BMRB Entry 17236

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17236
MolProbity Validation Chart

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Title:
cytochrome c domain of pp3183 protein from Pseudomonas putida
Deposition date:
2010-10-04
Original release date:
2011-01-18
Authors:
Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Kozyreva, Tatiana; Mori, Mirko; Wang, Shenlin
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Kozyreva, Tatiana; Mori, Mirko; Wang, Shenlin. "Sco proteins are involved in electron transfer processes."  J. Biol. Inorg. Chem. 16, 391-403 (2011).
PubMed: 21181421

Assembly members:

Assembly members:
cytochrome, polymer, 110 residues, 12147.896 Da.
FE (III) ION, non-polymer, 55.845 Da.
HEME C, non-polymer, 618.503 Da.

Natural source:

Natural source:   Common Name: Pseudomonas putida   Taxonomy ID: 303   Superkingdom: bacteria   Kingdom: not available   Genus/species: Pseudomonas putida

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEC86

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cytochrome: GSFTSGEQIFRTRCSSCHTV GNTEPGQPGIGPDLLGVTRQ RDANWLVRWLKVPDQMLAEK DPLAMLLFEQYNRLAMPNMR LGDAEVSALISYLEEETARL QTPVTNRGIP

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts92
1H chemical shifts134

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cytochrome1
2FE2
3HEC3

Entities:

Entity 1, cytochrome 110 residues - 12147.896 Da.

1   GLYSERPHETHRSERGLYGLUGLNILEPHE
2   ARGTHRARGCYSSERSERCYSHISTHRVAL
3   GLYASNTHRGLUPROGLYGLNPROGLYILE
4   GLYPROASPLEULEUGLYVALTHRARGGLN
5   ARGASPALAASNTRPLEUVALARGTRPLEU
6   LYSVALPROASPGLNMETLEUALAGLULYS
7   ASPPROLEUALAMETLEULEUPHEGLUGLN
8   TYRASNARGLEUALAMETPROASNMETARG
9   LEUGLYASPALAGLUVALSERALALEUILE
10   SERTYRLEUGLUGLUGLUTHRALAARGLEU
11   GLNTHRPROVALTHRASNARGGLYILEPRO

Entity 2, FE - Fe - 55.845 Da.

1   FE

Entity 3, HEC - C34 H34 Fe N4 O4 - 618.503 Da.

1   HEC

Samples:

sample_1: cytochrome c, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: cytochrome c, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
GB AAN68791 KMU94501 KMY34143
REF NP_745327 WP_010954068 WP_020192550

Download HSQC peak lists in one of the following formats:
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