BMRB Entry 17322

Name: High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH
Published: 2012-09-20

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PDB ID: 2l6r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17322
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH

Deposition date:

2010-11-24

Original release date:

2012-09-20

Authors:

Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva

Citation:

Citation: Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva. "Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage ." PLoS ONE 6, e26409-e26409 (2011).
PubMed: 22087227

Assembly members:

Assembly members:
gpW, polymer, 62 residues, 6989.108 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gpW: MVRQEELAAARAALHDLMTG KRVATVQKDGRRVEFTATSV SDLKKYIAELEVQTGMTQRR RG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	206
15N chemical shifts	62
1H chemical shifts	432

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	W protein of bacteriophage lambda	1

Entities:

Entity 1, W protein of bacteriophage lambda 62 residues - 6989.108 Da.

1

MET

VAL

ARG

GLN

GLU

LEU

ALA

2

ARG

ALA

LEU

HIS

ASP

LEU

MET

THR

GLY

3

LYS

ARG

VAL

ALA

THR

VAL

GLN

LYS

ASP

GLY

4

ARG

VAL

GLU

PHE

THR

ALA

THR

SER

VAL

5

SER

ASP

LEU

LYS

TYR

ILE

ALA

GLU

LEU

6

GLU

VAL

GLN

THR

GLY

MET

THR

GLN

ARG

7

ARG

GLY

Samples:

sample_1: gpW, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; glycine buffer 20 mM

sample_2: gpW, [U-13C; U-15N], 1 mM; D2O 100%; glycine buffer 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 3.5; pressure: 1 atm; temperature: 293.1 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
4D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

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

PIPP, Garrett - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	17321
PDB	1HYW 2L6Q 2L6R
DBJ	BAG76119 BAG77589 BAI23937 BAI29406 GAL55727
EMBL	CAP75664 CAQ31249 CAQ97648 CAQ98444 CAR11829
GB	AAA96535 AAG55981 AAN81624 AAZ89070 ABG69179
REF	NP_040582 WP_000198149 WP_000246867 WP_001571330 WP_001657975
SP	P68659 P68660
AlphaFold	P68659 P68660