Header list of 2vil.pdb file
Complete list - v 29 2 Bytes
HEADER ACTIN-BINDING PROTEIN 16-JAN-97 2VIL
TITLE REFINED STRUCTURE OF THE ACTIN-SEVERING DOMAIN VILLIN 14T, DETERMINED
TITLE 2 BY SOLUTION NMR, 11 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VILLIN 14T;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1 - 126;
COMPND 5 SYNONYM: VILLIN DOMAIN 1, VILLIN SEGMENT 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: INTESTINE;
SOURCE 7 CELL: EPITHELIAL CELLS;
SOURCE 8 GENE: T7;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PAED4, BASED ON T7 PROMOTER;
SOURCE 14 EXPRESSION_SYSTEM_GENE: T7
KEYWDS ACTIN-BINDING PROTEIN, CAPPING PROTEIN, CALCIUM-BINDING PROTEIN,
KEYWDS 2 CYTOSKELETAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR M.A.MARKUS,P.MATSUDAIRA,G.WAGNER
REVDAT 3 29-NOV-17 2VIL 1 REMARK HELIX
REVDAT 2 24-FEB-09 2VIL 1 VERSN
REVDAT 1 01-APR-97 2VIL 0
SPRSDE 01-APR-97 2VIL 1VIL
JRNL AUTH M.A.MARKUS,P.MATSUDAIRA,G.WAGNER
JRNL TITL REFINED STRUCTURE OF VILLIN 14T AND A DETAILED COMPARISON
JRNL TITL 2 WITH OTHER ACTIN-SEVERING DOMAINS.
JRNL REF PROTEIN SCI. V. 6 1197 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9194180
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.MARKUS,K.T.DAYIE,P.MATSUDAIRA,G.WAGNER
REMARK 1 TITL LOCAL MOBILITY WITHIN VILLIN 14T PROBED VIA HETERONUCLEAR
REMARK 1 TITL 2 RELAXATION MEASUREMENTS AND A REDUCED SPECTRAL DENSITY
REMARK 1 TITL 3 MAPPING
REMARK 1 REF BIOCHEMISTRY V. 35 1722 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.A.MARKUS,T.NAKAYAMA,P.MATSUDAIRA,G.WAGNER
REMARK 1 TITL SOLUTION STRUCTURE OF VILLIN 14T, A DOMAIN CONSERVED AMONG
REMARK 1 TITL 2 ACTIN-SEVERING PROTEINS
REMARK 1 REF PROTEIN SCI. V. 3 70 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.A.MARKUS,T.NAKAYAMA,P.MATSUDAIRA,G.WAGNER
REMARK 1 TITL 1H, 15N, 13C AND 13CO RESONANCE ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF VILLIN 14T, A DOMAIN CONSERVED AMONG
REMARK 1 TITL 3 ACTIN-SEVERING PROTEINS
REMARK 1 REF J.BIOMOL.NMR V. 4 553 1994
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2VIL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178734.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.15
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; HNCO; HCACO; 2D
REMARK 210 NOESY (H2O; D2O); 3D 15N
REMARK 210 SEPARATED NOESY; 3D 13C
REMARK 210 SEPARATED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII, IN INSIGHT II II
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : NOE VIOLATIONS < 0.5 A DIHEDRAL
REMARK 210 VIOL < 5 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 2 66.08 64.64
REMARK 500 1 SER A 4 150.56 -42.54
REMARK 500 1 LYS A 5 -72.27 80.49
REMARK 500 1 VAL A 7 -74.41 -157.20
REMARK 500 1 LYS A 10 47.46 164.12
REMARK 500 1 LEU A 11 -147.82 -68.96
