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 18215

Title: Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50.

Authors: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50."  To be published ., .-..

Assembly members:
HsR50, polymer, 191 residues, 20753.697 Da.

Natural source:   Common Name: Halobacterium salinarium   Taxonomy ID: 2242   Superkingdom: Archaea   Kingdom: not available   Genus/species: Halobacterium salinarium

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

Entity Sequences (FASTA):
HsR50: MSPIPLPVTDTDDAWRARIA AHRADKDEFLATHDQSPIPP ADRGAFDGLRYFDIDASFRV AARYQPARDPEAVELETTRG PPAEYTRAAVLGFDLGDSHH TLTAFRVEGESSLFVPFTDE TTDDGRTYEHGRYLDVDPAG ADGGDEVALDFNLAYNPFCA YGGSFSCALPPADNHVPAAI TAGERVDADLE

Data sets:
Data typeCount
13C chemical shifts704
15N chemical shifts169
1H chemical shifts1023

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HsR501

Entities:

Entity 1, HsR50 191 residues - 20753.697 Da.

1   METSERPROILEPROLEUPROVALTHRASP
2   THRASPASPALATRPARGALAARGILEALA
3   ALAHISARGALAASPLYSASPGLUPHELEU
4   ALATHRHISASPGLNSERPROILEPROPRO
5   ALAASPARGGLYALAPHEASPGLYLEUARG
6   TYRPHEASPILEASPALASERPHEARGVAL
7   ALAALAARGTYRGLNPROALAARGASPPRO
8   GLUALAVALGLULEUGLUTHRTHRARGGLY
9   PROPROALAGLUTYRTHRARGALAALAVAL
10   LEUGLYPHEASPLEUGLYASPSERHISHIS
11   THRLEUTHRALAPHEARGVALGLUGLYGLU
12   SERSERLEUPHEVALPROPHETHRASPGLU
13   THRTHRASPASPGLYARGTHRTYRGLUHIS
14   GLYARGTYRLEUASPVALASPPROALAGLY
15   ALAASPGLYGLYASPGLUVALALALEUASP
16   PHEASNLEUALATYRASNPROPHECYSALA
17   TYRGLYGLYSERPHESERCYSALALEUPRO
18   PROALAASPASNHISVALPROALAALAILE
19   THRALAGLYGLUARGVALASPALAASPLEU
20   GLU

Samples:

sample_1: hsr50.005, [U-100% 13C; U-100% 15N], 0.726 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_2: hsr50.009, [U-100% 13C; U-100% 15N; U-2H], 0.800 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_3: hsr50.007, [U-100% 13C; U-100% 15N], 0.674 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_conditions_1: pH: 6.5; 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 HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
cCH_NOESYsample_2isotropicsample_conditions_1
nNH_NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1
3D HA(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

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

TOPSPIN, Bruker Biospin - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

PDBStat v5.5-exp, Tejero; Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAP13480
GB AAG19211
REF WP_010902507