BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25237

Title: Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690

Deposition date: 2014-09-18 Original release date: 2014-12-08

Authors: Rossi, Paolo; Lange, Oliver; Sgourakis, Nikolaos; Song, Yifan; Lee, Hsiau-Wei; Aramini, James; Ertekin, Asli; Xiao, Rong; Acton, Thomas; Baker, David; Montelione, Gaetano

Citation: Rossi, Paolo; Lange, Oliver; Sgourakis, Nikolaos; Song, Yifan; Lee, Hsiau-Wei; Aramini, James; Ertekin, Asli; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Baker, David. "Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690"  To be published ., .-..

Assembly members:
ER690, polymer, 370 residues, 40724.547 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21_NESG

Entity Sequences (FASTA):
ER690: KIEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPRAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK

Data sets:
Data typeCount
13C chemical shifts1137
1H chemical shifts712
15N chemical shifts340

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MBP1

Entities:

Entity 1, MBP 370 residues - 40724.547 Da.

1   LYSILEGLUGLUGLYLYSLEUVALILETRP
2   ILEASNGLYASPLYSGLYTYRASNGLYLEU
3   ALAGLUVALGLYLYSLYSPHEGLULYSASP
4   THRGLYILELYSVALTHRVALGLUHISPRO
5   ASPLYSLEUGLUGLULYSPHEPROGLNVAL
6   ALAALATHRGLYASPGLYPROASPILEILE
7   PHETRPALAHISASPARGPHEGLYGLYTYR
8   ALAGLNSERGLYLEULEUALAGLUILETHR
9   PROASPLYSALAPHEGLNASPLYSLEUTYR
10   PROPHETHRTRPASPALAVALARGTYRASN
11   GLYLYSLEUILEALATYRPROILEALAVAL
12   GLUALALEUSERLEUILETYRASNLYSASP
13   LEULEUPROASNPROPROLYSTHRTRPGLU
14   GLUILEPROALALEUASPLYSGLULEULYS
15   ALALYSGLYLYSSERALALEUMETPHEASN
16   LEUGLNGLUPROTYRPHETHRTRPPROLEU
17   ILEALAALAASPGLYGLYTYRALAPHELYS
18   TYRGLUASNGLYLYSTYRASPILELYSASP
19   VALGLYVALASPASNALAGLYALALYSALA
20   GLYLEUTHRPHELEUVALASPLEUILELYS
21   ASNLYSHISMETASNALAASPTHRASPTYR
22   SERILEALAGLUALAALAPHEASNLYSGLY
23   GLUTHRALAMETTHRILEASNGLYPROARG
24   ALATRPSERASNILEASPTHRSERLYSVAL
25   ASNTYRGLYVALTHRVALLEUPROTHRPHE
26   LYSGLYGLNPROSERLYSPROPHEVALGLY
27   VALLEUSERALAGLYILEASNALAALASER
28   PROASNLYSGLULEUALALYSGLUPHELEU
29   GLUASNTYRLEULEUTHRASPGLUGLYLEU
30   GLUALAVALASNLYSASPLYSPROLEUGLY
31   ALAVALALALEULYSSERTYRGLUGLUGLU
32   LEUALALYSASPPROARGILEALAALATHR
33   METGLUASNALAGLNLYSGLYGLUILEMET
34   PROASNILEPROGLNMETSERALAPHETRP
35   TYRALAVALARGTHRALAVALILEASNALA
36   ALASERGLYARGGLNTHRVALASPGLUALA
37   LEULYSASPALAGLNTHRARGILETHRLYS

Samples:

sample_1: ER690 1.05 mM; H20 90%; D2O 10%

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D (h)CCH-TOCSYsample_1isotropicsample_conditions_1
3D (h)NNH HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
3D (h)CCH HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
3D (h)CNH HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
3D (h)NCH HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 4354
PDB
DBJ BAB38440 BAE78036 BAG79849 BAI28296 BAI33473
EMBL CAP78494 CAQ34383 CAR01012 CAR05669 CAR10711
GB AAB59056 AAB86559 AAB87675 AAC43128 AAC77004
REF NP_313044 NP_418458 NP_709885 WP_000367925 WP_000695369
SP P0AEX9 P0AEY0

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