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Found 1 Document (0.613 seconds)

BMRB: 34182

6EMR

Solution structure of the LEDGF/p75 IBD - IWS1 (aa 446-548) complex

Authors

Veverka, V.

Assembly

PC4 and SFRS1-interacting protein,Protein IWS1 homolog

Entity

1. PC4 and SFRS1-interacting protein,Protein IWS1 homolog (polymer, Thiol state: all free), 206 monomers, 23803.20 Da Detail

SNAASWETSM DSRLQRIHAE IKNSLKIDNL DVNRCIEALD ELASLQVTMQ QAQKHTEMIT TLKKIRRFKV SQVIMEKSTM LYNKFKNMFL VGEGDSVITQ VLNKELSDKK NEEKDLFGSD SESGNEEENL IADIFGESGD EEEEEFTGFN QEDLEEEKGE TQVKEAEDSD SDDNIKRGKH MDFLSDFEMM LQRKKSMSGK RRRNRD

Formula weight

23803.2 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.5 %, Completeness: 92.3 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.3 % (2240 of 2427)	91.2 % (1170 of 1283)	93.7 % (856 of 914)	93.0 % (214 of 230)
Backbone	97.1 % (1200 of 1236)	96.9 % (409 of 422)	97.4 % (592 of 608)	96.6 % (199 of 206)
Sidechain	88.3 % (1225 of 1387)	87.9 % (757 of 861)	90.4 % (454 of 502)	58.3 % (14 of 24)
Aromatic	69.7 % (85 of 122)	85.2 % (52 of 61)	53.3 % (32 of 60)	100.0 % (1 of 1)
Methyl	99.4 % (173 of 174)	98.9 % (86 of 87)	100.0 % (87 of 87)

1. entity 1

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7, Details 0.5 mM [U-13C; U-15N] LEDGF/p75 IBD-IWS1, 50 mM TRIS, 150 mM sodium chloride, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	LEDGF/p75 IBD-IWS1	[U-13C; U-15N]	0.5 mM
2	TRIS	natural abundance	50 mM
3	sodium chloride	natural abundance	150 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.22 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.22 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

Release date

2018-07-16

Citation

Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation
Sharma, S., Cermakova, K., De Rijck, J., Demeulemeester, J., Fabry, M., El Ashkar, S., Van Belle, S., Lepsik, M., Tesina, P., Duchoslav, V., Novak, P., Hubalek, M., Srb, P., Christ, F., Rezacova, P., Hodges, H.C., Debyser, Z., Veverka, V.
Proc. Natl. Acad. Sci. U. S. A. (2018), 115, E7053-E7062, PubMed 29997176 , DOI 10.1073/pnas.1803909115 , Abstract

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 34179 released on 2018-07-16
    Title Solution structure of the LEDGF/p75 IBD - JPO2 (aa 1-32) complex
  BMRB: 34180 released on 2018-07-16
    Title Solution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex
  BMRB: 34181 released on 2018-07-16
    Title Solution structure of the LEDGF/p75 IBD - MLL1 (aa 111-160) complex

Related entities 1. PC4 and SFRS1-interacting protein,Protein IWS1 homolog, : 1 : 3 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34182_6emr.nef
Input source #2: Coordindates	6emr.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	446	.	Not matched with CCD	None
A	443	.	Not matched with CCD	None
A	444	.	Not matched with CCD	None
A	445	.	Not matched with CCD	None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

---------                                                                                           
....SNAAS                                                                                           
    |||||                                                                                           
-.-.-N-ASWETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDS
 - - - ---------10--------20--------30--------40--------50--------60--------70--------80--------90--

                                                                                                    
                                                                                                    
                                                                                                    
VITQVLNKELSDKKNEEKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKGETQVKEAEDSDSDDNIKRGKHMDFLSDFEMMLQRKKS
-----100-------110-------120-------130-------140-------150-------160-------170-------180-------190--

          
          
          
MSGKRRRNRD
-----200--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	206	4	0	100.0

Content subtype: combined_34182_6emr.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Error	2191		97.6 (chain: A, length: 210)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Error	4064 (1)	noe	94.8 (chain: A, length: 210)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	226 (226)	.	63.8 (chain: A, length: 210)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Error
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 210, Sequence coverage: 97.6%
- Total number of assignments
  - ¹H chemical shifts: 1142
  - ¹³C chemical shifts: 838
  - ¹⁵N chemical shifts: 211
- Completeness of assignments
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Error
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 210, Sequence coverage: 94.8%
- Total number of restraints: 4064
- Weight of restraints: 1.0 (4064)
- Potential type of restraints: square-well-parabolic (4064)
- Range of distance target values: 1.22, 2.85 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 210, Sequence coverage: 63.8%
- Total number of restraints: 226
- Total number of restraints per polymer type: 226
- Weight of restraints: 1.0 (226)
- Potential type of restraints: square-well-parabolic (226)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords TRANSCRIPTION, epigenetics, leukemia, protein-protein complex

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Found 1 Document (0.613 seconds)

BMRB: 34182

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. PC4 and SFRS1-interacting protein,Protein IWS1 homolog, : 1 : 3 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail