BMRB Entry 18700

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18700
MolProbity Validation Chart

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Title:
The solution structure of XIAP(RING)-binding domain of human XAF1
Deposition date:
2012-09-03
Original release date:
2013-02-12
Authors:
Tse, Man Kit; Cho, Chi Kong; Guan, Xiao; Sze, Kong Hung
Citation:

Citation: Tse, Man Kit; Cho, Chi Kong; Wong, Wai Fung; Zou, Bing; Hui, Sin Kam; Wong, Benjamin Chun Yu; Sze, Kong Hung. "Domain organization of XAF1 and the identification and characterization of XIAP(RING) -binding domain of XAF1."  Protein Sci. 21, 1418-1428 (2012).
PubMed: 22811387

Assembly members:

Assembly members:
entity_1, polymer, 55 residues, 6202.163 Da.
ZINC ION, non-polymer, 65.409 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: pGB1-HIS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSEFTSSPRGDKAAYDILRR CSQCGILLPLPILNQHQEKC RWLASSKGKQVRNFS

Data sets:
Data typeCount
13C chemical shifts237
15N chemical shifts57
1H chemical shifts382

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1XIAP(RING)-binding domain of XAF11
2ZINC ION2

Entities:

Entity 1, XIAP(RING)-binding domain of XAF1 55 residues - 6202.163 Da.

1   GLYSERGLUPHETHRSERSERPROARGGLY
2   ASPLYSALAALATYRASPILELEUARGARG
3   CYSSERGLNCYSGLYILELEULEUPROLEU
4   PROILELEUASNGLNHISGLNGLULYSCYS
5   ARGTRPLEUALASERSERLYSGLYLYSGLN
6   VALARGASNPHESER

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: XAF1, [U-100% 13C; U-100% 15N], 1.2 mM; BisTris-HCl 20 mM; sodium chloride 150 mM; DTT, D10, 5 mM; PMSF 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - automated peak assignments, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAF82965 BAF85399 BAF85537 BAG51823
GB AAH73156 AIC51642 EAW90287 EAW90288 EAW90289
REF NP_059993 NP_954590 XP_001167990 XP_003274639 XP_003274640
SP Q6GPH4
AlphaFold Q6GPH4

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