BMRB Entry 50550

Name: 13C and 15N Chemical Shift Assignments for the Spherical Assembly of the Rous Sarcoma Virus Capsid Protein
Published: 2021-08-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50550

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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:

13C and 15N Chemical Shift Assignments for the Spherical Assembly of the Rous Sarcoma Virus Capsid Protein

Deposition date:

2020-11-07

Original release date:

2021-08-17

Authors:

Qiao, Xin; Thames, Tyrone; Bryer, Alexander; Janicki, Kaylie; Weed, Ryan; Jeon, Jaekyun; Hung, Ivan; Gorkov, Peter; Gan, Zhehong; Perilla, Juan; Chen, Bo

Citation:

Citation: Thames, Tyrone; Bryer, Alexander; Qiao, Xin; Jeon, Jaekyun; Weed, Ryan; Janicki, Kaylie; Hu, Bingwen; Gor'kov, Peter; Hung, Ivan; Gan, Zhehong; Perilla, Juan; Chen, Bo. "Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch" J. Phys. Chem. Lett. 12, 7768-7776 (2021).
PubMed: 34374542

Assembly members:

Assembly members:
entity_1, polymer, 237 residues, 25530 Da.

Natural source:

Natural source: Common Name: Rous sarcoma virus Taxonomy ID: 11886 Superkingdom: Viruses Kingdom: not available Genus/species: Alpharetrovirus Rous sarcoma virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PVVIKTEGPAWTPLEPKLIT RLADTVRTKGLRSPITMAEV EALMSSPLLPHDVTNLMRVI LGPAPYALWMDAWGVQLQTV IAAATRDPRHPANGQGRGER TNLNRLKGLADGMVGNPQGQ AALLRPGELVAITASALQAF REVARLAEPAGPWADIMQGP SESFVDFANRLIKAVEGSDL PPSARAPVIVDCFRQKSQPD IQQLIRTAPSTLTTPGEIIK YVLDRQKTAPLTDQGIA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	982
15N chemical shifts	219

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rous Sarcoma Virus Capsid Protein, Monomer 1	1
2	Rous Sarcoma Virus Capsid Protein, Monomer 2	1
3	Rous Sarcoma Virus Capsid Protein, Monomer 3	1
4	Rous Sarcoma Virus Capsid Protein, Monomer 4	1
5	Rous Sarcoma Virus Capsid Protein, Monomer 5	1

Entities:

Entity 1, Rous Sarcoma Virus Capsid Protein, Monomer 1 237 residues - 25530 Da.

1

PRO

VAL

ILE

LYS

THR

GLU

GLY

PRO

ALA

2

TRP

THR

PRO

LEU

GLU

PRO

LYS

LEU

ILE

THR

3

ARG

LEU

ALA

ASP

THR

VAL

ARG

THR

LYS

GLY

4

LEU

ARG

SER

PRO

ILE

THR

MET

ALA

GLU

VAL

5

GLU

ALA

LEU

MET

SER

PRO

LEU

PRO

6

HIS

ASP

VAL

THR

ASN

LEU

MET

ARG

VAL

ILE

7

LEU

GLY

PRO

ALA

PRO

TYR

ALA

LEU

TRP

MET

8

ASP

ALA

TRP

GLY

VAL

GLN

LEU

GLN

THR

VAL

9

ILE

ALA

THR

ARG

ASP

PRO

ARG

HIS

10

PRO

ALA

ASN

GLY

GLN

GLY

ARG

GLY

GLU

ARG

11

THR

ASN

LEU

ASN

ARG

LEU

LYS

GLY

LEU

ALA

12

ASP

GLY

MET

VAL

GLY

ASN

PRO

GLN

GLY

GLN

13

ALA

LEU

ARG

PRO

GLY

GLU

LEU

VAL

14

ALA

ILE

THR

ALA

SER

ALA

LEU

GLN

ALA

PHE

15

ARG

GLU

VAL

ALA

ARG

LEU

ALA

GLU

PRO

ALA

16

GLY

PRO

TRP

ALA

ASP

ILE

MET

GLN

GLY

PRO

17

SER

GLU

SER

PHE

VAL

ASP

PHE

ALA

ASN

ARG

18

LEU

ILE

LYS

ALA

VAL

GLU

GLY

SER

ASP

LEU

19

PRO

SER

ALA

ARG

ALA

PRO

VAL

ILE

VAL

20

ASP

CYS

PHE

ARG

GLN

LYS

SER

GLN

PRO

ASP

21

ILE

GLN

LEU

ILE

ARG

THR

ALA

PRO

SER

22

THR

LEU

THR

PRO

GLY

GLU

ILE

LYS

23

TYR

VAL

LEU

ASP

ARG

GLN

LYS

THR

ALA

PRO

24

LEU

THR

ASP

GLN

GLY

ILE

ALA

Samples:

sample_1: Capsid Protein, [U-100% 13C; U-100% 15N], 3 mg/mL; sodium phosphate 500 mM

sample_conditions_1: pH: 8.0; temperature: 277 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 13C-13C DARR	sample_1	isotropic	sample_conditions_1
2D 13C/13C TOBSY	sample_1	isotropic	sample_conditions_1
2D NCACX	sample_1	isotropic	sample_conditions_1
2D NCOCX	sample_1	isotropic	sample_conditions_1
3D NCACX	sample_1	isotropic	sample_conditions_1
3D NCOCX	sample_1	isotropic	sample_conditions_1

Software:

VNMRj v4.0 - collection

NMRPipe - processing

NMRFAM-SPARKY v1.470 - peak picking

mcassign2 - chemical shift assignment

NMR spectrometers:

Agilent DDR2 600 MHz
Brucker Avance 600 MHz
Brucker Avance 900 MHz