BMRB Entry 30737

Name: Dimeric form of the trans-stabilized Hemolysin II C-terminal domain
Published: 2021-03-19

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PDB ID: 6wa1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30737
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:

Dimeric form of the trans-stabilized Hemolysin II C-terminal domain

Deposition date:

2020-03-24

Original release date:

2021-03-19

Authors:

Kaplan, A.; Alexandrescu, A.

Citation:

Citation: Kaplan, A.; Olson, R.; Alexandrescu, A.. "Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states" Protein Sci. 30, 990-1005 (2021).
PubMed: 33733504

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, 10461.706 Da.

Natural source:

Natural source: Common Name: Bacillus cereus Taxonomy ID: 226900 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21 Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DNQKALEEQMNSINSVNDKL NKGKGKLSLSMNGNQLKATS SNAGYGISYEDKNWGIFVNG EKVYTFNEKSTVGNISNDIN KLNIKGMYIEIKQI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	241
15N chemical shifts	91
1H chemical shifts	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 94 residues - 10461.706 Da.

1

ASP

ASN

GLN

LYS

ALA

LEU

GLU

GLN

MET

2

ASN

SER

ILE

ASN

SER

VAL

ASN

ASP

LYS

LEU

3

ASN

LYS

GLY

LYS

GLY

LYS

LEU

SER

LEU

SER

4

MET

ASN

GLY

ASN

GLN

LEU

LYS

ALA

THR

SER

5

SER

ASN

ALA

GLY

TYR

GLY

ILE

SER

TYR

GLU

6

ASP

LYS

ASN

TRP

GLY

ILE

PHE

VAL

ASN

GLY

7

GLU

LYS

VAL

TYR

THR

PHE

ASN

GLU

LYS

SER

8

THR

VAL

GLY

ASN

ILE

SER

ASN

ASP

ILE

ASN

9

LYS

LEU

ASN

ILE

LYS

GLY

MET

TYR

ILE

GLU

10

ILE

LYS

GLN

ILE

Samples:

sample_1: HlyIIC, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 0.05 % w/v; AEBSF protease inhibitor 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 303.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (edited)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (filtered)	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking

TALOS vTALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

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

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Varian INOVA 600 MHz

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