BMRB Entry 30205

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30205
MolProbity Validation Chart

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Title:
Solution structure of apo PCP1 from yersiniabactin synthetase
Deposition date:
2016-12-02
Original release date:
2017-02-03
Authors:
Harden, B.; Frueh, D.
Citation:

Citation: Harden, B.; Frueh, D.. "Molecular Cross-Talk between Nonribosomal Peptide Synthetase Carrier Proteins and Unstructured Linker Regions"  Chembiochem 18, 629-632 (2017).
PubMed: 28120469

Assembly members:

Assembly members:
HMWP2 nonribosomal peptide synthetase, polymer, 111 residues, 12353.520 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 632   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HMWP2 nonribosomal peptide synthetase: GTIDYQALKRRHTPEAENPA EADLPQGDIEKQVAALWQQL LSTGNVTRETDFFQQGGDSL LATRLTGQLHQAGYEAQLSD LFNHPRLADFAATLRKTDVP VEQPFVHSPED

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts105
1H chemical shifts733

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 111 residues - 12353.520 Da.

1   GLYTHRILEASPTYRGLNALALEULYSARG
2   ARGHISTHRPROGLUALAGLUASNPROALA
3   GLUALAASPLEUPROGLNGLYASPILEGLU
4   LYSGLNVALALAALALEUTRPGLNGLNLEU
5   LEUSERTHRGLYASNVALTHRARGGLUTHR
6   ASPPHEPHEGLNGLNGLYGLYASPSERLEU
7   LEUALATHRARGLEUTHRGLYGLNLEUHIS
8   GLNALAGLYTYRGLUALAGLNLEUSERASP
9   LEUPHEASNHISPROARGLEUALAASPPHE
10   ALAALATHRLEUARGLYSTHRASPVALPRO
11   VALGLUGLNPROPHEVALHISSERPROGLU
12   ASP

Samples:

sample_1: protein 920 uM; DSS 400 uM; DTT 1 mM; EDTA 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_2: protein 1.4 mM; DSS 400 uM; DTT 1 mM; EDTA 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_3: protein 1.4 mM; DSS 400 uM; DTT 1 mM; EDTA 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.60; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HN(CA)CBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C HSQC-NOESYsample_3isotropicsample_conditions_1
3D H(CCCO)NHsample_2isotropicsample_conditions_1
3D (H)C(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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