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Found 1 Document (3.011 seconds)

BMRB: 16015

2KA6

Structure of protein complex

Authors

Wojciak, J.M., Martinez-Yamout, M.A., Dyson, H.J., Wright, P.E.

Assembly

TAZ2/STAT1 complex

Entity

1. TAZ2 (polymer, Thiol state: free and other bound), 92 monomers, 10505.38 Da Detail

SPQESRRLSI QRCIQSLVHA CQCRNANCSL PSCQKMKRVV QHTKGCKRKT NGGCPVCKQL IALCCYHAKH CQENKCPVPF CLNIKHKLRQ QQ

2. STAT1 (polymer, Thiol state: not present), 45 monomers, 5037.548 Da Detail

GSHMSEVHPS RLQTTDNLLP MSPEEFDEVS RIVGSVEFDS MMNTV

3. ZN (non-polymer), 65.409 × 3 Da

Total weight

15739.154 Da

Max. entity weight

10505.38 Da

Source organism

Mus musculus , Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 87.7 %, Completeness (bb): 82.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.7 % (1400 of 1597)	95.6 % (810 of 847)	74.4 % (448 of 602)	95.9 % (142 of 148)
Backbone	82.3 % (663 of 806)	97.4 % (264 of 271)	68.0 % (276 of 406)	95.3 % (123 of 129)
Sidechain	93.9 % (867 of 923)	94.8 % (546 of 576)	92.1 % (302 of 328)	100.0 % (19 of 19)
Aromatic	57.6 % (38 of 66)	69.7 % (23 of 33)	45.5 % (15 of 33)
Methyl	100.0 % (118 of 118)	100.0 % (59 of 59)	100.0 % (59 of 59)

1. TAZ2

SPQESRRLSI QRCIQSLVHA CQCRNANCSL PSCQKMKRVV QHTKGCKRKT NGGCPVCKQL IALCCYHAKH CQENKCPVPF CLNIKHKLRQ QQ

2. STAT1

GSHMSEVHPS RLQTTDNLLP MSPEEFDEVS RIVGSVEFDS MMNTV

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 290 K, pH 6.8

#	Name	Isotope labeling	Concentration
1	TAZ2	[U-100% 15N]	1 mM
2	STAT1	natural abundance
3	ZINC_ION	natural abundance
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

LACS Plot; CA

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

Referencing offset: 0.25 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.25 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2KA6, Strand ID: A, B Detail

Release date

2015-09-01

Citation

Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains
Wojciak, J.M., Martinez-Yamout, M.A., Dyson, H.J., Wright, P.E.
EMBO J. (2009), 28, 948-958, PubMed 19214187 , DOI 10.1038/emboj.2009.30 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 16014 released on 2009-02-15
Title Structure of protein complex

Related entities 1. TAZ2, : 9 : 44 entities Detail

Related entities 2. STAT1, : 1 : 8 entities Detail

Interaction partners 1. TAZ2, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Interaction partners 2. STAT1, : 74 : 1 interactors Detail

More details for 75 interactors identified by 36 citations

Experiments performed 1 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16015_2ka6.nef
Input source #2: Coordindates	2ka6.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:19:HIS:NE2	3:1:ZN:ZN	unknown	unknown	n/a
1:23:CYS:SG	3:1:ZN:ZN	unknown	unknown	n/a
1:28:CYS:SG	3:1:ZN:ZN	unknown	unknown	n/a
1:33:CYS:SG	3:1:ZN:ZN	unknown	unknown	n/a
1:42:HIS:NE2	3:2:ZN:ZN	unknown	unknown	n/a
1:46:CYS:SG	3:2:ZN:ZN	unknown	unknown	n/a
1:54:CYS:SG	3:2:ZN:ZN	unknown	unknown	n/a
1:57:CYS:SG	3:2:ZN:ZN	unknown	unknown	n/a
1:67:HIS:NE2	3:3:ZN:ZN	unknown	unknown	n/a
1:71:CYS:SG	3:3:ZN:ZN	unknown	unknown	n/a
1:76:CYS:SG	3:3:ZN:ZN	unknown	unknown	n/a
1:81:CYS:SG	3:3:ZN:ZN	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
C	1	ZN	ZINC ION	None
C	2	ZN	ZINC ION	None
C	3	ZN	ZINC ION	None

Sequence alignments

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

--------10--------20--------30--------40--------50--------60--------70--------80--------90--
SPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQ

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

--710-------720-------730-------740-------750
GSHMSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV
|||||||||||||||||||||||||||||||||||||||||||||
GSHMSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV
--------10--------20--------30--------40-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	92	0	0	100.0
B	B	45	0	0	100.0

Content subtype: combined_16015_2ka6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	12		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1391		100.0 (chain: A, length: 92), 100.0 (chain: B, length: 45)
1	Distance restraints	AMBER_distance_constraints_2	OK	3184 (1)	noe	100.0 (chain: A, length: 92), 91.1 (chain: B, length: 45)
1	Dihedral angle restraints	AMBER_dihedral_4	OK	193 (193)	.	88.0 (chain: A, length: 92), 33.3 (chain: B, length: 45)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 45, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 815
  - ¹³C chemical shifts: 434
  - ¹⁵N chemical shifts: 142
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- Peptide bond of PRO
- 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
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
43	THR	HG1	5.312

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	589	562	95.4
¹³C chemical shifts	406	296	72.9
¹⁵N chemical shifts	110	100	90.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	182	180	98.9
¹³C chemical shifts	184	91	49.5
¹⁵N chemical shifts	87	84	96.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	407	382	93.9
¹³C chemical shifts	222	205	92.3
¹⁵N chemical shifts	23	16	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	39	100.0
¹³C chemical shifts	39	39	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	14	73.7
¹³C chemical shifts	19	10	52.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	258	242	93.8
¹³C chemical shifts	196	138	70.4
¹⁵N chemical shifts	47	42	89.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	89	83	93.3
¹³C chemical shifts	90	43	47.8
¹⁵N chemical shifts	42	38	90.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	169	159	94.1
¹³C chemical shifts	106	95	89.6
¹⁵N chemical shifts	5	4	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	25	100.0
¹³C chemical shifts	25	25	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	9	64.3
¹³C chemical shifts	14	5	35.7

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: AMBER_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 45, Sequence coverage: 91.1%
- Total number of restraints: 2984
- Weight of restraints: 1.0 (2984)
- Potential type of restraints: square-well-parabolic (2984)
- Range of distance target values: 2.35, 5.7 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: AMBER_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 88.0%
  - Entity_assembly_ID: B, Chain length: 45, Sequence coverage: 33.3%
- Total number of restraints: 193
- Total number of restraints per polymer type: 193
- Weight of restraints: 1.0 (193)
- Potential type of restraints: square-well-parabolic (193)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords CBP/p300, STAT1, TAZ2, transactivation domain

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Found 1 Document (3.011 seconds)

BMRB: 16015

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. TAZ2, : 9 : 44 entities Detail

Related entities 2. STAT1, : 1 : 8 entities Detail

Interaction partners 1. TAZ2, : 1 interactors Detail

Interaction partners 2. STAT1, : 74 : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail