BMRB Entry 30821

Name: Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)
Published: 2021-12-03

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PDB ID: 7kwi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30821
MolProbity Validation Chart

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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:

Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)

Deposition date:

2020-12-01

Original release date:

2021-12-03

Authors:

Yadav, R.; Perera, Y.; Fitzkee, N.

Citation:

Citation: Perera, Y.; Yadav, R.; South, T.; McConnell, K.; Fitzkee, N.. "Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)" .

Assembly members:

Assembly members:
entity_1, polymer, 152 residues, 16739.672 Da.

Natural source:

Natural source: Common Name: Staphylococcus epidermidis Taxonomy ID: 1282 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus epidermidis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NNQLTVTNNSGVAQINAKNS GLYTTVYDTKGKTTNQIQRT LSVTKAATLGDKKFYLVGDY NTGTNYGWVKQDEVIYNTAK SPVKINQTYNVKPGVKLHTV PWGTYNQVAGTVSGKGDQTF KATKQQQIDKATYLYGTVNG KSGWISKYYLTA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	598
15N chemical shifts	141
1H chemical shifts	894

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 152 residues - 16739.672 Da.

1

ASN

GLN

LEU

THR

VAL

THR

ASN

SER

2

GLY

VAL

ALA

GLN

ILE

ASN

ALA

LYS

ASN

SER

3

GLY

LEU

TYR

THR

VAL

TYR

ASP

THR

LYS

4

GLY

LYS

THR

ASN

GLN

ILE

GLN

ARG

THR

5

LEU

SER

VAL

THR

LYS

ALA

THR

LEU

GLY

6

ASP

LYS

PHE

TYR

LEU

VAL

GLY

ASP

TYR

7

ASN

THR

GLY

THR

ASN

TYR

GLY

TRP

VAL

LYS

8

GLN

ASP

GLU

VAL

ILE

TYR

ASN

THR

ALA

LYS

9

SER

PRO

VAL

LYS

ILE

ASN

GLN

THR

TYR

ASN

10

VAL

LYS

PRO

GLY

VAL

LYS

LEU

HIS

THR

VAL

11

PRO

TRP

GLY

THR

TYR

ASN

GLN

VAL

ALA

GLY

12

THR

VAL

SER

GLY

LYS

GLY

ASP

GLN

THR

PHE

13

LYS

ALA

THR

LYS

GLN

ILE

ASP

LYS

14

ALA

THR

TYR

LEU

TYR

GLY

THR

VAL

ASN

GLY

15

LYS

SER

GLY

TRP

ILE

SER

LYS

TYR

LEU

16

THR

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCCO)NH	sample_2	isotropic	sample_conditions_1
3D (H)C(CCO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 30821

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: