BMRB Entry 18732

Name: NMR structure of the protein NP_390345.1 from Bacilus subtilis
Published: 2012-10-22

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PDB ID: 2lyx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18732
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Nicholas Rego and David Koes
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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_390345.1 from Bacilus subtilis

Deposition date:

2012-09-21

Original release date:

2012-10-22

Authors:

Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Proudfoot, Andrew; Wuthrich, Kurt. "NMR structure of the protein NP_390345.1 from Bacilus subtilis" .

Assembly members:

Assembly members:
NP_390345.1, polymer, 87 residues, 10333.016 Da.

Natural source:

Natural source: Common Name: Firmicutes 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: pSpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NP_390345.1: GEETPLVTARHMSKWEEIAV KEAKKRYPLAQVLFKQKVWD RKRKDEAVKQYHLTLREGSK EFGVFVTISFDPYSQKVNKI AILEEYQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	324
15N chemical shifts	90
1H chemical shifts	615

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NP_390345.1	1

Entities:

Entity 1, NP_390345.1 87 residues - 10333.016 Da.

1

GLY

GLU

THR

PRO

LEU

VAL

THR

ALA

ARG

2

HIS

MET

SER

LYS

TRP

GLU

ILE

ALA

VAL

3

LYS

GLU

ALA

LYS

ARG

TYR

PRO

LEU

ALA

4

GLN

VAL

LEU

PHE

LYS

GLN

LYS

VAL

TRP

ASP

5

ARG

LYS

ARG

LYS

ASP

GLU

ALA

VAL

LYS

GLN

6

TYR

HIS

LEU

THR

LEU

ARG

GLU

GLY

SER

LYS

7

GLU

PHE

GLY

VAL

PHE

VAL

THR

ILE

SER

PHE

8

ASP

PRO

TYR

SER

GLN

LYS

VAL

ASN

LYS

ILE

9

ALA

ILE

LEU

GLU

TYR

GLN

Samples:

sample_1: NP_390345.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; calcium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G ntert P. - refinement

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LYX
DBJ	BAI85984 BAM52951 BAM58525 GAK78312
EMBL	CAB14396 CCU58980 CEI57685 CEJ78107 CJS87682
GB	ADV93209 AEP91497 AFQ58416 AGA24194 AGE64116
REF	NP_390345 WP_003246051 WP_015384086 WP_017696198 WP_021480018
SP	O32019
AlphaFold	O32019