BMRB Entry 18346

Name: NMR structure of the protein NP_390037.1 from Bacillus subtilis.
Published: 2012-04-30

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PDB ID: 2lr4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18346
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the protein NP_390037.1 from Bacillus subtilis.

Deposition date:

2012-03-22

Original release date:

2012-04-30

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_390037.1 from Bacillus subtilis" .

Assembly members:

Assembly members:
entity, polymer, 128 residues, 14274.345 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAEALPLYYLQITGITSDGN DFAWDNLTSSQTKAPNVLKG NKLYVKARFMGYTKLTVITG KDGKNLLYNGTAKMFKSDAI LGQNKVVIGWDKYFEIPMDA LQDNSIQIKALSSGTTFVYS QKIDFERE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	432
15N chemical shifts	141
1H chemical shifts	926

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NP_390037.1 from Bacillus subtilis	1

Entities:

Entity 1, NP_390037.1 from Bacillus subtilis 128 residues - 14274.345 Da.

1

GLY

ALA

GLU

ALA

LEU

PRO

LEU

TYR

LEU

2

GLN

ILE

THR

GLY

ILE

THR

SER

ASP

GLY

ASN

3

ASP

PHE

ALA

TRP

ASP

ASN

LEU

THR

SER

4

GLN

THR

LYS

ALA

PRO

ASN

VAL

LEU

LYS

GLY

5

ASN

LYS

LEU

TYR

VAL

LYS

ALA

ARG

PHE

MET

6

GLY

TYR

THR

LYS

LEU

THR

VAL

ILE

THR

GLY

7

LYS

ASP

GLY

LYS

ASN

LEU

TYR

ASN

GLY

8

THR

ALA

LYS

MET

PHE

LYS

SER

ASP

ALA

ILE

9

LEU

GLY

GLN

ASN

LYS

VAL

ILE

GLY

TRP

10

ASP

LYS

TYR

PHE

GLU

ILE

PRO

MET

ASP

ALA

11

LEU

GLN

ASP

ASN

SER

ILE

GLN

ILE

LYS

ALA

12

LEU

SER

GLY

THR

PHE

VAL

TYR

SER

13

GLN

LYS

ILE

ASP

PHE

GLU

ARG

GLU

Samples:

sample_1: NP_390037.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.080 M; pH: 6.0; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - geometry optimization, refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, data analysis, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LR4
EMBL	CAB14072 CCU58559 CEI57363 CEJ77788
GB	AAC12986 AFQ58101 AGG61547 AIC40597 AIC44829
REF	NP_046565 NP_390037 WP_003246138 WP_019712873 WP_032725945
SP	O31994
AlphaFold	O31994