BMRB Entry 15899

Title:
1H, 13C and 15N backbone chemical shift assignments of the C-terminal CH domain of human alpha-parvin
Deposition date:
2008-07-31
Original release date:
2008-11-19
Authors:
Lorenz, Sonja; Vakonakis, Ioannis; Campbell, Iain
Citation:

Citation: Lorenz, Sonja; Vakonakis, Ioannis; Lowe, Edward; Campbell, Iain; Noble, Martin; Hoellerer, Maria. "Structural Analysis of the Interactions between Paxillin LD motifs and alpha-Parvin"  Structure 16, 1521-1531 (2008).
PubMed: 18940607

Assembly members:

Assembly members:
C-terminal_CH_domain_of_alpha-parvin, polymer, 135 residues, 15460.8 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: pGEX-6P1

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts120
1H chemical shifts120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal CH domain of alpha-parvin1

Entities:

Entity 1, C-terminal CH domain of alpha-parvin 135 residues - 15460.8 Da.

1   GLYPROLEUGLYSERGLYARGHISGLUARG
2   ASPALAPHEASPTHRLEUPHEASPHISALA
3   PROASPLYSLEUASNVALVALLYSLYSTHR
4   LEUILETHRPHEVALASNLYSHISLEUASN
5   LYSLEUASNLEUGLUVALTHRGLULEUGLU
6   THRGLNPHEALAASPGLYVALTYRLEUVAL
7   LEULEUMETGLYLEULEUGLUGLYTYRPHE
8   VALPROLEUHISSERPHEPHELEUTHRPRO
9   ASPSERPHEGLUGLNLYSVALLEUASNVAL
10   SERPHEALAPHEGLULEUMETGLNASPGLY
11   GLYLEUGLULYSPROLYSPROARGPROGLU
12   ASPILEVALASNCYSASPLEULYSSERTHR
13   LEUARGVALLEUTYRASNLEUPHETHRLYS
14   TYRARGASNVALGLU

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 0.1 mM; D2O 5%; CHAPS 1.5 mM; C-terminal CH domain of alpha-parvin, [U-98% 13C; U-98% 15N], 240 uM; DTT 2 mM; H2O 95%

sample_conditions_1: ionic strength: 325 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2_01, Johnson, One Moon Scientific - data analysis

TOPSPIN v1.3, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DMX 500 MHz
  • home-built n.a. 750 MHz

Related Database Links:

BMRB 15760
PDB
DBJ BAA91815 BAA97981 BAC36771 BAE28686 BAG73514
GB AAG09802 AAG09803 AAG27173 AAG27175 AAH14535
REF NP_001092614 NP_060692 NP_065631 NP_065707 XP_001091788
SP Q9EPC1 Q9HB97 Q9NVD7
TPG DAA22326
AlphaFold Q9HB97 Q9EPC1 Q9NVD7

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