Header list of 2ctf.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSPORT PROTEIN 24-MAY-05 2CTF
TITLE SOLUTION STRUCTURE OF THE 4TH KH TYPE I DOMAIN FROM HUMAN VIGILIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIGILIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KH DOMAIN;
COMPND 5 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: HDLBP;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050131-13;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS K HOMOLOGY TYPE I DOMAIN, RNA-BINDING, CELL STEROL METABOLISM, BETA-
KEYWDS 2 ALPHA-ALPHA-BETA-BETA-ALPHA STRUCTURE, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSPORT
KEYWDS 5 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 10-NOV-21 2CTF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CTF 1 VERSN
REVDAT 1 24-NOV-05 2CTF 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 4TH KH TYPE I DOMAIN FROM HUMAN
JRNL TITL 2 VIGILIN
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 2CTF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024602.
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 : 1.16MM KH DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 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 GLU A 8 54.36 34.63
REMARK 500 1 PRO A 9 -175.20 -69.78
REMARK 500 1 ALA A 23 120.86 -173.14
REMARK 500 1 ASN A 24 89.47 -69.47
REMARK 500 1 ALA A 32 106.76 -58.63
REMARK 500 2 SER A 2 -62.44 -98.97
REMARK 500 2 PRO A 9 -169.16 -69.77
REMARK 500 2 GLU A 18 116.01 -173.34
REMARK 500 2 ALA A 23 135.00 -39.46
REMARK 500 2 ALA A 32 105.42 -59.63
REMARK 500 3 VAL A 19 171.85 -47.50
REMARK 500 3 LYS A 45 35.93 35.34
REMARK 500 3 GLU A 65 -68.56 -95.87
REMARK 500 3 ARG A 96 39.40 -82.62
REMARK 500 4 LEU A 12 132.66 -174.56
REMARK 500 4 LEU A 16 77.59 -116.50
REMARK 500 4 LYS A 22 37.11 -97.97
REMARK 500 4 ALA A 32 102.83 -50.15
REMARK 500 4 MET A 56 78.22 -115.38
REMARK 500 5 LEU A 16 98.00 -64.23
REMARK 500 5 GLU A 18 136.27 -172.12
REMARK 500 5 PHE A 26 136.57 -36.27
REMARK 500 5 ALA A 32 102.75 -50.71
REMARK 500 5 THR A 76 -27.46 -39.98
REMARK 500 6 LYS A 11 38.75 -91.76
REMARK 500 6 ALA A 21 41.83 -108.90
REMARK 500 6 ALA A 23 49.04 -87.35
REMARK 500 6 ALA A 32 104.04 -56.06
REMARK 500 6 PRO A 34 -179.90 -69.85
REMARK 500 6 GLU A 65 -74.99 -66.40
REMARK 500 6 GLU A 67 -27.01 -39.66
REMARK 500 7 PRO A 9 -172.28 -69.78
REMARK 500 8 SER A 5 116.91 -173.63
REMARK 500 8 LYS A 11 44.17 -95.22
REMARK 500 8 LEU A 12 51.26 37.31
REMARK 500 8 GLN A 14 120.24 -170.50
REMARK 500 8 ALA A 15 110.33 -160.49
REMARK 500 8 GLU A 18 110.31 -174.45
REMARK 500 8 PRO A 34 -172.41 -69.69
REMARK 500 8 MET A 56 75.92 -118.83
REMARK 500 8 SER A 97 41.39 -91.38
REMARK 500 9 LYS A 11 143.57 -174.94
REMARK 500 9 LEU A 16 101.06 -35.23
REMARK 500 9 GLU A 18 -176.18 -65.27
REMARK 500 9 ALA A 21 76.81 -62.44
REMARK 500 9 PRO A 34 -176.37 -69.65
REMARK 500 9 LYS A 44 97.59 -61.75
REMARK 500 9 ARG A 96 48.12 -96.30
REMARK 500 9 SER A 100 100.32 -36.61
REMARK 500 10 PRO A 9 -170.32 -69.71
REMARK 500
REMARK 500 THIS ENTRY HAS 110 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002000906.6 RELATED DB: TARGETDB
DBREF 2CTF A 8 96 UNP Q00341 VIGLN_HUMAN 346 434
SEQADV 2CTF GLY A 1 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 2 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 3 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF GLY A 4 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 5 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 6 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF GLY A 7 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 80 UNP Q00341 ASN 418 ENGINEERED MUTATION
SEQADV 2CTF SER A 97 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF GLY A 98 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF PRO A 99 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 100 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF SER A 101 UNP Q00341 CLONING ARTIFACT
SEQADV 2CTF GLY A 102 UNP Q00341 CLONING ARTIFACT
SEQRES 1 A 102 GLY SER SER GLY SER SER GLY GLU PRO GLU LYS LEU GLY
SEQRES 2 A 102 GLN ALA LEU THR GLU VAL TYR ALA LYS ALA ASN SER PHE
SEQRES 3 A 102 THR VAL SER SER VAL ALA ALA PRO SER TRP LEU HIS ARG
SEQRES 4 A 102 PHE ILE ILE GLY LYS LYS GLY GLN ASN LEU ALA LYS ILE
SEQRES 5 A 102 THR GLN GLN MET PRO LYS VAL HIS ILE GLU PHE THR GLU
SEQRES 6 A 102 GLY GLU ASP LYS ILE THR LEU GLU GLY PRO THR GLU ASP
SEQRES 7 A 102 VAL SER VAL ALA GLN GLU GLN ILE GLU GLY MET VAL LYS
SEQRES 8 A 102 ASP LEU ILE ASN ARG SER GLY PRO SER SER GLY
HELIX 1 1 HIS A 38 GLY A 43 1 6
HELIX 2 2 GLN A 47 MET A 56 1 10
HELIX 3 3 PRO A 75 SER A 97 1 23
SHEET 1 A 3 THR A 27 ALA A 32 0
SHEET 2 A 3 LYS A 69 GLY A 74 -1 O LEU A 72 N SER A 29
SHEET 3 A 3 HIS A 60 PHE A 63 -1 N HIS A 60 O GLU A 73
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