BMRB Entry 34546

Name: Emfourin (M4in) from Serratia proteamaculans, M4 family peptidase inhibitor
Published: 2021-08-31

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PDB ID: 6zyg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34546
MolProbity Validation Chart

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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:

Emfourin (M4in) from Serratia proteamaculans, M4 family peptidase inhibitor

Deposition date:

2020-07-31

Original release date:

2021-08-31

Authors:

Bozin, T.; Chukhontseva, K.; Konarev, P.; Bocharov, E.; Demidyuk, I.

Citation:

Citation: Bozin, Timur; Berdyshev, Igor; Chukhontseva, Ksenia; Karaseva, Maria; Konarev, Petr; Varizhuk, Anna; Lesovoy, Dmitry; Arseniev, Alexander; Kostrov, Sergey; Bocharov, Eduard; Demidyuk, Ilya. "NMR structure of emfourin, a novel protein metalloprotease inhibitor: Insights into the mechanism of action" J. Biol. Chem. 299, 104585-104585 (2023).
PubMed: 36889586

Assembly members:

Assembly members:
entity_1, polymer, 113 residues, 12748.350 Da.

Natural source:

Natural source: Common Name: Serratia proteamaculans Taxonomy ID: 28151 Superkingdom: Bacteria Kingdom: not available Genus/species: Serratia proteamaculans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET23c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKPLPVLNQDTVIELAREGG FAFIPKLAGQRRIALADITP EQRQRLNQLLNQTLPYAQEE GQPDSPGSGDQRYFRVQISY YSQTLRSEIVLLIPETSAPQ ALVDLWKTGQVDE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	522
15N chemical shifts	125
1H chemical shifts	833

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 113 residues - 12748.350 Da.

1

MET

LYS

PRO

LEU

PRO

VAL

LEU

ASN

GLN

ASP

2

THR

VAL

ILE

GLU

LEU

ALA

ARG

GLU

GLY

3

PHE

ALA

PHE

ILE

PRO

LYS

LEU

ALA

GLY

GLN

4

ARG

ILE

ALA

LEU

ALA

ASP

ILE

THR

PRO

5

GLU

GLN

ARG

GLN

ARG

LEU

ASN

GLN

LEU

6

ASN

GLN

THR

LEU

PRO

TYR

ALA

GLN

GLU

7

GLY

GLN

PRO

ASP

SER

PRO

GLY

SER

GLY

ASP

8

GLN

ARG

TYR

PHE

ARG

VAL

GLN

ILE

SER

TYR

9

TYR

SER

GLN

THR

LEU

ARG

SER

GLU

ILE

VAL

10

LEU

ILE

PRO

GLU

THR

SER

ALA

PRO

GLN

11

ALA

LEU

VAL

ASP

LEU

TRP

LYS

THR

GLY

GLN

12

VAL

ASP

GLU

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 0.37 mM; Na2HPO4 5.76 mM; NaH2PO4 12.24 mM; TMSP 1.5 mM; NaN3 0.05%

sample_conditions_1: ionic strength: 35 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 35 mM; pH: 6.5; pressure: 1 atm; temperature: 300 K

sample_conditions_3: ionic strength: 35 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_4: ionic strength: 35 mM; pH: 6.5; pressure: 1 atm; temperature: 305 K

sample_conditions_5: ionic strength: 35 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_4
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_5
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_3
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_3
3D HNCO	sample_1	isotropic	sample_conditions_3
3D HN(CA)CO	sample_1	isotropic	sample_conditions_3
3D HNCA	sample_1	isotropic	sample_conditions_3
3D HN(CO)CA	sample_1	isotropic	sample_conditions_3
3D HNCACB	sample_1	isotropic	sample_conditions_3
3D HNHA	sample_1	isotropic	sample_conditions_3
3D HNHB	sample_1	isotropic	sample_conditions_3
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_3
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_3
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_3
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_3
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_3
2D 1H-15N TROSY-HSQC	sample_1	isotropic	sample_conditions_3
2D 1H-13C HSQC aliphatic, constant time	sample_1	isotropic	sample_conditions_3
2D 1H-13C HSQC aromatic, constant time	sample_1	isotropic	sample_conditions_3
2D 1H-13C{15N} spin-echo difference CT-HSQC, experiment to measure J(C-N)	sample_1	isotropic	sample_conditions_3
2D 1H-13C{13CO} spin-echo difference CT-HSQC, experiment to measure J(C-CO)	sample_1	isotropic	sample_conditions_3
2D 1H-13C{13CA} spin-echo difference CT-HSQC, experiment to measure J(CD-CA)	sample_1	isotropic	sample_conditions_3

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

MOLMOL, Koradi, Billeter and Wuthrich - data analysis

TALOS-N, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker AVANCE 600 MHz

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