Mass: 2522.882 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN(RESIDUE 132-152) / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P18509
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
TRNOESY
2
2
1
TRNOESY
NMR details
Text: Both TRNOE and NOE cross peaks were observed in the spectrum: the former reflects the conformation of PACAP21 in the receptor-bound form, while the latter reflects that of unbound PACAP21. Upon ...Text: Both TRNOE and NOE cross peaks were observed in the spectrum: the former reflects the conformation of PACAP21 in the receptor-bound form, while the latter reflects that of unbound PACAP21. Upon addition of a higher affinity ligand, PACAP27, the TRNOE cross peaks were selectively eliminated due to a competitive inhibition of the specific binding of PACAP21 to the receptor. Accordingly, the subtraction of these two spectra yields TRNOE-related cross peaks exclusively.
Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz
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Processing
NMR software
Name
Version
Developer
Classification
X-PLOR
3.1
Brunger, A.T.
structuresolution
IRMA
30-Jul-90
Kaptein, R.
iterativematrixrelaxation
X-PLOR
3.1
Brunger, A.T.
refinement
Refinement
Method: Iterative relaxation matrix analysis (IRMA), simulated annealing (SA) Software ordinal: 1 Details: The structures are calculated by SA protocol of X-PLOR based on a total of 387 TRNOE-derived distance restraints obtained from the IRMA refinement.
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 25
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