BMRB Entry 51391

Name: NMR Evidence for the Conformational Change of Phage Protein gVp Upon Binding to ssDNA
Published: 2022-07-05

Click here to enlarge.

PDB ID: 8acz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51391
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:

NMR Evidence for the Conformational Change of Phage Protein gVp Upon Binding to ssDNA

Deposition date:

2022-04-07

Original release date:

2022-07-05

Authors:

Kedem, Smadar; Hassid, Roni Rene; Shamir, Yoav; Goldbourt, Amir

Citation:

Citation: Kedem, Smadar; Hassid, Roni Rene; Shamir, Yoav; Goldbourt, Amir. "Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR" Viruses 14, 1264-1264 (2022).
PubMed: 35746735

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, Formula weight is not available

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: pET-30b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIKVEIKPSQAQFTTRSGVS RQGKPYSLNEQLCYVDLGNE YPVLVKITLDEGQPAYAPGL YTVHLSSFKVGQFGSLMIDR LRLVPAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gVp	1

Entities:

Entity 1, gVp 87 residues - Formula weight is not available

1

MET

ILE

LYS

VAL

GLU

ILE

LYS

PRO

SER

GLN

2

ALA

GLN

PHE

THR

ARG

SER

GLY

VAL

SER

3

ARG

GLN

GLY

LYS

PRO

TYR

SER

LEU

ASN

GLU

4

GLN

LEU

CYS

TYR

VAL

ASP

LEU

GLY

ASN

GLU

5

TYR

PRO

VAL

LEU

VAL

LYS

ILE

THR

LEU

ASP

6

GLU

GLY

GLN

PRO

ALA

TYR

ALA

PRO

GLY

LEU

7

TYR

THR

VAL

HIS

LEU

SER

PHE

LYS

VAL

8

GLY

GLN

PHE

GLY

SER

LEU

MET

ILE

ASP

ARG

9

LEU

ARG

LEU

VAL

PRO

ALA

LYS

Samples:

sample_1: gVp from fd bacteriophage, [U-100% 13C; U-100% 15N], 200 ± 50 g/L; NaCl 200 mM; EDTA 1 mM; Tris-HCl 10 mM

sample_2: gVp from fd bacteriophage, [1,3-13C]-glycerol, 200 ± 50 g/L; NaCl 200 mM; EDTA 1 mM; Tris-HCl 10 mM

sample_conditions_1: pH: 7.4; temperature: 263 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DARR5	sample_1	isotropic	sample_conditions_1
2D DARR15	sample_1	isotropic	sample_conditions_1
2D DARR100	sample_1	isotropic	sample_conditions_1
2D DARR250	sample_1	isotropic	sample_conditions_1
2D RFDR6	sample_1	isotropic	sample_conditions_1
2D INADEQUATE	sample_1	isotropic	sample_conditions_1
3D NCOCX25	sample_1	isotropic	sample_conditions_1
3D NCACX25	sample_1	isotropic	sample_conditions_1
2D DARR5	sample_2	isotropic	sample_conditions_1
2D DARR15	sample_2	isotropic	sample_conditions_1
2D DARR100	sample_2	isotropic	sample_conditions_1
2D DARR300	sample_2	isotropic	sample_conditions_1
2D NCA	sample_2	isotropic	sample_conditions_1
2D NCO	sample_2	isotropic	sample_conditions_1
3D NCOCX100	sample_2	isotropic	sample_conditions_1
3D NCACX100	sample_2	isotropic	sample_conditions_1
2D CORD150	sample_2	isotropic	sample_conditions_1
2D CORD300	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe vv9.3 - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz