BMRB Entry 17030

Name: Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F
Published: 2010-07-07

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PDB ID: 2l05
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17030
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F

Deposition date:

2010-06-30

Original release date:

2010-07-07

Authors:

Aramini, James; Janjua, Haleema; Ciccosanti, Colleen; Shastry, Ritu; Huang, Yuanpeng; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation:

Citation: Aramini, James; Janjua, Haleema; Ciccosanti, Colleen; Shastry, Ritu; Huang, Yuanpeng; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F" To be published ., .-..

Assembly members:

Assembly members:
HR4694F, polymer, 95 residues, 9778.635 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 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR4694F: MGHHHHHHSHMPKSPQKPIV RVFLPNKQRTVVPARCGVTV RDSLKKALMMRGLIPECCAV YRIQDGEKKPIGWDTDISWL TGEELHVEVLENVPL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	394
15N chemical shifts	89
1H chemical shifts	640

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR4694F	1

Entities:

Entity 1, HR4694F 95 residues - 9778.635 Da.

N-terminal MGHHHHHHSHM tag.

1

MET

GLY

HIS

SER

HIS

2

MET

PRO

LYS

SER

PRO

GLN

LYS

PRO

ILE

VAL

3

ARG

VAL

PHE

LEU

PRO

ASN

LYS

GLN

ARG

THR

4

VAL

PRO

ALA

ARG

CYS

GLY

VAL

THR

VAL

5

ARG

ASP

SER

LEU

LYS

ALA

LEU

MET

6

ARG

GLY

LEU

ILE

PRO

GLU

CYS

ALA

VAL

7

TYR

ARG

ILE

GLN

ASP

GLY

GLU

LYS

PRO

8

ILE

GLY

TRP

ASP

THR

ASP

ILE

SER

TRP

LEU

9

THR

GLY

GLU

LEU

HIS

VAL

GLU

VAL

LEU

10

GLU

ASN

VAL

PRO

LEU

Samples:

sample_1: HR4694F, [U-100% 13C; U-100% 15N], 0.84 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_2: HR4694F, [U-5% 13C; U-100% 15N], 0.69 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 15N-NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC high resolution (L/V methyl stereoassignment)	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-15N hetNOE	sample_1	isotropic	sample_conditions_1
1D 15N T1 and T2	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis

PSVS v1.4, Bhattacharya and Montelione - structure quality analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MolProbity v3.17, Richardson - structure quality analysis

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

PDBStat v5.1, Tejero & Montelione - PDB coordinate analysis

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.112, Goddard - data analysis, peak picking

TALOS+, Shen, Cornilescu, Delaglio and Bax - dihedral angle constraints

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2L05
DBJ	BAD19009 BAE02474 BAE24384 BAI47380
EMBL	CAA46301 CAA47436 CAB81555
GB	AAA35609 AAA49492 AAA49493 AAI01758 AAI12080
PIR	I51153
REF	NP_004324 NP_647455 NP_990633 XP_001070228 XP_001496314
SP	P15056 P28028 P34908 Q04982
TPG	DAA30146
AlphaFold	P15056 P28028 P34908 Q04982