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BMRB: 18462

2LT7

Solution NMR structure of Kaiso zinc finger DNA binding domain in complex with Kaiso binding site DNA

Authors

Buck-Koehntop, B.A., Stanfield, R.L., Ekiert, D.C., Martinez-Yamout, M.A., Dyson, H., Wilson, I.A., Wright, P.E.

Assembly

Kaiso

Entity

1. Kaiso (polymer, Thiol state: free and other bound), 133 monomers, 16052.29 Da Detail

ANKRMKVKHD DHYELIVDGR VYYICIVCKR SYVCLTSLRR HFNIHSWEKK YPCRYCEKVF PLAEYRTKHE IHHTGERRYQ CLACGKSFIN YQFMSSHIKS VHSQDPSGDS KLYRLHPCRS LQIRQYAYLS DRS

2. DNA strand 1 (polymer, Thiol state: not present), 19 monomers, 5843.719 Da Detail

GTGCTTCCTG CCAATAACG

3. DNA strand 2 (polymer, Thiol state: not present), 19 monomers, 5932.781 Da Detail

CGTTATTGGC AGGAAGCAC

4. ZINC ION (non-polymer, Thiol state: not present), 65.409 × 3 Da

Total weight

28025.018 Da

Max. entity weight

16052.29 Da

Entity Connection

na 12 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS25:SG	4:ZN1:ZN
2	na	sing	1:CYS28:SG	4:ZN1:ZN
3	na	sing	1:HIS41:ND1	4:ZN1:ZN
4	na	sing	1:HIS45:ND1	4:ZN1:ZN
5	na	sing	1:CYS53:SG	4:ZN1:ZN
6	na	sing	1:CYS56:SG	4:ZN1:ZN
7	na	sing	1:HIS69:ND1	4:ZN1:ZN
8	na	sing	1:HIS73:ND1	4:ZN1:ZN
9	na	sing	1:CYS81:SG	4:ZN1:ZN
10	na	sing	1:CYS84:SG	4:ZN1:ZN
11	na	sing	1:HIS97:ND1	4:ZN1:ZN
12	na	sing	1:HIS102:ND1	4:ZN1:ZN

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 94.4 %, Completeness (bb): 93.3 % Detail

Polymer type: polypeptide(L) polydeoxyribonucleotide

	Total	¹H	¹³C	¹⁵N
All	94.4 % (1898 of 2010)	93.4 % (1153 of 1234)	95.6 % (610 of 638)	97.8 % (135 of 138)
Backbone	93.3 % (985 of 1056)	88.5 % (471 of 532)	98.2 % (388 of 395)	97.7 % (126 of 129)
Sidechain	96.1 % (1041 of 1083)	97.2 % (682 of 702)	94.1 % (350 of 372)	100.0 % (9 of 9)
Aromatic	95.1 % (251 of 264)	96.5 % (164 of 170)	92.5 % (86 of 93)	100.0 % (1 of 1)
Methyl	100.0 % (119 of 119)	100.0 % (64 of 64)	100.0 % (55 of 55)

1. Kaiso

ANKRMKVKHD DHYELIVDGR VYYICIVCKR SYVCLTSLRR HFNIHSWEKK YPCRYCEKVF PLAEYRTKHE IHHTGERRYQ CLACGKSFIN YQFMSSHIKS VHSQDPSGDS KLYRLHPCRS LQIRQYAYLS DRS

2. DNA strand 1

GTGCTTCCTG CCAATAACG

3. DNA strand 2

CGTTATTGGC AGGAAGCAC

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	Kaiso	[U-13C; U-15N]	500 uM
2	Kaiso binding sequence (KBS)	natural abundance	500 uM
3	Tris	natural abundance	10 mM
4	TCEP	natural abundance	1 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
13	Kaiso	[U-13C; U-15N]	500 uM
14	Kaiso binding sequence (KBS)	natural abundance	500 uM
15	Tris	natural abundance	10 mM
16	TCEP	natural abundance	1 mM
17	D2O	natural abundance	100 %

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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.42 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.42 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.04 ppm, Outliers: 2 Detail

LACS Plot; CO

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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.24 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LT7, Strand ID: A Detail

