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 16093

Title: Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855). Northeast Structural Genomics Consortium target SrR106

Authors: Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS

Citation: Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh. "Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855) . Northeast Structural Genomics Consortium target SrR106"  Not known ., .-..

Assembly members:
SRU_2040, polymer, 153 residues, 17088.771 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
SRU_2040: MKTTPDILDQIRVHGADAYP EEGCGFLLGTVTDDGDNRVA ALHRATNRRSEQRTRRYELT ADDYRAADAAAQEQGLDVVG VYHSHPDHPARPSATDLEEA TFPGFTYVIVSVRDGAPEAL TAWALAPDRSEFHREDIVRP DPEAPLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts131
1H chemical shifts895

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SRU_20401

Entities:

Entity 1, SRU_2040 153 residues - 17088.771 Da.

1   METLYSTHRTHRPROASPILELEUASPGLN
2   ILEARGVALHISGLYALAASPALATYRPRO
3   GLUGLUGLYCYSGLYPHELEULEUGLYTHR
4   VALTHRASPASPGLYASPASNARGVALALA
5   ALALEUHISARGALATHRASNARGARGSER
6   GLUGLNARGTHRARGARGTYRGLULEUTHR
7   ALAASPASPTYRARGALAALAASPALAALA
8   ALAGLNGLUGLNGLYLEUASPVALVALGLY
9   VALTYRHISSERHISPROASPHISPROALA
10   ARGPROSERALATHRASPLEUGLUGLUALA
11   THRPHEPROGLYPHETHRTYRVALILEVAL
12   SERVALARGASPGLYALAPROGLUALALEU
13   THRALATRPALALEUALAPROASPARGSER
14   GLUPHEHISARGGLUASPILEVALARGPRO
15   ASPPROGLUALAPROLEUGLUHISHISHIS
16   HISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.7 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 10%; Protease Inhibitors 1

sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 5%; Protease Inhibitors 1

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
(4,3)D HABCAB(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
(4,3)D HCCHsample_1isotropicsample_conditions_1
(N15-H1, C13-H1) simNOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_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

XEASY, Bartels et al. - peak picking

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

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CBH25176
GB ABC44045
REF WP_011404768 YP_446146