BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19615

Title: Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase   PubMed: 24484052

Deposition date: 2013-11-15 Original release date: 2014-02-11

Authors: Driscoll, Paul

Citation: Rasheed, Masooma; Richter, Christine; Chisty, Liisa; Kirkpatrick, John; Blackledge, Martin; Webb, Martin; Driscoll, Paul. "Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase."  Biochemistry 53, 1092-1104 (2014).

Assembly members:
PaDDAH_TM, polymer, 254 residues, 28404.2231 Da.

Natural source:   Common Name: Pseudomonas aeruginosa PAO1   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:   Production method: recombinant technology   Host organism: Pseudomonas aeruginosa

Entity Sequences (FASTA):
PaDDAH_TM: MFKHIIARTPARSLVDGLTS SHLGKPDYAKALEQHNAYIE ALQTCDVDITLLPPDERFPD SVFVEDPVLCTSRCAIITRP GAESRRGETEIIEETVQHFY PGKVERIEAPGTVEAGDIMM VGDHFYIGESARTNAEGARQ MIAILEKHGLSGSVVRLEKV LHLKTGLAYLEHNNLLAAGE FVSKPEFQDFNIIEIPEEES YAANCIWVNERVIMPAGYPR TREKIARLGYRVIEVDTSEY RKIDGGVSSMSLRF

Data typeCount
13C chemical shifts481
15N chemical shifts235
1H chemical shifts243

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PaDDAH_TM1

Entities:

Entity 1, PaDDAH_TM 254 residues - 28404.2231 Da.

1   METPHELYSHISILEILEALAARGTHRPRO
2   ALAARGSERLEUVALASPGLYLEUTHRSER
3   SERHISLEUGLYLYSPROASPTYRALALYS
4   ALALEUGLUGLNHISASNALATYRILEGLU
5   ALALEUGLNTHRCYSASPVALASPILETHR
6   LEULEUPROPROASPGLUARGPHEPROASP
7   SERVALPHEVALGLUASPPROVALLEUCYS
8   THRSERARGCYSALAILEILETHRARGPRO
9   GLYALAGLUSERARGARGGLYGLUTHRGLU
10   ILEILEGLUGLUTHRVALGLNHISPHETYR
11   PROGLYLYSVALGLUARGILEGLUALAPRO
12   GLYTHRVALGLUALAGLYASPILEMETMET
13   VALGLYASPHISPHETYRILEGLYGLUSER
14   ALAARGTHRASNALAGLUGLYALAARGGLN
15   METILEALAILELEUGLULYSHISGLYLEU
16   SERGLYSERVALVALARGLEUGLULYSVAL
17   LEUHISLEULYSTHRGLYLEUALATYRLEU
18   GLUHISASNASNLEULEUALAALAGLYGLU
19   PHEVALSERLYSPROGLUPHEGLNASPPHE
20   ASNILEILEGLUILEPROGLUGLUGLUSER
21   TYRALAALAASNCYSILETRPVALASNGLU
22   ARGVALILEMETPROALAGLYTYRPROARG
23   THRARGGLULYSILEALAARGLEUGLYTYR
24   ARGVALILEGLUVALASPTHRSERGLUTYR
25   ARGLYSILEASPGLYGLYVALSERSERMET
26   SERLEUARGPHE

Samples:

Sample1: PaDDAH_TM, [U-100% 13C; U-100% 15N], 700.0 ± 0.05 mM; sodium phosphate 20 mM; NaCl 100 mM; H2O 90%; D2O, [U-100% 2H], 10%

condition1: ionic strength: 0.100 M; pH: 7.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCASample1isotropiccondition1
3D HN(CO)CASample1isotropiccondition1
3D HNCACBSample1isotropiccondition1
3D CBCA(CO)NHSample1isotropiccondition1
2D 1H-15N HSQC/HMQCSample1isotropiccondition1

Software:

ANALYSIS v2.1, CCPN - Assignment

NMRPipe v7.3, Frank Delaglio - Processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts