BMRB Entry 15355

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15355

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Title:
solution structure of human MEKK3 PB1 domain
Deposition date:
2007-06-29
Original release date:
2008-02-29
Authors:
Hu, Q.; Zhang, J.; Wu, J.; Shi, Y.
Citation:

Citation: Hu, Qi; Shen, Weiqun; Huang, Hongda; Liu, Jiangxin; Zhang, Jiahai; Huang, Xiaojuan; Wu, Jihui; Shi, Yunyu. "Insight into the binding properties of MEKK3 PB1 to MEK5 PB1 from its solution structure"  Biochemistry 46, 13478-13489 (2007).
PubMed: 17985933

Assembly members:

Assembly members:
Mitogen-activated_protein_kinase_kinase_kinase_3, polymer, 94 residues, Formula weight is not available

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: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mitogen-activated_protein_kinase_kinase_kinase_3: MQSDVRIKFEHNGERRIIAF SRPVKYEDVEHKVTTVFGQP LDLHYMNNELSILLKNQDDL DKAIDILDRSSSMKSLRILL LSQDRNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts92
1H chemical shifts617

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mitogen-activated protein kinase kinase kinase 31

Entities:

Entity 1, Mitogen-activated protein kinase kinase kinase 3 94 residues - Formula weight is not available

1   METGLNSERASPVALARGILELYSPHEGLU
2   HISASNGLYGLUARGARGILEILEALAPHE
3   SERARGPROVALLYSTYRGLUASPVALGLU
4   HISLYSVALTHRTHRVALPHEGLYGLNPRO
5   LEUASPLEUHISTYRMETASNASNGLULEU
6   SERILELEULEULYSASNGLNASPASPLEU
7   ASPLYSALAILEASPILELEUASPARGSER
8   SERSERMETLYSSERLEUARGILELEULEU
9   LEUSERGLNASPARGASNLEUGLUHISHIS
10   HISHISHISHIS

Samples:

sample: Mitogen-activated protein kinase kinase kinase 3, [U-100% 13C; U-100% 15N], 0.5 mM; phosphate buffer 50 mM; EDTA 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: n/a M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
2D 1H-15N HSQCsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D C(CO)NHsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HBHA(CO)NHsampleisotropicsample_conditions_1
3D HCCH-COSYsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1
3D H(CCO)NHsampleisotropicsample_conditions_1
3D HCACOsampleisotropicsample_conditions_1

Software:

NMRPipe v2.2, F.Delaglio - processing

CNS v1.1, A.T.Brunger - structure solution

Csi v1.0, David S. Wishart - data analysis

Molmol v2k.2, Koradi - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 500 MHz

Related Database Links:

BMRB 15332
PDB
DBJ BAD90481 BAE23244 BAG37709 BAG73407
EMBL CAD38973 CAL37711
GB AAB03535 AAB41729 AAH08336 AAH23781 AAH90859
REF NP_001100528 NP_001244715 NP_002392 NP_036077 NP_976226
SP Q61084 Q99759
TPG DAA18328
AlphaFold Q61084 Q99759

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