Header list of 1wfw.pdb file
Complete list - v 10 2 Bytes
HEADER SIGNALING PROTEIN 27-MAY-04 1WFW
TITLE SOLUTION STRUCTURE OF SH3 DOMAIN OF MOUSE KALIRIN-9A PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KALIRIN-9A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: UNNAMED PROTEIN PRODUCT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 2210407G14;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030120-92;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, NEURON-SPECIFIC GDP/GTP EXCHANGE FACTOR, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 SIGNALING PROTEIN
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 10-NOV-21 1WFW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WFW 1 VERSN
REVDAT 1 27-NOV-04 1WFW 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF SH3 DOMAIN OF MOUSE KALIRIN-9A PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
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), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFW 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_1000023535.
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 : 1MM SH3 DOMAIN U-15N, 13C; 20MM
REMARK 210 D-TRIS HCL; 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 5.0.4,
REMARK 210 KUJIRA 0.8994, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 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 GLN A 28 108.79 -59.26
REMARK 500 1 LEU A 44 95.87 -57.96
REMARK 500 1 ALA A 49 129.93 -38.73
REMARK 500 1 PRO A 67 99.74 -69.73
REMARK 500 1 SER A 72 52.69 35.35
REMARK 500 2 SER A 2 165.11 -44.06
REMARK 500 2 GLU A 30 159.09 -49.68
REMARK 500 2 ALA A 36 -177.68 -174.52
REMARK 500 2 LEU A 44 99.06 -66.89
REMARK 500 2 PHE A 68 84.77 -68.55
REMARK 500 3 SER A 3 42.28 -98.57
REMARK 500 3 GLN A 28 107.74 -52.80
REMARK 500 3 GLU A 30 171.96 -48.14
REMARK 500 3 ALA A 36 -176.99 -173.21
REMARK 500 4 SER A 5 97.37 -56.49
REMARK 500 4 GLN A 28 106.55 -56.83
REMARK 500 4 ASN A 41 35.94 73.54
REMARK 500 4 LEU A 44 98.74 -62.38
REMARK 500 4 ALA A 55 106.75 -47.92
REMARK 500 4 PRO A 67 94.36 -69.72
REMARK 500 4 PRO A 71 2.77 -69.74
REMARK 500 4 SER A 73 -58.59 -128.25
REMARK 500 5 GLU A 30 155.68 -48.56
REMARK 500 5 ALA A 36 -178.19 -175.09
REMARK 500 5 ALA A 49 125.76 -33.92
REMARK 500 5 PRO A 54 -178.16 -69.86
REMARK 500 5 PRO A 67 93.68 -69.68
REMARK 500 5 PRO A 71 85.49 -69.76
REMARK 500 5 SER A 72 108.60 -171.37
REMARK 500 6 LEU A 44 98.60 -61.63
REMARK 500 6 PRO A 54 -173.85 -69.80
REMARK 500 6 SER A 69 39.99 37.08
REMARK 500 6 PRO A 71 95.77 -69.81
REMARK 500 7 ALA A 18 96.16 -58.78
REMARK 500 7 GLU A 30 151.23 -43.62
REMARK 500 7 ALA A 49 134.17 -39.61
REMARK 500 7 PRO A 54 -176.26 -69.78
REMARK 500 7 ILE A 64 30.94 -93.17
REMARK 500 7 PRO A 67 93.27 -69.73
REMARK 500 8 GLU A 30 175.88 -50.53
REMARK 500 8 LEU A 44 104.88 -47.96
REMARK 500 8 ALA A 49 116.59 -36.98
REMARK 500 8 PRO A 67 97.10 -69.82
REMARK 500 9 SER A 2 127.66 -170.62
REMARK 500 9 ASP A 15 156.30 -48.82
REMARK 500 9 PRO A 54 -179.34 -69.77
REMARK 500 9 PRO A 67 95.56 -69.77
REMARK 500 10 SER A 3 102.68 -43.70
REMARK 500 10 SER A 6 41.97 -108.24
REMARK 500 10 LEU A 44 98.16 -62.85
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007008182.1 RELATED DB: TARGETDB
DBREF 1WFW A 8 68 GB 12843281 BAB25925 188 248
SEQADV 1WFW GLY A 1 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 2 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 3 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW GLY A 4 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 5 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 6 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW GLY A 7 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW GLY A 29 GB 12843281 SER 209 ENGINEERED MUTATION
SEQADV 1WFW GLU A 57 GB 12843281 LYS 237 ENGINEERED MUTATION
SEQADV 1WFW SER A 69 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW GLY A 70 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW PRO A 71 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 72 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW SER A 73 GB 12843281 CLONING ARTIFACT
SEQADV 1WFW GLY A 74 GB 12843281 CLONING ARTIFACT
SEQRES 1 A 74 GLY SER SER GLY SER SER GLY SER THR MET THR VAL ILE
SEQRES 2 A 74 LYS ASP TYR TYR ALA LEU LYS GLU ASN GLU ILE CYS VAL
SEQRES 3 A 74 SER GLN GLY GLU VAL VAL GLN VAL LEU ALA VAL ASN GLN
SEQRES 4 A 74 GLN ASN MET CYS LEU VAL TYR GLN PRO ALA SER ASP HIS
SEQRES 5 A 74 SER PRO ALA ALA GLU GLY TRP VAL PRO GLY SER ILE LEU
SEQRES 6 A 74 ALA PRO PHE SER GLY PRO SER SER GLY
HELIX 1 1 SER A 63 LEU A 65 5 3
SHEET 1 A 4 THR A 9 THR A 11 0
SHEET 2 A 4 VAL A 31 VAL A 37 -1 O VAL A 32 N MET A 10
SHEET 3 A 4 MET A 42 GLN A 47 -1 O TYR A 46 N GLN A 33
SHEET 4 A 4 ALA A 56 PRO A 61 -1 O ALA A 56 N GLN A 47
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 - v 10 2 Bytes