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 18029

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18029

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Title: 1H, 13C, and 15N Chemical Shift Assignments for sf-ALR   PubMed: 21383138

Deposition date: 2011-10-31 Original release date: 2011-11-04

Authors: Ivano, Bertini; Simone, Ciofi-Baffoni; Angelo, Gallo

Citation: Banci, Lucia; Bertini, Ivano; Calderone, Vito; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo; Kallergi, Emmanouela; Lionaki, Eirini; Pozidis, Charalambos; Tokatlidis, Kostas. "Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR."  Proc. Natl. Acad. Sci. U.S.A. 108, 4811-4816 (2011).

Assembly members:
sf-ALR, polymer, 129 residues, 14991.9 Da.
FAD, non-polymer, 785.550 Da.

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

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

Entity Sequences (FASTA):
sf-ALR: GSFTMRTQQKRDTKFREDCP PDREELGRHSWAVLHTLAAY YPDLPTPEQQQDMAQFIHLF SKFYPCEECAEDLRKRLARN HPDTRTRAAFTQWLCHLHNE VNRKLGKPDFDCSKVDERWR DGWKDGSCD

Data sets:
Data typeCount
13C chemical shifts411
15N chemical shifts107
1H chemical shifts503

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sf-ALR, chain 11
2sf-ALR, chain 21
3FAD, 12
4FAD, 22

Entities:

Entity 1, sf-ALR, chain 1 129 residues - 14991.9 Da.

The first four residue (GSFT) are remaining from the TEV cleavage site

1   GLYSERPHETHRMETARGTHRGLNGLNLYS
2   ARGASPTHRLYSPHEARGGLUASPCYSPRO
3   PROASPARGGLUGLULEUGLYARGHISSER
4   TRPALAVALLEUHISTHRLEUALAALATYR
5   TYRPROASPLEUPROTHRPROGLUGLNGLN
6   GLNASPMETALAGLNPHEILEHISLEUPHE
7   SERLYSPHETYRPROCYSGLUGLUCYSALA
8   GLUASPLEUARGLYSARGLEUALAARGASN
9   HISPROASPTHRARGTHRARGALAALAPHE
10   THRGLNTRPLEUCYSHISLEUHISASNGLU
11   VALASNARGLYSLEUGLYLYSPROASPPHE
12   ASPCYSSERLYSVALASPGLUARGTRPARG
13   ASPGLYTRPLYSASPGLYSERCYSASP

Entity 2, FAD, 1 - C27 H33 N9 O15 P2 - 785.550 Da.

1   FAD

Samples:

sample_1: sf-ALR, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 26515 26533
PDB
DBJ BAI46852
EMBL CAB87993
GB AAA96390 AAD17328 AAD36986 AAG43494 AAH02429
REF NP_005253 XP_004057029 XP_007980253
SP P55789

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