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Biological Magnetic Resonance Data Bank


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BMRB Entry 16347

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16347
MolProbity Validation Chart

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Title: Solution NMR structure of protein ATC0852 from Agrobacterium tumefaciens. Northeast Structural Genomics Consortium (NESG) target AtT2.

Deposition date: 2009-06-12 Original release date: 2009-07-07

Authors: Lemak, Alexander; Yee, Adelinda; Gutmanas, Aleksandras; Fares, Christophe; Garcia, Maite; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Gutmanas, Aleksandras; Fares, Christophe; Garcia, Maite; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution structure of protein ATC0852 from Agrobacterium tumefaciens"  Not known ., .-..

Assembly members:
ATC0852, polymer, 144 residues, 13259.014 Da.

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

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

Entity Sequences (FASTA):
ATC0852: MGSSHHHHHHSSGRENLYFQ GHMTHPDFTILYVDNPPAST QFYKALLGVDPVESSPTFSL FVLANGMKLGLWSRHTVEPK ASVTGGGGELAFRVENDAQV DETFAGWKASGVAMLQQPAK MEFGYTFTAADPDSHRLRVY AFAG

Data typeCount
13C chemical shifts465
15N chemical shifts119
1H chemical shifts774

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ATC0852_11
2ATC0852_21

Entities:

Entity 1, ATC0852_1 144 residues - 13259.014 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISMETTHRHISPROASPPHETHRILE
4   LEUTYRVALASPASNPROPROALASERTHR
5   GLNPHETYRLYSALALEULEUGLYVALASP
6   PROVALGLUSERSERPROTHRPHESERLEU
7   PHEVALLEUALAASNGLYMETLYSLEUGLY
8   LEUTRPSERARGHISTHRVALGLUPROLYS
9   ALASERVALTHRGLYGLYGLYGLYGLULEU
10   ALAPHEARGVALGLUASNASPALAGLNVAL
11   ASPGLUTHRPHEALAGLYTRPLYSALASER
12   GLYVALALAMETLEUGLNGLNPROALALYS
13   METGLUPHEGLYTYRTHRPHETHRALAALA
14   ASPPROASPSERHISARGLEUARGVALTYR
15   ALAPHEALAGLY

Samples:

sample_1: atc0852, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 300 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC (IPAP)sample_1anisotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAK86676 EGL65239 KEY55269 KJX89096
REF NP_353891 WP_006312208 WP_010971212

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