BMRB Entry 16970

Name: Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p peptide
Published: 2010-07-01

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PDB ID: 2kym
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16970
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p peptide

Deposition date:

2010-06-02

Original release date:

2010-07-01

Authors:

Gorelik, Maryna; Muhandiram, Ranjith; Davidson, Alan

Citation:

Citation: Gorelik, Maryna; Stanger, Karen; Davidson, Alan. "A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function." J. Biol. Chem. 286, 19470-19477 (2011).
PubMed: 21489982

Assembly members:

Assembly members:
Bud_emergence_protein_1, polymer, 120 residues, 13772.617 Da.
Peptide_from_Serine/Threonine_kinase_Ste20, polymer, 16 residues, 1639.933 Da.

Natural source:

Natural source: Common Name: ascomycetes Taxonomy ID: 36914 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Lodderomyces elongisporus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET 21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bud_emergence_protein_1: MAPLFAVTLYEFKAERDDEL DVSPGENLSICAHYDYEWFI AKPINRLGGPGLVPVSYVRI IDLMDPAKYASVDTYDREQV MKIIDEFKIPTVEQWKDQTR RYKESSIQIGNGHGQSQGLE
Peptide_from_Serine/Threonine_kinase_Ste20: GKFIPSRPAPKPPSSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	546
15N chemical shifts	122
1H chemical shifts	952

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Bud_emergence_protein_1	1
2	Peptide_from_Serine/Threonine_kinase_Ste20	2

Entities:

Entity 1, Bud_emergence_protein_1 120 residues - 13772.617 Da.

Residues 1-2 and 119-120 represent cloning artifacts

1	MET	ALA	PRO	LEU	PHE	ALA	VAL	THR	LEU	TYR
2	GLU	PHE	LYS	ALA	GLU	ARG	ASP	ASP	GLU	LEU
3	ASP	VAL	SER	PRO	GLY	GLU	ASN	LEU	SER	ILE
4	CYS	ALA	HIS	TYR	ASP	TYR	GLU	TRP	PHE	ILE
5	ALA	LYS	PRO	ILE	ASN	ARG	LEU	GLY	GLY	PRO
6	GLY	LEU	VAL	PRO	VAL	SER	TYR	VAL	ARG	ILE
7	ILE	ASP	LEU	MET	ASP	PRO	ALA	LYS	TYR	ALA
8	SER	VAL	ASP	THR	TYR	ASP	ARG	GLU	GLN	VAL
9	MET	LYS	ILE	ILE	ASP	GLU	PHE	LYS	ILE	PRO
10	THR	VAL	GLU	GLN	TRP	LYS	ASP	GLN	THR	ARG
11	ARG	TYR	LYS	GLU	SER	SER	ILE	GLN	ILE	GLY
12	ASN	GLY	HIS	GLY	GLN	SER	GLN	GLY	LEU	GLU

Entity 2, Peptide_from_Serine/Threonine_kinase_Ste20 16 residues - 1639.933 Da.

1

GLY

LYS

PHE

ILE

PRO

SER

ARG

PRO

ALA

PRO

2

LYS

PRO

SER

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions
3D HNCO	sample_1	isotropic	sample_conditions
3D HN(CO)CA	sample_1	isotropic	sample_conditions
3D HNCACB	sample_1	isotropic	sample_conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions
3D C(CO)NH	sample_1	isotropic	sample_conditions
3D HNCA	sample_1	isotropic	sample_conditions
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions
3D HCCH-COSY	sample_2	isotropic	sample_conditions
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions
15N C13 filtered 2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions
15N C13 filtered 2D 1H-1H NOESY	sample_3	isotropic	sample_conditions
15N C13 filtered 2D 1H-1H COSY	sample_4	isotropic	sample_conditions
13C half-filtered 1H-13C NOESY	sample_4	isotropic	sample_conditions

