BMRB Entry 51413

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51413

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Title:
Bromodomain Interactions with Acetylated Histone 4 Peptides in the Tandem Domain BRD4 -- Effects on Domain Dynamics and Internal Flexibility
Deposition date:
2022-04-26
Original release date:
2022-10-11
Authors:
Wernersson, Sven; Romel, Bobby; Flavell, Liz; Milbradt, Alexander; Holdgate, Geoff; Embrey, Kevin; Akke, Mikael
Citation:

Citation: Wernersson, Sven; Bobby, Romel; Flavell, Liz; Milbradt, Alexander; Holdgate, Geoffrey; Embrey, Kevin; Akke, Mikael. "Bromodomain Interactions with Acetylated Histone 4 Peptides in the BRD4 Tandem Domain: Effects on Domain Dynamics and Internal Flexibility"  Biochemistry 61, 2303-2318 (2022).
PubMed: 36215732

Assembly members:

Assembly members:
entity_1, polymer, 417 residues, Formula weight is not available
entity_2, polymer, 16 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   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NPPPPETSNPNKPKRQTNQL QYLLRVVLKTLWKHQFAWPF QQPVDAVKLNLPDYYKIIKT PMDMGTIKKRLENNYYWNAQ ECIQDFNTMFTNCYIYNKPG DDIVLMAEALEKLFLQKINE LPTEETEIMIVQAKGRGRGR KETGTAKPGVSTVPNTTQAS TPPQTQTPQPNPPPVQATPH PFPAVTPDLIVQTPVMTVVP PQPLQTPPPVPPQPQPPPAP APQPVQSHPPIIAATPQPVK TKKGVKRKADTTTPTTIDPI HEPPSLPPEPKTTKLGQRRE SSRPVKPPKKDVPDSQQHPA PEKSSKVSEQLKCCSGILKE MFAKKHAAYAWPFYKPVDVE ALGLHDYCDIIKHPMDMSTI KSKLEAREYRDAQEFGADVR LMFSNCYKYNPPDHEVVAMA RKLQDVFEMRFAKMPDE
entity_2: SGRGXGGXGLGXGGAX

Data typeCount
15N chemical shifts191
1H chemical shifts191
T1 relaxation values381
T2 relaxation values384
dipole-CSA cross correlation relaxation values180
heteronuclear NOE values377
order parameters71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BD1-link-BD21
2H4Kac2

Entities:

Entity 1, BD1-link-BD2 417 residues - Formula weight is not available

1   ASNPROPROPROPROGLUTHRSERASNPRO
2   ASNLYSPROLYSARGGLNTHRASNGLNLEU
3   GLNTYRLEULEUARGVALVALLEULYSTHR
4   LEUTRPLYSHISGLNPHEALATRPPROPHE
5   GLNGLNPROVALASPALAVALLYSLEUASN
6   LEUPROASPTYRTYRLYSILEILELYSTHR
7   PROMETASPMETGLYTHRILELYSLYSARG
8   LEUGLUASNASNTYRTYRTRPASNALAGLN
9   GLUCYSILEGLNASPPHEASNTHRMETPHE
10   THRASNCYSTYRILETYRASNLYSPROGLY
11   ASPASPILEVALLEUMETALAGLUALALEU
12   GLULYSLEUPHELEUGLNLYSILEASNGLU
13   LEUPROTHRGLUGLUTHRGLUILEMETILE
14   VALGLNALALYSGLYARGGLYARGGLYARG
15   LYSGLUTHRGLYTHRALALYSPROGLYVAL
16   SERTHRVALPROASNTHRTHRGLNALASER
17   THRPROPROGLNTHRGLNTHRPROGLNPRO
18   ASNPROPROPROVALGLNALATHRPROHIS
19   PROPHEPROALAVALTHRPROASPLEUILE
20   VALGLNTHRPROVALMETTHRVALVALPRO
21   PROGLNPROLEUGLNTHRPROPROPROVAL
22   PROPROGLNPROGLNPROPROPROALAPRO
23   ALAPROGLNPROVALGLNSERHISPROPRO
24   ILEILEALAALATHRPROGLNPROVALLYS
25   THRLYSLYSGLYVALLYSARGLYSALAASP
26   THRTHRTHRPROTHRTHRILEASPPROILE
27   HISGLUPROPROSERLEUPROPROGLUPRO
28   LYSTHRTHRLYSLEUGLYGLNARGARGGLU
29   SERSERARGPROVALLYSPROPROLYSLYS
30   ASPVALPROASPSERGLNGLNHISPROALA
31   PROGLULYSSERSERLYSVALSERGLUGLN
32   LEULYSCYSCYSSERGLYILELEULYSGLU
33   METPHEALALYSLYSHISALAALATYRALA
34   TRPPROPHETYRLYSPROVALASPVALGLU
35   ALALEUGLYLEUHISASPTYRCYSASPILE
36   ILELYSHISPROMETASPMETSERTHRILE
37   LYSSERLYSLEUGLUALAARGGLUTYRARG
38   ASPALAGLNGLUPHEGLYALAASPVALARG
39   LEUMETPHESERASNCYSTYRLYSTYRASN
40   PROPROASPHISGLUVALVALALAMETALA
41   ARGLYSLEUGLNASPVALPHEGLUMETARG
42   PHEALALYSMETPROASPGLU

Entity 2, H4Kac 16 residues - Formula weight is not available

1   SERGLYARGGLYALYGLYGLYALYGLYLEU
2   GLYALYGLYGLYALAALY

Samples:

sample_1: apo Bromodomain 1 (BD1) of BRD4, [U-100% 13C; U-100% 15N], 0.135 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 1 mM; H4Kac 1.5 mM

sample_conditions_1: ionic strength: 0.180 M; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
transverse cross-correlated dipole/CSA relaxationsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMRPipe - processing

Relax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • 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