BMRB Entry 17835

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17835
MolProbity Validation Chart

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Title:
NOT AVAILABLE
Deposition date:
2011-08-06
Original release date:
2012-04-30
Authors:
Cui, G.; Botuyan, M.V.; Mer, G.
Citation:

Citation: Cui, Gaofeng; Botuyan, Maria Victoria; Mer, Georges. "(1)H, (15)N and (13)C resonance assignments for the three LOTUS RNA binding domains of Tudor domain-containing protein TDRD7."  Biomol. NMR Assignments 7, 79-83 (2013).
PubMed: 22481467

Assembly members:

Assembly members:
TDRD7, polymer, 78 residues, 8681.178 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TDRD7: GHMLEADLVSKMLRAVLQSH KNGIVLPRLQGEYRSLTGDW IPFKQLGYPTLEAYLRSVPA VVRIEASRSGEIVCYAVA

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts84
1H chemical shifts577

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1TDRD71

Entities:

Entity 1, TDRD7 78 residues - 8681.178 Da.

1   GLYHISMETLEUGLUALAASPLEUVALSER
2   LYSMETLEUARGALAVALLEUGLNSERHIS
3   LYSASNGLYILEVALLEUPROARGLEUGLN
4   GLYGLUTYRARGSERLEUTHRGLYASPTRP
5   ILEPROPHELYSGLNLEUGLYTYRPROTHR
6   LEUGLUALATYRLEUARGSERVALPROALA
7   VALVALARGILEGLUALASERARGSERGLY
8   GLUILEVALCYSTYRALAVALALA

Samples:

sample_1: TDRD7, [U-100% 15N], 1.5 mM; sodium acetate 50 mM; H2O 90%; D2O 10%

sample_2: TDRD7, [U-100% 13C; U-100% 15N], 1.5 mM; sodium acetate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 4.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

SANE, Duggan, Legge, Dyson & Wright - chemical shift assignment

NMRView, Johnson, One Moon Scientific - processing

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAA82968 BAE36321
GB AAH29689 AAH90066 EDL02384 EDL98827
REF NP_001277404 NP_620226 NP_666254 XP_004581240 XP_006238169
SP Q8K1H1 Q9R1R4
AlphaFold Q8K1H1 Q9R1R4

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