BMRB Entry 34799

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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/BMR34799
MolProbity Validation Chart

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Title:
Structure of A4M4C bound to (KR)4 Solution backbone structure refined by PCS
Deposition date:
2023-03-20
Original release date:
2023-12-07
Authors:
Cucuzza, S.; Zerbe, O.
Citation:

Citation: Cucuzza, S.; Sitnik, M.; Jurt, S.; Michel, E.; Dai, W.; Muentener, T.; Ernst, P.; Haeussinger, D.; Plueckthun, A.; Zerbe, O.. "Unexpected dynamics in femtomolar complexes of binding proteins with peptides"  Nat. Commun. 14, 7823-7823 (2023).
PubMed: 38016954

Assembly members:

Assembly members:
entity_1, polymer, 239 residues, 25174.350 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PDLPKLVKLLKSSNEEILLK ALRALAEIASGGNEQIQAVI DAGALPALVQLLSSPNEQIL QEALWALSNIASGGNEQIQA VIDAGALPALVQLLSSPNEQ ILQEALWALSNIASGGNEQI QAVIDAGALPALVQLLSSPN EQILQEALWALSNIASGGNE QIQAVIDAGALPALVQLLSS PNEQILQEALWALSNIASGG NEQKQAVKEAGALEKLEQLQ SHENEKIQKEAQEALEKLQ

Data sets:
Data typeCount
15N chemical shifts224
1H chemical shifts218

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 239 residues - 25174.350 Da.

1   PROASPLEUPROLYSLEUVALLYSLEULEU
2   LYSSERSERASNGLUGLUILELEULEULYS
3   ALALEUARGALALEUALAGLUILEALASER
4   GLYGLYASNGLUGLNILEGLNALAVALILE
5   ASPALAGLYALALEUPROALALEUVALGLN
6   LEULEUSERSERPROASNGLUGLNILELEU
7   GLNGLUALALEUTRPALALEUSERASNILE
8   ALASERGLYGLYASNGLUGLNILEGLNALA
9   VALILEASPALAGLYALALEUPROALALEU
10   VALGLNLEULEUSERSERPROASNGLUGLN
11   ILELEUGLNGLUALALEUTRPALALEUSER
12   ASNILEALASERGLYGLYASNGLUGLNILE
13   GLNALAVALILEASPALAGLYALALEUPRO
14   ALALEUVALGLNLEULEUSERSERPROASN
15   GLUGLNILELEUGLNGLUALALEUTRPALA
16   LEUSERASNILEALASERGLYGLYASNGLU
17   GLNILEGLNALAVALILEASPALAGLYALA
18   LEUPROALALEUVALGLNLEULEUSERSER
19   PROASNGLUGLNILELEUGLNGLUALALEU
20   TRPALALEUSERASNILEALASERGLYGLY
21   ASNGLUGLNLYSGLNALAVALLYSGLUALA
22   GLYALALEUGLULYSLEUGLUGLNLEUGLN
23   SERHISGLUASNGLULYSILEGLNLYSGLU
24   ALAGLNGLUALALEUGLULYSLEUGLN

Samples:

sample_1: A4M4C, [U-100% 15N], 150 ± 10 uM; Na2HPO4, none, 20 ± 2 mM; TCEP, none, 0.2 ± 0.02 mM

sample_2: A4M4C, [U-100% 15N], 150 ± 10 uM; Na2HPO4, none, 20 ± 2 mM; TCEP, none, 0.2 ± 0.02 mM

sample_3: A4M4C, [U-100% 15N], 150 ± 10 uM; Na2HPO4, none, 20 ± 2 mM; TCEP, none, 0.2 ± 0.02 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TopSpin v4, Bruker Biospin - collection

CYANA v3.18.4, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich, Keller und Wuethrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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