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 18968

Title: Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1

Authors: Szpryngiel, Scarlett; Oliveberg, Mikael; Maler, Lena

Citation: Szpryngiel, Scarlett; Oliveberg, Mikael; Maler, Lena. "Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1"  Not known ., .-..

Assembly members:
SOD1, polymer, 153 residues, Formula weight is not available

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):
SOD1: ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts148
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SOD11

Entities:

Entity 1, SOD1 153 residues - Formula weight is not available

SOD1

1   ALATHRLYSALAVALALAVALLEULYSGLY
2   ASPGLYPROVALGLNGLYILEILEASNPHE
3   GLUGLNLYSGLUSERASNGLYPROVALLYS
4   VALTRPGLYSERILELYSGLYLEUTHRGLU
5   GLYLEUHISGLYPHEHISVALHISGLUGLU
6   GLUASPASNTHRALAGLYCYSTHRSERALA
7   GLYPROHISPHEASNPROLEUSERARGLYS
8   HISGLYGLYPROLYSASPGLUGLUARGHIS
9   VALGLYASPLEUGLYASNVALTHRALAASP
10   LYSASPGLYVALALAASPVALSERILEGLU
11   ASPSERVALILESERLEUSERGLYASPHIS
12   ALAILEILEGLYARGTHRLEUVALVALHIS
13   GLULYSALAASPASPLEUGLYLYSGLYGLY
14   ASNGLUGLUSERTHRLYSTHRGLYASNALA
15   GLYSERARGLEUALACYSGLYVALILEGLY
16   ILEALAGLN

Samples:

sample_1: SOD1, [U-100% 13C; U-100% 15N], 0.2-0.5 mM; D2O, [U-99% 2H], 10%; urea 9 M; bis-Tris 10 mM; H2O 90%

sample_conditions_1: ionic strength: 10 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CANCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15711 15712 15713 15714 18509 18708 26570 4202
PDB
DBJ BAA14373 BAC20345 BAG35052 BAG73767
EMBL CAA26182 CAG29351 CAG46542
GB AAA72747 AAA80237 AAB05661 AAD42179 AAH01034
REF NP_000445 NP_001009025 XP_003813274 XP_008976454
SP P00441 P60052