BMRB Entry 25860

Name: Backbone resonance assignments for S. aureus DHFR complexed with NADPH and Trimethoprim
Published: 2015-12-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25860

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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:

Backbone resonance assignments for S. aureus DHFR complexed with NADPH and Trimethoprim

Deposition date:

2015-10-26

Original release date:

2015-12-01

Authors:

Sahasrabudhe, Parag

Citation:

Citation: Sahasrabudhe, Parag. "Driving Drug Discovery with Biophysical Information Application to Staphylococcus aureus Dihydrofolate Reductase (DHFR)" .

Assembly members:

Assembly members:
DHFR, polymer, 158 residues, Formula weight is not available
entity_NDP, non-polymer, 745.421 Da.
entity_TOP, non-polymer, 290.318 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: NA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DHFR: TLSILVAHDLQRVIGFENQL PWHLPNDLKHVKKLSTGHTL VMGRKTFESIGKPLPNRRNV VLTSDTSFNVEGVDVIHSIE DIYQLPGHVFIFGGQTLFEE MIDKVDDMYITVIEGKFRGD TFFPPYTFEDWEVASSVEGK LDEKNTIPHTFLHLIRKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	435
15N chemical shifts	144
1H chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DHFR	1
2	NADPH	2
3	TRIMETHOPRIM	3

Entities:

Entity 1, DHFR 158 residues - Formula weight is not available

1

THR

LEU

SER

ILE

LEU

VAL

ALA

HIS

ASP

LEU

2

GLN

ARG

VAL

ILE

GLY

PHE

GLU

ASN

GLN

LEU

3

PRO

TRP

HIS

LEU

PRO

ASN

ASP

LEU

LYS

HIS

4

VAL

LYS

LEU

SER

THR

GLY

HIS

THR

LEU

5

VAL

MET

GLY

ARG

LYS

THR

PHE

GLU

SER

ILE

6

GLY

LYS

PRO

LEU

PRO

ASN

ARG

ASN

VAL

7

VAL

LEU

THR

SER

ASP

THR

SER

PHE

ASN

VAL

8

GLU

GLY

VAL

ASP

VAL

ILE

HIS

SER

ILE

GLU

9

ASP

ILE

TYR

GLN

LEU

PRO

GLY

HIS

VAL

PHE

10

ILE

PHE

GLY

GLN

THR

LEU

PHE

GLU

11

MET

ILE

ASP

LYS

VAL

ASP

MET

TYR

ILE

12

THR

VAL

ILE

GLU

GLY

LYS

PHE

ARG

GLY

ASP

13

THR

PHE

PRO

TYR

THR

PHE

GLU

ASP

14

TRP

GLU

VAL

ALA

SER

VAL

GLU

GLY

LYS

15

LEU

ASP

GLU

LYS

ASN

THR

ILE

PRO

HIS

THR

16

PHE

LEU

HIS

LEU

ILE

ARG

LYS

Entity 2, NADPH - C21 H30 N7 O17 P3 - 745.421 Da.

1

NDP

Entity 3, TRIMETHOPRIM - C14 H18 N4 O3 - 290.318 Da.

1

TOP

Samples:

sample_1: DHFR, [U-99% 13C; U-99% 15N], 0.250 mM; NADPH 1 mM; Trimethoprim 0.5 mM; HEPES, [U-2H], 10 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker DRX 600 MHz

UNP	P0A017
AlphaFold	P10167