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 11036

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11036

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Title: NMR solution structures of KAP-1PHD finger-bromodomain   PubMed: 18488044

Deposition date: 2008-03-20 Original release date: 2008-11-11

Authors: Zeng, Lei; Yap, Kyoko; Ivanov, Alexey; Wang, Xueqi; Mujtaba, Shiraz; Plotnikova, Olga; Rauscher, Frank

Citation: Zeng, Lei; Yap, Kyoko; Ivanov, Alexey; Wang, Xueqi; Mujtaba, Shiraz; Plotnikova, Olga; Rauscher, Frank; Zhou, Ming-Ming. "Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing."  Nat. Struct. Mol. Biol. 15, 626-633 (2008).

Assembly members:
KAP1 PHD Bromodomains, polymer, 189 residues, 21043.086 Da.
ZN, non-polymer, 65.409 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 BL21(DE3)

Entity Sequences (FASTA):
KAP1 PHD Bromodomains: SATICRVCQKPGDLVMCNQC EFCFHLDCHLPALQDVPGEE WSCSLCHVLPDLKEEDGSLS LDGADSTGVVAKLSPANQRK CERVLLALFCHEPCRPLHQL ATDSTFSLDQPGGTLDLTLI RARLQEKLSPPYSSPQEFAQ DVGRMFKQFNKLTEDKADVQ SIIGLQRFFETRMNEAFGDT KFSAVLVEP

Data sets:
Data typeCount
13C chemical shifts618
15N chemical shifts188
1H chemical shifts1192

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KAP1 PHD Bromodomains1
2ZINC ION No.12
3ZINC ION No.22

Entities:

Entity 1, KAP1 PHD Bromodomains 189 residues - 21043.086 Da.

1   SERALATHRILECYSARGVALCYSGLNLYS
2   PROGLYASPLEUVALMETCYSASNGLNCYS
3   GLUPHECYSPHEHISLEUASPCYSHISLEU
4   PROALALEUGLNASPVALPROGLYGLUGLU
5   TRPSERCYSSERLEUCYSHISVALLEUPRO
6   ASPLEULYSGLUGLUASPGLYSERLEUSER
7   LEUASPGLYALAASPSERTHRGLYVALVAL
8   ALALYSLEUSERPROALAASNGLNARGLYS
9   CYSGLUARGVALLEULEUALALEUPHECYS
10   HISGLUPROCYSARGPROLEUHISGLNLEU
11   ALATHRASPSERTHRPHESERLEUASPGLN
12   PROGLYGLYTHRLEUASPLEUTHRLEUILE
13   ARGALAARGLEUGLNGLULYSLEUSERPRO
14   PROTYRSERSERPROGLNGLUPHEALAGLN
15   ASPVALGLYARGMETPHELYSGLNPHEASN
16   LYSLEUTHRGLUASPLYSALAASPVALGLN
17   SERILEILEGLYLEUGLNARGPHEPHEGLU
18   THRARGMETASNGLUALAPHEGLYASPTHR
19   LYSPHESERALAVALLEUVALGLUPRO

Entity 2, ZINC ION No.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: KAP1 PHD Bromodomains, [U-100% 13C; U-100% 15N], 0.5 mM; NaCl 200 mM; D2O 99.9%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v2.1, Linge, O, . - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC40742 BAE24661 BAE29223 BAG11035 BAG36262
EMBL CAA66150 CAA67963
GB AAA74954 AAB17272 AAB37341 AAB51517 AAG02638
REF NP_001193738 NP_005753 NP_035718 NP_446368 XP_001098702
SP O08629 Q13263 Q62318
TPG DAA19313

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