BMRB Entry 27593

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27593

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Title:
1H, 13C, and 15N resonance assignments of N-acetylmuramyl-L-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae
Deposition date:
2018-08-29
Original release date:
2018-11-28
Authors:
Young, Brandon; Roth, Braden; Davies, Christopher
Citation:

Citation: Young, Brandon; Roth, Braden; Davies, Christopher. "1H, 13C, and 15N resonance assignments of N-acetylmuramyl-L-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae"  Biomol. NMR Assignments 13, 63-66 (2019).
PubMed: 30276628

Assembly members:

Assembly members:
AmiC-NTD, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Neisseria gonorrhoeae   Taxonomy ID: 485   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria gonorrhoeae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHGK-IF

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AmiC-NTD: SKTVRAPQFTAARIWPSHTY TRLTLESTAALKYQHFALDN PGRLVVDIQNANINTVLHGL SQKVMADDPFIRSIRAGQNT PTTVRLVIDLKQPTHAQVFA LPPVGGFKDRLVVDLYPHGM DADDPMMALLNG

Data sets:
Data typeCount
13C chemical shifts458
15N chemical shifts104
1H chemical shifts650

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1AmiC N-terminal domain1

Entities:

Entity 1, AmiC N-terminal domain 132 residues - Formula weight is not available

AmiC-NTD begins at lysine 29 and extends through glycine 159. The first serine is a byproduct of TEV cleavage site and is denoted as S, -1.

1   SERLYSTHRVALARGALAPROGLNPHETHR
2   ALAALAARGILETRPPROSERHISTHRTYR
3   THRARGLEUTHRLEUGLUSERTHRALAALA
4   LEULYSTYRGLNHISPHEALALEUASPASN
5   PROGLYARGLEUVALVALASPILEGLNASN
6   ALAASNILEASNTHRVALLEUHISGLYLEU
7   SERGLNLYSVALMETALAASPASPPROPHE
8   ILEARGSERILEARGALAGLYGLNASNTHR
9   PROTHRTHRVALARGLEUVALILEASPLEU
10   LYSGLNPROTHRHISALAGLNVALPHEALA
11   LEUPROPROVALGLYGLYPHELYSASPARG
12   LEUVALVALASPLEUTYRPROHISGLYMET
13   ASPALAASPASPPROMETMETALALEULEU
14   ASNGLY

Samples:

AmiC-NTD_triple_label: AmiC-NTD, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 150 uM; sodium chloride 100 mM

AmiC-NTD_15N: AmiC-NTD, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 150 uM; sodium chloride 100 mM

AmiC-NTD_sample_conditions: ionic strength: 120 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
3D HNCOAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
3D CBCA(CO)NHAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
2D 1H-13C HSQCAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
2D 1H-15N HSQCAmiC-NTD_15NisotropicAmiC-NTD_sample_conditions
3D 1H-15N TOCSYAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
3D HBHA(CO)NHAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
3D HcCH-TOCSYAmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions
hCCH-TOCSY(hC_CH.relayed)AmiC-NTD_triple_labelisotropicAmiC-NTD_sample_conditions

Software:

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking

NMRPipe v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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