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 15950

Title: solution structure of E.Coli SlyD   PubMed: 19356587

Deposition date: 2008-09-11 Original release date: 2009-04-02

Authors: Weininger, Ulrich; Balbach, Jochen

Citation: Weininger, Ulrich; Haupt, Caroline; Schweimer, Kristian; Graubner, Wenke; Kovermann, Michael; Bruser, Thomas; Scholz, Christian; Schaarschmidt, Peter; Zoldak, Gabriel; Schmid, Franz; Balbach, Jochen. "NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function"  J. Mol. Biol. 387, 295-305 (2009).

Assembly members:
METHIONINE, polymer, 171 residues, 149.207 Da.

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

Entity Sequences (FASTA):
METHIONINE: MKVAKDLVVSLAYQVRTEDG VLVDESPVSAPLDYLHGHGS LISGLETALEGHEVGDKFDV AVGANDAYGQYDENLVQRVP KDVFMGVDELQVGMRFLAET DQGPVPVEITAVEDDHVVVD GNHMLAGQNLKFNVEVVAIR EATEEELAHGHVHGAHDHHH DHDHDHHHHHH

Data sets:
Data typeCount
13C chemical shifts676
15N chemical shifts168
1H chemical shifts1104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1METHIONINE1

Entities:

Entity 1, METHIONINE 171 residues - 149.207 Da.

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   ASPHISASPHISASPHISHISHISHISHIS
18   HIS

Samples:

sample_1: entity_2, [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16240
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

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