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 18000

Title: Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology   PubMed: 22244764

Authors: Xie, Tao; Radhakrishnan, Ishwar

Citation: Xie, Tao; Graveline, Richard; Kumar, Ganesan Senthil; Zhang, Yongbo; Krishnan, Arvind; David, Gregory; Radhakrishnan, Ishwar. "Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology."  Structure 20, 151-160 (2012).

Assembly members:
Pf1, polymer, 42 residues, 4721.391 Da.
MRG15, polymer, 172 residues, 19870.898 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):
Pf1: DYVQPQLRRPFELLIAAAME RNPTQFQLPNELTCTTALPG SS
MRG15: SNAEVKVKIPEELKPWLVDD WDLITRQKQLFYLPAKKNVD SILEDYANYRKSRGNTDNKE YAVNEVVAGIKEYFNVMLGT QLLYKFERPQYAEILADHPD APMSQVYGAPHLLRLFVRIG AMLAYTPLDEKSLALLLNYL HDFLKYLAKNSATLFSASDY EVAPPEYHRKAV

Data sets:
Data typeCount
13C chemical shifts870
15N chemical shifts204
1H chemical shifts1387

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pf11
2MRG152

Entities:

Entity 1, Pf1 42 residues - 4721.391 Da.

This is the MRG binding domain of PHD factor 1 (Pf1) protein

1   ASPTYRVALGLNPROGLNLEUARGARGPRO
2   PHEGLULEULEUILEALAALAALAMETGLU
3   ARGASNPROTHRGLNPHEGLNLEUPROASN
4   GLULEUTHRCYSTHRTHRALALEUPROGLY
5   SERSER

Entity 2, MRG15 172 residues - 19870.898 Da.

Residues 1-3 is from a non-native affinity tag. This is the MRG domain of MRG15

1   SERASNALAGLUVALLYSVALLYSILEPRO
2   GLUGLULEULYSPROTRPLEUVALASPASP
3   TRPASPLEUILETHRARGGLNLYSGLNLEU
4   PHETYRLEUPROALALYSLYSASNVALASP
5   SERILELEUGLUASPTYRALAASNTYRARG
6   LYSSERARGGLYASNTHRASPASNLYSGLU
7   TYRALAVALASNGLUVALVALALAGLYILE
8   LYSGLUTYRPHEASNVALMETLEUGLYTHR
9   GLNLEULEUTYRLYSPHEGLUARGPROGLN
10   TYRALAGLUILELEUALAASPHISPROASP
11   ALAPROMETSERGLNVALTYRGLYALAPRO
12   HISLEULEUARGLEUPHEVALARGILEGLY
13   ALAMETLEUALATYRTHRPROLEUASPGLU
14   LYSSERLEUALALEULEULEUASNTYRLEU
15   HISASPPHELEULYSTYRLEUALALYSASN
16   SERALATHRLEUPHESERALASERASPTYR
17   GLUVALALAPROPROGLUTYRHISARGLYS
18   ALAVAL

Samples:

sample_1: Pf1, [U-100% 13C; U-100% 15N], 0.9 mM; MRG15 0.9 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 10%; DTT, [U-2H], 5 mM; sodium azide 0.2%; H2O 90%; D2O 10%

sample_2: Pf1, [U-100% 13C; U-100% 15N], 0.9 mM; MRG15 0.9 mM; potassium chloride 50 mM; D2O, [U-100% 2H], 100%; DTT, [U-2H], 5 mM; sodium azide 0.2%; D2O 100%

sample_3: Pf1 0.9 mM; MRG15, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 10%; DTT, [U-2H], 5 mM; sodium azide 0.2%; H2O 90%; D2O 10%

sample_4: Pf1 0.9 mM; MRG15, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 100%; DTT, [U-2H], 5 mM; sodium azide 0.2%; D2O 100%

sample_conditions_1: pH: 6.8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HCACOsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v1.2, Linge, O, . - structure solution

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17485
PDB
DBJ BAD18713 BAE00370 BAE24837 BAE33212 BAE41602 BAB30219 BAB58904 BAC37546 BAD90270 BAE00783
GB AAH01657 AAH43080 AAI10883 AAI21044 AAI21045 AAD20058 AAD20970 AAD29872 AAF29033 AAF80854
REF NP_001013135 NP_001028733 NP_001179060 NP_001253214 NP_001277060 NP_001011999 NP_001030525 NP_001034236 NP_001127679 NP_001240678
SP Q5SPL2 Q96QT6 P60762 Q5NVP9 Q6AYU1 Q9UBU8
TPG DAA18992 DAA17605
EMBL CAB70879 CAI29614