BMRB Entry 19047

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19047
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII
Deposition date:
2013-02-20
Original release date:
2013-08-14
Authors:
Karsisiotis, Andreas Ioannis; Damblon, Christian; Roberts, Gordon
Citation:

Citation: Karsisiotis, Andreas Ioannis; Damblon, Christian; Roberts, Gordon. "Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-beta-lactamase and its complex with the inhibitor R-thiomandelic acid"  Biomol. NMR Assign. ., .-. (2013).
PubMed: 23838816

Assembly members:

Assembly members:
BcII, polymer, 227 residues, 24995.738 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Firmicutes   Taxonomy ID: 1396   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus cereus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9a/BCII

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BcII: SQKVEKTVIKNETGTISISQ LNKNVWVHTELGSFNGEAVP SNGLVLNTSKGLVLVDSSWD DKLTKELIEMVEKKFQKRVT DVIITHAHADRIGGIKTLKE RGIKAHSTALTAELAKKNGY EEPLGDLQTVTNLKFGNMKV ETFYPGKGHTEDNIVVWLPQ YNILVGGCLVKSTSAKDLGN VADAYVNEWSTSIENVLKRY RNINAVVPGHGEVGDKGLLL HTLDLLK

Data sets:
Data typeCount
13C chemical shifts710
15N chemical shifts235
1H chemical shifts3129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BcII1
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, BcII 227 residues - 24995.738 Da.

1   SERGLNLYSVALGLULYSTHRVALILELYS
2   ASNGLUTHRGLYTHRILESERILESERGLN
3   LEUASNLYSASNVALTRPVALHISTHRGLU
4   LEUGLYSERPHEASNGLYGLUALAVALPRO
5   SERASNGLYLEUVALLEUASNTHRSERLYS
6   GLYLEUVALLEUVALASPSERSERTRPASP
7   ASPLYSLEUTHRLYSGLULEUILEGLUMET
8   VALGLULYSLYSPHEGLNLYSARGVALTHR
9   ASPVALILEILETHRHISALAHISALAASP
10   ARGILEGLYGLYILELYSTHRLEULYSGLU
11   ARGGLYILELYSALAHISSERTHRALALEU
12   THRALAGLULEUALALYSLYSASNGLYTYR
13   GLUGLUPROLEUGLYASPLEUGLNTHRVAL
14   THRASNLEULYSPHEGLYASNMETLYSVAL
15   GLUTHRPHETYRPROGLYLYSGLYHISTHR
16   GLUASPASNILEVALVALTRPLEUPROGLN
17   TYRASNILELEUVALGLYGLYCYSLEUVAL
18   LYSSERTHRSERALALYSASPLEUGLYASN
19   VALALAASPALATYRVALASNGLUTRPSER
20   THRSERILEGLUASNVALLEULYSARGTYR
21   ARGASNILEASNALAVALVALPROGLYHIS
22   GLYGLUVALGLYASPLYSGLYLEULEULEU
23   HISTHRLEUASPLEULEULYS

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: BcII, [U-99% 15N], 1 mM; MES 20 mM; Zinc Chloride 0.2 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: BcII, [U-99% 13C; U-99% 15N], 1 mM; MES 20 mM; Zinc Chloride 0.2 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HBHANHsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

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

CANDID, Herrmann, Guntert and Wuthrich - automated NOE assignment, structure solution

SPARKY, Goddard - data analysis, peak picking

Molmol, Koradi, Billeter and Wuthrich - data analysis

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

TOPSPIN, Bruker Biospin - collection, processing

xwinnmr, Bruker Biospin - collection

ProcheckNMR, Laskowski and MacArthur - validation

WhatIF, Vriend - validation

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

GB M11189 AAA22276 AGE79265 AHX19465 AHZ52262 AIA18213
GenPept AAA22276
BMRB 19048
PDB
EMBL CGG57718 COF89432 COP86624 COR95834 CRG01336
REF WP_000742467 WP_000742468 WP_000742469 WP_000742470 WP_000742471
SP P04190
AlphaFold P04190