BMRB Entry 30844

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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/BMR30844
MolProbity Validation Chart

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Title:
High resolution NMR solution structure of a de novo designed minimal thioredoxin fold protein
Deposition date:
2021-01-13
Original release date:
2022-07-06
Authors:
Urbauer, J.; Strauch, E.
Citation:

Citation: Linsky, T.; Noble, K.; Tobin, A.; Crow, R.; Carter, L.; Urbauer, J.; Baker, D.; Strauch, E.. "Sampling of structure and sequence space of small protein folds"  Nat. Commun. 13, 7151-7151 (2022).
PubMed: 36418330

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, 8366.353 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: synthetic construct

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDEVKVHVGDDQFEEVSREI KKAGWKVEVHKHPSNTSQVT VTKGNKQWTFKDPKQAVEFV QKSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts64
1H chemical shifts447

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 71 residues - 8366.353 Da.

1   METASPGLUVALLYSVALHISVALGLYASP
2   ASPGLNPHEGLUGLUVALSERARGGLUILE
3   LYSLYSALAGLYTRPLYSVALGLUVALHIS
4   LYSHISPROSERASNTHRSERGLNVALTHR
5   VALTHRLYSGLYASNLYSGLNTRPTHRPHE
6   LYSASPPROLYSGLNALAVALGLUPHEVAL
7   GLNLYSSERLEUGLUHISHISHISHISHIS
8   HIS

Samples:

sample_1: sodium phosphate 10 mM; sodium chloride 10 mM; ems_thioM_802 (protein), [U-98% 13C; U-98% 15N], 0.6 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-TOCSY relayed ct 1H-13C HMQCsample_1isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

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

Felix v2007, Accelrys Software Inc., now Felix NMR, Inc., Steve Unger - chemical shift assignment, peak picking, processing

VnmrJ v4.2, VnmrJ, Agilent - collection

NMR spectrometers:

  • Agilent DD2 600 MHz

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