BMRB Entry 6231
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6231
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C and 15N resonance assignments and secondary structure of human pancreatitis-associated protein (hPAP)
Deposition date: 2004-06-11 Original release date: 2004-12-16
Authors: Ho, Meng-Ru; Lou, Yuan-Chao; Lin, Wen-chang; Lyu, Ping-Ching; Chen, Chinpan
Citation: Ho, Meng-Ru; Lou, Yuan-Chao; Lin, Wen-chang; Lyu, Ping-Ching; Chen, Chinpan. "Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of human pancreatitis-associated protein (hPAP)" J. Biomol. NMR 30, 381-382 (2004).
Assembly members:
human pancreatitis-associated protein, polymer, 137 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hominidae Homo
Experimental source: Production method: recombinant technology Host organism: Escherichia
Entity Sequences (FASTA):
human pancreatitis-associated protein: RCPKGSKAYGSHCYALFLSP
KSWTDADLACQKRPSGNLVS
VLSGAEGSFVSSLVKSIGNS
YSYVWIGLHDPTQGTEPNGE
GWEWSSSDVMNYFAWERNPS
TISSPGHCASLSRSTAFLRW
KDYNCNVRLPYVCKFTD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 552 |
15N chemical shifts | 143 |
1H chemical shifts | 854 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hPAP, monomer | 1 |
Entities:
Entity 1, hPAP, monomer 137 residues - Formula weight is not available
1 | ARG | CYS | PRO | LYS | GLY | SER | LYS | ALA | TYR | GLY | ||||
2 | SER | HIS | CYS | TYR | ALA | LEU | PHE | LEU | SER | PRO | ||||
3 | LYS | SER | TRP | THR | ASP | ALA | ASP | LEU | ALA | CYS | ||||
4 | GLN | LYS | ARG | PRO | SER | GLY | ASN | LEU | VAL | SER | ||||
5 | VAL | LEU | SER | GLY | ALA | GLU | GLY | SER | PHE | VAL | ||||
6 | SER | SER | LEU | VAL | LYS | SER | ILE | GLY | ASN | SER | ||||
7 | TYR | SER | TYR | VAL | TRP | ILE | GLY | LEU | HIS | ASP | ||||
8 | PRO | THR | GLN | GLY | THR | GLU | PRO | ASN | GLY | GLU | ||||
9 | GLY | TRP | GLU | TRP | SER | SER | SER | ASP | VAL | MET | ||||
10 | ASN | TYR | PHE | ALA | TRP | GLU | ARG | ASN | PRO | SER | ||||
11 | THR | ILE | SER | SER | PRO | GLY | HIS | CYS | ALA | SER | ||||
12 | LEU | SER | ARG | SER | THR | ALA | PHE | LEU | ARG | TRP | ||||
13 | LYS | ASP | TYR | ASN | CYS | ASN | VAL | ARG | LEU | PRO | ||||
14 | TYR | VAL | CYS | LYS | PHE | THR | ASP |
Samples:
sample_1: human pancreatitis-associated protein, [U-95% 13C; U-90% 15N], 1.0 mM
sample_2: human pancreatitis-associated protein, [U-95% 13C; U-90% 15N; U-65% 2H], 1.0 mM
sample_3: human pancreatitis-associated protein, [U-90% 15N], 1.0 mM
cond_set_1: pH: 4.0; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
15N HSQC | not available | not available | not available |
13C HSQC | not available | not available | not available |
CBCA(CO)NH | not available | not available | not available |
HNCACB | not available | not available | not available |
HNCO | not available | not available | not available |
HN(CA)CO | not available | not available | not available |
C(CO)NH | not available | not available | not available |
H(CCO)NH | not available | not available | not available |
15N NOESY | not available | not available | not available |
HBHA(CO)NH | not available | not available | not available |
HBHA | not available | not available | not available |
13C HCCH-TOCSY | not available | not available | not available |
Software:
XWINNMR v3.5 - data processing
NMR spectrometers:
- Bruker AVA 500 MHz
- Bruker AVA 600 MHz
- Bruker DRX 600 MHz
Related Database Links:
PDB | |
DBJ | BAA02728 BAF84662 |
EMBL | CAA48605 |
GenBank | AAA36415 AAA60020 AAB24642 AAH36776 AAT11159 |
PRF | 1908220A |
REF | NP_002571 NP_620354 NP_620355 XP_001164292 XP_001164331 |
SWISS-PROT | Q06141 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts