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 15419

Title: Solution Structure of protein RPA3401, Northeast Structural Genomics Consortium Target RpT7, Ontario Center for Structural Proteomics Target RP3384

Authors: Ignatchenko, Alexandr; Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Arrowsmith, Cheryl

Citation: Ignatchenko, Alexandr; Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Arrowsmith, Cheryl. "Solution Structure of protein RPA3401, Northeast Structural Genomics Consortium Target RpT7, Ontario Center for Structural Proteomics Target RP3384"  The BMRB entry is the only known published source for the data..

Assembly members:
RPA3401, polymer, 65 residues, 7380.308 Da.

Natural source:   Common Name: Rhodopseudomonas palustris   Taxonomy ID: 1076   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustris

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

Entity Sequences (FASTA):
RPA3401: MATADDFKLIRDIHSTGGRR QVFGSREQKPFEDLVDLGWL KRSSVDSRATHYQITERGTS AALRS

Data sets:
Data typeCount
13C chemical shifts249
15N chemical shifts57
1H chemical shifts400

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RPA34011

Entities:

Entity 1, RPA3401 65 residues - 7380.308 Da.

1   METALATHRALAASPASPPHELYSLEUILE
2   ARGASPILEHISSERTHRGLYGLYARGARG
3   GLNVALPHEGLYSERARGGLUGLNLYSPRO
4   PHEGLUASPLEUVALASPLEUGLYTRPLEU
5   LYSARGSERSERVALASPSERARGALATHR
6   HISTYRGLNILETHRGLUARGGLYTHRSER
7   ALAALALEUARGSER

Samples:

sample_1: RHA3401, [U-13C; U-15N], 0.6 mM; NaCl 300 mM; TRIS, [U-99% 2H], 10 mM; Benzamidine 1 mM; NaN3 0.01%

sample_2: RHA3401, [U-13C; U-15N], 0.6 mM; NaCl 300 mM; TRIS, [U-99% 2H], 10 mM; Benzamidine 1 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 300 mM; pH: 7; 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 HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D (H)CCH TOCSYsample_2isotropicsample_conditions_1
3D H(C)CH TOCSYsample_2isotropicsample_conditions_1
4D(PR) HBHACBCA(CO)NHsample_1isotropicsample_conditions_1
4D(PR) HCC(CO)NH TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C aromatic NOESYsample_1isotropicsample_conditions_1

Software:

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

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAE28842
GB ACF02378
REF WP_011158943