BMRB Entry 18196

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18196

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Title:
Backbone assignment for an intracellular proteinase inhibitor of Bacillus Subtilis
Deposition date:
2012-01-14
Original release date:
2012-05-22
Authors:
Li, Qingxin; Chen, Angela Shuyi; Gayen, Shovanlal
Citation:

Citation: Li, Qingxin; Chen, Angela Shuyi; Gayen, Shovanlal; Kang, Congbao. "1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis."  Biomol. NMR Assignments 7, 129-132 (2013).
PubMed: 22585087

Assembly members:

Assembly members:
proteinase_inhibitor, polymer, 127 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   Host organism: Escherichia coli   Vector: pET29B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
proteinase_inhibitor: MGHHHHHHMENQEVVLSIDA IQEPEQIKFNMSLKNQSERA IEFQFSTGQKFELVVYDSEH KERYRYSKEKMFTQAFQNLT LESGETYDFSDVWKEVPEPG TYEVKVTFKGRAENLKQVQA VQQFEVK

Data sets:
Data typeCount
13C chemical shifts451
15N chemical shifts125
1H chemical shifts560

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1proteinase inhibitor1

Entities:

Entity 1, proteinase inhibitor 127 residues - Formula weight is not available

the first 8 residues was not shown

1   METGLYHISHISHISHISHISHISMETGLU
2   ASNGLNGLUVALVALLEUSERILEASPALA
3   ILEGLNGLUPROGLUGLNILELYSPHEASN
4   METSERLEULYSASNGLNSERGLUARGALA
5   ILEGLUPHEGLNPHESERTHRGLYGLNLYS
6   PHEGLULEUVALVALTYRASPSERGLUHIS
7   LYSGLUARGTYRARGTYRSERLYSGLULYS
8   METPHETHRGLNALAPHEGLNASNLEUTHR
9   LEUGLUSERGLYGLUTHRTYRASPPHESER
10   ASPVALTRPLYSGLUVALPROGLUPROGLY
11   THRTYRGLUVALLYSVALTHRPHELYSGLY
12   ARGALAGLUASNLEULYSGLNVALGLNALA
13   VALGLNGLNPHEGLUVALLYS

Samples:

sample_1: proteinase inhibitor, [U-100% 13C; U-100% 15N], 0.8 – 1 mM; H2O 90%; D2O 10%; NaCl 150 mM; NaPO4 20 mM; DTT 1 mM

sample_2: proteinase inhibitor 1 mM; D2O 100%; NaCl 150 mM; NaPO4 20 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView v5.2, Johnson, One Moon Scientific - data analysis

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA03820 BAI84659 BAM50030 BAM57298 GAK79757
EMBL CAA70631 CAB01835 CAB12953 CCU57578 CEI56247
GB ADV96100 AFQ57029 AGA21547 AGE62965 AGG60464
REF NP_388994 WP_003244660 WP_010886475 WP_014479419 WP_015483077
SP P39804
AlphaFold P39804

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