BMRB Entry 16372

Title:
Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351
Deposition date:
2009-06-29
Original release date:
2009-06-30
Authors:
Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Rumpel, Sigrun; Semest, Anthony; Arrowsmith, Cheryl
Citation:

Citation: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Rumpel, Sigrun; Semest, Anthony; Arrowsmith, Cheryl. "Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351"  .

Assembly members:

Assembly members:
af2351, polymer, 139 residues, 16693.863 Da.

Natural source:

Natural source:   Common Name: Archaeoglobus fulgidus   Taxonomy ID: 2234   Superkingdom: Archaea   Kingdom: not available   Genus/species: Archaeoglobus fulgidus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p11

Data sets:
Data typeCount
13C chemical shifts574
15N chemical shifts114
1H chemical shifts963

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1af23511

Entities:

Entity 1, af2351 139 residues - 16693.863 Da.

1   METSERLYSILEVALGLYVALTHRTYRPRO
2   ILEPROLYSARGPHEMETASPARGPHEPHE
3   LYSLYSGLYLYSASPVALPHEVALLYSPRO
4   ALATHRVALTRPLYSGLULEULYSPROGLY
5   METLYSPHEVALPHETYRGLNSERHISGLU
6   ASPTHRGLYPHEVALGLYGLUALAARGILE
7   LYSARGVALVALLEUSERGLUASNPROMET
8   GLNPHEPHEGLUTHRPHEGLYASPARGVAL
9   PHELEUTHRLYSASPGLULEULYSGLUTYR
10   METLYSSERGLNGLUARGTRPGLYARGARG
11   ARGGLUSERLYSLYSLYSLYSLEUTRPMET
12   ALAILEGLULEUGLUASPVALLYSLYSTYR
13   ASPLYSPROILELYSPROLYSARGLEUVAL
14   PROVALGLYGLYGLNTYRLEUARGGLU

Samples:

sample_1: af2351, [U-100% 13C; U-100% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; H2O 90%; D2O 10%

sample_2: af2351, [U-100% 13C; U-100% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; D2O 99.9%

sample_3: af2351, [U-7% 13C; U-99% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDGUI v1.0, Gutmanas and Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis, peak picking

FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment

PSVS, Bhattacharya and Montelione - NMR structure quality assessment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAB91313
REF WP_010879837

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