Header list of 2coa.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 17-MAY-05 2COA
TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF PROTEIN KINASE C, D2 TYPE FROM
TITLE 2 HUMAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C, D2 TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: NPKC-D2, PROTEIN KINASE D2, HSPC187;
COMPND 6 EC: 2.7.1.-;
COMPND 7 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: PKD2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041129-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PROTEIN KINASE D2, PH DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2COA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2COA 1 VERSN
REVDAT 1 17-NOV-05 2COA 0
JRNL AUTH H.LI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF PROTEIN KINASE C, D2
JRNL TITL 2 TYPE FROM HUMAN
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), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2COA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024442.
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 : 1.38MM PH DOMAIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.913, 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 LEAST RESTRAINT 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 LYS A 20 -48.29 -132.23
REMARK 500 1 ARG A 24 120.51 -31.04
REMARK 500 1 TYR A 28 96.70 -65.38
REMARK 500 1 GLN A 40 -39.28 -32.06
REMARK 500 1 THR A 44 148.70 -32.42
REMARK 500 1 GLN A 63 -30.87 -134.87
REMARK 500 1 PRO A 70 3.21 -69.80
REMARK 500 1 ASN A 73 119.05 -34.30
REMARK 500 1 PRO A 74 -166.66 -69.74
REMARK 500 1 ILE A 79 79.01 -106.47
REMARK 500 1 VAL A 80 107.27 -51.51
REMARK 500 1 ASN A 83 -38.40 -134.96
REMARK 500 1 ALA A 104 -62.51 -135.01
REMARK 500 1 PRO A 122 5.19 -69.81
REMARK 500 2 TYR A 17 146.25 -170.43
REMARK 500 2 ARG A 24 93.28 -60.69
REMARK 500 2 TYR A 28 97.49 -60.41
REMARK 500 2 TYR A 47 178.55 -55.07
REMARK 500 2 GLN A 63 -30.16 -134.95
REMARK 500 2 ASN A 73 126.85 -36.67
REMARK 500 2 PRO A 74 -169.20 -69.73
REMARK 500 2 ILE A 79 77.59 -102.84
REMARK 500 2 VAL A 80 109.53 -51.37
REMARK 500 2 ASN A 83 -39.75 -135.00
REMARK 500 2 PRO A 96 6.26 -69.71
REMARK 500 2 GLN A 102 -55.48 -125.92
REMARK 500 2 ALA A 104 -175.02 -176.44
REMARK 500 2 GLU A 105 -24.77 -37.71
REMARK 500 2 PRO A 122 -174.58 -69.68
REMARK 500 3 SER A 5 153.88 -44.86
REMARK 500 3 TYR A 17 144.03 -170.35
REMARK 500 3 ASN A 19 30.31 -95.03
REMARK 500 3 ARG A 24 94.36 -51.11
REMARK 500 3 TYR A 28 90.31 -60.28
REMARK 500 3 LYS A 34 -50.90 -122.90
REMARK 500 3 ARG A 46 146.17 -35.83
REMARK 500 3 TYR A 47 152.78 -45.28
REMARK 500 3 ALA A 62 113.80 -37.03
REMARK 500 3 GLN A 63 -30.04 -134.53
REMARK 500 3 PRO A 70 3.30 -69.80
REMARK 500 3 ASN A 73 129.83 -38.89
REMARK 500 3 PRO A 74 -172.98 -69.74
REMARK 500 3 ILE A 79 79.81 -103.88
REMARK 500 3 VAL A 80 102.93 -52.95
REMARK 500 3 ASN A 83 -38.57 -131.15
REMARK 500 3 GLU A 90 176.89 -49.05
REMARK 500 3 PRO A 99 1.60 -69.80
REMARK 500 3 GLN A 102 178.17 -49.01
REMARK 500 3 ALA A 104 -61.71 -130.40
REMARK 500 4 TYR A 17 145.64 -172.47
REMARK 500
REMARK 500 THIS ENTRY HAS 330 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002014776.1 RELATED DB: TARGETDB
DBREF 2COA A 8 119 UNP Q9BZL6 KPCD2_HUMAN 398 509
SEQADV 2COA GLY A 1 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 2 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 3 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA GLY A 4 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 5 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 6 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA GLY A 7 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 120 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA GLY A 121 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA PRO A 122 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 123 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA SER A 124 UNP Q9BZL6 CLONING ARTIFACT
SEQADV 2COA GLY A 125 UNP Q9BZL6 CLONING ARTIFACT
SEQRES 1 A 125 GLY SER SER GLY SER SER GLY THR LEU ARG GLU GLY TRP
SEQRES 2 A 125 VAL VAL HIS TYR SER ASN LYS ASP THR LEU ARG LYS ARG
SEQRES 3 A 125 HIS TYR TRP ARG LEU ASP CYS LYS CYS ILE THR LEU PHE
SEQRES 4 A 125 GLN ASN ASN THR THR ASN ARG TYR TYR LYS GLU ILE PRO
SEQRES 5 A 125 LEU SER GLU ILE LEU THR VAL GLU SER ALA GLN ASN PHE
SEQRES 6 A 125 SER LEU VAL PRO PRO GLY THR ASN PRO HIS CYS PHE GLU
SEQRES 7 A 125 ILE VAL THR ALA ASN ALA THR TYR PHE VAL GLY GLU MET
SEQRES 8 A 125 PRO GLY GLY THR PRO GLY GLY PRO SER GLY GLN GLY ALA
SEQRES 9 A 125 GLU ALA ALA ARG GLY TRP GLU THR ALA ILE ARG GLN ALA
SEQRES 10 A 125 LEU MET SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 105 SER A 120 1 16
SHEET 1 A 4 ARG A 10 HIS A 16 0
SHEET 2 A 4 LYS A 25 LEU A 31 -1
SHEET 3 A 4 CYS A 35 PHE A 39 -1
SHEET 4 A 4 LYS A 49 PRO A 52 -1
SHEET 1 B 3 THR A 58 SER A 61 0
SHEET 2 B 3 HIS A 75 VAL A 80 -1
SHEET 3 B 3 VAL A 88 GLY A 89 -1
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