BMRB Entry 17702
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17702
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Title: The protein complex for DNA replication
Deposition date: 2011-06-14 Original release date: 2012-12-17
Authors: LIU, Changdong; WEI, Zhun; ZHU, Guang
Citation: LIU, Changdong; WEI, Zhun; WU, Rentian; LIANG, Chun; ZHU, Guang. "The protein complex for DNA replication" Not known ., .-..
Assembly members:
protein_comp1, polymer, 114 residues, 13304.011 Da.
protein_comp2, polymer, 29 residues, 3361.944 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):
protein_comp1: APKASLRLGFSEYSRISNLI
VLHLRKVEEEEDESALKRSE
LVNWYLKEIESEIDSEEELI
NKKRIIEKVIHRLTHYDHVL
IELTQAGLKGSTEGSESYEE
DPYLVVNPNYLLED
protein_comp2: SALKGVSQDLLERIRAKEAQ
KQLAQMTRW
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 363 |
15N chemical shifts | 125 |
1H chemical shifts | 771 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | protein_comp1 | 1 |
2 | protein_comp2 | 2 |
Entities:
Entity 1, protein_comp1 114 residues - 13304.011 Da.
1 | ALA | PRO | LYS | ALA | SER | LEU | ARG | LEU | GLY | PHE | ||||
2 | SER | GLU | TYR | SER | ARG | ILE | SER | ASN | LEU | ILE | ||||
3 | VAL | LEU | HIS | LEU | ARG | LYS | VAL | GLU | GLU | GLU | ||||
4 | GLU | ASP | GLU | SER | ALA | LEU | LYS | ARG | SER | GLU | ||||
5 | LEU | VAL | ASN | TRP | TYR | LEU | LYS | GLU | ILE | GLU | ||||
6 | SER | GLU | ILE | ASP | SER | GLU | GLU | GLU | LEU | ILE | ||||
7 | ASN | LYS | LYS | ARG | ILE | ILE | GLU | LYS | VAL | ILE | ||||
8 | HIS | ARG | LEU | THR | HIS | TYR | ASP | HIS | VAL | LEU | ||||
9 | ILE | GLU | LEU | THR | GLN | ALA | GLY | LEU | LYS | GLY | ||||
10 | SER | THR | GLU | GLY | SER | GLU | SER | TYR | GLU | GLU | ||||
11 | ASP | PRO | TYR | LEU | VAL | VAL | ASN | PRO | ASN | TYR | ||||
12 | LEU | LEU | GLU | ASP |
Entity 2, protein_comp2 29 residues - 3361.944 Da.
1 | SER | ALA | LEU | LYS | GLY | VAL | SER | GLN | ASP | LEU | ||||
2 | LEU | GLU | ARG | ILE | ARG | ALA | LYS | GLU | ALA | GLN | ||||
3 | LYS | GLN | LEU | ALA | GLN | MET | THR | ARG | TRP |
Samples:
sample_1: MES 25 mM; sodium chloride 300 mM; glycerol 1%; protein_comp2, [U-100% 13C; U-100% 15N], 0.8 mM; protein_comp1 1 mM; H2O 90%; D2O 10%
sample_2: MES, [U-100% 15N], 25 mM; sodium chloride 300 mM; glycerol 1%; protein_comp1, [U-100% 13C; U-100% 15N], 0.8 mM; protein_comp2 1.0 mM; H2O 90%; D2O 10%
sample_3: MES 25 mM; sodium chloride 300 mM; glycerol 1%; protein_comp1, [U-100% 13C; U-100% 15N], 0.8 mM; protein_comp2 1.0 mM; D2O 100%
sample_4: MES 25 mM; sodium chloride 300 mM; glycerol 1%; protein_comp2, [U-100% 13C; U-100% 15N], 0.8 mM; protein_comp1 1.0 mM; D2O 100%
sample_conditions_1: ionic strength: 3 M; pH: 6.5; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
13C/15N filtered-C13 edited NOE | sample_3 | isotropic | sample_conditions_1 |
13C/15N filtered-C13 edited NOE | sample_4 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_4 | isotropic | sample_conditions_1 |
Software:
VNMR, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
HADDOCK1.3, Alexandre Bonvin - refinement
ProcheckNMR, Laskowski and MacArthur - geometry optimization
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 750 MHz
Related Database Links:
BMRB | 16396 16796 16796 |
PDB | |
DBJ | BAA12699 BAE01174 BAG35469 BAG61268 |
GB | AAB48165 AAC50766 AAH32374 AAI12449 AAO26043 AAH14202 EAW66764 ELK00500 |
REF | NP_001039699 NP_001247544 NP_001270984 NP_005906 XP_001154732 XP_006926820 XP_009249324 XP_009429704 |
SP | Q14566 Q2KIZ8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts