data_4220 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4220 _Entry.Title ; HIV-1 capsid protein major homology region peptide analog ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-07-28 _Entry.Accession_date 1998-07-28 _Entry.Last_release_date 2000-04-07 _Entry.Original_release_date 2000-04-07 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 C. Clish . B. . 4220 2 D. Peyton . H. . 4220 3 E. Barklis . . . 4220 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4220 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 178 4220 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 1 . . 2000-04-07 1998-07-28 original author . 4220 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4220 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 99013448 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 257 _Citation.Journal_issue . _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 69 _Citation.Page_last 77 _Citation.Year 1998 _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 C. Clish . B. . 4220 1 2 D. Peyton . H. . 4220 1 3 E. Barklis . . . 4220 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Capsid 4220 1 HIV 4220 1 'major homology region' 4220 1 MHR 4220 1 P24 4220 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HIV-1_capsid _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HIV-1_capsid _Assembly.Entry_ID 4220 _Assembly.ID 1 _Assembly.Name 'HIV-1 capsid' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not reported' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4220 1 stop_ 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 'HIV-1 capsid' 1 $HIV-1_capsid . . . native . . . . . 4220 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'HIV-1 capsid' abbreviation 4220 1 'HIV-1 capsid' system 4220 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HIV-1_capsid _Entity.Sf_category entity _Entity.Sf_framecode HIV-1_capsid _Entity.Entry_ID 4220 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'HIV-1 capsid' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; CSILDIRQGPKEPFRDYVDR FYKTLRAEQAS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 31 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 15137 . "CAC monomer" . . . . . 96.77 87 100.00 100.00 3.03e-12 . . . . 4220 1 2 no BMRB 16555 . HIV-1_Capsid_Protein . . . . . 96.77 88 100.00 100.00 4.48e-12 . . . . 4220 1 3 no BMRB 17307 . Capsid_protein_p24 . . . . . 96.77 105 100.00 100.00 2.44e-13 . . . . 4220 1 4 no BMRB 17738 . HIV-1_CA . . . . . 96.77 240 100.00 100.00 9.45e-13 . . . . 4220 1 5 no BMRB 19261 . HIVcapsid . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 6 no BMRB 19264 . entity . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 7 no BMRB 19575 . HIV1_CA . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 8 no BMRB 25532 . Gag . . . . . 96.77 432 100.00 100.00 1.78e-11 . . . . 4220 1 9 no PDB 1A43 . "Structure Of The Hiv-1 Capsid Protein Dimerization Domain At 2.6a Resolution" . . . . . 96.77 87 100.00 100.00 3.79e-12 . . . . 4220 1 10 no PDB 1A8O . "Hiv Capsid C-Terminal Domain" . . . . . 87.10 70 100.00 100.00 5.16e-10 . . . . 4220 1 11 no PDB 1AUM . "Hiv Capsid C-Terminal Domain (Cac146)" . . . . . 90.32 70 100.00 100.00 7.65e-11 . . . . 4220 1 12 no PDB 1BAJ . "Hiv-1 Capsid Protein C-Terminal Fragment Plus Gag P2 Domain" . . . . . 96.77 101 100.00 100.00 9.31e-13 . . . . 4220 1 13 no PDB 1BMX . "Hiv-1 Capsid Protein Major Homology Region Peptide Analog, Nmr, 8 Structures" . . . . . 100.00 31 100.00 100.00 4.89e-13 . . . . 4220 1 14 no PDB 1E6J . "Crystal Structure Of Hiv-1 Capsid Protein (p24) In Complex With Fab13b5" . . . . . 96.77 210 100.00 100.00 1.10e-12 . . . . 