BMRB Entry 50946

Name: Structure of Alpha-1-acid Glycoprotein bound to UCN-01 and complete backbone assignments and NMR
Published: 2021-11-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50946

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip 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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of Alpha-1-acid Glycoprotein bound to UCN-01 and complete backbone assignments and NMR

Deposition date:

2021-05-19

Original release date:

2021-11-23

Authors:

Landin, Erik; Williams, Christopher; Crump, Matthew

Citation:

Citation: Landin, Erik; Williams, Christopher; Ryan, Sara; Bochel, Alice; Akter, Nahida; Redfield, Christina; Sessions, Richard; Dedi, Neesha; Taylor, Richard; Crump, Matthew. "The structural basis for high affinity binding of Alpha-1-acid glycoprotein to the potent anti-tumour compound UCN-01" J. Biol. Chem. 297, 101392-101392 (2021).
PubMed: 34758357

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, Formula weight is not available
entity_UCN, non-polymer, 482.530 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: pOPINF

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPQIPLCANLVPVPITNATL DRITGKWFYIASAFRNEEYN KSVQEIQATFFYFTPNKTED TIFLREYQTRQNQCFYNSSY LNVQRENGTVSRYEGGREHV AHLLFLRDTKTLMFGSYLDD EKNWGLSFYADKPETTKEQL GEFYEALDCLRIPRSDVMYT DWKKDKCEPLEKQH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	543
15N chemical shifts	164
1H chemical shifts	491

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Alpha-1-acid Glycoprotein	1
2	UCN-01	2

Entities:

Entity 1, Alpha-1-acid Glycoprotein 174 residues - Formula weight is not available

1

GLY

PRO

GLN

ILE

PRO

LEU

CYS

ALA

ASN

LEU

2

VAL

PRO

VAL

PRO

ILE

THR

ASN

ALA

THR

LEU

3

ASP

ARG

ILE

THR

GLY

LYS

TRP

PHE

TYR

ILE

4

ALA

SER

ALA

PHE

ARG

ASN

GLU

TYR

ASN

5

LYS

SER

VAL

GLN

GLU

ILE

GLN

ALA

THR

PHE

6

PHE

TYR

PHE

THR

PRO

ASN

LYS

THR

GLU

ASP

7

THR

ILE

PHE

LEU

ARG

GLU

TYR

GLN

THR

ARG

8

GLN

ASN

GLN

CYS

PHE

TYR

ASN

SER

TYR

9

LEU

ASN

VAL

GLN

ARG

GLU

ASN

GLY

THR

VAL

10

SER

ARG

TYR

GLU

GLY

ARG

GLU

HIS

VAL

11

ALA

HIS

LEU

PHE

LEU

ARG

ASP

THR

LYS

12

THR

LEU

MET

PHE

GLY

SER

TYR

LEU

ASP

13

GLU

LYS

ASN

TRP

GLY

LEU

SER

PHE

TYR

ALA

14

ASP

LYS

PRO

GLU

THR

LYS

GLU

GLN

LEU

15

GLY

GLU

PHE

TYR

GLU

ALA

LEU

ASP

CYS

LEU

16

ARG

ILE

PRO

ARG

SER

ASP

VAL

MET

TYR

THR

17

ASP

TRP

LYS

ASP

LYS

CYS

GLU

PRO

LEU

18

GLU

LYS

GLN

HIS

Entity 2, UCN-01 - C28 H26 N4 O4 - 482.530 Da.

1

UCN

Samples:

sample_1: Alpha-1-acid Glycoprotein, [U-100% 15N], 1 mM; sodium phosphate 10 mM; 7-Hydroxystaurosporine 2 mM; sodium chloride 100 mM

sample_2: sodium phosphate 10 mM; 7-Hydroxystaurosporine 2 mM; Alpha-1-acid Glycoprotein, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D C(CO)NH	sample_2	isotropic	sample_conditions_2
3D H(CCO)NH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2

Software:

ANALYSIS v2.4.2 - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.6.1 - collection

NMRPipe v10.9 - processing

NMR spectrometers:

Bruker AVANCE III 700 MHz

UNP	P19652
AlphaFold	Q6IB74