BMRB Entry 10071

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10071
MolProbity Validation Chart

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Title:
Solution structure of RRM domain in RNA-binding protein NP_057951
Deposition date:
2006-12-25
Original release date:
2008-08-14
Authors:
He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation:

Citation: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.. "Solution structure of RRM domain in RNA-binding protein NP_057951"  .

Assembly members:

Assembly members:
RRM domain, polymer, 110 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P040223-76

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM domain: GSSGSSGMSLKLQASNVTNK NDPKSINSRVFIGNLNTALV KKSDVETIFSKYGRVAGCSV HKGYAFVQYSNERHARAAVL GENGRVLAGQTLDINMAGEP KPDRSGPSSG

Data sets:
Data typeCount
13C chemical shifts442
15N chemical shifts108
1H chemical shifts701

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RNA-binding protein Raly1

Entities:

Entity 1, RNA-binding protein Raly 110 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETSERLEU
2   LYSLEUGLNALASERASNVALTHRASNLYS
3   ASNASPPROLYSSERILEASNSERARGVAL
4   PHEILEGLYASNLEUASNTHRALALEUVAL
5   LYSLYSSERASPVALGLUTHRILEPHESER
6   LYSTYRGLYARGVALALAGLYCYSSERVAL
7   HISLYSGLYTYRALAPHEVALGLNTYRSER
8   ASNGLUARGHISALAARGALAALAVALLEU
9   GLYGLUASNGLYARGVALLEUALAGLYGLN
10   THRLEUASPILEASNMETALAGLYGLUPRO
11   LYSPROASPARGSERGLYPROSERSERGLY

Samples:

sample_1: RRM domain, [U-13C; U-15N], 0.8 mM; d-Tris-HCl(pH 7.0) 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1not availablecondition_1
3D 13C-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.863, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAD96635 BAF83743 BAF83768 BAG61653 BAI46166
GB AAC28898 AAF04487 AAI03754 AAI05019 ACA53514
REF NP_001267354 NP_031393 NP_057951 XP_001102633 XP_002747313
SP Q9UKM9
AlphaFold Q9UKM9

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