BMRB Entry 17232

Name: Solution structure of the PlyG catalytic domain
Published: 2012-07-25

Click here to enlarge.

PDB ID: 2l47
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17232
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:

Solution structure of the PlyG catalytic 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, 165 residues, 18555.006 Da.
ZN, non-polymer, 65.409 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: pBAD18

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PlyG: MEIQKKLVDPSKYGTKCPYT MKPKYITVHNTYNDAPAENE VSYMISNNNEVSFHIAVDDK KAIQGIPLERNAWACGDGNG SGNRQSISVEICYSKSGGDR YYKAEDNAVDVVRQLMSMYN IPIENVRTHQSWSGKYCPHR MLAEGRWGAFIQKVKNGNVA TTSPT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	530
15N chemical shifts	183
1H chemical shifts	1134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PlyG	1
2	ZINC	2

Entities:

Entity 1, PlyG 165 residues - 18555.006 Da.

1

MET

GLU

ILE

GLN

LYS

LEU

VAL

ASP

PRO

2

SER

LYS

TYR

GLY

THR

LYS

CYS

PRO

TYR

THR

3

MET

LYS

PRO

LYS

TYR

ILE

THR

VAL

HIS

ASN

4

THR

TYR

ASN

ASP

ALA

PRO

ALA

GLU

ASN

GLU

5

VAL

SER

TYR

MET

ILE

SER

ASN

GLU

6

VAL

SER

PHE

HIS

ILE

ALA

VAL

ASP

LYS

7

LYS

ALA

ILE

GLN

GLY

ILE

PRO

LEU

GLU

ARG

8

ASN

ALA

TRP

ALA

CYS

GLY

ASP

GLY

ASN

GLY

9

SER

GLY

ASN

ARG

GLN

SER

ILE

SER

VAL

GLU

10

ILE

CYS

TYR

SER

LYS

SER

GLY

ASP

ARG

11

TYR

LYS

ALA

GLU

ASP

ASN

ALA

VAL

ASP

12

VAL

ARG

GLN

LEU

MET

SER

MET

TYR

ASN

13

ILE

PRO

ILE

GLU

ASN

VAL

ARG

THR

HIS

GLN

14

SER

TRP

SER

GLY

LYS

TYR

CYS

PRO

HIS

ARG

15

MET

LEU

ALA

GLU

GLY

ARG

TRP

GLY

ALA

PHE

16

ILE

GLN

LYS

VAL

LYS

ASN

GLY

ASN

VAL

ALA

17

THR

SER

PRO

THR

Entity 2, ZINC - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: PlyG, [U-100% 13C; U-100% 15N], 1 mM; Bis-Tris, [U-99% 2H], 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 13 mM; pH: 6.0; pressure: 1 atm; temperature: 303 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	2L47
GB	AAM97149 ABA42708 ABA46392 ABA46449 ABA46501
REF	WP_001982889 YP_338149 YP_338200 YP_459981 YP_512326