BMRB Entry 27160

Name: 1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of wild type human flap endonuclease-1
Published: 2018-05-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27160

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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:

1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of wild type human flap endonuclease-1

Deposition date:

2017-06-23

Original release date:

2018-05-22

Authors:

Bennet, Ian; Baxter, Nicola

Citation:

Citation: Bennet, Ian; Finger, L David; Baxter, Nicola; Ambrose, Benjamin; Hounslow, Andrea; Thompson, Mark; Exell, Jack; Shahari, Nur Nazihah; Craggs, Timothy; Waltho, Jonathan; Grasby, Jane. "Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1" Nucleic Acids Res. 46, 5618-5633 (2018).
PubMed: 29718417

Assembly members:

Assembly members:
hFEN1, polymer, 341 residues, 38457.18 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: pET-29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hFEN1: GIQGLAKLIADVAPSAIREN DIKSYFGRKVAIDASMSIYQ FLIAVRQGGDVLQNEEGETT SHLMGMFYRTIRMMENGIKP VYVFDGKPPQLKSGELAKRS ERRAEAEKQLQQAQAAGAEQ EVEKFTKRLVKVTKQHNDEC KHLLSLMGIPYLDAPSEAEA SCAALVKAGKVYAAATEDMD CLTFGSPVLMRHLTASEAKK LPIQEFHLSRILQELGLNQE QFVDLCILLGSDYCESIRGI GPKRAVDLIQKHKSIEEIVR RLDPNKYPVPENWLHKEAHQ LFLEPEVLDPESVELKWSEP NEEELIKFMCGEKQFSEERI RSGVKRLSKSRQGSTLEVLF Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	797
15N chemical shifts	247
1H chemical shifts	247

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hFEN1-336	1

Entities:

Entity 1, hFEN1-336 341 residues - 38457.18 Da.

1

GLY

ILE

GLN

GLY

LEU

ALA

LYS

LEU

ILE

ALA

2

ASP

VAL

ALA

PRO

SER

ALA

ILE

ARG

GLU

ASN

3

ASP

ILE

LYS

SER

TYR

PHE

GLY

ARG

LYS

VAL

4

ALA

ILE

ASP

ALA

SER

MET

SER

ILE

TYR

GLN

5

PHE

LEU

ILE

ALA

VAL

ARG

GLN

GLY

ASP

6

VAL

LEU

GLN

ASN

GLU

GLY

GLU

THR

7

SER

HIS

LEU

MET

GLY

MET

PHE

TYR

ARG

THR

8

ILE

ARG

MET

GLU

ASN

GLY

ILE

LYS

PRO

9

VAL

TYR

VAL

PHE

ASP

GLY

LYS

PRO

GLN

10

LEU

LYS

SER

GLY

GLU

LEU

ALA

LYS

ARG

SER

11

GLU

ARG

ALA

GLU

ALA

GLU

LYS

GLN

LEU

12

GLN

ALA

GLN

ALA

GLY

ALA

GLU

GLN

13

GLU

VAL

GLU

LYS

PHE

THR

LYS

ARG

LEU

VAL

14

LYS

VAL

THR

LYS

GLN

HIS

ASN

ASP

GLU

CYS

15

LYS

HIS

LEU

SER

LEU

MET

GLY

ILE

PRO

16

TYR

LEU

ASP

ALA

PRO

SER

GLU

ALA

GLU

ALA

17

SER

CYS

ALA

LEU

VAL

LYS

ALA

GLY

LYS

18

VAL

TYR

ALA

THR

GLU

ASP

MET

ASP

19

CYS

LEU

THR

PHE

GLY

SER

PRO

VAL

LEU

MET

20

ARG

HIS

LEU

THR

ALA

SER

GLU

ALA

LYS

21

LEU

PRO

ILE

GLN

GLU

PHE

HIS

LEU

SER

ARG

22

ILE

LEU

GLN

GLU

LEU

GLY

LEU

ASN

GLN

GLU

23

GLN

PHE

VAL

ASP

LEU

CYS

ILE

LEU

GLY

24

SER

ASP

TYR

CYS

GLU

SER

ILE

ARG

GLY

ILE

25

GLY

PRO

LYS

ARG

ALA

VAL

ASP

LEU

ILE

GLN

26

LYS

HIS

LYS

SER

ILE

GLU

ILE

VAL

ARG

27

ARG

LEU

ASP

PRO

ASN

LYS

TYR

PRO

VAL

PRO

28

GLU

ASN

TRP

LEU

HIS

LYS

GLU

ALA

HIS

GLN

29

LEU

PHE

LEU

GLU

PRO

GLU

VAL

LEU

ASP

PRO

30

GLU

SER

VAL

GLU

LEU

LYS

TRP

SER

GLU

PRO

31

ASN

GLU

LEU

ILE

LYS

PHE

MET

CYS

32

GLY

GLU

LYS

GLN

PHE

SER

GLU

ARG

ILE

33

ARG

SER

GLY

VAL

LYS

ARG

LEU

SER

LYS

SER

34

ARG

GLN

GLY

SER

THR

LEU

GLU

VAL

LEU

PHE

35

GLN

Samples:

sample_1: hFEN1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 10 mM; potassium chloride 76 mM; EDTA 0.1 mM; sodium azide 4 mM; D2O, [U-99% 2H], 10%; H2O 90%; TSP, [U-99% 2H], 0.05 mM; beta-mercaptoethanol 100 mM

sample_conditions_1: ionic strength: 90 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

Felix, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking, processing

CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking

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