BMRB Entry 25043
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25043
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Title: Structural Investigation of hnRNP L bound to RNA
Deposition date: 2014-06-24 Original release date: 2015-12-21
Authors: Blatter, Markus; Allain, Frederic
Citation: Blatter, Markus; Allain, Frederic. "Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA" To be Published ., .-..
Assembly members:
entity_1, polymer, 215 residues,   24141.418 Da.
RNA_(5'-R(*AP*CP*AP*CP*A)-3'), polymer, 5 residues,   1553.035 Da.
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: YGPHADSPVLMVYGLDQSKM
NCDRVFNVFCLYGNVEKVKF
MKSKPGAAMVEMADGYAVDR
AITHLNNNFMFGQKMNVCVS
KQPAIMPGQSYGLEDGSCSY
KDFSESRNNRFSTPEQAAKN
RIQHPSNVLHFFNAPLEVTE
ENFFEICDELGVKRPTSVKV
FSGKSERSSSGLLEWDSKSD
ALETLGFLNHYQMKNPNGPY
PYTLKLCFSTAQHAS
RNA_(5'-R(*AP*CP*AP*CP*A)-3'): ACACA
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 700 | 
| 15N chemical shifts | 223 | 
| 1H chemical shifts | 1466 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | entity_1 | 1 | 
| 2 | RNA (5'-R(*AP*CP*AP*CP*A)-3')_1 | 2 | 
| 3 | RNA (5'-R(*AP*CP*AP*CP*A)-3')_2 | 2 | 
Entities:
Entity 1, entity_1 215 residues - 24141.418 Da.
| 1 | TYR | GLY | PRO | HIS | ALA | ASP | SER | PRO | VAL | LEU | ||||
| 2 | MET | VAL | TYR | GLY | LEU | ASP | GLN | SER | LYS | MET | ||||
| 3 | ASN | CYS | ASP | ARG | VAL | PHE | ASN | VAL | PHE | CYS | ||||
| 4 | LEU | TYR | GLY | ASN | VAL | GLU | LYS | VAL | LYS | PHE | ||||
| 5 | MET | LYS | SER | LYS | PRO | GLY | ALA | ALA | MET | VAL | ||||
| 6 | GLU | MET | ALA | ASP | GLY | TYR | ALA | VAL | ASP | ARG | ||||
| 7 | ALA | ILE | THR | HIS | LEU | ASN | ASN | ASN | PHE | MET | ||||
| 8 | PHE | GLY | GLN | LYS | MET | ASN | VAL | CYS | VAL | SER | ||||
| 9 | LYS | GLN | PRO | ALA | ILE | MET | PRO | GLY | GLN | SER | ||||
| 10 | TYR | GLY | LEU | GLU | ASP | GLY | SER | CYS | SER | TYR | ||||
| 11 | LYS | ASP | PHE | SER | GLU | SER | ARG | ASN | ASN | ARG | ||||
| 12 | PHE | SER | THR | PRO | GLU | GLN | ALA | ALA | LYS | ASN | ||||
| 13 | ARG | ILE | GLN | HIS | PRO | SER | ASN | VAL | LEU | HIS | ||||
| 14 | PHE | PHE | ASN | ALA | PRO | LEU | GLU | VAL | THR | GLU | ||||
| 15 | GLU | ASN | PHE | PHE | GLU | ILE | CYS | ASP | GLU | LEU | ||||
| 16 | GLY | VAL | LYS | ARG | PRO | THR | SER | VAL | LYS | VAL | ||||
| 17 | PHE | SER | GLY | LYS | SER | GLU | ARG | SER | SER | SER | ||||
| 18 | GLY | LEU | LEU | GLU | TRP | ASP | SER | LYS | SER | ASP | ||||
| 19 | ALA | LEU | GLU | THR | LEU | GLY | PHE | LEU | ASN | HIS | ||||
| 20 | TYR | GLN | MET | LYS | ASN | PRO | ASN | GLY | PRO | TYR | ||||
| 21 | PRO | TYR | THR | LEU | LYS | LEU | CYS | PHE | SER | THR | ||||
| 22 | ALA | GLN | HIS | ALA | SER | 
Entity 2, RNA (5'-R(*AP*CP*AP*CP*A)-3')_1 5 residues - 1553.035 Da.
| 1 | A | C | A | C | A | 
Samples:
sample_1: entity_1, [U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_2: entity_1, [U-100% 13C; U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_3: entity_1, [U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%
sample_4: entity_1, [U-100% 13C; U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 313.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 | 
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 | 
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 | 
| 3D F3-filtered-F2-edited NOESY | sample_4 | isotropic | sample_conditions_1 | 
| 2D F2-filtered NOESY | sample_4 | isotropic | sample_conditions_1 | 
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
 - Bruker Avance 700 MHz
 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts