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:
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or all simulated shifts
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or all simulated shifts