BMRB Entry 17233

Name: Solution structure of the PlyG cell wall binding domain
Published: 2012-07-25

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PDB ID: 2l48
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17233
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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 structure of the PlyG cell wall binding domain

Deposition date:

2010-10-01

Original release date:

2012-07-25

Authors:

Volkman, B.; Dias, J.; Peterson, F.

Citation:

Citation: Dias, J.; Peterson, F.; Volkman, B.. "TBD" To be published ., .-..

Assembly members:

Assembly members:
PlyG, polymer, 85 residues, 9447.814 Da.

Natural source:

Natural source: Common Name: Bacillus phage Gamma Taxonomy ID: 347962 Superkingdom: viruses Kingdom: not available Genus/species: not available Bacillus phage Gamma

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PlyG: GSIQKVKNGNVATTSPTKQN IIQSGAFSPYETPDVMGALT SLKMTADFILQSDGLTYFIS KPTSDAQLKAMKEYLDRKGW WYEVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	376
15N chemical shifts	96
1H chemical shifts	634

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PlyG_1	1
2	PlyG_2	1

Entities:

Entity 1, PlyG_1 85 residues - 9447.814 Da.

The GS dipeptide, residues 149 and 150, are a cloning artifact.

1

GLY

SER

ILE

GLN

LYS

VAL

LYS

ASN

GLY

ASN

2

VAL

ALA

THR

SER

PRO

THR

LYS

GLN

ASN

3

ILE

GLN

SER

GLY

ALA

PHE

SER

PRO

TYR

4

GLU

THR

PRO

ASP

VAL

MET

GLY

ALA

LEU

THR

5

SER

LEU

LYS

MET

THR

ALA

ASP

PHE

ILE

LEU

6

GLN

SER

ASP

GLY

LEU

THR

TYR

PHE

ILE

SER

7

LYS

PRO

THR

SER

ASP

ALA

GLN

LEU

LYS

ALA

8

MET

LYS

GLU

TYR

LEU

ASP

ARG

LYS

GLY

TRP

9

TRP

TYR

GLU

VAL

LYS

Samples:

sample_1: PlyG, [U-100% 13C; U-100% 15N], 1.25 mM; Bis-Tris, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 13 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

Bruker DRX 600 MHz

PDB	2L48
GB	AAM97149 ABA42708 ABA46392 ABA46449 ABA46501
REF	WP_001982889 YP_338149 YP_338200 YP_459981 YP_512326