BMRB Entry 25923

Click here to enlarge.

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/BMR25923
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:
ULD complex
Deposition date:
2015-12-17
Original release date:
2016-11-14
Authors:
Cierpicki, Tomasz; Gray, Felicia; Cho, Hyo Je
Citation:

Citation: Gray, Felicia; Cho, Hyo Je; Shulka, Shirish; He, Shihan; Harris, Ashley; Boytsov, Bohdan; Jaremko, Lukasz; Jaremko, Mariusz; Demeler, Borries; Lawlor, Elizabeth; Grembecka, Jolanta; Cierpicki, Tomasz. "BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization"  Nat. Commun. 9, 13343-13343 (2016).
PubMed: 27827373

Assembly members:

Assembly members:
entity, polymer, 155 residues, 17139.982 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: pET32p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPAMGKPQILTHVIEGFVIQ EGAEPFPVGRSSLLVGNLKG DKRIITDDEIISLSIEFFDQ NRLDRKVNKDKEKSKEEVND KRYLRCPAAMTVMHLRKFLR SKMDIPNTFQIDVMYEEEPL KDYYTLMDIAYIYTWRRNGP LPLKYRVRPTCKRMK

Data sets:
Data typeCount
13C chemical shifts469
15N chemical shifts129
1H chemical shifts553

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 155 residues - 17139.982 Da.

Residues 1-5 are cloning artifact. Sequence contains fusion of PHC2_B residues 30-64 directly to N-terminus of BMI1 residues 121-235.

1   GLYPROALAMETGLYLYSPROGLNILELEU
2   THRHISVALILEGLUGLYPHEVALILEGLN
3   GLUGLYALAGLUPROPHEPROVALGLYARG
4   SERSERLEULEUVALGLYASNLEULYSGLY
5   ASPLYSARGILEILETHRASPASPGLUILE
6   ILESERLEUSERILEGLUPHEPHEASPGLN
7   ASNARGLEUASPARGLYSVALASNLYSASP
8   LYSGLULYSSERLYSGLUGLUVALASNASP
9   LYSARGTYRLEUARGCYSPROALAALAMET
10   THRVALMETHISLEUARGLYSPHELEUARG
11   SERLYSMETASPILEPROASNTHRPHEGLN
12   ILEASPVALMETTYRGLUGLUGLUPROLEU
13   LYSASPTYRTYRTHRLEUMETASPILEALA
14   TYRILETYRTHRTRPARGARGASNGLYPRO
15   LEUPROLEULYSTYRARGVALARGPROTHR
16   CYSLYSARGMETLYS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.2 mM; D2O, [U-2H], 10%; sodium chloride 50 mM; TCEP 1 mM; TRIS 100 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303.2 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 HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY, Goddard - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PSVS, Bhattacharya and Montelione - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Rosetta, (Rosetta-Relax)- Tyka, Keedy, Andre, Dimaio, Song, Richardson, Richardson and Baker - refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

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