BMRB Entry 27528

Name: Backbone Assignments for human WDR5
Published: 2019-08-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27528

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:

Backbone Assignments for human WDR5

Deposition date:

2018-06-26

Original release date:

2019-08-27

Authors:

Lemak, Alexander; Kaustov, Lilia; Houliston, Scott; Arrowsmith, Cheryl

Citation:

Citation: Kaustov, Lilia; Lemak, Alexander; Wu, Hong; Faini, Marco; Fan, Lixin; Fang, Xianyang; Zeng, Hong; Duan, Shili; Allali-Hassani, Abdellah; Li, Fengling; Wei, Yong; Vedadi, Masoud; Aebersold, Ruedi; Wang, Yunxing; Houliston, Scott; Arrowsmith, Cheryl. "The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions" Nucleic Acids Res. 47, 9433-9447 (2019).
PubMed: 31400120

Assembly members:

Assembly members:
WDR5, polymer, 314 residues, 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: pET28-MHL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WDR5: SSATQSKPTPVKPNYALKFT LAGHTKAVSSVKFSPNGEWL ASSSADKLIKIWGAYDGKFE KTISGHKLGISDVAWSSDSN LLVSASDDKTLKIWDVSSGK CLKTLKGHSNYVFCCNFNPQ SNLIVSGSFDESVRIWDVKT GKCLKTLPAHSDPVSAVHFN RDGSLIVSSSYDGLCRIWDT ASGQCLKTLIDDDNPPVSFV KFSPNGKYILAATLDNTLKL WDYSKGKCLKTYTGHKNEKY CIFANFSVTGGKWIVSGSED NLVYIWNLQTKEIVQKLQGH TDVVISTACHPTENIIASAA LENDKTIKLWKSDC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	838
15N chemical shifts	256
1H chemical shifts	256

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WDR5	1

Entities:

Entity 1, WDR5 314 residues - Formula weight is not available

1

SER

ALA

THR

GLN

SER

LYS

PRO

THR

PRO

2

VAL

LYS

PRO

ASN

TYR

ALA

LEU

LYS

PHE

THR

3

LEU

ALA

GLY

HIS

THR

LYS

ALA

VAL

SER

4

VAL

LYS

PHE

SER

PRO

ASN

GLY

GLU

TRP

LEU

5

ALA

SER

ALA

ASP

LYS

LEU

ILE

LYS

6

ILE

TRP

GLY

ALA

TYR

ASP

GLY

LYS

PHE

GLU

7

LYS

THR

ILE

SER

GLY

HIS

LYS

LEU

GLY

ILE

8

SER

ASP

VAL

ALA

TRP

SER

ASP

SER

ASN

9

LEU

VAL

SER

ALA

SER

ASP

LYS

THR

10

LEU

LYS

ILE

TRP

ASP

VAL

SER

GLY

LYS

11

CYS

LEU

LYS

THR

LEU

LYS

GLY

HIS

SER

ASN

12

TYR

VAL

PHE

CYS

ASN

PHE

ASN

PRO

GLN

13

SER

ASN

LEU

ILE

VAL

SER

GLY

SER

PHE

ASP

14

GLU

SER

VAL

ARG

ILE

TRP

ASP

VAL

LYS

THR

15

GLY

LYS

CYS

LEU

LYS

THR

LEU

PRO

ALA

HIS

16

SER

ASP

PRO

VAL

SER

ALA

VAL

HIS

PHE

ASN

17

ARG

ASP

GLY

SER

LEU

ILE

VAL

SER

18

TYR

ASP

GLY

LEU

CYS

ARG

ILE

TRP

ASP

THR

19

ALA

SER

GLY

GLN

CYS

LEU

LYS

THR

LEU

ILE

20

ASP

ASN

PRO

VAL

SER

PHE

VAL

21

LYS

PHE

SER

PRO

ASN

GLY

LYS

TYR

ILE

LEU

22

ALA

THR

LEU

ASP

ASN

THR

LEU

LYS

LEU

23

TRP

ASP

TYR

SER

LYS

GLY

LYS

CYS

LEU

LYS

24

THR

TYR

THR

GLY

HIS

LYS

ASN

GLU

LYS

TYR

25

CYS

ILE

PHE

ALA

ASN

PHE

SER

VAL

THR

GLY

26

GLY

LYS

TRP

ILE

VAL

SER

GLY

SER

GLU

ASP

27

ASN

LEU

VAL

TYR

ILE

TRP

ASN

LEU

GLN

THR

28

LYS

GLU

ILE

VAL

GLN

LYS

LEU

GLN

GLY

HIS

29

THR

ASP

VAL

ILE

SER

THR

ALA

CYS

HIS

30

PRO

THR

GLU

ASN

ILE

ALA

SER

ALA

31

LEU

GLU

ASN

ASP

LYS

THR

ILE

LYS

LEU

TRP

32

LYS

SER

ASP

CYS

Samples:

sample_1: WDR5, [U-100% 13C; U-100% 15N; U-80% 2H], 200 uM; PMSF 1 mM; TRIS 20 mM; beta-mercaptoethanol 2 mM; DTT 2 mM; sodium chloride 250 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - peak picking

FMCGUI, Lemak et al., University Health Network, Toronto - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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