BMRB Entry 25575

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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/BMR25575
MolProbity Validation Chart

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Title:
Structure of SAP30L corepressor protein
Deposition date:
2015-04-23
Original release date:
2015-11-23
Authors:
Tossavainen, Helena; Permi, Perttu
Citation:

Citation: Laitaoja, Mikko; Tossavainen, Helena; Pihlajamaa, Tero; Valjakka, Jarkko; Viiri, Keijo; Lohi, Olli; Permi, Perttu; Janis, Janne. "Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function"  Protein Sci. 25, 572-586 (2016).
PubMed: 26609676

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 8120.513 Da.
ZINC ION, non-polymer, 65.409 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: pGEX-4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSYGQSCCLIEDGERCVRPA GNASFSKRVQKSISQKKLKL DIDKSVRHLYICDFHKNFIQ SVRNKRKRKT

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts64
1H chemical shifts484

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION2

Entities:

Entity 1, entity_1 70 residues - 8120.513 Da.

1   GLYSERTYRGLYGLNSERCYSCYSLEUILE
2   GLUASPGLYGLUARGCYSVALARGPROALA
3   GLYASNALASERPHESERLYSARGVALGLN
4   LYSSERILESERGLNLYSLYSLEULYSLEU
5   ASPILEASPLYSSERVALARGHISLEUTYR
6   ILECYSASPPHEHISLYSASNPHEILEGLN
7   SERVALARGASNLYSARGLYSARGLYSTHR

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.5 mM; ZINC ION 0.5 mM; BIS-TRIS 20 mM; sodium chloride 30 mM; sodium azide 0.04%; H2O 93%; D2O 7%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
(HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

VNMRJ, Agilent - collection, processing

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - minimization

NMR spectrometers:

  • Varian INOVA 800 MHz

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