BMRB Entry 51083

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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/BMR51083
MolProbity Validation Chart

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Title:
Backbone and Sidechain 1H, 13C, and 15N Chemical Shift Assignments for Domain 3 of Heligmosomoides polygyrus protein Transforming Growth Factor Beta Mimic 1 (TGM-1 D3)
Deposition date:
2021-09-14
Original release date:
2021-09-18
Authors:
Mukundan, Ananya; Byeon, Chang-Hyeock
Citation:

Citation: Mukundan, Ananya; Byeon, Chang-Hyeock; Hinck, Cynthia; Cunningham, Kyle; Campion, Tiffany; Smyth, Danielle; Maizels, Rick; Hinck, Andrew. "Convergent evolution of a parasite-encoded complement control protein-scaffold to mimic binding of mammalian TGF-b to its receptors, TbRI and TbRII"  J. Biol. Chem. 298, 101994-101994 (2022).
PubMed: 35500648

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Heligmosomoides polygyrus   Taxonomy ID: 6339   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Heligmosomoides polygyrus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGTGCPPLPDDGIVFYEYY GYAGDRHTVGPVVTKDSSGN YPSPTHARRRCRALSQEADP GEFVAICYKSGTTGESHWEY YKNIGKCPDP

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts95
1H chemical shifts551

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TGM-1 D31

Entities:

Entity 1, TGM-1 D3 90 residues - Formula weight is not available

The first two residues GS are part of a thrombin tag, the second two residues GT are part of a linker. The native protein starts from residue 5 'GCPP...' until 'CPDP'. The residue labeling starts from residue 173.

1   GLYSERGLYTHRGLYCYSPROPROLEUPRO
2   ASPASPGLYILEVALPHETYRGLUTYRTYR
3   GLYTYRALAGLYASPARGHISTHRVALGLY
4   PROVALVALTHRLYSASPSERSERGLYASN
5   TYRPROSERPROTHRHISALAARGARGARG
6   CYSARGALALEUSERGLNGLUALAASPPRO
7   GLYGLUPHEVALALAILECYSTYRLYSSER
8   GLYTHRTHRGLYGLUSERHISTRPGLUTYR
9   TYRLYSASNILEGLYLYSCYSPROASPPRO

Samples:

sample_1: TGM-1 D3, [U-98% 15N; U-95% 13C], 250 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_2: TGM-1 D3, [U-98% 15N; U-95% 13C], 250 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_3: TGM-1 D3, [U-98% 15N], [U-95% 13C], 250 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_4: TGM-1 D3, [U-98% 15N], 250 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_5: TGM-1 D3 250 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_conditions_1: pH: 6.0; temperature: 310 K

sample_conditions_2: pH: 6.0; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_4anisotropicsample_conditions_2
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D CB(CGCDCD)HDsample_1isotropicsample_conditions_1
1H 13C HSQC-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D CB(CGCDCD)HEsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCA(CO)Nsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4 - chemical shift assignment, chemical shift calculation

TOPSPIN v3.1 - collection

NMRFAM-SPARKY v1.2 - chemical shift assignment, chemical shift calculation

NMRPipe v2.6 - data analysis

PINE vI-PINE - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance II 800 MHz
  • Bruker Avance II 900 MHz

Related Database Links:

NCBI MG099712

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