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 16711

Title: NMR structure of the protein NP_415897.1

Deposition date: 2010-02-06 Original release date: 2012-08-03

Authors: Serrano, Pedro; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Wuthrich, Kurt; Wilson, Ian

Citation: Serrano, Pedro; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Wilson, Ian; Wuthrich, Kurt. "NMR structure of the protein NP_415897.1"  .

Assembly members:
NP_415897.1, polymer, 117 residues, 12846.825 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET25b

Entity Sequences (FASTA):
NP_415897.1: MVTPEQLQHHRFVLESVNGK PVTSDKNPPEISFGEKMMIS GSMCNRFSGEGKLSNGELTA KGLAMTRMMCANPQLNELDN TISEMLKEGAQVDLTANQLT LATAKQTLTYKLADLMN

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts131
1H chemical shifts822

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_415897.11

Entities:

Entity 1, NP_415897.1 117 residues - 12846.825 Da.

1   METVALTHRPROGLUGLNLEUGLNHISHIS
2   ARGPHEVALLEUGLUSERVALASNGLYLYS
3   PROVALTHRSERASPLYSASNPROPROGLU
4   ILESERPHEGLYGLULYSMETMETILESER
5   GLYSERMETCYSASNARGPHESERGLYGLU
6   GLYLYSLEUSERASNGLYGLULEUTHRALA
7   LYSGLYLEUALAMETTHRARGMETMETCYS
8   ALAASNPROGLNLEUASNGLULEUASPASN
9   THRILESERGLUMETLEULYSGLUGLYALA
10   GLNVALASPLEUTHRALAASNGLNLEUTHR
11   LEUALATHRALALYSGLNTHRLEUTHRTYR
12   LYSLEUALAASPLEUMETASN

Samples:

sample_1: NP_415897.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (Ali)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY (Aro)sample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1
APSY 4D-HACANHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, peak picking, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA14984 BAB35424 BAG76988 BAI25261 BAI30341
EMBL CAP75894 CAQ31880 CAQ98238 CAR02814 CAR07740
GB AAC74461 AAG56381 AAN80290 AAZ88432 ABB66292
REF NP_310028 NP_415897 WP_000129114 WP_001295716 WP_001296048
SP P52644
AlphaFold P52644

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