BMRB Entry 25481

Name: Backbone 1H, 13C and 15N chemical shift assignment for perforin C2 quad mutant
Published: 2016-11-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25481

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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:

Backbone 1H, 13C and 15N chemical shift assignment for perforin C2 quad mutant

Deposition date:

2015-02-09

Original release date:

2016-11-02

Authors:

Yagi, Hiromasa; Conroy, Paul; Leung, Eleanor; Law, Ruby; Whisstock, James; Norton, Raymond

Citation:

Citation: Yagi, Hiromasa; Conroy, Paul; Leung, Eleanor; Law, Ruby; Whisstock, James; Norton, Raymond. "Structural Basis for Ca2+-mediated Interaction of the Perforin C2 Domain with Lipid Membranes" J. Biol. Chem. 290, 25213-25226 (2015).
PubMed: 26306037

Assembly members:

Assembly members:
perforin_C2_domain, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pComb3X

Entity Sequences (FASTA):

Entity Sequences (FASTA):
perforin_C2_domain: AQRGLAHLVVSNFRAEHLAG DATTATDAYLKVFFGGQEFR TGVVWNNNNPRWTDKMDFEN VLLSTGGPLRVQVWDADAGA DDDLLGSCDRSPHSGFHEVT CELNHGRVKFSYHAKSLPGH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	211
15N chemical shifts	108
1H chemical shifts	108

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	perforin C2 quad mutant	1

Entities:

Entity 1, perforin C2 quad mutant 125 residues - Formula weight is not available

An extra Alanine is remained at N-terminal as a result of cleavage of the signal sequence. Gly + His6 tag are attached at C-terminal.

1

ALA

GLN

ARG

GLY

LEU

ALA

HIS

LEU

VAL

2

SER

ASN

PHE

ARG

ALA

GLU

HIS

LEU

ALA

GLY

3

ASP

ALA

THR

ALA

THR

ASP

ALA

TYR

LEU

4

LYS

VAL

PHE

GLY

GLN

GLU

PHE

ARG

5

THR

GLY

VAL

TRP

ASN

PRO

6

ARG

TRP

THR

ASP

LYS

MET

ASP

PHE

GLU

ASN

7

VAL

LEU

SER

THR

GLY

PRO

LEU

ARG

8

VAL

GLN

VAL

TRP

ASP

ALA

ASP

ALA

GLY

ALA

9

ASP

LEU

GLY

SER

CYS

ASP

ARG

10

SER

PRO

HIS

SER

GLY

PHE

HIS

GLU

VAL

THR

11

CYS

GLU

LEU

ASN

HIS

GLY

ARG

VAL

LYS

PHE

12

SER

TYR

HIS

ALA

LYS

SER

LEU

PRO

GLY

HIS

13

HIS

Samples:

sample_1: perforin C2 domain, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; sodium chloride 150 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz

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