4220 1 15 no PDB 1VU4 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 16 no PDB 1VU5 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 17 no PDB 1VU6 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 18 no PDB 1VU7 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 19 no PDB 1VU8 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 20 no PDB 1VU9 . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 21 no PDB 1VUA . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 22 no PDB 1VUC . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 23 no PDB 1VUD . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 24 no PDB 1VUE . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 25 no PDB 1VUF . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 26 no PDB 1VUG . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 27 no PDB 1VUH . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 28 no PDB 1VUI . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 29 no PDB 1VUJ . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 30 no PDB 1VUK . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 31 no PDB 1VUL . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 32 no PDB 1VUM . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 33 no PDB 1VUN . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 34 no PDB 1VUO . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 35 no PDB 1VUP . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 36 no PDB 1VUQ . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 37 no PDB 1VUR . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 38 no PDB 1VUS . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 39 no PDB 1VUT . "Atomic-level Structure Of The Entire Hiv-1 Capsid" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 40 no PDB 1VUU . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 41 no PDB 1VUV . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 42 no PDB 1VUW . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 43 no PDB 1VUX . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 44 no PDB 1VUY . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 45 no PDB 1VUZ . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 46 no PDB 1VV0 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 47 no PDB 1VV1 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 48 no PDB 1VV2 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 49 no PDB 1VV3 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 50 no PDB 1VV4 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 51 no PDB 1VV5 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 52 no PDB 1VV6 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 53 no PDB 1VV7 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 54 no PDB 1VV8 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 55 no PDB 1VV9 . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 56 no PDB 1VVA . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 57 no PDB 1VVB . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 58 no PDB 1VVF . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 59 no PDB 1VVG . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 60 no PDB 1VVH . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 61 no PDB 1VVI . "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 62 no PDB 2BUO . "Hiv-1 Capsid C-Terminal Domain In Complex With An Inhibitor Of Particle Assembly" . . . . . 96.77 86 100.00 100.00 4.09e-12 . . . . 4220 1 63 no PDB 2JO0 . "The Solution Structure Of The Monomeric Species Of The C Terminal Domain Of The Ca Protein Of Hiv-1" . . . . . 96.77 87 100.00 100.00 3.03e-12 . . . . 4220 1 64 no PDB 2JYG . "Solution Structure Of The W184aM185A MUTANT OF THE CARBOXY- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" . . . . . 96.77 84 100.00 100.00 3.21e-12 . . . . 4220 1 65 no PDB 2JYL . "Solution Structure Of A Double Mutant Of The Carboxy- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" . . . . . 