BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17002

Title: Solution NMR structure of the protein YP_510488.1   PubMed: NA

Deposition date: 2010-06-15 Original release date: 2010-09-02

Authors: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT

Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT. "Solution NMR structure of the protein YP_510488.1"  Not known ., .-..

Assembly members:
entity, polymer, 85 residues, 9367.771 Da.

Natural source:   Common Name: Jannaschia sp. CCS1   Taxonomy ID: 290400   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Jannaschia not available

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

Entity Sequences (FASTA):
entity: GMQFKAEARRNKLMGLWVAE VLGKSGDEANAYAAEVVKAD FEEAGHEDVMRKVLGDLDGK RPEAEVRAKYEGLMAVAKAQ LMDEL

Data sets:
Data typeCount
13C chemical shifts352
15N chemical shifts90
1H chemical shifts595

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_510488.11

Entities:

Entity 1, YP_510488.1 85 residues - 9367.771 Da.

1   GLYMETGLNPHELYSALAGLUALAARGARG
2   ASNLYSLEUMETGLYLEUTRPVALALAGLU
3   VALLEUGLYLYSSERGLYASPGLUALAASN
4   ALATYRALAALAGLUVALVALLYSALAASP
5   PHEGLUGLUALAGLYHISGLUASPVALMET
6   ARGLYSVALLEUGLYASPLEUASPGLYLYS
7   ARGPROGLUALAGLUVALARGALALYSTYR
8   GLUGLYLEUMETALAVALALALYSALAGLN
9   LEUMETASPGLULEU

Samples:

sample_1: PC07345C, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D APSY - HACANHsample_1isotropicsample_conditions_1
5D APSY - HACACONHsample_1isotropicsample_conditions_1
5D APSY - CBCACONHsample_1isotropicsample_conditions_1
15N Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Cali Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Caro Resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - TORSION ANGLE DYNAMICS

UNIO vUNIO2.0.0, Torsten Herrmann - structure solution

TOPSPIN v1.3, Bruker Biospin - processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB ABD55463
REF WP_011455667

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