BMRB Entry 18801

Title:
The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus   PubMed: 27349962
Deposition date:
2012-10-22
Original release date:
2014-04-21
Authors:
Lederer, Christoph; Bayer, Peter
Citation:

Citation: Hoppstock, Lukas; Trusch, Franziska; Lederer, Christoph; van West, Pieter; Koenneke, Martin; Bayer, Peter. "NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase"  BMC Biol. 14, 53-53 (2016).

Assembly members:

Assembly members:
entity, polymer, 93 residues, 10198.002 Da.

Natural source:

Natural source:   Common Name: Nitrosopumilus maritimus   Taxonomy ID: 338192   Superkingdom: Archaea   Kingdom: not available   Genus/species: Nitrosopumilus maritimus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41 (a-c)

Experimental source:

Natural source:   Common Name: Nitrosopumilus maritimus   Taxonomy ID: 338192   Superkingdom: Archaea   Kingdom: not available   Genus/species: Nitrosopumilus maritimus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41 (a-c)

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts94
1H chemical shifts646

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NmPin1

Entities:

Entity 1, NmPin 93 residues - 10198.002 Da.

1   GLYPROSERASNLYSILELYSCYSSERHIS
2   ILELEUVALSERLYSGLNSERGLUALALEU
3   ALAILEMETGLULYSLEULYSSERGLYGLU
4   LYSPHEGLYLYSLEUALALYSGLULEUSER
5   ILEASPSERGLYSERALALYSLYSASNGLY
6   ASNLEUGLYTYRPHETHRLYSGLYMETMET
7   VALLYSPROPHEGLUASPALAALAPHELYS
8   LEUGLNVALGLYGLUVALSERGLUPROILE
9   LYSSERGLUPHEGLYTYRHISILEILELYS
10   ARGPHEGLY

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 50 mM; DSS 2 uM

sample_2: entity, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 50 mM; DSS 2 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 301.5 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

CCPN v2.1, CCPN - chemical shift assignment, chemical shift calculation, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - data analysis, refinement, structure solution

WhatIF, Vriend - refinement

NMR spectrometers:

  • Bruker Ultrashield 700 MHz

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