BMRB Entry 50360

Name: BBP28(23-148) oxidized
Published: 2020-11-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50360

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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:

BBP28(23-148) oxidized

Deposition date:

2020-06-25

Original release date:

2020-11-03

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:
entity_1, polymer, 154 residues, 17203.91 Da.

Natural source:

Natural source: Common Name: Borreliella burgdorferi 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) Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKHHHHHHPMSDYDIPTTEN LYFQGAMGNDTLKNNAQQTK SRGKRDLTQKEATPEKPKSK EELLREKLSEDQKTHLDWLK EALGNDGEFDKFLGYDESKI KTALDHIKSELDKCNGNDAD QQKTTFKQTVQGALSGGIDG FGSNNAVTTCGNGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	615
15N chemical shifts	154
1H chemical shifts	968

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_1 154 residues - 17203.91 Da.

1

MET

LYS

HIS

PRO

MET

2

SER

ASP

TYR

ASP

ILE

PRO

THR

GLU

ASN

3

LEU

TYR

PHE

GLN

GLY

ALA

MET

GLY

ASN

ASP

4

THR

LEU

LYS

ASN

ALA

GLN

THR

LYS

5

SER

ARG

GLY

LYS

ARG

ASP

LEU

THR

GLN

LYS

6

GLU

ALA

THR

PRO

GLU

LYS

PRO

LYS

SER

LYS

7

GLU

LEU

ARG

GLU

LYS

LEU

SER

GLU

8

ASP

GLN

LYS

THR

HIS

LEU

ASP

TRP

LEU

LYS

9

GLU

ALA

LEU

GLY

ASN

ASP

GLY

GLU

PHE

ASP

10

LYS

PHE

LEU

GLY

TYR

ASP

GLU

SER

LYS

ILE

11

LYS

THR

ALA

LEU

ASP

HIS

ILE

LYS

SER

GLU

12

LEU

ASP

LYS

CYS

ASN

GLY

ASN

ASP

ALA

ASP

13

GLN

LYS

THR

PHE

LYS

GLN

THR

VAL

14

GLN

GLY

ALA

LEU

SER

GLY

ILE

ASP

GLY

15

PHE

GLY

SER

ASN

ALA

VAL

THR

CYS

16

GLY

ASN

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 HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8.4 - chemical shift assignment, peak picking

TOPSPIN v3.5 - 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