BMRB Entry 36360

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36360
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solution structure of monomeric superoxide dismutase 1 with an additional mutation H46W in a crowded environment
Deposition date:
2020-07-14
Original release date:
2025-10-13
Authors:
Iwakawa, N.; Morimoto, D.; Walinda, E.; Danielsson, J.; Shirakawa, M.; Sugase, K.
Citation:

Citation: Iwakawa, Naoto; Morimoto, Daichi; Walinda, Erik; Leeb, Sarah; Shirakawa, Masahiro; Danielsson, Jens; Sugase, Kenji. "Transient Diffusive Interactions with a Protein Crowder Affect Aggregation Processes of Superoxide Dismutase 1 b-Barrel."  J. Phys. Chem. B 125, 2521-2532 (2021).
PubMed: 33657322

Assembly members:

Assembly members:
Monomeric Human Cu,Zn Superoxide dismutase, polymer, 110 residues, 11038.354 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Monomeric Human Cu,Zn Superoxide dismutase: ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFWVHGAGGDLGNVTAD KDGVADVSIEDSVISLSGDH SIIGRTLVVHEKAGAGAGSR LASGVIGIAQ

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts113
1H chemical shifts722

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 110 residues - 11038.354 Da.

1   ALATHRLYSALAVALALAVALLEULYSGLY
2   ASPGLYPROVALGLNGLYILEILEASNPHE
3   GLUGLNLYSGLUSERASNGLYPROVALLYS
4   VALTRPGLYSERILELYSGLYLEUTHRGLU
5   GLYLEUHISGLYPHETRPVALHISGLYALA
6   GLYGLYASPLEUGLYASNVALTHRALAASP
7   LYSASPGLYVALALAASPVALSERILEGLU
8   ASPSERVALILESERLEUSERGLYASPHIS
9   SERILEILEGLYARGTHRLEUVALVALHIS
10   GLULYSALAGLYALAGLYALAGLYSERARG
11   LEUALASERGLYVALILEGLYILEALAGLN

Samples:

sample_1: Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, with an additional mutation H46W, [U-13C; U-15N], 1 mM; Bis-Tris 10 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe v9.6, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - structure calculation

CcpNmr Analysis v2.4.2, CCPN - data analysis

MOLMOL v2K.2, Koradi, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker AVANCE II 700 MHz

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