BMRB Entry 18801

Name: The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus
Published: 2014-04-21

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PDB ID: 2m08
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18801
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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

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

Entity Sequences (FASTA):
entity: GPSNKIKCSHILVSKQSEAL AIMEKLKSGEKFGKLAKELS IDSGSAKKNGNLGYFTKGMM VKPFEDAAFKLQVGEVSEPI KSEFGYHIIKRFG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	94
1H chemical shifts	646

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NmPin	1

Entities:

Entity 1, NmPin 93 residues - 10198.002 Da.

1

GLY

PRO

SER

ASN

LYS

ILE

LYS

CYS

SER

HIS

2

ILE

LEU

VAL

SER

LYS

GLN

SER

GLU

ALA

LEU

3

ALA

ILE

MET

GLU

LYS

LEU

LYS

SER

GLY

GLU

4

LYS

PHE

GLY

LYS

LEU

ALA

LYS

GLU

LEU

SER

5

ILE

ASP

SER

GLY

SER

ALA

LYS

ASN

GLY

6

ASN

LEU

GLY

TYR

PHE

THR

LYS

GLY

MET

7

VAL

LYS

PRO

PHE

GLU

ASP

ALA

PHE

LYS

8

LEU

GLN

VAL

GLY

GLU

VAL

SER

GLU

PRO

ILE

9

LYS

SER

GLU

PHE

GLY

TYR

HIS

ILE

LYS

10

ARG

PHE

GLY

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts