BMRB Entry 27042

Name: FHA-Chk2
Published: 2021-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27042

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:

FHA-Chk2

Deposition date:

2017-03-05

Original release date:

2021-07-22

Authors:

Hembram, Dambarudhar; Das, Ranabir; Negi, Hitendra; Shet, Divya

Citation:

Citation: Hembram, Dambarudhar Shiba Sankar; Negi, Hitendra; Biswas, Poulomi; Tripathi, Vasvi; Bhushan, Lokesh; Shet, Divya; Kumar, Vikas; Das, Ranabir. "The Viral SUMO-Targeted Ubiquitin Ligase ICP0 is Phosphorylated and Activated by Host Kinase Chk2" J. Mol. Biol. 432, 1952-1977 (2020).
PubMed: 32001251

Assembly members:

Assembly members:
FHA-Chk2, polymer, 162 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FHA-Chk2: MHHHHHHLVPRGSETVSTQE LYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVN DNYWFGRDKSCEYCFDEPLL KRTDKYRTYSKKHFRIFREV GPKNSYIAYIEDHSGNGTFV NTELVGKGKRRPLNNNSEIA LSLSRNKVFVFFDLTVDDQS VY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FHA-Chk2	1

Entities:

Entity 1, FHA-Chk2 162 residues - Formula weight is not available

1

MET

HIS

LEU

VAL

PRO

2

ARG

GLY

SER

GLU

THR

VAL

SER

THR

GLN

GLU

3

LEU

TYR

SER

ILE

PRO

GLU

ASP

GLN

GLU

PRO

4

GLU

ASP

GLN

GLU

PRO

GLU

PRO

THR

PRO

5

ALA

PRO

TRP

ALA

ARG

LEU

TRP

ALA

LEU

GLN

6

ASP

GLY

PHE

ALA

ASN

LEU

GLU

CYS

VAL

ASN

7

ASP

ASN

TYR

TRP

PHE

GLY

ARG

ASP

LYS

SER

8

CYS

GLU

TYR

CYS

PHE

ASP

GLU

PRO

LEU

9

LYS

ARG

THR

ASP

LYS

TYR

ARG

THR

TYR

SER

10

LYS

HIS

PHE

ARG

ILE

PHE

ARG

GLU

VAL

11

GLY

PRO

LYS

ASN

SER

TYR

ILE

ALA

TYR

ILE

12

GLU

ASP

HIS

SER

GLY

ASN

GLY

THR

PHE

VAL

13

ASN

THR

GLU

LEU

VAL

GLY

LYS

GLY

LYS

ARG

14

ARG

PRO

LEU

ASN

SER

GLU

ILE

ALA

15

LEU

SER

LEU

SER

ARG

ASN

LYS

VAL

PHE

VAL

16

PHE

ASP

LEU

THR

VAL

ASP

GLN

SER

17

VAL

TYR

Samples:

sample_1: FHA-Chk2, [U-100% 13C; U-100% 15N], 200 uM; Phosphate 50 mM; NaCl 300 mM; DTT 2 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.4; pressure: 1 atm; temperature: 293 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - 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