BMRB Entry 34248

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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/BMR34248
MolProbity Validation Chart

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Title:
NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)
Deposition date:
2018-03-16
Original release date:
2018-09-14
Authors:
Michel, E.; Schuetz, S.; Damberger, F.; Allain, F.; Panse, V.
Citation:

Citation: Schutz, S.; Michel, E.; Damberger, F.; Oplova, M.; Pena, C.; Leitner, A.; Aebersold, R.; Allain, F.; Panse, V.. "Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2."  Nat. Commun. 9, 3669-3669 (2018).
PubMed: 30201955

Assembly members:

Assembly members:
entity_1, polymer, 156 residues, 17938.062 Da.
entity_2, polymer, 26 residues, 2903.303 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGSHMSTQYIDETAFVQAEQ GKTNLMFSDEKQQARFELGV SMVIYKWDALDVAVENSWGG PDSAEKRDWITGIVVDLFKN EKVVDAALIEETLLYAMIDE FETNVEDDSALPIAVEVINI YNDCFNLNYNKVEKLYLEWQ EKQRTKKSKRVVHIEG
entity_2: SGSQHMRPRFNRENKVSPAD AAKKAL

Data sets:
Data typeCount
13C chemical shifts638
15N chemical shifts202
1H chemical shifts1294

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 156 residues - 17938.062 Da.

1   SERGLYSERHISMETSERTHRGLNTYRILE
2   ASPGLUTHRALAPHEVALGLNALAGLUGLN
3   GLYLYSTHRASNLEUMETPHESERASPGLU
4   LYSGLNGLNALAARGPHEGLULEUGLYVAL
5   SERMETVALILETYRLYSTRPASPALALEU
6   ASPVALALAVALGLUASNSERTRPGLYGLY
7   PROASPSERALAGLULYSARGASPTRPILE
8   THRGLYILEVALVALASPLEUPHELYSASN
9   GLULYSVALVALASPALAALALEUILEGLU
10   GLUTHRLEULEUTYRALAMETILEASPGLU
11   PHEGLUTHRASNVALGLUASPASPSERALA
12   LEUPROILEALAVALGLUVALILEASNILE
13   TYRASNASPCYSPHEASNLEUASNTYRASN
14   LYSVALGLULYSLEUTYRLEUGLUTRPGLN
15   GLULYSGLNARGTHRLYSLYSSERLYSARG
16   VALVALHISILEGLUGLY

Entity 2, entity_2 26 residues - 2903.303 Da.

1   SERGLYSERGLNHISMETARGPROARGPHE
2   ASNARGGLUASNLYSVALSERPROALAASP
3   ALAALALYSLYSALALEU

Samples:

sample_1: Tsr2(1-152), [U-13C; U-15N], 0.5 mM; S26A(100-119) 0.5 mM; sodium phosphate 20 mM; DTT, [U-2H], 1 mM; EDTA 10 uM

sample_2: Tsr2(1-152) 0.5 mM; S26A(100-119), [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; DTT, [U-2H], 1 mM; EDTA 10 uM

sample_conditions_1: ionic strength: 41 mM; pH: 7; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz
  • 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