BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16564

Title: NMR Structure of Agrobacterium tumefaciens protein Atu1219: Northeast Structural Genomics Consortium target AtT14

Deposition date: 2009-10-18 Original release date: 2012-08-03

Authors: Cort, John; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael

Citation: Cort, John; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael. "NMR Structure of Agrobacterium tumefaciens protein Atu1219"  .

Assembly members:
Atu1219, polymer, 100 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11

Entity Sequences (FASTA):
Atu1219: MEVQSMLLNDVKWEKPVTIS LQNGAPRIFNGVYEAFDFLQ HEWPARGDRAHEQALRLCRA SLMGDVAGEIARTAFVAASR QAHCLMEDKAEAPNTIASGS

Data sets:
Data typeCount
13C chemical shifts421
15N chemical shifts107
1H chemical shifts636

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Atu12191

Entities:

Entity 1, Atu1219 100 residues - Formula weight is not available

1   METGLUVALGLNSERMETLEULEUASNASP
2   VALLYSTRPGLULYSPROVALTHRILESER
3   LEUGLNASNGLYALAPROARGILEPHEASN
4   GLYVALTYRGLUALAPHEASPPHELEUGLN
5   HISGLUTRPPROALAARGGLYASPARGALA
6   HISGLUGLNALALEUARGLEUCYSARGALA
7   SERLEUMETGLYASPVALALAGLYGLUILE
8   ALAARGTHRALAPHEVALALAALASERARG
9   GLNALAHISCYSLEUMETGLUASPLYSALA
10   GLUALAPROASNTHRILEALASERGLYSER

Samples:

sample_1: Atu1219, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 450 mM; MES 20 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_2: Atu1219, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 450 mM; MES 20 mM; DTT 5 mM; D2O 100%

sample_3: Atu1219, [U-100% 15N], 7% 13C biosynthetically directed labeling, 0.9 mM; sodium chloride 450 mM; MES 20 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.45 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
4D 1H-13C-13C-1H HMQC-NOESY-HMQCsample_2isotropicsample_conditions_1

Software:

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

SPARKY, Goddard - chemical shift assignment

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

PSVS, Bhattacharya and Montelione - refinement

FELIX, Accelrys Software Inc. - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

PDB
GB AAK87021 EGL64935 KEY55612 KJX88779
REF NP_354236 WP_006312770 WP_010971479 WP_035256530

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts