BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17030

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

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

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:
HR4694F, polymer, 95 residues, 9778.635 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data typeCount
13C chemical shifts394
15N chemical shifts89
1H chemical shifts640

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4694F1

Entities:

Entity 1, HR4694F 95 residues - 9778.635 Da.

N-terminal MGHHHHHHSHM tag.

1   METGLYHISHISHISHISHISHISSERHIS
2   METPROLYSSERPROGLNLYSPROILEVAL
3   ARGVALPHELEUPROASNLYSGLNARGTHR
4   VALVALPROALAARGCYSGLYVALTHRVAL
5   ARGASPSERLEULYSLYSALALEUMETMET
6   ARGGLYLEUILEPROGLUCYSCYSALAVAL
7   TYRARGILEGLNASPGLYGLULYSLYSPRO
8   ILEGLYTRPASPTHRASPILESERTRPLEU
9   THRGLYGLUGLULEUHISVALGLUVALLEU
10   GLUASNVALPROLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 15N-NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC high resolution (L/V methyl stereoassignment)sample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N hetNOEsample_1isotropicsample_conditions_1
1D 15N T1 and T2sample_1isotropicsample_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

Related Database Links:

PDB
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