BMRB Entry 50152

Name: Coat protein of filamentous bacteriophage IKe (fIKE); backbone chemical shifts assignment by 4D Non-uniformly sampled CANCOCX
Published: 2020-07-01

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50152

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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:

Coat protein of filamentous bacteriophage IKe (fIKE); backbone chemical shifts assignment by 4D Non-uniformly sampled CANCOCX

Deposition date:

2020-01-07

Original release date:

2020-07-01

Authors:

Porat, Gal; Goldbourt, Amir

Citation:

Citation: Porat, Gal; Lusky, Orr; Dayan, Nir; Goldbourt, Amir. "Nonuniformly sampled exclusively-13C/15N 4D solid-state NMR experiments: Assignment and characterization of IKe phage capsid" Magn. Reson. Chem. 59, 237-246 (2021).
PubMed: 32603513

Assembly members:

Assembly members:
fIKE Coat Protein, polymer, 53 residues, Formula weight is not available

Natural source:

Natural source: Common Name: inovirus Taxonomy ID: 10861 Superkingdom: Viruses Kingdom: not available Genus/species: inovirus not available

Experimental source:

Experimental source: Production method: purified from the natural source

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fIKE Coat Protein: AEPNAATNYATEAMDSLKTQ AIDLISQTWPVVTTVVVAGL VIRLFKKFSSKAV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	201
15N chemical shifts	36

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	g8p	1

Entities:

Entity 1, g8p 53 residues - Formula weight is not available

1

ALA

GLU

PRO

ASN

ALA

THR

ASN

TYR

ALA

2

THR

GLU

ALA

MET

ASP

SER

LEU

LYS

THR

GLN

3

ALA

ILE

ASP

LEU

ILE

SER

GLN

THR

TRP

PRO

4

VAL

THR

VAL

ALA

GLY

LEU

5

VAL

ILE

ARG

LEU

PHE

LYS

PHE

SER

6

LYS

ALA

VAL

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 250 mg/mL

sample_2: entity_1, [U-100% 13C; U-100% 15N], 250 mg/mL

sample_conditions_1: pH: 8.0; temperature: 263 K

Experiments:

Name	Sample	Sample state	Sample conditions
4D CANCOCX	sample_1	isotropic	sample_conditions_1
2D J-based zfr-INADEQUATE	sample_1	isotropic	sample_conditions_1
2D RFDR 3ms	sample_1	isotropic	sample_conditions_1
2D RFDR 8ms	sample_1	isotropic	sample_conditions_1
2D DARR 15ms	sample_1	isotropic	sample_conditions_1
2D DARR 100ms	sample_1	isotropic	sample_conditions_1
2D DARR 350ms	sample_2	isotropic	sample_conditions_1

Software:

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

NMRbox, UConn Health Center - virtual machine

SPARKY, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - secondary structure prediction

SMILE, Ying, Delaglio, Torchia, and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz