BMRB Entry 34642

Name: Solution structure of the N-terminal domain of human telomeric Repeat-binding factor 2-interacting protein 1 (hRap1): implication for Rap1-TRF2 interaction in Human.
Published: 2022-09-30

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PDB ID: 7oz0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34642
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 N-terminal domain of human telomeric Repeat-binding factor 2-interacting protein 1 (hRap1): implication for Rap1-TRF2 interaction in Human.

Deposition date:

2021-06-25

Original release date:

2022-09-30

Authors:

Miron, S.; LeDU, M.; Gaullier, G.; Zinn-justin, S.; Cuniasse, P.

Citation:

Citation: Miron, S.; LeDU, M.; Gaullier, G.; Zinn-justin, S.; Cuniasse, P.. "Solution structure of the N-terminal domain of human telomeric Repeat-binding factor 2-interacting protein 1 (hRap1): implication for Rap1-TRF2 interaction in Human." .

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, 12138.556 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAEAMDLGKDPNGPTHSSTL FVRDDGSSMSFYVRPSPAKR RLSTLILHGGGTVCRVQEPG AVLLAQPGEALAEASGDFIS TQYILDCVERNERLELEAYR LGPASAADTGSEAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	442
15N chemical shifts	107
1H chemical shifts	660

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_1 114 residues - 12138.556 Da.

1

MET

ALA

GLU

ALA

MET

ASP

LEU

GLY

LYS

ASP

2

PRO

ASN

GLY

PRO

THR

HIS

SER

THR

LEU

3

PHE

VAL

ARG

ASP

GLY

SER

MET

SER

4

PHE

TYR

VAL

ARG

PRO

SER

PRO

ALA

LYS

ARG

5

ARG

LEU

SER

THR

LEU

ILE

LEU

HIS

GLY

6

GLY

THR

VAL

CYS

ARG

VAL

GLN

GLU

PRO

GLY

7

ALA

VAL

LEU

ALA

GLN

PRO

GLY

GLU

ALA

8

LEU

ALA

GLU

ALA

SER

GLY

ASP

PHE

ILE

SER

9

THR

GLN

TYR

ILE

LEU

ASP

CYS

VAL

GLU

ARG

10

ASN

GLU

ARG

LEU

GLU

LEU

GLU

ALA

TYR

ARG

11

LEU

GLY

PRO

ALA

SER

ALA

ASP

THR

GLY

12

SER

GLU

ALA

LYS

Samples:

sample_1: human Telomeric Repeat-binding factor 2-interacting protein 1 (hRAP1), [U-100% 13C; U-100% 15N], 100 ± 10 uM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOSCY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 13C (aromatic)NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 13C(aliphatic)NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v4.0.7, Bruker Biospin - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

CYANA v3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker AVANCE II 700 MHz
Bruker AVANCE III 950 MHz

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