BMRB Entry 30583

Name: Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags
Published: 2019-07-18

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PDB ID: 6o6i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30583
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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:

Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags

Deposition date:

2019-03-06

Original release date:

2019-07-18

Authors:

Bahramzadeh, A.; Huber, T.; Otting, G.

Citation:

Citation: Bahramzadeh, A.; Huber, T.; Otting, G.. "3D protein structure determination using pseudocontact shifts of backbone amide protons generated by double-histidine Co2+-binding motifs at multiple sites." Biochemistry 58, 3243-3250 (2019).
PubMed: 31282649

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, 11787.470 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PGCLPAYDALAGQFIEASSR EARQAILKQGQDGLSGVKET DKKWASQYLKIMGKILDQGE DFPASELARISKLIENKMSE GKKEELQRSLNILTAFRKKG AEKEEL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	297
15N chemical shifts	103
1H chemical shifts	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 106 residues - 11787.470 Da.

1

PRO

GLY

CYS

LEU

PRO

ALA

TYR

ASP

ALA

LEU

2

ALA

GLY

GLN

PHE

ILE

GLU

ALA

SER

ARG

3

GLU

ALA

ARG

GLN

ALA

ILE

LEU

LYS

GLN

GLY

4

GLN

ASP

GLY

LEU

SER

GLY

VAL

LYS

GLU

THR

5

ASP

LYS

TRP

ALA

SER

GLN

TYR

LEU

LYS

6

ILE

MET

GLY

LYS

ILE

LEU

ASP

GLN

GLY

GLU

7

ASP

PHE

PRO

ALA

SER

GLU

LEU

ALA

ARG

ILE

8

SER

LYS

LEU

ILE

GLU

ASN

LYS

MET

SER

GLU

9

GLY

LYS

GLU

LEU

GLN

ARG

SER

LEU

10

ASN

ILE

LEU

THR

ALA

PHE

ARG

LYS

GLY

11

ALA

GLU

LYS

GLU

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
3D HNCO	sample_5	isotropic	sample_conditions_1
3D HNCACO	sample_5	isotropic	sample_conditions_1
3D HNCA	sample_5	isotropic	sample_conditions_1
3D HNCACB	sample_5	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	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 30583

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: