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Biological Magnetic Resonance Data Bank


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BMRB Entry 17579

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17579
MolProbity Validation Chart

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Title: H/ACA RNP protein Nhp2p   PubMed: 21708174

Deposition date: 2011-04-07 Original release date: 2011-06-30

Authors: Koo, Bon-Kyung; Park, Chin-Ju; Fernandez, Cesar; Chim, Nicholas; Ding, Yi; Chanfreau, Guillaume; Feigon, Juli

Citation: Koo, Bon-Kyung; Park, Chin-Ju; Fernandez, Cesar; Chim, Nicholas; Ding, Yi; Chanfreau, Guillaume; Feigon, Juli. "Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface."  J. Mol. Biol. 411, 927-942 (2011).

Assembly members:
Nhp2p, polymer, 121 residues, 13207.657 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: recombinant technology   Host organism: Saccharomyces cerevisiae

Entity Sequences (FASTA):
Nhp2p: SKKLNKKVLKTVKKASKAKN VKRGVKEVVKALRKGEKGLV VIAGDISPADVISHIPVLCE DHSVPYIFIPSKQDLGAAGA TKRPTSVVFIVPGSNKKKDG KNKEEEYKESFNEVVKEVQA L

Data sets:
Data typeCount
13C chemical shifts430
15N chemical shifts114
1H chemical shifts661

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Nhp2p1

Entities:

Entity 1, Nhp2p 121 residues - 13207.657 Da.

1   SERLYSLYSLEUASNLYSLYSVALLEULYS
2   THRVALLYSLYSALASERLYSALALYSASN
3   VALLYSARGGLYVALLYSGLUVALVALLYS
4   ALALEUARGLYSGLYGLULYSGLYLEUVAL
5   VALILEALAGLYASPILESERPROALAASP
6   VALILESERHISILEPROVALLEUCYSGLU
7   ASPHISSERVALPROTYRILEPHEILEPRO
8   SERLYSGLNASPLEUGLYALAALAGLYALA
9   THRLYSARGPROTHRSERVALVALPHEILE
10   VALPROGLYSERASNLYSLYSLYSASPGLY
11   LYSASNLYSGLUGLUGLUTYRLYSGLUSER
12   PHEASNGLUVALVALLYSGLUVALGLNALA
13   LEU

Samples:

13C_15N_sample: HEPES, [U-13C; U-15N], 20 mM; potassium chloride 200 mM; DTT 1 mM; D2O 100%

15N_sample: HEPES, [U-15N], 20 mM; potassium chloride 200 mM; DTT 1 mM; D2O 10%; H2O 90%

13C_15N_sample_2: HEPES, [U-13C; U-15N], 20 mM; potassium chloride 200 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACB13C_15N_sampleisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N_sampleisotropicsample_conditions_1
3D HNCO13C_15N_sampleisotropicsample_conditions_1
3D HBHA(CO)NH15N_sampleisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N_sampleisotropicsample_conditions_1
3D 1H-13C NOESY13C_15N_sample_2isotropicsample_conditions_1
3D 1H-15N NOESY15N_sampleisotropicsample_conditions_1
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
2D 1H-13C HSQC13C_15N_sampleisotropicsample_conditions_1
3D C(CO)NH13C_15N_sampleisotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17578
PDB
DBJ GAA22045
EMBL CAA40885 CAA67483 CAA98786 CAY79077
GB AHY74809 AJP37550 AJU57662 AJU58365 AJU59054
REF NP_010073
SP P32495
TPG DAA11656

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