BMRB Entry 34518

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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/BMR34518
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
De-novo Maquette 2 protein with buried ion-pair
Deposition date:
2020-05-19
Original release date:
2021-04-05
Authors:
Baumgart, M.; Roepke, M.; Muehlbauer, M.; Asami, S.; Mader, S.; Fredriksson, K.; Groll, M.; Gamiz-Hernandez, A.; Kaila, V.
Citation:

Citation: Baumgart, M.; Roepke, M.; Muehlbauer, M.; Asami, S.; Mader, S.; Fredriksson, K.; Groll, M.; Gamiz-Hernandez, A.; Kaila, V.. "Design of Buried Charged Networks in Artificial Proteins"  Nat. Commun. 12, 1895-1895 (2021).
PubMed: 33767131

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 12929.207 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: SEFEKLRQTGDELVQAEQRL REIFDKGDDDSLEQVLEEIE ELIQKHRQLFDNRQEAADTE AAKQGDQWVQLKQRFREAID KGDKDSLEQLLEELEQALQK IRELAEKKN

Data sets:
Data typeCount
13C chemical shifts494
15N chemical shifts126
1H chemical shifts818

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 109 residues - 12929.207 Da.

1   SERGLUPHEGLULYSLEUARGGLNTHRGLY
2   ASPGLULEUVALGLNALAGLUGLNARGLEU
3   ARGGLUILEPHEASPLYSGLYASPASPASP
4   SERLEUGLUGLNVALLEUGLUGLUILEGLU
5   GLULEUILEGLNLYSHISARGGLNLEUPHE
6   ASPASNARGGLNGLUALAALAASPTHRGLU
7   ALAALALYSGLNGLYASPGLNTRPVALGLN
8   LEULYSGLNARGPHEARGGLUALAILEASP
9   LYSGLYASPLYSASPSERLEUGLUGLNLEU
10   LEUGLUGLULEUGLUGLNALALEUGLNLYS
11   ILEARGGLULEUALAGLULYSLYSASN

Samples:

sample_1: Maquette 2-1ip, [U-13C; U-15N], 800 uM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 293 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
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp v1.4, Koradi, Billeter and Guntert - refinement

TopSpin v3.5pl7, Bruker Biospin - processing

Sparky, Goddard - chemical shift assignment, peak picking

CARA, Keller and Wuthrich - peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 950 MHz

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