data_15137 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15137 _Entry.Title ; The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-02-17 _Entry.Accession_date 2007-02-17 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Luis Alcaraz . A. . 15137 2 Marta 'del Alamo' . . . 15137 3 Francisco Barrera . N. . 15137 4 Mauricio Mateu . G. . 15137 5 Jose Neira . L . 15137 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID . 'not applicable' 'not applicable' . 15137 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'CAPSIS PROTEIN' . 15137 HIV . 15137 MONOMER . 15137 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15137 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 68 15137 '1H chemical shifts' 526 15137 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 3 . . 2010-05-26 2007-02-17 update BMRB 'update entity name' 15137 2 . . 2009-02-02 2007-02-17 update BMRB 'addition of author residue codes' 15137 1 . . 2007-10-24 2007-02-17 original author 'original release' 15137 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1A43 'DIMERIC PROTEIN' 15137 PDB 2JO0 'BMRB Entry Tracking System' 15137 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15137 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17526561 _Citation.Full_citation . _Citation.Title 'Flexibility in HIV-1 assembly units: solution structure and dynamics of the monomeric C-terminal domain of the capsid protein' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biophys. J.' _Citation.Journal_name_full . _Citation.Journal_volume 93 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1264 _Citation.Page_last 1276 _Citation.Year 2007 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Luis Alcaraz . A. . 15137 1 2 Marta 'del Alamo' . . . 15137 1 3 Francisco Barrera . N. . 15137 1 4 Mauricio Mateu . G. . 15137 1 5 Jose Neira . L. . 15137 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15137 _Assembly.ID 1 _Assembly.Name 'CAC monomer' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'CAC monomer' 1 $entity A . yes native no no . . . 15137 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 15137 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'CAC monomer' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MSPTSILDIRQGPKEPFRDY VDRFYKTLRAEQASQEVKNA MTETLLVQNANPDCKTILKA LGPAATLEEMMTACQGVGGP GHKARVL ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 87 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation Trp40Ala _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 9567.128 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 16555 . HIV-1_Capsid_Protein . . . . . 98.85 88 98.84 98.84 2.30e-55 . . . . 15137 1 2 no BMRB 17307 . Capsid_protein_p24 . . . . . 96.55 105 98.81 98.81 5.20e-54 . . . . 15137 1 3 no BMRB 17738 . HIV-1_CA . . . . . 98.85 240 97.67 97.67 2.95e-53 . . . . 15137 1 4 no BMRB 19261 . HIVcapsid . . . . . 98.85 231 97.67 97.67 1.49e-53 . . . . 15137 1 5 no BMRB 19264 . entity . . . . . 98.85 231 97.67 97.67 3.00e-53 . . . . 15137 1 6 no BMRB 19575 . HIV1_CA . . . . . 98.85 231 97.67 97.67 1.49e-53 . . . . 15137 1 7 no BMRB 25532 . Gag . . . . . 98.85 432 98.84 98.84 4.18e-52 . . . . 15137 1 8 no PDB 1A43 . "Structure Of The Hiv-1 Capsid Protein Dimerization Domain At 2.6a Resolution" . . . . . 100.00 87 97.70 97.70 1.32e-55 . . . . 15137 1 9 no PDB 1AUM . "Hiv Capsid C-Terminal Domain (Cac146)" . . . . . 80.46 70 97.14 97.14 7.22e-42 . . . . 15137 1 10 no PDB 1BAJ . "Hiv-1 Capsid Protein C-Terminal Fragment Plus Gag P2 Domain" . . . . . 100.00 101 97.70 97.70 9.33e-56 . . . . 15137 1 11 no PDB 1E6J . "Crystal Structure Of Hiv-1 Capsid Protein (p24) In Complex With Fab13b5" . . . . . 86.21 210 98.67 98.67 2.84e-45 . . . . 15137 1 12 no PDB 1VU4 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 13 no PDB 1VU5 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 14 no PDB 1VU6 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 15 no PDB 1VU7 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 16 no PDB 1VU8 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 17 no PDB 1VU9 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 18 no PDB 1VUA . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 19 no PDB 1VUC . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 20 no PDB 1VUD . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 21 no PDB 1VUE . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 22 no PDB 1VUF . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 23 no PDB 1VUG . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 24 no PDB 1VUH . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 25 no PDB 1VUI . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 26 no PDB 1VUJ . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 27 no PDB 1VUK . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 28 no PDB 1VUL . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 29 no PDB 1VUM . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 30 no PDB 1VUN . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 31 no PDB 1VUO . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 32 no PDB 1VUP . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 33 no PDB 1VUQ . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 34 no PDB 1VUR . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 35 no PDB 1VUS . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 36 no PDB 1VUT . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 37 no PDB 1VUU . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 38 no PDB 1VUV . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 39 no PDB 1VUW . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 40 no PDB 1VUX . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 41 no PDB 1VUY . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 42 no PDB 1VUZ . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 43 no PDB 1VV0 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 44 no PDB 1VV1 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 45 no PDB 1VV2 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 46 no PDB 1VV3 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 47 no PDB 1VV4 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 48 no PDB 1VV5 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 49 no PDB 1VV6 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 50 no PDB 1VV7 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 51 no PDB 1VV8 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 52 no PDB 1VV9 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 53 no PDB 1VVA . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 54 no PDB 1VVB . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 55 no PDB 1VVF . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 56 no PDB 1VVG . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 57 no PDB 1VVH . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 58 no PDB 1VVI . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 59 no PDB 2BUO . "Hiv-1 Capsid C-Terminal Domain In Complex With An Inhibitor Of Particle Assembly" . . . . . 98.85 86 97.67 97.67 1.12e-54 . . . . 15137 1 60 no PDB 2JO0 . "The Solution Structure Of The Monomeric Species Of The C Terminal Domain Of The Ca Protein Of Hiv-1" . . . . . 100.00 87 100.00 100.00 5.31e-57 . . . . 15137 1 61 no PDB 2JYG . "Solution Structure Of The W184aM185A MUTANT OF THE CARBOXY- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" . . . . . 96.55 84 97.62 97.62 6.31e-53 . . . . 15137 1 62 no PDB 2JYL . "Solution Structure Of A Double Mutant Of The Carboxy- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" . . . . . 96.55 105 97.62 97.62 2.12e-53 . . . . 15137 1 63 no PDB 2KOD . "A High-Resolution Nmr Structure Of The Dimeric C-Terminal Domain Of Hiv-1 Ca" . . . . . 98.85 88 98.84 98.84 2.30e-55 . . . . 15137 1 64 no PDB 2L6E . "Nmr Structure Of The Monomeric Mutant C-Terminal Domain Of Hiv-1 Capsid In Complex With Stapled Peptide Inhibitor" . . . . . 96.55 105 98.81 98.81 5.20e-54 . . . . 15137 1 65 no PDB 2LF4 . "Structure Of A Monomeric Mutant Of The Hiv-1 Capsid Protein" . . . . . 98.85 240 97.67 97.67 2.95e-53 . . . . 15137 1 66 no PDB 2M8L . "Hiv Capsid Dimer Structure" . . . . . 87.36 221 97.37 97.37 3.29e-45 . . . . 15137 1 67 no PDB 2M8N . "Hiv-1 Capsid Monomer Structure" . . . . . 87.36 221 97.37 97.37 3.29e-45 . . . . 15137 1 68 no PDB 2M8P . "The Structure Of The W184am185a Mutant Of The Hiv-1 Capsid Protein" . . . . . 87.36 221 97.37 97.37 7.31e-45 . . . . 15137 1 69 no PDB 2XT1 . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-231) In Complex With A Camelid Vhh" . . . . . 98.85 86 97.67 97.67 1.12e-54 . . . . 15137 1 70 no PDB 2XV6 . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-220) In Complex With A Camelid Vhh." . . . . . 86.21 75 97.33 97.33 1.18e-45 . . . . 15137 1 71 no PDB 2XXM . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain In Complex With A Camelid Vhh And The Cai Peptide" . . . . . 86.21 75 97.33 97.33 1.18e-45 . . . . 15137 1 72 no PDB 3DIK . "Pseudo-Atomic Model Of The Hiv-1 Ca Hexameric Lattice" . . . . . 85.06 219 97.30 97.30 1.17e-43 . . . . 15137 1 73 no PDB 3GV2 . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 89.66 342 97.44 97.44 1.46e-45 . . . . 15137 1 74 no PDB 3H47 . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 75 no PDB 3H4E . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 76 no PDB 3J34 . "Structure Of Hiv-1 Capsid Protein By Cryo-em" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 77 no PDB 3J4F . "Structure Of Hiv-1 Capsid Protein By Cryo-em" . . . . . 98.85 231 98.84 98.84 3.41e-54 . . . . 15137 1 78 no PDB 3LRY . "Crystal Structure Of Synthetic Hiv-1 Capsid C-Terminal Domain (Cca)" . . . . . 98.85 86 97.67 97.67 1.12e-54 . . . . 15137 1 79 no PDB 3MGE . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 98.85 231 97.67 97.67 6.54e-53 . . . . 15137 1 80 no PDB 3NTE . "Crystal Structure Of The Wild-type Full-length Hiv-1 Capsid Protein" . . . . . 87.36 221 98.68 98.68 7.36e-46 . . . . 15137 1 81 no PDB 3P05 . "X-Ray Structure Of Pentameric Hiv-1 Ca" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 82 no PDB 3P0A . "X-Ray Structure Of Pentameric Hiv-1 Ca" . . . . . 98.85 231 97.67 97.67 5.68e-53 . . . . 15137 1 83 no PDB 4ARG . "Structure Of The Immature Retroviral Capsid At 8a Resolution By Cryo-Electron Microscopy" . . . . . 79.31 69 97.10 97.10 1.07e-40 . . . . 15137 1 84 no PDB 4IPY . "Hiv Capsid C-terminal Domain" . . . . . 100.00 87 97.70 97.70 1.32e-55 . . . . 15137 1 85 no PDB 4QNB . "Disulfide Stabilized Hiv-1 Ca Hexamer In Complex With Phenyl-l- Phenylalaninamide Inhibitor" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 86 no PDB 4U0A . "Hexameric Hiv-1 Ca In Complex With Cpsf6 Peptide, P6 Crystal Form" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 87 no PDB 4U0B . "Hexamer Hiv-1 Ca In Complex With Cpsf6 Peptide, P212121 Crystal Form" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 88 no PDB 4U0C . "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P6 Crystal Form" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 89 no PDB 4U0D . "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P212121 Crystal Form" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 90 no PDB 4U0E . "Hexameric Hiv-1 Ca In Complex With Pf3450074" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 91 no PDB 4U0F . "Hexameric Hiv-1 Ca In Complex With Bi-2" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 92 no PDB 4WYM . "Structural Basis Of Hiv-1 Capsid Recognition By Cpsf6" . . . . . 98.85 231 97.67 97.67 5.93e-53 . . . . 15137 1 93 no PDB 4XFX . "Structure Of The Native Full-length Hiv-1 Capsid Protein" . . . . . 98.85 231 97.67 97.67 1.49e-53 . . . . 15137 1 94 no PDB 4XFY . "Structure Of The Native Full-length Dehydrated Hiv-1 Capsid Protein" . . . . . 98.85 231 97.67 97.67 1.49e-53 . . . . 15137 1 95 no PDB 4XFZ . "Structure Of The Native Full-length Hiv-1 Capsid Protein In Complex With Pf-3450074 (pf74)" . . . . . 98.85 231 97.67 97.67 1.49e-53 . . . . 15137 1 96 no DBJ BAA00992 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 98.85 500 98.84 98.84 2.17e-51 . . . . 15137 1 97 no DBJ BAA12988 . "Gag [Human immunodeficiency virus 1]" . . . . . 98.85 512 98.84 98.84 3.47e-51 . . . . 15137 1 98 no DBJ BAA12996 . "Gag [Human immunodeficiency virus 1]" . . . . . 98.85 512 98.84 98.84 3.43e-51 . . . . 15137 1 99 no DBJ BAA93773 . "gag protein [Human immunodeficiency virus 1]" . . . . . 98.85 231 97.67 98.84 1.42e-53 . . . . 15137 1 100 no DBJ BAA93774 . "gag protein [Human immunodeficiency virus 1]" . . . . . 98.85 231 97.67 98.84 1.55e-53 . . . . 15137 1 101 no EMBL CAA06946 . "gag polyprotein precursor [Human immunodeficiency virus 1]" . . . . . 98.85 503 97.67 98.84 1.04e-50 . . . . 15137 1 102 no EMBL CAA11880 . "p24 [Human immunodeficiency virus 1]" . . . . . 74.71 189 98.46 98.46 2.45e-37 . . . . 15137 1 103 no EMBL CAA11886 . "p24 [Human immunodeficiency virus 1]" . . . . . 74.71 190 98.46 98.46 2.63e-37 . . . . 15137 1 104 no EMBL CAA77621 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 98.85 500 97.67 97.67 1.30e-50 . . . . 15137 1 105 no EMBL CAA82791 . "gag [Human immunodeficiency virus 1]" . . . . . 95.40 146 98.80 98.80 2.59e-52 . . . . 15137 1 106 no GB AAA44201 . "gag polyprotein precursor [Human immunodeficiency virus 1]" . . . . . 98.85 512 98.84 98.84 3.97e-51 . . . . 15137 1 107 no GB AAA44306 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 98.85 500 97.67 97.67 1.54e-50 . . . . 15137 1 108 no GB AAA44652 . "gag polyprotein precursor [Human immunodeficiency virus 1]" . . . . . 98.85 512 98.84 98.84 4.14e-51 . . . . 15137 1 109 no GB AAA44987 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 98.85 500 97.67 97.67 8.60e-51 . . . . 15137 1 110 no GB AAA45003 . "gag protein, partial [Human immunodeficiency virus 1]" . . . . . 98.85 491 97.67 98.84 7.23e-51 . . . . 15137 1 111 no PIR FOVWLV . "gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a)" . . . . . 98.85 500 98.84 98.84 2.22e-51 . . . . 15137 1 112 no PRF 1102247B . "protein gag" . . . . . 98.85 512 98.84 98.84 3.97e-51 . . . . 15137 1 113 no PRF 1103299C . "gag gene" . . . . . 98.85 478 98.84 98.84 1.45e-51 . . . . 15137 1 114 no REF NP_057849 . "Gag-Pol [Human immunodeficiency virus 1]" . . . . . 98.85 1435 98.84 98.84 1.08e-49 . . . . 15137 1 115 no REF NP_057850 . "Pr55(Gag) [Human immunodeficiency virus 1]" . . . . . 98.85 500 98.84 98.84 2.71e-51 . . . . 15137 1 116 no REF NP_579880 . "capsid [Human immunodeficiency virus 1]" . . . . . 98.85 231 98.84 98.84 3.00e-54 . . . . 15137 1 117 no SP P03347 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 98.85 512 98.84 98.84 3.97e-51 . . . . 15137 1 118 no SP P03348 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 98.85 512 98.84 98.84 3.47e-51 . . . . 15137 1 119 no SP P03349 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 98.85 502 97.67 98.84 9.35e-51 . . . . 15137 1 120 no SP P03366 . "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " . . . . . 98.85 1447 98.84 98.84 1.01e-49 . . . . 15137 1 121 no SP P03367 . "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " . . . . . 98.85 1447 98.84 98.84 9.56e-50 . . . . 15137 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'structural protein of the HIV capsid' 15137 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 -2 MET . 15137 1 2 -1 SER . 15137 1 3 0 PRO . 15137 1 4 1 THR . 15137 1 5 2 SER . 15137 1 6 3 ILE . 15137 1 7 4 LEU . 15137 1 8 5 ASP . 15137 1 9 6 ILE . 15137 1 10 7 ARG . 15137 1 11 8 GLN . 15137 1 12 9 GLY . 15137 1 13 10 PRO . 15137 1 14 11 LYS . 15137 1 15 12 GLU . 15137 1 16 13 PRO . 15137 1 17 14 PHE . 15137 1 18 15 ARG . 15137 1 19 16 ASP . 15137 1 20 17 TYR . 15137 1 21 18 VAL . 15137 1 22 19 ASP . 15137 1 23 20 ARG . 15137 1 24 21 PHE . 15137 1 25 22 TYR . 15137 1 26 23 LYS . 15137 1 27 24 THR . 15137 1 28 25 LEU . 15137 1 29 26 ARG . 15137 1 30 27 ALA . 15137 1 31 28 GLU . 15137 1 32 29 GLN . 15137 1 33 30 ALA . 15137 1 34 31 SER . 15137 1 35 32 GLN . 15137 1 36 33 GLU . 