##gff-version 3
P07998	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1587793,ECO:0000269|PubMed:2049798,ECO:0000269|PubMed:2383019,ECO:0000269|PubMed:3202829,ECO:0000269|PubMed:6201087,ECO:0000269|PubMed:8280059;Dbxref=PMID:1587793,PMID:2049798,PMID:2383019,PMID:3202829,PMID:6201087,PMID:8280059	
P07998	UniProtKB	Chain	29	156	.	.	.	ID=PRO_0000030921;Note=Ribonuclease pancreatic	
P07998	UniProtKB	Region	33	53	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P07998	UniProtKB	Active site	40	40	.	.	.	Note=Proton acceptor	
P07998	UniProtKB	Active site	147	147	.	.	.	Note=Proton donor	
P07998	UniProtKB	Binding site	35	35	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P07998	UniProtKB	Binding site	38	38	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P07998	UniProtKB	Binding site	69	73	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P07998	UniProtKB	Binding site	94	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P07998	UniProtKB	Binding site	113	113	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P07998	UniProtKB	Glycosylation	62	62	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3202829;Dbxref=PMID:3202829	
P07998	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3202829;Dbxref=PMID:3202829	
P07998	UniProtKB	Glycosylation	116	116	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3202829;Dbxref=PMID:3202829	
P07998	UniProtKB	Disulfide bond	54	112	.	.	.	.	
P07998	UniProtKB	Disulfide bond	68	123	.	.	.	.	
P07998	UniProtKB	Disulfide bond	86	138	.	.	.	.	
P07998	UniProtKB	Disulfide bond	93	100	.	.	.	.	
P07998	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Substantially decreases binding affinity for RNH1 but maintains high conformational stability%3B when associated with D-95%2C A-116%2C D-117 and D-119. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17350650;Dbxref=PMID:17350650	
P07998	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Substantially decreases binding affinity for RNH1 but maintains high conformational stability%3B when associated with D-67%2C A-116%2C D-117 and D-119. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17350650;Dbxref=PMID:17350650	
P07998	UniProtKB	Mutagenesis	116	117	.	.	.	Note=No effect on inhibition by RNH1. NG->RS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11021969;Dbxref=PMID:11021969	
P07998	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Substantially decreases binding affinity for RNH1 but maintains high conformational stability%3B when associated with D-67%2C D-95%2C D-117 and D-119. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17350650;Dbxref=PMID:17350650	
P07998	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Substantially decreases binding affinity for RNH1 but maintains high conformational stability%3B when associated with D-67%2C D-95%2C A-116 and D-119. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17350650;Dbxref=PMID:17350650	
P07998	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Substantially decreases binding affinity for RNH1 but maintains high conformational stability%3B when associated with D-67%2C D-95%2C A-116 and D-117. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17350650;Dbxref=PMID:17350650	
P07998	UniProtKB	Sequence conflict	2	2	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Sequence conflict	4	4	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Sequence conflict	9	11	.	.	.	Note=RLL->VLP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Sequence conflict	16	22	.	.	.	Note=ILLVLGW->VLLLVR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Sequence conflict	67	67	.	.	.	Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Sequence conflict	151	151	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P07998	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Turn	47	50	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1H8X	
P07998	UniProtKB	Helix	53	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0L	
P07998	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	70	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Helix	79	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	107	114	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F8G	
P07998	UniProtKB	Beta strand	125	139	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Turn	140	143	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J	
P07998	UniProtKB	Beta strand	144	152	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E0J