BMRB Entry 36752

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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/BMR36752
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
A designed protein-A339
Deposition date:
2025-04-18
Original release date:
2026-06-06
Authors:
Yurui, Z.; Yajun, J.; Peng, Z.
Citation:

Citation: Yurui, Z.; Yajun, J.; Peng, Z.. "Structure of a designed Titan-like protein at 1.0 AngStrom resolution."  .

Assembly members:

Assembly members:
A339, polymer, 112 residues, 12404.406 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):
A339: MVEGVLTIELSDSVPEEVKE KVKATVEELAERARKEMGLE VKIEEKDGVITVKAKGEEEK VKKFFEEVIAALKKIAAENG LKVETELTEEKAKVENGKEI KGKITGKVRISA

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts110
1H chemical shifts652

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 112 residues - 12404.406 Da.

1   METVALGLUGLYVALLEUTHRILEGLULEU
2   SERASPSERVALPROGLUGLUVALLYSGLU
3   LYSVALLYSALATHRVALGLUGLULEUALA
4   GLUARGALAARGLYSGLUMETGLYLEUGLU
5   VALLYSILEGLUGLULYSASPGLYVALILE
6   THRVALLYSALALYSGLYGLUGLUGLULYS
7   VALLYSLYSPHEPHEGLUGLUVALILEALA
8   ALALEULYSLYSILEALAALAGLUASNGLY
9   LEULYSVALGLUTHRGLULEUTHRGLUGLU
10   LYSALALYSVALGLUASNGLYLYSGLUILE
11   LYSGLYLYSILETHRGLYLYSVALARGILE
12   SERALA

Samples:

sample_1: A339, [U-13C; U-15N], 0.8 mM; sodium azide 1 mM; potassium chloride 75 mM; sodium phosphate 20 mM; H2O 93%; D2O, [U-2H], 7%

sample_conditions_1: ionic strength: 95 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCCONHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

NMRFAM-SPARKY, Lee, W., M. Tonelli, and J.L. Markley - peak picking

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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