BMRB Entry 27151

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27151
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Human Guanylate Kinase
Deposition date:
2017-06-21
Original release date:
2017-09-29
Authors:
Sabo, Michael; Khan, Nazimuddin; Ban, David; Trigo-Mourino, Pablo; Carneiro, Marta; Konrad, Manfred; Lee, Donghan
Citation:

Citation: Khan, Nazimuddin; Ban, David; Trigo-Mourino, Pablo; Carneiro, Marta; Konrad, Manfred; Lee, Donghan; Sabo, Michael. "1H, 13C and 15N resonance assignment of human guanylate kinase"  Biomol. NMR Assignments 12, 11-14 (2018).
PubMed: 28861857

Assembly members:

Assembly members:
hGMPK, polymer, 198 residues, 21862.73 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-14bSUMO Thr

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hGMPK: HMSGPRPVVLSGPSGAGKST LLKRLLQEHSGIFGFSVSHT TRNPRPGEENGKDYYFVTRE VMQRDIAAGDFIEHAEFSGN LYGTSKVAVQAVQAMNRICV LDVDLQGVRNIKATDLRPIY ISVQPPSLHVLEQRLRQRNT ETEESLVKRLAAAQADMESS KEPGLFDVVIINDSLDQAYA ELKEALSEEIKKAQRTGA

Data sets:
Data typeCount
13C chemical shifts812
15N chemical shifts196
1H chemical shifts1371

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hGMPK1

Entities:

Entity 1, hGMPK 198 residues - 21862.73 Da.

Residue 1 is an artifact

1   HISMETSERGLYPROARGPROVALVALLEU
2   SERGLYPROSERGLYALAGLYLYSSERTHR
3   LEULEULYSARGLEULEUGLNGLUHISSER
4   GLYILEPHEGLYPHESERVALSERHISTHR
5   THRARGASNPROARGPROGLYGLUGLUASN
6   GLYLYSASPTYRTYRPHEVALTHRARGGLU
7   VALMETGLNARGASPILEALAALAGLYASP
8   PHEILEGLUHISALAGLUPHESERGLYASN
9   LEUTYRGLYTHRSERLYSVALALAVALGLN
10   ALAVALGLNALAMETASNARGILECYSVAL
11   LEUASPVALASPLEUGLNGLYVALARGASN
12   ILELYSALATHRASPLEUARGPROILETYR
13   ILESERVALGLNPROPROSERLEUHISVAL
14   LEUGLUGLNARGLEUARGGLNARGASNTHR
15   GLUTHRGLUGLUSERLEUVALLYSARGLEU
16   ALAALAALAGLNALAASPMETGLUSERSER
17   LYSGLUPROGLYLEUPHEASPVALVALILE
18   ILEASNASPSERLEUASPGLNALATYRALA
19   GLULEULYSGLUALALEUSERGLUGLUILE
20   LYSLYSALAGLNARGTHRGLYALA

Samples:

sample_1: hGMPK, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 20 mM; TCEP 1 mM; sodium azide 3 mM; H2O 90%; D2O 10%; DSS 5 uM

sample_2: hGMPK, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 20 mM; TCEP 1 mM; sodium azide 3 mM; D2O 100%

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

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