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Biological Magnetic Resonance Data Bank


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BMRB Entry 18046

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18046
MolProbity Validation Chart

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Title: Sixth Gelsolin-like domain of villin   PubMed: 24070253

Deposition date: 2011-11-07 Original release date: 2012-11-05

Authors: Pfaff, Danielle; Brockerman, Jacob; Fedechkin, Stanislav; Burns, Lucian; Zhang, Fengli; McKnight, C. James; Smirnov, Serge

Citation: Fedechkin, Stanislav; Brockerman, Jacob; Pfaff, Danielle; Burns, Lucian; Webb, Terry; Nelson, Alexander; Zhang, Fengli; Sabantsev, Anton; Melnikov, Alexey; McKnight, C. James; Smirnov, Serge. "Gelsolin-like activation of villin: calcium sensitivity of the long helix in domain 6."  Biochemistry 52, 7890-7900 (2013).

Assembly members:
D6, polymer, 107 residues, 12427.814 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
D6: PRLFECSNKTGRFLATEIVD FTQDDLDENDVYLLDTWDQI FFWIGKGANESEKEAAAETA QEYLRSHPGSRDLDTPIIVV KQGFEPPTFTGWFMAWDPLC WSDRKSY

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts108
1H chemical shifts631

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1D61

Entities:

Entity 1, D6 107 residues - 12427.814 Da.

Corresponds to 107 residue polypeptide from villin [gallus gallus] starting at position 619 and ending at 725

1   PROARGLEUPHEGLUCYSSERASNLYSTHR
2   GLYARGPHELEUALATHRGLUILEVALASP
3   PHETHRGLNASPASPLEUASPGLUASNASP
4   VALTYRLEULEUASPTHRTRPASPGLNILE
5   PHEPHETRPILEGLYLYSGLYALAASNGLU
6   SERGLULYSGLUALAALAALAGLUTHRALA
7   GLNGLUTYRLEUARGSERHISPROGLYSER
8   ARGASPLEUASPTHRPROILEILEVALVAL
9   LYSGLNGLYPHEGLUPROPROTHRPHETHR
10   GLYTRPPHEMETALATRPASPPROLEUCYS
11   TRPSERASPARGLYSSERTYR

Samples:

sample_1: H2O 50 M; D2O, [U-2H], 5 M; DTT, [U-2H], 10 mM; sodium azide 0.01%; Calcium Chloride 5 mM; PIPES, [U-2H], 20 mM; D6, [U-99% 13C; U-99% 15N], 1 mM

sample_2: H2O 50 M; D2O, [U-2H], 5 M; DTT, [U-2H], 10 mM; sodium azide 0.01%; Calcium Chloride 5 mM; PIPES, [U-2H], 20 mM; D6 1 mM

sample_3: D2O, [U-2H], 55 M; DTT, [U-2H], 10 mM; sodium azide 0.01%; Calcium Chloride 5 mM; PIPES, [U-2H], 20 mM; D6 1 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 273 K

sample_conditions_2: pH: 7; pressure: 1 atm; temperature: 273 K

sample_conditions_3: pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRView v5.2.2, Johnson, One Moon Scientific - peak picking

NMRPipe v5.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

PREDITOR v1.0, Berjanskii MV, Neal S, Wishart DS - dihedral prediction, geometry optimization, structure solution

NMR spectrometers:

  • Varian INOVA 720 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15097 19497
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts