BMRB Entry 6649

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PDB ID: 1x60
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6649
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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:

Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC: Characterization of the sporulation-related repeats by NMR

Deposition date:

2005-05-26

Original release date:

2005-12-05

Authors:

Mishima, M.; Shida, T.; Yabuki, K.; Kato, K.; Sekiguchi, J.; Kojima, C.

Citation:

Citation: Mishima, M.; Shida, T.; Yabuki, K.; Kato, K.; Sekiguchi, J.; Kojima, C.. "Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR." Biochemistry 44, 10153-10163 (2005).
PubMed: 16042392

Assembly members:

Assembly members:
Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28), polymer, 79 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28): LKKTSSSGLYKVQIGAFKVK ANADSLASNAEAKGFDSIVL LKDGLYKVQIGAFSSKDNAD TLAARAKNAGFDAIVILES

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	444
13C chemical shifts	212
15N chemical shifts	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sporulation-specific N-acetylmuramoyl-L-alanine amidase	1

Entities:

Entity 1, Sporulation-specific N-acetylmuramoyl-L-alanine amidase 79 residues - Formula weight is not available

1

LEU

LYS

THR

SER

GLY

LEU

TYR

2

LYS

VAL

GLN

ILE

GLY

ALA

PHE

LYS

VAL

LYS

3

ALA

ASN

ALA

ASP

SER

LEU

ALA

SER

ASN

ALA

4

GLU

ALA

LYS

GLY

PHE

ASP

SER

ILE

VAL

LEU

5

LEU

LYS

ASP

GLY

LEU

TYR

LYS

VAL

GLN

ILE

6

GLY

ALA

PHE

SER

LYS

ASP

ASN

ALA

ASP

7

THR

LEU

ALA

ARG

ALA

LYS

ASN

ALA

GLY

8

PHE

ASP

ALA

ILE

VAL

ILE

LEU

GLU

SER

Samples:

sample_1: Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28), [U-15N; U-13C], 1.7 mM; phosphate buffer K 50 mM; D2O 100%

sample_2: Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28), [U-15N], 1.7 mM; phosphate buffer K 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.9; temperature: 303 K; ionic strength: 70 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	not available	not available	not available
3D 15N-separated NOESY	not available	not available	not available

Software:

NMRPipe vver 2.3 - processing

Sparky vver 3.110 - data analysis

CYANA vver 1.05 - structure solution

CNS vver 1.1 - refinement

NMR spectrometers:

Bruker AVANCE 500 MHz

PDB	1X60
DBJ	BAA03500 BAM52388 BAM57964
EMBL	CAA92813 CAB13625 CCU58317 CEI56925 CEJ77332
GB	AEP90898 AFQ57673 AGA23958 AGE63582 AGG61112
REF	NP_389623 WP_003244862 WP_014476879 WP_015252039 WP_015383726
SP	Q06320
AlphaFold	Q06320