BMRB Entry 25767

Title:
NMR structure of the Vta1NTD-Did2(176-204) complex
Deposition date:
2015-08-25
Original release date:
2016-09-29
Authors:
Shen, Jie; Yang, Zhongzheng; Wang, Jiaolong; Vild, Cody
Citation:

Citation: Shen, Jie; Yang, Zhongzheng; Wang, Jiaolong; Zhao, Bin; Lan, Wenxian; Wang, Chunxi; Zhang, Xu; Wild, Cody; Liu, Maili; Xu, Zhaohui; Cao, Chunyang. "NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway"  Sci. Rep. 6, 38710-38710 (2016).
PubMed: 27924850

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 19062.176 Da.
entity_2, polymer, 29 residues, 3341.826 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Data sets:
Data typeCount
13C chemical shifts688
15N chemical shifts185
1H chemical shifts1304

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 167 residues - 19062.176 Da.

1   METALASERASNALAALAARGVALVALALA
2   THRALALYSASPPHEASPLYSVALGLYLEU
3   GLYILEILEGLYTYRTYRLEUGLNLEUTYR
4   ALAVALGLULEUILELEUSERGLUGLUASP
5   ARGSERGLNGLUMETTHRALALEUALATHR
6   GLULEULEUASPTHRILEGLUALAPHELYS
7   LYSGLUILEGLYGLYGLUSERGLUALAGLU
8   ASPSERASPLYSSERLEUHISVALMETASN
9   THRLEUILEHISASPGLNGLULYSALALYS
10   ILETYRMETLEUASNPHETHRMETSERLEU
11   TYRASNGLULYSLEULYSGLNLEULYSASP
12   GLYPROTRPASPVALMETLEULYSARGSER
13   LEUTRPCYSCYSILEASPLEUPHESERCYS
14   ILELEUHISLEUTRPLYSGLUASNILESER
15   GLUTHRSERTHRASNSERLEUGLNLYSARG
16   ILELYSTYRCYSLYSILETYRLEUSERLYS
17   LEUALALYSGLYGLUILEGLY

Entity 2, entity_2 29 residues - 3341.826 Da.

1   ASNVALPROGLUILELYSALALYSGLUVAL
2   ASNVALASPASPGLULYSGLUASPLYSLEU
3   ALAGLNARGLEUARGALALEUARGGLY

Samples:

sample_1: entity_1, [U-13C; U-15N], 1.5 mM; entity_1, [U-13C; U-15N; U-70% 2H], 1.5 mM; entity_2 1.8 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 5 mM; D2O, [U-100% 2H], 10%; sodium azide 0.02%

sample_2: entity_1 1.8 mM; entity_2, [U-13C; U-15N], 1.5 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 5 mM; D2O, [U-100% 2H], 10%; sodium azide 0.02%

sample_conditions_1: ionic strength: 175 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 13C-F1 edited NOESYsample_1isotropicsample_conditions_1
3D 13C-F1 edited NOESYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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