BMRB Entry 25157

Name: Strcucture of Decorin Binding Protein A from strain PBr of Borrelia garinii
Published: 2015-03-23

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PDB ID: 2mtd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25157
MolProbity Validation Chart

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

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Title: Strcucture of Decorin Binding Protein A from strain PBr of Borrelia garinii 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:
entity, polymer, 164 residues, 35781.660 Da.

Natural source: Common Name: spirochetes Taxonomy ID: 498743 Superkingdom: Bacteria Kingdom: not available Genus/species: Borrelia garinii

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

Entity Sequences (FASTA):
entity: GLTGETKIRLESSAQEIKDE INKIKANAKKEGVKFEAFTN TQTGSKISEKPEFILKAKIK AIQVAERFVKAIKEEAEKLK KSGSSGAFSAMYDLMIDVSK PLEEIGIQKMTGTVKEAAQK TPATTADGIIAIAQAMEDKL NNVNKKQHDALKNLKEKAKT ATTT

Data sets:

assigned_chemical_shifts
- PBr_list

Data type	Count
13C chemical shifts	682
15N chemical shifts	155
1H chemical shifts	973

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 164 residues - 35781.660 Da.

1

GLY

LEU

THR

GLY

GLU

THR

LYS

ILE

ARG

LEU

2

GLU

SER

ALA

GLN

GLU

ILE

LYS

ASP

GLU

3

ILE

ASN

LYS

ILE

LYS

ALA

ASN

ALA

LYS

4

GLU

GLY

VAL

LYS

PHE

GLU

ALA

PHE

THR

ASN

5

THR

GLN

THR

GLY

SER

LYS

ILE

SER

GLU

LYS

6

PRO

GLU

PHE

ILE

LEU

LYS

ALA

LYS

ILE

LYS

7

ALA

ILE

GLN

VAL

ALA

GLU

ARG

PHE

VAL

LYS

8

ALA

ILE

LYS

GLU

ALA

GLU

LYS

LEU

LYS

9

LYS

SER

GLY

SER

GLY

ALA

PHE

SER

ALA

10

MET

TYR

ASP

LEU

MET

ILE

ASP

VAL

SER

LYS

11

PRO

LEU

GLU

ILE

GLY

ILE

GLN

LYS

MET

12

THR

GLY

THR

VAL

LYS

GLU

ALA

GLN

LYS

13

THR

PRO

ALA

THR

ALA

ASP

GLY

ILE

14

ALA

ILE

ALA

GLN

ALA

MET

GLU

ASP

LYS

LEU

15

ASN

VAL

ASN

LYS

GLN

HIS

ASP

ALA

16

LEU

LYS

ASN

LEU

LYS

GLU

LYS

ALA

LYS

THR

17

ALA

THR

Samples:

sample: PBr, [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