BMRB Entry 5959

Title:
Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions
Deposition date:
2003-09-29
Original release date:
2004-09-30
Authors:
Byeon, In-Ja; Li, Hongyuan; Tsai, Ming-Daw
Citation:

Citation: Li, Hongyuan; Byeon, In-Ja; Tsai, Ming-Daw. "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions "  J. Mol. Biol. 335, 371-381 (2004).
PubMed: 14659764

Assembly members:

Assembly members:
Antigen Ki-67, polymer, 128 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

Data sets:
Data typeCount
1H chemical shifts692
13C chemical shifts434
15N chemical shifts103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ki67 FHA monomer1

Entities:

Entity 1, ki67 FHA monomer 128 residues - Formula weight is not available

1   GLYSERPROGLUPHEPROGLYGLYMETTRP
2   PROTHRARGARGLEUVALTHRILELYSARG
3   SERGLYVALASPGLYPROHISPHEPROLEU
4   SERLEUSERTHRCYSLEUPHEGLYARGGLY
5   ILEGLUCYSASPILEARGILEGLNLEUPRO
6   VALVALSERLYSGLNHISCYSLYSILEGLU
7   ILEHISGLUGLNGLUALAILELEUHISASN
8   PHESERSERTHRASNPROTHRGLNVALASN
9   GLYSERVALILEASPGLUPROVALARGLEU
10   LYSHISGLYASPVALILETHRILEILEASP
11   ARGSERPHEARGTYRGLUASNGLUSERLEU
12   GLNASNGLYARGLYSSERTHRGLUPHEPRO
13   ARGLYSILEARGGLUGLNGLUPRO

Samples:

sample_1: Antigen Ki-67, [U-13C; U-15N], 0.3 – 0.5 mM; TrisHCl buffer 10 mM; DTT 2 mM; EDTA 1 mM

sample_2: Antigen Ki-670.3 – 0.5 mM; TrisHCl buffer 10 mM; DTT 2 mM; EDTA 1 mM

condition_1: pH: 8.4; temperature: 290 K; ionic strength: 0.01 M

condition_2: pH: 7.5; temperature: 290 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
HNCACBnot availablenot availablenot available
CBCACONHnot availablenot availablenot available
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available
15N-edited NOESYnot availablenot availablenot available
15N-edited TOCSYnot availablenot availablenot available
13C-edited NOESYnot availablenot availablenot available

Software:

XWINNMR v2.6 - processing

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DMX 600 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAA46519 CAA46520
GB EAW49178 EAW49179
PIR B48666
REF NP_001139438 NP_002408 XP_002821326 XP_002821327 XP_004050323
SP P46013
AlphaFold P46013

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