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 17318

Title: NMR solution structure of the protein YP_001092504.1

Deposition date: 2010-11-23 Original release date: 2010-12-16

Authors: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt. "NMR solution structure of the protein YP_001092504.1"  Not known ., .-..

Assembly members:
YP_001092504.1, polymer, 132 residues, 14833.001 Da.

Natural source:   Common Name: Shewanella loihica PV-4   Taxonomy ID: 323850   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shewanella loihica

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

Entity Sequences (FASTA):
YP_001092504.1: GMTPQSDTPKVTGLKLKRKS RQLEISFDNGQQFTLSCELL RVYSPSAEVHGHGNPVLVTH KKNVNINAITPVGNYAVKLV FDDGHDTGLYSWKVLYDLAS NQVDLWENYLARLRAAKASR EPLIDMAVKYHT

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts140
1H chemical shifts933

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_001092504.11

Entities:

Entity 1, YP_001092504.1 132 residues - 14833.001 Da.

1   GLYMETTHRPROGLNSERASPTHRPROLYS
2   VALTHRGLYLEULYSLEULYSARGLYSSER
3   ARGGLNLEUGLUILESERPHEASPASNGLY
4   GLNGLNPHETHRLEUSERCYSGLULEULEU
5   ARGVALTYRSERPROSERALAGLUVALHIS
6   GLYHISGLYASNPROVALLEUVALTHRHIS
7   LYSLYSASNVALASNILEASNALAILETHR
8   PROVALGLYASNTYRALAVALLYSLEUVAL
9   PHEASPASPGLYHISASPTHRGLYLEUTYR
10   SERTRPLYSVALLEUTYRASPLEUALASER
11   ASNGLNVALASPLEUTRPGLUASNTYRLEU
12   ALAARGLEUARGALAALALYSALASERARG
13   GLUPROLEUILEASPMETALAVALLYSTYR
14   HISTHR

Samples:

sample_1: sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; Protein-YP_001092504.1, [U-98% 13C; U-98% 15N], 1.2 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
2D 1H-13C 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
15 N {1H} - NOEsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

UNIO v2.0.1, Herrmann and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - energy refinement

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - Acquisition, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ABO22245 KIO35783
REF WP_011864179 WP_041510794

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