REMARK 500 1 THR A 14 69.99 -160.80
REMARK 500 1 THR A 15 124.20 -175.33
REMARK 500 1 ILE A 23 43.89 -96.49
REMARK 500 1 ASN A 25 24.60 47.18
REMARK 500 1 GLU A 27 -111.22 -148.24
REMARK 500 1 MET A 28 153.91 178.88
REMARK 500 1 PRO A 32 -161.80 -78.78
REMARK 500 1 SER A 35 21.07 -159.99
REMARK 500 1 TYR A 36 32.64 -90.00
REMARK 500 1 TYR A 40 155.19 -39.42
REMARK 500 1 ASP A 43 -148.11 -162.92
REMARK 500 1 SER A 55 -54.69 -133.73
REMARK 500 1 LEU A 65 65.21 -119.28
REMARK 500 1 LYS A 67 88.02 -37.74
REMARK 500 1 ASN A 68 -43.65 -162.75
REMARK 500 1 SER A 103 -107.55 -48.63
REMARK 500 1 GLN A 112 -80.43 -171.33
REMARK 500 1 LYS A 117 -155.40 -82.28
REMARK 500 1 SER A 123 25.48 45.85
REMARK 500 1 MET A 125 -154.37 -112.18
REMARK 500 2 GLU A 2 60.29 173.87
REMARK 500 2 LYS A 5 -72.57 80.20
REMARK 500 2 VAL A 7 -71.23 -123.93
REMARK 500 2 LYS A 10 -37.96 -155.29
REMARK 500 2 LEU A 11 -144.84 64.20
REMARK 500 2 THR A 14 49.59 -160.15
REMARK 500 2 ILE A 23 37.19 -95.08
REMARK 500 2 ASN A 25 27.47 44.33
REMARK 500 2 PRO A 32 -156.58 -77.12
REMARK 500 2 TYR A 36 158.31 -45.05
REMARK 500 2 TYR A 40 131.90 -39.33
REMARK 500 2 GLU A 41 56.68 -90.66
REMARK 500 2 ASP A 43 -129.04 -162.16
REMARK 500 2 ASN A 60 88.25 -158.89
REMARK 500 2 LEU A 65 65.01 -116.83
REMARK 500 2 LYS A 67 91.38 -39.44
REMARK 500 2 ASN A 68 -44.22 -162.66
REMARK 500 2 SER A 69 -153.09 -63.93
REMARK 500 2 GLU A 102 30.26 -90.09
REMARK 500 2 SER A 103 -127.66 -57.30
REMARK 500 2 GLU A 104 -24.62 -39.92
REMARK 500 2 GLN A 112 78.58 78.48
REMARK 500 2 LYS A 117 -165.79 -79.69
REMARK 500 2 ALA A 122 -71.09 -74.56
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 22 0.22 SIDE CHAIN
REMARK 500 1 ARG A 51 0.21 SIDE CHAIN
REMARK 500 1 ARG A 96 0.11 SIDE CHAIN
REMARK 500 1 ARG A 107 0.10 SIDE CHAIN
REMARK 500 2 ARG A 22 0.27 SIDE CHAIN
REMARK 500 2 ARG A 51 0.27 SIDE CHAIN
REMARK 500 2 ARG A 96 0.24 SIDE CHAIN
REMARK 500 2 ARG A 107 0.30 SIDE CHAIN
REMARK 500 3 ARG A 22 0.28 SIDE CHAIN
REMARK 500 3 ARG A 51 0.31 SIDE CHAIN
REMARK 500 3 ARG A 96 0.21 SIDE CHAIN
REMARK 500 3 ARG A 107 0.17 SIDE CHAIN
REMARK 500 4 ARG A 22 0.30 SIDE CHAIN
REMARK 500 4 ARG A 51 0.24 SIDE CHAIN
REMARK 500 4 ARG A 96 0.27 SIDE CHAIN
REMARK 500 4 ARG A 107 0.31 SIDE CHAIN
REMARK 500 5 ARG A 22 0.18 SIDE CHAIN
REMARK 500 5 ARG A 51 0.32 SIDE CHAIN
REMARK 500 5 ARG A 96 0.31 SIDE CHAIN
REMARK 500 5 ARG A 107 0.27 SIDE CHAIN
REMARK 500 6 ARG A 22 0.23 SIDE CHAIN
REMARK 500 6 ARG A 51 0.12 SIDE CHAIN
REMARK 500 6 ARG A 96 0.27 SIDE CHAIN
REMARK 500 6 ARG A 107 0.32 SIDE CHAIN
REMARK 500 7 ARG A 22 0.17 SIDE CHAIN
REMARK 500 7 ARG A 51 0.11 SIDE CHAIN
REMARK 500 7 ARG A 96 0.16 SIDE CHAIN
REMARK 500 7 ARG A 107 0.16 SIDE CHAIN
REMARK 500 8 ARG A 22 0.09 SIDE CHAIN
REMARK 500 8 ARG A 51 0.21 SIDE CHAIN
REMARK 500 8 ARG A 96 0.19 SIDE CHAIN