96.77 105 100.00 100.00 2.44e-13 . . . . 4220 1 66 no PDB 2KOD . "A High-Resolution Nmr Structure Of The Dimeric C-Terminal Domain Of Hiv-1 Ca" . . . . . 96.77 88 100.00 100.00 4.48e-12 . . . . 4220 1 67 no PDB 2L6E . "Nmr Structure Of The Monomeric Mutant C-Terminal Domain Of Hiv-1 Capsid In Complex With Stapled Peptide Inhibitor" . . . . . 96.77 105 100.00 100.00 2.44e-13 . . . . 4220 1 68 no PDB 2LF4 . "Structure Of A Monomeric Mutant Of The Hiv-1 Capsid Protein" . . . . . 96.77 240 100.00 100.00 9.45e-13 . . . . 4220 1 69 no PDB 2M8L . "Hiv Capsid Dimer Structure" . . . . . 96.77 221 100.00 100.00 8.74e-13 . . . . 4220 1 70 no PDB 2M8N . "Hiv-1 Capsid Monomer Structure" . . . . . 96.77 221 100.00 100.00 8.74e-13 . . . . 4220 1 71 no PDB 2M8P . "The Structure Of The W184am185a Mutant Of The Hiv-1 Capsid Protein" . . . . . 96.77 221 100.00 100.00 1.11e-12 . . . . 4220 1 72 no PDB 2XT1 . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-231) In Complex With A Camelid Vhh" . . . . . 96.77 86 100.00 100.00 4.09e-12 . . . . 4220 1 73 no PDB 2XV6 . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-220) In Complex With A Camelid Vhh." . . . . . 96.77 75 100.00 100.00 3.50e-12 . . . . 4220 1 74 no PDB 2XXM . "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain In Complex With A Camelid Vhh And The Cai Peptide" . . . . . 96.77 75 100.00 100.00 3.50e-12 . . . . 4220 1 75 no PDB 3DIK . "Pseudo-Atomic Model Of The Hiv-1 Ca Hexameric Lattice" . . . . . 96.77 219 100.00 100.00 1.07e-12 . . . . 4220 1 76 no PDB 3DPH . "Hiv-1 Capsid C-Terminal Domain Mutant (L211s)" . . . . . 96.77 86 100.00 100.00 4.09e-12 . . . . 4220 1 77 no PDB 3DS0 . "Hiv-1 Capsid C-Terminal Domain Mutant (N183a) In Complex With An Inhibitor Of Particle Assembly (Cai)" . . . . . 96.77 86 100.00 100.00 4.31e-12 . . . . 4220 1 78 no PDB 3DS1 . "Hiv-1 Capsid C-Terminal Domain Mutant (E187a) In Complex With An Inhibitor Of Particle Assembly (Cai)" . . . . . 96.77 86 100.00 100.00 3.88e-12 . . . . 4220 1 79 no PDB 3DS4 . "Hiv-1 Capsid C-Terminal Domain Mutant (L211s) In Complex With An Inhibitor Of Particle Assembly (Cai)" . . . . . 96.77 86 100.00 100.00 4.09e-12 . . . . 4220 1 80 no PDB 3DS5 . "Hiv-1 Capsid C-Terminal Domain Mutant (N183a)" . . . . . 96.77 86 100.00 100.00 4.31e-12 . . . . 4220 1 81 no PDB 3DTJ . "Hiv-1 Capsid C-terminal Domain Mutant (e187a)" . . . . . 96.77 86 100.00 100.00 3.88e-12 . . . . 4220 1 82 no PDB 3GV2 . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 96.77 342 100.00 100.00 2.77e-12 . . . . 4220 1 83 no PDB 3H47 . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 84 no PDB 3H4E . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 85 no PDB 3J34 . "Structure Of Hiv-1 Capsid Protein By Cryo-em" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 86 no PDB 3J4F . "Structure Of Hiv-1 Capsid Protein By Cryo-em" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 87 no PDB 3LRY . "Crystal Structure Of Synthetic Hiv-1 Capsid C-Terminal Domain (Cca)" . . . . . 96.77 86 100.00 100.00 4.09e-12 . . . . 4220 1 88 no PDB 3MGE . "X-Ray Structure Of Hexameric Hiv-1 Ca" . . . . . 96.77 231 100.00 100.00 1.03e-12 . . . . 4220 1 89 no PDB 3NTE . "Crystal Structure Of The Wild-type Full-length Hiv-1 Capsid Protein" . . . . . 96.77 221 100.00 100.00 9.74e-13 . . . . 4220 1 90 no PDB 3P05 . "X-Ray Structure Of Pentameric Hiv-1 Ca" . . . . . 96.77 231 100.00 100.00 1.12e-12 . . . . 4220 1 91 no PDB 3P0A . "X-Ray Structure Of Pentameric Hiv-1 Ca" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 92 no PDB 4ARG . "Structure Of The Immature Retroviral Capsid At 8a Resolution By Cryo-Electron Microscopy" . . . . . 90.32 69 100.00 100.00 6.46e-11 . . . . 4220 1 93 no PDB 4IPY . "Hiv Capsid C-terminal Domain" . . . . . 