Release date

2012-05-15

Citation

Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso
Buck-Koehntop, B.A., Stanfield, R.L., Ekiert, D.C., Martinez-Yamout, M.A., Dyson, H., Wilson, I.A., Wright, P.E.
Proc. Natl. Acad. Sci. U. S. A. (2012), 109, 15229-15234, PubMed 22949637 , DOI 10.1073/pnas.1213726109 , Abstract

Related entities 1. Kaiso, : 1 : 13 : 2 : 2 : 160 entities Detail

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	Kaiso	[U-13C; U-15N]	500 uM
2	Kaiso binding sequence (KBS)	natural abundance	500 uM
3	Tris	natural abundance	10 mM
4	TCEP	natural abundance	1 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

2 2D 1H-13C HSQC

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
13	Kaiso	[U-13C; U-15N]	500 uM
14	Kaiso binding sequence (KBS)	natural abundance	500 uM
15	Tris	natural abundance	10 mM
16	TCEP	natural abundance	1 mM
17	D2O	natural abundance	100 %

3 3D HNCO

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

4 3D HNCA

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

5 3D HNCACB

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

6 3D CBCA(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

7 3D HN(CO)CA

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

8 3D HCCH-COSY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
13	Kaiso	[U-13C; U-15N]	500 uM
14	Kaiso binding sequence (KBS)	natural abundance	500 uM
15	Tris	natural abundance	10 mM
16	TCEP	natural abundance	1 mM
17	D2O	natural abundance	100 %

9 3D CBCGCD

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
13	Kaiso	[U-13C; U-15N]	500 uM
14	Kaiso binding sequence (KBS)	natural abundance	500 uM
15	Tris	natural abundance	10 mM
16	TCEP	natural abundance	1 mM
17	D2O	natural abundance	100 %

10 3D 1H-15N NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	Kaiso	[U-13C; U-15N]	500 uM
2	Kaiso binding sequence (KBS)	natural abundance	500 uM
3	Tris	natural abundance	10 mM
4	TCEP	natural abundance	1 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

11 3D 1H-13C NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
13	Kaiso	[U-13C; U-15N]	500 uM
14	Kaiso binding sequence (KBS)	natural abundance	500 uM
15	Tris	natural abundance	10 mM
16	TCEP	natural abundance	1 mM
17	D2O	natural abundance	100 %

12 2D 1H-1H NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
7	Kaiso	[U-100% 13C; U-100% 15N; U-80% 2H]	500 uM
8	Kaiso binding sequence (KBS)	natural abundance	500 uM
9	Tris	natural abundance	10 mM
10	TCEP	natural abundance	1 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18462_2lt7.nef
Input source #2: Coordindates	2lt7.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)
1:41:HIS:NE2	4:1:ZN:ZN	unknown	unknown	n/a
1:45:HIS:NE2	4:1:ZN:ZN	unknown	unknown	n/a
1:73:HIS:NE2	4:2:ZN:ZN	unknown	unknown	n/a
1:97:HIS:NE2	4:3:ZN:ZN	unknown	unknown	n/a
1:102:HIS:NE2	4:3:ZN:ZN	unknown	unknown	n/a
1:69:HIS:NE2	4:2:ZN:ZN	unknown	unknown	n/a
1:56:CYS:SG	4:2:ZN:ZN	unknown	unknown	n/a
1:25:CYS:SG	4:1:ZN:ZN	unknown	unknown	n/a
1:84:CYS:SG	4:3:ZN:ZN	unknown	unknown	n/a
1:28:CYS:SG	4:1:ZN:ZN	unknown	unknown	n/a
1:81:CYS:SG	4:3:ZN:ZN	unknown	unknown	n/a
1:53:CYS:SG	4:2:ZN:ZN	unknown	unknown	n/a

Non-standard residues

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

Sequence alignments

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

------480-------490-------500-------510-------520-------530-------540-------550-------560-------570-
ANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQCLACGKSFINYQFMSSHIKS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQCLACGKSFINYQFMSSHIKS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

------580-------590-------600----
VHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRS
|||||||||||||||||||||||||||||||||
VHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRS
-------110-------120-------130---

Entity_assembly_ID (NMR): D vs Auth_asym_ID (model): D
Entity_assembly_ID (NMR): E vs Auth_asym_ID (model): E

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	133	100.0
D	D	19	100.0
E	E	19	100.0

