BMRB Entry 51320

Name: Backbone and sidechain 1H, 13C, 15N chemical shift assignments for the isolated human HtrA2-PDZ domain
Published: 2024-04-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51320

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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:

Backbone and sidechain 1H, 13C, 15N chemical shift assignments for the isolated human HtrA2-PDZ domain

Deposition date:

2022-02-10

Original release date:

2024-04-17

Authors:

Aspholm, Emelie; Lidman, Jens; Burmann, Bjorn

Citation:

Citation: Aspholm, Emelie; Lidman, Jens; Burmann, Bjorn. "Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease" Nat. Commun. 15, 4592-4592 (2024).
PubMed: 38816423

Assembly members:

Assembly members:
entity_1, polymer, 156 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NSGGPLVNLDGEVIGVNTMK VTAGISFAIPSDRLREFLHR GEKKNSSSGISGSQRRYIGV MMLTLSPSILAELQLREPSF PDVQHGVLIHKVILGSPAHR AGLRPGDVILAIGEQMVQNA EDVYEAVRTQSQLAVQIRRG RETLTLYVTPEVTELE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	442
15N chemical shifts	80
1H chemical shifts	724

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HtrA2-PDZ	1

Entities:

Entity 1, HtrA2-PDZ 156 residues - Formula weight is not available

1

ASN

SER

GLY

PRO

LEU

VAL

ASN

LEU

ASP

2

GLY

GLU

VAL

ILE

GLY

VAL

ASN

THR

MET

LYS

3

VAL

THR

ALA

GLY

ILE

SER

PHE

ALA

ILE

PRO

4

SER

ASP

ARG

LEU

ARG

GLU

PHE

LEU

HIS

ARG

5

GLY

GLU

LYS

ASN

SER

GLY

ILE

6

SER

GLY

SER

GLN

ARG

TYR

ILE

GLY

VAL

7

MET

LEU

THR

LEU

SER

PRO

SER

ILE

LEU

8

ALA

GLU

LEU

GLN

LEU

ARG

GLU

PRO

SER

PHE

9

PRO

ASP

VAL

GLN

HIS

GLY

VAL

LEU

ILE

HIS

10

LYS

VAL

ILE

LEU

GLY

SER

PRO

ALA

HIS

ARG

11

ALA

GLY

LEU

ARG

PRO

GLY

ASP

VAL

ILE

LEU

12

ALA

ILE

GLY

GLU

GLN

MET

VAL

GLN

ASN

ALA

13

GLU

ASP

VAL

TYR

GLU

ALA

VAL

ARG

THR

GLN

14

SER

GLN

LEU

ALA

VAL

GLN

ILE

ARG

GLY

15

ARG

GLU

THR

LEU

THR

LEU

TYR

VAL

THR

PRO

16

GLU

VAL

THR

GLU

LEU

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_1	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 51320

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: