BMRB Entry 34696

Name: Llp mutant C1G, lytic conversion lipoprotein of phage T5
Published: 2023-01-02

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PDB ID: 7qjf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34696
MolProbity Validation Chart

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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: Llp mutant C1G, lytic conversion lipoprotein of phage T5

Deposition date: 2021-12-16 Original release date: 2023-01-02

Authors: Degroux, S.; Mestdach, E.; Vives, C.; Le Roy, A.; Salmon, L.; Herrman, T.; Breyton, C.

Citation: Degroux, S.; Mestdach, E.; Vives, C.; Le Roy, A.; Salmon, L.; Herrman, T.; Breyton, C.. "Llp mutant C1G, lytic conversion lipoprotein of phage T5" .

Assembly members:
entity_1, polymer, 62 residues, 7052.991 Da.

Natural source: Common Name: Escherichia phage T5 Taxonomy ID: 2695836 Superkingdom: Viruses Kingdom: not available Genus/species: Tequintavirus Escherichia phage T5

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pMAL-p2E

Entity Sequences (FASTA):
entity_1: GSTFGPKDIKCEAYYMQDHV KYKANVFDRKGDMFLVSPIM AYGSFWAPVSYFTEGNTCEG VF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	151
15N chemical shifts	55
1H chemical shifts	296

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 62 residues - 7052.991 Da.

1

GLY

SER

THR

PHE

GLY

PRO

LYS

ASP

ILE

LYS

2

CYS

GLU

ALA

TYR

MET

GLN

ASP

HIS

VAL

3

LYS

TYR

LYS

ALA

ASN

VAL

PHE

ASP

ARG

LYS

4

GLY

ASP

MET

PHE

LEU

VAL

SER

PRO

ILE

MET

5

ALA

TYR

GLY

SER

PHE

TRP

ALA

PRO

VAL

SER

6

TYR

PHE

THR

GLU

GLY

ASN

THR

CYS

GLU

GLY

7

VAL

PHE

Samples:

sample_1: Tris 25 ± 0.2 mM; NaCl 75 ± 0.2 mM; Sol-Llp, [U-13C; U-15N], 1.024 ± 0.02 mM

sample_conditions_1: ionic strength: 75 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
HAHBNH	sample_1	isotropic	sample_conditions_1
HAHB(CO)NH	sample_1	isotropic	sample_conditions_1
2D 15N-HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

UNIO v2.9.5, Torsten Herrmann - chemical shift assignment, data analysis

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.3, Brunger - refinement

CcpNmr Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE 1000 MHz

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