BMRB Entry 18455

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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/BMR18455
MolProbity Validation Chart

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Title:
Structure of the C-terminal domain from human REV1
Deposition date:
2012-05-09
Original release date:
2012-12-18
Authors:
Pozhidaeva, Alexandra; Pustovalova, Yulia; Bezsonova, Irina; Korzhnev, Dmitry
Citation:

Citation: Pozhidaeva, Alexandra; Pustovalova, Yulia; Bezsonova, Sanjay; Walker, Irina; Korzhnev, Graham. "NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase ."  Biochemistry 51, 5506-5520 (2012).
PubMed: 22691049

Assembly members:

Assembly members:
entity, polymer, 95 residues, 11011.758 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GNLAGAVEFNDVKTLLREWI TTISDPMEEDILQVVKYCTD LIEEKDLEKLDLVIKYMKRL MQQSVESVWNMAFDFILDNV QVVLQQTYGSTLKVT

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts98
1H chemical shifts646

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1REV1-CT1

Entities:

Entity 1, REV1-CT 95 residues - 11011.758 Da.

1   GLYASNLEUALAGLYALAVALGLUPHEASN
2   ASPVALLYSTHRLEULEUARGGLUTRPILE
3   THRTHRILESERASPPROMETGLUGLUASP
4   ILELEUGLNVALVALLYSTYRCYSTHRASP
5   LEUILEGLUGLULYSASPLEUGLULYSLEU
6   ASPLEUVALILELYSTYRMETLYSARGLEU
7   METGLNGLNSERVALGLUSERVALTRPASN
8   METALAPHEASPPHEILELEUASPASNVAL
9   GLNVALVALLEUGLNGLNTHRTYRGLYSER
10   THRLEULYSVALTHR

Samples:

sample_1: REV1-CT, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 0.25 mM; DTT 5 mM; sodium azide 0.05%; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

VNMRJ, Varian - collection

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 18432 18434
PDB
DBJ BAB21441
EMBL CAB38231 CAH93279
GB AAF06731 AAF18986 AAI30412 AAK43708 AAY24314
REF NP_001032961 NP_001126930 NP_057400 XP_001160264 XP_001363717
SP Q5R4N7 Q9UBZ9
AlphaFold Q5R4N7 Q9UBZ9

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