Header list of 1wyr.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYR
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN RHO GUANINE NUCLEOTIDE
TITLE 2 EXCHANGE FACTOR 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 SYNONYM: PAK-INTERACTING EXCHANGE FACTOR ALPHA, ALPHA-PIX, COOL-2;
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: ARHGEF6;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040910-16;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CH DOMAIN, ALL-ALPHA, NPPSFA, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WYR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WYR 1 VERSN
REVDAT 1 15-AUG-05 1WYR 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN RHO GUANINE
JRNL TITL 2 NUCLEOTIDE EXCHANGE FACTOR 6
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), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WYR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024162.
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 : 1.32MM CH DOMAIN U-15N,13C; 20MM
REMARK 210 D-TRIS-HCL(PH 7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 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 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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 SER A 2 49.69 36.38
REMARK 500 1 SER A 5 92.53 -65.27
REMARK 500 1 LYS A 40 -71.36 -35.29
REMARK 500 1 LEU A 48 -70.50 -54.39
REMARK 500 1 LYS A 59 124.71 -174.08
REMARK 500 1 THR A 106 -39.67 -37.85
REMARK 500 1 GLU A 115 125.40 -35.24
REMARK 500 1 SER A 120 133.92 -36.73
REMARK 500 2 LYS A 26 171.30 -50.29
REMARK 500 2 ILE A 28 90.56 -44.61
REMARK 500 2 LEU A 48 -70.81 -67.05
REMARK 500 2 LYS A 79 -30.55 -38.05
REMARK 500 3 LYS A 25 47.23 -83.90
REMARK 500 3 PRO A 64 98.43 -69.77
REMARK 500 3 SER A 101 -39.20 -37.88
REMARK 500 3 VAL A 103 -38.87 -39.14
REMARK 500 4 LYS A 26 169.06 -48.52
REMARK 500 4 PRO A 54 98.24 -69.77
REMARK 500 4 ALA A 68 -38.80 -38.70
REMARK 500 4 LYS A 79 -35.08 -35.16
REMARK 500 5 LYS A 26 168.80 -44.05
REMARK 500 5 LYS A 59 112.95 -167.38
REMARK 500 5 ALA A 68 -39.09 -36.13
REMARK 500 6 SER A 6 42.24 -105.16
REMARK 500 6 LYS A 26 177.85 -48.41
REMARK 500 6 ALA A 68 -35.77 -38.43
REMARK 500 6 LYS A 79 -37.39 -37.73
REMARK 500 6 SER A 101 -38.73 -35.26
REMARK 500 6 THR A 114 33.67 -87.49
REMARK 500 6 SER A 116 117.73 -39.75
REMARK 500 6 SER A 119 92.82 -67.75
REMARK 500 7 SER A 5 164.10 -44.73
REMARK 500 7 LEU A 48 -71.73 -73.01
REMARK 500 7 ILE A 49 -35.09 -36.98
REMARK 500 7 GLU A 87 156.16 -47.32
REMARK 500 7 SER A 101 -38.78 -37.82
REMARK 500 8 LEU A 48 -72.49 -71.26
REMARK 500 8 LYS A 59 129.03 -174.97
REMARK 500 8 SER A 101 -33.08 -38.66
REMARK 500 9 SER A 5 119.13 -170.00
REMARK 500 9 LYS A 26 174.64 -51.91
REMARK 500 9 ILE A 28 91.81 -43.94
REMARK 500 9 LYS A 40 -70.65 -34.28
REMARK 500 9 LEU A 48 -71.52 -65.62
REMARK 500 9 ALA A 68 -39.98 -39.57
REMARK 500 9 GLU A 115 144.87 -39.43
REMARK 500 10 PRO A 64 98.97 -69.85
REMARK 500 10 SER A 101 -38.99 -35.47
REMARK 500 10 SER A 116 47.92 -93.33
REMARK 500 11 LYS A 26 179.14 -48.91
REMARK 500
REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK001000001.2 RELATED DB: TARGETDB
DBREF 1WYR A 8 115 UNP Q15052 ARHG6_HUMAN 4 111
SEQADV 1WYR GLY A 1 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 2 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 3 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR GLY A 4 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 5 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 6 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR GLY A 7 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 116 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR GLY A 117 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR PRO A 118 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 119 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR SER A 120 UNP Q15052 CLONING ARTIFACT
SEQADV 1WYR GLY A 121 UNP Q15052 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER SER GLY SER SER GLY GLU GLU GLN ILE VAL THR
SEQRES 2 A 121 TRP LEU ILE SER LEU GLY VAL LEU GLU SER PRO LYS LYS
SEQRES 3 A 121 THR ILE CYS ASP PRO GLU GLU PHE LEU LYS SER SER LEU
SEQRES 4 A 121 LYS ASN GLY VAL VAL LEU CYS LYS LEU ILE ASN ARG LEU
SEQRES 5 A 121 MET PRO GLY SER VAL GLU LYS PHE CYS LEU ASP PRO GLN
SEQRES 6 A 121 THR GLU ALA ASP CYS ILE ASN ASN ILE ASN ASP PHE LEU
SEQRES 7 A 121 LYS GLY CYS ALA THR LEU GLN VAL GLU ILE PHE ASP PRO
SEQRES 8 A 121 ASP ASP LEU TYR SER GLY VAL ASN PHE SER LYS VAL LEU
SEQRES 9 A 121 SER THR LEU LEU ALA VAL ASN LYS ALA THR GLU SER GLY
SEQRES 10 A 121 PRO SER SER GLY
HELIX 1 1 GLY A 7 GLY A 19 1 13
HELIX 2 2 ASP A 30 GLY A 42 1 13
HELIX 3 3 GLY A 42 MET A 53 1 12
HELIX 4 4 THR A 66 GLN A 85 1 20
HELIX 5 5 ASP A 90 SER A 96 1 7
HELIX 6 6 ASN A 99 GLU A 115 1 17
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