BMRBj - BMREntryMaster

Found 1 Document (1.538 seconds)

BMRB: 25171

2MTN

Solution structure of MLL-IBD complex

Authors

Cierpicki, T., Pollock, J., Murai, M.

Assembly

MLL-IBD complex

Entity

1. MLL-IBD complex, entity 1 (polymer, Thiol state: not present), 50 monomers, 4933.302 Da Detail

GPAMAPGFDA ALQVSAAIGT NLRRFRAVFG ESGGGGGSGE DEQFLGFGSD

2. MLL-IBD complex, entity 2 (polymer), 114 monomers, 13266.38 Da Detail

EEVRVRGSVK KVEKKRETSM DSRLQRIHAE IKNSLKIDNL DVNRCIEALD ELASLQVTMQ QAQKHTEMIT TLKKIRRFKV SQVIMEKSTM LYNKFKNMFL VGEGDSVITQ VLNK

Total weight

18199.682 Da

Max. entity weight

13266.38 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.1 %, Completeness: 67.9 %, Completeness (bb): 85.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	67.9 % (1294 of 1906)	60.6 % (605 of 999)	73.9 % (539 of 729)	84.3 % (150 of 178)
Backbone	85.7 % (840 of 980)	78.6 % (268 of 341)	89.9 % (429 of 477)	88.3 % (143 of 162)
Sidechain	54.8 % (589 of 1075)	51.2 % (337 of 658)	61.1 % (245 of 401)	43.8 % (7 of 16)
Aromatic	42.7 % (41 of 96)	85.4 % (41 of 48)	0.0 % (0 of 48)
Methyl	83.1 % (148 of 178)	82.0 % (73 of 89)	84.3 % (75 of 89)

1. entity 1

GPAMAPGFDA ALQVSAAIGT NLRRFRAVFG ESGGGGGSGE DEQFLGFGSD

2. entity 2

EEVRVRGSVK KVEKKRETSM DSRLQRIHAE IKNSLKIDNL DVNRCIEALD ELASLQVTMQ QAQKHTEMIT TLKKIRRFKV SQVIMEKSTM LYNKFKNMFL VGEGDSVITQ VLNK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.34mM MLL-IBD in 50mM phosphate buffer, pH 6.5, 50mM NaCl

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	0.34 mM
2	entity_2	natural abundance	0.34 mM
3	potassium phosphate	natural abundance	50 mM
4	sodium chloride	natural abundance	50 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	water	protons	4.75 ppm	internal	direct	1.0

Referencing offset: -0.28 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	water	protons	4.75 ppm	internal	direct	1.0

Referencing offset: -0.28 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	water	protons	4.75 ppm	internal	direct	1.0

Referencing offset: -0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	water	protons	4.75 ppm	internal	direct	1.0

Referencing offset: 0.06 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MTN, Strand ID: A Detail

Release date

2016-09-27

Citation

The same site on the integrase-binding domain of lens epithelium-derived growth factor is a therapeutic target for MLL leukemia and HIV
Cierpicki, T., Pollock, J., Murai, M.
Blood (2014), 124, 3730-3737, PubMed 25305204 , DOI 10.1182/blood-2014-01-550079 , Abstract

Related entities 1. MLL-IBD complex, entity 1, : 1 : 1 : 15 entities Detail

Related entities 2. MLL-IBD complex, entity 2, : 3 : 6 entities Detail

Interaction partners 1. MLL-IBD complex, entity 1, : 38 interactors Detail

More details for 38 interactors identified by 16 citations

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_25171_2mtn.nef
Input source #2: Coordindates	2mtn.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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Sequence alignments

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

---110-------120-------130-------140-------150---330-------340-------350-------360-------370-------3
GPAMAPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRGSVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GPAMAPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRGSVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALD
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

80-------390-------400-------410-------420-------430-------440--
ELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNK
-------110-------120-------130-------140-------150-------160----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	164	0	0	100.0

Content subtype: combined_25171_2mtn.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1269		91.5 (chain: A, length: 164)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	400 (1)	noe	51.8 (chain: A, length: 164)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	126 (126)	.	44.5 (chain: A, length: 164)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 164, Sequence coverage: 91.5%
- Total number of assignments
  - ¹H chemical shifts: 588
  - ¹³C chemical shifts: 533
  - ¹⁵N chemical shifts: 148
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	999	588	58.9
¹³C chemical shifts	729	533	73.1
¹⁵N chemical shifts	189	148	78.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	341	265	77.7
¹³C chemical shifts	328	295	89.9
¹⁵N chemical shifts	162	142	87.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	658	323	49.1
¹³C chemical shifts	401	238	59.4
¹⁵N chemical shifts	27	6	22.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	96	78	81.2
¹³C chemical shifts	96	77	80.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	41	85.4
¹³C chemical shifts	48	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 164, Sequence coverage: 51.8%
- Total number of restraints: 400
- Weight of restraints: 1.0 (400)
- Potential type of restraints: upper-bound-parabolic (400)
- Range of distance target values: 2.84, 5.5 (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: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 164, Sequence coverage: 44.5%
- Total number of restraints: 126
- Total number of restraints per polymer type: 126
- Weight of restraints: 1.0 (126)
- Potential type of restraints: square-well-parabolic (126)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords Protein-protein complex

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.538 seconds)

BMRB: 25171

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. MLL-IBD complex, entity 1, : 1 : 1 : 15 entities Detail

Related entities 2. MLL-IBD complex, entity 2, : 3 : 6 entities Detail

Interaction partners 1. MLL-IBD complex, entity 1, : 38 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail