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 25760

Click here to enlarge.

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/BMR25760
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits

Deposition date: 2015-08-19 Original release date: 2015-10-12

Authors: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael. "NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits"  to be published ., .-..

Assembly members:
entity, polymer, 172 residues, 19155.244 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: MKVPMLVLDPALPANITLKD LPSLYPSFHSASDIFNVAKP KNPSTNVSVVVFDSTKDVED AHSGLLKGNSRQTVWRGYLT TDKEVPGLVLMQDLAFLSGF PPTFKETNQLKTKLPENLSS KVKLLQLYSEASVALLKLNN PKDFQELNKQTKKNMTIDGK ELTISPAYLLWD

Data sets:
Data typeCount
13C chemical shifts679
15N chemical shifts179
1H chemical shifts1183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 172 residues - 19155.244 Da.

1   METLYSVALPROMETLEUVALLEUASPPRO
2   ALALEUPROALAASNILETHRLEULYSASP
3   LEUPROSERLEUTYRPROSERPHEHISSER
4   ALASERASPILEPHEASNVALALALYSPRO
5   LYSASNPROSERTHRASNVALSERVALVAL
6   VALPHEASPSERTHRLYSASPVALGLUASP
7   ALAHISSERGLYLEULEULYSGLYASNSER
8   ARGGLNTHRVALTRPARGGLYTYRLEUTHR
9   THRASPLYSGLUVALPROGLYLEUVALLEU
10   METGLNASPLEUALAPHELEUSERGLYPHE
11   PROPROTHRPHELYSGLUTHRASNGLNLEU
12   LYSTHRLYSLEUPROGLUASNLEUSERSER
13   LYSVALLYSLEULEUGLNLEUTYRSERGLU
14   ALASERVALALALEULEULYSLEUASNASN
15   PROLYSASPPHEGLNGLULEUASNLYSGLN
16   THRLYSLYSASNMETTHRILEASPGLYLYS
17   GLULEUTHRILESERPROALATYRLEULEU
18   TRPASP

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.240 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB71102
EMBL CAJ30014
GB AAH71687 AAI31788 AAV98624 EAW97682 EHH21112
REF NP_077288 XP_001092998 XP_001155334 XP_002823695 XP_003832629
SP Q3T906

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