PDB	2KYM 2KYM 2LCS 2RQW
GB	EDK46053 AAA35038 AAA35111 AAB69747 AHY77690 EDN62227
REF	XP_001524262 NP_011856
BMRB	17629
DBJ	GAA23703
SP	Q03497
TPG	DAA06681
AlphaFold	Q03497

BMRB Entry 16970

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	ALA	PRO	LEU	PHE	ALA	VAL	THR	LEU	TYR
2	GLU	PHE	LYS	ALA	GLU	ARG	ASP	ASP	GLU	LEU
3	ASP	VAL	SER	PRO	GLY	GLU	ASN	LEU	SER	ILE
4	CYS	ALA	HIS	TYR	ASP	TYR	GLU	TRP	PHE	ILE
5	ALA	LYS	PRO	ILE	ASN	ARG	LEU	GLY	GLY	PRO
6	GLY	LEU	VAL	PRO	VAL	SER	TYR	VAL	ARG	ILE
7	ILE	ASP	LEU	MET	ASP	PRO	ALA	LYS	TYR	ALA
8	SER	VAL	ASP	THR	TYR	ASP	ARG	GLU	GLN	VAL
9	MET	LYS	ILE	ILE	ASP	GLU	PHE	LYS	ILE	PRO
10	THR	VAL	GLU	GLN	TRP	LYS	ASP	GLN	THR	ARG
11	ARG	TYR	LYS	GLU	SER	SER	ILE	GLN	ILE	GLY
12	ASN	GLY	HIS	GLY	GLN	SER	GLN	GLY	LEU	GLU

1	MET	ALA	PRO	LEU	PHE	ALA	VAL	THR	LEU	TYR
2	GLU	PHE	LYS	ALA	GLU	ARG	ASP	ASP	GLU	LEU
3	ASP	VAL	SER	PRO	GLY	GLU	ASN	LEU	SER	ILE
4	CYS	ALA	HIS	TYR	ASP	TYR	GLU	TRP	PHE	ILE
5	ALA	LYS	PRO	ILE	ASN	ARG	LEU	GLY	GLY	PRO
6	GLY	LEU	VAL	PRO	VAL	SER	TYR	VAL	ARG	ILE
7	ILE	ASP	LEU	MET	ASP	PRO	ALA	LYS	TYR	ALA
8	SER	VAL	ASP	THR	TYR	ASP	ARG	GLU	GLN	VAL
9	MET	LYS	ILE	ILE	ASP	GLU	PHE	LYS	ILE	PRO
10	THR	VAL	GLU	GLN	TRP	LYS	ASP	GLN	THR	ARG
11	ARG	TYR	LYS	GLU	SER	SER	ILE	GLN	ILE	GLY
12	ASN	GLY	HIS	GLY	GLN	SER	GLN	GLY	LEU	GLU

1	MET	ALA	PRO	LEU	PHE	ALA	VAL	THR	LEU	TYR
2	GLU	PHE	LYS	ALA	GLU	ARG	ASP	ASP	GLU	LEU
3	ASP	VAL	SER	PRO	GLY	GLU	ASN	LEU	SER	ILE
4	CYS	ALA	HIS	TYR	ASP	TYR	GLU	TRP	PHE	ILE
5	ALA	LYS	PRO	ILE	ASN	ARG	LEU	GLY	GLY	PRO
6	GLY	LEU	VAL	PRO	VAL	SER	TYR	VAL	ARG	ILE
7	ILE	ASP	LEU	MET	ASP	PRO	ALA	LYS	TYR	ALA
8	SER	VAL	ASP	THR	TYR	ASP	ARG	GLU	GLN	VAL
9	MET	LYS	ILE	ILE	ASP	GLU	PHE	LYS	ILE	PRO
10	THR	VAL	GLU	GLN	TRP	LYS	ASP	GLN	THR	ARG
11	ARG	TYR	LYS	GLU	SER	SER	ILE	GLN	ILE	GLY
12	ASN	GLY	HIS	GLY	GLN	SER	GLN	GLY	LEU	GLU