BMRB Entry 16467

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16467
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
The Solution structure of the eTAFH domain of AML1-ETO complexed with HEB peptide
Deposition date:
2009-08-25
Original release date:
2009-12-11
Authors:
Park, Sangho; Cierpicki, Tomasz; Tonelli, Marco; Bushweller, John
Citation:

Citation: Park, Sangho; Chen, Wei; Cierpicki, Tomasz; Tonelli, Marco; Cai, Xiongwei; Speck, Nancy; Bushweller, John. "Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity."  Blood 113, 3558-3567 (2009).
PubMed: 19204326

Assembly members:

Assembly members:
entity_1, polymer, 103 residues, 11623.564 Da.
entity_2, polymer, 18 residues, 1990.227 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: pHis parallal2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGSGARQLSKLKRFLTTL QQFGNDISPEIGERVRTLVL GLVNSTLTIEEFHSKLQEAT NFPLRPFVIPFLKANLPLLQ RELLHCARLAKQNPAQYLAQ HEQ
entity_2: IGTDKELSDLLDFSAMFS

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts108
1H chemical shifts760

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 103 residues - 11623.564 Da.

1   GLYALAMETGLYSERGLYALAARGGLNLEU
2   SERLYSLEULYSARGPHELEUTHRTHRLEU
3   GLNGLNPHEGLYASNASPILESERPROGLU
4   ILEGLYGLUARGVALARGTHRLEUVALLEU
5   GLYLEUVALASNSERTHRLEUTHRILEGLU
6   GLUPHEHISSERLYSLEUGLNGLUALATHR
7   ASNPHEPROLEUARGPROPHEVALILEPRO
8   PHELEULYSALAASNLEUPROLEULEUGLN
9   ARGGLULEULEUHISCYSALAARGLEUALA
10   LYSGLNASNPROALAGLNTYRLEUALAGLN
11   HISGLUGLN

Entity 2, entity_2 18 residues - 1990.227 Da.

1   ILEGLYTHRASPLYSGLULEUSERASPLEU
2   LEUASPPHESERALAMETPHESER

Samples:

sample_1: Bis-Tris 25 mM; EDTA 1 mM; sodium chloride 350 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 350 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAA03089 BAA03247 BAA03558 BAA03559 BAA03560 BAE21989 BAE25324 BAE41376 BAG10617 BAG57800
EMBL CAA56311 CAF99400 CAG33073 CAH65373 CAA46052 CAD89914 CAG31482 CAL38596 CDQ61893
GB AAB34819 AAB34820 AAB92651 AAC28931 AAC28932 AAA42115 AAA58632 AAB62389 AAH50556 AAH92888
REF NP_001025751 NP_001070244 NP_001089065 NP_001101923 NP_001102127 NP_001071353 NP_001187118 NP_001187135 NP_001187247 NP_001240791
SP O54972 O75081 Q06455 Q5F3B1 Q61909 P51514 Q61286 Q99081
TPG DAA20254 DAA01129 DAA25320
BMRB 16851
AlphaFold O54972 O75081 Q06455 Q5F3B1 Q61909 P51514 Q61286 Q99081

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