Header list of 1wym.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYM
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN TRANSGELIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSGELIN-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 SYNONYM: SM22-ALPHA HOMOLOG;
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: TAGLN2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040315-88;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CH DOMAIN, F-ACTIN BINDING, ALL HELIX, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, STRUCTURAL
KEYWDS 4 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 1WYM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WYM 1 VERSN
REVDAT 1 15-AUG-05 1WYM 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN TRANSGELIN-2
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 1WYM 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_1000024157.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.19MM CH 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_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 GLU A 11 43.47 -88.52
REMARK 500 1 ARG A 31 -72.14 -55.15
REMARK 500 1 ARG A 36 97.08 -33.96
REMARK 500 1 PRO A 37 -168.75 -69.84
REMARK 500 1 LEU A 61 -73.76 -65.57
REMARK 500 1 PHE A 136 149.34 -37.71
REMARK 500 1 LYS A 146 151.30 -49.22
REMARK 500 1 SER A 153 160.04 -47.82
REMARK 500 2 LYS A 9 136.11 -171.36
REMARK 500 2 TYR A 14 157.81 -45.83
REMARK 500 2 LYS A 32 -179.23 -66.90
REMARK 500 2 ASP A 33 74.10 -113.04
REMARK 500 2 ARG A 36 107.82 -52.12
REMARK 500 2 PRO A 37 -165.02 -69.69
REMARK 500 2 LEU A 57 -72.96 -67.81
REMARK 500 2 LEU A 61 -72.58 -62.78
REMARK 500 2 MET A 122 -39.39 -36.87
REMARK 500 2 SER A 147 77.52 -109.88
REMARK 500 3 SER A 3 129.35 -39.09
REMARK 500 3 GLN A 13 171.04 -58.36
REMARK 500 3 ARG A 36 101.66 -40.63
REMARK 500 3 PRO A 37 -164.61 -69.73
REMARK 500 3 PRO A 39 3.07 -69.75
REMARK 500 3 LEU A 61 -74.04 -63.87
REMARK 500 3 ALA A 67 128.84 -37.29
REMARK 500 3 PHE A 136 140.58 -39.80
REMARK 500 3 LYS A 148 163.67 -47.04
REMARK 500 4 SER A 5 41.26 -96.30
REMARK 500 4 GLN A 13 70.91 -105.18
REMARK 500 4 ARG A 36 96.58 -33.38
REMARK 500 4 PRO A 37 -166.15 -69.74
REMARK 500 4 PRO A 39 3.37 -69.81
REMARK 500 4 ARG A 41 -60.06 -99.98
REMARK 500 4 THR A 52 -38.64 -37.19
REMARK 500 4 LEU A 57 -71.30 -70.01
REMARK 500 4 LEU A 61 -72.79 -65.30
REMARK 500 4 GLU A 64 133.56 -39.92
REMARK 500 4 ALA A 67 126.78 -34.70
REMARK 500 4 MET A 77 125.35 -36.68
REMARK 500 5 SER A 2 49.91 39.40
REMARK 500 5 SER A 3 48.12 -87.55
REMARK 500 5 ASP A 33 63.65 -106.66
REMARK 500 5 VAL A 34 -30.41 -36.74
REMARK 500 5 ARG A 36 96.67 -33.52
REMARK 500 5 PRO A 37 -164.62 -69.66
REMARK 500 5 PRO A 39 3.61 -69.78
REMARK 500 5 GLN A 87 -38.18 -38.37
REMARK 500 5 ASP A 107 -33.94 -35.16
REMARK 500 5 MET A 114 35.26 34.62
REMARK 500 5 PHE A 136 148.90 -37.48
REMARK 500
REMARK 500 THIS ENTRY HAS 240 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000118.1 RELATED DB: TARGETDB
DBREF 1WYM A 8 149 UNP P37802 TAGL2_HUMAN 16 157
SEQADV 1WYM GLY A 1 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 2 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 3 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM GLY A 4 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 5 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 6 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM GLY A 7 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 150 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM GLY A 151 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM PRO A 152 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 153 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM SER A 154 UNP P37802 CLONING ARTIFACT
SEQADV 1WYM GLY A 155 UNP P37802 CLONING ARTIFACT
SEQRES 1 A 155 GLY SER SER GLY SER SER GLY GLN LYS ILE GLU LYS GLN
SEQRES 2 A 155 TYR ASP ALA ASP LEU GLU GLN ILE LEU ILE GLN TRP ILE
SEQRES 3 A 155 THR THR GLN CYS ARG LYS ASP VAL GLY ARG PRO GLN PRO
SEQRES 4 A 155 GLY ARG GLU ASN PHE GLN ASN TRP LEU LYS ASP GLY THR
SEQRES 5 A 155 VAL LEU CYS GLU LEU ILE ASN ALA LEU TYR PRO GLU GLY
SEQRES 6 A 155 GLN ALA PRO VAL LYS LYS ILE GLN ALA SER THR MET ALA
SEQRES 7 A 155 PHE LYS GLN MET GLU GLN ILE SER GLN PHE LEU GLN ALA
SEQRES 8 A 155 ALA GLU ARG TYR GLY ILE ASN THR THR ASP ILE PHE GLN
SEQRES 9 A 155 THR VAL ASP LEU TRP GLU GLY LYS ASN MET ALA CYS VAL
SEQRES 10 A 155 GLN ARG THR LEU MET ASN LEU GLY GLY LEU ALA VAL ALA
SEQRES 11 A 155 ARG ASP ASP GLY LEU PHE SER GLY ASP PRO ASN TRP PHE
SEQRES 12 A 155 PRO LYS LYS SER LYS GLU SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 15 CYS A 30 1 16
HELIX 2 2 GLY A 40 ASP A 50 1 11
HELIX 3 3 GLY A 51 TYR A 62 1 12
HELIX 4 4 MET A 77 GLY A 96 1 20
HELIX 5 5 GLN A 104 GLU A 110 1 7
HELIX 6 6 ASN A 113 VAL A 129 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