BMRB Entry 18776

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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/BMR18776
MolProbity Validation Chart

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Title:
1H, 13C, 15N backbone NMR resonance assignments for N-terminal RNA recognition motif of HvRBP1 from Hordeum vulgare L. (barley)
Deposition date:
2012-10-10
Original release date:
2013-01-22
Authors:
Mason, Katelyn; Tripet, Brian; Fischer, Andreas; Copie, Valerie
Citation:

Citation: Mason, Katelyn; Tripet, Brian; Parrott, David; Fischer, Andreas; Copie, Valerie. "(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23417794

Assembly members:

Assembly members:
RBP1, polymer, 92 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: barley   Taxonomy ID: 4513   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Hordeum Hordeum vulgare L.

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET46 ek/LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RBP1: MAESDGAEYRCFVGSLSWNT DDRGLEAAFSSFGEILDAKI INDRETGRSRGFGFVSFSNE QAMQDAIEGMNGKELDGRSI VVNEAQSRGYGG

Data sets:
Data typeCount
13C chemical shifts248
15N chemical shifts91
1H chemical shifts443

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Hordeum vulgare glycine rich- RNA binding protein 11

Entities:

Entity 1, Hordeum vulgare glycine rich- RNA binding protein 1 92 residues - Formula weight is not available

N-Terminal RNA recognition Domain of RBP1

1   METALAGLUSERASPGLYALAGLUTYRARG
2   CYSPHEVALGLYSERLEUSERTRPASNTHR
3   ASPASPARGGLYLEUGLUALAALAPHESER
4   SERPHEGLYGLUILELEUASPALALYSILE
5   ILEASNASPARGGLUTHRGLYARGSERARG
6   GLYPHEGLYPHEVALSERPHESERASNGLU
7   GLNALAMETGLNASPALAILEGLUGLYMET
8   ASNGLYLYSGLULEUASPGLYARGSERILE
9   VALVALASNGLUALAGLNSERARGGLYTYR
10   GLYGLY

Samples:

15N_13C_HvGR-RBP1: RBP1, [U-99% 13C; U-99% 15N], 15 mM; sodium azide 0.01%; potassium phosphate 50 mM; D2O 5%; EDTA 1 mM; sodium chloride 500 mM; PMSF 1 mM

15N_13C_HvGr_RBP1_conditions_1: ionic strength: 1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
2D 1H-13C HSQC15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D HCCH-TOCSY15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D H(CCO)NH15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D CBCA(CO)NH15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D C(CO)NH15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D HNCACB15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D HBHA(CO)NH15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D 1H-15N NOESY15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1
3D 1H-13C NOESY15N_13C_HvGR-RBP1isotropic15N_13C_HvGr_RBP1_conditions_1

Software:

TOPSPIN v2.1, Bruker BioSpin - collection

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift indexing, Spectrum processing

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AFP52931 EMT31367

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