96.77 87 100.00 100.00 3.79e-12 . . . . 4220 1 94 no PDB 4QNB . "Disulfide Stabilized Hiv-1 Ca Hexamer In Complex With Phenyl-l- Phenylalaninamide Inhibitor" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 95 no PDB 4U0A . "Hexameric Hiv-1 Ca In Complex With Cpsf6 Peptide, P6 Crystal Form" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 96 no PDB 4U0B . "Hexamer Hiv-1 Ca In Complex With Cpsf6 Peptide, P212121 Crystal Form" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 97 no PDB 4U0C . "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P6 Crystal Form" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 98 no PDB 4U0D . "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P212121 Crystal Form" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 99 no PDB 4U0E . "Hexameric Hiv-1 Ca In Complex With Pf3450074" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 100 no PDB 4U0F . "Hexameric Hiv-1 Ca In Complex With Bi-2" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 101 no PDB 4WYM . "Structural Basis Of Hiv-1 Capsid Recognition By Cpsf6" . . . . . 96.77 231 100.00 100.00 9.27e-13 . . . . 4220 1 102 no PDB 4XFX . "Structure Of The Native Full-length Hiv-1 Capsid Protein" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 103 no PDB 4XFY . "Structure Of The Native Full-length Dehydrated Hiv-1 Capsid Protein" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 104 no PDB 4XFZ . "Structure Of The Native Full-length Hiv-1 Capsid Protein In Complex With Pf-3450074 (pf74)" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 105 no DBJ BAA00992 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 96.77 500 100.00 100.00 3.85e-11 . . . . 4220 1 106 no DBJ BAA12988 . "Gag [Human immunodeficiency virus 1]" . . . . . 96.77 512 100.00 100.00 7.86e-11 . . . . 4220 1 107 no DBJ BAA12996 . "Gag [Human immunodeficiency virus 1]" . . . . . 96.77 512 100.00 100.00 9.02e-11 . . . . 4220 1 108 no DBJ BAA93773 . "gag protein [Human immunodeficiency virus 1]" . . . . . 96.77 231 100.00 100.00 1.01e-12 . . . . 4220 1 109 no DBJ BAA93774 . "gag protein [Human immunodeficiency virus 1]" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 110 no EMBL CAA11880 . "p24 [Human immunodeficiency virus 1]" . . . . . 96.77 189 100.00 100.00 1.90e-12 . . . . 4220 1 111 no EMBL CAA11882 . "p24 [Human immunodeficiency virus 1]" . . . . . 96.77 190 100.00 100.00 1.27e-12 . . . . 4220 1 112 no EMBL CAA11884 . "p24 [Human immunodeficiency virus 1]" . . . . . 96.77 191 100.00 100.00 9.63e-13 . . . . 4220 1 113 no EMBL CAA11885 . "p24 [Human immunodeficiency virus 1]" . . . . . 93.55 183 100.00 100.00 6.07e-12 . . . . 4220 1 114 no EMBL CAA11886 . "p24 [Human immunodeficiency virus 1]" . . . . . 96.77 190 100.00 100.00 1.95e-12 . . . . 4220 1 115 no GB AAA44201 . "gag polyprotein precursor [Human immunodeficiency virus 1]" . . . . . 96.77 512 100.00 100.00 8.02e-11 . . . . 4220 1 116 no GB AAA44224 . "gag protein, partial [Human immunodeficiency virus 1]" . . . . . 96.77 493 100.00 100.00 5.28e-11 . . . . 4220 1 117 no GB AAA44306 . "gag polyprotein [Human immunodeficiency virus 1]" . . . . . 96.77 500 100.00 100.00 7.21e-11 . . . . 4220 1 118 no GB AAA44313 . "gag protein, partial [Human immunodeficiency virus 1]" . . . . . 96.77 492 100.00 100.00 3.42e-11 . . . . 4220 1 119 no GB AAA44324 . "gag protein [Human immunodeficiency virus 1]" . . . . . 96.77 500 100.00 100.00 4.08e-11 . . . . 4220 1 120 no PIR FOVWLV . "gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a)" . . . . . 96.77 500 100.00 100.00 5.48e-11 . . . . 4220 1 121 no PRF 1102247B . "protein gag" . . . . . 96.77 512 100.00 100.00 8.02e-11 . . . . 4220 1 122 no PRF 1103299C . "gag gene" . . . . . 96.77 478 100.00 100.00 3.93e-11 . . . . 4220 1 123 no REF NP_057849 . "Gag-Pol [Human immunodeficiency virus 1]" . . . . . 