Content subtype: combined_18462_2lt7.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_KBS	Warning	1929		100.0 (chain: A, length: 133), 100.0 (chain: D, length: 19), 100.0 (chain: E, length: 19)
1	Distance restraints	AMBER_distance_constraints_2	OK	1760 (1)	noe	97.0 (chain: A, length: 133), 100.0 (chain: D, length: 19), 100.0 (chain: E, length: 19)
1	Dihedral angle restraints	AMBER_dihedral_7	Warning	474 (447)	.	100.0 (chain: A, length: 133), 100.0 (chain: D, length: 19), 100.0 (chain: E, length: 19)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_KBS

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 100.0%

------480-------490-------500-------510-------520-------530-------540-------550-------560-------570-
ANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQCLACGKSFINYQFMSSHIKS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQCLACGKSFINYQFMSSHIKS

------580-------590-------600----
VHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRS
|||||||||||||||||||||||||||||||||
VHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRS

Entity_assembly_ID: D, Chain length: 19, Sequence coverage: 100.0%

--------10---------
GTGCTTCCTGCCAATAACG
|||||||||||||||||||
GTGCTTCCTGCCAATAACG

Entity_assembly_ID: E, Chain length: 19, Sequence coverage: 100.0%

20-------30--------
CGTTATTGGCAGGAAGCAC
|||||||||||||||||||
CGTTATTGGCAGGAAGCAC

Total number of assignments
- ¹H chemical shifts: 1158
- ¹³C chemical shifts: 607
- ¹⁵N chemical shifts: 164

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
480	HIS	ND1	200.103
480	HIS	NE2	177.428
483	HIS	ND1	205.16
483	HIS	NE2	180.13
512	HIS	HD1	12.785
512	HIS	ND1	175.97
512	HIS	NE2	214.773
516	HIS	ND1	169.208
516	HIS	NE2	213.846
540	HIS	ND1	173.489
540	HIS	NE2	217.21
543	HIS	ND1	190.035
543	HIS	NE2	177.109
544	HIS	ND1	172.212
544	HIS	NE2	215.603
568	HIS	ND1	174.478
568	HIS	NE2	217.699
573	HIS	ND1	171.233
573	HIS	NE2	214.171
587	HIS	ND1	235.363
587	HIS	NE2	168.675

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	863	846	98.0
¹³C chemical shifts	638	607	95.1
¹⁵N chemical shifts	151	144	95.4

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	266	260	97.7
¹³C chemical shifts	266	260	97.7
¹⁵N chemical shifts	129	126	97.7

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	597	586	98.2
¹³C chemical shifts	372	347	93.3
¹⁵N chemical shifts	22	18	81.8

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	57	56	98.2
¹³C chemical shifts	57	56	98.2

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	94	91	96.8
¹³C chemical shifts	93	86	92.5
¹⁵N chemical shifts	1	1	100.0

Entity_assemble_ID: D
Entity_assemble_ID: E

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	188	159	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	106	79.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	53	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	5	100.0
¹³C chemical shifts	5	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	12	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	183	152	83.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	107	80.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	45	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	15	93.8

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: 133, Sequence coverage: 97.0%
  - Entity_assembly_ID: D, Chain length: 19, Sequence coverage: 100.0%
  - Entity_assembly_ID: E, Chain length: 19, Sequence coverage: 100.0%
- Total number of restraints: 1740
- Weight of restraints: 1.0 (1740)
- Potential type of restraints: square-well-parabolic (1740)
- Range of distance target values: 2.15, 10.93 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
  - Chain_ID: D
  - Chain_ID: E
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: AMBER_dihedral_7
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 100.0%
  - Entity_assembly_ID: D, Chain length: 19, Sequence coverage: 100.0%
  - Entity_assembly_ID: E, Chain length: 19, Sequence coverage: 100.0%
- Total number of restraints: 447
- Total number of restraints per polymer type: 447
- Weight of restraints: 1.0 (447)
- Potential type of restraints: square-well-parabolic (447)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: D
  - Chain_ID: E

Keywords double helix, protein-DNA complex, zinc finger

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Found 1 Document (0.828 seconds)

BMRB: 18462

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Kaiso, : 1 : 13 : 2 : 2 : 160 entities Detail

Experiments performed 12 experiments Detail

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NMR combined restraints 4 contents Detail