BMRB Entry 25156

Name: Structure of decorin binding protein A from strain N40 of Borrelia burgdorferi
Published: 2015-03-23

Click here to enlarge.

PDB ID: 2mtc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25156
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Structure of decorin binding protein A from strain N40 of Borrelia burgdorferi PubMed: 25695518

Deposition date: 2014-08-16 Original release date: 2015-03-23

Authors: Wang, Xu; Morgan, Ashli

Citation: Wang, Xu; Morgan, Ashli. "Structural Mechanisms Underlying Sequence-Dependent Variations in GAG Affinities of Decorin Binding Protein A, a Borrelia burgdorferi Adhesin" Biochem. J. 467, 439-451 (2015).

Assembly members:
DBPA, polymer, 166 residues, 36566.016 Da.

Natural source: Common Name: Lime Disease causing bacterium Taxonomy ID: 521007 Superkingdom: Bacteria Kingdom: not available Genus/species: Borrelia burgdorferi

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

Entity Sequences (FASTA):
DBPA: GLKGETKIILERSAKDITDE INKIKKDAADNNVNFAAFTD SETGSKVSENSFILEAKVRA TTVAEKFVTAIEGEATKLKK TGSSGEFSAMYNMMLEVSGP LEELGVLRMTKTVTDAAEQH PTTTAEGILEIAKIMKTKLQ RVHTKNYCALEKKKNPNFTD EKCKNN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	156
1H chemical shifts	663

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DBPA	1

Entities:

Entity 1, DBPA 166 residues - 36566.016 Da.

disulfide bond between C176 and C191

1

GLY

LEU

LYS

GLY

GLU

THR

LYS

ILE

LEU

2

GLU

ARG

SER

ALA

LYS

ASP

ILE

THR

ASP

GLU

3

ILE

ASN

LYS

ILE

LYS

ASP

ALA

ASP

4

ASN

VAL

ASN

PHE

ALA

PHE

THR

ASP

5

SER

GLU

THR

GLY

SER

LYS

VAL

SER

GLU

ASN

6

SER

PHE

ILE

LEU

GLU

ALA

LYS

VAL

ARG

ALA

7

THR

VAL

ALA

GLU

LYS

PHE

VAL

THR

ALA

8

ILE

GLU

GLY

GLU

ALA

THR

LYS

LEU

LYS

9

THR

GLY

SER

GLY

GLU

PHE

SER

ALA

MET

10

TYR

ASN

MET

LEU

GLU

VAL

SER

GLY

PRO

11

LEU

GLU

LEU

GLY

VAL

LEU

ARG

MET

THR

12

LYS

THR

VAL

THR

ASP

ALA

GLU

GLN

HIS

13

PRO

THR

ALA

GLU

GLY

ILE

LEU

GLU

14

ILE

ALA

LYS

ILE

MET

LYS

THR

LYS

LEU

GLN

15

ARG

VAL

HIS

THR

LYS

ASN

TYR

CYS

ALA

LEU

16

GLU

LYS

ASN

PRO

ASN

PHE

THR

ASP

17

GLU

LYS

CYS

LYS

ASN

Samples:

sample: DBPA, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample	isotropic	sample_conditions
2D 1H-15N HSQC	sample	isotropic	sample_conditions
3D 1H-13C NOESY aliphatic	sample	isotropic	sample_conditions
3D HNCACB	sample	isotropic	sample_conditions
3D CBCA(CO)NH	sample	isotropic	sample_conditions
3D H(CCO)NH	sample	isotropic	sample_conditions
3D C(CO)NH	sample	isotropic	sample_conditions
3D 1H-13C NOESY	sample	isotropic	sample_conditions
3D 1H-15N NOESY	sample	isotropic	sample_conditions

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian INOVA 800 MHz
Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts