BMRB Entry 34329

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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/BMR34329
MolProbity Validation Chart

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Title:
NMR structure of the third TPR domain of the human SPAG1 protein
Deposition date:
2018-11-13
Original release date:
2019-05-31
Authors:
Chagot, M.; Quinternet, M.
Citation:

Citation: Chagot, M.; Dos Santos Morais, R.; Dermouche, S.; Lefebvre, D.; Manival, X.; Chipot, C.; Dehez, F.; Quinternet, M.. "Binding properties of the quaternary assembly protein SPAG1."  Biochem. J. 476, 1679-1694 (2019).
PubMed: 31118266

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14381.639 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMTFKALKEEGNQCVNDK NYKDALSKYSECLKINNKEC AIYTNRALCYLKLCQFEEAK QDCDQALQLADGNVKAFYRR ALAHKGLKNYQKSLIDLNKV ILLDPSIIEAKMELEEVTRL LNLKD

Data sets:
Data typeCount
13C chemical shifts555
15N chemical shifts143
1H chemical shifts940

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14381.639 Da.

1   GLYPROHISMETTHRPHELYSALALEULYS
2   GLUGLUGLYASNGLNCYSVALASNASPLYS
3   ASNTYRLYSASPALALEUSERLYSTYRSER
4   GLUCYSLEULYSILEASNASNLYSGLUCYS
5   ALAILETYRTHRASNARGALALEUCYSTYR
6   LEULYSLEUCYSGLNPHEGLUGLUALALYS
7   GLNASPCYSASPGLNALALEUGLNLEUALA
8   ASPGLYASNVALLYSALAPHETYRARGARG
9   ALALEUALAHISLYSGLYLEULYSASNTYR
10   GLNLYSSERLEUILEASPLEUASNLYSVAL
11   ILELEULEUASPPROSERILEILEGLUALA
12   LYSMETGLULEUGLUGLUVALTHRARGLEU
13   LEUASNLEULYSASP

Samples:

sample_1: SPAG1-TPR3, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin v3.2, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS, Cornilescu, Delaglio and Bax - structure calculation

PREDITOR, Berjanskii MV, Neal S, Wishart DS. - structure calculation

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

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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