BMRB Entry 16256

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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/BMR16256
MolProbity Validation Chart

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Title:
Drosha RNA Binding Domain
Deposition date:
2009-04-13
Original release date:
2010-04-01
Authors:
Mueller, Geoffrey; Miller, Matthew; Ghosh, Mahua; DeRose, Eugene; London, Robert; Hall, Traci
Citation:

Citation: Mueller, Geoffrey; Miller, Matthew; DeRose, Eugene; Ghosh, Mahua; London, Robert; Hall, Traci. "Solution structure of the Drosha double-stranded RNA-binding domain"  Silence 1, 2-. (2010).
PubMed: 20226070

Assembly members:

Assembly members:
binding domain, polymer, 90 residues, 8761.069 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
binding domain: GSPQFMLNQDWNDPKSQLQQ CCLTLRTEGKEPDIPLYKTL QTVGPSHARTYTVAVYFKGE RIGCGKGPSIQQAEMGAAMD ALEKYNFPQM

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts68
1H chemical shifts473

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1binding domain1

Entities:

Entity 1, binding domain 90 residues - 8761.069 Da.

1   GLYSERPROGLNPHEMETLEUASNGLNASP
2   TRPASNASPPROLYSSERGLNLEUGLNGLN
3   CYSCYSLEUTHRLEUARGTHRGLUGLYLYS
4   GLUPROASPILEPROLEUTYRLYSTHRLEU
5   GLNTHRVALGLYPROSERHISALAARGTHR
6   TYRTHRVALALAVALTYRPHELYSGLYGLU
7   ARGILEGLYCYSGLYLYSGLYPROSERILE
8   GLNGLNALAGLUMETGLYALAALAMETASP
9   ALALEUGLULYSTYRASNPHEPROGLNMET

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 – 2 mM; TRIS, [U-2H], 25 mM; potassium chloride 100 mM; DTT, [U-2H], 1 mM; EDTA 1 mM; DSS 10 uM

sample_conditions_1: ionic strength: 0.125 M; pH: 7.0; pressure: 1.0 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
CN-4D simultaneous NOESYsample_1isotropicsample_conditions_1
HB-HE/HD-aromaticsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA91511 BAB22917 BAE25729 BAE28629 BAO93839
EMBL CAG32380 CBN82191 CDQ74551
GB AAD29637 AAF80558 AAH41162 AAH50057 AAH55696
REF NP_001006379 NP_001093882 NP_001101125 NP_001103942 NP_001107152
SP Q5HZJ0 Q9NRR4
TPG DAA17862 DAA17863
AlphaFold Q5HZJ0 Q9NRR4

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