BMRB Entry 5390
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PDB ID: 1lr1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5390
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Title: 1H,13C and 15N Chemical Shifts Assignments for the Oligomerization Domain of H-NS PubMed: 12460581
Deposition date: 2002-06-12 Original release date: 2003-02-25
Authors: Esposito, D.; Petrovic, A.; Harris, R.; Shusuke, O.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.
Citation: Esposito, D.; Petrovic, A.; Harris, R.; Ono, S.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.. "H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein" J. Mol. Biol. 324, 841-850 (2002).
Assembly members:
H-NS, polymer, 61 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
H-NS: GSHMSEALKILNNIRTLRAQ
ARESTLETLEEMLEKLEVVV
NERREEESAAAAEVEERTRK
L
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 366 |
| 13C chemical shifts | 193 |
| 15N chemical shifts | 62 |
Additional metadata:
Related Database Links:
| BMRB | 18814 4802 |
| PDB | 1LR1 1NI8 3NR7 |
| DBJ | BAA36117 BAB35162 BAG76811 BAI25048 BAI30173 |
| EMBL | CAA30530 CAA32549 CAA40507 CAA42565 CAA47322 |
| GB | AAB61148 AAC74319 AAG56094 AAL20669 AAN42850 |
| PIR | AC0650 |
| PRF | 1607341A |
| REF | NP_287482 NP_309766 NP_415753 NP_455749 NP_460710 |
| SP | P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9 |
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