BMRB Entry 15408

Name: NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1
Published: 2008-08-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15408

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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:

NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1

Deposition date:

2007-07-29

Original release date:

2008-08-18

Authors:

Crowhurst, Karin; Mayo, Stephen

Citation:

Citation: Crowhurst, Karin; Mayo, Stephen. "NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1" Protein Eng. Des. Sel. 21, 577-587 (2008).
PubMed: 18586670

Assembly members:

Assembly members:
delta1.5, polymer, 57 residues, 6342 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
delta1.5: MTTFKLIINGKTLKGETTTE AVDAATAEKVLKQYINDNGI DGEWTYDDATKTWTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
heteronucl_T1_relaxation
- heteronuclear_T1_list
heteronucl_T2_relaxation
- heteronuclear_T2_list
H_exch_protection_factors
- H_exch_protection_factor_list

Data type	Count
13C chemical shifts	241
15N chemical shifts	61
1H chemical shifts	371
H exchange protection factors	55
T1 relaxation values	54
T2 relaxation values	55

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	delta1.5	1

Entities:

Entity 1, delta1.5 57 residues - 6342 Da.

1

MET

THR

PHE

LYS

LEU

ILE

ASN

GLY

2

LYS

THR

LEU

LYS

GLY

GLU

THR

GLU

3

ALA

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

4

LEU

LYS

GLN

TYR

ILE

ASN

ASP

ASN

GLY

ILE

5

ASP

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

6

LYS

THR

TRP

THR

VAL

THR

GLU

Samples:

sample_1: delta1.5, [U-13C; U-15N], 1.5 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%

sample_2: delta1.5, [U-13C; U-15N], 2.2 mM; sodium phosphate 50 mM; DSS 0.2 mM; D2O 100%

sample_3: delta1.5, [U-15N], 2.6 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%

sample_4: delta1.5, [U-15N; U-2H], 2.6 mM; sodium phosphate 50 mM; DSS 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 6; pressure: 1 atm; temperature: 298.15 K

sample_conditions_2: ionic strength: 0.3 M; pH*: 6.3; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCC-TOCSY-NNH	sample_1	isotropic	sample_conditions_1
3D CCC-TOCSY_NNH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D CLEANEX-PM	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
2D nz cross-correlation	sample_4	isotropic	sample_conditions_1
2D nxy cross-correlation	sample_4	isotropic	sample_conditions_1

Software:

NMRDraw v1995, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe v1995, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, peak picking

CurveFit v1998, Palmer III - data analysis

NMR spectrometers:

Varian INOVA 600 MHz