BMRB Entry 17841

Name: GB98-T25I,L20A
Published: 2012-02-28

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PDB ID: 2lhe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17841
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

GB98-T25I,L20A

Deposition date:

2011-08-08

Original release date:

2012-02-28

Authors:

He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John

Citation:

Citation: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John. "Mutational tipping points for switching protein folds and functions" Structure 20, 283-291 (2012).
PubMed: 22325777

Assembly members:

Assembly members:
entity, polymer, 56 residues, 6375.410 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: PPAL8

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: TTYKLILNLKQAKEEAIKEA VDAGIAEKYFKLIANAKTVE GVWTYKDEIKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	238
15N chemical shifts	59
1H chemical shifts	359

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GB98-T25I,L20A	1

Entities:

Entity 1, GB98-T25I,L20A 56 residues - 6375.410 Da.

1

THR

TYR

LYS

LEU

ILE

LEU

ASN

LEU

LYS

2

GLN

ALA

LYS

GLU

ALA

ILE

LYS

GLU

ALA

3

VAL

ASP

ALA

GLY

ILE

ALA

GLU

LYS

TYR

PHE

4

LYS

LEU

ILE

ALA

ASN

ALA

LYS

THR

VAL

GLU

5

GLY

VAL

TRP

THR

TYR

LYS

ASP

GLU

ILE

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: GB98-T25I,L20A, [U-100% 13C; U-100% 15N], 0.1 – 0.3 mM; potassium phosphate 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - structure determination

TOPSPIN, Bruker Biospin - data collection

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing display

SPARKY, Goddard - data analysis

CSI, Wishart, D.S. and B.D. Sykes. - secondary structure prediction

TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints determination

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - protein structure quality check

NOEID, Lisa Parsons - generate noe peak lists

NMR spectrometers:

Bruker DMX 600 MHz