BMRB Entry 34203

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34203
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR solution structure of non-bound [des-Arg10]-kallidin (DAKD)
Deposition date:
2017-11-23
Original release date:
2018-01-03
Authors:
Richter, C.; Jonker, H.; Schwalbe, H.; Joedicke, L.; Mao, J.; Kuenze, G.; Reinhart, C.; Kalavacherla, T.; Meiler, J.; Preu, J.; Michel, H.; Glaubitz, C.
Citation:

Citation: Joedicke, Lisa; Mao, Jiafei; Kuenze, Georg; Reinhart, Christoph; Kalavacherla, Tejaswi; Jonker, Hendrik; Richter, Christian; Schwalbe, Harald; Meiler, Jens; Preu, Julia; Michel, Hartmut; Glaubitz, Clemens. "The molecular basis of subtype selectivity of human kinin G-protein-coupled receptors."  Nat. Chem. Biol. 14, 284-290 (2018).
PubMed: 29334381

Assembly members:

Assembly members:
entity_1, polymer, 9 residues, 1034.210 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KRPPGFSPF

Data sets:
Data typeCount
13C chemical shifts44
15N chemical shifts6
1H chemical shifts61

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 9 residues - 1034.210 Da.

1   LYSARGPROPROGLYPHESERPROPHE

Samples:

sample_1: DAKD 3 mM; MES 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 111 mM; pH: 5.6; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H ROESYsample_1not availablesample_conditions_1
2D 1H-1H TOCSYsample_1not availablesample_conditions_1
2D 1H-13C HSQC (edited)sample_1not availablesample_conditions_1
2D 1H-13C HMBCsample_1not availablesample_conditions_1
2D 1H-15N HMQC (sofast)sample_1not availablesample_conditions_1

Software:

SPARKY v3.114, Goddard and Kneller - chemical shift assignment, peak picking

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ARIA v1.2 HJ webportal version, Linge, O'Donoghue and Nilges - refinement

TALOS vN, Shen and Bax - data analysis

TOPSPIN v3.5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance III HD 600 MHz

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