15137 1 37 34 VAL . 15137 1 38 35 LYS . 15137 1 39 36 ASN . 15137 1 40 37 ALA . 15137 1 41 38 MET . 15137 1 42 39 THR . 15137 1 43 40 GLU . 15137 1 44 41 THR . 15137 1 45 42 LEU . 15137 1 46 43 LEU . 15137 1 47 44 VAL . 15137 1 48 45 GLN . 15137 1 49 46 ASN . 15137 1 50 47 ALA . 15137 1 51 48 ASN . 15137 1 52 49 PRO . 15137 1 53 50 ASP . 15137 1 54 51 CYS . 15137 1 55 52 LYS . 15137 1 56 53 THR . 15137 1 57 54 ILE . 15137 1 58 55 LEU . 15137 1 59 56 LYS . 15137 1 60 57 ALA . 15137 1 61 58 LEU . 15137 1 62 59 GLY . 15137 1 63 60 PRO . 15137 1 64 61 ALA . 15137 1 65 62 ALA . 15137 1 66 63 THR . 15137 1 67 64 LEU . 15137 1 68 65 GLU . 15137 1 69 66 GLU . 15137 1 70 67 MET . 15137 1 71 68 MET . 15137 1 72 69 THR . 15137 1 73 70 ALA . 15137 1 74 71 CYS . 15137 1 75 72 GLN . 15137 1 76 73 GLY . 15137 1 77 74 VAL . 15137 1 78 75 GLY . 15137 1 79 76 GLY . 15137 1 80 77 PRO . 15137 1 81 78 GLY . 15137 1 82 79 HIS . 15137 1 83 80 LYS . 15137 1 84 81 ALA . 15137 1 85 82 ARG . 15137 1 86 83 VAL . 15137 1 87 84 LEU . 15137 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 15137 1 . SER 2 2 15137 1 . PRO 3 3 15137 1 . THR 4 4 15137 1 . SER 5 5 15137 1 . ILE 6 6 15137 1 . LEU 7 7 15137 1 . ASP 8 8 15137 1 . ILE 9 9 15137 1 . ARG 10 10 15137 1 . GLN 11 11 15137 1 . GLY 12 12 15137 1 . PRO 13 13 15137 1 . LYS 14 14 15137 1 . GLU 15 15 15137 1 . PRO 16 16 15137 1 . PHE 17 17 15137 1 . ARG 18 18 15137 1 . ASP 19 19 15137 1 . TYR 20 20 15137 1 . VAL 21 21 15137 1 . ASP 22 22 15137 1 . ARG 23 23 15137 1 . PHE 24 24 15137 1 . TYR 25 25 15137 1 . LYS 26 26 15137 1 . THR 27 27 15137 1 . LEU 28 28 15137 1 . ARG 29 29 15137 1 . ALA 30 30 15137 1 . GLU 31 31 15137 1 . GLN 32 32 15137 1 . ALA 33 33 15137 1 . SER 34 34 15137 1 . GLN 35 35 15137 1 . GLU 36 36 15137 1 . VAL 37 37 15137 1 . LYS 38 38 15137 1 . ASN 39 39 15137 1 . ALA 40 40 15137 1 . MET 41 41 15137 1 . THR 42 42 15137 1 . GLU 43 43 15137 1 . THR 44 44 15137 1 . LEU 45 45 15137 1 . LEU 46 46 15137 1 . VAL 47 47 15137 1 . GLN 48 48 15137 1 . ASN 49 49 15137 1 . ALA 50 50 15137 1 . ASN 51 51 15137 1 . PRO 52 52 15137 1 . ASP 53 53 15137 1 . CYS 54 54 15137 1 . LYS 55 55 15137 1 . THR 56 56 15137 1 . ILE 57 57 15137 1 . LEU 58 58 15137 1 . LYS 59 59 15137 1 . ALA 60 60 15137 1 . LEU 61 61 15137 1 . GLY 62 62 15137 1 . PRO 63 63 15137 1 . ALA 64 64 15137 1 . ALA 65 65 15137 1 . THR 66 66 15137 1 . LEU 67 67 15137 1 . GLU 68 68 15137 1 . GLU 69 69 15137 1 . MET 70 70 15137 1 . MET 71 71 15137 1 . THR 72 72 15137 1 . ALA 73 73 15137 1 . CYS 74 74 15137 1 . GLN 75 75 15137 1 . GLY 76 76 15137 1 . VAL 77 77 15137 1 . GLY 78 78 15137 1 . GLY 79 79 15137 1 . PRO 80 80 15137 1 . GLY 81 81 15137 1 . HIS 82 82 15137 1 . LYS 83 83 15137 1 . ALA 84 84 15137 1 . ARG 85 85 15137 1 . VAL 86 86 15137 1 . LEU 87 87 15137 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 15137 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity . 11676 virus . HIV HIV . . Viruses . Lentivirus HIV . . . . . . . . . . . . . . . . . . . . . 15137 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 15137 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity . 'recombinant technology' 'Escherichia coli' . . . . . BL21 . . . . . . . . . . . . . . . pET21b . . . . . . 15137 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15137 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 entity [U-15N] . . 1 $entity . . 1 . . mM . . . . 15137 1 2 'potassium phosphate' none . . . . . . 100 . . mM . . . . 15137 1 3 TSP none . . . . . . 0.00001 . . mM . . . . 15137 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 15137 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.1 . M 15137 1 pH 7 . pH 15137 1 pressure 1 . atm 15137 1 temperature 293 . K 15137 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 15137 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'P Guntert, C Mumenthaler and K Wuthrich' . . 15137 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 15137 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 15137 _Software.ID 2 _Software.Name SPARKY _Software.Version 3.0 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'T Goddard' . . 15137 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15137 2 'peak picking' 15137 2 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 15137 _Software.ID 3 _Software.Name AMBER _Software.Version 8 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'DA Case, TA Darden, TE Cheatham, III, CL Simmerling, J Wang, RE Duke,' . . 15137 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 15137 3 stop_ save_ save_xwinnmr _Software.Sf_category software _Software.Sf_framecode xwinnmr _Software.Entry_ID 15137 _Software.ID 4 _Software.Name xwinnmr _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 15137 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 15137 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 15137 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 15137 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker DRX . 500 . . . 15137 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 15137 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15137 1 2 '2D TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15137 1 3 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15137 1 4 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15137 1 5 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15137 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 15137 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 TSP 'methyl carbon' . . . . ppm 0 internal indirect 1.0 . . . . . . . . . 15137 1 N 15 NH3 nitrogen . . . . ppm 0 external indirect 1.0 . . . . . . . . . 15137 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 15137 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D NOESY' 1 $sample_1 isotropic 15137 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 THR HA H 1 4.373 0.020 . 1 . . . . 4 THR HA . 15137 1 2 . 1 1 4 4 THR HB H 1 4.313 0.020 . 1 . . . . 4 THR HB . 15137 1 3 . 1 1 4 4 THR HG21 H 1 1.208 0.020 . 1 . . . . 4 THR HG21 . 15137 1 4 . 1 1 4 4 THR HG22 H 1 1.208 0.020 . 1 . . . . 4 THR HG22 . 15137 1 5 . 1 1 4 4 THR HG23 H 1 1.208 0.020 . 1 . . . . 4 THR HG23 . 15137 1 6 . 1 1 4 4 THR N N 15 117.50 . . . . . . . 4 THR N . 15137 1 7 . 1 1 5 5 SER H H 1 8.396 0.020 . 1 . . . . 5 SER H . 15137 1 8 . 1 1 5 5 SER HA H 1 4.270 0.020 . 1 . . . . 5 SER HA . 15137 1 9 . 1 1 5 5 SER HB2 H 1 3.959 0.020 . 2 . . . . 5 SER HB2 . 15137 1 10 . 1 1 5 5 SER HB3 H 1 3.836 0.020 . 2 . . . . 5 SER HB3 . 15137 1 11 . 1 1 6 6 ILE H H 1 7.685 0.020 . 1 . . . . 6 ILE H . 15137 1 12 . 1 1 6 6 ILE HA H 1 4.068 0.020 . 1 . . . . 6 ILE HA . 15137 1 13 . 1 1 6 6 ILE HB H 1 1.596 0.020 . 1 . . . . 6 ILE HB . 15137 1 14 . 1 1 6 6 ILE HD11 H 1 0.196 0.020 . 1 . . . . 6 ILE HD11 . 15137 1 15 . 1 1 6 6 ILE HD12 H 1 0.196 0.020 . 1 . . . . 6 ILE HD12 . 15137 1 16 . 1 1 6 6 ILE HD13 H 1 0.196 0.020 . 1 . . . . 6 ILE HD13 . 15137 1 17 . 1 1 6 6 ILE HG12 H 1 0.933 0.020 . 2 . . . . 6 ILE HG12 . 15137 1 18 . 1 1 6 6 ILE HG13 H 1 1.119 0.020 . 2 . . . . 6 ILE HG13 . 15137 1 19 . 1 1 6 6 ILE HG21 H 1 0.727 0.020 . 1 . . . . 6 ILE HG21 . 15137 1 20 . 1 1 6 6 ILE HG22 H 1 0.727 0.020 . 1 . . . . 6 ILE HG22 . 15137 1 21 . 1 1 6 6 ILE HG23 H 1 0.727 0.020 . 1 . . . . 6 ILE HG23 . 15137 1 22 . 1 1 7 7 LEU H H 1 8.636 0.020 . 1 . . . . 7 LEU H . 15137 1 23 . 1 1 7 7 LEU HA H 1 4.286 0.020 . 1 . . . . 7 LEU HA . 15137 1 24 . 1 1 7 7 LEU HB2 H 1 1.784 0.020 . 1 . . . . 7 LEU HB2 . 15137 1 25 . 1 1 7 7 LEU HB3 H 1 1.784 0.020 . 1 . . . . 7 LEU HB3 . 15137 1 26 . 1 1 7 7 LEU HD11 H 1 0.647 0.020 . 2 . . . . 7 LEU HD11 . 15137 1 27 . 1 1 7 7 LEU HD12 H 1 0.647 0.020 . 2 . . . . 7 LEU HD12 . 15137 1 28 . 1 1 7 7 LEU HD13 H 1 0.647 0.020 . 2 . . . . 7 LEU HD13 . 15137 1 29 . 1 1 7 7 LEU HD21 H 1 0.647 0.020 . 2 . . . . 7 LEU HD21 . 15137 1 30 . 1 1 7 7 LEU HD22 H 1 0.647 0.020 . 2 . . . . 7 LEU HD22 . 15137 1 31 . 1 1 7 7 LEU HD23 H 1 0.647 0.020 . 2 . . . . 7 LEU HD23 . 15137 1 32 . 1 1 7 7 LEU HG H 1 1.582 0.020 . 1 . . . . 7 LEU HG . 15137 1 33 . 