BMRB Entry 15371

Name: antimicrobial resistance protein
Published: 2008-08-18

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PDB ID: 2jso
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15371
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:

antimicrobial resistance protein

Deposition date:

2007-07-10

Original release date:

2008-08-18

Authors:

Jin, Changwen; Fu, Wenyu

Citation:

Citation: Fu, Wenyu; Yang, Fan; Kang, Xue; Zhang, Xinxin; Li, You; Xia, Bin; Jin, Changwen. "First structure of the polymyxin resistance proteins" Biochem. Biophys. Res. Commun. 361, 1033-1037 (2007).
PubMed: 17686460

Assembly members:

Assembly members:
antimicrobial_resistance_protein, polymer, 88 residues, 9887.615 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
antimicrobial_resistance_protein: MEWLVKKSCCNKQDNRHVLM LCDAGGAIKMIAEVKSDFAV KVGDLLSPLQNALYCINREK LHTVKVLSASSYSPDEWERQ CKVAGKTQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	368
15N chemical shifts	95
1H chemical shifts	591

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	antimicrobial resistance protein	1

Entities:

Entity 1, antimicrobial resistance protein 88 residues - 9887.615 Da.

1

MET

GLU

TRP

LEU

VAL

LYS

SER

CYS

2

ASN

LYS

GLN

ASP

ASN

ARG

HIS

VAL

LEU

MET

3

LEU

CYS

ASP

ALA

GLY

ALA

ILE

LYS

MET

4

ILE

ALA

GLU

VAL

LYS

SER

ASP

PHE

ALA

VAL

5

LYS

VAL

GLY

ASP

LEU

SER

PRO

LEU

GLN

6

ASN

ALA

LEU

TYR

CYS

ILE

ASN

ARG

GLU

LYS

7

LEU

HIS

THR

VAL

LYS

VAL

LEU

SER

ALA

SER

8

SER

TYR

SER

PRO

ASP

GLU

TRP

GLU

ARG

GLN

9

CYS

LYS

VAL

ALA

GLY

LYS

THR

GLN

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-labeled	isotropic	sample_conditions_1
2D 1H-13C HSQC	15N_13C-labeled	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C-labeled	isotropic	sample_conditions_1
3D HNCO	15N_13C-labeled	isotropic	sample_conditions_1
3D HNCA	15N_13C-labeled	isotropic	sample_conditions_1
3D HNCACB	15N_13C-labeled	isotropic	sample_conditions_1
3D HBHA(CO)NH	15N_13C-labeled	isotropic	sample_conditions_1
3D HN(CO)CA	15N_13C-labeled	isotropic	sample_conditions_1
3D HCCH-TOCSY	15N_13C-labeled	isotropic	sample_conditions_1
3D HNHA	15N_13C-labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_13C-labeled	isotropic	sample_conditions_1
3D 1H-13C NOESY	15N_13C-labeled	isotropic	sample_conditions_1
3D HCCH-COSY	15N_13C-labeled	isotropic	sample_conditions_1

PDB	2JSO 4HN7
DBJ	BAA16079 BAB36570 BAG78043 BAI26457 BAI31496
EMBL	CAQ32662 CAQ99179 CAR13784 CAU98375 CBG35335
GB	AAC75319 AAG57391 AAG57392 AAV92796 AAV92797
REF	NP_311174 NP_416762 WP_000854949 WP_001295285 WP_001297080
SP	P37590
AlphaFold	P37590

BMRB Entry 15371

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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