96.77 1435 100.00 100.00 4.23e-11 . . . . 4220 1 124 no REF NP_057850 . "Pr55(Gag) [Human immunodeficiency virus 1]" . . . . . 96.77 500 100.00 100.00 5.59e-11 . . . . 4220 1 125 no REF NP_579880 . "capsid [Human immunodeficiency virus 1]" . . . . . 96.77 231 100.00 100.00 9.09e-13 . . . . 4220 1 126 no SP P03347 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 96.77 512 100.00 100.00 8.02e-11 . . . . 4220 1 127 no SP P03348 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 96.77 512 100.00 100.00 7.86e-11 . . . . 4220 1 128 no SP P03349 . "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " . . . . . 96.77 502 100.00 100.00 5.95e-11 . . . . 4220 1 129 no SP P03366 . "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " . . . . . 96.77 1447 100.00 100.00 4.24e-11 . . . . 4220 1 130 no SP P03367 . "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " . . . . . 96.77 1447 100.00 100.00 4.33e-11 . . . . 4220 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'HIV-1 capsid' abbreviation 4220 1 'HIV-1 capsid' common 4220 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 . CYS . 4220 1 2 . SER . 4220 1 3 . ILE . 4220 1 4 . LEU . 4220 1 5 . ASP . 4220 1 6 . ILE . 4220 1 7 . ARG . 4220 1 8 . GLN . 4220 1 9 . GLY . 4220 1 10 . PRO . 4220 1 11 . LYS . 4220 1 12 . GLU . 4220 1 13 . PRO . 4220 1 14 . PHE . 4220 1 15 . ARG . 4220 1 16 . ASP . 4220 1 17 . TYR . 4220 1 18 . VAL . 4220 1 19 . ASP . 4220 1 20 . ARG . 4220 1 21 . PHE . 4220 1 22 . TYR . 4220 1 23 . LYS . 4220 1 24 . THR . 4220 1 25 . LEU . 4220 1 26 . ARG . 4220 1 27 . ALA . 4220 1 28 . GLU . 4220 1 29 . GLN . 4220 1 30 . ALA . 4220 1 31 . SER . 4220 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 . CYS 1 1 4220 1 . SER 2 2 4220 1 . ILE 3 3 4220 1 . LEU 4 4 4220 1 . ASP 5 5 4220 1 . ILE 6 6 4220 1 . ARG 7 7 4220 1 . GLN 8 8 4220 1 . GLY 9 9 4220 1 . PRO 10 10 4220 1 . LYS 11 11 4220 1 . GLU 12 12 4220 1 . PRO 13 13 4220 1 . PHE 14 14 4220 1 . ARG 15 15 4220 1 . ASP 16 16 4220 1 . TYR 17 17 4220 1 . VAL 18 18 4220 1 . ASP 19 19 4220 1 . ARG 20 20 4220 1 . PHE 21 21 4220 1 . TYR 22 22 4220 1 . LYS 23 23 4220 1 . THR 24 24 4220 1 . LEU 25 25 4220 1 . ARG 26 26 4220 1 . ALA 27 27 4220 1 . GLU 28 28 4220 1 . GLN 29 29 4220 1 . ALA 30 30 4220 1 . SER 31 31 4220 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 4220 _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 $HIV-1_capsid . 9606 . . 'Homo sapiens' human . . Eukaryota . Homo sapiens . . . . . . . . . . . . . . . . . . . . . 4220 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 4220 _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 $HIV-1_capsid . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4220 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4220 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'HIV-1 capsid' . . . 1 $HIV-1_capsid . . . 5 7 mM . . . . 4220 1 2 H2O . . . . . . . 90 . . % . . . . 4220 1 3 D2O . . . . . . . 10 . . % . . . . 4220 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 4220 _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 pH 3.1 . n/a 4220 1 temperature 298 . K 4220 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4220 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4220 _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 NMR_spectrometer Bruker AMX . 400 . . . 4220 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 4220 _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 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4220 1 2 COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4220 1 3 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4220 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4220 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4220 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4220 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_ref _Chem_shift_reference.Entry_ID 4220 _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 . . . . . . . . . . . . . . . . . . . . 