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 15344

Title: The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5

Authors: Wang, Lincong; Chen, Chen; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Wang, Lincong; Montelione, Gaetano. "The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5"  Proteins ., .-..

Assembly members:
RhR5, polymer, 95 residues, 10881.731 Da.

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

Entity Sequences (FASTA):
RhR5: MYLKRVDGPRQVTLPDGTVL SRADLPPLDTRRWVASRKAA VVKAVIHGLITEREALDRYS LSEEEFALWRSAVAAHGEKA LKVTMIQKYRQLHHH

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts97
1H chemical shifts672

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RhR51

Entities:

Entity 1, RhR5 95 residues - 10881.731 Da.

Residues 93-95 represent a non-native affinity tag

1   METTYRLEULYSARGVALASPGLYPROARG
2   GLNVALTHRLEUPROASPGLYTHRVALLEU
3   SERARGALAASPLEUPROPROLEUASPTHR
4   ARGARGTRPVALALASERARGLYSALAALA
5   VALVALLYSALAVALILEHISGLYLEUILE
6   THRGLUARGGLUALALEUASPARGTYRSER
7   LEUSERGLUGLUGLUPHEALALEUTRPARG
8   SERALAVALALAALAHISGLYGLULYSALA
9   LEULYSVALTHRMETILEGLNLYSTYRARG
10   GLNLEUHISHISHIS

Samples:

sample_1: RhR5, [U-5% 13C; U-100% 15N], 1.0 mM; DTT 10 mM; sodium chloride 100 mM

sample_2: RhR5, [U-100% 13C; U-100% 15N], 1.0 mM; DTT 10 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293.0 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - data analysis

X-PLOR, Brunger - structure solution

PSVS, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB ABA78777 ABN76388 ACM00792 EGJ21075
REF WP_002719769 WP_011840915 YP_352678