BMRB Entry 19563

Name: chemical shift assignments for human dihdyrofolate reductase bound to folate
Published: 2016-04-04

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19563

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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:

chemical shift assignments for human dihdyrofolate reductase bound to folate

Deposition date:

2013-10-18

Original release date:

2016-04-04

Authors:

Wright, Peter; Bhabha, Gira; Tuttle, Lisa; Kroon, Gerard

Citation:

Citation: Tuttle, Lisa; Dyson, H. Jane; Wright, Peter. "Side Chain Conformational Averaging in Human Dihydrofolate Reductase" Biochemistry 53, 1134-1145 (2014).
PubMed: 24498949

Assembly members:

Assembly members:
DHFR, polymer, 187 residues, Formula weight is not available
FOLIC ACID, non-polymer, 441.397 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DHFR: MVGSLNCIVAVSQNMGIGKN GDLPWPPLRNEFRYFQRMTT TSSVEGKQNLVIMGKKTWFS IPEKNRPLKGRINLVLSREL KEPPQGAHFLSRSLDDALKL TEQPELANKVDMVWIVGGSS VYKEAMNHPGHLKLFVTRIM QDFESDTFFPEIDLEKYKLL PEYPGVLSDVQEEKGIKYKF EVYEKND

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	180
15N chemical shifts	168
1H chemical shifts	168

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DHFR	1
2	Folate	2

Entities:

Entity 1, DHFR 187 residues - Formula weight is not available

1

MET

VAL

GLY

SER

LEU

ASN

CYS

ILE

VAL

ALA

2

VAL

SER

GLN

ASN

MET

GLY

ILE

GLY

LYS

ASN

3

GLY

ASP

LEU

PRO

TRP

PRO

LEU

ARG

ASN

4

GLU

PHE

ARG

TYR

PHE

GLN

ARG

MET

THR

5

THR

SER

VAL

GLU

GLY

LYS

GLN

ASN

LEU

6

VAL

ILE

MET

GLY

LYS

THR

TRP

PHE

SER

7

ILE

PRO

GLU

LYS

ASN

ARG

PRO

LEU

LYS

GLY

8

ARG

ILE

ASN

LEU

VAL

LEU

SER

ARG

GLU

LEU

9

LYS

GLU

PRO

GLN

GLY

ALA

HIS

PHE

LEU

10

SER

ARG

SER

LEU

ASP

ALA

LEU

LYS

LEU

11

THR

GLU

GLN

PRO

GLU

LEU

ALA

ASN

LYS

VAL

12

ASP

MET

VAL

TRP

ILE

VAL

GLY

SER

13

VAL

TYR

LYS

GLU

ALA

MET

ASN

HIS

PRO

GLY

14

HIS

LEU

LYS

LEU

PHE

VAL

THR

ARG

ILE

MET

15

GLN

ASP

PHE

GLU

SER

ASP

THR

PHE

PRO

16

GLU

ILE

ASP

LEU

GLU

LYS

TYR

LYS

LEU

17

PRO

GLU

TYR

PRO

GLY

VAL

LEU

SER

ASP

VAL

18

GLN

GLU

LYS

GLY

ILE

LYS

TYR

LYS

PHE

19

GLU

VAL

TYR

GLU

LYS

ASN

ASP

Entity 2, Folate - 441.397 Da.

1

FOL

Samples:

sample_1: DHFR, [U-99% 15N], 1000 uM; potassium phosphate 50 mM; potassium chloride 50 mM; EDTA 1 mM; DTT 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 750 MHz
Bruker DRX 600 MHz

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