4220 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_chem_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4220 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_ref _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 $sample_1 . 4220 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 1 1 CYS HA H 1 4.277 . . . . . . . . . . . 4220 1 2 . 1 1 1 1 CYS HB2 H 1 3.036 . . . . . . . . . . . 4220 1 3 . 1 1 1 1 CYS HB3 H 1 3.115 . . . . . . . . . . . 4220 1 4 . 1 1 2 2 SER H H 1 8.823 . . . . . . . . . . . 4220 1 5 . 1 1 2 2 SER HA H 1 4.693 . . . . . . . . . . . 4220 1 6 . 1 1 2 2 SER HB2 H 1 4.023 . . . . . . . . . . . 4220 1 7 . 1 1 2 2 SER HB3 H 1 3.847 . . . . . . . . . . . 4220 1 8 . 1 1 3 3 ILE H H 1 8.323 . . . . . . . . . . . 4220 1 9 . 1 1 3 3 ILE HA H 1 4.082 . . . . . . . . . . . 4220 1 10 . 1 1 3 3 ILE HB H 1 1.855 . . . . . . . . . . . 4220 1 11 . 1 1 3 3 ILE HG12 H 1 1.237 . . . . . . . . . . . 4220 1 12 . 1 1 3 3 ILE HG13 H 1 1.459 . . . . . . . . . . . 4220 1 13 . 1 1 3 3 ILE HG21 H 1 0.910 . . . . . . . . . . . 4220 1 14 . 1 1 3 3 ILE HG22 H 1 0.910 . . . . . . . . . . . 4220 1 15 . 1 1 3 3 ILE HG23 H 1 0.910 . . . . . . . . . . . 4220 1 16 . 1 1 3 3 ILE HD11 H 1 0.863 . . . . . . . . . . . 4220 1 17 . 1 1 3 3 ILE HD12 H 1 0.863 . . . . . . . . . . . 4220 1 18 . 1 1 3 3 ILE HD13 H 1 0.863 . . . . . . . . . . . 4220 1 19 . 1 1 4 4 LEU H H 1 7.706 . . . . . . . . . . . 4220 1 20 . 1 1 4 4 LEU HA H 1 4.147 . . . . . . . . . . . 4220 1 21 . 1 1 4 4 LEU HG H 1 1.558 . . . . . . . . . . . 4220 1 22 . 1 1 4 4 LEU HD11 H 1 0.878 . . . . . . . . . . . 4220 1 23 . 1 1 4 4 LEU HD12 H 1 0.878 . . . . . . . . . . . 4220 1 24 . 1 1 4 4 LEU HD13 H 1 0.878 . . . . . . . . . . . 4220 1 25 . 1 1 4 4 LEU HB2 H 1 1.588 . . . . . . . . . . . 4220 1 26 . 1 1 4 4 LEU HD21 H 1 0.810 . . . . . . . . . . . 4220 1 27 . 1 1 4 4 LEU HD22 H 1 0.810 . . . . . . . . . . . 4220 1 28 . 1 1 4 4 LEU HD23 H 1 0.810 . . . . . . . . . . . 4220 1 29 . 1 1 5 5 ASP H H 1 7.847 . . . . . . . . . . . 4220 1 30 . 1 1 5 5 ASP HA H 1 4.583 . . . . . . . . . . . 4220 1 31 . 1 1 5 5 ASP HB2 H 1 2.845 . . . . . . . . . . . 4220 1 32 . 1 1 6 6 ILE H H 1 7.601 . . . . . . . . . . . 4220 1 33 . 1 1 6 6 ILE HA H 1 4.012 . . . . . . . . . . . 4220 1 34 . 1 1 6 6 ILE HB H 1 1.969 . . . . . . . . . . . 4220 1 35 . 1 1 6 6 ILE HG12 H 1 1.506 . . . . . . . . . . . 4220 1 36 . 1 1 6 6 ILE HG13 H 1 1.216 . . . . . . . . . . . 4220 1 37 . 1 1 6 6 ILE HG21 H 1 0.898 . . . . . . . . . . . 4220 1 38 . 1 1 6 6 ILE HG22 H 1 0.898 . . . . . . . . . . . 4220 1 39 . 1 1 6 6 ILE HG23 H 1 0.898 . . . . . . . . . . . 4220 1 40 . 1 1 6 6 ILE HD11 H 1 0.831 . . . . . . . . . . . 4220 1 41 . 1 1 6 6 ILE HD12 H 1 0.831 . . . . . . . . . . . 4220 1 42 . 1 1 6 6 ILE HD13 H 1 0.831 . . . . . . . . . . . 4220 1 43 . 1 1 7 7 ARG HE H 1 7.281 . . . . . . . . . . . 4220 1 44 . 1 1 7 7 ARG H H 1 8.053 . . . . . . . . . . . 4220 1 45 . 1 1 7 7 ARG HD2 H 1 3.145 . . . . . . . . . . . 4220 1 46 . 1 1 7 7 ARG HA H 1 4.191 . . . . . . . . . . . 4220 1 47 . 1 1 7 7 ARG HB3 H 1 1.831 . . . . . . . . . . . 4220 1 48 . 1 1 7 7 ARG HG3 H 1 1.647 . . . . . . . . . . . 4220 1 49 . 1 1 7 7 ARG HG2 H 1 1.716 . . . . . . . . . . . 4220 1 50 . 1 1 7 7 ARG HB2 H 1 1.880 . . . . . . . . . . . 4220 1 51 . 1 1 8 8 GLN H H 1 7.960 . . . . . . . . . . . 4220 1 52 . 1 1 8 8 GLN HA H 1 4.406 . . . . . . . . . . . 4220 1 53 . 1 1 8 8 GLN HB2 H 1 2.021 . . . . . . . . . . . 4220 1 54 . 1 1 8 8 GLN HG2 H 1 2.184 . . . . . . . . . . . 4220 1 55 . 1 1 8 8 GLN HG3 H 1 2.377 . . . . . . . . . . . 4220 1 56 . 