BMRB Entry 30221

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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/BMR30221
MolProbity Validation Chart

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Title:
Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43
Deposition date:
2016-12-21
Original release date:
2017-08-16
Authors:
Damry, A.; Davey, J.; Goto, N.; Chica, R.
Citation:

Citation: Davey, J.; Damry, A.; Goto, N.; Chica, R.. "Rational design of proteins that exchange on functional timescales."  Nat. Chem. Biol. 13, 1280-1285 (2017).
PubMed: 29058725

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, 6289.934 Da.

Natural source:

Natural source:   Common Name: Streptococcus sp. GX7805   Taxonomy ID: 1325   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus Streptococcus sp. GX7805

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJ414

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTFKLIINGKTLKGETTTEA VDAATAEKVFKQYFNDNGID GEWTYDDATKTFTITE

Data typeCount
13C chemical shifts240
15N chemical shifts61
1H chemical shifts342

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 - 6289.934 Da.

1   METTHRPHELYSLEUILEILEASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRPHEASNASPASNGLYILEASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRILETHRGLU

Samples:

sample_1: EDTA 100 uM; protein (GB1), [U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM

sample_2: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM

sample_3: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 1 mM; sodium azide 0.02%; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz
  • Varian Inova 500 MHz

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