BMRB Entry 34116

Name: Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein
Published: 2017-04-20

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PDB ID: 5nhq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34116
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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:

Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein

Deposition date:

2017-03-22

Original release date:

2017-04-20

Authors:

Coric, P.; Saribas, A.; Abou-Gharbia, M.; Childers, W.; Condra, J.; White, M.; Safak, M.; Bouaziz, S.

Citation:

Citation: Coric, P.; Saribas, A.; Abou-Gharbia, M.; Childers, W.; Condra, J.; White, M.; Safak, M.; Bouaziz, S.; Coric, P.; Saribas, A.; Abou-Gharbia, M.; Childers, W.; White, M.; Bouaziz, S.; Safak, M.. "Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein." J. Cell. Biochem. 118, 3268-3280 (2017).
PubMed: 28295503

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, 8096.414 Da.

Natural source:

Natural source: Common Name: JCPyV Taxonomy ID: 10632 Superkingdom: Viruses Kingdom: not available Genus/species: Betapolyomavirus JCPyV

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVLRQLSRKASVKVSKTWSG TKKRAQRILIFLLEFLLDFC TGEDSVDGKKRQRHSGLTEQ TYSALPEPKAT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	457

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 71 residues - 8096.414 Da.

1

MET

VAL

LEU

ARG

GLN

LEU

SER

ARG

LYS

ALA

2

SER

VAL

LYS

VAL

SER

LYS

THR

TRP

SER

GLY

3

THR

LYS

ARG

ALA

GLN

ARG

ILE

LEU

ILE

4

PHE

LEU

GLU

PHE

LEU

ASP

PHE

CYS

5

THR

GLY

GLU

ASP

SER

VAL

ASP

GLY

LYS

6

ARG

GLN

ARG

HIS

SER

GLY

LEU

THR

GLU

GLN

7

THR

TYR

SER

ALA

LEU

PRO

GLU

PRO

LYS

ALA

8

THR

Samples:

sample_1: agnoprotein 0.2 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 3.0; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1
2D DQF-COSY	sample_1	anisotropic	sample_conditions_1

Software:

Analysis v2.4, CCPN - peak picking

Analysis v2.4.0, CCPN - chemical shift assignment

CNS vVersion: 1.2 at patch level 1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

TOPSPIN v3.2, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 600 MHz