BMRB Entry 16240

Title:
Solution structure of full-length SlyD from E.coli   PubMed: 19760519
Deposition date:
2009-04-03
Original release date:
2009-09-24
Authors:
Martino, Luigi; Kelly, Geoff; Conte, Maria
Citation:

Citation: Martino, Luigi; Kelly, Geoff; Conte, Maria. "Resonance assignment of SlyD from E. coli"  Biomol. NMR Assignments 3, 235-237 (2009).

Assembly members:

Assembly members:
SlyD, polymer, 196 residues, 20883.012 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE60

Experimental source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE60

Data sets:
Data typeCount
13C chemical shifts609
15N chemical shifts148
1H chemical shifts920

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SlyD1

Entities:

Entity 1, SlyD 196 residues - 20883.012 Da.

Full length native protein

1   METLYSVALALALYSASPLEUVALVALSER
2   LEUALATYRGLNVALARGTHRGLUASPGLY
3   VALLEUVALASPGLUSERPROVALSERALA
4   PROLEUASPTYRLEUHISGLYHISGLYSER
5   LEUILESERGLYLEUGLUTHRALALEUGLU
6   GLYHISGLUVALGLYASPLYSPHEASPVAL
7   ALAVALGLYALAASNASPALATYRGLYGLN
8   TYRASPGLUASNLEUVALGLNARGVALPRO
9   LYSASPVALPHEMETGLYVALASPGLULEU
10   GLNVALGLYMETARGPHELEUALAGLUTHR
11   ASPGLNGLYPROVALPROVALGLUILETHR
12   ALAVALGLUASPASPHISVALVALVALASP
13   GLYASNHISMETLEUALAGLYGLNASNLEU
14   LYSPHEASNVALGLUVALVALALAILEARG
15   GLUALATHRGLUGLUGLULEUALAHISGLY
16   HISVALHISGLYALAHISASPHISHISHIS
17   ASPHISASPHISASPGLYCYSCYSGLYGLY
18   HISGLYHISASPHISGLYHISGLUHISGLY
19   GLYGLUGLYCYSCYSGLYGLYLYSGLYASN
20   GLYGLYCYSGLYCYSHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 – 0.9 mM; TRIS 20 mM; potassium chloride 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.25; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15950
PDB
DBJ BAB37623 BAE77942 BAG79134 BAH65509 BAI27607
EMBL CAA79705 CAD08158 CAP77801 CAQ33668 CAQ90798
GB AAA18574 AAA58146 AAC41458 AAC76374 AAG58456
PIR AB1004
REF NP_312227 NP_417808 NP_458445 NP_462359 NP_709123
SP P0A9K9 P0A9L0 P0A9L1 P0A9L2
AlphaFold P0A9L1

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