BMRB Entry 50033

Name: CDC25B - W550A
Published: 2019-10-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50033

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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:

CDC25B - W550A

Deposition date:

2019-10-04

Original release date:

2019-10-29

Authors:

Reis, Andre

Citation:

Citation: Reis, Andre; Sayegh, Raphael; Marana, Sandro; Arantes, Guilherme. "Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins" J. Chem. Inf. Model. 60, 890-897 (2020).
PubMed: 31738549

Assembly members:

Assembly members:
entity_1, polymer, 218 residues, -4 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 Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MEFQSDHRELIGDYSKAFLL QTVDGKHQDLKYISPETMVA LLTGKFSNIVDKFVIVDCRY PYEYEGGHIKTAVNLPLERD AESFLLKSPIAPCSLDKRVI LIFHCEFSSERGPRMCRFIR ERDRAVNDYPSLYYPEMYIL KGGYKEFFPQHPNFCEPQDY RPMNHEAFKDELKTFRLKTR SAAGERSRRELCSRLQDQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	144
1H chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CDC25B - W550A	1

Entities:

Entity 1, CDC25B - W550A 218 residues - -4 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLU

PHE

GLN

SER

ASP

HIS

ARG

GLU

LEU

4

ILE

GLY

ASP

TYR

SER

LYS

ALA

PHE

LEU

5

GLN

THR

VAL

ASP

GLY

LYS

HIS

GLN

ASP

LEU

6

LYS

TYR

ILE

SER

PRO

GLU

THR

MET

VAL

ALA

7

LEU

THR

GLY

LYS

PHE

SER

ASN

ILE

VAL

8

ASP

LYS

PHE

VAL

ILE

VAL

ASP

CYS

ARG

TYR

9

PRO

TYR

GLU

TYR

GLU

GLY

HIS

ILE

LYS

10

THR

ALA

VAL

ASN

LEU

PRO

LEU

GLU

ARG

ASP

11

ALA

GLU

SER

PHE

LEU

LYS

SER

PRO

ILE

12

ALA

PRO

CYS

SER

LEU

ASP

LYS

ARG

VAL

ILE

13

LEU

ILE

PHE

HIS

CYS

GLU

PHE

SER

GLU

14

ARG

GLY

PRO

ARG

MET

CYS

ARG

PHE

ILE

ARG

15

GLU

ARG

ASP

ARG

ALA

VAL

ASN

ASP

TYR

PRO

16

SER

LEU

TYR

PRO

GLU

MET

TYR

ILE

LEU

17

LYS

GLY

TYR

LYS

GLU

PHE

PRO

GLN

18

HIS

PRO

ASN

PHE

CYS

GLU

PRO

GLN

ASP

TYR

19

ARG

PRO

MET

ASN

HIS

GLU

ALA

PHE

LYS

ASP

20

GLU

LEU

LYS

THR

PHE

ARG

LEU

LYS

THR

ARG

21

SER

ALA

GLY

GLU

ARG

SER

ARG

GLU

22

LEU

CYS

SER

ARG

LEU

GLN

ASP

GLN

Samples:

sample_1: entity_1, [U-100% 15N], 0.2 mM; NaH2PO4 20 mM; NaCl 50 mM; BMER 5 mM; dithiotreitol 2 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker AIII 800 MHz

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