BMRB Entry 34586

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34586
MolProbity Validation Chart

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Title:
NMR structure of an optimized version of the first TPR domain of the human SPAG1 protein
Deposition date:
2020-12-29
Original release date:
2021-03-26
Authors:
Dermouche, S.; Chagot, M.; Quinternet, M.
Citation:

Citation: Dermouche, S.; Chagot, M.; Manival, X.; Quinternet, M.. "Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties"  Biochemistry 60, 2349-2363 (2021).
PubMed: 33739091

Assembly members:

Assembly members:
entity_1, polymer, 126 residues, 14527.270 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: GPHMDYLATREKEKGNEAFN SGDYEEAVMYYTRSISALPT VVAYNNRAQAYIKLQNWNSA EQDCEKVLELEPGNVKALLR RATAYKHQNKLREAREDLKK VLKVEPDNDLAKKTLSEVER DLKNSE

Data sets:
Data typeCount
13C chemical shifts551
15N chemical shifts142
1H chemical shifts915

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 126 residues - 14527.270 Da.

1   GLYPROHISMETASPTYRLEUALATHRARG
2   GLULYSGLULYSGLYASNGLUALAPHEASN
3   SERGLYASPTYRGLUGLUALAVALMETTYR
4   TYRTHRARGSERILESERALALEUPROTHR
5   VALVALALATYRASNASNARGALAGLNALA
6   TYRILELYSLEUGLNASNTRPASNSERALA
7   GLUGLNASPCYSGLULYSVALLEUGLULEU
8   GLUPROGLYASNVALLYSALALEULEUARG
9   ARGALATHRALATYRLYSHISGLNASNLYS
10   LEUARGGLUALAARGGLUASPLEULYSLYS
11   VALLEULYSVALGLUPROASPASNASPLEU
12   ALALYSLYSTHRLEUSERGLUVALGLUARG
13   ASPLEULYSASNSERGLU

Samples:

sample_1: SPAG1-TPR1, [U-13C; U-15N], 1 ± 0.1 mM; NaPi 10 mM; NaCl 150 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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