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Biological Magnetic Resonance Data Bank


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BMRB Entry 18919

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18919
MolProbity Validation Chart

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Full-Length Rabbit Cytochrome b5   PubMed: 24105099

Deposition date: 2012-12-26 Original release date: 2013-02-05

Authors: Subramanian, Vivekanandan; Ahuja, Shivani; Popovych, Nataliya; Huang, Rui; Le Clair, Stephanie; Jahr, Nicole; Soong, Ronald; Xu, Jiadi; Yamamoto, Kazutoshi; Nanga, Ravi; Im, Sang-Choul; Waskell, Lucy; Ramamoorthy, Ayyalusamy

Citation: Vivekanandan, Subramanian; Ahuja, Shivani; Im, Sang-Choul; Waskell, Lucy; Ramamoorthy, Ayyalusamy. "(1)H, (13)C and (15)N resonance assignments for the full-length mammalian cytochrome b5 in a membrane environment."  Biomol. NMR Assignments ., .-. (2013).

Assembly members:
Full-length_cytochrome_b5, polymer, 134 residues, 15350 Da.
entity_HEB, non-polymer, 618.503 Da.

Natural source:   Common Name: rabbit   Taxonomy ID: 9986   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oryctolagus cuniculus

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

Entity Sequences (FASTA):
Full-length_cytochrome_b5: MAAQSDKDVKYYTLEEIKKH NHSKSTWLILHHKVYDLTKF LEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFI IGELHPDDRSKLSKPMETLI TTVDSNSSWWTNWVIPAISA LIVALMYRLYMADD

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts101
1H chemical shifts681

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Full-length cytochrome b51
2heme B2

Entities:

Entity 1, Full-length cytochrome b5 134 residues - 15350 Da.

1   METALAALAGLNSERASPLYSASPVALLYS
2   TYRTYRTHRLEUGLUGLUILELYSLYSHIS
3   ASNHISSERLYSSERTHRTRPLEUILELEU
4   HISHISLYSVALTYRASPLEUTHRLYSPHE
5   LEUGLUGLUHISPROGLYGLYGLUGLUVAL
6   LEUARGGLUGLNALAGLYGLYASPALATHR
7   GLUASNPHEGLUASPVALGLYHISSERTHR
8   ASPALAARGGLULEUSERLYSTHRPHEILE
9   ILEGLYGLULEUHISPROASPASPARGSER
10   LYSLEUSERLYSPROMETGLUTHRLEUILE
11   THRTHRVALASPSERASNSERSERTRPTRP
12   THRASNTRPVALILEPROALAILESERALA
13   LEUILEVALALALEUMETTYRARGLEUTYR
14   METALAASPASP

Entity 2, heme B - C34 H34 Fe N4 O4 - 618.503 Da.

1   HEB

Samples:

sample_1: Full-length cytochrome b5, [U-100% 13C; U-100% 15N; U-80% 2H], 0.1 – 0.5 mM; Heme B0.1 – 0.5 mM; potassium phosphate 100 mM; glycerol 5%; DPC micelles 45 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.113, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

BMRB 295 4602
PDB
DBJ BAA01712
GB AAB03878 AAB32285
PRF 1205244A 1908210A
REF NP_001164734 NP_001164735
SP P00169

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