BMRB Entry 51043

Name: WT Pin1 with 5x FFpSPR ligand
Published: 2022-08-11

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PDB ID: 7suq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51043
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:

WT Pin1 with 5x FFpSPR ligand

Deposition date:

2021-07-29

Original release date:

2022-08-11

Authors:

Born, Alexandra; Henen, Morkos; Vogeli, Beat

Citation:

Citation: Born, Alexandra; Soetbeer, Janne; Henen, Morkos; Breitgoff, Frauke; Nichols, Parker; Jeschke, Gunnar; Vogeli, Beat. "Ligand-specific conformational change drives interdomain allostery in Pin1" Nat. Commun. 13, 4546-4546 (2022).
PubMed: 35927276

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 18243 Da.
entity_2, polymer, 5 residues, 774 Da.

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):
entity_1: MADEEKLPPGWEKRMSRSSG RVYYFNHITNASQWERPSGN SSSGGKNGQGEPARVRCSHL LVKHSQSRRPSSWRQEKITR TKEEALELINGYIQKIKSGE EDFESLASQFSDCSSAKARG DLGAFSRGQMQKPFEDASFA LRTGEMSGPVFTDSGIHIIL RTE
entity_2: FFXPR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	168
1H chemical shifts	1068

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pin1	1
2	FFpSPR	2

Entities:

Entity 1, Pin1 163 residues - 18243 Da.

Starting at 1, should be 163 amino acids long

1

MET

ALA

ASP

GLU

LYS

LEU

PRO

GLY

2

TRP

GLU

LYS

ARG

MET

SER

ARG

SER

GLY

3

ARG

VAL

TYR

PHE

ASN

HIS

ILE

THR

ASN

4

ALA

SER

GLN

TRP

GLU

ARG

PRO

SER

GLY

ASN

5

SER

GLY

LYS

ASN

GLY

GLN

GLY

6

GLU

PRO

ALA

ARG

VAL

ARG

CYS

SER

HIS

LEU

7

LEU

VAL

LYS

HIS

SER

GLN

SER

ARG

PRO

8

SER

TRP

ARG

GLN

GLU

LYS

ILE

THR

ARG

9

THR

LYS

GLU

ALA

LEU

GLU

LEU

ILE

ASN

10

GLY

TYR

ILE

GLN

LYS

ILE

LYS

SER

GLY

GLU

11

GLU

ASP

PHE

GLU

SER

LEU

ALA

SER

GLN

PHE

12

SER

ASP

CYS

SER

ALA

LYS

ALA

ARG

GLY

13

ASP

LEU

GLY

ALA

PHE

SER

ARG

GLY

GLN

MET

14

GLN

LYS

PRO

PHE

GLU

ASP

ALA

SER

PHE

ALA

15

LEU

ARG

THR

GLY

GLU

MET

SER

GLY

PRO

VAL

16

PHE

THR

ASP

SER

GLY

ILE

HIS

ILE

LEU

17

ARG

THR

GLU

Entity 2, FFpSPR 5 residues - 774 Da.

phosphorylated serine (pS) at position X

1

PHE

SEP

PRO

ARG

Samples:

sample_1: Pin1, [U-99% 13C; U-99% 15N], 600 uM; FFpSPR 3.6 mM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

Varian INOVA 900 MHz