BMRB Entry 17839

Name: Ga98 solution structure
Published: 2012-02-28

Click here to enlarge.

PDB ID: 2lhc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17839
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Ga98 solution structure

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:
Ga98, polymer, 56 residues, 6355.419 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):
Ga98: TTYKLILNLKQAKEEAIKEL VDAGTAEKYFKLIANAKTVE GVWTLKDEIKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	213
15N chemical shifts	56
1H chemical shifts	334

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ga98	1

Entities:

Entity 1, Ga98 56 residues - 6355.419 Da.

1

THR

TYR

LYS

LEU

ILE

LEU

ASN

LEU

LYS

2

GLN

ALA

LYS

GLU

ALA

ILE

LYS

GLU

LEU

3

VAL

ASP

ALA

GLY

THR

ALA

GLU

LYS

TYR

PHE

4

LYS

LEU

ILE

ALA

ASN

ALA

LYS

THR

VAL

GLU

5

GLY

VAL

TRP

THR

LEU

LYS

ASP

GLU

ILE

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: Ga98, [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 vcns_solve 1.21, Brunger A. T. et.al. - refinement, structure solution

SPARKY, Goddard et al - data analysis

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

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

CSI v2.0, David Wishart, Brian Sykes - secondary structure prediction

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

Molmol, Koradi, Billeter and Wuthrich - structure display

TOPSPIN v2.0, Bruker Biospin - data collection

NOEID v1.20, Lisa Parsons - make noesy peak lists and CNS input tables

NMR spectrometers:

Bruker DMX 600 MHz