BMRB Entry 26779

Name: Human Cdc25B complete catalytic domain: backbone assignments (1H, 13CA, 13CB, 13C&#039;, 15N), 15N relaxation times (T1 and T2), heteronuclear NOEs and residual dipolar couplings (NH)
Published: 2016-08-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26779

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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:

Human Cdc25B complete catalytic domain: backbone assignments (1H, 13CA, 13CB, 13C', 15N), 15N relaxation times (T1 and T2), heteronuclear NOEs and residual dipolar couplings (NH)

Deposition date:

2016-04-14

Original release date:

2016-08-01

Authors:

Sayegh, Raphael; Tamaki, Fabio; Marana, Sandro; Salinas, Roberto; Arantes, Guilherme

Citation:

Citation: Sayegh, Raphael; Tamaki, Fabio; Marana, Sandro; Salinas, Roberto; Arantes, Guilherme. "Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases" Proteins 84, 1567-1575 (2016).
PubMed: 27410025

Assembly members:

Assembly members:
Cdc25B, polymer, 201 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: p28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cdc25B: GSHMEFQSDHRELIGDYSKA FLLQTVDGKHQDLKYISPET MVALLTGKFSNIVDKFVIVD CRYPYEYEGGHIKTAVNLPL ERDAESFLLKSPIAPCSLDK RVILIFHCEFSSERGPRMCR FIRERDRAVNDYPSLYYPEM YILKGGYKEFFPQHPNFCEP QDYRPMNHEAFKDELKTFRL KTRSWAGERSRRELCSRLQD Q

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
order_parameters
- order_parameter_list_1

Data type	Count
13C chemical shifts	467
15N chemical shifts	143
1H chemical shifts	143
T1 relaxation values	137
T2 relaxation values	86
heteronuclear NOE values	135
order parameters	80
residual dipolar couplings	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cdc25B monomer	1

Entities:

Entity 1, Cdc25B monomer 201 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLU

PHE

GLN

SER

ASP

HIS

2

ARG

GLU

LEU

ILE

GLY

ASP

TYR

SER

LYS

ALA

3

PHE

LEU

GLN

THR

VAL

ASP

GLY

LYS

HIS

4

GLN

ASP

LEU

LYS

TYR

ILE

SER

PRO

GLU

THR

5

MET

VAL

ALA

LEU

THR

GLY

LYS

PHE

SER

6

ASN

ILE

VAL

ASP

LYS

PHE

VAL

ILE

VAL

ASP

7

CYS

ARG

TYR

PRO

TYR

GLU

TYR

GLU

GLY

8

HIS

ILE

LYS

THR

ALA

VAL

ASN

LEU

PRO

LEU

9

GLU

ARG

ASP

ALA

GLU

SER

PHE

LEU

LYS

10

SER

PRO

ILE

ALA

PRO

CYS

SER

LEU

ASP

LYS

11

ARG

VAL

ILE

LEU

ILE

PHE

HIS

CYS

GLU

PHE

12

SER

GLU

ARG

GLY

PRO

ARG

MET

CYS

ARG

13

PHE

ILE

ARG

GLU

ARG

ASP

ARG

ALA

VAL

ASN

14

ASP

TYR

PRO

SER

LEU

TYR

PRO

GLU

MET

15

TYR

ILE

LEU

LYS

GLY

TYR

LYS

GLU

PHE

16

PHE

PRO

GLN

HIS

PRO

ASN

PHE

CYS

GLU

PRO

17

GLN

ASP

TYR

ARG

PRO

MET

ASN

HIS

GLU

ALA

18

PHE

LYS

ASP

GLU

LEU

LYS

THR

PHE

ARG

LEU

19

LYS

THR

ARG

SER

TRP

ALA

GLY

GLU

ARG

SER

20

ARG

GLU

LEU

CYS

SER

ARG

LEU

GLN

ASP

21

GLN

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_2	anisotropic	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 26779

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: