Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53619

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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

Please specify the pdb ID.

Name: 1H,15N HMQC titration of Pin1 PPIase domain with 4-methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid
Published: 2026-03-27

Title:

1H,15N HMQC titration of Pin1 PPIase domain with 4-methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid

Deposition date:

2026-03-12

Original release date:

2026-03-27

Authors:

Hazlett, Sophia; Harvey, Nikita; Davis, Ben; Waudby, Christopher

Citation:

Citation: Hazlett, Sophia; Harvey, Nikita; Davis, Ben; Waudby, Christopher. "Kinetic NMR screening to rapidly quantify ligand dissociation in fragment mixtures using 19F relaxation dispersion" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 135 residues, Formula weight is not available
entity_2, non-polymer, 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: pRT4025

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKHHHHHHHHGGLVPRGSHG EPARVRCSHLLVKHSQSRRP SSWRQEKITRTKEEALELIN GYIQKIKSGEEDFESLASQF SDCSSAKARGDLGAFSRGQM QKPFEDASFALRTGEMSGPV FTDSGIHIILRTEGS

Data sets:

assigned_chemical_shifts

Data type	Count
15N chemical shifts	717
1H chemical shifts	717

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pin1	1
2	ligand	2

Entities:

Entity 1, Pin1 135 residues - Formula weight is not available

1

MET

LYS

HIS

2

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

GLY

3

GLU

PRO

ALA

ARG

VAL

ARG

CYS

SER

HIS

LEU

4

LEU

VAL

LYS

HIS

SER

GLN

SER

ARG

PRO

5

SER

TRP

ARG

GLN

GLU

LYS

ILE

THR

ARG

6

THR

LYS

GLU

ALA

LEU

GLU

LEU

ILE

ASN

7

GLY

TYR

ILE

GLN

LYS

ILE

LYS

SER

GLY

GLU

8

GLU

ASP

PHE

GLU

SER

LEU

ALA

SER

GLN

PHE

9

SER

ASP

CYS

SER

ALA

LYS

ALA

ARG

GLY

10

ASP

LEU

GLY

ALA

PHE

SER

ARG

GLY

GLN

MET

11

GLN

LYS

PRO

PHE

GLU

ASP

ALA

SER

PHE

ALA

12

LEU

ARG

THR

GLY

GLU

MET

SER

GLY

PRO

VAL

13

PHE

THR

ASP

SER

GLY

ILE

HIS

ILE

LEU

14

ARG

THR

GLU

GLY

SER

Entity 2, ligand - C12H9F3N2O2 - Formula weight is not available

1

Samples:

sample_1: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v

sample_2: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 250 uM

sample_3: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 500 uM

sample_4: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 750 uM

sample_5: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 1000 uM

sample_6: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 1500 uM

sample_7: Pin1 PPIase, [U-15N], 50 uM; sodium phosphate 10 mM; D2O 10 % v/v; 4-Methyl-2-[3-(trifluoromethyl)phenyl]-1H-imidazole-5-carboxylic acid 2000 uM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
0uM	sample_1	isotropic	sample_conditions_1
250uM	sample_2	isotropic	sample_conditions_1
500uM	sample_3	isotropic	sample_conditions_1
750uM	sample_4	isotropic	sample_conditions_1
1000uM	sample_5	isotropic	sample_conditions_1
1500uM	sample_6	isotropic	sample_conditions_1
2000um	sample_7	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment, chemical shift calculation, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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

BMRB Entry 53619