BMRB Entry 18695

Name: Allosteric communication in the KIX domain proceeds through dynamic re-packing of the hydrophobic core
Published: 2013-06-04

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PDB ID: 2lxt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18695
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Allosteric communication in the KIX domain proceeds through dynamic re-packing of the hydrophobic core

Deposition date:

2012-08-31

Original release date:

2013-06-04

Authors:

Bruschweiler, Sven; Schanda, Paul; Konrat, Robert; Tollinger, Martin

Citation:

Citation: Bruschweiler, Sven; Konrat, Robert; Tollinger, Martin. "Allosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic Core." ACS Chem. Biol. 8, 1600-1610 (2013).
PubMed: 23651431

Assembly members:

Assembly members:
KIX_1, polymer, 87 residues, 10353.954 Da.
KIX_2, polymer, 19 residues, 2061.352 Da.
KIX_3, polymer, 34 residues, 3944.323 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KIX_1: GVRKGWHEHVTQDLRSHLVH KLVQAIFPTPDPAALKDRRM ENLVAYAKKVEGDMYESANS RDEYYHLLAEKIYKIQKELE EKRRSRL
KIX_2: DAGNILPSDIMDFVLKNTP
KIX_3: DSVTDSQKRREILSRRPXYR KILNDLSSDAPGVP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	92
1H chemical shifts	558

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KIX domain complex (3), 1	1
2	KIX domain complex (3), 2	2
3	KIX domain complex (3), 3	3

Entities:

Entity 1, KIX domain complex (3), 1 87 residues - 10353.954 Da.

1

GLY

VAL

ARG

LYS

GLY

TRP

HIS

GLU

HIS

VAL

2

THR

GLN

ASP

LEU

ARG

SER

HIS

LEU

VAL

HIS

3

LYS

LEU

VAL

GLN

ALA

ILE

PHE

PRO

THR

PRO

4

ASP

PRO

ALA

LEU

LYS

ASP

ARG

MET

5

GLU

ASN

LEU

VAL

ALA

TYR

ALA

LYS

VAL

6

GLU

GLY

ASP

MET

TYR

GLU

SER

ALA

ASN

SER

7

ARG

ASP

GLU

TYR

HIS

LEU

ALA

GLU

8

LYS

ILE

TYR

LYS

ILE

GLN

LYS

GLU

LEU

GLU

9

GLU

LYS

ARG

SER

ARG

LEU

Entity 2, KIX domain complex (3), 2 19 residues - 2061.352 Da.

1

ASP

ALA

GLY

ASN

ILE

LEU

PRO

SER

ASP

ILE

2

MET

ASP

PHE

VAL

LEU

LYS

ASN

THR

PRO

Entity 3, KIX domain complex (3), 3 34 residues - 3944.323 Da.

1

ASP

SER

VAL

THR

ASP

SER

GLN

LYS

ARG

2

GLU

ILE

LEU

SER

ARG

PRO

SEP

TYR

ARG

3

LYS

ILE

LEU

ASN

ASP

LEU

SER

ASP

ALA

4

PRO

GLY

VAL

PRO

Samples:

sample_1: KIX_1, [U-100% 13C; U-100% 15N], 1 mM; KIX_2 2 mM; KIX_3, [U-100% 13C; U-100% 15N], 2 mM; sodium chloride 25 mM; potassium phosphate 50 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 500 MHz

Related Database Links:

BMRB	16851 18314 18315 18694 18694 6784 6788
PDB	1KDX 1SB0 2AGH 2KWF 2LQH 2LQI 2LXS 2LXT 2LXS 2LXT 1KDX 2LXT
DBJ	BAE06125 BAG65526 BAI45616 BAD92745 BAA36482 BAC32173 BAC32174 BAG11405 BAG35615
GB	AAB28651 AAC08447 AAC51331 AAC51770 AAH72594 AAA58669 AAA62593 AAQ63624 ABM46715 ABM54290 AAA35715 AAA35716 AAA35717 AAA37456 AAB20597
PRF	1923401A 1504306A
REF	NP_001020603 NP_001073315 NP_001157494 NP_001247644 NP_004371 NP_001074518 NP_001184033 NP_005924 XP_001093874 XP_002188579 NP_001017818 NP_001032815 NP_001041721 NP_001093399 NP_001153276
SP	P45481 Q6JHU9 Q92793 P55200 Q03164 P15337 P16220 P27925 Q01147
TPG	DAA15549 DAA22311 DAA32469
EMBL	CAA93625 CAA32890 CAA39151 CAA40347 CAA42620 CAA47953
PIR	A48205 A40120
AlphaFold	P45481 Q6JHU9 Q92793 P55200 Q03164 P15337 P16220 P27925 Q01147

Download HSQC peak lists in one of the following formats:
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SPARKY: Backbone or all simulated peaks