1 1 7 7 LEU N N 15 119.50 . . . . . . . 7 LEU N . 15137 1 34 . 1 1 8 8 ASP H H 1 7.729 0.020 . 1 . . . . 8 ASP H . 15137 1 35 . 1 1 8 8 ASP HB2 H 1 2.623 0.020 . 2 . . . . 8 ASP HB2 . 15137 1 36 . 1 1 8 8 ASP HB3 H 1 2.911 0.020 . 2 . . . . 8 ASP HB3 . 15137 1 37 . 1 1 8 8 ASP N N 15 115.70 . . . . . . . 8 ASP N . 15137 1 38 . 1 1 9 9 ILE H H 1 7.494 0.020 . 1 . . . . 9 ILE H . 15137 1 39 . 1 1 9 9 ILE HA H 1 4.171 0.020 . 1 . . . . 9 ILE HA . 15137 1 40 . 1 1 9 9 ILE HB H 1 2.316 0.020 . 1 . . . . 9 ILE HB . 15137 1 41 . 1 1 9 9 ILE HD11 H 1 0.976 0.020 . 1 . . . . 9 ILE HD11 . 15137 1 42 . 1 1 9 9 ILE HD12 H 1 0.976 0.020 . 1 . . . . 9 ILE HD12 . 15137 1 43 . 1 1 9 9 ILE HD13 H 1 0.976 0.020 . 1 . . . . 9 ILE HD13 . 15137 1 44 . 1 1 9 9 ILE HG12 H 1 1.331 0.020 . 2 . . . . 9 ILE HG12 . 15137 1 45 . 1 1 9 9 ILE HG13 H 1 1.629 0.020 . 2 . . . . 9 ILE HG13 . 15137 1 46 . 1 1 9 9 ILE HG21 H 1 0.703 0.020 . 1 . . . . 9 ILE HG21 . 15137 1 47 . 1 1 9 9 ILE HG22 H 1 0.703 0.020 . 1 . . . . 9 ILE HG22 . 15137 1 48 . 1 1 9 9 ILE HG23 H 1 0.703 0.020 . 1 . . . . 9 ILE HG23 . 15137 1 49 . 1 1 9 9 ILE N N 15 122.30 . . . . . . . 9 ILE N . 15137 1 50 . 1 1 10 10 ARG H H 1 8.332 0.020 . 1 . . . . 10 ARG H . 15137 1 51 . 1 1 10 10 ARG HB2 H 1 1.833 0.020 . 1 . . . . 10 ARG HB2 . 15137 1 52 . 1 1 10 10 ARG HB3 H 1 1.833 0.020 . 1 . . . . 10 ARG HB3 . 15137 1 53 . 1 1 10 10 ARG HD2 H 1 3.214 0.020 . 2 . . . . 10 ARG HD2 . 15137 1 54 . 1 1 10 10 ARG HD3 H 1 3.145 0.020 . 2 . . . . 10 ARG HD3 . 15137 1 55 . 1 1 10 10 ARG HE H 1 9.389 0.020 . 1 . . . . 10 ARG HE . 15137 1 56 . 1 1 10 10 ARG HG2 H 1 1.543 0.020 . 2 . . . . 10 ARG HG2 . 15137 1 57 . 1 1 10 10 ARG HG3 H 1 1.647 0.020 . 2 . . . . 10 ARG HG3 . 15137 1 58 . 1 1 10 10 ARG N N 15 124.50 . . . . . . . 10 ARG N . 15137 1 59 . 1 1 11 11 GLN H H 1 7.122 0.020 . 1 . . . . 11 GLN H . 15137 1 60 . 1 1 11 11 GLN HB2 H 1 2.110 0.020 . 2 . . . . 11 GLN HB2 . 15137 1 61 . 1 1 11 11 GLN HB3 H 1 2.329 0.020 . 2 . . . . 11 GLN HB3 . 15137 1 62 . 1 1 11 11 GLN HG2 H 1 2.912 0.020 . 2 . . . . 11 GLN HG2 . 15137 1 63 . 1 1 11 11 GLN HG3 H 1 2.662 0.020 . 2 . . . . 11 GLN HG3 . 15137 1 64 . 1 1 11 11 GLN N N 15 126.00 . . . . . . . 11 GLN N . 15137 1 65 . 1 1 12 12 GLY H H 1 9.905 0.020 . 1 . . . . 12 GLY H . 15137 1 66 . 1 1 12 12 GLY HA2 H 1 3.995 0.020 . 2 . . . . 12 GLY HA2 . 15137 1 67 . 1 1 12 12 GLY HA3 H 1 4.414 0.020 . 2 . . . . 12 GLY HA3 . 15137 1 68 . 1 1 12 12 GLY N N 15 117.20 . . . . . . . 12 GLY N . 15137 1 69 . 1 1 13 13 PRO HA H 1 4.455 0.020 . 1 . . . . 13 PRO HA . 15137 1 70 . 1 1 13 13 PRO HB2 H 1 2.087 0.020 . 1 . . . . 13 PRO HB2 . 15137 1 71 . 1 1 13 13 PRO HB3 H 1 2.087 0.020 . 1 . . . . 13 PRO HB3 . 15137 1 72 . 1 1 13 13 PRO HD2 H 1 3.171 0.020 . 2 . . . . 13 PRO HD2 . 15137 1 73 . 1 1 13 13 PRO HD3 H 1 3.827 0.020 . 2 . . . . 13 PRO HD3 . 15137 1 74 . 1 1 13 13 PRO HG2 H 1 2.902 0.020 . 2 . . . . 13 PRO HG2 . 15137 1 75 . 1 1 13 13 PRO HG3 H 1 2.337 0.020 . 2 . . . . 13 PRO HG3 . 15137 1 76 . 1 1 14 14 LYS H H 1 7.694 0.020 . 1 . . . . 14 LYS H . 15137 1 77 . 1 1 14 14 LYS HA H 1 3.825 0.020 . 1 . . . . 14 LYS HA . 15137 1 78 . 1 1 14 14 LYS HB2 H 1 1.776 0.020 . 2 . . . . 14 LYS HB2 . 15137 1 79 . 1 1 14 14 LYS HB3 H 1 1.833 0.020 . 2 . . . . 14 LYS HB3 . 15137 1 80 . 1 1 14 14 LYS N N 15 127.00 . . . . . . . 14 LYS N . 15137 1 81 . 1 1 15 15 GLU H H 1 8.325 0.020 . 1 . . . . 15 GLU H . 15137 1 82 . 1 1 15 15 GLU HA H 1 4.099 0.020 . 1 . . . . 15 GLU HA . 15137 1 83 . 1 1 15 15 GLU HB2 H 1 2.140 0.020 . 2 . . . . 15 GLU HB2 . 15137 1 84 . 1 1 15 15 GLU HB3 H 1 2.407 0.020 . 2 . . . . 15 GLU HB3 . 15137 1 85 . 1 1 15 15 GLU HG2 H 1 2.392 0.020 . 1 . . . . 15 GLU HG2 . 15137 1 86 . 1 1 15 15 GLU HG3 H 1 2.392 0.020 . 1 . . . . 15 GLU HG3 . 15137 1 87 . 1 1 15 15 GLU N N 15 119.20 . . . . . . . 15 GLU N . 15137 1 88 . 1 1 16 16 PRO HA H 1 4.233 0.020 . 1 . . . . 16 PRO HA . 15137 1 89 . 1 1 16 16 PRO HB2 H 1 2.015 0.020 . 2 . . . . 16 PRO HB2 . 15137 1 90 . 1 1 16 16 PRO HB3 H 1 2.135 0.020 . 2 . . . . 16 PRO HB3 . 15137 1 91 . 1 1 16 16 PRO HG2 H 1 2.272 0.020 . 1 . . . . 16 PRO HG2 . 15137 1 92 . 1 1 16 16 PRO HG3 H 1 2.272 0.020 . 1 . . . . 16 PRO HG3 . 15137 1 93 . 1 1 17 17 PHE H H 1 9.254 0.020 . 1 . . . . 17 PHE H . 15137 1 94 . 1 1 17 17 PHE HA H 1 4.210 0.020 . 1 . . . . 17 PHE HA . 15137 1 95 . 1 1 17 17 PHE HB2 H 1 2.572 0.020 . 2 . . . . 17 PHE HB2 . 15137 1 96 . 1 1 17 17 PHE HB3 H 1 2.986 0.020 . 2 . . . . 17 PHE HB3 . 15137 1 97 . 1 1 17 17 PHE HD1 H 1 7.344 0.020 . 1 . . . . 17 PHE HD1 . 15137 1 98 . 1 1 17 17 PHE HD2 H 1 7.344 0.020 . 1 . . . . 17 PHE HD2 . 15137 1 99 . 1 1 17 17 PHE HE1 H 1 7.123 0.020 . 1 . . . . 17 PHE HE1 . 15137 1 100 . 1 1 17 17 PHE HE2 H 1 7.123 0.020 . 1 . . . . 17 PHE HE2 . 15137 1 101 . 1 1 17 17 PHE HZ H 1 6.946 0.020 . 1 . . . . 17 PHE HZ . 15137 1 102 . 1 1 17 17 PHE N N 15 128.30 . . . . . . . 17 PHE N . 15137 1 103 . 1 1 18 18 ARG H H 1 9.219 0.020 . 1 . . . . 18 ARG H . 15137 1 104 . 1 1 18 18 ARG HA H 1 3.808 0.020 . 1 . . . . 18 ARG HA . 15137 1 105 . 1 1 18 18 ARG HB2 H 1 1.999 0.020 . 2 . . . . 18 ARG HB2 . 15137 1 106 . 1 1 18 18 ARG HB3 H 1 1.825 0.020 . 2 . . . . 18 ARG HB3 . 15137 1 107 . 1 1 18 18 ARG HD2 H 1 3.233 0.020 . 2 . . . . 18 ARG HD2 . 15137 1 108 . 1 1 18 18 ARG HD3 H 1 3.420 0.020 . 2 . . . . 18 ARG HD3 . 15137 1 109 . 1 1 18 18 ARG HG2 H 1 1.779 0.020 . 2 . . . . 18 ARG HG2 . 15137 1 110 . 1 1 18 18 ARG HG3 H 1 1.542 0.020 . 2 . . . . 18 ARG HG3 . 15137 1 111 . 1 1 18 18 ARG N N 15 115.50 . . . . . . . 18 ARG N . 15137 1 112 . 1 1 19 19 ASP H H 1 7.028 0.020 . 1 . . . . 19 ASP H . 15137 1 113 . 1 1 19 19 ASP HA H 1 4.461 0.020 . 1 . . . . 19 ASP HA . 15137 1 114 . 1 1 19 19 ASP HB2 H 1 2.917 0.020 . 1 . . . . 19 ASP HB2 . 15137 1 115 . 1 1 19 19 ASP HB3 H 1 2.917 0.020 . 1 . . . . 19 ASP HB3 . 15137 1 116 . 1 1 19 19 ASP N N 15 119.00 . . . . . . . 19 ASP N . 15137 1 117 . 1 1 20 20 TYR H H 1 7.596 0.020 . 1 . . . . 20 TYR H . 15137 1 118 . 1 1 20 20 TYR HA H 1 4.474 0.020 . 1 . . . . 20 TYR HA . 15137 1 119 . 1 1 20 20 TYR HB2 H 1 2.913 0.020 . 2 . . . . 20 TYR HB2 . 15137 1 120 . 1 1 20 20 TYR HB3 H 1 2.892 0.020 . 2 . . . . 20 TYR HB3 . 15137 1 121 . 1 1 20 20 TYR HD1 H 1 6.947 0.020 . 1 . . . . 20 TYR HD1 . 15137 1 122 . 1 1 20 20 TYR HD2 H 1 6.947 0.020 . 1 . . . . 20 TYR HD2 . 15137 1 123 . 1 1 20 20 TYR HE1 H 1 6.427 0.020 . 1 . . . . 20 TYR HE1 . 15137 1 124 . 1 1 20 20 TYR HE2 H 1 6.427 0.020 . 1 . . . . 20 TYR HE2 . 15137 1 125 . 1 1 20 20 TYR HH H 1 9.061 0.020 . 1 . . . . 20 TYR HH . 15137 1 126 . 1 1 20 20 TYR N N 15 124.50 . . . . . . . 20 TYR N . 15137 1 127 . 1 1 21 21 VAL H H 1 8.315 0.020 . 1 . . . . 21 VAL H . 15137 1 128 . 1 1 21 21 VAL HA H 1 2.749 0.020 . 1 . . . . 21 VAL HA . 15137 1 129 . 1 1 21 21 VAL HB H 1 1.835 0.020 . 1 . . . . 21 VAL HB . 15137 1 130 . 1 1 21 21 VAL HG11 H 1 0.244 0.020 . 2 . . . . 21 VAL HG11 . 15137 1 131 . 1 1 21 21 VAL HG12 H 1 0.244 0.020 . 2 . . . . 21 VAL HG12 . 15137 1 132 . 1 1 21 21 VAL HG13 H 1 0.244 0.020 . 2 . . . . 21 VAL HG13 . 15137 1 133 . 1 1 21 21 VAL HG21 H 1 0.868 0.020 . 2 . . . . 21 VAL HG21 . 15137 1 134 . 1 1 21 21 VAL HG22 H 1 0.868 0.020 . 2 . . . . 21 VAL HG22 . 15137 1 135 . 1 1 21 21 VAL HG23 H 1 0.868 0.020 . 2 . . . . 21 VAL HG23 . 15137 1 136 . 1 1 21 21 VAL N N 15 120.60 . . . . . . . 21 VAL N . 15137 1 137 . 1 1 22 22 ASP H H 1 7.542 0.020 . 1 . . . . 22 ASP H . 15137 1 138 . 1 1 22 22 ASP HA H 1 4.475 0.020 . 1 . . . . 22 ASP HA . 15137 1 139 . 1 1 22 22 ASP HB2 H 1 2.739 0.020 . 2 . . . . 22 ASP HB2 . 15137 1 140 . 1 1 22 22 ASP HB3 H 1 2.844 0.020 . 2 . . . . 22 ASP HB3 . 15137 1 141 . 1 1 22 22 ASP N N 15 118.00 . . . . . . . 22 ASP N . 15137 1 142 . 1 1 23 23 ARG H H 1 7.969 0.020 . 1 . . . . 23 ARG H . 15137 1 143 . 1 1 23 23 ARG HA H 1 4.048 0.020 . 1 . . . . 23 ARG HA . 15137 1 144 . 1 1 23 23 ARG HB2 H 1 1.906 0.020 . 2 . . . . 23 ARG HB2 . 15137 1 145 . 1 1 23 23 ARG HB3 H 1 2.067 0.020 . 2 . . . . 23 ARG HB3 . 15137 1 146 . 1 1 23 23 ARG HD2 H 1 3.238 0.020 . 2 . . . . 23 ARG HD2 . 15137 1 147 . 1 1 23 23 ARG HD3 H 1 3.441 0.020 . 2 . . . . 23 ARG HD3 . 15137 1 148 . 1 1 23 23 ARG HE H 1 9.465 0.020 . 1 . . . . 23 ARG HE . 15137 1 149 . 1 1 23 23 ARG HG2 H 1 1.574 0.020 . 2 . . . . 23 ARG HG2 . 15137 1 150 . 1 1 23 23 ARG HG3 H 1 1.603 0.020 . 2 . . . . 23 ARG HG3 . 15137 1 151 . 1 1 23 23 ARG N N 15 119.70 . . . . . . . 23 ARG N . 15137 1 152 . 1 1 24 24 PHE H H 1 9.021 0.020 . 1 . . . . 24 PHE H . 15137 1 153 . 1 1 24 24 PHE HA H 1 3.688 0.020 . 1 . . . . 24 PHE HA . 15137 1 154 . 1 1 24 24 PHE HB2 H 1 2.304 0.020 . 2 . . . . 24 PHE HB2 . 15137 1 155 . 1 1 24 24 PHE HB3 H 1 2.935 0.020 . 2 . . . . 24 PHE HB3 . 15137 1 156 . 1 1 24 24 PHE HD1 H 1 6.424 0.020 . 1 . . . . 24 PHE HD1 . 15137 1 157 . 1 1 24 24 PHE HD2 H 1 6.424 0.020 . 1 . . . . 24 PHE HD2 . 15137 1 158 . 1 1 24 24 PHE HE1 H 1 6.955 0.020 . 1 . . . . 24 PHE HE1 . 15137 1 159 . 1 1 24 24 PHE HE2 H 1 6.955 0.020 . 1 . . . . 24 PHE HE2 . 15137 1 160 . 1 1 24 24 PHE HZ H 1 7.017 0.020 . 1 . . . . 24 PHE HZ . 15137 1 161 . 1 1 24 24 PHE N N 15 124.50 . . . . . . . 24 PHE N . 15137 1 162 . 1 1 25 25 TYR H H 1 8.756 0.020 . 1 . . . . 25 TYR H . 15137 1 163 . 1 1 25 25 TYR HA H 1 4.150 0.020 . 1 . . . . 25 TYR HA . 15137 1 164 . 1 1 25 25 TYR HB2 H 1 3.054 0.020 . 1 . . . . 25 TYR HB2 . 15137 1 165 . 1 1 25 25 TYR HB3 H 1 3.054 0.020 . 1 . . . . 25 TYR HB3 . 15137 1 166 . 1 1 25 25 TYR HD1 H 1 7.341 0.020 . 1 . . . . 25 TYR HD1 . 15137 1 167 . 1 1 25 25 TYR HD2 H 1 7.341 0.020 . 1 . . . . 25 TYR HD2 . 15137 1 168 . 1 1 25 25 TYR HE1 H 1 6.736 0.020 . 1 . . . . 25 TYR HE1 . 15137 1 169 . 1 1 25 25 TYR HE2 H 1 6.736 0.020 . 1 . . . . 25 TYR HE2 . 15137 1 170 . 1 1 25 25 TYR HH H 1 9.277 0.020 . 1 . . . . 25 TYR HH . 15137 1 171 . 1 1 25 25 TYR N N 15 117.00 . . . . . . . 25 TYR N . 15137 1 172 . 1 1 26 26 LYS H H 1 8.372 0.020 . 1 . . . . 26 LYS H . 15137 1 173 . 1 1 26 26 LYS HA H 1 4.049 0.020 . 1 . . . . 26 LYS HA . 15137 1 174 . 1 1 26 26 LYS HB2 H 1 1.982 0.020 . 2 . . . . 26 LYS HB2 . 15137 1 175 . 1 1 26 26 LYS HB3 H 1 1.952 0.020 . 2 . . . . 26 LYS HB3 . 15137 1 176 . 1 1 26 26 LYS HD2 H 1 1.630 0.020 . 1 . . . . 26 LYS HD2 . 15137 1 177 . 1 1 26 26 LYS HD3 H 1 1.630 0.020 . 1 . . . . 26 LYS HD3 . 15137 1 178 . 1 1 26 26 LYS N N 15 120.80 . . . . . . . 26 LYS N . 15137 1 179 . 1 1 27 27 THR H H 1 7.743 0.020 . 1 . . . . 27 THR H . 15137 1 180 . 1 1 27 27 THR HA H 1 4.050 0.020 . 1 . . . . 27 THR HA . 15137 1 181 . 1 1 27 27 THR HB H 1 3.948 0.020 . 1 . . . . 27 THR HB . 15137 1 182 . 1 1 27 27 THR HG21 H 1 0.981 0.020 . 1 . . . . 27 THR HG21 . 15137 1 183 . 1 1 27 27 THR HG22 H 1 0.981 0.020 . 1 . . . . 27 THR HG22 . 15137 1 184 . 1 1 27 27 THR HG23 H 1 0.981 0.020 . 1 . . . . 27 THR HG23 . 15137 1 185 . 1 1 27 27 THR N N 15 117.50 . . . . . . . 27 THR N . 15137 1 186 . 1 1 28 28 LEU H H 1 8.101 0.020 . 1 . . . . 28 LEU H . 15137 1 187 . 1 1 28 28 LEU HA H 1 3.815 0.020 . 1 . . . . 28 LEU HA . 15137 1 188 . 1 1 28 28 LEU HB2 H 1 1.890 0.020 . 2 . . . . 28 LEU HB2 . 15137 1 189 . 1 1 28 28 LEU HB3 H 1 1.985 0.020 . 2 . . . . 28 LEU HB3 . 15137 1 190 . 1 1 28 28 LEU HD11 H 1 0.741 0.020 . 2 . . . . 28 LEU HD11 . 15137 1 191 . 1 1 28 28 LEU HD12 H 1 0.741 0.020 . 2 . . . . 28 LEU HD12 . 15137 1 192 . 1 1 28 28 LEU HD13 H 1 0.741 0.020 . 2 . . . . 28 LEU HD13 . 15137 1 193 . 1 1 28 28 LEU HD21 H 1 0.806 0.020 . 2 . . . . 28 LEU HD21 . 15137 1 194 . 1 1 28 28 LEU HD22 H 1 0.806 0.020 . 2 . . . . 28 LEU HD22 . 15137 1 195 . 1 1 28 28 LEU HD23 H 1 0.806 0.020 . 2 . . . . 28 LEU HD23 . 15137 1 196 . 1 1 28 28 LEU HG H 1 1.641 0.020 . 1 . . . . 28 LEU HG . 15137 1 197 . 1 1 28 28 LEU N N 15 122.80 . . . . . . . 28 LEU N . 15137 1 198 . 1 1 29 29 ARG H H 1 8.026 0.020 . 1 . . . . 29 ARG H . 15137 1 199 . 1 1 29 29 ARG HA H 1 4.144 0.020 . 1 . . . . 29 ARG HA . 15137 1 200 . 1 1 29 29 ARG HB2 H 1 1.645 0.020 . 2 . . . . 29 ARG HB2 . 15137 1 201 . 1 1 29 29 ARG HB3 H 1 1.890 0.020 . 2 . . . . 29 ARG HB3 . 15137 1 202 . 1 1 29 29 ARG HD2 H 1 3.240 0.020 . 1 . . . . 29 ARG HD2 . 15137 1 203 . 1 1 29 29 ARG HD3 H 1 3.240 0.020 . 1 . . . . 29 ARG HD3 . 15137 1 204 . 1 1 29 29 ARG HG2 H 1 1.362 0.020 . 2 . . . . 29 ARG HG2 . 15137 1 205 . 1 1 29 29 ARG HG3 H 1 1.491 0.020 . 2 . . . . 29 ARG HG3 . 15137 1 206 . 1 1 29 29 ARG N N 15 116.60 . . . . . . . 29 ARG N . 15137 1 207 . 1 1 30 30 ALA H H 1 7.534 0.020 . 1 . . . . 30 ALA H . 15137 1 208 . 1 1 30 30 ALA HA H 1 4.284 0.020 . 1 . . . . 30 ALA HA . 15137 1 209 . 1 1 30 30 ALA HB1 H 1 1.529 0.020 . 1 . . . . 30 ALA HB1 . 15137 1 210 . 1 1 30 30 ALA HB2 H 1 1.529 0.020 . 1 . . . . 30 ALA HB2 . 15137 1 211 . 1 1 30 30 ALA HB3 H 1 1.529 0.020 . 1 . . . . 30 ALA HB3 . 15137 1 212 . 1 1 30 30 ALA N N 15 121.30 . . . . . . . 30 ALA N . 15137 1 213 . 1 1 31 31 GLU H H 1 7.837 0.020 . 1 . . . . 31 GLU H . 15137 1 214 . 1 1 31 31 GLU HA H 1 4.274 0.020 . 1 . . . . 31 GLU HA . 15137 1 215 . 1 1 31 31 GLU HB2 H 1 2.030 0.020 . 2 . . . . 31 GLU HB2 . 15137 1 216 . 1 1 31 31 GLU HB3 H 1 2.416 0.020 . 2 . . . . 31 GLU HB3 . 15137 1 217 . 1 1 31 31 GLU HG2 H 1 2.210 0.020 . 2 . . . . 31 GLU HG2 . 15137 1 218 . 1 1 31 31 GLU HG3 H 1 2.281 0.020 . 2 . . . . 31 GLU HG3 . 15137 1 219 . 1 1 31 31 GLU N N 15 118.00 . . . . . . . 31 GLU N . 15137 1 220 . 1 1 32 32 GLN HB2 H 1 2.144 0.020 . 1 . . . . 32 GLN HB2 . 15137 1 221 . 1 1 32 32 GLN HB3 H 1 2.144 0.020 . 1 . . . . 32 GLN HB3 . 15137 1 222 . 1 1 32 32 GLN HE21 H 1 6.857 0.020 . 2 . . . . 32 GLN HE21 . 15137 1 223 . 1 1 32 32 GLN HG2 H 1 2.270 0.020 . 2 . . . . 32 GLN HG2 . 15137 1 224 . 1 1 32 32 GLN HG3 H 1 2.406 0.020 . 2 . . . . 32 GLN HG3 . 15137 1 225 . 1 1 32 32 GLN N N 15 118.00 . . . . . . . 32 GLN N . 15137 1 226 . 1 1 33 33 ALA H H 1 8.301 0.020 . 1 . . . . 33 ALA H . 15137 1 227 . 1 1 33 33 ALA HA H 1 4.473 0.020 . 1 . . . . 33 ALA HA . 15137 1 228 . 1 1 33 33 ALA HB1 H 1 1.383 0.020 . 1 . . . . 33 ALA HB1 . 15137 1 229 . 1 1 33 33 ALA HB2 H 1 1.383 0.020 . 1 . . . . 33 ALA HB2 . 15137 1 230 . 1 1 33 33 ALA HB3 H 1 1.383 0.020 . 1 . . . . 33 ALA HB3 . 15137 1 231 . 1 1 33 33 ALA N N 15 115.00 . . . . . . . 33 ALA N . 15137 1 232 . 1 1 34 34 SER H H 1 8.271 0.020 . 1 . . . . 34 SER H . 15137 1 233 . 1 1 34 34 SER HA H 1 4.328 0.020 . 1 . . . . 34 SER HA . 15137 1 234 . 1 1 34 34 SER HB2 H 1 4.139 0.020 . 1 . . . . 34 SER HB2 . 15137 1 235 . 1 1 34 34 SER HB3 H 1 4.139 0.020 . 1 . . . . 34 SER HB3 . 15137 1 236 . 1 1 35 35 GLN H H 1 8.121 0.020 . 1 . . . . 35 GLN H . 15137 1 237 . 1 1 35 35 GLN HA H 1 4.521 0.020 . 1 . . . . 35 GLN HA . 15137 1 238 . 1 1 35 35 GLN HB2 H 1 1.857 0.020 . 2 . . . . 35 GLN HB2 . 15137 1 239 . 1 1 35 35 GLN HB3 H 1 1.971 0.020 . 2 . . . . 35 GLN HB3 . 15137 1 240 . 1 1 35 35 GLN HE21 H 1 6.941 0.020 . 2 . . . . 35 GLN HE21 . 15137 1 241 . 1 1 35 35 GLN HE22 H 1 7.562 0.020 . 2 . . . . 35 GLN HE22 . 15137 1 242 . 1 1 35 35 GLN HG2 H 1 2.507 0.020 . 2 . . . . 35 GLN HG2 . 15137 1 243 . 1 1 35 35 GLN HG3 H 1 2.431 0.020 . 2 . . . . 35 GLN HG3 . 15137 1 244 . 1 1 36 36 GLU HA H 1 4.187 0.020 . 1 . . . . 36 GLU HA . 15137 1 245 . 1 1 36 36 GLU HB2 H 1 2.031 0.020 . 2 . . . . 36 GLU HB2 . 15137 1 246 . 1 1 36 36 GLU HB3 H 1 2.103 0.020 . 2 . . . . 36 GLU HB3 . 15137 1 247 . 1 1 36 36 GLU HG2 H 1 2.897 0.020 . 2 . . . . 36 GLU HG2 . 15137 1 248 . 1 1 36 36 GLU HG3 H 1 2.609 0.020 . 2 . . . . 36 GLU HG3 . 15137 1 249 . 1 1 37 37 VAL H H 1 7.787 0.020 . 1 . . . . 37 VAL H . 15137 1 250 . 1 1 37 37 VAL HA H 1 3.942 0.020 . 1 . . . . 37 VAL HA . 15137 1 251 . 1 1 37 37 VAL HB H 1 2.141 0.020 . 1 . . . . 37 VAL HB . 15137 1 252 . 1 1 37 37 VAL HG11 H 1 0.951 0.020 . 2 . . . . 37 VAL HG11 . 15137 1 253 . 1 1 37 37 VAL HG12 H 1 0.951 0.020 . 2 . . . . 37 VAL HG12 . 15137 1 254 . 1 1 37 37 VAL HG13 H 1 0.951 0.020 . 2 . . . . 37 VAL HG13 . 15137 1 255 . 1 1 37 37 VAL HG21 H 1 0.990 0.020 . 2 . . . . 37 VAL HG21 . 15137 1 256 . 1 1 37 37 VAL HG22 H 1 0.990 0.020 . 2 . . . . 37 VAL HG22 . 15137 1 257 . 1 1 37 37 VAL HG23 H 1 0.990 0.020 . 2 . . . . 37 VAL HG23 . 15137 1 258 . 1 1 37 37 VAL N N 15 121.50 . . . . . . . 37 VAL N . 15137 1 259 . 