BMRB Entry 15371

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PDB ID:
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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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:
Data typeCount
13C chemical shifts368
15N chemical shifts95
1H chemical shifts591

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1antimicrobial resistance protein1

Entities:

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

1   METGLUTRPLEUVALLYSLYSSERCYSCYS
2   ASNLYSGLNASPASNARGHISVALLEUMET
3   LEUCYSASPALAGLYGLYALAILELYSMET
4   ILEALAGLUVALLYSSERASPPHEALAVAL
5   LYSVALGLYASPLEULEUSERPROLEUGLN
6   ASNALALEUTYRCYSILEASNARGGLULYS
7   LEUHISTHRVALLYSVALLEUSERALASER
8   SERTYRSERPROASPGLUTRPGLUARGGLN
9   CYSLYSVALALAGLYLYSTHRGLN

Samples:

15N-labeled: antimicrobial resistance protein, [U-100% 15N], 1 mM

15N_13C-labeled: antimicrobial resistance protein, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 80 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-labeledisotropicsample_conditions_1
2D 1H-13C HSQC15N_13C-labeledisotropicsample_conditions_1
3D CBCA(CO)NH15N_13C-labeledisotropicsample_conditions_1
3D HNCO15N_13C-labeledisotropicsample_conditions_1
3D HNCA15N_13C-labeledisotropicsample_conditions_1
3D HNCACB15N_13C-labeledisotropicsample_conditions_1
3D HBHA(CO)NH15N_13C-labeledisotropicsample_conditions_1
3D HN(CO)CA15N_13C-labeledisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C-labeledisotropicsample_conditions_1
3D HNHA15N_13C-labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N_13C-labeledisotropicsample_conditions_1
3D 1H-13C NOESY15N_13C-labeledisotropicsample_conditions_1
3D HCCH-COSY15N_13C-labeledisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - peak picking

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v7.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
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

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