BMRB Entry 4064
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4064
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Citation: Moy, Franklin; Pisano, Michael; Chanda, Pranab; Urbano, Charlotte; Killar, Loran; Sung, Mei-Li; Powers, Robert. "Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic
Fragment of Human Fibroblast Collagenase" J. Biomol. NMR 10, 9-19 (1997).
Assembly members:
human fibroblast collagenase, polymer, 169 residues, 18700 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 Vector: pNOT-3A
Entity Sequences (FASTA):
human fibroblast collagenase: VLTEGNPRWEQTHLTYRIEN
YTPDLPRADVDHAIEKAFQL
WSNVTPLTFTKVSEGQADIM
ISFVRGDHRDNSPFDGPGGN
LAHAFQPGPGIGGDAHFDED
ERWTNNFREYNLHRVAAHEL
GHSLGLSHSTDIGALMYPSY
TFSGDVQLAQDDIDGIQAIY
GRSQNPVQP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 716 |
| 15N chemical shifts | 158 |
| 1H chemical shifts | 1094 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | collagenase | 1 |
Entities:
Entity 1, collagenase 169 residues - 18700 Da.
| 1 | VAL | LEU | THR | GLU | GLY | ASN | PRO | ARG | TRP | GLU | ||||
| 2 | GLN | THR | HIS | LEU | THR | TYR | ARG | ILE | GLU | ASN | ||||
| 3 | TYR | THR | PRO | ASP | LEU | PRO | ARG | ALA | ASP | VAL | ||||
| 4 | ASP | HIS | ALA | ILE | GLU | LYS | ALA | PHE | GLN | LEU | ||||
| 5 | TRP | SER | ASN | VAL | THR | PRO | LEU | THR | PHE | THR | ||||
| 6 | LYS | VAL | SER | GLU | GLY | GLN | ALA | ASP | ILE | MET | ||||
| 7 | ILE | SER | PHE | VAL | ARG | GLY | ASP | HIS | ARG | ASP | ||||
| 8 | ASN | SER | PRO | PHE | ASP | GLY | PRO | GLY | GLY | ASN | ||||
| 9 | LEU | ALA | HIS | ALA | PHE | GLN | PRO | GLY | PRO | GLY | ||||
| 10 | ILE | GLY | GLY | ASP | ALA | HIS | PHE | ASP | GLU | ASP | ||||
| 11 | GLU | ARG | TRP | THR | ASN | ASN | PHE | ARG | GLU | TYR | ||||
| 12 | ASN | LEU | HIS | ARG | VAL | ALA | ALA | HIS | GLU | LEU | ||||
| 13 | GLY | HIS | SER | LEU | GLY | LEU | SER | HIS | SER | THR | ||||
| 14 | ASP | ILE | GLY | ALA | LEU | MET | TYR | PRO | SER | TYR | ||||
| 15 | THR | PHE | SER | GLY | ASP | VAL | GLN | LEU | ALA | GLN | ||||
| 16 | ASP | ASP | ILE | ASP | GLY | ILE | GLN | ALA | ILE | TYR | ||||
| 17 | GLY | ARG | SER | GLN | ASN | PRO | VAL | GLN | PRO |
Related Database Links:
| PDB | 1AYK 1CGE 1CGF 1CGL 1HFC 1SU3 2AYK 2CLT 2J0T 2TCL 3AYK 3SHI 4AUO 4AYK 966C |
| DBJ | BAD96754 BAD96755 BAD96756 BAD96776 BAD97001 |
| EMBL | CAA28858 CAA38691 |
| GB | AAA35699 AAB34887 AAB36941 AAH13875 AAP35520 |
| REF | NP_001139410 NP_002412 XP_002822446 XP_003253096 XP_003253097 |
| SP | P03956 |
| AlphaFold | P03956 |
Download HSQC peak lists in one of the following formats:
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