRO GLU ARG GLN PRO ARG PHE ILE VAL TYR SER
SEQRES 7 A 151 TYR LYS TYR GLN 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 LYS LEU
SEQRES 10 A 151 VAL GLN THR ALA GLU LEU THR LYS VAL PHE GLU ILE ARG
SEQRES 11 A 151 ASN THR GLU ASP LEU THR GLU GLU TRP LEU ARG GLU LYS
SEQRES 12 A 151 LEU GLY SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 17 PHE A 29 1 13
HELIX 2 2 SER A 59 LYS A 64 1 6
HELIX 3 3 ASP A 65 LEU A 67 5 3
HELIX 4 4 LYS A 103 ALA A 121 1 19
HELIX 5 5 ASN A 131 LEU A 135 5 5
HELIX 6 6 THR A 136 SER A 146 1 11
SHEET 1 A 6 ASP A 15 VAL A 16 0
SHEET 2 A 6 LEU A 48 GLU A 56 1 O VAL A 49 N ASP A 15
SHEET 3 A 6 ALA A 36 ILE A 42 -1 N ALA A 37 O LEU A 55
SHEET 4 A 6 ARG A 73 SER A 78 -1 O VAL A 76 N ILE A 38
SHEET 5 A 6 LEU A 92 SER A 97 -1 O SER A 97 N ARG A 73
SHEET 6 A 6 LYS A 125 ILE A 129 1 O PHE A 127 N PHE A 96
SHEET 1 B 2 TYR A 81 GLN 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 - r 2 2 Bytes