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BMRB: 15001

2LD1

Structures and chemical shift assignments for the ADD domain of the ATRX protein

Authors

Yang, J., Neuhaus, D.

Assembly

ADD domain

Entity

1. ADD domain 156-296 (polymer, Thiol state: free and other bound), 142 monomers, 16254.43 Da Detail

GAMADKRGDG LHGIVSCTAC GQQVNHFQKD SIYRHPSLQV LICKNCFKYY MSDDISRDSD GMDEQCRWCA EGGNLICCDF CHNAFCKKCI LRNLGRKELS TIMDENNQWY CYICHPEPLL DLVTACNSVF ENLEQLLQQN KK

2. ZN (non-polymer), 65.409 × 3 Da

Total weight

16450.656 Da

Max. entity weight

16254.43 Da

Entity Connection

na 12 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS17:SG	2:ZN1:ZN
2	na	sing	1:CYS20:SG	2:ZN1:ZN
3	na	sing	1:CYS43:SG	2:ZN1:ZN
4	na	sing	1:CYS46:SG	2:ZN1:ZN
5	na	sing	1:CYS66:SG	2:ZN1:ZN
6	na	sing	1:CYS69:SG	2:ZN1:ZN
7	na	sing	1:CYS86:SG	2:ZN1:ZN
8	na	sing	1:CYS89:SG	2:ZN1:ZN
9	na	sing	1:CYS78:SG	2:ZN1:ZN
10	na	sing	1:CYS81:SG	2:ZN1:ZN
11	na	sing	1:CYS111:SG	2:ZN1:ZN
12	na	sing	1:CYS114:SG	2:ZN1:ZN

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 79.8 %, Completeness (bb): 83.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	79.8 % (1317 of 1650)	85.5 % (738 of 863)	69.9 % (438 of 627)	88.1 % (141 of 160)
Backbone	83.8 % (709 of 846)	97.2 % (282 of 290)	69.8 % (291 of 417)	97.8 % (136 of 139)
Sidechain	78.8 % (738 of 937)	79.6 % (456 of 573)	80.8 % (277 of 343)	23.8 % (5 of 21)
Aromatic	91.0 % (122 of 134)	100.0 % (67 of 67)	81.5 % (53 of 65)	100.0 % (2 of 2)
Methyl	99.2 % (121 of 122)	98.4 % (60 of 61)	100.0 % (61 of 61)

1. ADD domain 156-296

GAMADKRGDG LHGIVSCTAC GQQVNHFQKD SIYRHPSLQV LICKNCFKYY MSDDISRDSD GMDEQCRWCA EGGNLICCDF CHNAFCKKCI LRNLGRKELS TIMDENNQWY CYICHPEPLL DLVTACNSVF ENLEQLLQQN KK

Show sample condition

Sample

Pressure 1 atm, Temperature 300 K, pH 6.7

#	Name	Isotope labeling	Concentration
1	ADD domain 156-296	[U-15N]	0.6 ~ 0.8 mM
2	TRIS	none	20 mM
3	DTT	none	1 mM
4	zinc chloride	none	100 uM
5	sodium chloride	none	0.5 M

LACS Plot; CA

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

Referencing offset: -0.03 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: -0.03 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: -0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 34 models in PDB: 2LD1, Strand ID: A Detail

Release date

2007-06-17

Citation

Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX
Argentaro, A., Yang, J., Chapman, L., Kowalczyk, M.S., Gibbons, R.J., Higgs, D.R., Neuhaus, D., Rhodes, D.
Proc. Natl. Acad. Sci. U. S. A. (2007), 104, 11939-11944, PubMed 17609377 , DOI 10.1073/pnas.0704057104 , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P46100 released on 1995-11-01
Title ATRX_HUMAN Entity Transcriptional regulator ATRX

Related entities 1. ADD domain 156-296, : 1 : 1 : 20 entities Detail

Interaction partners 1. ADD domain 156-296, : 33 interactors Detail

More details for 33 interactors identified by 16 citations

Experiments performed 15 experiments Detail

1 2D 1H-15N HSQC