BMRB Entry 15097

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15097

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Title:
Dynamics and Calcium-Dependent Actin Bundling by the two Carboxy Terminal Domains of Villin
Deposition date:
2007-01-08
Original release date:
2007-08-21
Authors:
Smirnov, Serge; Isern, Nancy; Hoyt, David; Jiang, Zhenghi; McKnight, C. James
Citation:

Citation: Smirnov, Serge; Isern, Nancy; Jiang, Zhenghui; Hoyt, David; McKnight, C. James. "The Isolated Sixth Gelsolin Repeat and Headpiece Domain of Villin Bundle F-Actin in the Presence of Calcium and Are Linked by a 40-Residue Unstructured Sequence"  Biochemistry 46, 7488-7496 (2007).
PubMed: 17547371

Assembly members:

Assembly members:
D6-HP, polymer, 208 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pD6-HP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
D6-HP: PRLFECSNKTGRFLATEIVD FTQDDLDENDVYLLDTWDQI FFWIGKGANESEKEAAAETA QEYLRSHPGSRDLDTPIIVV KQGFEPPTFTGWFMAWDPLC WSDRKSYDELKAELGDNASI GQLVSGLTSKNEVFTATTTL VPTKLETFPLDVLVNTAAED LPRGVDPSRKENHLSDEDFK AVFGMTRSAFANLPLWKQQN LKKEKGLF

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts176
1H chemical shifts905
heteronuclear NOE values144
order parameters107
T1 relaxation values144
T2 relaxation values144

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1D6-HP1

Entities:

Entity 1, D6-HP 208 residues - Formula weight is not available

1   PROARGLEUPHEGLUCYSSERASNLYSTHR
2   GLYARGPHELEUALATHRGLUILEVALASP
3   PHETHRGLNASPASPLEUASPGLUASNASP
4   VALTYRLEULEUASPTHRTRPASPGLNILE
5   PHEPHETRPILEGLYLYSGLYALAASNGLU
6   SERGLULYSGLUALAALAALAGLUTHRALA
7   GLNGLUTYRLEUARGSERHISPROGLYSER
8   ARGASPLEUASPTHRPROILEILEVALVAL
9   LYSGLNGLYPHEGLUPROPROTHRPHETHR
10   GLYTRPPHEMETALATRPASPPROLEUCYS
11   TRPSERASPARGLYSSERTYRASPGLULEU
12   LYSALAGLULEUGLYASPASNALASERILE
13   GLYGLNLEUVALSERGLYLEUTHRSERLYS
14   ASNGLUVALPHETHRALATHRTHRTHRLEU
15   VALPROTHRLYSLEUGLUTHRPHEPROLEU
16   ASPVALLEUVALASNTHRALAALAGLUASP
17   LEUPROARGGLYVALASPPROSERARGLYS
18   GLUASNHISLEUSERASPGLUASPPHELYS
19   ALAVALPHEGLYMETTHRARGSERALAPHE
20   ALAASNLEUPROLEUTRPLYSGLNGLNASN
21   LEULYSLYSGLULYSGLYLEUPHE

Samples:

sample_1: D6-HP, [U-98% 13C; U-98% 15N], 1.1 ± 0.1 mM; DTT, [U-2H], 10 mM; TSP 1 mM; PIPES, [U-2H], 20 mM; Ca2+ 5 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 0.01 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
15N T1sample_1isotropicsample_conditions_1
15N T2sample_1isotropicsample_conditions_1
1H,15N NOEsample_1isotropicsample_conditions_1

Software:

fastModelFree, J. Patrick Loria - model-free analysis

NMRView, Johnson, One Moon Scientific - peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18046 19497
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks