BMRB Entry 34361

Name: NMR structure of BB_A03, Borrelia burgdorferi outer surface lipoprotein
Published: 2020-03-16

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PDB ID: 6qs0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34361
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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:

NMR structure of BB_A03, Borrelia burgdorferi outer surface lipoprotein

Deposition date:

2019-02-20

Original release date:

2020-03-16

Authors:

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

Citation:

Citation: Fridmanis, Jekabs; Bobrovs, Raitis; Brangulis, Kalvis; Tars, Kaspars; Jaudzems, Kristaps. "Structural and Functional Analysis of BBA03, Borrelia burgdorferi Competitive Advantage Promoting Outer Surface Lipoprotein" Pathogens 9, .-. (2020).
PubMed: 33050189

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 13746.589 Da.

Natural source:

Natural source: Common Name: Borreliella burgdorferi B31 Taxonomy ID: 224326 Superkingdom: Bacteria Kingdom: not available Genus/species: Borreliella burgdorferi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGTPLEKLVSRLNLNNTE KETLTFLTNLLKEKLVDPNI GLHFKNSGGDESKIEESVQK FLSELKEDEIKDLLAKIKEN KDKKEKDPEELNTYKSILAS GFDGIFNQADSKTTLNKLKD TI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	129
1H chemical shifts	911

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_1 122 residues - 13746.589 Da.

1

GLY

ALA

MET

GLY

THR

PRO

LEU

GLU

LYS

LEU

2

VAL

SER

ARG

LEU

ASN

LEU

ASN

THR

GLU

3

LYS

GLU

THR

LEU

THR

PHE

LEU

THR

ASN

LEU

4

LEU

LYS

GLU

LYS

LEU

VAL

ASP

PRO

ASN

ILE

5

GLY

LEU

HIS

PHE

LYS

ASN

SER

GLY

ASP

6

GLU

SER

LYS

ILE

GLU

SER

VAL

GLN

LYS

7

PHE

LEU

SER

GLU

LEU

LYS

GLU

ASP

GLU

ILE

8

LYS

ASP

LEU

ALA

LYS

ILE

LYS

GLU

ASN

9

LYS

ASP

LYS

GLU

LYS

ASP

PRO

GLU

10

LEU

ASN

THR

TYR

LYS

SER

ILE

LEU

ALA

SER

11

GLY

PHE

ASP

GLY

ILE

PHE

ASN

GLN

ALA

ASP

12

SER

LYS

THR

LEU

ASN

LYS

LEU

LYS

ASP

13

THR

ILE

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_A03, [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-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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