1 1 8 8 GLN HE21 H 1 7.349 . . . . . . . . . . . 4220 1 57 . 1 1 8 8 GLN HE22 H 1 6.636 . . . . . . . . . . . 4220 1 58 . 1 1 9 9 GLY H H 1 7.901 . . . . . . . . . . . 4220 1 59 . 1 1 9 9 GLY HA2 H 1 4.071 . . . . . . . . . . . 4220 1 60 . 1 1 10 10 PRO HD2 H 1 3.596 . . . . . . . . . . . 4220 1 61 . 1 1 10 10 PRO HA H 1 4.490 . . . . . . . . . . . 4220 1 62 . 1 1 10 10 PRO HB3 H 1 1.928 . . . . . . . . . . . 4220 1 63 . 1 1 10 10 PRO HG2 H 1 2.012 . . . . . . . . . . . 4220 1 64 . 1 1 10 10 PRO HB2 H 1 2.297 . . . . . . . . . . . 4220 1 65 . 1 1 11 11 LYS H H 1 8.408 . . . . . . . . . . . 4220 1 66 . 1 1 11 11 LYS HA H 1 4.362 . . . . . . . . . . . 4220 1 67 . 1 1 11 11 LYS HE2 H 1 3.012 . . . . . . . . . . . 4220 1 68 . 1 1 11 11 LYS HB2 H 1 1.796 . . . . . . . . . . . 4220 1 69 . 1 1 11 11 LYS HD2 H 1 1.691 . . . . . . . . . . . 4220 1 70 . 1 1 11 11 LYS HG2 H 1 1.481 . . . . . . . . . . . 4220 1 71 . 1 1 13 13 PRO HD2 H 1 3.690 . . . . . . . . . . . 4220 1 72 . 1 1 13 13 PRO HA H 1 4.400 . . . . . . . . . . . 4220 1 73 . 1 1 13 13 PRO HD3 H 1 3.559 . . . . . . . . . . . 4220 1 74 . 1 1 13 13 PRO HB3 H 1 2.258 . . . . . . . . . . . 4220 1 75 . 1 1 13 13 PRO HB2 H 1 1.799 . . . . . . . . . . . 4220 1 76 . 1 1 13 13 PRO HG2 H 1 1.972 . . . . . . . . . . . 4220 1 77 . 1 1 14 14 PHE H H 1 7.502 . . . . . . . . . . . 4220 1 78 . 1 1 14 14 PHE HA H 1 4.494 . . . . . . . . . . . 4220 1 79 . 1 1 14 14 PHE HB2 H 1 3.150 . . . . . . . . . . . 4220 1 80 . 1 1 14 14 PHE HE1 H 1 7.246 . . . . . . . . . . . 4220 1 81 . 1 1 15 15 ARG HE H 1 7.207 . . . . . . . . . . . 4220 1 82 . 1 1 15 15 ARG H H 1 8.049 . . . . . . . . . . . 4220 1 83 . 1 1 15 15 ARG HA H 1 3.913 . . . . . . . . . . . 4220 1 84 . 1 1 15 15 ARG HB2 H 1 1.869 . . . . . . . . . . . 4220 1 85 . 1 1 15 15 ARG HG2 H 1 1.642 . . . . . . . . . . . 4220 1 86 . 1 1 15 15 ARG HG3 H 1 1.706 . . . . . . . . . . . 4220 1 87 . 1 1 15 15 ARG HD2 H 1 3.204 . . . . . . . . . . . 4220 1 88 . 1 1 16 16 ASP H H 1 8.290 . . . . . . . . . . . 4220 1 89 . 1 1 16 16 ASP HA H 1 4.418 . . . . . . . . . . . 4220 1 90 . 1 1 16 16 ASP HB2 H 1 2.771 . . . . . . . . . . . 4220 1 91 . 1 1 17 17 TYR H H 1 7.773 . . . . . . . . . . . 4220 1 92 . 1 1 17 17 TYR HA H 1 4.179 . . . . . . . . . . . 4220 1 93 . 1 1 17 17 TYR HB2 H 1 3.121 . . . . . . . . . . . 4220 1 94 . 1 1 17 17 TYR HD1 H 1 7.005 . . . . . . . . . . . 4220 1 95 . 1 1 17 17 TYR HE1 H 1 6.730 . . . . . . . . . . . 4220 1 96 . 1 1 18 18 VAL H H 1 8.088 . . . . . . . . . . . 4220 1 97 . 1 1 18 18 VAL HA H 1 3.528 . . . . . . . . . . . 4220 1 98 . 1 1 18 18 VAL HB H 1 1.995 . . . . . . . . . . . 4220 1 99 . 1 1 18 18 VAL HG11 H 1 0.828 . . . . . . . . . . . 4220 1 100 . 1 1 18 18 VAL HG12 H 1 0.828 . . . . . . . . . . . 4220 1 101 . 1 1 18 18 VAL HG13 H 1 0.828 . . . . . . . . . . . 4220 1 102 . 1 1 18 18 VAL HG21 H 1 0.938 . . . . . . . . . . . 4220 1 103 . 1 1 18 18 VAL HG22 H 1 0.938 . . . . . . . . . . . 4220 1 104 . 1 1 18 18 VAL HG23 H 1 0.938 . . . . . . . . . . . 4220 1 105 . 1 1 19 19 ASP H H 1 8.245 . . . . . . . . . . . 4220 1 106 . 1 1 19 19 ASP HA H 1 4.499 . . . . . . . . . . . 4220 1 107 . 1 1 19 19 ASP HB3 H 1 2.959 . . . . . . . . . . . 4220 1 108 . 1 1 19 19 ASP HB2 H 1 2.806 . . . . . . . . . . . 4220 1 109 . 1 1 20 20 ARG HE H 1 7.187 . . . . . . . . . . . 4220 1 110 . 1 1 20 20 ARG H H 1 7.829 . . . . . . . . . . . 4220 1 111 . 1 1 20 20 ARG HD2 H 1 3.099 . . . . . . . . . . . 4220 1 112 . 1 1 20 20 ARG HA H 1 3.965 . . . . . . . . . . . 4220 1 113 . 1 1 20 20 ARG HB2 H 1 1.852 . . . . . . . . . . . 4220 1 114 . 1 1 20 20 ARG HG3 H 1 1.650 . . . . . . . . . . . 4220 1 115 . 1 1 20 20 ARG HG2 H 1 1.509 . . . . . . . . . . . 4220 1 116 . 1 1 21 21 PHE H H 1 8.405 . . . . . . . . . . . 4220 1 117 . 1 1 21 21 PHE HA H 1 4.141 . . . . . . . . . . . 4220 1 118 . 