BMRB Entry 11587

Name: Solution structure of Human Pin1 PPIase mutant C113A
Published: 2016-01-04

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PDB ID: 2ruq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11587
MolProbity Validation Chart

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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: Solution structure of Human Pin1 PPIase mutant C113A PubMed: 26226559

Deposition date: 2015-01-20 Original release date: 2016-01-04

Authors: Jing, Wang; Tochio, Naoya; Tate, Shin-ichi

Citation: Wang, Jing; Tochio, Naoya; Kawasaki, Ryosuke; Tamari, Yu; Xu, Ning; Uewaki, Jun-ichi; Utsunomiya-Tate, Naoko; Tate, Shin-ichi. "Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase" Biochemistry 54, 5242-5253 (2015).

Assembly members:
entity, polymer, 117 residues, 13089.776 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

Entity Sequences (FASTA):
entity: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDASSAKARGDLGAFS RGQMQKPFEDASFALRTGEM SGPVFTDSGIHIILRTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	505
15N chemical shifts	125
1H chemical shifts	803

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 117 residues - 13089.776 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

ALA

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: sodium sulfate 100 mM; sodium phosphate 50 mM; EDTA 5 mM; D2O, [U-2H], 6%; H2O 94%; DTT 1 mM; NaN3 0.03%

sample_conditions_1: ionic strength: 150 mM; pH: 6.6; pressure: 1 atm; temperature: 299 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

MAGRO, Kobayashi N. - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - data analysis

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 700 MHz

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