BMRB Entry 51078

Name: Backbone and side-chain resonance assignments of the harmonin homology domain 1 (HHD1) of human RTEL1
Published: 2022-05-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51078

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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 side-chain resonance assignments of the harmonin homology domain 1 (HHD1) of human RTEL1

Deposition date:

2021-09-07

Original release date:

2022-05-06

Authors:

Ghosh, Meenakshi; Kumar, Niranjan; Manikandan, Parthasarathy; Basak, Sanmoyee; Singh, Mahavir

Citation:

Citation: Kumar, Niranjan; Ghosh, Meenakshi; Manikandan, Parthasarathy; Basak, Sanmoyee; Deepa, Akula; Singh, Mahavir. "Resonance assignment and secondary structure of the tandem harmonin homology domains of human RTEL1" Biomol. NMR Assign. 16, 159-164 (2022).
PubMed: 35320499

Assembly members:

Assembly members:
entity_1, polymer, 104 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSEPVAGAQTD RAKLFMVAVKQELSQANFAT FTQALQDYKGSDDFAALAAC LGPLFAEDPKKHNLLQGFYQ FVRPHHKQQFEEVCIQLTGR GCGY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	316
15N chemical shifts	92
1H chemical shifts	498

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RTEL1_HHD1	1

Entities:

Entity 1, RTEL1_HHD1 104 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLU

PRO

VAL

ALA

GLY

ALA

GLN

THR

ASP

3

ARG

ALA

LYS

LEU

PHE

MET

VAL

ALA

VAL

LYS

4

GLN

GLU

LEU

SER

GLN

ALA

ASN

PHE

ALA

THR

5

PHE

THR

GLN

ALA

LEU

GLN

ASP

TYR

LYS

GLY

6

SER

ASP

PHE

ALA

LEU

ALA

CYS

7

LEU

GLY

PRO

LEU

PHE

ALA

GLU

ASP

PRO

LYS

8

LYS

HIS

ASN

LEU

GLN

GLY

PHE

TYR

GLN

9

PHE

VAL

ARG

PRO

HIS

LYS

GLN

PHE

10

GLU

VAL

CYS

ILE

GLN

LEU

THR

GLY

ARG

11

GLY

CYS

GLY

TYR

Samples:

sample_1: RTEL1_HHD1, [U-99% 13C; U-99% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

VNMRj - collection

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Agilent DRX 600 MHz

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