BMRB Entry 34462

Name: Solution structure of the modulator of repression (MOR) of the temperate bacteriophage TP901-1 from Lactococcus lactis
Published: 2020-08-03

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PDB ID: 6to6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34462
MolProbity Validation Chart

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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:

Solution structure of the modulator of repression (MOR) of the temperate bacteriophage TP901-1 from Lactococcus lactis

Deposition date:

2019-12-11

Original release date:

2020-08-03

Authors:

Rasmussen, K.; Blackledge, M.; Herrmann, T.; Lo Leggio, L.; Jensen, M.

Citation:

Citation: Rasmussen, Kim Krighaar; Palencia, Andres; Varming, Anders; El-Wali, Habiba; Boeri Erba, Elisabetta; Blackledge, Martin; Hammer, Karin; Herrmann, Torsten; Kilstrup, Mogens; Lo Leggio, Leila; Jensen, Malene Ringkjobing. "Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage" Proc. Natl. Acad. Sci. U. S. A. 117, 20576-20585 (2020).
PubMed: 32788352

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, 8422.644 Da.

Natural source:

Natural source: Common Name: Lactococcus phage TP901-1 Taxonomy ID: 35345 Superkingdom: Viruses Kingdom: not available Genus/species: not available Lactococcus phage TP901-1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMSYDYSSLLGKITEKCGT QYNFAIAMGLSERTVSLKLN DKVTWKDDEILKAVHVLELN PQDIPKYFFNAKVH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	76
1H chemical shifts	519

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 74 residues - 8422.644 Da.

1

GLY

SER

MET

SER

TYR

ASP

TYR

SER

LEU

2

LEU

GLY

LYS

ILE

THR

GLU

LYS

CYS

GLY

THR

3

GLN

TYR

ASN

PHE

ALA

ILE

ALA

MET

GLY

LEU

4

SER

GLU

ARG

THR

VAL

SER

LEU

LYS

LEU

ASN

5

ASP

LYS

VAL

THR

TRP

LYS

ASP

GLU

ILE

6

LEU

LYS

ALA

VAL

HIS

VAL

LEU

GLU

LEU

ASN

7

PRO

GLN

ASP

ILE

PRO

LYS

TYR

PHE

ASN

8

ALA

LYS

VAL

HIS

Samples:

sample_1: MOR, [U-13C; U-15N], 700 uM; Tris buffer 20 mM; NaCl 100 mM; dithiothreitol (DTT) 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
[1H-1H] NOESY-15N-HSQC	sample_1	isotropic	sample_conditions_1
aliphatic [1H-1H]-NOESY-13C-HSQC	sample_1	isotropic	sample_conditions_1
aromatic [1H-1H]-NOESY-13C-HSQC	sample_1	isotropic	sample_conditions_1
HNCO	sample_1	isotropic	sample_conditions_1
HN(CA)CO	sample_1	isotropic	sample_conditions_1
HN(CO)CACB	sample_1	isotropic	sample_conditions_1
HNCACB	sample_1	isotropic	sample_conditions_1
HSQC	sample_1	isotropic	sample_conditions_1

Software:

UNIO, Herrmann, T. et al - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CcpNmr Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz
Bruker AVANCE III 700 MHz
Bruker AVANCE III 600 MHz

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