BMRB Entry 52731

Name: AtPmtA SAH-bound state at 25C
Published: 2025-09-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52731

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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:

AtPmtA SAH-bound state at 25C

Deposition date:

2024-11-28

Original release date:

2025-09-05

Authors:

Kumeta, Hiroyuki; Watanabe, Yasunori; Watanabe, Seiya

Citation:

Citation: Kumeta, Hiroyuki; Watanabe, Yasunori; Watanabe, Seiya. "Structural basis for phosphatidylcholine synthesis by bacterial phospholipid N-methyltransferases" J. Biol. Chem. 301, 108507-108507 (2025).
PubMed: 40222548

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, Formula weight is not available
entity_SAH, non-polymer, 384.411 Da.

Natural source:

Natural source: Common Name: Agrobacterium tumefaciens Taxonomy ID: 358 Superkingdom: Bacteria Kingdom: not available Genus/species: Agrobacterium tumefaciens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETDuet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPQPKKVGAIVPTSSITAKK MASVINPHSGLPVLELGPGT GVITKAILARGIKPESLTAI EYSTDFYNQLLRSYPGVNFV NGDAFDLDATLGEHKGQMFD SVISAVPMLNFPMAARIKLL DELLKRVPHGRPVVQISYGP ISPIVAQPHLYHIRHFDFIV RNIPPAQLWTYTRA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	152
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AtPmtA deltaN25	1
2	SAH	2

Entities:

Entity 1, AtPmtA deltaN25 174 residues - Formula weight is not available

1

GLY

PRO

GLN

PRO

LYS

VAL

GLY

ALA

ILE

2

VAL

PRO

THR

SER

ILE

THR

ALA

LYS

3

MET

ALA

SER

VAL

ILE

ASN

PRO

HIS

SER

GLY

4

LEU

PRO

VAL

LEU

GLU

LEU

GLY

PRO

GLY

THR

5

GLY

VAL

ILE

THR

LYS

ALA

ILE

LEU

ALA

ARG

6

GLY

ILE

LYS

PRO

GLU

SER

LEU

THR

ALA

ILE

7

GLU

TYR

SER

THR

ASP

PHE

TYR

ASN

GLN

LEU

8

LEU

ARG

SER

TYR

PRO

GLY

VAL

ASN

PHE

VAL

9

ASN

GLY

ASP

ALA

PHE

ASP

LEU

ASP

ALA

THR

10

LEU

GLY

GLU

HIS

LYS

GLY

GLN

MET

PHE

ASP

11

SER

VAL

ILE

SER

ALA

VAL

PRO

MET

LEU

ASN

12

PHE

PRO

MET

ALA

ARG

ILE

LYS

LEU

13

ASP

GLU

LEU

LYS

ARG

VAL

PRO

HIS

GLY

14

ARG

PRO

VAL

GLN

ILE

SER

TYR

GLY

PRO

15

ILE

SER

PRO

ILE

VAL

ALA

GLN

PRO

HIS

LEU

16

TYR

HIS

ILE

ARG

HIS

PHE

ASP

PHE

ILE

VAL

17

ARG

ASN

ILE

PRO

ALA

GLN

LEU

TRP

THR

18

TYR

THR

ARG

ALA

Entity 2, SAH - C14 H20 N6 O5 S - 384.411 Da.

1

SAH

Samples:

sample_1: AtPmtA deltaN25, [U-99% 13C; U-99% 15N], 0.3 mM; SAH 3 mM; DMSO, [U-99% 2H], 10%; HEPES 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.7 - collection

NMRPipe v8.3 - processing

SPARKY v3.113 - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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