BMRB Entry 6838

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR6838

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Title:
1H, 13C and 15N backbone resonance assignment for PSE-4, a 29.5 kDa class A beta-lactamase from Pseudomonas aeruginosa
Deposition date:
2008-10-08
Original release date:
2006-05-02
Authors:
Morin, Sebastien; Levesque, Roger; Gagne, Stephane
Citation:

Citation: Morin, Sebastien; Gagne, Stephane. "NMR dynamics of PSE-4 beta-lactamase: an interplay of ps-ns order and mus-ms motions in the active site"  Biophys. J. 96, 4681-4691 (2009).
PubMed: 19486690

Assembly members:

Assembly members:
PSE-4_mature_enzyme, polymer, 271 residues, 29527.2 Da.

Natural source:

Natural source:   Common Name: P. aeruginosa   Taxonomy ID: 287   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Pseudomonas Aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEt24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PSE-4_mature_enzyme: SSSKFQQVEQDVKAIEVSLS ARIGVSVLDTQNGEYWDYNG NQRFPLTSTFKTIACAKLLY DAEQGKVNPNSTVEIKKADL VTYSPVIEKQVGQAITLDDA CFATMTTSDNTAANIILSAV GGPKGVTDFLRQIGDKETRL DRIEPDLNEGKLGDLRDTTT PKAIASTLNKFLFGSALSEM NQKKLESWMVNNQVTGNLLR SVLPAGWNIADRSGAGGFGA RSITAVVWSEHQAPIIVSIY LAQTQASMEERNDAIVKIGH SIFDVYTSQSR

Data typeCount
13C chemical shifts782
15N chemical shifts258
1H chemical shifts258
heteronuclear NOE values703
H exchange protection factors262
H exchange rates420
order parameters230
T1 relaxation values703
T2 relaxation values701

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PSE-4 mature enzyme1

Entities:

Entity 1, PSE-4 mature enzyme 271 residues - 29527.2 Da.

The numbering scheme starts at 22 and ends up to 295, as in the standard Ambler numbering, with gaps at positions 58, 239 and 253. This is the numbering scheme used in the two crystal structures of PSE-4 (1G68 and 1G6A).

1   SERSERSERLYSPHEGLNGLNVALGLUGLN
2   ASPVALLYSALAILEGLUVALSERLEUSER
3   ALAARGILEGLYVALSERVALLEUASPTHR
4   GLNASNGLYGLUTYRTRPASPTYRASNGLY
5   ASNGLNARGPHEPROLEUTHRSERTHRPHE
6   LYSTHRILEALACYSALALYSLEULEUTYR
7   ASPALAGLUGLNGLYLYSVALASNPROASN
8   SERTHRVALGLUILELYSLYSALAASPLEU
9   VALTHRTYRSERPROVALILEGLULYSGLN
10   VALGLYGLNALAILETHRLEUASPASPALA
11   CYSPHEALATHRMETTHRTHRSERASPASN
12   THRALAALAASNILEILELEUSERALAVAL
13   GLYGLYPROLYSGLYVALTHRASPPHELEU
14   ARGGLNILEGLYASPLYSGLUTHRARGLEU
15   ASPARGILEGLUPROASPLEUASNGLUGLY
16   LYSLEUGLYASPLEUARGASPTHRTHRTHR
17   PROLYSALAILEALASERTHRLEUASNLYS
18   PHELEUPHEGLYSERALALEUSERGLUMET
19   ASNGLNLYSLYSLEUGLUSERTRPMETVAL
20   ASNASNGLNVALTHRGLYASNLEULEUARG
21   SERVALLEUPROALAGLYTRPASNILEALA
22   ASPARGSERGLYALAGLYGLYPHEGLYALA
23   ARGSERILETHRALAVALVALTRPSERGLU
24   HISGLNALAPROILEILEVALSERILETYR
25   LEUALAGLNTHRGLNALASERMETGLUGLU
26   ARGASNASPALAILEVALLYSILEGLYHIS
27   SERILEPHEASPVALTYRTHRSERGLNSER
28   ARG

Samples:

sample_1: PSE-4, [U-98% 13C; U-96% 15N], 0.6 mM; DSS 0.1 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 10%; H2O 90%; Protease inhibitors cocktail 0.1 mM

sample_2: PSE-4, [U-91% 2H; U-98% 13C; U-96% 15N], 0.6 mM; DSS 0.1 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 10%; H2O 90%; Protease inhibitors cocktail 0.1 mM

sample_3: PSE-4, [U-98% 13CE]-Lys; [U-98% 15NZ]-Lys; [U-98% 15N]-Thr, 0.6 mM; DSS 0.1 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 10%; H2O 90%; Protease inhibitors cocktail 0.1 mM

sample_4: PSE-4, [U-96% 15N], 0.6 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 10%; H2O 90%

sample_5: PSE-4, [U-96% 15N], 0.5 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 100%

sample_6: PSE-4, [U-96% 15N], 0.5 mM; Imidazole 3 mM; Sodium azide 0.1%; D2O 100%

conditions_1: ionic strength: 0 mM; pH: 6.65; temperature: 303.15 K

conditions_2: ionic strength: 0 mM; pH: 6.65; temperature: 304.65 K

conditions_3: ionic strength: 0 mM; pH: 6.65; temperature: 304.65 K

conditions_4: ionic strength: 0 mM; pH: 7.85; temperature: 304.65 K

Experiments:

NameSampleSample stateSample conditions
15N-TROSY-HSQCsample_1isotropicconditions_1
TROSY-HNCOsample_1isotropicconditions_1
TROSY-HN(CA)COsample_2isotropicconditions_1
TROSY-HNCAsample_1isotropicconditions_1
TROSY-HN(CO)CAsample_1isotropicconditions_1
TROSY-HNCACBsample_2isotropicconditions_1
TROSY-CBCA(CO)NHsample_1isotropicconditions_1
15N-T1sample_4isotropicconditions_2
15N-T2sample_4isotropicconditions_2
1H-15N-NOEsample_4isotropicconditions_2
15N-TROSY-HSQCsample_5isotropicconditions_3
15N-TROSY-HSQCsample_6isotropicconditions_4

Software:

NMRView v5.2.2, One Moon Scientific Inc. - Peak picks and assign chemical shifts.

NMRPipe v2.3, The Ad Bax Group - Process fids.

Smartbotebook v5.0.5, PENCE (The Canadian Protein Engineering Network) - Assign chemical shifts.

VNMR v6.1c, Varian Inc. - Acquire NMR data.

Relax, relax - Study of the dynamics of proteins or other macromolecules through the analysis of NMR relaxation data.

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA02497 BAA24531 BAD02330 BAE54322 BAE71359
EMBL CAA79480 CAG23929 CAH04650 CAZ48630 CCS92734
GB AAA25740 AAA25741 AAA25979 AAB19430 AAC98498
PIR A49789
REF NP_848173 WP_001931474 WP_011113050 WP_029364662 WP_032490377
SP P16897 P37322 Q03170
AlphaFold P16897 P37322 Q03170

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