BMRB Entry 30223

Name: Solution NMR-derived model of the minor species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)
Published: 2017-08-16

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PDB ID: 5ucf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30223
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR-derived model of the minor species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)

Deposition date:

2016-12-22

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, 6233.827 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: MTFKAIINGKTLKGETTTEA VDAATAEKVFKQYFNDNGLD GEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	230
15N chemical shifts	61
1H chemical shifts	329

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 56 residues - 6233.827 Da.

1

MET

THR

PHE

LYS

ALA

ILE

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

PHE

ASN

ASP

ASN

GLY

LEU

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: EDTA 100 uM; protein (GB1), [U-98% 15N], 200 uM; sodium azide 0.02%; sodium phosphate 10 mM

sample_2: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 200 uM; sodium azide 0.02%; sodium phosphate 10 mM

sample_3: EDTA 100 uM; protein (GB1), [U-99% 13C; U-98% 15N], 200 uM; 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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_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

NMR spectrometers:

Bruker AVANCE III HD 600 MHz

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