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 16371

Title: Solution Structure Of Protein DSY2949 From Desulfitobacterium hafniense. Northeast Structural Genomics Consortium Target DhR27

Authors: Wu, Yibing; Mills, Jeffrey; Wang, H.; Ciccosanti, C.; Jiang, M.; Sukumaran, Dinesh; Zhang, Qi; Nair, R.; Rost, B.; Acton, T.B.; Xiao, R.; Swapna, G.V.T.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas

Citation: Wu, Yibing; Mills, Jeffrey; Wang, H.; Ciccosanti, C.; Jiang, M.; Sukumaran, Dinesh; Zhang, Qi; Nair, R.; Rost, B.; Acton, T.B.; Xiao, R.; Swapna, G.V.T.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas. "Solution Structure Of Protein DSY2949 From Desulfitobacterium hafniense. Northeast Structural Genomics Consortium Target DhR27"  Not known ., .-..

Assembly members:
DSY2949, polymer, 146 residues, 16823.293 Da.

Natural source:   Common Name: Desulfitobacterium hafniense   Taxonomy ID: 49338   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Desulfitobacterium hafniense

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

Entity Sequences (FASTA):
DSY2949: MITLTKKQMEEMLAHARQAL PNEACGLLGGRRDGDDRWVE RVYPLNNLDQSPEHFSMDPR EQLTAVKDMRKNGWVMLGNF HSHPATPARPSAEDKRLAFD PSLSYLIISLAEPQKPVCKS FLIKKDGVDEEEIILKEELE HHHHHH

Data sets:
Data typeCount
13C chemical shifts486
15N chemical shifts142
1H chemical shifts1015

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DSY29491

Entities:

Entity 1, DSY2949 146 residues - 16823.293 Da.

1   METILETHRLEUTHRLYSLYSGLNMETGLU
2   GLUMETLEUALAHISALAARGGLNALALEU
3   PROASNGLUALACYSGLYLEULEUGLYGLY
4   ARGARGASPGLYASPASPARGTRPVALGLU
5   ARGVALTYRPROLEUASNASNLEUASPGLN
6   SERPROGLUHISPHESERMETASPPROARG
7   GLUGLNLEUTHRALAVALLYSASPMETARG
8   LYSASNGLYTRPVALMETLEUGLYASNPHE
9   HISSERHISPROALATHRPROALAARGPRO
10   SERALAGLUASPLYSARGLEUALAPHEASP
11   PROSERLEUSERTYRLEUILEILESERLEU
12   ALAGLUPROGLNLYSPROVALCYSLYSSER
13   PHELEUILELYSLYSASPGLYVALASPGLU
14   GLUGLUILEILELEULYSGLUGLULEUGLU
15   HISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.9 mM; H2O 90%; D2O 10%

sample_2: entity, [U-10% 13C; U-100% 15N], 0.9 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
simNOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - refinement

TALOS, Cornilescu, Delaglio and Bax - refinement

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAE84738
EMBL CDX03072
GB ACL22117 EHL04548
REF WP_005816173 WP_018212606