BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 19807

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19807
MolProbity Validation Chart

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Title: NMR structure of hypothetical protein ZP_02069618.1 from Bacteroides uniformis ATCC 8492.

Deposition date: 2014-02-19 Original release date: 2014-03-10

Authors: Wallmann, Arndt; Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Wallmann, Arndt; Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of hypothetical protein ZP_02069618.1 from Bacteroides uniformis ATCC 8492."  Not known ., .-..

Assembly members:
entity, polymer, 148 residues, 17313.006 Da.

Natural source:   Common Name: Bacteroides uniformis   Taxonomy ID: 820   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides uniformis

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

Entity Sequences (FASTA):
entity: GAEEEDFKTFLQKFTSSASF QYSRIKFPLKSPIALLKDDG ETEQTFPFTREKWALLDEET LKEGRTTEEEGGTYISHFTV NEPAHKEFEAGYDESEPSLR VVFELTDGKWYVTDCYNDWY NFDLPINELEETIQAVQEEN KAFEELHP

Data sets:
Data typeCount
13C chemical shifts496
15N chemical shifts157
1H chemical shifts1017

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Hypothetical protein ZP_02069618.11

Entities:

Entity 1, Hypothetical protein ZP_02069618.1 148 residues - 17313.006 Da.

1   GLYALAGLUGLUGLUASPPHELYSTHRPHE
2   LEUGLNLYSPHETHRSERSERALASERPHE
3   GLNTYRSERARGILELYSPHEPROLEULYS
4   SERPROILEALALEULEULYSASPASPGLY
5   GLUTHRGLUGLNTHRPHEPROPHETHRARG
6   GLULYSTRPALALEULEUASPGLUGLUTHR
7   LEULYSGLUGLYARGTHRTHRGLUGLUGLU
8   GLYGLYTHRTYRILESERHISPHETHRVAL
9   ASNGLUPROALAHISLYSGLUPHEGLUALA
10   GLYTYRASPGLUSERGLUPROSERLEUARG
11   VALVALPHEGLULEUTHRASPGLYLYSTRP
12   TYRVALTHRASPCYSTYRASNASPTRPTYR
13   ASNPHEASPLEUPROILEASNGLULEUGLU
14   GLUTHRILEGLNALAVALGLNGLUGLUASN
15   LYSALAPHEGLUGLULEUHISPRO

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.2 mM; sodium azide 0.03%; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Bruker Biospin, Guntert P. - collection, data analysis, processing, structure solution

CYANA, Bruker Biospin, Guntert P. - collection, data analysis, processing, structure solution

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

j-UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

GAPRO, Hiller - peak picking

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CDE01124 CUN97444 CUO14297 CUO43665 CUO53226
GB EDO55360 EFA20067 EFV27640 EIY75132 EIY78188
REF WP_005826053 WP_044467933 WP_057281877

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