BMRB Entry 36014

Name: Solution structure of the Pin1-PPIase (S138A) mutant
Published: 2017-08-07

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PDB ID: 5gph
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36014
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the Pin1-PPIase (S138A) mutant PubMed: 28617332

Deposition date: 2016-08-02 Original release date: 2017-08-07

Authors: Tochio, N.; Wang, J.; Tate, S.

Citation: Wang, Jing; Kawasaki, Ryosuke; Uewaki, Jun-Ichi; Rashid, Arif; Tochio, Naoya; Tate, Shin-Ichi. "Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1." Molecules 22, E992-E992 (2017).

Assembly members:
entity_1, polymer, 117 residues, 13105.732 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDCSSAKARGDLGAFS RGQMQKPFEDAAFALRTGEM SGPVFTDSGIHIILRTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	510
15N chemical shifts	127
1H chemical shifts	804

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 117 residues - 13105.732 Da.

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

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: Pin1 PPIase S138A mutant, [U-13C; U-15N], 1 mM; DTT 1 mM; EDTA 5 mM; sodium azide 0.03%; sodium phosphate 50 mM; sodium sulfate 100 mM; H2O 94%; D2O, [U-2H], 6%

sample_conditions_1: ionic strength: 250 mM; pH: 6.6; pressure: 1 atm; temperature: 299 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

KUJIRA, Kobayashi, N. - data analysis

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AvanceII 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts