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 15482

Title: Solution NMR Structure of R. sphaeroides protein RSP_1027: Northeast Structural Genomics Consortium Target RhR95.

Deposition date: 2007-09-21 Original release date: 2007-10-02

Authors: Eletsky, Alexander; Sukumaran, Dinesh; Zhang, Qi; Parish, David; Xu, Duanxiang; Wang, Huang; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of R. sphaeroides protein RHOS4_26430: Northeast Structural Genomics Consortium Target RhR95"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
rhr95_protein, polymer, 80 residues, Formula weight is not available

Natural source:   Common Name: Rhodobacter sphaeroides   Taxonomy ID: 1063   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodobacter sphaeroides

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts296
15N chemical shifts80
1H chemical shifts463

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, protein 80 residues - Formula weight is not available

8-residue C-terminal His-tag LEHHHHHH



NC: rhr95_protein, [U-100% 13C; U-100% 15N], 0.7 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5: rhr95_protein, [U-5% 13C; U-100% 15N], 0.7 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 135 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
(4,3)D GFT CABCA(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HNNCABCANCisotropicsample_conditions_1
(4,3)D GFT HABCABCA(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphaticNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aromaticNCisotropicsample_conditions_1
2D 1H-15N long-range HSQCNCisotropicsample_conditions_1
2D 1H-13C ct-HSQC 28msNC5isotropicsample_conditions_1
3D 1H-15N/13C NOESYNCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNCisotropicsample_conditions_1
2D 1H-13C ct-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C ct-HSQC aromaticNCisotropicsample_conditions_1
3D (H)CCH-TOCSYNCisotropicsample_conditions_1
2D 1H-13C ct-HSQC 56msNC5isotropicsample_conditions_1


VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller - chemical shift assignment, data analysis, peak picking

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

PSVS, Bhattacharya and Montelione - structure validation

XEASY v1.3.12, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

GB ABA80211 ABN77790 ACM02281 EGJ22528 EKX58095
REF WP_002721359 YP_354112

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