BMRB Entry 30088

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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/BMR30088
MolProbity Validation Chart

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Title:
Solid-state MAS NMR structure of beta 1 domain of protein G (GB1)
Deposition date:
2016-05-13
Original release date:
2016-08-08
Authors:
Andreas, L.; Jaudzems, K.; Stanek, J.; Lalli, D.; Bertarello, A.; Le Marchand, T.; Cala-De Paepe, D.; Kotelovica, S.; Akopjana, I.; Knott, B.; Wegner, S.; Engelke, F.; Lesage, A.; Emsley, L.; Tars, K.; Herrmann, T.; Pintacuda, G.
Citation:

Citation: Andreas, Loren; Jaudzems, Kristaps; Stanek, Jan; Lalli, Daniela; Bertarello, Andrea; Marchand, Tanguy; Paepe, Diane; Kotelovica, Svetlana; Akopjana, Inara; Knott, Benno; Wegner, Sebastian; Engelke, Frank; Lesage, Anne; Emsley, Lyndon; Tars, Kaspars; Herrmann, Torsten; Pintacuda, Guido. "Structure of fully protonated proteins by proton-detected magic-angle spinning NMR"  Proc. Natl. Acad. Sci. U. S. A. 113, 9187-9192 (2016).
PubMed: 27489348

Assembly members:

Assembly members:
Immunoglobulin G-binding protein G, polymer, 56 residues, 6228.809 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 119602   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus Streptococcus dysgalactiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Immunoglobulin G-binding protein G: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts65
1H chemical shifts360

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 56 residues - 6228.809 Da.

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: B1 domain of Immunoglobulin G-Binding protein G, [U-99% 13C; U-99% 15N], 800 ± 300 mg/mL; isopropyl alcohol 22.5 ± 5 %; methyl-2,4-pentane diol 45 ± 5 %; sodium phosphate 12.5 ± 5 mM

sample_conditions_1: ionic strength: 12.5 mM; pH: 5.6; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
(H)NCAHsample_1isotropicsample_conditions_1
(H)CANHsample_1isotropicsample_conditions_1
(H)(CO)CA(CO)NHsample_1isotropicsample_conditions_1
(H)(CA)CB(CA)NHsample_1isotropicsample_conditions_1
(H)N(CA)(CO)NHsample_1isotropicsample_conditions_1
(H)N(CO)(CA)NHsample_1isotropicsample_conditions_1
(H)CCH-TOCSYsample_1isotropicsample_conditions_1
(H)NHH-RFDRsample_1isotropicsample_conditions_1
(H)CHH-RFDRsample_1isotropicsample_conditions_1
H(H)CH-RFDR-aromatic13Csample_1isotropicsample_conditions_1

Software:

CANDID v2.6.0, Herrmann, Guntert and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 1000 MHz

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