Header list of 2cso.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 22-MAY-05 2CSO
TITLE SOLUTION STRUCTURE OF THE DEP DOMAIN OF HUMAN PLECKSTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLECKSTRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEP DOMAIN;
COMPND 5 SYNONYM: PLATELET P47 PROTEIN;
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: PLEK, P47;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DEP DOMAIN, PLECKSTRIN, PLATELET P47 PROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CSO 1 VERSN
REVDAT 1 22-NOV-05 2CSO 0
JRNL AUTH K.INOUE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE DEP DOMAIN OF HUMAN PLECKSTRIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024578.
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 : 1.35MM U-15N, 13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 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; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, 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 : 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: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY,
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C_SEPARATED_NOESY
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 MET A 88 -74.86 -62.94
REMARK 500 1 ASP A 103 47.43 33.72
REMARK 500 2 ASP A 40 49.11 35.79
REMARK 500 2 LYS A 90 -31.29 -37.63
REMARK 500 2 THR A 96 49.07 -92.18
REMARK 500 2 ASP A 103 44.54 33.20
REMARK 500 2 ASN A 121 100.38 -42.37
REMARK 500 2 SER A 122 109.33 -160.49
REMARK 500 2 PRO A 124 1.82 -69.77
REMARK 500 3 SER A 3 41.75 35.17
REMARK 500 3 LYS A 39 -74.90 -128.70
REMARK 500 3 LYS A 41 26.63 38.93
REMARK 500 3 ASP A 103 50.91 34.00
REMARK 500 3 GLU A 120 78.41 -60.48
REMARK 500 3 PRO A 124 98.72 -69.79
REMARK 500 3 SER A 126 106.06 -34.95
REMARK 500 4 SER A 5 42.94 -105.01
REMARK 500 4 MET A 88 -71.88 -47.29
REMARK 500 4 ASP A 94 48.27 -108.84
REMARK 500 4 GLU A 98 -35.80 -34.74
REMARK 500 4 ASP A 103 47.25 33.60
REMARK 500 4 SER A 122 -63.52 -94.07
REMARK 500 5 MET A 88 -73.22 -61.34
REMARK 500 5 ASP A 103 50.20 35.46
REMARK 500 5 PHE A 116 148.76 -37.08
REMARK 500 5 PRO A 124 98.83 -69.79
REMARK 500 6 ASP A 40 47.63 35.58
REMARK 500 6 LYS A 90 -27.83 -38.25
REMARK 500 6 ASP A 103 46.88 33.52
REMARK 500 6 ASN A 121 124.66 -36.96
REMARK 500 6 PRO A 124 89.31 -69.73
REMARK 500 6 SER A 126 113.87 -161.86
REMARK 500 7 SER A 5 88.90 -69.36
REMARK 500 7 LEU A 12 157.78 -47.30
REMARK 500 7 LYS A 39 -75.05 -82.43
REMARK 500 7 LYS A 41 26.67 39.83
REMARK 500 7 HIS A 46 26.31 49.55
REMARK 500 7 THR A 49 168.21 -47.88
REMARK 500 7 MET A 88 -72.65 -39.43
REMARK 500 7 GLU A 98 -39.11 -35.01
REMARK 500 7 ASP A 103 48.55 34.43
REMARK 500 7 GLU A 120 94.80 -38.72
REMARK 500 7 ASN A 121 163.83 -41.80
REMARK 500 8 SER A 2 143.40 -173.89
REMARK 500 8 ARG A 8 132.85 -173.77
REMARK 500 8 SER A 9 153.66 -47.96
REMARK 500 8 THR A 96 40.13 -86.64
REMARK 500 8 ASP A 103 43.78 -76.33
REMARK 500 9 SER A 6 56.82 -101.75
REMARK 500 9 PRO A 13 97.70 -69.78
REMARK 500
REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003763.2 RELATED DB: TARGETDB
DBREF 2CSO A 8 121 UNP P08567 PLEK_HUMAN 116 229
SEQADV 2CSO GLY A 1 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 2 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 3 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO GLY A 4 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 5 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 6 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO GLY A 7 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 122 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO GLY A 123 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO PRO A 124 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 125 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO SER A 126 UNP P08567 CLONING ARTIFACT
SEQADV 2CSO GLY A 127 UNP P08567 CLONING ARTIFACT
SEQRES 1 A 127 GLY SER SER GLY SER SER GLY ARG SER ILE ARG LEU PRO
SEQRES 2 A 127 GLU THR ILE ASP LEU GLY ALA LEU TYR LEU SER MET LYS
SEQRES 3 A 127 ASP THR GLU LYS GLY ILE LYS GLU LEU ASN LEU GLU LYS
SEQRES 4 A 127 ASP LYS LYS ILE PHE ASN HIS CYS PHE THR GLY ASN CYS
SEQRES 5 A 127 VAL ILE ASP TRP LEU VAL SER ASN GLN SER VAL ARG ASN
SEQRES 6 A 127 ARG GLN GLU GLY LEU MET ILE ALA SER SER LEU LEU ASN
SEQRES 7 A 127 GLU GLY TYR LEU GLN PRO ALA GLY ASP MET SER LYS SER
SEQRES 8 A 127 ALA VAL ASP GLY THR ALA GLU ASN PRO PHE LEU ASP ASN
SEQRES 9 A 127 PRO ASP ALA PHE TYR TYR PHE PRO ASP SER GLY PHE PHE
SEQRES 10 A 127 CYS GLU GLU ASN SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 17 ASP A 27 1 11
HELIX 2 2 GLY A 50 ASN A 60 1 11
HELIX 3 3 ASN A 65 GLY A 80 1 16
HELIX 4 4 GLY A 86 GLY A 95 1 10
SHEET 1 A 4 LEU A 35 LYS A 39 0
SHEET 2 A 4 LYS A 42 THR A 49 -1 O LYS A 42 N LYS A 39
SHEET 3 A 4 PHE A 108 TYR A 110 -1 O TYR A 109 N PHE A 48
SHEET 4 A 4 GLN A 83 ALA A 85 -1 N GLN A 83 O TYR A 110
SHEET 1 B 3 LEU A 35 LYS A 39 0
SHEET 2 B 3 LYS A 42 THR A 49 -1 O LYS A 42 N LYS A 39
SHEET 3 B 3 CYS A 118 GLU A 120 -1 O GLU A 119 N ILE A 43
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 9 2 Bytes