BMRB Entry 52193

Title:
ModA - molybdate binding protein at two pHs
Deposition date:
2023-10-25
Original release date:
2024-04-23
Authors:
Nguyen, Hiep; Crowhurst, Karin
Citation:

Citation: Nguyen, Hiep; Crowhurst, Karin. "Solution NMR chemical shift assignment of apo and molybdate-bound ModA at two pHs"  Biomol. NMR Assign. 18, 93-98 (2024).
PubMed: 38642264

Assembly members:

Assembly members:
entity_1, polymer, 233 residues, Formula weight is not available

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   Vector: pET11a

Data sets:
Data typeCount
13C chemical shifts1356
15N chemical shifts459
1H chemical shifts1380

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ModA1

Entities:

Entity 1, ModA 233 residues - Formula weight is not available

1   ASPGLUGLYLYSILETHRVALPHEALAALA
2   ALASERLEUTHRASNALAMETGLNASPILE
3   ALATHRGLNPHELYSLYSGLULYSGLYVAL
4   ASPVALVALSERSERPHEALASERSERSER
5   THRLEUALAARGGLNILEGLUALAGLYALA
6   PROALAASPLEUPHEILESERALAASPGLN
7   LYSTRPMETASPTYRALAVALASPLYSLYS
8   ALAILEASPTHRALATHRARGGLNTHRLEU
9   LEUGLYASNSERLEUVALVALVALALAPRO
10   LYSALASERVALGLNLYSASPPHETHRILE
11   ASPSERLYSTHRASNTRPTHRSERLEULEU
12   ASNGLYGLYARGLEUALAVALGLYASPPRO
13   GLUHISVALPROALAGLYILETYRALALYS
14   GLUALALEUGLNLYSLEUGLYALATRPASP
15   THRLEUSERPROLYSLEUALAPROALAGLU
16   ASPVALARGGLYALALEUALALEUVALGLU
17   ARGASNGLUALAPROLEUGLYILEVALTYR
18   GLYSERASPALAVALALASERLYSGLYVAL
19   LYSVALVALALATHRPHEPROGLUASPSER
20   HISLYSLYSVALGLUTYRPROVALALAVAL
21   VALGLUGLYHISASNASNALATHRVALLYS
22   ALAPHETYRASPTYRLEULYSGLYPROGLN
23   ALAALAGLUILEPHELYSARGTYRGLYPHE
24   THRILELYS

Samples:

sample_1: ModA, [U-100% 13C; U-100% 15N], 1 mM; citrate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.05 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2

Software:

VNMRj v4.0 - collection

NMRPipe - processing

NMRViewJ v9.2.0-b27 - chemical shift assignment, data analysis

NMR spectrometers:

  • Agilent DD2 600 MHz

Related Database Links:

UNP P37329
GB CAD6018812.1

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