BMRB Entry 27620

Name: human CYPA/PPIA
Published: 2018-09-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27620

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

human CYPA/PPIA

Deposition date:

2018-09-24

Original release date:

2018-09-25

Authors:

Jewginski, Michal; Mackereth, Cameron

Citation:

Citation: Vallade, Maelle; Jewginski, Michal; Fischer, Lucile; Buratto, Jeremie; Bathany, Katell; Schmitter, Jean-Marie; Stupfel, Marine; Godde, Frederic; Mackereth, Cameron; Huc, Ivan. "Assessing interactions between helical aromatic oligoamide foldamers and protein surfaces: a tethering approach" Bioconjug. Chem. 30, 54-62 (2019).
PubMed: 30395443

Assembly members:

Assembly members:
CYPA, polymer, 167 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: pET-His1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CYPA: GAMVNPTVFFDIAVDGEPLG RVSFELFADKVPKTAENFRA LSTGEKGFGYKGSCFHRIIP GFMCQGGDFTRHNGTGGKSI YGEKFEDENFILKHTGPGIL SMANAGPNTNGSQFFICTAK TEWLDGKHVVFGKVKEGMNI VEAMERFGSRNGKTSKKITI ADCGQLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	472
15N chemical shifts	157
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CYPA	1

Entities:

Entity 1, CYPA 167 residues - Formula weight is not available

The initial Gly-Ala remains from the cleaved His6-tag.

1

GLY

ALA

MET

VAL

ASN

PRO

THR

VAL

PHE

2

ASP

ILE

ALA

VAL

ASP

GLY

GLU

PRO

LEU

GLY

3

ARG

VAL

SER

PHE

GLU

LEU

PHE

ALA

ASP

LYS

4

VAL

PRO

LYS

THR

ALA

GLU

ASN

PHE

ARG

ALA

5

LEU

SER

THR

GLY

GLU

LYS

GLY

PHE

GLY

TYR

6

LYS

GLY

SER

CYS

PHE

HIS

ARG

ILE

PRO

7

GLY

PHE

MET

CYS

GLN

GLY

ASP

PHE

THR

8

ARG

HIS

ASN

GLY

THR

GLY

LYS

SER

ILE

9

TYR

GLY

GLU

LYS

PHE

GLU

ASP

GLU

ASN

PHE

10

ILE

LEU

LYS

HIS

THR

GLY

PRO

GLY

ILE

LEU

11

SER

MET

ALA

ASN

ALA

GLY

PRO

ASN

THR

ASN

12

GLY

SER

GLN

PHE

ILE

CYS

THR

ALA

LYS

13

THR

GLU

TRP

LEU

ASP

GLY

LYS

HIS

VAL

14

PHE

GLY

LYS

VAL

LYS

GLU

GLY

MET

ASN

ILE

15

VAL

GLU

ALA

MET

GLU

ARG

PHE

GLY

SER

ARG

16

ASN

GLY

LYS

THR

SER

LYS

ILE

THR

ILE

17

ALA

ASP

CYS

GLY

GLN

LEU

GLU

Samples:

sample_1: CYPA, [U-99% 13C; U-99% 15N], 600 uM; TRIS 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 60 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

SP	P62937
AlphaFold	Q9UC61