BMRB Entry 17974
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17974
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Title: Structural and mechanistic insights into the interaction between PAT Pyk2 and Paxillin LD motif
Deposition date: 2011-10-04 Original release date: 2012-10-09
Authors: Vanarotti, Murugendra; Miller, Darcie; Guibao, Cristina; Zheng, Jie
Citation: Vanarotti, Murugendra; Miller, Darcie; Guibao, Cristina; Zheng, Jie. "Structural and mechanistic insights into the interaction between PAT Pyk2 and Paxillin LD motif" Not known ., .-..
Assembly members:
entity, polymer, 135 residues,   14815.178 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):
entity: ANLDRTDDLVYLNVMELVRA
VLELKNELSQLPPEGYVVVV
KNVGLTLRKLIGSVDDLLPS
LPSSSRTEIEGTQKLLNKDL
AELINKMRLAQQNAVTSLSE
EAKRQMLTASHTLAVDAKNL
LDAVDQAKVLANLAH
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 438 | 
| 15N chemical shifts | 143 | 
| 1H chemical shifts | 998 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | PAT Pyk2 and Paxillin LD motif | 1 | 
Entities:
Entity 1, PAT Pyk2 and Paxillin LD motif 135 residues - 14815.178 Da.
| 1 | ALA | ASN | LEU | ASP | ARG | THR | ASP | ASP | LEU | VAL | ||||
| 2 | TYR | LEU | ASN | VAL | MET | GLU | LEU | VAL | ARG | ALA | ||||
| 3 | VAL | LEU | GLU | LEU | LYS | ASN | GLU | LEU | SER | GLN | ||||
| 4 | LEU | PRO | PRO | GLU | GLY | TYR | VAL | VAL | VAL | VAL | ||||
| 5 | LYS | ASN | VAL | GLY | LEU | THR | LEU | ARG | LYS | LEU | ||||
| 6 | ILE | GLY | SER | VAL | ASP | ASP | LEU | LEU | PRO | SER | ||||
| 7 | LEU | PRO | SER | SER | SER | ARG | THR | GLU | ILE | GLU | ||||
| 8 | GLY | THR | GLN | LYS | LEU | LEU | ASN | LYS | ASP | LEU | ||||
| 9 | ALA | GLU | LEU | ILE | ASN | LYS | MET | ARG | LEU | ALA | ||||
| 10 | GLN | GLN | ASN | ALA | VAL | THR | SER | LEU | SER | GLU | ||||
| 11 | GLU | ALA | LYS | ARG | GLN | MET | LEU | THR | ALA | SER | ||||
| 12 | HIS | THR | LEU | ALA | VAL | ASP | ALA | LYS | ASN | LEU | ||||
| 13 | LEU | ASP | ALA | VAL | ASP | GLN | ALA | LYS | VAL | LEU | ||||
| 14 | ALA | ASN | LEU | ALA | HIS | 
Samples:
sample_1: MES, [U-100% 13C; U-100% 15N], 0.5  1 mM; H2O, natural source, 90%; D2O, natural source, 10%
sample_conditions_1: ionic strength: 7 mM; pH: 6.2; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 | 
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
 - Bruker Avance 800 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAI45770 | 
| EMBL | CAH92304 | 
| GB | AAB35701 AAB47217 AAC05330 AAC50203 AAH36651 | 
| PRF | 2119367A 2208337A | 
| REF | NP_001095722 NP_001127536 NP_004094 NP_775266 NP_775267 | 
| SP | Q14289 | 
| TPG | DAA26677 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
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SPARKY: Backbone
            or all simulated shifts