1 1 38 38 LYS H H 1 8.456 0.020 . 1 . . . . 38 LYS H . 15137 1 260 . 1 1 38 38 LYS HA H 1 4.143 0.020 . 1 . . . . 38 LYS HA . 15137 1 261 . 1 1 38 38 LYS HB2 H 1 1.859 0.020 . 2 . . . . 38 LYS HB2 . 15137 1 262 . 1 1 38 38 LYS HB3 H 1 1.992 0.020 . 2 . . . . 38 LYS HB3 . 15137 1 263 . 1 1 38 38 LYS HG2 H 1 1.270 0.020 . 2 . . . . 38 LYS HG2 . 15137 1 264 . 1 1 38 38 LYS HG3 H 1 1.554 0.020 . 2 . . . . 38 LYS HG3 . 15137 1 265 . 1 1 38 38 LYS N N 15 122.50 . . . . . . . 38 LYS N . 15137 1 266 . 1 1 39 39 ASN HA H 1 4.463 0.020 . 1 . . . . 39 ASN HA . 15137 1 267 . 1 1 39 39 ASN HB2 H 1 3.150 0.020 . 2 . . . . 39 ASN HB2 . 15137 1 268 . 1 1 39 39 ASN HB3 H 1 3.435 0.020 . 2 . . . . 39 ASN HB3 . 15137 1 269 . 1 1 39 39 ASN HD21 H 1 7.744 0.020 . 2 . . . . 39 ASN HD21 . 15137 1 270 . 1 1 39 39 ASN HD22 H 1 6.374 0.020 . 2 . . . . 39 ASN HD22 . 15137 1 271 . 1 1 40 40 ALA HB1 H 1 1.525 0.020 . 1 . . . . 40 ALA HB1 . 15137 1 272 . 1 1 40 40 ALA HB2 H 1 1.525 0.020 . 1 . . . . 40 ALA HB2 . 15137 1 273 . 1 1 40 40 ALA HB3 H 1 1.525 0.020 . 1 . . . . 40 ALA HB3 . 15137 1 274 . 1 1 41 41 MET H H 1 8.537 0.020 . 1 . . . . 41 MET H . 15137 1 275 . 1 1 41 41 MET HA H 1 4.395 0.020 . 1 . . . . 41 MET HA . 15137 1 276 . 1 1 41 41 MET HB2 H 1 2.088 0.020 . 2 . . . . 41 MET HB2 . 15137 1 277 . 1 1 41 41 MET HB3 H 1 2.256 0.020 . 2 . . . . 41 MET HB3 . 15137 1 278 . 1 1 41 41 MET HG2 H 1 2.588 0.020 . 2 . . . . 41 MET HG2 . 15137 1 279 . 1 1 41 41 MET HG3 H 1 2.727 0.020 . 2 . . . . 41 MET HG3 . 15137 1 280 . 1 1 41 41 MET N N 15 118.00 . . . . . . . 41 MET N . 15137 1 281 . 1 1 42 42 THR H H 1 8.154 0.020 . 1 . . . . 42 THR H . 15137 1 282 . 1 1 42 42 THR HA H 1 4.426 0.020 . 1 . . . . 42 THR HA . 15137 1 283 . 1 1 42 42 THR HB H 1 4.023 0.020 . 1 . . . . 42 THR HB . 15137 1 284 . 1 1 42 42 THR HG21 H 1 1.300 0.020 . 1 . . . . 42 THR HG21 . 15137 1 285 . 1 1 42 42 THR HG22 H 1 1.300 0.020 . 1 . . . . 42 THR HG22 . 15137 1 286 . 1 1 42 42 THR HG23 H 1 1.300 0.020 . 1 . . . . 42 THR HG23 . 15137 1 287 . 1 1 42 42 THR N N 15 116.10 . . . . . . . 42 THR N . 15137 1 288 . 1 1 43 43 GLU H H 1 8.902 0.020 . 1 . . . . 43 GLU H . 15137 1 289 . 1 1 43 43 GLU HA H 1 4.031 0.020 . 1 . . . . 43 GLU HA . 15137 1 290 . 1 1 43 43 GLU HB2 H 1 2.158 0.020 . 2 . . . . 43 GLU HB2 . 15137 1 291 . 1 1 43 43 GLU HB3 H 1 2.098 0.020 . 2 . . . . 43 GLU HB3 . 15137 1 292 . 1 1 43 43 GLU HG2 H 1 2.633 0.020 . 2 . . . . 43 GLU HG2 . 15137 1 293 . 1 1 43 43 GLU HG3 H 1 2.889 0.020 . 2 . . . . 43 GLU HG3 . 15137 1 294 . 1 1 43 43 GLU N N 15 117.20 . . . . . . . 43 GLU N . 15137 1 295 . 1 1 44 44 THR H H 1 7.734 0.020 . 1 . . . . 44 THR H . 15137 1 296 . 1 1 44 44 THR HA H 1 4.439 0.020 . 1 . . . . 44 THR HA . 15137 1 297 . 1 1 44 44 THR HB H 1 4.220 0.020 . 1 . . . . 44 THR HB . 15137 1 298 . 1 1 44 44 THR HG21 H 1 1.305 0.020 . 1 . . . . 44 THR HG21 . 15137 1 299 . 1 1 44 44 THR HG22 H 1 1.305 0.020 . 1 . . . . 44 THR HG22 . 15137 1 300 . 1 1 44 44 THR HG23 H 1 1.305 0.020 . 1 . . . . 44 THR HG23 . 15137 1 301 . 1 1 44 44 THR N N 15 112.50 . . . . . . . 44 THR N . 15137 1 302 . 1 1 45 45 LEU H H 1 8.130 0.020 . 1 . . . . 45 LEU H . 15137 1 303 . 1 1 45 45 LEU HA H 1 4.186 0.020 . 1 . . . . 45 LEU HA . 15137 1 304 . 1 1 45 45 LEU HB2 H 1 1.101 0.020 . 2 . . . . 45 LEU HB2 . 15137 1 305 . 1 1 45 45 LEU HB3 H 1 1.572 0.020 . 2 . . . . 45 LEU HB3 . 15137 1 306 . 1 1 45 45 LEU HD11 H 1 0.142 0.020 . 2 . . . . 45 LEU HD11 . 15137 1 307 . 1 1 45 45 LEU HD12 H 1 0.142 0.020 . 2 . . . . 45 LEU HD12 . 15137 1 308 . 1 1 45 45 LEU HD13 H 1 0.142 0.020 . 2 . . . . 45 LEU HD13 . 15137 1 309 . 1 1 45 45 LEU HD21 H 1 0.716 0.020 . 2 . . . . 45 LEU HD21 . 15137 1 310 . 1 1 45 45 LEU HD22 H 1 0.716 0.020 . 2 . . . . 45 LEU HD22 . 15137 1 311 . 1 1 45 45 LEU HD23 H 1 0.716 0.020 . 2 . . . . 45 LEU HD23 . 15137 1 312 . 1 1 45 45 LEU HG H 1 0.918 0.020 . 1 . . . . 45 LEU HG . 15137 1 313 . 1 1 45 45 LEU N N 15 122.50 . . . . . . . 45 LEU N . 15137 1 314 . 1 1 46 46 LEU H H 1 7.549 0.020 . 1 . . . . 46 LEU H . 15137 1 315 . 1 1 46 46 LEU HA H 1 3.484 0.020 . 1 . . . . 46 LEU HA . 15137 1 316 . 1 1 46 46 LEU HB2 H 1 1.600 0.020 . 2 . . . . 46 LEU HB2 . 15137 1 317 . 1 1 46 46 LEU HB3 H 1 0.811 0.020 . 2 . . . . 46 LEU HB3 . 15137 1 318 . 1 1 46 46 LEU HD11 H 1 -0.038 0.020 . 2 . . . . 46 LEU HD11 . 15137 1 319 . 1 1 46 46 LEU HD12 H 1 -0.038 0.020 . 2 . . . . 46 LEU HD12 . 15137 1 320 . 1 1 46 46 LEU HD13 H 1 -0.038 0.020 . 2 . . . . 46 LEU HD13 . 15137 1 321 . 1 1 46 46 LEU HD21 H 1 0.641 0.020 . 2 . . . . 46 LEU HD21 . 15137 1 322 . 1 1 46 46 LEU HD22 H 1 0.641 0.020 . 2 . . . . 46 LEU HD22 . 15137 1 323 . 1 1 46 46 LEU HD23 H 1 0.641 0.020 . 2 . . . . 46 LEU HD23 . 15137 1 324 . 1 1 46 46 LEU HG H 1 1.059 0.020 . 1 . . . . 46 LEU HG . 15137 1 325 . 1 1 46 46 LEU N N 15 119.50 . . . . . . . 46 LEU N . 15137 1 326 . 1 1 47 47 VAL H H 1 7.586 0.020 . 1 . . . . 47 VAL H . 15137 1 327 . 1 1 47 47 VAL HA H 1 3.647 0.020 . 1 . . . . 47 VAL HA . 15137 1 328 . 1 1 47 47 VAL HB H 1 2.067 0.020 . 1 . . . . 47 VAL HB . 15137 1 329 . 1 1 47 47 VAL HG11 H 1 0.914 0.020 . 2 . . . . 47 VAL HG11 . 15137 1 330 . 1 1 47 47 VAL HG12 H 1 0.914 0.020 . 2 . . . . 47 VAL HG12 . 15137 1 331 . 1 1 47 47 VAL HG13 H 1 0.914 0.020 . 2 . . . . 47 VAL HG13 . 15137 1 332 . 1 1 47 47 VAL HG21 H 1 1.064 0.020 . 2 . . . . 47 VAL HG21 . 15137 1 333 . 1 1 47 47 VAL HG22 H 1 1.064 0.020 . 2 . . . . 47 VAL HG22 . 15137 1 334 . 1 1 47 47 VAL HG23 H 1 1.064 0.020 . 2 . . . . 47 VAL HG23 . 15137 1 335 . 1 1 47 47 VAL N N 15 116.50 . . . . . . . 47 VAL N . 15137 1 336 . 1 1 48 48 GLN H H 1 7.887 0.020 . 1 . . . . 48 GLN H . 15137 1 337 . 1 1 48 48 GLN HA H 1 3.897 0.020 . 1 . . . . 48 GLN HA . 15137 1 338 . 1 1 48 48 GLN HB2 H 1 2.099 0.020 . 2 . . . . 48 GLN HB2 . 15137 1 339 . 1 1 48 48 GLN HB3 H 1 2.191 0.020 . 2 . . . . 48 GLN HB3 . 15137 1 340 . 1 1 48 48 GLN HE22 H 1 7.599 0.020 . 2 . . . . 48 GLN HE22 . 15137 1 341 . 1 1 48 48 GLN HG2 H 1 2.468 0.020 . 2 . . . . 48 GLN HG2 . 15137 1 342 . 1 1 48 48 GLN HG3 H 1 2.988 0.020 . 2 . . . . 48 GLN HG3 . 15137 1 343 . 1 1 48 48 GLN N N 15 117.30 . . . . . . . 48 GLN N . 15137 1 344 . 1 1 49 49 ASN H H 1 7.889 0.020 . 1 . . . . 49 ASN H . 15137 1 345 . 1 1 49 49 ASN HA H 1 4.968 0.020 . 1 . . . . 49 ASN HA . 15137 1 346 . 1 1 49 49 ASN HB2 H 1 3.385 0.020 . 2 . . . . 49 ASN HB2 . 15137 1 347 . 1 1 49 49 ASN HB3 H 1 3.626 0.020 . 2 . . . . 49 ASN HB3 . 15137 1 348 . 1 1 49 49 ASN HD21 H 1 7.777 0.020 . 2 . . . . 49 ASN HD21 . 15137 1 349 . 1 1 49 49 ASN HD22 H 1 6.542 0.020 . 2 . . . . 49 ASN HD22 . 15137 1 350 . 1 1 49 49 ASN N N 15 115.20 . . . . . . . 49 ASN N . 15137 1 351 . 1 1 50 50 ALA H H 1 7.334 0.020 . 1 . . . . 50 ALA H . 15137 1 352 . 1 1 50 50 ALA HA H 1 4.274 0.020 . 1 . . . . 50 ALA HA . 15137 1 353 . 1 1 50 50 ALA HB1 H 1 1.637 0.020 . 1 . . . . 50 ALA HB1 . 15137 1 354 . 1 1 50 50 ALA HB2 H 1 1.637 0.020 . 1 . . . . 50 ALA HB2 . 15137 1 355 . 1 1 50 50 ALA HB3 H 1 1.637 0.020 . 1 . . . . 50 ALA HB3 . 15137 1 356 . 1 1 50 50 ALA N N 15 124.50 . . . . . . . 50 ALA N . 15137 1 357 . 1 1 51 51 ASN H H 1 9.057 0.020 . 1 . . . . 51 ASN H . 15137 1 358 . 1 1 51 51 ASN HB2 H 1 2.355 0.020 . 2 . . . . 51 ASN HB2 . 15137 1 359 . 1 1 51 51 ASN HB3 H 1 3.103 0.020 . 2 . . . . 51 ASN HB3 . 15137 1 360 . 1 1 51 51 ASN HD21 H 1 7.471 0.020 . 2 . . . . 51 ASN HD21 . 15137 1 361 . 1 1 51 51 ASN HD22 H 1 6.733 0.020 . 2 . . . . 51 ASN HD22 . 15137 1 362 . 1 1 51 51 ASN N N 15 119.50 . . . . . . . 51 ASN N . 15137 1 363 . 1 1 52 52 PRO HA H 1 4.305 0.020 . 1 . . . . 52 PRO HA . 15137 1 364 . 1 1 52 52 PRO HB2 H 1 2.021 0.020 . 2 . . . . 52 PRO HB2 . 15137 1 365 . 1 1 52 52 PRO HB3 H 1 2.173 0.020 . 2 . . . . 52 PRO HB3 . 15137 1 366 . 1 1 52 52 PRO HD2 H 1 3.836 0.020 . 1 . . . . 52 PRO HD2 . 15137 1 367 . 1 1 52 52 PRO HD3 H 1 3.836 0.020 . 1 . . . . 52 PRO HD3 . 15137 1 368 . 1 1 52 52 PRO HG2 H 1 2.444 0.020 . 1 . . . . 52 PRO HG2 . 15137 1 369 . 1 1 52 52 PRO HG3 H 1 2.444 0.020 . 1 . . . . 52 PRO HG3 . 15137 1 370 . 1 1 53 53 ASP H H 1 7.993 0.020 . 1 . . . . 53 ASP H . 15137 1 371 . 1 1 53 53 ASP HA H 1 4.421 0.020 . 1 . . . . 53 ASP HA . 15137 1 372 . 1 1 53 53 ASP HB2 H 1 2.607 0.020 . 1 . . . . 53 ASP HB2 . 15137 1 373 . 1 1 53 53 ASP HB3 H 1 2.607 0.020 . 1 . . . . 53 ASP HB3 . 15137 1 374 . 1 1 53 53 ASP N N 15 116.50 . . . . . . . 53 ASP N . 15137 1 375 . 1 1 54 54 CYS H H 1 8.342 0.020 . 1 . . . . 54 CYS H . 15137 1 376 . 1 1 54 54 CYS HB2 H 1 2.824 0.020 . 2 . . . . 54 CYS HB2 . 15137 1 377 . 1 1 54 54 CYS HB3 H 1 3.452 0.020 . 2 . . . . 54 CYS HB3 . 15137 1 378 . 1 1 54 54 CYS N N 15 117.80 . . . . . . . 54 CYS N . 15137 1 379 . 1 1 55 55 LYS H H 1 9.304 0.020 . 1 . . . . 55 LYS H . 15137 1 380 . 1 1 55 55 LYS HA H 1 3.701 0.020 . 1 . . . . 55 LYS HA . 15137 1 381 . 1 1 55 55 LYS HB2 H 1 1.779 0.020 . 2 . . . . 55 LYS HB2 . 15137 1 382 . 1 1 55 55 LYS HB3 H 1 1.831 0.020 . 2 . . . . 55 LYS HB3 . 15137 1 383 . 1 1 55 55 LYS HD2 H 1 1.507 0.020 . 2 . . . . 55 LYS HD2 . 15137 1 384 . 1 1 55 55 LYS HD3 H 1 1.784 0.020 . 2 . . . . 55 LYS HD3 . 15137 1 385 . 1 1 55 55 LYS HG2 H 1 1.329 0.020 . 2 . . . . 55 LYS HG2 . 15137 1 386 . 1 1 55 55 LYS HG3 H 1 1.518 0.020 . 2 . . . . 55 LYS HG3 . 15137 1 387 . 1 1 55 55 LYS N N 15 120.70 . . . . . . . 55 LYS N . 15137 1 388 . 1 1 56 56 THR H H 1 7.819 0.020 . 1 . . . . 56 THR H . 15137 1 389 . 1 1 56 56 THR HA H 1 4.227 0.020 . 1 . . . . 56 THR HA . 15137 1 390 . 1 1 56 56 THR HB H 1 3.828 0.020 . 1 . . . . 56 THR HB . 15137 1 391 . 1 1 56 56 THR HG21 H 1 1.274 0.020 . 1 . . . . 56 THR HG21 . 15137 1 392 . 1 1 56 56 THR HG22 H 1 1.274 0.020 . 1 . . . . 56 THR HG22 . 15137 1 393 . 1 1 56 56 THR HG23 H 1 1.274 0.020 . 1 . . . . 56 THR HG23 . 15137 1 394 . 1 1 56 56 THR N N 15 113.50 . . . . . . . 56 THR N . 15137 1 395 . 1 1 57 57 ILE H H 1 7.080 0.020 . 1 . . . . 57 ILE H . 15137 1 396 . 1 1 57 57 ILE HA H 1 3.722 0.020 . 1 . . . . 57 ILE HA . 15137 1 397 . 1 1 57 57 ILE HB H 1 2.172 0.020 . 1 . . . . 57 ILE HB . 15137 1 398 . 1 1 57 57 ILE HD11 H 1 0.931 0.020 . 1 . . . . 57 ILE HD11 . 15137 1 399 . 1 1 57 57 ILE HD12 H 1 0.931 0.020 . 1 . . . . 57 ILE HD12 . 15137 1 400 . 1 1 57 57 ILE HD13 H 1 0.931 0.020 . 1 . . . . 57 ILE HD13 . 15137 1 401 . 1 1 57 57 ILE HG12 H 1 1.095 0.020 . 2 . . . . 57 ILE HG12 . 15137 1 402 . 1 1 57 57 ILE HG13 H 1 1.755 0.020 . 2 . . . . 57 ILE HG13 . 15137 1 403 . 1 1 57 57 ILE HG21 H 1 0.766 0.020 . 1 . . . . 57 ILE HG21 . 15137 1 404 . 1 1 57 57 ILE HG22 H 1 0.766 0.020 . 1 . . . . 57 ILE HG22 . 15137 1 405 . 1 1 57 57 ILE HG23 H 1 0.766 0.020 . 1 . . . . 57 ILE HG23 . 15137 1 406 . 1 1 57 57 ILE N N 15 123.80 . . . . . . . 57 ILE N . 15137 1 407 . 1 1 58 58 LEU H H 1 8.657 0.020 . 1 . . . . 58 LEU H . 15137 1 408 . 1 1 58 58 LEU HA H 1 3.927 0.020 . 1 . . . . 58 LEU HA . 15137 1 409 . 1 1 58 58 LEU HB2 H 1 1.866 0.020 . 2 . . . . 58 LEU HB2 . 15137 1 410 . 1 1 58 58 LEU HB3 H 1 1.928 0.020 . 2 . . . . 58 LEU HB3 . 15137 1 411 . 1 1 58 58 LEU HD11 H 1 0.661 0.020 . 2 . . . . 58 LEU HD11 . 15137 1 412 . 1 1 58 58 LEU HD12 H 1 0.661 0.020 . 2 . . . . 58 LEU HD12 . 15137 1 413 . 1 1 58 58 LEU HD13 H 1 0.661 0.020 . 2 . . . . 58 LEU HD13 . 15137 1 414 . 1 1 58 58 LEU HD21 H 1 0.793 0.020 . 2 . . . . 58 LEU HD21 . 15137 1 415 . 1 1 58 58 LEU HD22 H 1 0.793 0.020 . 2 . . . . 58 LEU HD22 . 15137 1 416 . 1 1 58 58 LEU HD23 H 1 0.793 0.020 . 2 . . . . 58 LEU HD23 . 15137 1 417 . 1 1 58 58 LEU HG H 1 1.353 0.020 . 1 . . . . 58 LEU HG . 15137 1 418 . 1 1 58 58 LEU N N 15 118.70 . . . . . . . 58 LEU N . 15137 1 419 . 1 1 59 59 LYS H H 1 8.397 0.020 . 1 . . . . 59 LYS H . 15137 1 420 . 1 1 59 59 LYS HA H 1 4.021 0.020 . 1 . . . . 59 LYS HA . 15137 1 421 . 1 1 59 59 LYS HB2 H 1 1.901 0.020 . 2 . . . . 59 LYS HB2 . 15137 1 422 . 1 1 59 59 LYS HB3 H 1 1.914 0.020 . 2 . . . . 59 LYS HB3 . 15137 1 423 . 1 1 59 59 LYS HE2 H 1 2.979 0.020 . 1 . . . . 59 LYS HE2 . 15137 1 424 . 1 1 59 59 LYS HE3 H 1 2.979 0.020 . 1 . . . . 59 LYS HE3 . 15137 1 425 . 1 1 59 59 LYS HG2 H 1 1.456 0.020 . 2 . . . . 59 LYS HG2 . 15137 1 426 . 1 1 59 59 LYS HG3 H 1 1.617 0.020 . 2 . . . . 59 LYS HG3 . 15137 1 427 . 1 1 59 59 LYS N N 15 119.40 . . . . . . . 59 LYS N . 15137 1 428 . 1 1 60 60 ALA H H 1 7.208 0.020 . 1 . . . . 60 ALA H . 15137 1 429 . 1 1 60 60 ALA HA H 1 4.303 0.020 . 1 . . . . 60 ALA HA . 15137 1 430 . 1 1 60 60 ALA HB1 H 1 1.522 0.020 . 1 . . . . 60 ALA HB1 . 15137 1 431 . 1 1 60 60 ALA HB2 H 1 1.522 0.020 . 1 . . . . 60 ALA HB2 . 15137 1 432 . 1 1 60 60 ALA HB3 H 1 1.522 0.020 . 1 . . . . 60 ALA HB3 . 15137 1 433 . 1 1 60 60 ALA N N 15 120.00 . . . . . . . 60 ALA N . 15137 1 434 . 1 1 61 61 LEU H H 1 7.535 0.020 . 1 . . . . 61 LEU H . 15137 1 435 . 1 1 61 61 LEU HA H 1 4.217 0.020 . 1 . . . . 61 LEU HA . 15137 1 436 . 1 1 61 61 LEU HB2 H 1 1.882 0.020 . 2 . . . . 61 LEU HB2 . 15137 1 437 . 1 1 61 61 LEU HB3 H 1 1.912 0.020 . 2 . . . . 61 LEU HB3 . 15137 1 438 . 1 1 61 61 LEU HD11 H 1 0.799 0.020 . 2 . . . . 61 LEU HD11 . 15137 1 439 . 1 1 61 61 LEU HD12 H 1 0.799 0.020 . 2 . . . . 61 LEU HD12 . 15137 1 440 . 1 1 61 61 LEU HD13 H 1 0.799 0.020 . 2 . . . . 61 LEU HD13 . 15137 1 441 . 1 1 61 61 LEU HD21 H 1 0.799 0.020 . 2 . . . . 61 LEU HD21 . 15137 1 442 . 1 1 61 61 LEU HD22 H 1 0.799 0.020 . 2 . . . . 61 LEU HD22 . 15137 1 443 . 1 1 61 61 LEU HD23 H 1 0.799 0.020 . 2 . . . . 61 LEU HD23 . 15137 1 444 . 1 1 61 61 LEU HG H 1 1.688 0.020 . 1 . . . . 61 LEU HG . 15137 1 445 . 1 1 61 61 LEU N N 15 118.50 . . . . . . . 61 LEU N . 15137 1 446 . 1 1 62 62 GLY H H 1 7.523 0.020 . 1 . . . . 62 GLY H . 15137 1 447 . 1 1 62 62 GLY HA2 H 1 4.405 0.020 . 2 . . . . 62 GLY HA2 . 15137 1 448 . 1 1 62 62 GLY HA3 H 1 3.997 0.020 . 2 . . . . 62 GLY HA3 . 15137 1 449 . 1 1 62 62 GLY N N 15 104.50 . . . . . . . 62 GLY N . 15137 1 450 . 1 1 63 63 PRO HA H 1 4.398 0.020 . 1 . . . . 63 PRO HA . 15137 1 451 . 1 1 63 63 PRO HB2 H 1 2.304 0.020 . 2 . . . . 63 PRO HB2 . 15137 1 452 . 1 1 63 63 PRO HB3 H 1 2.051 0.020 . 2 . . . . 63 PRO HB3 . 15137 1 453 . 1 1 63 63 PRO HD2 H 1 3.613 0.020 . 2 . . . . 63 PRO HD2 . 15137 1 454 . 1 1 63 63 PRO HD3 H 1 3.737 0.020 . 2 . . . . 63 PRO HD3 . 15137 1 455 . 1 1 63 63 PRO HG2 H 1 2.437 0.020 . 1 . . . . 63 PRO HG2 . 15137 1 456 . 1 1 63 63 PRO HG3 H 1 2.437 0.020 . 1 . . . . 63 PRO HG3 . 15137 1 457 . 1 1 64 64 ALA H H 1 8.598 0.020 . 1 . . . . 64 ALA H . 15137 1 458 . 1 1 64 64 ALA HA H 1 4.479 0.020 . 1 . . . . 64 ALA HA . 15137 1 459 . 1 1 64 64 ALA HB1 H 1 1.369 0.020 . 1 . . . . 64 ALA HB1 . 15137 1 460 . 1 1 64 64 ALA HB2 H 1 1.369 0.020 . 1 . . . . 64 ALA HB2 . 15137 1 461 . 1 1 64 64 ALA HB3 H 1 1.369 0.020 . 1 . . . . 64 ALA HB3 . 15137 1 462 . 1 1 64 64 ALA N N 15 113.20 . . . . . . . 64 ALA N . 15137 1 463 . 1 1 65 65 ALA H H 1 7.206 0.020 . 1 . . . . 65 ALA H . 15137 1 464 . 1 1 65 65 ALA HA H 1 4.409 0.020 . 1 . . . . 65 ALA HA . 15137 1 465 . 1 1 65 65 ALA HB1 H 1 1.359 0.020 . 1 . . . . 65 ALA HB1 . 15137 1 466 . 1 1 65 65 ALA HB2 H 1 1.359 0.020 . 1 . . . . 65 ALA HB2 . 15137 1 467 . 1 1 65 65 ALA HB3 H 1 1.359 0.020 . 1 . . . . 65 ALA HB3 . 15137 1 468 . 1 1 65 65 ALA N N 15 122.50 . . . . . . . 65 ALA N . 15137 1 469 . 1 1 66 66 THR H H 1 8.420 0.020 . 1 . . . . 66 THR H . 15137 1 470 . 1 1 66 66 THR HA H 1 4.468 0.020 . 1 . . . . 66 THR HA . 15137 1 471 . 1 1 66 66 THR HB H 1 3.987 0.020 . 1 . . . . 66 THR HB . 15137 1 472 . 1 1 66 66 THR HG21 H 1 1.373 0.020 . 1 . . . . 66 THR HG21 . 15137 1 473 . 1 1 66 66 THR HG22 H 1 1.373 0.020 . 1 . . . . 66 THR HG22 . 15137 1 474 . 1 1 66 66 THR HG23 H 1 1.373 0.020 . 1 . . . . 66 THR HG23 . 15137 1 475 . 1 1 66 66 THR N N 15 122.50 . . . . . . . 66 THR N . 15137 1 476 . 1 1 67 67 LEU H H 1 8.930 0.020 . 1 . . . . 67 LEU H . 15137 1 477 . 1 1 67 67 LEU HA H 1 4.268 0.020 . 1 . . . . 67 LEU HA . 15137 1 478 . 1 1 67 67 LEU HB2 H 1 1.681 0.020 . 2 . . . . 67 LEU HB2 . 15137 1 479 . 1 1 67 67 LEU HB3 H 1 1.724 0.020 . 2 . . . . 67 LEU HB3 . 15137 1 480 . 1 1 67 67 LEU HD11 H 1 0.902 0.020 . 2 . . . . 67 LEU HD11 . 15137 1 481 . 1 1 67 67 LEU HD12 H 1 0.902 0.020 . 2 . . . . 67 LEU HD12 . 15137 1 482 . 1 1 67 67 LEU HD13 H 1 0.902 0.020 . 2 . . . . 67 LEU HD13 . 