BMRB Entry 11557

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion
Published: 2018-12-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11557

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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 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion

Deposition date:

2014-03-24

Original release date:

2018-12-18

Authors:

Xu, Ning; Tamari, Yu; Tochio, Naoya; Tate, Shin-ichi

Citation:

Citation: Xu, Ning; Tochio, Naoya; Wang, Jong; Tamari, Yu; Uewaki, Jun-ichi; Utsunomiya-Tate, Naoko; Igarashi, Kazuhiko; Shiraki, Takuma; Kobayashi, Naohiro; Tate, Shin-ichi. "The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif." Biochemistry 53, 5568-5578 (2014).
PubMed: 25100325

Assembly members:

Assembly members:
wild_type_hPin1_PPIase_domain, polymer, 117 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):
wild_type_hPin1_PPIase_domain: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDCSSAKARGDLGAFS RGQMQKPFEDASFALRTGEM SGPVFTDSGIHIILRTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	328
15N chemical shifts	109
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIase	1

Entities:

Entity 1, PPIase 117 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLU

PRO

ALA

ARG

VAL

ARG

2

CYS

SER

HIS

LEU

VAL

LYS

HIS

SER

GLN

3

SER

ARG

PRO

SER

TRP

ARG

GLN

GLU

4

LYS

ILE

THR

ARG

THR

LYS

GLU

ALA

LEU

5

GLU

LEU

ILE

ASN

GLY

TYR

ILE

GLN

LYS

ILE

6

LYS

SER

GLY

GLU

ASP

PHE

GLU

SER

LEU

7

ALA

SER

GLN

PHE

SER

ASP

CYS

SER

ALA

8

LYS

ALA

ARG

GLY

ASP

LEU

GLY

ALA

PHE

SER

9

ARG

GLY

GLN

MET

GLN

LYS

PRO

PHE

GLU

ASP

10

ALA

SER

PHE

ALA

LEU

ARG

THR

GLY

GLU

MET

11

SER

GLY

PRO

VAL

PHE

THR

ASP

SER

GLY

ILE

12

HIS

ILE

LEU

ARG

THR

GLU

Samples:

sample_1: wild type hPin1 PPIase domain, [U-13C; U-15N], 0.2 mM; TRIS 50 mM; DTT 1 mM; sodium azide 0.03%; H2O 94.12%; D2O 5.88%

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 299 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 HN(CO)CA	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 C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

Magro, Kobayashi - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker Avance 700 MHz

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