BMRB Entry 25263

Name: NMR assignments of the CUS-3 phage coat protein insertion domain.
Published: 2015-08-07

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PDB ID: 6mnt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25263
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR assignments of the CUS-3 phage coat protein insertion domain. PubMed: 25694158

Deposition date: 2014-10-02 Original release date: 2015-08-07

Authors: Tripler, Therese; Maciejewski, Mark; Teschke, Carolyn; Alexandrescu, Andrei

Citation: Tripler, Therese; Maciejewski, Mark; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein" Biomol. NMR Assign. 9, 333-336 (2015).

Assembly members:
CUS-3id, polymer, 126 residues, Formula weight is not available

Natural source: Common Name: Viruses Taxonomy ID: 38018 Superkingdom: Viruses Kingdom: not available Genus/species: CUS-3 Bacteriophage

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
CUS-3id: MASGSTESLTVSGQPEHKVE AKDSNGMPVDNRQGTITVSA SGLQVGDAFTIAGVNSVHQI TKDTTGQPQVFRVLAVSGTT VTISPKILPVENTDVASRPY ANVDAKPAESAAITILNKLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	461
15N chemical shifts	119
1H chemical shifts	742

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CUS-3id, chain 1	1
2	CUS-3id, chain 2	1

Entities:

Entity 1, CUS-3id, chain 1 126 residues - Formula weight is not available

contains C-terminal 6x his-tag; additional residues: at N-terminus: MAS from vector design and C-terminus: LE

1

MET

ALA

SER

GLY

SER

THR

GLU

SER

LEU

THR

2

VAL

SER

GLY

GLN

PRO

GLU

HIS

LYS

VAL

GLU

3

ALA

LYS

ASP

SER

ASN

GLY

MET

PRO

VAL

ASP

4

ASN

ARG

GLN

GLY

THR

ILE

THR

VAL

SER

ALA

5

SER

GLY

LEU

GLN

VAL

GLY

ASP

ALA

PHE

THR

6

ILE

ALA

GLY

VAL

ASN

SER

VAL

HIS

GLN

ILE

7

THR

LYS

ASP

THR

GLY

GLN

PRO

GLN

VAL

8

PHE

ARG

VAL

LEU

ALA

VAL

SER

GLY

THR

9

VAL

THR

ILE

SER

PRO

LYS

ILE

LEU

PRO

VAL

10

GLU

ASN

THR

ASP

VAL

ALA

SER

ARG

PRO

TYR

11

ALA

ASN

VAL

ASP

ALA

LYS

PRO

ALA

GLU

SER

12

ALA

ILE

THR

ILE

LEU

ASN

LYS

LEU

GLU

13

HIS

Samples:

sample_1: insertion domain, [U-100% 15N], 1.9 mM; insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; H2O 90%; D2O 10%

sample_2: insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-C13 HSQC	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
2D TOCSY	sample_2	isotropic	sample_conditions_1
2D NOESY	sample_2	isotropic	sample_conditions_1

Software:

Ccpnmr_analysis, CCPN - chemical shift assignment, peak picking

Felix, Accelrys Software Inc. - processing

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts