BMRB Entry 26857

Name: Backbone 1H, 15N assignments of lipoprotein signal peptidase in complex with globomycin
Published: 2016-11-22

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26857

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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, 15N assignments of lipoprotein signal peptidase in complex with globomycin

Deposition date:

2016-07-22

Original release date:

2016-11-22

Authors:

Laguerre, Aisha

Citation:

Citation: Laguerre, Aisha; Lohr, Frank; Henrich, Erik; Hoffmann, Beate; Abdul-Manan, Norzehan; Connolly, Peter; Perozo, Eduardo; Moore, Jonathan; Bernhard, Frank; Dotsch, Volker. "From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins" Structure 24, 1830-1841 (2016).
PubMed: 27618661

Assembly members:

Assembly members:
lipoprotein_signal_peptidase, polymer, 194 residues, Formula weight is not available

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: Escherichia coli Vector: pET-28(b)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lipoprotein_signal_peptidase: MGSSHHHHHHSSAWSHPQFE KSGLVPRGSHMSQSICSTGL RWLWLVVVVLIIDLGSKYLI LQNFALGDTVPLFPSLNLHY ARNYGAAFSFLADSGGWQRW FFAGIAIGISVILAVMMYRS KATQKLNNIAYALIIGGALG NLFDRLWHGFVVDMIDFYVG DWHFATFNLADTAICVGAAL IVLEGFLPSRAKKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	485
15N chemical shifts	178
1H chemical shifts	178

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lipoprotein signal peptide	1

Entities:

Entity 1, Lipoprotein signal peptide 194 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

ALA

TRP

SER

HIS

PRO

GLN

PHE

GLU

3

LYS

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

4

MET

SER

GLN

SER

ILE

CYS

SER

THR

GLY

LEU

5

ARG

TRP

LEU

TRP

LEU

VAL

LEU

6

ILE

ASP

LEU

GLY

SER

LYS

TYR

LEU

ILE

7

LEU

GLN

ASN

PHE

ALA

LEU

GLY

ASP

THR

VAL

8

PRO

LEU

PHE

PRO

SER

LEU

ASN

LEU

HIS

TYR

9

ALA

ARG

ASN

TYR

GLY

ALA

PHE

SER

PHE

10

LEU

ALA

ASP

SER

GLY

TRP

GLN

ARG

TRP

11

PHE

ALA

GLY

ILE

ALA

ILE

GLY

ILE

SER

12

VAL

ILE

LEU

ALA

VAL

MET

TYR

ARG

SER

13

LYS

ALA

THR

GLN

LYS

LEU

ASN

ILE

ALA

14

TYR

ALA

LEU

ILE

GLY

ALA

LEU

GLY

15

ASN

LEU

PHE

ASP

ARG

LEU

TRP

HIS

GLY

PHE

16

VAL

ASP

MET

ILE

ASP

PHE

TYR

VAL

GLY

17

ASP

TRP

HIS

PHE

ALA

THR

PHE

ASN

LEU

ALA

18

ASP

THR

ALA

ILE

CYS

VAL

GLY

ALA

LEU

19

ILE

VAL

LEU

GLU

GLY

PHE

LEU

PRO

SER

ARG

20

ALA

LYS

GLN

Samples:

sample_1: lipoprotein signal peptidase, [U-13C; U-15N; U-2H], 300 uM; sodium acetate buffer 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 4.0; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 950 MHz

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