BMRB Entry 25986

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25986
MolProbity Validation Chart

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Title:
Solution structure of the F87M/L110M variant of transthyretin in the monomeric state
Deposition date:
2016-03-09
Original release date:
2017-02-16
Authors:
Kim, Jin Hae; Oroz, Javier; Zweckstetter, Markus
Citation:

Citation: Oroz, Javier; Kim, Jin Hae; Chang, Bliss; Zweckstetter, Markus. "Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90"  Nat. Struct. Mol. Biol. 24, 407-413 (2017).
PubMed: 28218749

Assembly members:

Assembly members:
M-TTR, polymer, 127 residues, 13779.540 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: pQE

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M-TTR: GPTGTGESKCPLMVKVLDAV RGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPMHEHAEVVFTANDS GPRRYTIAAMLSPYSYSTTA VVTNPKE

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts102
1H chemical shifts706

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1transthyretin1

Entities:

Entity 1, transthyretin 127 residues - 13779.540 Da.

1   GLYPROTHRGLYTHRGLYGLUSERLYSCYS
2   PROLEUMETVALLYSVALLEUASPALAVAL
3   ARGGLYSERPROALAILEASNVALALAVAL
4   HISVALPHEARGLYSALAALAASPASPTHR
5   TRPGLUPROPHEALASERGLYLYSTHRSER
6   GLUSERGLYGLULEUHISGLYLEUTHRTHR
7   GLUGLUGLUPHEVALGLUGLYILETYRLYS
8   VALGLUILEASPTHRLYSSERTYRTRPLYS
9   ALALEUGLYILESERPROMETHISGLUHIS
10   ALAGLUVALVALPHETHRALAASNASPSER
11   GLYPROARGARGTYRTHRILEALAALAMET
12   LEUSERPROTYRSERTYRSERTHRTHRALA
13   VALVALTHRASNPROLYSGLU

Samples:

sample_1: M-TTR, [U-13C; U-15N], 0.3 – 0.7 mM; MES 50 mM; sodium chloride 100 mM; DTT 5 mM; DSS 0.1 mM; H2O 90%; D2O, [U-2H], 10%

sample_D2O: M-TTR, [U-13C; U-15N], 0.7 mM; MES 50 mM; sodium chloride 100 mM; DTT 5 mM; DSS 0.1 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 500 bar; temperature: 298 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCsample_D2Oisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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