15137 1 483 . 1 1 67 67 LEU HD21 H 1 1.049 0.020 . 2 . . . . 67 LEU HD21 . 15137 1 484 . 1 1 67 67 LEU HD22 H 1 1.049 0.020 . 2 . . . . 67 LEU HD22 . 15137 1 485 . 1 1 67 67 LEU HD23 H 1 1.049 0.020 . 2 . . . . 67 LEU HD23 . 15137 1 486 . 1 1 67 67 LEU HG H 1 1.628 0.020 . 1 . . . . 67 LEU HG . 15137 1 487 . 1 1 67 67 LEU N N 15 122.50 . . . . . . . 67 LEU N . 15137 1 488 . 1 1 68 68 GLU H H 1 8.613 0.020 . 1 . . . . 68 GLU H . 15137 1 489 . 1 1 68 68 GLU HA H 1 3.991 0.020 . 1 . . . . 68 GLU HA . 15137 1 490 . 1 1 68 68 GLU HB2 H 1 1.934 0.020 . 2 . . . . 68 GLU HB2 . 15137 1 491 . 1 1 68 68 GLU HB3 H 1 2.064 0.020 . 2 . . . . 68 GLU HB3 . 15137 1 492 . 1 1 68 68 GLU HG2 H 1 2.297 0.020 . 2 . . . . 68 GLU HG2 . 15137 1 493 . 1 1 68 68 GLU HG3 H 1 2.428 0.020 . 2 . . . . 68 GLU HG3 . 15137 1 494 . 1 1 68 68 GLU N N 15 117.50 . . . . . . . 68 GLU N . 15137 1 495 . 1 1 69 69 GLU H H 1 7.761 0.020 . 1 . . . . 69 GLU H . 15137 1 496 . 1 1 69 69 GLU HA H 1 4.010 0.020 . 1 . . . . 69 GLU HA . 15137 1 497 . 1 1 69 69 GLU HB2 H 1 2.074 0.020 . 2 . . . . 69 GLU HB2 . 15137 1 498 . 1 1 69 69 GLU HB3 H 1 1.947 0.020 . 2 . . . . 69 GLU HB3 . 15137 1 499 . 1 1 69 69 GLU HG2 H 1 2.309 0.020 . 2 . . . . 69 GLU HG2 . 15137 1 500 . 1 1 69 69 GLU HG3 H 1 2.477 0.020 . 2 . . . . 69 GLU HG3 . 15137 1 501 . 1 1 69 69 GLU N N 15 120.30 . . . . . . . 69 GLU N . 15137 1 502 . 1 1 70 70 MET H H 1 8.492 0.020 . 1 . . . . 70 MET H . 15137 1 503 . 1 1 70 70 MET HA H 1 3.661 0.020 . 1 . . . . 70 MET HA . 15137 1 504 . 1 1 70 70 MET HB2 H 1 1.847 0.020 . 2 . . . . 70 MET HB2 . 15137 1 505 . 1 1 70 70 MET HB3 H 1 2.217 0.020 . 2 . . . . 70 MET HB3 . 15137 1 506 . 1 1 70 70 MET HG2 H 1 2.864 0.020 . 2 . . . . 70 MET HG2 . 15137 1 507 . 1 1 70 70 MET HG3 H 1 2.440 0.020 . 2 . . . . 70 MET HG3 . 15137 1 508 . 1 1 70 70 MET N N 15 120.30 . . . . . . . 70 MET N . 15137 1 509 . 1 1 71 71 MET H H 1 8.673 0.020 . 1 . . . . 71 MET H . 15137 1 510 . 1 1 71 71 MET HA H 1 4.213 0.020 . 1 . . . . 71 MET HA . 15137 1 511 . 1 1 71 71 MET HB2 H 1 2.171 0.020 . 2 . . . . 71 MET HB2 . 15137 1 512 . 1 1 71 71 MET HB3 H 1 2.399 0.020 . 2 . . . . 71 MET HB3 . 15137 1 513 . 1 1 71 71 MET HG2 H 1 2.548 0.020 . 2 . . . . 71 MET HG2 . 15137 1 514 . 1 1 71 71 MET HG3 H 1 2.995 0.020 . 2 . . . . 71 MET HG3 . 15137 1 515 . 1 1 71 71 MET N N 15 116.50 . . . . . . . 71 MET N . 15137 1 516 . 1 1 72 72 THR H H 1 8.093 0.020 . 1 . . . . 72 THR H . 15137 1 517 . 1 1 72 72 THR HA H 1 4.164 0.020 . 1 . . . . 72 THR HA . 15137 1 518 . 1 1 72 72 THR HB H 1 3.920 0.020 . 1 . . . . 72 THR HB . 15137 1 519 . 1 1 72 72 THR HG21 H 1 1.219 0.020 . 1 . . . . 72 THR HG21 . 15137 1 520 . 1 1 72 72 THR HG22 H 1 1.219 0.020 . 1 . . . . 72 THR HG22 . 15137 1 521 . 1 1 72 72 THR HG23 H 1 1.219 0.020 . 1 . . . . 72 THR HG23 . 15137 1 522 . 1 1 72 72 THR N N 15 115.30 . . . . . . . 72 THR N . 15137 1 523 . 1 1 73 73 ALA H H 1 7.936 0.020 . 1 . . . . 73 ALA H . 15137 1 524 . 1 1 73 73 ALA HA H 1 4.122 0.020 . 1 . . . . 73 ALA HA . 15137 1 525 . 1 1 73 73 ALA HB1 H 1 1.397 0.020 . 1 . . . . 73 ALA HB1 . 15137 1 526 . 1 1 73 73 ALA HB2 H 1 1.397 0.020 . 1 . . . . 73 ALA HB2 . 15137 1 527 . 1 1 73 73 ALA HB3 H 1 1.397 0.020 . 1 . . . . 73 ALA HB3 . 15137 1 528 . 1 1 73 73 ALA N N 15 123.80 . . . . . . . 73 ALA N . 15137 1 529 . 1 1 74 74 CYS H H 1 7.645 0.020 . 1 . . . . 74 CYS H . 15137 1 530 . 1 1 74 74 CYS HA H 1 4.598 0.020 . 1 . . . . 74 CYS HA . 15137 1 531 . 1 1 74 74 CYS HB2 H 1 2.560 0.020 . 2 . . . . 74 CYS HB2 . 15137 1 532 . 1 1 74 74 CYS HB3 H 1 3.058 0.020 . 2 . . . . 74 CYS HB3 . 15137 1 533 . 1 1 74 74 CYS N N 15 111.00 . . . . . . . 74 CYS N . 15137 1 534 . 1 1 75 75 GLN H H 1 7.651 0.020 . 1 . . . . 75 GLN H . 15137 1 535 . 1 1 75 75 GLN HA H 1 4.341 0.020 . 1 . . . . 75 GLN HA . 15137 1 536 . 1 1 75 75 GLN HB2 H 1 2.263 0.020 . 2 . . . . 75 GLN HB2 . 15137 1 537 . 1 1 75 75 GLN HB3 H 1 2.400 0.020 . 2 . . . . 75 GLN HB3 . 15137 1 538 . 1 1 75 75 GLN HG2 H 1 2.580 0.020 . 2 . . . . 75 GLN HG2 . 15137 1 539 . 1 1 75 75 GLN HG3 H 1 2.640 0.020 . 2 . . . . 75 GLN HG3 . 15137 1 540 . 1 1 75 75 GLN N N 15 121.00 . . . . . . . 75 GLN N . 15137 1 541 . 1 1 77 77 VAL H H 1 7.599 0.020 . 1 . . . . 77 VAL H . 15137 1 542 . 1 1 77 77 VAL HA H 1 4.027 0.020 . 1 . . . . 77 VAL HA . 15137 1 543 . 1 1 77 77 VAL HB H 1 2.119 0.020 . 1 . . . . 77 VAL HB . 15137 1 544 . 1 1 77 77 VAL HG11 H 1 0.877 0.020 . 2 . . . . 77 VAL HG11 . 15137 1 545 . 1 1 77 77 VAL HG12 H 1 0.877 0.020 . 2 . . . . 77 VAL HG12 . 15137 1 546 . 1 1 77 77 VAL HG13 H 1 0.877 0.020 . 2 . . . . 77 VAL HG13 . 15137 1 547 . 1 1 77 77 VAL HG21 H 1 0.931 0.020 . 2 . . . . 77 VAL HG21 . 15137 1 548 . 1 1 77 77 VAL HG22 H 1 0.931 0.020 . 2 . . . . 77 VAL HG22 . 15137 1 549 . 1 1 77 77 VAL HG23 H 1 0.931 0.020 . 2 . . . . 77 VAL HG23 . 15137 1 550 . 1 1 77 77 VAL N N 15 119.50 . . . . . . . 77 VAL N . 15137 1 551 . 1 1 78 78 GLY H H 1 8.635 0.020 . 1 . . . . 78 GLY H . 15137 1 552 . 1 1 78 78 GLY N N 15 124.00 . . . . . . . 78 GLY N . 15137 1 553 . 1 1 79 79 GLY N N 15 125.00 . . . . . . . 79 GLY N . 15137 1 554 . 1 1 81 81 GLY HA2 H 1 3.933 0.020 . 2 . . . . 81 GLY HA2 . 15137 1 555 . 1 1 81 81 GLY HA3 H 1 4.135 0.020 . 2 . . . . 81 GLY HA3 . 15137 1 556 . 1 1 81 81 GLY N N 15 108.50 . . . . . . . 81 GLY N . 15137 1 557 . 1 1 82 82 HIS H H 1 8.396 0.020 . 1 . . . . 82 HIS H . 15137 1 558 . 1 1 82 82 HIS HA H 1 4.546 0.020 . 1 . . . . 82 HIS HA . 15137 1 559 . 1 1 82 82 HIS HB2 H 1 3.093 0.020 . 1 . . . . 82 HIS HB2 . 15137 1 560 . 1 1 82 82 HIS HB3 H 1 3.093 0.020 . 1 . . . . 82 HIS HB3 . 15137 1 561 . 1 1 82 82 HIS HD2 H 1 6.981 0.020 . 1 . . . . 82 HIS HD2 . 15137 1 562 . 1 1 83 83 LYS H H 1 7.596 0.020 . 1 . . . . 83 LYS H . 15137 1 563 . 1 1 83 83 LYS HA H 1 4.276 0.020 . 1 . . . . 83 LYS HA . 15137 1 564 . 1 1 83 83 LYS HB2 H 1 1.583 0.020 . 2 . . . . 83 LYS HB2 . 15137 1 565 . 1 1 83 83 LYS HB3 H 1 1.667 0.020 . 2 . . . . 83 LYS HB3 . 15137 1 566 . 1 1 83 83 LYS HG2 H 1 1.380 0.020 . 1 . . . . 83 LYS HG2 . 15137 1 567 . 1 1 83 83 LYS HG3 H 1 1.380 0.020 . 1 . . . . 83 LYS HG3 . 15137 1 568 . 1 1 84 84 ALA N N 15 121.00 . . . . . . . 84 ALA N . 15137 1 569 . 1 1 85 85 ARG H H 1 8.748 0.020 . 1 . . . . 85 ARG H . 15137 1 570 . 1 1 85 85 ARG HA H 1 4.303 0.020 . 1 . . . . 85 ARG HA . 15137 1 571 . 1 1 85 85 ARG HB2 H 1 1.918 0.020 . 2 . . . . 85 ARG HB2 . 15137 1 572 . 1 1 85 85 ARG HB3 H 1 1.978 0.020 . 2 . . . . 85 ARG HB3 . 15137 1 573 . 1 1 85 85 ARG HD2 H 1 3.101 0.020 . 1 . . . . 85 ARG HD2 . 15137 1 574 . 1 1 85 85 ARG HD3 H 1 3.101 0.020 . 1 . . . . 85 ARG HD3 . 15137 1 575 . 1 1 85 85 ARG HG2 H 1 1.615 0.020 . 1 . . . . 85 ARG HG2 . 15137 1 576 . 1 1 85 85 ARG HG3 H 1 1.615 0.020 . 1 . . . . 85 ARG HG3 . 15137 1 577 . 1 1 86 86 VAL HA H 1 4.114 0.020 . 1 . . . . 86 VAL HA . 15137 1 578 . 1 1 86 86 VAL HB H 1 2.154 0.020 . 1 . . . . 86 VAL HB . 15137 1 579 . 1 1 86 86 VAL HG11 H 1 0.809 0.020 . 2 . . . . 86 VAL HG11 . 15137 1 580 . 1 1 86 86 VAL HG12 H 1 0.809 0.020 . 2 . . . . 86 VAL HG12 . 15137 1 581 . 1 1 86 86 VAL HG13 H 1 0.809 0.020 . 2 . . . . 86 VAL HG13 . 15137 1 582 . 1 1 86 86 VAL HG21 H 1 0.953 0.020 . 2 . . . . 86 VAL HG21 . 15137 1 583 . 1 1 86 86 VAL HG22 H 1 0.953 0.020 . 2 . . . . 86 VAL HG22 . 15137 1 584 . 1 1 86 86 VAL HG23 H 1 0.953 0.020 . 2 . . . . 86 VAL HG23 . 15137 1 585 . 1 1 86 86 VAL N N 15 123.00 . . . . . . . 86 VAL N . 15137 1 586 . 1 1 87 87 LEU HB2 H 1 1.862 0.020 . 1 . . . . 87 LEU HB2 . 15137 1 587 . 1 1 87 87 LEU HB3 H 1 1.862 0.020 . 1 . . . . 87 LEU HB3 . 15137 1 588 . 1 1 87 87 LEU HD11 H 1 0.925 0.020 . 2 . . . . 87 LEU HD11 . 15137 1 589 . 1 1 87 87 LEU HD12 H 1 0.925 0.020 . 2 . . . . 87 LEU HD12 . 15137 1 590 . 1 1 87 87 LEU HD13 H 1 0.925 0.020 . 2 . . . . 87 LEU HD13 . 15137 1 591 . 1 1 87 87 LEU HD21 H 1 0.961 0.020 . 2 . . . . 87 LEU HD21 . 15137 1 592 . 1 1 87 87 LEU HD22 H 1 0.961 0.020 . 2 . . . . 87 LEU HD22 . 15137 1 593 . 1 1 87 87 LEU HD23 H 1 0.961 0.020 . 2 . . . . 87 LEU HD23 . 15137 1 594 . 1 1 87 87 LEU N N 15 132.00 . . . . . . . 87 LEU N . 15137 1 stop_ save_