1 1 21 21 PHE HB2 H 1 2.885 . . . . . . . . . . . 4220 1 119 . 1 1 21 21 PHE HB3 H 1 3.146 . . . . . . . . . . . 4220 1 120 . 1 1 21 21 PHE HE1 H 1 7.164 . . . . . . . . . . . 4220 1 121 . 1 1 21 21 PHE HD1 H 1 6.927 . . . . . . . . . . . 4220 1 122 . 1 1 22 22 TYR H H 1 8.544 . . . . . . . . . . . 4220 1 123 . 1 1 22 22 TYR HA H 1 4.046 . . . . . . . . . . . 4220 1 124 . 1 1 22 22 TYR HB3 H 1 3.099 . . . . . . . . . . . 4220 1 125 . 1 1 22 22 TYR HD1 H 1 7.134 . . . . . . . . . . . 4220 1 126 . 1 1 22 22 TYR HE1 H 1 6.779 . . . . . . . . . . . 4220 1 127 . 1 1 23 23 LYS H H 1 8.240 . . . . . . . . . . . 4220 1 128 . 1 1 23 23 LYS HA H 1 3.839 . . . . . . . . . . . 4220 1 129 . 1 1 23 23 LYS HD2 H 1 1.654 . . . . . . . . . . . 4220 1 130 . 1 1 23 23 LYS HG2 H 1 1.417 . . . . . . . . . . . 4220 1 131 . 1 1 23 23 LYS HE2 H 1 2.953 . . . . . . . . . . . 4220 1 132 . 1 1 23 23 LYS HB3 H 1 1.860 . . . . . . . . . . . 4220 1 133 . 1 1 23 23 LYS HB2 H 1 1.924 . . . . . . . . . . . 4220 1 134 . 1 1 24 24 THR H H 1 7.868 . . . . . . . . . . . 4220 1 135 . 1 1 24 24 THR HA H 1 3.864 . . . . . . . . . . . 4220 1 136 . 1 1 24 24 THR HB H 1 4.250 . . . . . . . . . . . 4220 1 137 . 1 1 24 24 THR HG21 H 1 1.147 . . . . . . . . . . . 4220 1 138 . 1 1 24 24 THR HG22 H 1 1.147 . . . . . . . . . . . 4220 1 139 . 1 1 24 24 THR HG23 H 1 1.147 . . . . . . . . . . . 4220 1 140 . 1 1 25 25 LEU H H 1 7.981 . . . . . . . . . . . 4220 1 141 . 1 1 25 25 LEU HA H 1 3.898 . . . . . . . . . . . 4220 1 142 . 1 1 25 25 LEU HB2 H 1 1.429 . . . . . . . . . . . 4220 1 143 . 1 1 25 25 LEU HD11 H 1 0.696 . . . . . . . . . . . 4220 1 144 . 1 1 25 25 LEU HD12 H 1 0.696 . . . . . . . . . . . 4220 1 145 . 1 1 25 25 LEU HD13 H 1 0.696 . . . . . . . . . . . 4220 1 146 . 1 1 26 26 ARG HE H 1 7.115 . . . . . . . . . . . 4220 1 147 . 1 1 26 26 ARG H H 1 8.048 . . . . . . . . . . . 4220 1 148 . 1 1 26 26 ARG HD2 H 1 3.050 . . . . . . . . . . . 4220 1 149 . 1 1 26 26 ARG HA H 1 3.947 . . . . . . . . . . . 4220 1 150 . 1 1 26 26 ARG HB2 H 1 1.741 . . . . . . . . . . . 4220 1 151 . 1 1 26 26 ARG HG2 H 1 1.529 . . . . . . . . . . . 4220 1 152 . 1 1 26 26 ARG HG3 H 1 1.440 . . . . . . . . . . . 4220 1 153 . 1 1 27 27 ALA H H 1 7.822 . . . . . . . . . . . 4220 1 154 . 1 1 27 27 ALA HA H 1 4.121 . . . . . . . . . . . 4220 1 155 . 1 1 27 27 ALA HB1 H 1 1.481 . . . . . . . . . . . 4220 1 156 . 1 1 27 27 ALA HB2 H 1 1.481 . . . . . . . . . . . 4220 1 157 . 1 1 27 27 ALA HB3 H 1 1.481 . . . . . . . . . . . 4220 1 158 . 1 1 28 28 GLU H H 1 8.046 . . . . . . . . . . . 4220 1 159 . 1 1 28 28 GLU HA H 1 4.145 . . . . . . . . . . . 4220 1 160 . 1 1 28 28 GLU HG3 H 1 2.576 . . . . . . . . . . . 4220 1 161 . 1 1 28 28 GLU HB2 H 1 2.146 . . . . . . . . . . . 4220 1 162 . 1 1 28 28 GLU HG2 H 1 2.461 . . . . . . . . . . . 4220 1 163 . 1 1 29 29 GLN HG2 H 1 2.465 . . . . . . . . . . . 4220 1 164 . 1 1 29 29 GLN HG3 H 1 2.386 . . . . . . . . . . . 4220 1 165 . 1 1 29 29 GLN HB3 H 1 2.140 . . . . . . . . . . . 4220 1 166 . 1 1 29 29 GLN HB2 H 1 2.061 . . . . . . . . . . . 4220 1 167 . 1 1 29 29 GLN HA H 1 4.189 . . . . . . . . . . . 4220 1 168 . 1 1 29 29 GLN H H 1 7.942 . . . . . . . . . . . 4220 1 169 . 1 1 29 29 GLN HE21 H 1 7.226 . . . . . . . . . . . 4220 1 170 . 1 1 29 29 GLN HE22 H 1 6.513 . . . . . . . . . . . 4220 1 171 . 1 1 30 30 ALA H H 1 7.788 . . . . . . . . . . . 4220 1 172 . 1 1 30 30 ALA HA H 1 4.366 . . . . . . . . . . . 4220 1 173 . 1 1 30 30 ALA HB1 H 1 1.437 . . . . . . . . . . . 4220 1 174 . 1 1 30 30 ALA HB2 H 1 1.437 . . . . . . . . . . . 4220 1 175 . 1 1 30 30 ALA HB3 H 1 1.437 . . . . . . . . . . . 4220 1 176 . 1 1 31 31 SER H H 1 7.777 . . . . . . . . . . . 4220 1 177 . 1 1 31 31 SER HA H 1 4.432 . . . . . . . . . . . 4220 1 178 . 1 1 31 31 SER HB2 H 1 3.936 . . . . . . . . . . . 4220 1 stop_ save_