date: 2016-12-15T14:35:06Z pdf:unmappedUnicodeCharsPerPage: 0 pdf:PDFVersion: 1.4 pdf:docinfo:title: Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism xmp:CreatorTool: Arbortext Advanced Print Publisher 9.1.510/W Unicode access_permission:modify_annotations: true access_permission:can_print_degraded: true dcterms:created: 2016-09-21T22:46:10Z Last-Modified: 2016-12-15T14:35:06Z dcterms:modified: 2016-12-15T14:35:06Z dc:format: application/pdf; version=1.4 title: Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism xmpMM:DocumentID: uuid:364f3393-1dd2-11b2-0a00-d308271d9a00 Last-Save-Date: 2016-12-15T14:35:06Z pdf:docinfo:creator_tool: Arbortext Advanced Print Publisher 9.1.510/W Unicode CrossMarkDomains[1]: www.pnas.org access_permission:fill_in_form: true pdf:docinfo:modified: 2016-12-15T14:35:06Z meta:save-date: 2016-12-15T14:35:06Z pdf:encrypted: false dc:title: Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism modified: 2016-12-15T14:35:06Z pdf:docinfo:custom:CrossMarkDomains[1]: www.pnas.org Content-Type: application/pdf X-Parsed-By: org.apache.tika.parser.DefaultParser meta:creation-date: 2016-09-21T22:46:10Z pdf:docinfo:custom:CrossmarkMajorVersionDate: 2016-09-22 created: 2016-09-21T22:46:10Z access_permission:extract_for_accessibility: true access_permission:assemble_document: true xmpTPg:NPages: 15 Creation-Date: 2016-09-21T22:46:10Z pdf:charsPerPage: 6387 access_permission:extract_content: true access_permission:can_print: true pdf:docinfo:custom:doi: 10.1073/pnas.1613630113 pdf:docinfo:custom:CrossmarkDomainExclusive: false producer: Acrobat Distiller 10.0.0 (Windows) CrossmarkDomainExclusive: false access_permission:can_modify: true pdf:docinfo:producer: Acrobat Distiller 10.0.0 (Windows) pdf:docinfo:created: 2016-09-21T22:46:10Z CrossmarkMajorVersionDate: 2016-09-22 doi: 10.1073/pnas.1613630113