BMRB: 11286

Solution structure of the BSD domain of human Synapse associated protein 1

Authors

Yoneyama, M., Tochio, N., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.

Assembly

Synapse associated protein 1

Entity

1. Synapse associated protein 1 (polymer, Thiol state: not present), 100 monomers, 11279.63 Da Detail

GSSGSSGTND EETIQQQILA LSADKRNFLR DPPAGVQFNF DFDQMYPVAL VMLQEDELLS KMRFALVPKL VKEEVFWRNY FYRVSLIKQS AQLTSGPSSG

Formula weight

11279.63 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.0 %, Completeness: 94.8 %, Completeness (bb): 95.3 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	94.8 % (1127 of 1189)	93.2 % (579 of 621)	97.2 % (447 of 460)	93.5 % (101 of 108)
Backbone	95.3 % (562 of 590)	92.0 % (185 of 201)	97.3 % (286 of 294)	95.8 % (91 of 95)
Sidechain	94.8 % (657 of 693)	93.8 % (394 of 420)	97.3 % (253 of 260)	76.9 % (10 of 13)
Aromatic	90.6 % (96 of 106)	90.6 % (48 of 53)	90.4 % (47 of 52)	100.0 % (1 of 1)
Methyl	100.0 % (102 of 102)	100.0 % (51 of 51)	100.0 % (51 of 51)

1. BSD domain

GSSGSSGTND EETIQQQILA LSADKRNFLR DPPAGVQFNF DFDQMYPVAL VMLQEDELLS KMRFALVPKL VKEEVFWRNY FYRVSLIKQS AQLTSGPSSG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.001) atm, Temperature 296 (±0.1) K, pH 7.0 (±0.05), Details 1.03mM BSD domain U-15N, {13C;} 20mM d-Tris-HCl {(pH7.0);} 100mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	BSD domain	[U-13C; U-15N]	protein	1.03 mM
2	d-Tris-HCl	natural abundance	buffer	20 mM
3	NaCl	natural abundance	salt	100 mM
4	d-DTT	natural abundance	salt	1 mM
5	NaN3	natural abundance	salt	0.02 %
6	H2O		solvent	90 %
7	D2O		solvent	10 %

Hide sample codition

LACS Plot; CA

Referencing offset: -0.27 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; CB

Referencing offset: -0.27 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; HA

Referencing offset: 0.01 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; CO

Referencing offset: -0.04 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

Protein Blocks Logo

Calculated from 20 models in PDB: 1X3A, Strand ID: A Detail

---

Release date

2011-08-17

Citation

Structural and dynamical insights into the PH domain of p62 in human TFIIH
Yoneyama, M., Tochio, N., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.
Nucleic Acids Res. (2021), 49, 2916-2930, PubMed 33211877 , DOI 10.1093/nar/gkaa1045 , Abstract

Related entities 1. Synapse associated protein 1, : 1 : 16 entities Detail

Interaction partners 1. Synapse associated protein 1, : 5 interactors Detail

Experiments performed 2 experiments Detail