BMRB Entry 15269

Title:
Complete resonance assignments and solution structure calcualtion of ATC2521 (NESG ID: AtT6) from Agrobacterium tumeraciens
Deposition date:
2007-05-29
Original release date:
2007-07-05
Authors:
Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl
Citation:

Citation: Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl. "Solution Structure of a protein (ATC2521)of unknow function from Agrobacterium tumefaciens"  .

Assembly members:

Assembly members:
ATC2521, polymer, 188 residues, 11548.9 Da.

Natural source:

Natural source:   Common Name: Agrobacterium tumefaciens   Taxonomy ID: 358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Agrobacterium tumefaciens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21-CodonPlus(DE3)-RP

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts77
1H chemical shifts560

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ATC25211

Entities:

Entity 1, ATC2521 188 residues - 11548.9 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISMETASNALATHRILEARGGLUILE
4   LEUALALYSPHEGLYGLNLEUPROTHRPRO
5   VALASPTHRILEALAASPGLUALAASPLEU
6   TYRALAALAGLYLEUSERSERPHEALASER
7   VALGLNLEUMETLEUGLYILEGLUGLUALA
8   PHEASPILEGLUPHEPROASPASNLEULEU
9   ASNARGLYSSERPHEALASERILELYSALA
10   ILEGLUASPTHRVALLYSLEUILELEUASP
11   GLYLYSGLUALAALAMETASNALATHRILE
12   ARGGLUILELEUALALYSPHEGLYGLNLEU
13   PROTHRPROVALASPTHRILEALAASPGLU
14   ALAASPLEUTYRALAALAGLYLEUSERSER
15   PHEALASERVALGLNLEUMETLEUGLYILE
16   GLUGLUALAPHEASPILEGLUPHEPROASP
17   ASNLEULEUASNARGLYSSERPHEALASER
18   ILELYSALAILEGLUASPTHRVALLYSLEU
19   ILELEUASPGLYLYSGLUALAALA

Samples:

sample_1: ATC2521, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; TRIS 10 ± 0.2 mM; glycerol 5 ± 0.2 %; Benzamidine 1 ± 0.2 mM; sodium chloride 300 ± 0.2 mM; sodium azide 0.01 ± 0.1 %

sample_2: ATC2521, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; TRIS 10 ± 0.2 mM; glycerol 5 ± 0.2 %; Benzamidine 1 ± 0.2 mM; sodium chloride 300 ± 0.2 mM; sodium azide 0.01 ± 0.1 %

sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • 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