BMRB Entry 17646

Title:
Solution structure of the N-terminal domain of human anamorsin
Deposition date:
2011-05-13
Original release date:
2011-06-30
Authors:
Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Boscaro, Francesca; Chatzi, Afroditi; Mikolajczyk, Maciej; Tokatlidis, Kostas; Winkelmann, Julia
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Boscaro, Francesca; Chatzi, Afroditi; Mikolajczyk, Maciej; Tokatlidis, Kostas; Winkelmann, Julia. "Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery."  Chem. Biol. 18, 794-804 (2011).
PubMed: 21700214

Assembly members:

Assembly members:
Anamorsin, polymer, 172 residues, 18539.293 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCOLD-DEST

Data sets:
Data typeCount
13C chemical shifts707
15N chemical shifts181
1H chemical shifts1141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Anamorsin1

Entities:

Entity 1, Anamorsin 172 residues - 18539.293 Da.

This is the N-terminal folded domain (from 1 to 172 residues) of anamorsin

1   METALAASPPHEGLYILESERALAGLYGLN
2   PHEVALALAVALVALTRPASPLYSSERSER
3   PROVALGLUALALEULYSGLYLEUVALASP
4   LYSLEUGLNALALEUTHRGLYASNGLUGLY
5   ARGVALSERVALGLUASNILELYSGLNLEU
6   LEUGLNSERALAHISLYSGLUSERSERPHE
7   ASPILEILELEUSERGLYLEUVALPROGLY
8   SERTHRTHRLEUHISSERALAGLUILELEU
9   ALAGLUILEALAARGILELEUARGPROGLY
10   GLYCYSLEUPHELEULYSGLUPROVALGLU
11   THRALAVALASPASNASNSERLYSVALLYS
12   THRALASERLYSLEUCYSSERALALEUTHR
13   LEUSERGLYLEUVALGLUVALLYSGLULEU
14   GLNARGGLUPROLEUTHRPROGLUGLUVAL
15   GLNSERVALARGGLUHISLEUGLYHISGLU
16   SERASPASNLEULEUPHEVALGLNILETHR
17   GLYLYSLYSPROASNPHEGLUVALGLYSER
18   SERARG

Samples:

sample_1: Anamorsin, [U-100% 15N], 0.5 – 1 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_2: anamorsin, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA v2.0, Keller and Wuthrich - chemical shift assignment

CANDID, Herrmann, Guntert and Wuthrich - automatic NOEs assignment

TALOS, Cornilescu, Delaglio and Bax - Backbone torsion angle calculation

CYANA v1.3, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

ProcheckNMR, Laskowski and MacArthur - data analysis

WhatIF, Vriend - data analysis

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAG58080 BAK62448
GB AAC24311 AAG44562 AAH02568 AAH24196 AAH67303
REF NP_001233553 NP_001295287 NP_064709 XP_003263147 XP_003823791
SP Q6FI81
AlphaFold Q6FI81

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