BMRB Entry 31082

Name: Solution Structure of the model miniprotein EEHEE_rd4_0871
Published: 2024-04-16

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PDB ID: 8skd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31082
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 model miniprotein EEHEE_rd4_0871

Deposition date:

2023-04-19

Original release date:

2024-04-16

Authors:

Houliston, S.; Carter, L.; Baker, D.; Arrowsmith, C.; Rocklin, G.

Citation:

Citation: Houliston, S.; Carter, L.; Baker, D.; Arrowsmith, C.; Rocklin, G.. "Solution Structure of the model miniprotein EEHEE_rd4_0871" .

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7198.985 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MTQVHVDGVTYTFSNPEEAK KFADEMAKRKGGTWEIKDGH IHVE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	197
15N chemical shifts	45
1H chemical shifts	302

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 64 residues - 7198.985 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

THR

GLN

VAL

HIS

VAL

ASP

GLY

VAL

THR

4

TYR

THR

PHE

SER

ASN

PRO

GLU

ALA

LYS

5

LYS

PHE

ALA

ASP

GLU

MET

ALA

LYS

ARG

LYS

6

GLY

THR

TRP

GLU

ILE

LYS

ASP

GLY

HIS

7

ILE

HIS

VAL

GLU

Samples:

sample_1: buffered miniprotein, [U-100% 13C; U-100% 15N], 250 uM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE II 800 MHz
Bruker AVANCE III 600 MHz

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