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Biological Magnetic Resonance Data Bank


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BMRB Entry 17811

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17811
MolProbity Validation Chart

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Title: Solution structure of MsPTH

Deposition date: 2011-07-27 Original release date: 2012-08-30

Authors: Yadav, Rahul; Pathak, Prem Prakash; Pulavarti, SVSR Krishna; Jain, Anupam; Kumar, Ashok; Shukla, Vaibhav Kumar; Arora, Ashish

Citation: Yadav, Rahul; Pathak, Prem Prakash; Pulavarti, SVSR Krishna; Jain, Anupam; Kumar, Ashok; Shukla, Vaibhav Kumar; Arora, Ashish. "Solution structure of MsPTH"  J. Biol. Chem. ., .-..

Assembly members:
MsPTH, polymer, 191 residues, 20306.486 Da.

Natural source:   Common Name: Mycobacterium smegmatis   Taxonomy ID: 1772   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium smegmatis

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

Entity Sequences (FASTA):
MsPTH: MAEPLLVVGLGNPGPTYAKT RHNLGFMVADVLAGRIGSAF KVHKKSGAEVVTGRLAGTSV VLAKPRCYMNESGRQVGPLA KFYSVPPQQIVVIHDELDID FGRIRLKLGGGEGGHNGLRS VASALGTKNFHRVRIGVGRP PGRKDPAAFVLENFTAAERA EVPTIVEQAADATELLIAQG LEPAQNTVHAW

Data sets:
Data typeCount
13C chemical shifts735
15N chemical shifts165
1H chemical shifts1191

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MsPTH1

Entities:

Entity 1, MsPTH 191 residues - 20306.486 Da.

1   METALAGLUPROLEULEUVALVALGLYLEU
2   GLYASNPROGLYPROTHRTYRALALYSTHR
3   ARGHISASNLEUGLYPHEMETVALALAASP
4   VALLEUALAGLYARGILEGLYSERALAPHE
5   LYSVALHISLYSLYSSERGLYALAGLUVAL
6   VALTHRGLYARGLEUALAGLYTHRSERVAL
7   VALLEUALALYSPROARGCYSTYRMETASN
8   GLUSERGLYARGGLNVALGLYPROLEUALA
9   LYSPHETYRSERVALPROPROGLNGLNILE
10   VALVALILEHISASPGLULEUASPILEASP
11   PHEGLYARGILEARGLEULYSLEUGLYGLY
12   GLYGLUGLYGLYHISASNGLYLEUARGSER
13   VALALASERALALEUGLYTHRLYSASNPHE
14   HISARGVALARGILEGLYVALGLYARGPRO
15   PROGLYARGLYSASPPROALAALAPHEVAL
16   LEUGLUASNPHETHRALAALAGLUARGALA
17   GLUVALPROTHRILEVALGLUGLNALAALA
18   ASPALATHRGLULEULEUILEALAGLNGLY
19   LEUGLUPROALAGLNASNTHRVALHISALA
20   TRP

Samples:

sample_1: MsPTH, [U-98% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; AEBSF protease inhibitor 1 mM; sodium azide 1%; H2O 93%; D2O 7%

sample_2: MsPTH, [U-98% 13C; U-98% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; AEBSF protease inhibitor 1 mM; sodium azide 1%; H2O 93%; D2O 7%

sample_3: MsPTH, [U-98% 13C; U-98% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; AEBSF protease inhibitor 1 mM; sodium azide 1%; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
HB(CBCGCE)HEsample_2isotropicsample_conditions_1
HB(CBCGCD)HDsample_2isotropicsample_conditions_1

Software:

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

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

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

TALOS v+, Cornilescu, Delaglio and Bax - structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CKI31238
GB ABK75581 AFP41725 AIU10451 AIU17076 AIU23699
REF WP_003896829 WP_011730530 YP_889671
SP A0R3D3

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts