BMRB Entry 5392
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5392
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Title: Solution structure of HMG box 5 in human upstream binding factor PubMed: 12590579
Deposition date: 2002-06-10 Original release date: 2003-12-08
Authors: Yang, W.; Xu, Y.; Wu, J.; Zeng, W.; Shi, Y.
Citation: Yang, W.; Xu, Y.; Wu, J.; Zeng, W.; Shi, Y.. "Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor" Biochemistry 42, 1930-1938 (2003).
Assembly members:
UBF1, polymer, 84 residues, Formula weight is not available
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):
UBF1: GKLPESPKRAEEIWQQSVIG
DYLARFKNDRVKALKAMEMT
WNNMEKKEKLMWIKKAAEDQ
KRYERELSEMRAPPAATNSS
KKLE
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 537 |
13C chemical shifts | 363 |
15N chemical shifts | 89 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | upstream binding factor 1 | 1 |
Entities:
Entity 1, upstream binding factor 1 84 residues - Formula weight is not available
1 | GLY | LYS | LEU | PRO | GLU | SER | PRO | LYS | ARG | ALA | ||||
2 | GLU | GLU | ILE | TRP | GLN | GLN | SER | VAL | ILE | GLY | ||||
3 | ASP | TYR | LEU | ALA | ARG | PHE | LYS | ASN | ASP | ARG | ||||
4 | VAL | LYS | ALA | LEU | LYS | ALA | MET | GLU | MET | THR | ||||
5 | TRP | ASN | ASN | MET | GLU | LYS | LYS | GLU | LYS | LEU | ||||
6 | MET | TRP | ILE | LYS | LYS | ALA | ALA | GLU | ASP | GLN | ||||
7 | LYS | ARG | TYR | GLU | ARG | GLU | LEU | SER | GLU | MET | ||||
8 | ARG | ALA | PRO | PRO | ALA | ALA | THR | ASN | SER | SER | ||||
9 | LYS | LYS | LEU | GLU |
Samples:
sample1: UBF1, [U-15N; U-13C], 3 mM; NaPO4 45 mM; H20 90%; D20 10%
sample2: UBF1, [U-15N; U-13C], 3 mM; NaPO4 45 mM; D20 100%
sample_cond_1: pH: 5.5; temperature: 300 K; ionic strength: 45 mM; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated-NOESY | not available | not available | not available |
3D 13C-separated-NOESY | not available | not available | not available |
Software:
NMRPipe - processing
PIPP - data analysis
CNS v1.0 - structure solution, refinement
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
PDB | |
DBJ | BAB23701 BAE01971 BAE90957 BAF84422 BAF85207 |
EMBL | CAA37469 CAA37548 CAA40016 CAA43222 |
GB | AAB38418 AAB38419 AAC51239 AAH42297 EAW51616 |
PRF | 1608205A |
REF | NP_001037848 NP_001070151 NP_001070152 NP_001099193 NP_001121162 |
SP | P17480 P25976 P25977 |
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