REMARK 500 8 ARG A 107 0.24 SIDE CHAIN
REMARK 500 9 ARG A 22 0.18 SIDE CHAIN
REMARK 500 9 ARG A 51 0.27 SIDE CHAIN
REMARK 500 9 ARG A 96 0.21 SIDE CHAIN
REMARK 500 9 ARG A 107 0.25 SIDE CHAIN
REMARK 500 10 ARG A 22 0.30 SIDE CHAIN
REMARK 500 10 ARG A 51 0.31 SIDE CHAIN
REMARK 500 10 ARG A 96 0.20 SIDE CHAIN
REMARK 500 10 ARG A 107 0.29 SIDE CHAIN
REMARK 500 11 ARG A 22 0.23 SIDE CHAIN
REMARK 500 11 ARG A 51 0.17 SIDE CHAIN
REMARK 500 11 ARG A 96 0.32 SIDE CHAIN
REMARK 500 11 ARG A 107 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CENTER OF ACTIN MONOMER BINDING SITE, BASED ON
REMARK 800 COMPARISON WITH THE GELSOLIN SEGMENT 1-ACTIN COCRYSTAL (CENTERED
REMARK 800 ON ILE 79).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SIDE CHAINS THAT PROVIDE LIGANDS TO CALCIUM IN
REMARK 800 THE STRONGER BINDING SITE, BASED ON COMPARISON TO GELSOLIN
REMARK 800 SEGMENT 1 AND CALCIUM TITRATIONS MONITORED BY NMR. NOTE THIS
REMARK 800 CORRESPONDS TO THE INTRAMOLECULAR SITE IN THE GELSOLIN SEGMENT 1-
REMARK 800 ACTIN CO-CRYSTAL (ASP 43, GLU 73).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SIDE CHAIN THAT PROVIDES LIGANDS TO CALCIUM IN
REMARK 800 THE WEAKER BINDING SITE, BASED ON COMPARISON TO GELSOLIN SEGMENT
REMARK 800 1 AND CALCIUM TITRATIONS MONITORED BY NMR. NOTE THIS CORRESPONDS
REMARK 800 TO THE INTERMOLECULAR SITE IN THE GELSOLIN SEGMENT 1-ACTIN CO-
REMARK 800 CRYSTAL (ASP 85).
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VIK RELATED DB: PDB
DBREF 2VIL A 1 126 UNP P02640 VILI_CHICK 2 127
SEQRES 1 A 126 VAL GLU LEU SER LYS LYS VAL THR GLY LYS LEU ASP LYS
SEQRES 2 A 126 THR THR PRO GLY ILE GLN ILE TRP ARG ILE GLU ASN MET
SEQRES 3 A 126 GLU MET VAL PRO VAL PRO THR LYS SER TYR GLY ASN PHE
SEQRES 4 A 126 TYR GLU GLY ASP CYS TYR VAL LEU LEU SER THR ARG LYS
SEQRES 5 A 126 THR GLY SER GLY PHE SER TYR ASN ILE HIS TYR TRP LEU
SEQRES 6 A 126 GLY LYS ASN SER SER GLN ASP GLU GLN GLY ALA ALA ALA
SEQRES 7 A 126 ILE TYR THR THR GLN MET ASP GLU TYR LEU GLY SER VAL
SEQRES 8 A 126 ALA VAL GLN HIS ARG GLU VAL GLN GLY HIS GLU SER GLU
SEQRES 9 A 126 THR PHE ARG ALA TYR PHE LYS GLN GLY LEU ILE TYR LYS
SEQRES 10 A 126 GLN GLY GLY VAL ALA SER GLY MET LYS
HELIX 1 A1 LEU A 3 LYS A 10 1 8
HELIX 2 A2 GLN A 71 LEU A 88 1 18
HELIX 3 A3 SER A 103 TYR A 109 1 7
SHEET 1 CEN 5 VAL A 29 VAL A 31 0
SHEET 2 CEN 5 GLY A 17 ILE A 23 -1 N ARG A 22 O VAL A 29
SHEET 3 CEN 5 CYS A 44 LYS A 52 -1 N LEU A 48 O GLN A 19
SHEET 4 CEN 5 PHE A 57 LEU A 65 -1 N HIS A 62 O LEU A 47
SHEET 5 CEN 5 GLN A 94 VAL A 98 1 O HIS A 95 N TYR A 63
SHEET 1 PAR 2 ASN A 38 TYR A 40 0
SHEET 2 PAR 2 ILE A 115 LYS A 117 1 O ILE A 115 N PHE A 39
SITE 1 ACT 1 ILE A 79
SITE 1 CA1 2 ASP A 43 GLU A 73
SITE 1 CA2 1 ASP A 85
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 29 2 Bytes