BMRB Entry 17206

Title:
villin head piece domain of human ABLIM2
Deposition date:
2010-09-24
Original release date:
2010-10-22
Authors:
Bruton, Shaun; Pfuhl, Mark
Citation:

Citation: Bruton, Shaun; Pfuhl, Mark. "Solution NMR study of the actin binding domain of ABLIM2"  .

Assembly members:

Assembly members:
VHD, polymer, 67 residues, 8212.633 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLEICS-07

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts331
15N chemical shifts68
1H chemical shifts529

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VHD in monomer1

Entities:

Entity 1, VHD in monomer 67 residues - 8212.633 Da.

1   GLNTYRLYSILETYRPROTYRASPSERLEU
2   ILEVALTHRASNARGILEARGVALLYSLEU
3   PROLYSASPVALASPARGTHRARGLEUGLU
4   ARGHISLEUSERPROGLUGLUPHEGLNGLU
5   VALPHEGLYMETSERILEGLUGLUPHEASP
6   ARGLEUALALEUTRPLYSARGASNASPLEU
7   LYSLYSLYSALALEULEUPHE

Samples:

sample_1: VHD 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 100%

sample_2: VHD, [U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 5%; H2O 95%

sample_3: VHD, [U-99% 13C; U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 5%; H2O 95%

sample_4: VHD, [U-99% 13C; U-99% 15N], 0.7 ± 0.02 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; sodium azide 0.02 ± 0.0005 %; D2O 100%

sample_conditions_1: ionic strength: 90 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACOsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
2D 13C CT-HSQCsample_4isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPN_Analysis v2.1, CCPN (Laue et al.) - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB47437 BAC04414 BAC04427 BAC32651 BAC32905
EMBL CAD38885 CAG28314 CAG28315 CAG38375 CAG38376
GB AAI22568 AAI41126 AAI56705 AAP23233 ABD83328
REF NP_001001514 NP_001123555 NP_001123556 NP_001123557 NP_001123558
SP Q6H8Q1 Q6KC51 Q8BL65
AlphaFold Q6H8Q1 Q6KC51 Q8BL65

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