BMRB Entry 34344

Name: NMR structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein
Published: 2020-01-24

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PDB ID: 6qbi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34344
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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 structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein

Deposition date:

2018-12-21

Original release date:

2020-01-24

Authors:

Fridmanis, J.; Otikovs, M.; Brangulis, K.; Jaudzems, K.

Citation:

Citation: Fridmanis, Jekabs; Otikovs, Martins; Brangulis, Kalvis; Tars, Kaspars; Jaudzems, Kristaps. "Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family" Proteins: Struct. Funct. Bioinf. 89, 588-594 (2021).
PubMed: 32949018

Assembly members:

Assembly members:
Surface protein, mlp lipoprotein family, polymer, 102 residues, 11038.109 Da.

Natural source:

Natural source: Common Name: Borreliella burgdorferi Taxonomy ID: 224326 Superkingdom: Bacteria Kingdom: not available Genus/species: Borreliella Borreliella burgdorferi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Surface protein, mlp lipoprotein family: GAMGPKSKEELLREKLSEDQ KTHLDWLKEALGNDGEFDKF LGYDESKIKTALDHIKSELD KCNGNDADQQKTTFKQTVQG ALSGGIDGFGSNNAVTTCGN GS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	414
15N chemical shifts	114
1H chemical shifts	677

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_1 102 residues - 11038.109 Da.

1

GLY

ALA

MET

GLY

PRO

LYS

SER

LYS

GLU

2

LEU

ARG

GLU

LYS

LEU

SER

GLU

ASP

GLN

3

LYS

THR

HIS

LEU

ASP

TRP

LEU

LYS

GLU

ALA

4

LEU

GLY

ASN

ASP

GLY

GLU

PHE

ASP

LYS

PHE

5

LEU

GLY

TYR

ASP

GLU

SER

LYS

ILE

LYS

THR

6

ALA

LEU

ASP

HIS

ILE

LYS

SER

GLU

LEU

ASP

7

LYS

CYS

ASN

GLY

ASN

ASP

ALA

ASP

GLN

8

LYS

THR

PHE

LYS

GLN

THR

VAL

GLN

GLY

9

ALA

LEU

SER

GLY

ILE

ASP

GLY

PHE

GLY

10

SER

ASN

ALA

VAL

THR

CYS

GLY

ASN

11

GLY

SER

Samples:

sample_1: sodium phosphate 20 ± 1 mM; sodium chloride 50 ± 1 mM; sodium azide 0.03 ± 0.0001 % w/v; EDTA 1 ± 0.01 mM; BB_P28, [U-13C; U-15N], 2 ± 0.1 mM

sample_conditions_1: ionic strength: 0.08 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CANDID v2.02, Herrmann, Guntert and Wuthrich - structure calculation

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN v3.5, Bruker Biospin - collection

NMR spectrometers:

Varian UNITY 600 MHz

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