BMRB Entry 30691

Name: NMR Structure of C-terminal Domain of phi29 ATPase
Published: 2020-09-28

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PDB ID: 6v1w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30691
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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:

NMR Structure of C-terminal Domain of phi29 ATPase

Deposition date:

2019-11-21

Original release date:

2020-09-28

Authors:

Mahler, B.; Mao, H.; Morais, M.

Citation:

Citation: Woodson, Michael; Pajak, Joshua; Mahler, Bryon; Zhao, Wei; Zhang, Wei; Arya, Gaurav; White, Mark; Jardine, Paul; Morais, Marc. "A viral genome packaging motor transitions between cyclic and helical symmetry to translocate dsDNA" Sci. Adv. 7, eabc1955-eabc1955 (2021).
PubMed: 33962953

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 14195.173 Da.

Natural source:

Natural source: Common Name: Bacillus phage phi29 Taxonomy ID: 10756 Superkingdom: Viruses Kingdom: not available Genus/species: Salasvirus Bacillus phage phi29

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MFIGDSQVFIEKRSKDSKFV FSIVYNGFTLGVWVDVNQGL MYIDTAHDPSTKNVYTLTTD DLNENMMLITNYKNNYHLRK LASAFMNGYLRFDNQVIRNI AYELFRKMRIQLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	441
15N chemical shifts	103
1H chemical shifts	641

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 119 residues - 14195.173 Da.

1

MET

PHE

ILE

GLY

ASP

SER

GLN

VAL

PHE

ILE

2

GLU

LYS

ARG

SER

LYS

ASP

SER

LYS

PHE

VAL

3

PHE

SER

ILE

VAL

TYR

ASN

GLY

PHE

THR

LEU

4

GLY

VAL

TRP

VAL

ASP

VAL

ASN

GLN

GLY

LEU

5

MET

TYR

ILE

ASP

THR

ALA

HIS

ASP

PRO

SER

6

THR

LYS

ASN

VAL

TYR

THR

LEU

THR

ASP

7

ASP

LEU

ASN

GLU

ASN

MET

LEU

ILE

THR

8

ASN

TYR

LYS

ASN

TYR

HIS

LEU

ARG

LYS

9

LEU

ALA

SER

ALA

PHE

MET

ASN

GLY

TYR

LEU

10

ARG

PHE

ASP

ASN

GLN

VAL

ILE

ARG

ASN

ILE

11

ALA

TYR

GLU

LEU

PHE

ARG

LYS

MET

ARG

ILE

12

GLN

LEU

GLU

HIS

Name	Sample	Sample state	Sample conditions
3D 15N NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 13C-edited NOESY-HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 13C-editied NOESY-HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HSQC-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
HD-exchange	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 30691

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: