BMRB Entry 15419

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15419
MolProbity Validation Chart

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Title:
Solution Structure of protein RPA3401, Northeast Structural Genomics Consortium Target RpT7, Ontario Center for Structural Proteomics Target RP3384
Deposition date:
2007-08-07
Original release date:
2007-08-13
Authors:
Ignatchenko, Alexandr; Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Arrowsmith, Cheryl
Citation:

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:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p15Tv lic

Entity Sequences (FASTA):

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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks