data_6683 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6683 _Entry.Title ; Backbone Resonance Assignments of Human Normal Adult Hemoglobin in the Deoxy Form ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2005-06-10 _Entry.Accession_date 2005-06-13 _Entry.Last_release_date 2007-06-05 _Entry.Original_release_date 2007-06-05 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 Sarata Sahu . C. . 6683 2 Virgil Simplaceanu . . . 6683 3 Nancy Ho . T. . 6683 4 Janel Giovannelli . L. . 6683 5 Chien Ho . . . 6683 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID . . 'Carnegie Mellon University' . 6683 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6683 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 694 6683 '15N chemical shifts' 222 6683 '1H chemical shifts' 222 6683 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 . . 2007-06-05 2005-06-10 original author . 6683 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6683 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16703421 _Citation.Full_citation . _Citation.Title 'Backbone Resonance Assignment of Human Adult Hemoglobin in the Deoxy Form' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 36 _Citation.Journal_issue 'Suppl. 5' _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 1 _Citation.Page_last 1 _Citation.Year 2006 _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 Sarata Sahu . C. . 6683 1 2 Virgil Simplaceanu . . . 6683 1 3 Nancy Ho . T. . 6683 1 4 Janel Giovannelli . L. . 6683 1 5 Chien Ho . . . 6683 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'backbone resonance assignments' 6683 1 deoxy-hemoglobin 6683 1 'protein NMR' 6683 1 'triple resonance experiments' 6683 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 6683 _Assembly.ID 1 _Assembly.Name 'deoxy-Hb A' _Assembly.BMRB_code . _Assembly.Number_of_components 8 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 4 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic yes _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass 64000 _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 'globin subunit alpha one' 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . no native no no 1 . . 6683 1 2 'globin subunit alpha two' 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . no native no no 1 . . 6683 1 3 'globin subunit beta one' 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . no native no no 2 . . 6683 1 4 'globin subunit beta two' 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . no native no no 2 . . 6683 1 5 'heme, 1' 3 $HEM . . no native no no . . . 6683 1 6 'heme, 2' 3 $HEM . . no native no no . . . 6683 1 7 'heme, 3' 3 $HEM . . no native no no . . . 6683 1 8 'heme, 4' 3 $HEM . . no native no no . . . 6683 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form _Entity.Sf_category entity _Entity.Sf_framecode human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form _Entity.Entry_ID 6683 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'deoxy-Hb A alpha' _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 ; VLSPADKTNVKAAWGKVGAH AGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGK KVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKL LSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKY R ; _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 141 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic yes _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 64000 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 1053 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 2 no BMRB 1102 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 3 no BMRB 2006 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 4 no BMRB 2708 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 5 no BMRB 2710 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 6 no BMRB 5856 . beta_subunit . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 7 no BMRB 6230 . bHb . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 8 no BMRB 7125 . globin_subunit_beta . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 9 no BMRB 908 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 10 no PDB 1A00 . "Hemoglobin (Val Beta1 Met, Trp Beta37 Tyr) Mutant" . . . . . 100.00 146 98.63 100.00 1.02e-99 . . . . 6683 1 11 no PDB 1A01 . "Hemoglobin (Val Beta1 Met, Trp Beta37 Ala) Mutant" . . . . . 100.00 146 98.63 99.32 4.99e-99 . . . . 6683 1 12 no PDB 1A0U . "Hemoglobin (Val Beta1 Met) Mutant" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 13 no PDB 1A0Z . "Hemoglobin (Val Beta1 Met) Mutant" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 14 no PDB 1A3N . "Deoxy Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 15 no PDB 1A3O . "Artificial Mutant (Alpha Y42h) Of Deoxy Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 16 no PDB 1ABW . "Deoxy Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 6683 1 17 no PDB 1ABY . "Cyanomet Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 6683 1 18 no PDB 1AJ9 . "R-State Human Carbonmonoxyhemoglobin Alpha-A53s" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 19 no PDB 1B86 . "Human Deoxyhaemoglobin-2,3-Diphosphoglycerate Complex" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 20 no PDB 1BAB . "Hemoglobin Thionville: An Alpha-Chain Variant With A Substitution Of A Glutamate For Valine At Na-1 And Having An Acetylated Me" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 21 no PDB 1BBB . "A Third Quaternary Structure Of Human Hemoglobin A At 1.7-angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 22 no PDB 1BIJ . "Crosslinked, Deoxy Human Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 23 no PDB 1BUW . "Crystal Structure Of S-Nitroso-Nitrosyl Human Hemoglobin A" . . . . . 100.00 146 99.32 99.32 1.91e-99 . . . . 6683 1 24 no PDB 1BZ0 . "Hemoglobin A (Human, Deoxy, High Salt)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 25 no PDB 1BZ1 . "Hemoglobin (Alpha + Met) Variant" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 26 no PDB 1BZZ . "Hemoglobin (Alpha V1m) Mutant" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 27 no PDB 1C7B . "Deoxy Rhb1.0 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 6683 1 28 no PDB 1C7C . "Deoxy Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 6683 1 29 no PDB 1C7D . "Deoxy Rhb1.2 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 6683 1 30 no PDB 1CBL . "The 1.9 Angstrom Structure Of Deoxy-Beta4 Hemoglobin: Analysis Of The Partitioning Of Quaternary-Associated And Ligand-Induced " . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 31 no PDB 1CBM . "The 1.8 Angstrom Structure Of Carbonmonoxy-Beta4 Hemoglobin: Analysis Of A Homotetramer With The R Quaternary Structure Of Liga" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 32 no PDB 1CLS . "Cross-Linked Human Hemoglobin Deoxy" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 33 no PDB 1CMY . "The Mutation Beta99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State Of Human Hemoglobin" . . . . . 100.00 146 99.32 99.32 1.44e-99 . . . . 6683 1 34 no PDB 1COH . "Structure Of Haemoglobin In The Deoxy Quaternary State With Ligand Bound At The Alpha Haems" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 35 no PDB 1DKE . "Ni Beta Heme Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 36 no PDB 1DXT . "High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 37 no PDB 1DXU . "High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 38 no PDB 1DXV . "High-resolution X-ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-globins Having Mutated Amino Termini" . . . . . 99.32 146 100.00 100.00 1.97e-100 . . . . 6683 1 39 no PDB 1FN3 . "Crystal Structure Of Nickel Reconstituted Hemoglobin-A Case For Permanent, T-State Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 40 no PDB 1G9V . "High Resolution Crystal Structure Of Deoxy Hemoglobin Complexed With A Potent Allosteric Effector" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 41 no PDB 1GBU . "Deoxy (Beta-(C93a,C112g)) Human Hemoglobin" . . . . . 100.00 146 98.63 98.63 3.20e-98 . . . . 6683 1 42 no PDB 1GBV . "(Alpha-Oxy, Beta-(C112g)deoxy) T-State Human Hemoglobin" . . . . . 100.00 146 99.32 99.32 2.92e-99 . . . . 6683 1 43 no PDB 1GLI . "Deoxyhemoglobin T38w (alpha Chains), V1g (alpha And Beta Chains)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 44 no PDB 1GZX . "Oxy T State Haemoglobin: Oxygen Bound At All Four Haems" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 45 no PDB 1HAB . "Crosslinked Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 46 no PDB 1HAC . "Crosslinked Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 47 no PDB 1HBA . "High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Bi" . . . . . 100.00 146 99.32 99.32 2.59e-99 . . . . 6683 1 48 no PDB 1HBB . "High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Bi" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 49 no PDB 1HBS . "Refined Crystal Structure Of Deoxyhemoglobin S. I. Restrained Least-Squares Refinement At 3.0-Angstroms Resolution" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 6683 1 50 no PDB 1HCO . "The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 51 no PDB 1HDB . "Analysis Of The Crystal Structure, Molecular Modeling And Infrared Spectroscopy Of The Distal Beta-Heme Pocket Valine67(E11)-Th" . . . . . 100.00 146 99.32 99.32 1.90e-100 . . . . 6683 1 52 no PDB 1HGA . "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-state Haemoglobins: T(alpha-o" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 53 no PDB 1HGB . "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-State Haemoglobins: T(Alpha-O" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 54 no PDB 1HGC . "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-state Haemoglobins: T(alpha-o" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 55 no PDB 1HHO . "Structure Of Human Oxyhaemoglobin At 2.1 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 56 no PDB 1IRD . "Crystal Structure Of Human Carbonmonoxy-Haemoglobin At 1.25 A Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 57 no PDB 1J3Y . "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Hemoglobin; Crystal Structure Of Alpha(Fe)-Beta(N" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 58 no PDB 1J3Z . "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Fe-Co)-Be" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 59 no PDB 1J40 . "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 60 no PDB 1J41 . "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 61 no PDB 1J7S . "Crystal Structure Of Deoxy Hbalphayq, A Mutant Of Hba" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 62 no PDB 1J7W . "Crystal Structure Of Deoxy Hbbetayq, A Site Directed Mutant Of Hba" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 6683 1 63 no PDB 1J7Y . "Crystal Structure Of Partially Ligated Mutant Of Hba" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 6683 1 64 no PDB 1JY7 . "The Structure Of Human Methemoglobin. The Variation Of A Theme" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 65 no PDB 1K0Y . "X-ray Crystallographic Analyses Of Symmetrical Allosteric Effectors Of Hemoglobin. Compounds Designed To Link Primary And Secon" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 66 no PDB 1K1K . "Structure Of Mutant Human Carbonmonoxyhemoglobin C (beta E6k) At 2.0 Angstrom Resolution In Phosphate Buffer." . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 67 no PDB 1KD2 . "Crystal Structure Of Human Deoxyhemoglobin In Absence Of Any Anions" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 68 no PDB 1LFL . "Deoxy Hemoglobin (90% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 69 no PDB 1LFQ . "Oxy Hemoglobin (93% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 70 no PDB 1LFT . "Oxy Hemoglobin (90% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 71 no PDB 1LFV . "Oxy Hemoglobin (88% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 72 no PDB 1LFY . "Oxy Hemoglobin (84% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 73 no PDB 1LFZ . "Oxy Hemoglobin (25% Methanol)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 74 no PDB 1LJW . "Crystal Structure Of Human Carbonmonoxy Hemoglobin At 2.16 A: A Snapshot Of The Allosteric Transition" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 75 no PDB 1M9P . "Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State At Neutral Ph In The Presence Of Polyethylene Glyc" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 76 no PDB 1MKO . "A Fourth Quaternary Structure Of Human Hemoglobin A At 2.18 A Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 77 no PDB 1NEJ . "Crystalline Human Carbonmonoxy Hemoglobin S (liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral Ph In" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 6683 1 78 no PDB 1NIH . "Structure Of Deoxy-Quaternary Haemoglobin With Liganded Beta Subunits" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 79 no PDB 1NQP . "Crystal Structure Of Human Hemoglobin E At 1.73 A Resolution" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 80 no PDB 1O1I . "Cyanomet Hemoglobin (a-gly-c:v1m,l29f,h58q; B,d:v1m,l106w)" . . . . . 100.00 146 98.63 99.32 2.35e-99 . . . . 6683 1 81 no PDB 1O1J . "Deoxy Hemoglobin (a-gly-c:v1m,l29f,h58q; B,d:v1m,l106w)" . . . . . 100.00 146 98.63 99.32 2.35e-99 . . . . 6683 1 82 no PDB 1O1K . "Deoxy Hemoglobin (A,C:v1m; B,D:v1m,V67w)" . . . . . 100.00 146 98.63 99.32 2.89e-99 . . . . 6683 1 83 no PDB 1O1L . "Deoxy Hemoglobin (A-Gly-C:v1m,L29w,H58q; B,D:v1m)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 84 no PDB 1O1M . "Deoxy Hemoglobin (a-glyglygly-c:v1m,l29f,h58q B,d:v1m,v67w)" . . . . . 100.00 146 98.63 99.32 2.89e-99 . . . . 6683 1 85 no PDB 1O1N . "Deoxy Hemoglobin (A-Glyglygly-C:v1m,L29w; B,D:v1m)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 86 no PDB 1O1O . "Deoxy Hemoglobin (A,C:v1m,V62l; B,D:v1m,V67l)" . . . . . 100.00 146 98.63 100.00 4.13e-100 . . . . 6683 1 87 no PDB 1O1P . "Deoxy Hemoglobin (A-Gly-C:v1m; B,D:v1m,C93a,N108k)" . . . . . 100.00 146 97.95 98.63 2.00e-98 . . . . 6683 1 88 no PDB 1QI8 . "Deoxygenated Structure Of A Distal Pocket Hemoglobin Mutant" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 6683 1 89 no PDB 1QSH . "Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongl" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 90 no PDB 1QSI . "Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongl" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 91 no PDB 1QXD . "Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 92 no PDB 1QXE . "Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 93 no PDB 1R1X . "Crystal Structure Of Oxy-Human Hemoglobin Bassett At 2.15 Angstrom" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 94 no PDB 1R1Y . "Crystal Structure Of Deoxy-Human Hemoglobin Bassett At 1.8 Angstrom" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 95 no PDB 1RPS . "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Hemoglobin Exposed To No Under" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 96 no PDB 1RQ3 . "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 97 no PDB 1RQ4 . "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin, Hemoglobin Exposed To No Under" . . . . . 100.00 146 99.32 99.32 1.91e-99 . . . . 6683 1 98 no PDB 1RQA . "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Beta W73e Hemoglobin Exposed T" . . . . . 100.00 146 98.63 99.32 7.31e-99 . . . . 6683 1 99 no PDB 1RVW . "R State Human Hemoglobin [alpha V96w], Carbonmonoxy" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 100 no PDB 1SDK . "Cross-linked, Carbonmonoxy Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 101 no PDB 1SDL . "Cross-Linked, Carbonmonoxy Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 102 no PDB 1THB . "Refinement Of A Partially Oxygenated T State Haemoglobin At 1.5 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 103 no PDB 1UIW . "Crystal Structures Of Unliganded And Half-Liganded Human Hemoglobin Derivatives Cross-Linked Between Lys 82beta1 And Lys 82beta" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 104 no PDB 1VWT . "T State Human Hemoglobin [alpha V96w], Alpha Aquomet, Beta Deoxy" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 105 no PDB 1XXT . "The T-To-T High Transitions In Human Hemoglobin: Wild-Type Deoxy Hb A (Low Salt, One Test Set)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 106 no PDB 1XY0 . "T-To-Thigh Transitions In Human Hemoglobin: Alphak40g Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 107 no PDB 1XYE . "T-to-thigh Transitions In Human Hemoglobin: Alpha Y42a Deoxy Low Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 108 no PDB 1XZ2 . "Wild-Type Hemoglobin Deoxy No-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 109 no PDB 1XZ4 . "Intersubunit Interactions Associated With Tyr42alpha Stabilize The Quaternary-T Tetramer But Are Not Major Quaternary Constrain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 110 no PDB 1XZ5 . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphal91a Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 111 no PDB 1XZ7 . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphar92a Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 112 no PDB 1XZU . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphad94g Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 113 no PDB 1XZV . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphap95a Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 114 no PDB 1Y09 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphan97a Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 115 no PDB 1Y0A . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140a Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 116 no PDB 1Y0C . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140f Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 117 no PDB 1Y0D . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Desarg141alpha Deoxy Low-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 118 no PDB 1Y0T . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 119 no PDB 1Y0W . "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 120 no PDB 1Y22 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 4.87e-100 . . . . 6683 1 121 no PDB 1Y2Z . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav34g Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.85e-99 . . . . 6683 1 122 no PDB 1Y31 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 2.40e-99 . . . . 6683 1 123 no PDB 1Y35 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 100.00 7.46e-100 . . . . 6683 1 124 no PDB 1Y45 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 1.66e-99 . . . . 6683 1 125 no PDB 1Y46 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 100.00 1.02e-99 . . . . 6683 1 126 no PDB 1Y4B . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 1.04e-98 . . . . 6683 1 127 no PDB 1Y4F . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 4.99e-99 . . . . 6683 1 128 no PDB 1Y4G . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 9.40e-99 . . . . 6683 1 129 no PDB 1Y4P . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Deoxy Low-Salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 7.31e-99 . . . . 6683 1 130 no PDB 1Y4Q . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf42a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.81e-99 . . . . 6683 1 131 no PDB 1Y4R . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf45a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.81e-99 . . . . 6683 1 132 no PDB 1Y4V . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betac93a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 2.53e-99 . . . . 6683 1 133 no PDB 1Y5F . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betal96a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 7.96e-100 . . . . 6683 1 134 no PDB 1Y5J . "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betah97a Deoxy Low-salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.95e-99 . . . . 6683 1 135 no PDB 1Y5K . "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betad99a Deoxy Low-salt (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 1.75e-99 . . . . 6683 1 136 no PDB 1Y7C . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.66e-99 . . . . 6683 1 137 no PDB 1Y7D . "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betap100g Deoxy Low-salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 2.86e-99 . . . . 6683 1 138 no PDB 1Y7G . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan102a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.87e-99 . . . . 6683 1 139 no PDB 1Y7Z . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan108a Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.87e-99 . . . . 6683 1 140 no PDB 1Y83 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay145g Deoxy Low-Salt (1 Test Set)" . . . . . 100.00 146 98.63 99.32 4.72e-99 . . . . 6683 1 141 no PDB 1Y85 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Deshis146beta Deoxy Low-Salt" . . . . . 99.32 145 100.00 100.00 4.66e-100 . . . . 6683 1 142 no PDB 1Y8W . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphar92a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 143 no PDB 1YDZ . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphay140f Oxy (2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 144 no PDB 1YE0 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 99.32 4.87e-100 . . . . 6683 1 145 no PDB 1YE1 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 99.32 2.40e-99 . . . . 6683 1 146 no PDB 1YE2 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Oxy (2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 100.00 7.46e-100 . . . . 6683 1 147 no PDB 1YEN . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 1.66e-99 . . . . 6683 1 148 no PDB 1YEO . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 4.99e-99 . . . . 6683 1 149 no PDB 1YEQ . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Oxy (10 Test Sets)" . . . . . 100.00 146 98.63 100.00 1.02e-99 . . . . 6683 1 150 no PDB 1YEU . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Oxy (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 9.40e-99 . . . . 6683 1 151 no PDB 1YEV . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Oxy (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 7.31e-99 . . . . 6683 1 152 no PDB 1YFF . "Structure Of Human Carbonmonoxyhemoglobin C (beta E6k): Two Quaternary States (r2 And R3) In One Crystal" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 153 no PDB 1YG5 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 1.04e-98 . . . . 6683 1 154 no PDB 1YGD . "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betaw37e Alpha Zinc Beta Oxy (10 Test Sets)" . . . . . 100.00 146 98.63 99.32 7.31e-99 . . . . 6683 1 155 no PDB 1YGF . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betah97a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.95e-99 . . . . 6683 1 156 no PDB 1YH9 . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 157 no PDB 1YHE . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (5.0mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 158 no PDB 1YHR . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (10.0mm Ihp, 20% Peg) (10 Test Sets)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 159 no PDB 1YIE . "T-to-thigh Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (2.2mm Ihp, 13% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 99.32 4.99e-99 . . . . 6683 1 160 no PDB 1YIH . "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Oxy (2.2mm Ihp, 20% Peg) (1 Test Set)" . . . . . 100.00 146 98.63 99.32 1.66e-99 . . . . 6683 1 161 no PDB 1YVQ . "The Low Salt (Peg) Crystal Structure Of Co Hemoglobin E (Betae26k) Approaching Physiological Ph (Ph 7.5)" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 162 no PDB 1YVT . "The High Salt (Phosphate) Crystal Structure Of Co Hemoglobin E (Glu26lys) At Physiological Ph (Ph 7.35)" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 163 no PDB 1YZI . "A Novel Quaternary Structure Of Human Carbonmonoxy Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 164 no PDB 2D5Z . "Crystal Structure Of T-State Human Hemoglobin Complexed With Three L35 Molecules" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 165 no PDB 2D60 . "Crystal Structure Of Deoxy Human Hemoglobin Complexed With Two L35 Molecules" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 166 no PDB 2DN1 . "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Oxy Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 167 no PDB 2DN2 . "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Deoxy Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 168 no PDB 2DN3 . "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Carbonmonoxy Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 169 no PDB 2DXM . "Neutron Structure Analysis Of Deoxy Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 170 no PDB 2H35 . "Solution Structure Of Human Normal Adult Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 171 no PDB 2HBC . "High Resolution X-ray Structures Of Myoglobin-and Hemoglobin-alkyl Isocyanide Complexes" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 172 no PDB 2HBD . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 173 no PDB 2HBE . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 174 no PDB 2HBF . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 175 no PDB 2HBS . "The High Resolution Crystal Structure Of Deoxyhemoglobin S" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 6683 1 176 no PDB 2HCO . "The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 177 no PDB 2HHB . "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 178 no PDB 2HHD . "Oxygen Affinity Modulation By The N-Termini Of The Beta- Chains In Human And Bovine Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 179 no PDB 2HHE . "Oxygen Affinity Modulation By The N-Termini Of The Beta Chains In Human And Bovine Hemoglobin" . . . . . 98.63 145 100.00 100.00 1.48e-99 . . . . 6683 1 180 no PDB 2M6Z . "Refined Solution Structure Of Human Adult Hemoglobin In The Carbonmonoxy Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 181 no PDB 2W6V . "Structure Of Human Deoxy Hemoglobin A In Complex With Xenon" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 182 no PDB 2W72 . "Deoxygenated Structure Of A Distal Site Hemoglobin Mutant Plus Xe" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 6683 1 183 no PDB 2YRS . "Human Hemoglobin D Los Angeles: Crystal Structure" . . . . . 100.00 146 99.32 100.00 1.61e-100 . . . . 6683 1 184 no PDB 3B75 . "Crystal Structure Of Glycated Human Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 185 no PDB 3D17 . "A Triply Ligated Crystal Structure Of Relaxed State Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 186 no PDB 3D7O . "Human Hemoglobin, Nitrogen Dioxide Anion Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 187 no PDB 3DUT . "The High Salt (Phosphate) Crystal Structure Of Deoxy Hemoglobin E (Glu26lys) At Physiological Ph (Ph 7.35)" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 188 no PDB 3HHB . "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 189 no PDB 3HXN . "The Structure Of Human Carbonmonoxyhemoglobin Complex To Ihp At 2.0 Angstrons Resolution." . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 190 no PDB 3IC0 . "Crystal Structure Of Liganded Hemoglobin In Complex With A Potent Antisickling Agent, Inn-298" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 191 no PDB 3IC2 . "Crystal Structure Of Liganded Hemoglobin In Complex With A Potent Antisickling Agent, Inn-266" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 192 no PDB 3KMF . "Room Temperature Time-Of-Flight Neutron Diffraction Study Of Deoxy Human Normal Adult Hemoglobin" . . . . . 99.32 146 100.00 100.00 3.55e-100 . . . . 6683 1 193 no PDB 3NL7 . "Human Hemoglobin A Mutant Beta H63w Carbonmonoxy-Form" . . . . . 100.00 146 99.32 99.32 2.27e-99 . . . . 6683 1 194 no PDB 3NMM . "Human Hemoglobin A Mutant Alpha H58w Deoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 195 no PDB 3ODQ . "Structure Of A Crystal Form Of Human Methemoglobin Indicative Of Fiber Formation" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 196 no PDB 3ONZ . "Human Tetrameric Hemoglobin: Proximal Nitrite Ligand At Beta" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 197 no PDB 3OO4 . "R-State Human Hemoglobin: Nitriheme Modified At Alpha" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 198 no PDB 3OO5 . "R-State Human Hemoglobin: Nitriheme Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 199 no PDB 3P5Q . "Ferric R-State Human Aquomethemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 200 no PDB 3QJB . "Human Hemoglobin A Mutant Alpha H58l Carbonmonoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 201 no PDB 3QJC . "Human Hemoglobin A Mutant Beta H63l Carbonmonoxy-Form" . . . . . 100.00 146 99.32 99.32 1.53e-99 . . . . 6683 1 202 no PDB 3QJD . "Human Hemoglobin A Mutant Alpha H58l Deoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 203 no PDB 3QJE . "Human Hemoglobin A Mutant Beta H63l Deoxy-Form" . . . . . 100.00 146 99.32 99.32 1.53e-99 . . . . 6683 1 204 no PDB 3R5I . "Crystal Structure Of Liganded Hemoglobin Complexed With A Potent Antisickling Agent, Inn-312" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 205 no PDB 3S65 . "Structures And Oxygen Affinities Of Crystalline Human Hemoglobin C (Beta6 Lys) In The R2 Quaternary Structures" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 206 no PDB 3S66 . "Structures And Oxygen Affinities Of Crystalline Human Hemoglobin C (Beta6 Lys) In The R Quaternary Structures" . . . . . 100.00 146 99.32 100.00 3.04e-100 . . . . 6683 1 207 no PDB 3SZK . "Crystal Structure Of Human Methaemoglobin Complexed With The First Neat Domain Of Isdh From Staphylococcus Aureus" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 208 no PDB 3W4U . "Human Zeta-2 Beta-2-s Hemoglobin" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 6683 1 209 no PDB 3WCP . "Deoxyhemoglobin Sh-drug Complex" . . . . . 100.00 146 99.32 99.32 1.91e-99 . . . . 6683 1 210 no PDB 3WHM . "Structure Of Hemoglobin Complex With 18-crown-6" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 211 no PDB 4FC3 . "Crystal Structure Of Human Methaemoglobin Complexed With The Second Neat Domain Of Isdh From Staphylococcus Aureus" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 212 no PDB 4HHB . "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 213 no PDB 4IJ2 . "Human Methemoglobin In Complex With The Second And Third Neat Domains Of Isdh From Staphylococcus Aureus" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 214 no PDB 4L7Y . "Deoxygenated Hb In Complex With The Allosteric Effectors, Irl2500 And 2,3-dpg" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 215 no PDB 4M4A . "Human Hemoglobin Nitromethane Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 216 no PDB 4M4B . "Human Hemoglobin Nitroethane Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 217 no PDB 4MQC . "Carbonmonoxy Structure Of Hemoglobin Evans Alphav62mbetawt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 218 no PDB 4MQG . "Structure Of Carbonmonoxy Adult Hemoglobin Bristol-alesha Alphawtbetav67m" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 219 no PDB 4MQH . "Structure Of Aquomet Hemoglobin Evans Alphav62mbetawt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 220 no PDB 4MQI . "Structure Of Aquomet Hemoglobin Bristol-alesha Alphawtbetav67m" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 6683 1 221 no PDB 4N7N . "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Full-liganded Human Haemoglobin " . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 222 no PDB 4N7O . "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Half-liganded Human Haemoglobin " . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 223 no PDB 4N7P . "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Half-liganded Human Haemoglobin " . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 224 no PDB 4N8T . "Human Hemoglobin Nitric Oxide Adduct" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 225 no PDB 4NI0 . "Quaternary R3 Co-liganded Hemoglobin Structure In Complex With A Thiol Containing Compound" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 226 no PDB 4NI1 . "Qauternary R Co-liganded Hemoglobin Structure In Complex With A Thiol Containing Compound" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 227 no PDB 4WJG . "Structure Of T. Brucei Haptoglobin-hemoglobin Receptor Binding To Human Haptoglobin-hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 228 no PDB 6HBW . "Crystal Structure Of Deoxy-human Hemoglobin Beta6 Glu->trp" . . . . . 100.00 146 99.32 99.32 1.73e-99 . . . . 6683 1 229 no DBJ BAG34767 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 230 no EMBL CAA23756 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 231 no EMBL CAA23758 . "beta globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 232 no EMBL CAA23759 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 98.63 98.63 5.05e-99 . . . . 6683 1 233 no EMBL CAA43421 . "beta-globin [Gorilla gorilla]" . . . . . 82.19 121 99.17 100.00 4.37e-80 . . . . 6683 1 234 no EMBL CAG38767 . "HBB [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 235 no GB AAA16334 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 236 no GB AAA21100 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 237 no GB AAA21101 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 238 no GB AAA21102 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 239 no GB AAA21103 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 240 no PRF 0404170B . "hemoglobin beta" . . . . . 100.00 146 98.63 98.63 5.69e-99 . . . . 6683 1 241 no PRF 0907233B . "hemoglobin beta" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 6683 1 242 no REF NP_000509 . "hemoglobin subunit beta [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 243 no REF XP_002822173 . "PREDICTED: hemoglobin subunit beta isoform X2 [Pongo abelii]" . . . . . 100.00 147 98.63 98.63 5.39e-99 . . . . 6683 1 244 no REF XP_003819077 . "PREDICTED: hemoglobin subunit beta [Pan paniscus]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 245 no REF XP_004050595 . "PREDICTED: hemoglobin subunit beta [Gorilla gorilla gorilla]" . . . . . 95.21 143 99.28 100.00 4.51e-95 . . . . 6683 1 246 no REF XP_004090697 . "PREDICTED: LOW QUALITY PROTEIN: hemoglobin subunit beta [Nomascus leucogenys]" . . . . . 100.00 147 97.95 97.95 2.96e-98 . . . . 6683 1 247 no SP P02024 . "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Gorilla gorilla gorilla]" . . . . . 100.00 147 99.32 100.00 2.34e-100 . . . . 6683 1 248 no SP P02025 . "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Hylobates lar]" . . . . . 100.00 146 98.63 98.63 4.99e-99 . . . . 6683 1 249 no SP P02032 . "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Semnopithecus entellus]" . . . . . 100.00 146 97.26 98.63 4.58e-98 . . . . 6683 1 250 no SP P68871 . "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain; Contains: RecName: Full=" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 251 no SP P68872 . "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Pan paniscus]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 6683 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'oxygen transport' 6683 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'deoxy-Hb A' . 6683 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 . VAL . 6683 1 2 . LEU . 6683 1 3 . SER . 6683 1 4 . PRO . 6683 1 5 . ALA . 6683 1 6 . ASP . 6683 1 7 . LYS . 6683 1 8 . THR . 6683 1 9 . ASN . 6683 1 10 . VAL . 6683 1 11 . LYS . 6683 1 12 . ALA . 6683 1 13 . ALA . 6683 1 14 . TRP . 6683 1 15 . GLY . 6683 1 16 . LYS . 6683 1 17 . VAL . 6683 1 18 . GLY . 6683 1 19 . ALA . 6683 1 20 . HIS . 6683 1 21 . ALA . 6683 1 22 . GLY . 6683 1 23 . GLU . 6683 1 24 . TYR . 6683 1 25 . GLY . 6683 1 26 . ALA . 6683 1 27 . GLU . 6683 1 28 . ALA . 6683 1 29 . LEU . 6683 1 30 . GLU . 6683 1 31 . ARG . 6683 1 32 . MET . 6683 1 33 . PHE . 6683 1 34 . LEU . 6683 1 35 . SER . 6683 1 36 . PHE . 6683 1 37 . PRO . 6683 1 38 . THR . 6683 1 39 . THR . 6683 1 40 . LYS . 6683 1 41 . THR . 6683 1 42 . TYR . 6683 1 43 . PHE . 6683 1 44 . PRO . 6683 1 45 . HIS . 6683 1 46 . PHE . 6683 1 47 . ASP . 6683 1 48 . LEU . 6683 1 49 . SER . 6683 1 50 . HIS . 6683 1 51 . GLY . 6683 1 52 . SER . 6683 1 53 . ALA . 6683 1 54 . GLN . 6683 1 55 . VAL . 6683 1 56 . LYS . 6683 1 57 . GLY . 6683 1 58 . HIS . 6683 1 59 . GLY . 6683 1 60 . LYS . 6683 1 61 . LYS . 6683 1 62 . VAL . 6683 1 63 . ALA . 6683 1 64 . ASP . 6683 1 65 . ALA . 6683 1 66 . LEU . 6683 1 67 . THR . 6683 1 68 . ASN . 6683 1 69 . ALA . 6683 1 70 . VAL . 6683 1 71 . ALA . 6683 1 72 . HIS . 6683 1 73 . VAL . 6683 1 74 . ASP . 6683 1 75 . ASP . 6683 1 76 . MET . 6683 1 77 . PRO . 6683 1 78 . ASN . 6683 1 79 . ALA . 6683 1 80 . LEU . 6683 1 81 . SER . 6683 1 82 . ALA . 6683 1 83 . LEU . 6683 1 84 . SER . 6683 1 85 . ASP . 6683 1 86 . LEU . 6683 1 87 . HIS . 6683 1 88 . ALA . 6683 1 89 . HIS . 6683 1 90 . LYS . 6683 1 91 . LEU . 6683 1 92 . ARG . 6683 1 93 . VAL . 6683 1 94 . ASP . 6683 1 95 . PRO . 6683 1 96 . VAL . 6683 1 97 . ASN . 6683 1 98 . PHE . 6683 1 99 . LYS . 6683 1 100 . LEU . 6683 1 101 . LEU . 6683 1 102 . SER . 6683 1 103 . HIS . 6683 1 104 . CYS . 6683 1 105 . LEU . 6683 1 106 . LEU . 6683 1 107 . VAL . 6683 1 108 . THR . 6683 1 109 . LEU . 6683 1 110 . ALA . 6683 1 111 . ALA . 6683 1 112 . HIS . 6683 1 113 . LEU . 6683 1 114 . PRO . 6683 1 115 . ALA . 6683 1 116 . GLU . 6683 1 117 . PHE . 6683 1 118 . THR . 6683 1 119 . PRO . 6683 1 120 . ALA . 6683 1 121 . VAL . 6683 1 122 . HIS . 6683 1 123 . ALA . 6683 1 124 . SER . 6683 1 125 . LEU . 6683 1 126 . ASP . 6683 1 127 . LYS . 6683 1 128 . PHE . 6683 1 129 . LEU . 6683 1 130 . ALA . 6683 1 131 . SER . 6683 1 132 . VAL . 6683 1 133 . SER . 6683 1 134 . THR . 6683 1 135 . VAL . 6683 1 136 . LEU . 6683 1 137 . THR . 6683 1 138 . SER . 6683 1 139 . LYS . 6683 1 140 . TYR . 6683 1 141 . ARG . 6683 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 . VAL 1 1 6683 1 . LEU 2 2 6683 1 . SER 3 3 6683 1 . PRO 4 4 6683 1 . ALA 5 5 6683 1 . ASP 6 6 6683 1 . LYS 7 7 6683 1 . THR 8 8 6683 1 . ASN 9 9 6683 1 . VAL 10 10 6683 1 . LYS 11 11 6683 1 . ALA 12 12 6683 1 . ALA 13 13 6683 1 . TRP 14 14 6683 1 . GLY 15 15 6683 1 . LYS 16 16 6683 1 . VAL 17 17 6683 1 . GLY 18 18 6683 1 . ALA 19 19 6683 1 . HIS 20 20 6683 1 . ALA 21 21 6683 1 . GLY 22 22 6683 1 . GLU 23 23 6683 1 . TYR 24 24 6683 1 . GLY 25 25 6683 1 . ALA 26 26 6683 1 . GLU 27 27 6683 1 . ALA 28 28 6683 1 . LEU 29 29 6683 1 . GLU 30 30 6683 1 . ARG 31 31 6683 1 . MET 32 32 6683 1 . PHE 33 33 6683 1 . LEU 34 34 6683 1 . SER 35 35 6683 1 . PHE 36 36 6683 1 . PRO 37 37 6683 1 . THR 38 38 6683 1 . THR 39 39 6683 1 . LYS 40 40 6683 1 . THR 41 41 6683 1 . TYR 42 42 6683 1 . PHE 43 43 6683 1 . PRO 44 44 6683 1 . HIS 45 45 6683 1 . PHE 46 46 6683 1 . ASP 47 47 6683 1 . LEU 48 48 6683 1 . SER 49 49 6683 1 . HIS 50 50 6683 1 . GLY 51 51 6683 1 . SER 52 52 6683 1 . ALA 53 53 6683 1 . GLN 54 54 6683 1 . VAL 55 55 6683 1 . LYS 56 56 6683 1 . GLY 57 57 6683 1 . HIS 58 58 6683 1 . GLY 59 59 6683 1 . LYS 60 60 6683 1 . LYS 61 61 6683 1 . VAL 62 62 6683 1 . ALA 63 63 6683 1 . ASP 64 64 6683 1 . ALA 65 65 6683 1 . LEU 66 66 6683 1 . THR 67 67 6683 1 . ASN 68 68 6683 1 . ALA 69 69 6683 1 . VAL 70 70 6683 1 . ALA 71 71 6683 1 . HIS 72 72 6683 1 . VAL 73 73 6683 1 . ASP 74 74 6683 1 . ASP 75 75 6683 1 . MET 76 76 6683 1 . PRO 77 77 6683 1 . ASN 78 78 6683 1 . ALA 79 79 6683 1 . LEU 80 80 6683 1 . SER 81 81 6683 1 . ALA 82 82 6683 1 . LEU 83 83 6683 1 . SER 84 84 6683 1 . ASP 85 85 6683 1 . LEU 86 86 6683 1 . HIS 87 87 6683 1 . ALA 88 88 6683 1 . HIS 89 89 6683 1 . LYS 90 90 6683 1 . LEU 91 91 6683 1 . ARG 92 92 6683 1 . VAL 93 93 6683 1 . ASP 94 94 6683 1 . PRO 95 95 6683 1 . VAL 96 96 6683 1 . ASN 97 97 6683 1 . PHE 98 98 6683 1 . LYS 99 99 6683 1 . LEU 100 100 6683 1 . LEU 101 101 6683 1 . SER 102 102 6683 1 . HIS 103 103 6683 1 . CYS 104 104 6683 1 . LEU 105 105 6683 1 . LEU 106 106 6683 1 . VAL 107 107 6683 1 . THR 108 108 6683 1 . LEU 109 109 6683 1 . ALA 110 110 6683 1 . ALA 111 111 6683 1 . HIS 112 112 6683 1 . LEU 113 113 6683 1 . PRO 114 114 6683 1 . ALA 115 115 6683 1 . GLU 116 116 6683 1 . PHE 117 117 6683 1 . THR 118 118 6683 1 . PRO 119 119 6683 1 . ALA 120 120 6683 1 . VAL 121 121 6683 1 . HIS 122 122 6683 1 . ALA 123 123 6683 1 . SER 124 124 6683 1 . LEU 125 125 6683 1 . ASP 126 126 6683 1 . LYS 127 127 6683 1 . PHE 128 128 6683 1 . LEU 129 129 6683 1 . ALA 130 130 6683 1 . SER 131 131 6683 1 . VAL 132 132 6683 1 . SER 133 133 6683 1 . THR 134 134 6683 1 . VAL 135 135 6683 1 . LEU 136 136 6683 1 . THR 137 137 6683 1 . SER 138 138 6683 1 . LYS 139 139 6683 1 . TYR 140 140 6683 1 . ARG 141 141 6683 1 stop_ save_ save_human_normal_adult_hemoglobin_beta_chain_in_deoxy_form _Entity.Sf_category entity _Entity.Sf_framecode human_normal_adult_hemoglobin_beta_chain_in_deoxy_form _Entity.Entry_ID 6683 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'deoxy-Hb A beta' _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 ; VHLTPEEKSAVTALWGKVNV DEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKV KAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDP ENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANA LAHKYH ; _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 146 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic yes _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 64000 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'oxygen transport' 6683 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'deoxy-Hb A' . 6683 2 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 . VAL . 6683 2 2 . HIS . 6683 2 3 . LEU . 6683 2 4 . THR . 6683 2 5 . PRO . 6683 2 6 . GLU . 6683 2 7 . GLU . 6683 2 8 . LYS . 6683 2 9 . SER . 6683 2 10 . ALA . 6683 2 11 . VAL . 6683 2 12 . THR . 6683 2 13 . ALA . 6683 2 14 . LEU . 6683 2 15 . TRP . 6683 2 16 . GLY . 6683 2 17 . LYS . 6683 2 18 . VAL . 6683 2 19 . ASN . 6683 2 20 . VAL . 6683 2 21 . ASP . 6683 2 22 . GLU . 6683 2 23 . VAL . 6683 2 24 . GLY . 6683 2 25 . GLY . 6683 2 26 . GLU . 6683 2 27 . ALA . 6683 2 28 . LEU . 6683 2 29 . GLY . 6683 2 30 . ARG . 6683 2 31 . LEU . 6683 2 32 . LEU . 6683 2 33 . VAL . 6683 2 34 . VAL . 6683 2 35 . TYR . 6683 2 36 . PRO . 6683 2 37 . TRP . 6683 2 38 . THR . 6683 2 39 . GLN . 6683 2 40 . ARG . 6683 2 41 . PHE . 6683 2 42 . PHE . 6683 2 43 . GLU . 6683 2 44 . SER . 6683 2 45 . PHE . 6683 2 46 . GLY . 6683 2 47 . ASP . 6683 2 48 . LEU . 6683 2 49 . SER . 6683 2 50 . THR . 6683 2 51 . PRO . 6683 2 52 . ASP . 6683 2 53 . ALA . 6683 2 54 . VAL . 6683 2 55 . MET . 6683 2 56 . GLY . 6683 2 57 . ASN . 6683 2 58 . PRO . 6683 2 59 . LYS . 6683 2 60 . VAL . 6683 2 61 . LYS . 6683 2 62 . ALA . 6683 2 63 . HIS . 6683 2 64 . GLY . 6683 2 65 . LYS . 6683 2 66 . LYS . 6683 2 67 . VAL . 6683 2 68 . LEU . 6683 2 69 . GLY . 6683 2 70 . ALA . 6683 2 71 . PHE . 6683 2 72 . SER . 6683 2 73 . ASP . 6683 2 74 . GLY . 6683 2 75 . LEU . 6683 2 76 . ALA . 6683 2 77 . HIS . 6683 2 78 . LEU . 6683 2 79 . ASP . 6683 2 80 . ASN . 6683 2 81 . LEU . 6683 2 82 . LYS . 6683 2 83 . GLY . 6683 2 84 . THR . 6683 2 85 . PHE . 6683 2 86 . ALA . 6683 2 87 . THR . 6683 2 88 . LEU . 6683 2 89 . SER . 6683 2 90 . GLU . 6683 2 91 . LEU . 6683 2 92 . HIS . 6683 2 93 . CYS . 6683 2 94 . ASP . 6683 2 95 . LYS . 6683 2 96 . LEU . 6683 2 97 . HIS . 6683 2 98 . VAL . 6683 2 99 . ASP . 6683 2 100 . PRO . 6683 2 101 . GLU . 6683 2 102 . ASN . 6683 2 103 . PHE . 6683 2 104 . ARG . 6683 2 105 . LEU . 6683 2 106 . LEU . 6683 2 107 . GLY . 6683 2 108 . ASN . 6683 2 109 . VAL . 6683 2 110 . LEU . 6683 2 111 . VAL . 6683 2 112 . CYS . 6683 2 113 . VAL . 6683 2 114 . LEU . 6683 2 115 . ALA . 6683 2 116 . HIS . 6683 2 117 . HIS . 6683 2 118 . PHE . 6683 2 119 . GLY . 6683 2 120 . LYS . 6683 2 121 . GLU . 6683 2 122 . PHE . 6683 2 123 . THR . 6683 2 124 . PRO . 6683 2 125 . PRO . 6683 2 126 . VAL . 6683 2 127 . GLN . 6683 2 128 . ALA . 6683 2 129 . ALA . 6683 2 130 . TYR . 6683 2 131 . GLN . 6683 2 132 . LYS . 6683 2 133 . VAL . 6683 2 134 . VAL . 6683 2 135 . ALA . 6683 2 136 . GLY . 6683 2 137 . VAL . 6683 2 138 . ALA . 6683 2 139 . ASN . 6683 2 140 . ALA . 6683 2 141 . LEU . 6683 2 142 . ALA . 6683 2 143 . HIS . 6683 2 144 . LYS . 6683 2 145 . TYR . 6683 2 146 . HIS . 6683 2 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 . VAL 1 1 6683 2 . HIS 2 2 6683 2 . LEU 3 3 6683 2 . THR 4 4 6683 2 . PRO 5 5 6683 2 . GLU 6 6 6683 2 . GLU 7 7 6683 2 . LYS 8 8 6683 2 . SER 9 9 6683 2 . ALA 10 10 6683 2 . VAL 11 11 6683 2 . THR 12 12 6683 2 . ALA 13 13 6683 2 . LEU 14 14 6683 2 . TRP 15 15 6683 2 . GLY 16 16 6683 2 . LYS 17 17 6683 2 . VAL 18 18 6683 2 . ASN 19 19 6683 2 . VAL 20 20 6683 2 . ASP 21 21 6683 2 . GLU 22 22 6683 2 . VAL 23 23 6683 2 . GLY 24 24 6683 2 . GLY 25 25 6683 2 . GLU 26 26 6683 2 . ALA 27 27 6683 2 . LEU 28 28 6683 2 . GLY 29 29 6683 2 . ARG 30 30 6683 2 . LEU 31 31 6683 2 . LEU 32 32 6683 2 . VAL 33 33 6683 2 . VAL 34 34 6683 2 . TYR 35 35 6683 2 . PRO 36 36 6683 2 . TRP 37 37 6683 2 . THR 38 38 6683 2 . GLN 39 39 6683 2 . ARG 40 40 6683 2 . PHE 41 41 6683 2 . PHE 42 42 6683 2 . GLU 43 43 6683 2 . SER 44 44 6683 2 . PHE 45 45 6683 2 . GLY 46 46 6683 2 . ASP 47 47 6683 2 . LEU 48 48 6683 2 . SER 49 49 6683 2 . THR 50 50 6683 2 . PRO 51 51 6683 2 . ASP 52 52 6683 2 . ALA 53 53 6683 2 . VAL 54 54 6683 2 . MET 55 55 6683 2 . GLY 56 56 6683 2 . ASN 57 57 6683 2 . PRO 58 58 6683 2 . LYS 59 59 6683 2 . VAL 60 60 6683 2 . LYS 61 61 6683 2 . ALA 62 62 6683 2 . HIS 63 63 6683 2 . GLY 64 64 6683 2 . LYS 65 65 6683 2 . LYS 66 66 6683 2 . VAL 67 67 6683 2 . LEU 68 68 6683 2 . GLY 69 69 6683 2 . ALA 70 70 6683 2 . PHE 71 71 6683 2 . SER 72 72 6683 2 . ASP 73 73 6683 2 . GLY 74 74 6683 2 . LEU 75 75 6683 2 . ALA 76 76 6683 2 . HIS 77 77 6683 2 . LEU 78 78 6683 2 . ASP 79 79 6683 2 . ASN 80 80 6683 2 . LEU 81 81 6683 2 . LYS 82 82 6683 2 . GLY 83 83 6683 2 . THR 84 84 6683 2 . PHE 85 85 6683 2 . ALA 86 86 6683 2 . THR 87 87 6683 2 . LEU 88 88 6683 2 . SER 89 89 6683 2 . GLU 90 90 6683 2 . LEU 91 91 6683 2 . HIS 92 92 6683 2 . CYS 93 93 6683 2 . ASP 94 94 6683 2 . LYS 95 95 6683 2 . LEU 96 96 6683 2 . HIS 97 97 6683 2 . VAL 98 98 6683 2 . ASP 99 99 6683 2 . PRO 100 100 6683 2 . GLU 101 101 6683 2 . ASN 102 102 6683 2 . PHE 103 103 6683 2 . ARG 104 104 6683 2 . LEU 105 105 6683 2 . LEU 106 106 6683 2 . GLY 107 107 6683 2 . ASN 108 108 6683 2 . VAL 109 109 6683 2 . LEU 110 110 6683 2 . VAL 111 111 6683 2 . CYS 112 112 6683 2 . VAL 113 113 6683 2 . LEU 114 114 6683 2 . ALA 115 115 6683 2 . HIS 116 116 6683 2 . HIS 117 117 6683 2 . PHE 118 118 6683 2 . GLY 119 119 6683 2 . LYS 120 120 6683 2 . GLU 121 121 6683 2 . PHE 122 122 6683 2 . THR 123 123 6683 2 . PRO 124 124 6683 2 . PRO 125 125 6683 2 . VAL 126 126 6683 2 . GLN 127 127 6683 2 . ALA 128 128 6683 2 . ALA 129 129 6683 2 . TYR 130 130 6683 2 . GLN 131 131 6683 2 . LYS 132 132 6683 2 . VAL 133 133 6683 2 . VAL 134 134 6683 2 . ALA 135 135 6683 2 . GLY 136 136 6683 2 . VAL 137 137 6683 2 . ALA 138 138 6683 2 . ASN 139 139 6683 2 . ALA 140 140 6683 2 . LEU 141 141 6683 2 . ALA 142 142 6683 2 . HIS 143 143 6683 2 . LYS 144 144 6683 2 . TYR 145 145 6683 2 . HIS 146 146 6683 2 stop_ save_ save_HEM _Entity.Sf_category entity _Entity.Sf_framecode HEM _Entity.Entry_ID 6683 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name HEM _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _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 . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID HEM _Entity.Nonpolymer_comp_label $chem_comp_HEM _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _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 . 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 . HEM . 6683 3 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 6683 _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 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 6683 1 2 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 6683 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 6683 _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 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . 'recombinant technology' . 'E. Coli' 'Escherichia coli' . . . JM109 . . . . . . . . . . . . . . . . . . . . . . 6683 1 2 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . 'recombinant technology' . 'E. Coli' 'Escherichia coli' . . . JM109 . . . . . . . . . . . . . . . . . . . . . . 6683 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_HEM _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_HEM _Chem_comp.Entry_ID 6683 _Chem_comp.ID HEM _Chem_comp.Provenance . _Chem_comp.Name 'PROTOPORPHYRIN IX CONTAINING FE' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code HEM _Chem_comp.Ambiguous_flag yes _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2009-08-11 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces MHM _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code HEM _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms HEME _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C34 H32 Fe N4 O4' _Chem_comp.Formula_weight 616.487 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag . _Chem_comp.Model_coordinates_db_code 3IA3 _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 9 10:17:59 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID Cc1c2/cc/3\nc(/cc\4/c(c(/c(/[nH]4)c/c5n/c(c\c(c1CCC(=O)O)[nH]2)/C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C SMILES_CANONICAL 'OpenEye OEToolkits' 1.7.0 6683 HEM Cc1c2cc3nc(cc4c(c(c([nH]4)cc5nc(cc(c1CCC(=O)O)[nH]2)C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C SMILES 'OpenEye OEToolkits' 1.7.0 6683 HEM Cc1c2[nH]c(cc3nc(cc4[nH]c(cc5nc(c2)c(C)c5C=C)c(C)c4C=C)c(C)c3CCC(O)=O)c1CCC(O)=O SMILES CACTVS 3.352 6683 HEM Cc1c2[nH]c(cc3nc(cc4[nH]c(cc5nc(c2)c(C)c5C=C)c(C)c4C=C)c(C)c3CCC(O)=O)c1CCC(O)=O SMILES_CANONICAL CACTVS 3.352 6683 HEM FEDYMSUPMFCVOD-UJJXFSCMSA-N InChIKey InChI 1.02 6683 HEM InChI=1S/C34H34N4O4/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25/h7-8,13-16,36-37H,1-2,9-12H2,3-6H3,(H,39,40)(H,41,42)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16- InChI InChI 1.02 6683 HEM O=C(O)CCc5c(c2nc5cc1nc(C(=C1CCC(=O)O)C)cc4c(c(c(cc3nc(c2)C(=C3\C=C)C)n4)C)\C=C)C SMILES ACDLabs 11.02 6683 HEM stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '3,3'-(7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-diyl)dipropanoic acid' 'SYSTEMATIC NAME' ACDLabs 11.02 6683 HEM '3-[(5Z,10Z,14Z,19Z)-18-(2-carboxyethyl)-8,13-bis(ethenyl)-3,7,12,17-tetramethyl-21,23-dihydroporphyrin-2-yl]propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.6.1 6683 HEM stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CHA . CHA . . C . . N 0 . . . . yes no . . . . 2.748 . -19.531 . 39.896 . -2.161 -0.125 0.490 1 . 6683 HEM CHB . CHB . . C . . N 0 . . . . yes no . . . . 3.258 . -17.744 . 35.477 . 1.458 -3.419 0.306 2 . 6683 HEM CHC . CHC . . C . . N 0 . . . . yes no . . . . 1.703 . -21.900 . 33.637 . 4.701 0.169 -0.069 3 . 6683 HEM CHD . CHD . . C . . N 0 . . . . yes no . . . . 1.149 . -23.677 . 38.059 . 1.075 3.460 0.018 4 . 6683 HEM C1A . C1A . . C . . N 0 . . . . yes no . . . . 3.031 . -18.673 . 38.872 . -1.436 -1.305 0.380 5 . 6683 HEM C2A . C2A . . C . . N 0 . . . . yes no . . . . 3.578 . -17.325 . 39.013 . -2.015 -2.587 0.320 6 . 6683 HEM C3A . C3A . . C . . N 0 . . . . yes no . . . . 3.705 . -16.820 . 37.785 . -1.009 -3.500 0.270 7 . 6683 HEM C4A . C4A . . C . . N 0 . . . . yes no . . . . 3.256 . -17.863 . 36.862 . 0.216 -2.803 0.298 8 . 6683 HEM CMA . CMA . . C . . N 0 . . . . no no . . . . 4.227 . -15.469 . 37.393 . -1.175 -4.996 0.197 9 . 6683 HEM CAA . CAA . . C . . N 0 . . . . no no . . . . 3.945 . -16.670 . 40.296 . -3.490 -2.893 0.314 10 . 6683 HEM CBA . CBA . . C . . N 0 . . . . no no . . . . 5.391 . -17.138 . 40.581 . -3.998 -2.926 -1.129 11 . 6683 HEM CGA . CGA . . C . . N 0 . . . . no no . . . . 6.095 . -16.663 . 41.825 . -5.473 -3.232 -1.136 12 . 6683 HEM O1A . O1A . . O . . N 0 . . . . no no . . . . 7.098 . -15.928 . 41.683 . -6.059 -3.405 -0.094 13 . 6683 HEM O2A . O2A . . O . . N 0 . . . . no no . . . . 5.657 . -17.040 . 42.940 . -6.137 -3.311 -2.300 14 . 6683 HEM C1B . C1B . . C . . N 0 . . . . yes no . . . . 2.888 . -18.698 . 34.579 . 2.664 -2.707 0.308 15 . 6683 HEM C2B . C2B . . C . . N 0 . . . . yes no . . . . 2.933 . -18.535 . 33.146 . 3.937 -3.328 0.418 16 . 6683 HEM C3B . C3B . . C . . N 0 . . . . yes no . . . . 2.499 . -19.716 . 32.632 . 4.874 -2.341 0.314 17 . 6683 HEM C4B . C4B . . C . . N 0 . . . . yes no . . . . 2.187 . -20.580 . 33.743 . 4.117 -1.079 0.139 18 . 6683 HEM CMB . CMB . . C . . N 0 . . . . no no . . . . 3.391 . -17.290 . 32.422 . 4.203 -4.798 0.613 19 . 6683 HEM CAB . CAB . . C . . N 0 . . . . no no . . . . 2.345 . -20.140 . 31.217 . 6.339 -2.497 0.365 20 . 6683 HEM CBB . CBB . . C . . N 0 . . . . no no . . . . 1.755 . -19.492 . 30.233 . 6.935 -3.419 -0.385 21 . 6683 HEM C1C . C1C . . C . . N 0 . . . . yes no . . . . 1.395 . -22.786 . 34.659 . 3.964 1.345 -0.174 22 . 6683 HEM C2C . C2C . . C . . N 0 . . . . yes no . . . . 0.854 . -24.130 . 34.500 . 4.531 2.601 -0.445 23 . 6683 HEM C3C . C3C . . C . . N 0 . . . . yes no . . . . 0.689 . -24.626 . 35.757 . 3.510 3.536 -0.437 24 . 6683 HEM C4C . C4C . . C . . N 0 . . . . yes no . . . . 1.139 . -23.583 . 36.674 . 2.304 2.846 -0.139 25 . 6683 HEM CMC . CMC . . C . . N 0 . . . . no no . . . . 0.550 . -24.782 . 33.175 . 5.991 2.880 -0.697 26 . 6683 HEM CAC . CAC . . C . . N 0 . . . . no no . . . . 0.164 . -25.943 . 36.196 . 3.649 4.981 -0.692 27 . 6683 HEM CBC . CBC . . C . . N 0 . . . . no no . . . . 0.498 . -27.158 . 35.750 . 4.201 5.407 -1.823 28 . 6683 HEM C1D . C1D . . C . . N 0 . . . . yes no . . . . 1.550 . -22.718 . 38.980 . -0.102 2.753 0.298 29 . 6683 HEM C2D . C2D . . C . . N 0 . . . . yes no . . . . 1.513 . -22.879 . 40.415 . -1.382 3.388 0.641 30 . 6683 HEM C3D . C3D . . C . . N 0 . . . . yes no . . . . 1.951 . -21.691 . 40.929 . -2.283 2.389 0.774 31 . 6683 HEM C4D . C4D . . C . . N 0 . . . . yes no . . . . 2.277 . -20.826 . 39.811 . -1.561 1.137 0.511 32 . 6683 HEM CMD . CMD . . C . . N 0 . . . . no no . . . . 1.055 . -24.094 . 41.156 . -1.639 4.863 0.811 33 . 6683 HEM CAD . CAD . . C . . N 0 . . . . no no . . . . 2.048 . -21.326 . 42.352 . -3.741 2.532 1.123 34 . 6683 HEM CBD . CBD . . C . . N 0 . . . . no no . . . . 0.741 . -20.498 . 42.530 . -4.573 2.563 -0.160 35 . 6683 HEM CGD . CGD . . C . . N 0 . . . . no no . . . . 0.578 . -19.987 . 43.892 . -6.032 2.706 0.189 36 . 6683 HEM O1D . O1D . . O . . N 0 . . . . no no . . . . 1.387 . -19.103 . 44.303 . -6.372 2.776 1.347 37 . 6683 HEM O2D . O2D . . O . . N 0 . . . . no no . . . . -0.401 . -20.468 . 44.537 . -6.954 2.755 -0.785 38 . 6683 HEM NA . NA . . N . . N 0 . . . . yes no . . . . 2.863 . -18.969 . 37.554 . -0.068 -1.456 0.321 39 . 6683 HEM NB . NB . . N . . N 0 . . . . yes no . . . . 2.439 . -19.944 . 34.911 . 2.820 -1.386 0.207 40 . 6683 HEM NC . NC . . N . . N 0 . . . . yes no . . . . 1.537 . -22.509 . 35.976 . 2.604 1.506 -0.033 41 . 6683 HEM ND . ND . . N . . N 0 . . . . yes no . . . . 2.008 . -21.465 . 38.663 . -0.276 1.431 0.298 42 . 6683 HEM FE . FE . . FE . . S 0 . . . . no no . . . . 2.196 . -20.749 . 36.814 . 1.010 0.157 -0.060 43 . 6683 HEM HHB . HHB . . H . . N 0 . . . . no no . . . . 3.587 . -16.798 . 35.072 . 1.498 -4.508 0.309 44 . 6683 HEM HHC . HHC . . H . . N 0 . . . . no no . . . . 1.553 . -22.268 . 32.633 . 5.786 0.229 -0.153 45 . 6683 HEM HHD . HHD . . H . . N 0 . . . . no no . . . . 0.802 . -24.613 . 38.472 . 1.018 4.543 -0.083 46 . 6683 HEM HMA . HMA . . H . . N 0 . . . . no no . . . . 5.316 . -15.524 . 37.249 . -1.220 -5.306 -0.847 47 . 6683 HEM HMAA . HMAA . . H . . N 0 . . . . no no . . . . 3.749 . -15.149 . 36.455 . -0.328 -5.480 0.683 48 . 6683 HEM HMAB . HMAB . . H . . N 0 . . . . no no . . . . 3.998 . -14.743 . 38.187 . -2.097 -5.285 0.702 49 . 6683 HEM HAA . HAA . . H . . N 0 . . . . no no . . . . 3.894 . -15.575 . 40.209 . -3.662 -3.862 0.782 50 . 6683 HEM HAAA . HAAA . . H . . N 0 . . . . no no . . . . 3.264 . -16.976 . 41.104 . -4.024 -2.121 0.869 51 . 6683 HEM HBA . HBA . . H . . N 0 . . . . no no . . . . 5.351 . -18.235 . 40.650 . -3.825 -1.956 -1.597 52 . 6683 HEM HBAA . HBAA . . H . . N 0 . . . . no no . . . . 5.999 . -16.792 . 39.732 . -3.464 -3.697 -1.684 53 . 6683 HEM HMB . HMB . . H . . N 0 . . . . no no . . . . 3.319 . -17.449 . 31.336 . 3.256 -5.336 0.660 54 . 6683 HEM HMBA . HMBA . . H . . N 0 . . . . no no . . . . 2.753 . -16.442 . 32.711 . 4.794 -5.175 -0.222 55 . 6683 HEM HMBB . HMBB . . H . . N 0 . . . . no no . . . . 4.435 . -17.072 . 32.692 . 4.752 -4.948 1.543 56 . 6683 HEM HAB . HAB . . H . . N 0 . . . . no no . . . . 2.770 . -21.100 . 30.963 . 6.927 -1.863 1.011 57 . 6683 HEM HBB . HBB . . H . . N 0 . . . . no no . . . . 1.719 . -19.927 . 29.245 . 7.994 -3.600 -0.277 58 . 6683 HEM HBBA . HBBA . . H . . N 0 . . . . no no . . . . 1.308 . -18.526 . 30.414 . 6.360 -3.987 -1.102 59 . 6683 HEM HMC . HMC . . H . . N 0 . . . . no no . . . . 1.438 . -25.328 . 32.822 . 6.554 1.949 -0.639 60 . 6683 HEM HMCA . HMCA . . H . . N 0 . . . . no no . . . . -0.288 . -25.484 . 33.296 . 6.110 3.316 -1.689 61 . 6683 HEM HMCB . HMCB . . H . . N 0 . . . . no no . . . . 0.278 . -24.010 . 32.440 . 6.362 3.578 0.053 62 . 6683 HEM HAC . HAC . . H . . N 0 . . . . no no . . . . -0.583 . -25.916 . 36.975 . 3.303 5.694 0.042 63 . 6683 HEM HBC . HBC . . H . . N 0 . . . . no no . . . . 0.027 . -28.035 . 36.169 . 4.614 4.696 -2.523 64 . 6683 HEM HBCA . HBCA . . H . . N 0 . . . . no no . . . . 1.239 . -27.263 . 34.971 . 4.235 6.464 -2.043 65 . 6683 HEM HMD . HMD . . H . . N 0 . . . . no no . . . . 1.142 . -23.919 . 42.238 . -0.715 5.415 0.639 66 . 6683 HEM HMDA . HMDA . . H . . N 0 . . . . no no . . . . 0.006 . -24.304 . 40.902 . -2.394 5.185 0.094 67 . 6683 HEM HMDB . HMDB . . H . . N 0 . . . . no no . . . . 1.680 . -24.954 . 40.872 . -1.994 5.055 1.824 68 . 6683 HEM HAD . HAD . . H . . N 0 . . . . no no . . . . 2.081 . -22.206 . 43.011 . -4.052 1.687 1.738 69 . 6683 HEM HADA . HADA . . H . . N 0 . . . . no no . . . . 2.951 . -20.739 . 42.575 . -3.893 3.459 1.677 70 . 6683 HEM HBD . HBD . . H . . N 0 . . . . no no . . . . 0.775 . -19.642 . 41.839 . -4.262 3.408 -0.775 71 . 6683 HEM HBDA . HBDA . . H . . N 0 . . . . no no . . . . -0.116 . -21.147 . 42.297 . -4.421 1.636 -0.714 72 . 6683 HEM H2A . H2A . . H . . N 0 . . . . no no . . . . 6.201 . -16.682 . 43.632 . -7.082 -3.510 -2.254 73 . 6683 HEM H2D . H2D . . H . . N 0 . . . . no no . . . . -0.445 . -20.063 . 45.395 . -7.877 2.847 -0.512 74 . 6683 HEM HHA . HHA . . H . . N 0 . . . . no no . . . . 2.913 . -19.150 . 40.893 . -3.246 -0.188 0.567 75 . 6683 HEM stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING CHA C1A yes N 1 . 6683 HEM 2 . DOUB CHA C4D yes N 2 . 6683 HEM 3 . SING CHA HHA no N 3 . 6683 HEM 4 . SING CHB C4A yes N 4 . 6683 HEM 5 . DOUB CHB C1B yes N 5 . 6683 HEM 6 . SING CHB HHB no N 6 . 6683 HEM 7 . SING CHC C4B yes N 7 . 6683 HEM 8 . DOUB CHC C1C yes N 8 . 6683 HEM 9 . SING CHC HHC no N 9 . 6683 HEM 10 . DOUB CHD C4C yes N 10 . 6683 HEM 11 . SING CHD C1D yes N 11 . 6683 HEM 12 . SING CHD HHD no N 12 . 6683 HEM 13 . DOUB C1A C2A yes N 13 . 6683 HEM 14 . SING C1A NA yes N 14 . 6683 HEM 15 . SING C2A C3A yes N 15 . 6683 HEM 16 . SING C2A CAA no N 16 . 6683 HEM 17 . DOUB C3A C4A yes N 17 . 6683 HEM 18 . SING C3A CMA no N 18 . 6683 HEM 19 . SING C4A NA yes N 19 . 6683 HEM 20 . SING CMA HMA no N 20 . 6683 HEM 21 . SING CMA HMAA no N 21 . 6683 HEM 22 . SING CMA HMAB no N 22 . 6683 HEM 23 . SING CAA CBA no N 23 . 6683 HEM 24 . SING CAA HAA no N 24 . 6683 HEM 25 . SING CAA HAAA no N 25 . 6683 HEM 26 . SING CBA CGA no N 26 . 6683 HEM 27 . SING CBA HBA no N 27 . 6683 HEM 28 . SING CBA HBAA no N 28 . 6683 HEM 29 . DOUB CGA O1A no N 29 . 6683 HEM 30 . SING CGA O2A no N 30 . 6683 HEM 31 . SING C1B C2B no N 31 . 6683 HEM 32 . SING C1B NB yes N 32 . 6683 HEM 33 . DOUB C2B C3B yes N 33 . 6683 HEM 34 . SING C2B CMB yes N 34 . 6683 HEM 35 . SING C3B C4B no N 35 . 6683 HEM 36 . SING C3B CAB yes N 36 . 6683 HEM 37 . DOUB C4B NB no N 37 . 6683 HEM 38 . SING CMB HMB yes N 38 . 6683 HEM 39 . SING CMB HMBA no N 39 . 6683 HEM 40 . SING CMB HMBB no N 40 . 6683 HEM 41 . DOUB CAB CBB no N 41 . 6683 HEM 42 . SING CAB HAB no N 42 . 6683 HEM 43 . SING CBB HBB no N 43 . 6683 HEM 44 . SING CBB HBBA no N 44 . 6683 HEM 45 . SING C1C C2C no N 45 . 6683 HEM 46 . SING C1C NC yes N 46 . 6683 HEM 47 . DOUB C2C C3C yes N 47 . 6683 HEM 48 . SING C2C CMC yes N 48 . 6683 HEM 49 . SING C3C C4C no N 49 . 6683 HEM 50 . SING C3C CAC yes N 50 . 6683 HEM 51 . SING C4C NC no N 51 . 6683 HEM 52 . SING CMC HMC yes N 52 . 6683 HEM 53 . SING CMC HMCA no N 53 . 6683 HEM 54 . SING CMC HMCB no N 54 . 6683 HEM 55 . DOUB CAC CBC no N 55 . 6683 HEM 56 . SING CAC HAC no N 56 . 6683 HEM 57 . SING CBC HBC no N 57 . 6683 HEM 58 . SING CBC HBCA no N 58 . 6683 HEM 59 . SING C1D C2D no N 59 . 6683 HEM 60 . DOUB C1D ND yes N 60 . 6683 HEM 61 . DOUB C2D C3D yes N 61 . 6683 HEM 62 . SING C2D CMD yes N 62 . 6683 HEM 63 . SING C3D C4D no N 63 . 6683 HEM 64 . SING C3D CAD yes N 64 . 6683 HEM 65 . SING C4D ND no N 65 . 6683 HEM 66 . SING CMD HMD yes N 66 . 6683 HEM 67 . SING CMD HMDA no N 67 . 6683 HEM 68 . SING CMD HMDB no N 68 . 6683 HEM 69 . SING CAD CBD no N 69 . 6683 HEM 70 . SING CAD HAD no N 70 . 6683 HEM 71 . SING CAD HADA no N 71 . 6683 HEM 72 . SING CBD CGD no N 72 . 6683 HEM 73 . SING CBD HBD no N 73 . 6683 HEM 74 . SING CBD HBDA no N 74 . 6683 HEM 75 . DOUB CGD O1D no N 75 . 6683 HEM 76 . SING CGD O2D no N 76 . 6683 HEM 77 . SING O2A H2A no N 77 . 6683 HEM 78 . SING O2D H2D no N 78 . 6683 HEM 79 . SING FE NA no N 79 . 6683 HEM 80 . SING FE NB no N 80 . 6683 HEM 81 . SING FE NC no N 81 . 6683 HEM 82 . SING FE ND no N 82 . 6683 HEM stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_deoxy-Hb_A_1 _Sample.Sf_category sample _Sample.Sf_framecode deoxy-Hb_A_1 _Sample.Entry_ID 6683 _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 alpha_chain '[U-13C; U-15N; U-2H]' 1 $assembly 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . 2 . . mM . . . . 6683 1 2 beta_chain . 1 $assembly 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . 2 . . mM . . . . 6683 1 3 heme . 1 $assembly 3 $HEM . . 4 . . mM . . . . 6683 1 stop_ save_ save_deoxy-Hb_A_2 _Sample.Sf_category sample _Sample.Sf_framecode deoxy-Hb_A_2 _Sample.Entry_ID 6683 _Sample.ID 2 _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 alpha_chain . 1 $assembly 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . 2 . . mM . . . . 6683 2 2 beta_chain '[U-13C; U-15N; U-2H]' 1 $assembly 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . 2 . . mM . . . . 6683 2 3 heme . 1 $assembly 3 $HEM . . 4 . . mM . . . . 6683 2 stop_ save_ save_deoxy-Hb_A_3 _Sample.Sf_category sample _Sample.Sf_framecode deoxy-Hb_A_3 _Sample.Entry_ID 6683 _Sample.ID 3 _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 alpha_chain '[U-15N; U-2H]' 1 $assembly 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . 2 . . mM . . . . 6683 3 2 beta_chain . 1 $assembly 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . 2 . . mM . . . . 6683 3 3 heme . 1 $assembly 3 $HEM . . 4 . . mM . . . . 6683 3 stop_ save_ save_deoxy-Hb_A_4 _Sample.Sf_category sample _Sample.Sf_framecode deoxy-Hb_A_4 _Sample.Entry_ID 6683 _Sample.ID 4 _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 alpha_chain . 1 $assembly 1 $human_normal_adult_hemoglobin_alpha_chain_in_deoxy_form . . 2 . . mM . . . . 6683 4 2 beta_chain '[U-15N; U-2H]' 1 $assembly 2 $human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . 2 . . mM . . . . 6683 4 3 heme . 1 $assembly 3 $HEM . . 2 . . mM . . . . 6683 4 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 6683 _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 0.005 M 6683 1 pH 7 0.2 pH 6683 1 temperature 302 0.2 K 6683 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 600MHz_spectrometer _NMR_spectrometer.Entry_ID 6683 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details ; Bruker Avance DRX-600 spectrometer equipped with five RF channels using either room temperature or cryo probes ; _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance_DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode NMR_experiment_list _Experiment_list.Entry_ID 6683 _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 (1H_15N)-TROSY_HSQC no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 2 TROSY-HNCA no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 3 TROSY-HNCOCA no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 4 TROSY-HNCACB no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 5 TROSY-HN(CO)CACB no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 6 TROSY-HNCO no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 7 '3D HSQC-NOESY-TROSY' no 1 $(1H_15N)-TROSY_HSQC . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6683 1 stop_ save_ save_(1H_15N)-TROSY_HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode (1H_15N)-TROSY_HSQC _NMR_spec_expt.Entry_ID 6683 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name (1H_15N)-TROSY_HSQC _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 1 _NMR_spec_expt.NMR_spectrometer_label $600MHz_spectrometer _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_chemical_shift_referencing _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_referencing _Chem_shift_reference.Entry_ID 6683 _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 C 13 DSS 'methyl protons' . . . . ppm 0.0 external indirect 0.25144952 . . . . . . . . . 6683 1 H 1 H2O protons . . . . ppm 4.76 internal direct 1.0 . . . . . . . . . 6683 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 external indirect 0.10132905 . . . . . . . . . 6683 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_deoxy-Hb_A_alpha _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode deoxy-Hb_A_alpha _Assigned_chem_shift_list.Entry_ID 6683 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _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 'deoxy-Hb A alpha chain' _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 $deoxy-Hb_A_1 isotropic 6683 1 . . 2 $deoxy-Hb_A_2 isotropic 6683 1 . . 3 $deoxy-Hb_A_3 isotropic 6683 1 . . 4 $deoxy-Hb_A_4 isotropic 6683 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 VAL CA C 13 57.37 0.20 . 1 . . . . 1 VAL CA . 6683 1 2 . 1 1 1 1 VAL CB C 13 30.08 0.20 . 1 . . . . 1 VAL CB . 6683 1 3 . 1 1 2 2 LEU H H 1 8.22 0.03 . 1 . . . . 2 LEU H . 6683 1 4 . 1 1 2 2 LEU C C 13 176.27 0.20 . 1 . . . . 2 LEU C . 6683 1 5 . 1 1 2 2 LEU CA C 13 54.29 0.20 . 1 . . . . 2 LEU CA . 6683 1 6 . 1 1 2 2 LEU CB C 13 41.17 0.20 . 1 . . . . 2 LEU CB . 6683 1 7 . 1 1 2 2 LEU N N 15 119.94 0.30 . 1 . . . . 2 LEU N . 6683 1 8 . 1 1 3 3 SER H H 1 9.83 0.03 . 1 . . . . 3 SER H . 6683 1 9 . 1 1 3 3 SER CA C 13 56.86 0.20 . 1 . . . . 3 SER CA . 6683 1 10 . 1 1 3 3 SER CB C 13 63.15 0.20 . 1 . . . . 3 SER CB . 6683 1 11 . 1 1 3 3 SER N N 15 125.78 0.30 . 1 . . . . 3 SER N . 6683 1 12 . 1 1 4 4 PRO C C 13 179.77 0.20 . 1 . . . . 4 PRO C . 6683 1 13 . 1 1 4 4 PRO CA C 13 66.51 0.20 . 1 . . . . 4 PRO CA . 6683 1 14 . 1 1 4 4 PRO CB C 13 31.12 0.20 . 1 . . . . 4 PRO CB . 6683 1 15 . 1 1 5 5 ALA H H 1 7.88 0.03 . 1 . . . . 5 ALA H . 6683 1 16 . 1 1 5 5 ALA C C 13 180.16 0.20 . 1 . . . . 5 ALA C . 6683 1 17 . 1 1 5 5 ALA CA C 13 54.78 0.20 . 1 . . . . 5 ALA CA . 6683 1 18 . 1 1 5 5 ALA CB C 13 17.77 0.20 . 1 . . . . 5 ALA CB . 6683 1 19 . 1 1 5 5 ALA N N 15 121.10 0.30 . 1 . . . . 5 ALA N . 6683 1 20 . 1 1 6 6 ASP H H 1 8.08 0.03 . 1 . . . . 6 ASP H . 6683 1 21 . 1 1 6 6 ASP C C 13 179.23 0.20 . 1 . . . . 6 ASP C . 6683 1 22 . 1 1 6 6 ASP CA C 13 57.44 0.20 . 1 . . . . 6 ASP CA . 6683 1 23 . 1 1 6 6 ASP CB C 13 41.56 0.20 . 1 . . . . 6 ASP CB . 6683 1 24 . 1 1 6 6 ASP N N 15 119.59 0.30 . 1 . . . . 6 ASP N . 6683 1 25 . 1 1 7 7 LYS H H 1 8.15 0.03 . 1 . . . . 7 LYS H . 6683 1 26 . 1 1 7 7 LYS C C 13 178.73 0.20 . 1 . . . . 7 LYS C . 6683 1 27 . 1 1 7 7 LYS CA C 13 61.01 0.20 . 1 . . . . 7 LYS CA . 6683 1 28 . 1 1 7 7 LYS CB C 13 31.45 0.20 . 1 . . . . 7 LYS CB . 6683 1 29 . 1 1 7 7 LYS N N 15 119.84 0.30 . 1 . . . . 7 LYS N . 6683 1 30 . 1 1 8 8 THR H H 1 8.06 0.03 . 1 . . . . 8 THR H . 6683 1 31 . 1 1 8 8 THR C C 13 177.14 0.20 . 1 . . . . 8 THR C . 6683 1 32 . 1 1 8 8 THR CA C 13 66.66 0.20 . 1 . . . . 8 THR CA . 6683 1 33 . 1 1 8 8 THR CB C 13 68.38 0.20 . 1 . . . . 8 THR CB . 6683 1 34 . 1 1 8 8 THR N N 15 117.47 0.30 . 1 . . . . 8 THR N . 6683 1 35 . 1 1 9 9 ASN H H 1 8.34 0.03 . 1 . . . . 9 ASN H . 6683 1 36 . 1 1 9 9 ASN C C 13 177.86 0.20 . 1 . . . . 9 ASN C . 6683 1 37 . 1 1 9 9 ASN CA C 13 55.49 0.20 . 1 . . . . 9 ASN CA . 6683 1 38 . 1 1 9 9 ASN CB C 13 37.89 0.20 . 1 . . . . 9 ASN CB . 6683 1 39 . 1 1 9 9 ASN N N 15 122.50 0.30 . 1 . . . . 9 ASN N . 6683 1 40 . 1 1 10 10 VAL H H 1 8.43 0.03 . 1 . . . . 10 VAL H . 6683 1 41 . 1 1 10 10 VAL C C 13 177.59 0.20 . 1 . . . . 10 VAL C . 6683 1 42 . 1 1 10 10 VAL CA C 13 66.77 0.20 . 1 . . . . 10 VAL CA . 6683 1 43 . 1 1 10 10 VAL CB C 13 30.77 0.20 . 1 . . . . 10 VAL CB . 6683 1 44 . 1 1 10 10 VAL N N 15 120.83 0.30 . 1 . . . . 10 VAL N . 6683 1 45 . 1 1 11 11 LYS H H 1 7.98 0.03 . 1 . . . . 11 LYS H . 6683 1 46 . 1 1 11 11 LYS C C 13 180.43 0.20 . 1 . . . . 11 LYS C . 6683 1 47 . 1 1 11 11 LYS CA C 13 60.18 0.20 . 1 . . . . 11 LYS CA . 6683 1 48 . 1 1 11 11 LYS CB C 13 31.83 0.20 . 1 . . . . 11 LYS CB . 6683 1 49 . 1 1 11 11 LYS N N 15 119.62 0.30 . 1 . . . . 11 LYS N . 6683 1 50 . 1 1 12 12 ALA H H 1 8.15 0.03 . 1 . . . . 12 ALA H . 6683 1 51 . 1 1 12 12 ALA C C 13 181.09 0.20 . 1 . . . . 12 ALA C . 6683 1 52 . 1 1 12 12 ALA CA C 13 54.72 0.20 . 1 . . . . 12 ALA CA . 6683 1 53 . 1 1 12 12 ALA CB C 13 17.53 0.20 . 1 . . . . 12 ALA CB . 6683 1 54 . 1 1 12 12 ALA N N 15 123.09 0.30 . 1 . . . . 12 ALA N . 6683 1 55 . 1 1 13 13 ALA H H 1 8.02 0.03 . 1 . . . . 13 ALA H . 6683 1 56 . 1 1 13 13 ALA C C 13 179.48 0.20 . 1 . . . . 13 ALA C . 6683 1 57 . 1 1 13 13 ALA CA C 13 55.27 0.20 . 1 . . . . 13 ALA CA . 6683 1 58 . 1 1 13 13 ALA CB C 13 17.56 0.20 . 1 . . . . 13 ALA CB . 6683 1 59 . 1 1 13 13 ALA N N 15 121.69 0.30 . 1 . . . . 13 ALA N . 6683 1 60 . 1 1 14 14 TRP H H 1 8.92 0.03 . 1 . . . . 14 TRP H . 6683 1 61 . 1 1 14 14 TRP HE1 H 1 10.07 0.03 . 1 . . . . 14 TRP HE1 . 6683 1 62 . 1 1 14 14 TRP C C 13 179.94 0.20 . 1 . . . . 14 TRP C . 6683 1 63 . 1 1 14 14 TRP CA C 13 59.73 0.20 . 1 . . . . 14 TRP CA . 6683 1 64 . 1 1 14 14 TRP CB C 13 28.78 0.20 . 1 . . . . 14 TRP CB . 6683 1 65 . 1 1 14 14 TRP N N 15 118.56 0.30 . 1 . . . . 14 TRP N . 6683 1 66 . 1 1 14 14 TRP NE1 N 15 131.03 0.30 . 1 . . . . 14 TRP NE1 . 6683 1 67 . 1 1 15 15 GLY H H 1 7.96 0.03 . 1 . . . . 15 GLY H . 6683 1 68 . 1 1 15 15 GLY C C 13 176.24 0.20 . 1 . . . . 15 GLY C . 6683 1 69 . 1 1 15 15 GLY CA C 13 46.47 0.20 . 1 . . . . 15 GLY CA . 6683 1 70 . 1 1 15 15 GLY N N 15 107.31 0.30 . 1 . . . . 15 GLY N . 6683 1 71 . 1 1 16 16 LYS H H 1 7.13 0.03 . 1 . . . . 16 LYS H . 6683 1 72 . 1 1 16 16 LYS C C 13 178.77 0.20 . 1 . . . . 16 LYS C . 6683 1 73 . 1 1 16 16 LYS CA C 13 56.23 0.20 . 1 . . . . 16 LYS CA . 6683 1 74 . 1 1 16 16 LYS CB C 13 31.08 0.20 . 1 . . . . 16 LYS CB . 6683 1 75 . 1 1 16 16 LYS N N 15 120.99 0.30 . 1 . . . . 16 LYS N . 6683 1 76 . 1 1 17 17 VAL H H 1 7.29 0.03 . 1 . . . . 17 VAL H . 6683 1 77 . 1 1 17 17 VAL C C 13 177.65 0.20 . 1 . . . . 17 VAL C . 6683 1 78 . 1 1 17 17 VAL CA C 13 66.02 0.20 . 1 . . . . 17 VAL CA . 6683 1 79 . 1 1 17 17 VAL CB C 13 29.88 0.20 . 1 . . . . 17 VAL CB . 6683 1 80 . 1 1 17 17 VAL N N 15 122.61 0.30 . 1 . . . . 17 VAL N . 6683 1 81 . 1 1 18 18 GLY H H 1 7.04 0.03 . 1 . . . . 18 GLY H . 6683 1 82 . 1 1 18 18 GLY CA C 13 46.85 0.20 . 1 . . . . 18 GLY CA . 6683 1 83 . 1 1 18 18 GLY N N 15 104.00 0.30 . 1 . . . . 18 GLY N . 6683 1 84 . 1 1 19 19 ALA C C 13 178.30 0.20 . 1 . . . . 19 ALA C . 6683 1 85 . 1 1 19 19 ALA CA C 13 52.91 0.20 . 1 . . . . 19 ALA CA . 6683 1 86 . 1 1 19 19 ALA CB C 13 17.31 0.20 . 1 . . . . 19 ALA CB . 6683 1 87 . 1 1 20 20 HIS H H 1 7.68 0.03 . 1 . . . . 20 HIS H . 6683 1 88 . 1 1 20 20 HIS C C 13 173.92 0.20 . 1 . . . . 20 HIS C . 6683 1 89 . 1 1 20 20 HIS CA C 13 55.27 0.20 . 1 . . . . 20 HIS CA . 6683 1 90 . 1 1 20 20 HIS CB C 13 28.02 0.20 . 1 . . . . 20 HIS CB . 6683 1 91 . 1 1 20 20 HIS N N 15 116.51 0.30 . 1 . . . . 20 HIS N . 6683 1 92 . 1 1 21 21 ALA H H 1 6.72 0.03 . 1 . . . . 21 ALA H . 6683 1 93 . 1 1 21 21 ALA C C 13 178.05 0.20 . 1 . . . . 21 ALA C . 6683 1 94 . 1 1 21 21 ALA CA C 13 55.95 0.20 . 1 . . . . 21 ALA CA . 6683 1 95 . 1 1 21 21 ALA CB C 13 17.31 0.20 . 1 . . . . 21 ALA CB . 6683 1 96 . 1 1 21 21 ALA N N 15 122.96 0.30 . 1 . . . . 21 ALA N . 6683 1 97 . 1 1 22 22 GLY H H 1 8.16 0.03 . 1 . . . . 22 GLY H . 6683 1 98 . 1 1 22 22 GLY C C 13 176.56 0.20 . 1 . . . . 22 GLY C . 6683 1 99 . 1 1 22 22 GLY CA C 13 47.07 0.20 . 1 . . . . 22 GLY CA . 6683 1 100 . 1 1 22 22 GLY N N 15 105.45 0.30 . 1 . . . . 22 GLY N . 6683 1 101 . 1 1 23 23 GLU H H 1 7.55 0.03 . 1 . . . . 23 GLU H . 6683 1 102 . 1 1 23 23 GLU C C 13 179.76 0.20 . 1 . . . . 23 GLU C . 6683 1 103 . 1 1 23 23 GLU CA C 13 58.68 0.20 . 1 . . . . 23 GLU CA . 6683 1 104 . 1 1 23 23 GLU CB C 13 28.19 0.20 . 1 . . . . 23 GLU CB . 6683 1 105 . 1 1 23 23 GLU N N 15 125.76 0.30 . 1 . . . . 23 GLU N . 6683 1 106 . 1 1 24 24 TYR H H 1 7.83 0.03 . 1 . . . . 24 TYR H . 6683 1 107 . 1 1 24 24 TYR C C 13 178.41 0.20 . 1 . . . . 24 TYR C . 6683 1 108 . 1 1 24 24 TYR CA C 13 56.89 0.20 . 1 . . . . 24 TYR CA . 6683 1 109 . 1 1 24 24 TYR CB C 13 33.75 0.20 . 1 . . . . 24 TYR CB . 6683 1 110 . 1 1 24 24 TYR N N 15 122.15 0.30 . 1 . . . . 24 TYR N . 6683 1 111 . 1 1 25 25 GLY H H 1 8.22 0.03 . 1 . . . . 25 GLY H . 6683 1 112 . 1 1 25 25 GLY C C 13 174.00 0.20 . 1 . . . . 25 GLY C . 6683 1 113 . 1 1 25 25 GLY CA C 13 45.77 0.20 . 1 . . . . 25 GLY CA . 6683 1 114 . 1 1 25 25 GLY N N 15 108.67 0.30 . 1 . . . . 25 GLY N . 6683 1 115 . 1 1 26 26 ALA H H 1 7.19 0.03 . 1 . . . . 26 ALA H . 6683 1 116 . 1 1 26 26 ALA C C 13 178.58 0.20 . 1 . . . . 26 ALA C . 6683 1 117 . 1 1 26 26 ALA CA C 13 54.36 0.20 . 1 . . . . 26 ALA CA . 6683 1 118 . 1 1 26 26 ALA CB C 13 17.87 0.20 . 1 . . . . 26 ALA CB . 6683 1 119 . 1 1 26 26 ALA N N 15 122.15 0.30 . 1 . . . . 26 ALA N . 6683 1 120 . 1 1 27 27 GLU H H 1 7.54 0.03 . 1 . . . . 27 GLU H . 6683 1 121 . 1 1 27 27 GLU C C 13 178.16 0.20 . 1 . . . . 27 GLU C . 6683 1 122 . 1 1 27 27 GLU CA C 13 58.74 0.20 . 1 . . . . 27 GLU CA . 6683 1 123 . 1 1 27 27 GLU CB C 13 28.54 0.20 . 1 . . . . 27 GLU CB . 6683 1 124 . 1 1 27 27 GLU N N 15 120.80 0.30 . 1 . . . . 27 GLU N . 6683 1 125 . 1 1 28 28 ALA H H 1 7.96 0.03 . 1 . . . . 28 ALA H . 6683 1 126 . 1 1 28 28 ALA C C 13 179.36 0.20 . 1 . . . . 28 ALA C . 6683 1 127 . 1 1 28 28 ALA CA C 13 55.28 0.20 . 1 . . . . 28 ALA CA . 6683 1 128 . 1 1 28 28 ALA CB C 13 16.65 0.20 . 1 . . . . 28 ALA CB . 6683 1 129 . 1 1 28 28 ALA N N 15 122.74 0.30 . 1 . . . . 28 ALA N . 6683 1 130 . 1 1 29 29 LEU H H 1 6.62 0.03 . 1 . . . . 29 LEU H . 6683 1 131 . 1 1 29 29 LEU C C 13 176.54 0.20 . 1 . . . . 29 LEU C . 6683 1 132 . 1 1 29 29 LEU CA C 13 56.85 0.20 . 1 . . . . 29 LEU CA . 6683 1 133 . 1 1 29 29 LEU CB C 13 39.57 0.20 . 1 . . . . 29 LEU CB . 6683 1 134 . 1 1 29 29 LEU N N 15 117.09 0.30 . 1 . . . . 29 LEU N . 6683 1 135 . 1 1 30 30 GLU H H 1 7.56 0.03 . 1 . . . . 30 GLU H . 6683 1 136 . 1 1 30 30 GLU C C 13 179.95 0.20 . 1 . . . . 30 GLU C . 6683 1 137 . 1 1 30 30 GLU CA C 13 60.20 0.20 . 1 . . . . 30 GLU CA . 6683 1 138 . 1 1 30 30 GLU CB C 13 28.70 0.20 . 1 . . . . 30 GLU CB . 6683 1 139 . 1 1 30 30 GLU N N 15 119.61 0.30 . 1 . . . . 30 GLU N . 6683 1 140 . 1 1 31 31 ARG H H 1 8.52 0.03 . 1 . . . . 31 ARG H . 6683 1 141 . 1 1 31 31 ARG C C 13 178.77 0.20 . 1 . . . . 31 ARG C . 6683 1 142 . 1 1 31 31 ARG CA C 13 60.93 0.20 . 1 . . . . 31 ARG CA . 6683 1 143 . 1 1 31 31 ARG CB C 13 27.13 0.20 . 1 . . . . 31 ARG CB . 6683 1 144 . 1 1 31 31 ARG N N 15 117.18 0.30 . 1 . . . . 31 ARG N . 6683 1 145 . 1 1 32 32 MET H H 1 8.04 0.03 . 1 . . . . 32 MET H . 6683 1 146 . 1 1 32 32 MET C C 13 177.88 0.20 . 1 . . . . 32 MET C . 6683 1 147 . 1 1 32 32 MET CA C 13 60.58 0.20 . 1 . . . . 32 MET CA . 6683 1 148 . 1 1 32 32 MET CB C 13 32.01 0.20 . 1 . . . . 32 MET CB . 6683 1 149 . 1 1 32 32 MET N N 15 124.59 0.30 . 1 . . . . 32 MET N . 6683 1 150 . 1 1 33 33 PHE H H 1 8.66 0.03 . 1 . . . . 33 PHE H . 6683 1 151 . 1 1 33 33 PHE C C 13 178.91 0.20 . 1 . . . . 33 PHE C . 6683 1 152 . 1 1 33 33 PHE CA C 13 58.81 0.20 . 1 . . . . 33 PHE CA . 6683 1 153 . 1 1 33 33 PHE CB C 13 37.72 0.20 . 1 . . . . 33 PHE CB . 6683 1 154 . 1 1 33 33 PHE N N 15 120.15 0.30 . 1 . . . . 33 PHE N . 6683 1 155 . 1 1 34 34 LEU H H 1 7.70 0.03 . 1 . . . . 34 LEU H . 6683 1 156 . 1 1 34 34 LEU C C 13 179.50 0.20 . 1 . . . . 34 LEU C . 6683 1 157 . 1 1 34 34 LEU CA C 13 56.68 0.20 . 1 . . . . 34 LEU CA . 6683 1 158 . 1 1 34 34 LEU CB C 13 42.35 0.20 . 1 . . . . 34 LEU CB . 6683 1 159 . 1 1 34 34 LEU N N 15 115.15 0.30 . 1 . . . . 34 LEU N . 6683 1 160 . 1 1 35 35 SER H H 1 8.15 0.03 . 1 . . . . 35 SER H . 6683 1 161 . 1 1 35 35 SER C C 13 173.76 0.20 . 1 . . . . 35 SER C . 6683 1 162 . 1 1 35 35 SER CA C 13 63.11 0.20 . 1 . . . . 35 SER CA . 6683 1 163 . 1 1 35 35 SER CB C 13 64.01 0.20 . 1 . . . . 35 SER CB . 6683 1 164 . 1 1 35 35 SER N N 15 114.91 0.30 . 1 . . . . 35 SER N . 6683 1 165 . 1 1 36 36 PHE H H 1 8.64 0.03 . 1 . . . . 36 PHE H . 6683 1 166 . 1 1 36 36 PHE CA C 13 55.02 0.20 . 1 . . . . 36 PHE CA . 6683 1 167 . 1 1 36 36 PHE CB C 13 39.15 0.20 . 1 . . . . 36 PHE CB . 6683 1 168 . 1 1 36 36 PHE N N 15 119.08 0.30 . 1 . . . . 36 PHE N . 6683 1 169 . 1 1 37 37 PRO C C 13 180.97 0.20 . 1 . . . . 37 PRO C . 6683 1 170 . 1 1 37 37 PRO CA C 13 65.15 0.20 . 1 . . . . 37 PRO CA . 6683 1 171 . 1 1 37 37 PRO CB C 13 31.80 0.20 . 1 . . . . 37 PRO CB . 6683 1 172 . 1 1 38 38 THR H H 1 8.63 0.03 . 1 . . . . 38 THR H . 6683 1 173 . 1 1 38 38 THR C C 13 178.25 0.20 . 1 . . . . 38 THR C . 6683 1 174 . 1 1 38 38 THR CA C 13 66.81 0.20 . 1 . . . . 38 THR CA . 6683 1 175 . 1 1 38 38 THR N N 15 113.35 0.30 . 1 . . . . 38 THR N . 6683 1 176 . 1 1 39 39 THR H H 1 9.16 0.03 . 1 . . . . 39 THR H . 6683 1 177 . 1 1 39 39 THR C C 13 178.09 0.20 . 1 . . . . 39 THR C . 6683 1 178 . 1 1 39 39 THR CA C 13 66.92 0.20 . 1 . . . . 39 THR CA . 6683 1 179 . 1 1 39 39 THR CB C 13 71.40 0.20 . 1 . . . . 39 THR CB . 6683 1 180 . 1 1 39 39 THR N N 15 118.50 0.30 . 1 . . . . 39 THR N . 6683 1 181 . 1 1 40 40 LYS H H 1 8.10 0.03 . 1 . . . . 40 LYS H . 6683 1 182 . 1 1 40 40 LYS C C 13 180.75 0.20 . 1 . . . . 40 LYS C . 6683 1 183 . 1 1 40 40 LYS CA C 13 59.74 0.20 . 1 . . . . 40 LYS CA . 6683 1 184 . 1 1 40 40 LYS CB C 13 31.36 0.20 . 1 . . . . 40 LYS CB . 6683 1 185 . 1 1 40 40 LYS N N 15 120.26 0.30 . 1 . . . . 40 LYS N . 6683 1 186 . 1 1 41 41 THR H H 1 7.96 0.03 . 1 . . . . 41 THR H . 6683 1 187 . 1 1 41 41 THR C C 13 175.42 0.20 . 1 . . . . 41 THR C . 6683 1 188 . 1 1 41 41 THR CA C 13 64.67 0.20 . 1 . . . . 41 THR CA . 6683 1 189 . 1 1 41 41 THR CB C 13 69.02 0.20 . 1 . . . . 41 THR CB . 6683 1 190 . 1 1 41 41 THR N N 15 110.38 0.30 . 1 . . . . 41 THR N . 6683 1 191 . 1 1 42 42 TYR H H 1 7.39 0.03 . 1 . . . . 42 TYR H . 6683 1 192 . 1 1 42 42 TYR C C 13 174.42 0.20 . 1 . . . . 42 TYR C . 6683 1 193 . 1 1 42 42 TYR CA C 13 60.27 0.20 . 1 . . . . 42 TYR CA . 6683 1 194 . 1 1 42 42 TYR CB C 13 38.65 0.20 . 1 . . . . 42 TYR CB . 6683 1 195 . 1 1 42 42 TYR N N 15 116.96 0.30 . 1 . . . . 42 TYR N . 6683 1 196 . 1 1 43 43 PHE H H 1 7.99 0.03 . 1 . . . . 43 PHE H . 6683 1 197 . 1 1 43 43 PHE CA C 13 55.34 0.20 . 1 . . . . 43 PHE CA . 6683 1 198 . 1 1 43 43 PHE CB C 13 40.39 0.20 . 1 . . . . 43 PHE CB . 6683 1 199 . 1 1 43 43 PHE N N 15 118.69 0.30 . 1 . . . . 43 PHE N . 6683 1 200 . 1 1 44 44 PRO C C 13 176.73 0.20 . 1 . . . . 44 PRO C . 6683 1 201 . 1 1 44 44 PRO CA C 13 65.35 0.20 . 1 . . . . 44 PRO CA . 6683 1 202 . 1 1 44 44 PRO CB C 13 29.01 0.20 . 1 . . . . 44 PRO CB . 6683 1 203 . 1 1 45 45 HIS H H 1 9.72 0.03 . 1 . . . . 45 HIS H . 6683 1 204 . 1 1 45 45 HIS C C 13 175.77 0.20 . 1 . . . . 45 HIS C . 6683 1 205 . 1 1 45 45 HIS CA C 13 55.51 0.20 . 1 . . . . 45 HIS CA . 6683 1 206 . 1 1 45 45 HIS CB C 13 29.51 0.20 . 1 . . . . 45 HIS CB . 6683 1 207 . 1 1 45 45 HIS N N 15 118.87 0.30 . 1 . . . . 45 HIS N . 6683 1 208 . 1 1 46 46 PHE H H 1 7.61 0.03 . 1 . . . . 46 PHE H . 6683 1 209 . 1 1 46 46 PHE C C 13 176.27 0.20 . 1 . . . . 46 PHE C . 6683 1 210 . 1 1 46 46 PHE CA C 13 55.05 0.20 . 1 . . . . 46 PHE CA . 6683 1 211 . 1 1 46 46 PHE CB C 13 39.22 0.20 . 1 . . . . 46 PHE CB . 6683 1 212 . 1 1 46 46 PHE N N 15 124.39 0.30 . 1 . . . . 46 PHE N . 6683 1 213 . 1 1 47 47 ASP H H 1 7.73 0.03 . 1 . . . . 47 ASP H . 6683 1 214 . 1 1 47 47 ASP C C 13 176.91 0.20 . 1 . . . . 47 ASP C . 6683 1 215 . 1 1 47 47 ASP CA C 13 53.66 0.20 . 1 . . . . 47 ASP CA . 6683 1 216 . 1 1 47 47 ASP CB C 13 39.81 0.20 . 1 . . . . 47 ASP CB . 6683 1 217 . 1 1 47 47 ASP N N 15 120.17 0.30 . 1 . . . . 47 ASP N . 6683 1 218 . 1 1 48 48 LEU H H 1 8.68 0.03 . 1 . . . . 48 LEU H . 6683 1 219 . 1 1 48 48 LEU CA C 13 53.65 0.20 . 1 . . . . 48 LEU CA . 6683 1 220 . 1 1 48 48 LEU CB C 13 39.82 0.20 . 1 . . . . 48 LEU CB . 6683 1 221 . 1 1 48 48 LEU N N 15 129.90 0.30 . 1 . . . . 48 LEU N . 6683 1 222 . 1 1 49 49 SER H H 1 8.27 0.03 . 1 . . . . 49 SER H . 6683 1 223 . 1 1 49 49 SER C C 13 177.52 0.20 . 1 . . . . 49 SER C . 6683 1 224 . 1 1 49 49 SER CA C 13 59.24 0.20 . 1 . . . . 49 SER CA . 6683 1 225 . 1 1 49 49 SER CB C 13 63.96 0.20 . 1 . . . . 49 SER CB . 6683 1 226 . 1 1 49 49 SER N N 15 118.77 0.30 . 1 . . . . 49 SER N . 6683 1 227 . 1 1 50 50 HIS C C 13 177.34 0.20 . 1 . . . . 50 HIS C . 6683 1 228 . 1 1 50 50 HIS CA C 13 60.11 0.20 . 1 . . . . 50 HIS CA . 6683 1 229 . 1 1 50 50 HIS CB C 13 28.07 0.20 . 1 . . . . 50 HIS CB . 6683 1 230 . 1 1 51 51 GLY H H 1 8.89 0.03 . 1 . . . . 51 GLY H . 6683 1 231 . 1 1 51 51 GLY C C 13 174.39 0.20 . 1 . . . . 51 GLY C . 6683 1 232 . 1 1 51 51 GLY CA C 13 44.79 0.20 . 1 . . . . 51 GLY CA . 6683 1 233 . 1 1 51 51 GLY N N 15 117.12 0.30 . 1 . . . . 51 GLY N . 6683 1 234 . 1 1 52 52 SER H H 1 7.43 0.03 . 1 . . . . 52 SER H . 6683 1 235 . 1 1 52 52 SER C C 13 176.63 0.20 . 1 . . . . 52 SER C . 6683 1 236 . 1 1 52 52 SER CA C 13 57.11 0.20 . 1 . . . . 52 SER CA . 6683 1 237 . 1 1 52 52 SER CB C 13 64.62 0.20 . 1 . . . . 52 SER CB . 6683 1 238 . 1 1 52 52 SER N N 15 116.27 0.30 . 1 . . . . 52 SER N . 6683 1 239 . 1 1 53 53 ALA H H 1 9.08 0.03 . 1 . . . . 53 ALA H . 6683 1 240 . 1 1 53 53 ALA C C 13 181.57 0.20 . 1 . . . . 53 ALA C . 6683 1 241 . 1 1 53 53 ALA CA C 13 54.88 0.20 . 1 . . . . 53 ALA CA . 6683 1 242 . 1 1 53 53 ALA CB C 13 17.79 0.20 . 1 . . . . 53 ALA CB . 6683 1 243 . 1 1 53 53 ALA N N 15 132.14 0.30 . 1 . . . . 53 ALA N . 6683 1 244 . 1 1 54 54 GLN H H 1 8.25 0.03 . 1 . . . . 54 GLN H . 6683 1 245 . 1 1 54 54 GLN C C 13 179.44 0.20 . 1 . . . . 54 GLN C . 6683 1 246 . 1 1 54 54 GLN CA C 13 58.77 0.20 . 1 . . . . 54 GLN CA . 6683 1 247 . 1 1 54 54 GLN CB C 13 28.36 0.20 . 1 . . . . 54 GLN CB . 6683 1 248 . 1 1 54 54 GLN N N 15 120.33 0.30 . 1 . . . . 54 GLN N . 6683 1 249 . 1 1 55 55 VAL H H 1 7.41 0.03 . 1 . . . . 55 VAL H . 6683 1 250 . 1 1 55 55 VAL C C 13 177.87 0.20 . 1 . . . . 55 VAL C . 6683 1 251 . 1 1 55 55 VAL CA C 13 67.17 0.20 . 1 . . . . 55 VAL CA . 6683 1 252 . 1 1 55 55 VAL CB C 13 31.11 0.20 . 1 . . . . 55 VAL CB . 6683 1 253 . 1 1 55 55 VAL N N 15 122.98 0.30 . 1 . . . . 55 VAL N . 6683 1 254 . 1 1 56 56 LYS H H 1 7.81 0.03 . 1 . . . . 56 LYS H . 6683 1 255 . 1 1 56 56 LYS C C 13 180.50 0.20 . 1 . . . . 56 LYS C . 6683 1 256 . 1 1 56 56 LYS CA C 13 59.60 0.20 . 1 . . . . 56 LYS CA . 6683 1 257 . 1 1 56 56 LYS CB C 13 31.34 0.20 . 1 . . . . 56 LYS CB . 6683 1 258 . 1 1 56 56 LYS N N 15 120.95 0.30 . 1 . . . . 56 LYS N . 6683 1 259 . 1 1 57 57 GLY H H 1 8.22 0.03 . 1 . . . . 57 GLY H . 6683 1 260 . 1 1 57 57 GLY C C 13 176.81 0.20 . 1 . . . . 57 GLY C . 6683 1 261 . 1 1 57 57 GLY CA C 13 46.66 0.20 . 1 . . . . 57 GLY CA . 6683 1 262 . 1 1 57 57 GLY N N 15 107.86 0.30 . 1 . . . . 57 GLY N . 6683 1 263 . 1 1 58 58 HIS H H 1 8.08 0.03 . 1 . . . . 58 HIS H . 6683 1 264 . 1 1 58 58 HIS C C 13 176.41 0.20 . 1 . . . . 58 HIS C . 6683 1 265 . 1 1 58 58 HIS CA C 13 59.36 0.20 . 1 . . . . 58 HIS CA . 6683 1 266 . 1 1 58 58 HIS CB C 13 31.12 0.20 . 1 . . . . 58 HIS CB . 6683 1 267 . 1 1 58 58 HIS N N 15 124.83 0.30 . 1 . . . . 58 HIS N . 6683 1 268 . 1 1 59 59 GLY H H 1 8.13 0.03 . 1 . . . . 59 GLY H . 6683 1 269 . 1 1 59 59 GLY C C 13 174.24 0.20 . 1 . . . . 59 GLY C . 6683 1 270 . 1 1 59 59 GLY CA C 13 45.75 0.20 . 1 . . . . 59 GLY CA . 6683 1 271 . 1 1 59 59 GLY N N 15 106.87 0.30 . 1 . . . . 59 GLY N . 6683 1 272 . 1 1 60 60 LYS H H 1 6.82 0.03 . 1 . . . . 60 LYS H . 6683 1 273 . 1 1 60 60 LYS CA C 13 58.99 0.20 . 1 . . . . 60 LYS CA . 6683 1 274 . 1 1 60 60 LYS CB C 13 31.25 0.20 . 1 . . . . 60 LYS CB . 6683 1 275 . 1 1 60 60 LYS N N 15 120.73 0.30 . 1 . . . . 60 LYS N . 6683 1 276 . 1 1 66 66 LEU C C 13 178.41 0.20 . 1 . . . . 66 LEU C . 6683 1 277 . 1 1 66 66 LEU CA C 13 57.20 0.20 . 1 . . . . 66 LEU CA . 6683 1 278 . 1 1 66 66 LEU CB C 13 39.79 0.20 . 1 . . . . 66 LEU CB . 6683 1 279 . 1 1 67 67 THR H H 1 8.58 0.03 . 1 . . . . 67 THR H . 6683 1 280 . 1 1 67 67 THR C C 13 177.05 0.20 . 1 . . . . 67 THR C . 6683 1 281 . 1 1 67 67 THR CA C 13 66.60 0.20 . 1 . . . . 67 THR CA . 6683 1 282 . 1 1 67 67 THR CB C 13 68.02 0.20 . 1 . . . . 67 THR CB . 6683 1 283 . 1 1 67 67 THR N N 15 119.14 0.30 . 1 . . . . 67 THR N . 6683 1 284 . 1 1 68 68 ASN H H 1 7.80 0.03 . 1 . . . . 68 ASN H . 6683 1 285 . 1 1 68 68 ASN C C 13 177.55 0.20 . 1 . . . . 68 ASN C . 6683 1 286 . 1 1 68 68 ASN CA C 13 56.56 0.20 . 1 . . . . 68 ASN CA . 6683 1 287 . 1 1 68 68 ASN CB C 13 38.43 0.20 . 1 . . . . 68 ASN CB . 6683 1 288 . 1 1 68 68 ASN N N 15 122.16 0.30 . 1 . . . . 68 ASN N . 6683 1 289 . 1 1 69 69 ALA H H 1 8.18 0.03 . 1 . . . . 69 ALA H . 6683 1 290 . 1 1 69 69 ALA C C 13 178.30 0.20 . 1 . . . . 69 ALA C . 6683 1 291 . 1 1 69 69 ALA CA C 13 55.75 0.20 . 1 . . . . 69 ALA CA . 6683 1 292 . 1 1 69 69 ALA CB C 13 17.33 0.20 . 1 . . . . 69 ALA CB . 6683 1 293 . 1 1 69 69 ALA N N 15 124.30 0.30 . 1 . . . . 69 ALA N . 6683 1 294 . 1 1 70 70 VAL H H 1 8.01 0.03 . 1 . . . . 70 VAL H . 6683 1 295 . 1 1 70 70 VAL C C 13 178.97 0.20 . 1 . . . . 70 VAL C . 6683 1 296 . 1 1 70 70 VAL CA C 13 66.61 0.20 . 1 . . . . 70 VAL CA . 6683 1 297 . 1 1 70 70 VAL CB C 13 31.12 0.20 . 1 . . . . 70 VAL CB . 6683 1 298 . 1 1 70 70 VAL N N 15 117.77 0.30 . 1 . . . . 70 VAL N . 6683 1 299 . 1 1 71 71 ALA H H 1 7.70 0.03 . 1 . . . . 71 ALA H . 6683 1 300 . 1 1 71 71 ALA C C 13 178.94 0.20 . 1 . . . . 71 ALA C . 6683 1 301 . 1 1 71 71 ALA CA C 13 53.96 0.20 . 1 . . . . 71 ALA CA . 6683 1 302 . 1 1 71 71 ALA CB C 13 17.51 0.20 . 1 . . . . 71 ALA CB . 6683 1 303 . 1 1 71 71 ALA N N 15 121.38 0.30 . 1 . . . . 71 ALA N . 6683 1 304 . 1 1 72 72 HIS H H 1 7.56 0.03 . 1 . . . . 72 HIS H . 6683 1 305 . 1 1 72 72 HIS C C 13 176.88 0.20 . 1 . . . . 72 HIS C . 6683 1 306 . 1 1 72 72 HIS CA C 13 54.86 0.20 . 1 . . . . 72 HIS CA . 6683 1 307 . 1 1 72 72 HIS CB C 13 28.23 0.20 . 1 . . . . 72 HIS CB . 6683 1 308 . 1 1 72 72 HIS N N 15 117.02 0.30 . 1 . . . . 72 HIS N . 6683 1 309 . 1 1 73 73 VAL H H 1 6.60 0.03 . 1 . . . . 73 VAL H . 6683 1 310 . 1 1 73 73 VAL C C 13 176.48 0.20 . 1 . . . . 73 VAL C . 6683 1 311 . 1 1 73 73 VAL CA C 13 65.06 0.20 . 1 . . . . 73 VAL CA . 6683 1 312 . 1 1 73 73 VAL CB C 13 31.34 0.20 . 1 . . . . 73 VAL CB . 6683 1 313 . 1 1 73 73 VAL N N 15 121.27 0.30 . 1 . . . . 73 VAL N . 6683 1 314 . 1 1 74 74 ASP H H 1 8.19 0.03 . 1 . . . . 74 ASP H . 6683 1 315 . 1 1 74 74 ASP C C 13 176.24 0.20 . 1 . . . . 74 ASP C . 6683 1 316 . 1 1 74 74 ASP CA C 13 55.32 0.20 . 1 . . . . 74 ASP CA . 6683 1 317 . 1 1 74 74 ASP CB C 13 40.86 0.20 . 1 . . . . 74 ASP CB . 6683 1 318 . 1 1 74 74 ASP N N 15 120.64 0.30 . 1 . . . . 74 ASP N . 6683 1 319 . 1 1 75 75 ASP H H 1 8.36 0.03 . 1 . . . . 75 ASP H . 6683 1 320 . 1 1 75 75 ASP C C 13 176.34 0.20 . 1 . . . . 75 ASP C . 6683 1 321 . 1 1 75 75 ASP CA C 13 52.97 0.20 . 1 . . . . 75 ASP CA . 6683 1 322 . 1 1 75 75 ASP CB C 13 41.10 0.20 . 1 . . . . 75 ASP CB . 6683 1 323 . 1 1 75 75 ASP N N 15 123.56 0.30 . 1 . . . . 75 ASP N . 6683 1 324 . 1 1 76 76 MET H H 1 8.69 0.03 . 1 . . . . 76 MET H . 6683 1 325 . 1 1 76 76 MET CA C 13 61.75 0.20 . 1 . . . . 76 MET CA . 6683 1 326 . 1 1 76 76 MET CB C 13 32.49 0.20 . 1 . . . . 76 MET CB . 6683 1 327 . 1 1 76 76 MET N N 15 123.82 0.30 . 1 . . . . 76 MET N . 6683 1 328 . 1 1 77 77 PRO C C 13 179.29 0.20 . 1 . . . . 77 PRO C . 6683 1 329 . 1 1 77 77 PRO CA C 13 66.45 0.20 . 1 . . . . 77 PRO CA . 6683 1 330 . 1 1 77 77 PRO CB C 13 30.27 0.20 . 1 . . . . 77 PRO CB . 6683 1 331 . 1 1 78 78 ASN H H 1 7.36 0.03 . 1 . . . . 78 ASN H . 6683 1 332 . 1 1 78 78 ASN C C 13 178.44 0.20 . 1 . . . . 78 ASN C . 6683 1 333 . 1 1 78 78 ASN CA C 13 55.71 0.20 . 1 . . . . 78 ASN CA . 6683 1 334 . 1 1 78 78 ASN CB C 13 38.59 0.20 . 1 . . . . 78 ASN CB . 6683 1 335 . 1 1 78 78 ASN N N 15 113.95 0.30 . 1 . . . . 78 ASN N . 6683 1 336 . 1 1 79 79 ALA H H 1 8.02 0.03 . 1 . . . . 79 ALA H . 6683 1 337 . 1 1 79 79 ALA C C 13 179.93 0.20 . 1 . . . . 79 ALA C . 6683 1 338 . 1 1 79 79 ALA CA C 13 55.01 0.20 . 1 . . . . 79 ALA CA . 6683 1 339 . 1 1 79 79 ALA CB C 13 17.97 0.20 . 1 . . . . 79 ALA CB . 6683 1 340 . 1 1 79 79 ALA N N 15 124.44 0.30 . 1 . . . . 79 ALA N . 6683 1 341 . 1 1 80 80 LEU H H 1 8.16 0.03 . 1 . . . . 80 LEU H . 6683 1 342 . 1 1 80 80 LEU C C 13 177.83 0.20 . 1 . . . . 80 LEU C . 6683 1 343 . 1 1 80 80 LEU CA C 13 53.95 0.20 . 1 . . . . 80 LEU CA . 6683 1 344 . 1 1 80 80 LEU CB C 13 40.93 0.20 . 1 . . . . 80 LEU CB . 6683 1 345 . 1 1 80 80 LEU N N 15 115.04 0.30 . 1 . . . . 80 LEU N . 6683 1 346 . 1 1 81 81 SER H H 1 7.28 0.03 . 1 . . . . 81 SER H . 6683 1 347 . 1 1 81 81 SER CA C 13 62.33 0.20 . 1 . . . . 81 SER CA . 6683 1 348 . 1 1 81 81 SER CB C 13 63.07 0.20 . 1 . . . . 81 SER CB . 6683 1 349 . 1 1 81 81 SER N N 15 118.40 0.30 . 1 . . . . 81 SER N . 6683 1 350 . 1 1 88 88 ALA C C 13 177.83 0.20 . 1 . . . . 88 ALA C . 6683 1 351 . 1 1 88 88 ALA CA C 13 53.70 0.20 . 1 . . . . 88 ALA CA . 6683 1 352 . 1 1 88 88 ALA CB C 13 18.10 0.20 . 1 . . . . 88 ALA CB . 6683 1 353 . 1 1 89 89 HIS H H 1 6.83 0.03 . 1 . . . . 89 HIS H . 6683 1 354 . 1 1 89 89 HIS CA C 13 54.85 0.20 . 1 . . . . 89 HIS CA . 6683 1 355 . 1 1 89 89 HIS CB C 13 30.20 0.20 . 1 . . . . 89 HIS CB . 6683 1 356 . 1 1 89 89 HIS N N 15 109.07 0.30 . 1 . . . . 89 HIS N . 6683 1 357 . 1 1 95 95 PRO C C 13 179.61 0.20 . 1 . . . . 95 PRO C . 6683 1 358 . 1 1 95 95 PRO CA C 13 65.90 0.20 . 1 . . . . 95 PRO CA . 6683 1 359 . 1 1 95 95 PRO CB C 13 32.87 0.20 . 1 . . . . 95 PRO CB . 6683 1 360 . 1 1 96 96 VAL H H 1 9.86 0.03 . 1 . . . . 96 VAL H . 6683 1 361 . 1 1 96 96 VAL CA C 13 66.40 0.20 . 1 . . . . 96 VAL CA . 6683 1 362 . 1 1 96 96 VAL CB C 13 31.43 0.20 . 1 . . . . 96 VAL CB . 6683 1 363 . 1 1 96 96 VAL N N 15 121.14 0.30 . 1 . . . . 96 VAL N . 6683 1 364 . 1 1 99 99 LYS C C 13 177.80 0.20 . 1 . . . . 99 LYS C . 6683 1 365 . 1 1 100 100 LEU H H 1 8.08 0.03 . 1 . . . . 100 LEU H . 6683 1 366 . 1 1 100 100 LEU CA C 13 57.64 0.20 . 1 . . . . 100 LEU CA . 6683 1 367 . 1 1 100 100 LEU CB C 13 39.79 0.20 . 1 . . . . 100 LEU CB . 6683 1 368 . 1 1 100 100 LEU N N 15 126.68 0.30 . 1 . . . . 100 LEU N . 6683 1 369 . 1 1 102 102 SER C C 13 175.36 0.20 . 1 . . . . 102 SER C . 6683 1 370 . 1 1 102 102 SER CA C 13 64.10 0.20 . 1 . . . . 102 SER CA . 6683 1 371 . 1 1 102 102 SER CB C 13 62.20 0.20 . 1 . . . . 102 SER CB . 6683 1 372 . 1 1 103 103 HIS H H 1 7.92 0.03 . 1 . . . . 103 HIS H . 6683 1 373 . 1 1 103 103 HIS C C 13 177.03 0.20 . 1 . . . . 103 HIS C . 6683 1 374 . 1 1 103 103 HIS CA C 13 60.02 0.20 . 1 . . . . 103 HIS CA . 6683 1 375 . 1 1 103 103 HIS CB C 13 30.89 0.20 . 1 . . . . 103 HIS CB . 6683 1 376 . 1 1 103 103 HIS N N 15 121.39 0.30 . 1 . . . . 103 HIS N . 6683 1 377 . 1 1 104 104 CYS H H 1 7.68 0.03 . 1 . . . . 104 CYS H . 6683 1 378 . 1 1 104 104 CYS C C 13 178.03 0.20 . 1 . . . . 104 CYS C . 6683 1 379 . 1 1 104 104 CYS CA C 13 65.72 0.20 . 1 . . . . 104 CYS CA . 6683 1 380 . 1 1 104 104 CYS CB C 13 27.44 0.20 . 1 . . . . 104 CYS CB . 6683 1 381 . 1 1 104 104 CYS N N 15 115.88 0.30 . 1 . . . . 104 CYS N . 6683 1 382 . 1 1 105 105 LEU H H 1 8.70 0.03 . 1 . . . . 105 LEU H . 6683 1 383 . 1 1 105 105 LEU C C 13 177.70 0.20 . 1 . . . . 105 LEU C . 6683 1 384 . 1 1 105 105 LEU CA C 13 58.17 0.20 . 1 . . . . 105 LEU CA . 6683 1 385 . 1 1 105 105 LEU CB C 13 40.74 0.20 . 1 . . . . 105 LEU CB . 6683 1 386 . 1 1 105 105 LEU N N 15 126.34 0.30 . 1 . . . . 105 LEU N . 6683 1 387 . 1 1 106 106 LEU H H 1 7.98 0.03 . 1 . . . . 106 LEU H . 6683 1 388 . 1 1 106 106 LEU C C 13 178.37 0.20 . 1 . . . . 106 LEU C . 6683 1 389 . 1 1 106 106 LEU CA C 13 58.80 0.20 . 1 . . . . 106 LEU CA . 6683 1 390 . 1 1 106 106 LEU CB C 13 40.94 0.20 . 1 . . . . 106 LEU CB . 6683 1 391 . 1 1 106 106 LEU N N 15 122.29 0.30 . 1 . . . . 106 LEU N . 6683 1 392 . 1 1 107 107 VAL H H 1 8.03 0.03 . 1 . . . . 107 VAL H . 6683 1 393 . 1 1 107 107 VAL C C 13 176.66 0.20 . 1 . . . . 107 VAL C . 6683 1 394 . 1 1 107 107 VAL CA C 13 66.63 0.20 . 1 . . . . 107 VAL CA . 6683 1 395 . 1 1 107 107 VAL CB C 13 31.56 0.20 . 1 . . . . 107 VAL CB . 6683 1 396 . 1 1 107 107 VAL N N 15 118.51 0.30 . 1 . . . . 107 VAL N . 6683 1 397 . 1 1 108 108 THR H H 1 7.05 0.03 . 1 . . . . 108 THR H . 6683 1 398 . 1 1 108 108 THR C C 13 176.13 0.20 . 1 . . . . 108 THR C . 6683 1 399 . 1 1 108 108 THR CA C 13 67.46 0.20 . 1 . . . . 108 THR CA . 6683 1 400 . 1 1 108 108 THR CB C 13 68.28 0.20 . 1 . . . . 108 THR CB . 6683 1 401 . 1 1 108 108 THR N N 15 116.12 0.30 . 1 . . . . 108 THR N . 6683 1 402 . 1 1 109 109 LEU H H 1 7.87 0.03 . 1 . . . . 109 LEU H . 6683 1 403 . 1 1 109 109 LEU C C 13 177.94 0.20 . 1 . . . . 109 LEU C . 6683 1 404 . 1 1 109 109 LEU CA C 13 58.33 0.20 . 1 . . . . 109 LEU CA . 6683 1 405 . 1 1 109 109 LEU CB C 13 40.05 0.20 . 1 . . . . 109 LEU CB . 6683 1 406 . 1 1 109 109 LEU N N 15 121.60 0.30 . 1 . . . . 109 LEU N . 6683 1 407 . 1 1 110 110 ALA H H 1 7.80 0.03 . 1 . . . . 110 ALA H . 6683 1 408 . 1 1 110 110 ALA C C 13 178.44 0.20 . 1 . . . . 110 ALA C . 6683 1 409 . 1 1 110 110 ALA CA C 13 55.16 0.20 . 1 . . . . 110 ALA CA . 6683 1 410 . 1 1 110 110 ALA CB C 13 17.72 0.20 . 1 . . . . 110 ALA CB . 6683 1 411 . 1 1 110 110 ALA N N 15 122.94 0.30 . 1 . . . . 110 ALA N . 6683 1 412 . 1 1 111 111 ALA H H 1 7.34 0.03 . 1 . . . . 111 ALA H . 6683 1 413 . 1 1 111 111 ALA C C 13 179.76 0.20 . 1 . . . . 111 ALA C . 6683 1 414 . 1 1 111 111 ALA CA C 13 53.04 0.20 . 1 . . . . 111 ALA CA . 6683 1 415 . 1 1 111 111 ALA CB C 13 17.14 0.20 . 1 . . . . 111 ALA CB . 6683 1 416 . 1 1 111 111 ALA N N 15 114.88 0.30 . 1 . . . . 111 ALA N . 6683 1 417 . 1 1 112 112 HIS H H 1 7.08 0.03 . 1 . . . . 112 HIS H . 6683 1 418 . 1 1 112 112 HIS C C 13 174.81 0.20 . 1 . . . . 112 HIS C . 6683 1 419 . 1 1 112 112 HIS CA C 13 56.68 0.20 . 1 . . . . 112 HIS CA . 6683 1 420 . 1 1 112 112 HIS CB C 13 30.23 0.20 . 1 . . . . 112 HIS CB . 6683 1 421 . 1 1 112 112 HIS N N 15 113.61 0.30 . 1 . . . . 112 HIS N . 6683 1 422 . 1 1 113 113 LEU H H 1 7.90 0.03 . 1 . . . . 113 LEU H . 6683 1 423 . 1 1 113 113 LEU CA C 13 52.20 0.20 . 1 . . . . 113 LEU CA . 6683 1 424 . 1 1 113 113 LEU CB C 13 41.14 0.20 . 1 . . . . 113 LEU CB . 6683 1 425 . 1 1 113 113 LEU N N 15 122.28 0.30 . 1 . . . . 113 LEU N . 6683 1 426 . 1 1 114 114 PRO C C 13 180.61 0.20 . 1 . . . . 114 PRO C . 6683 1 427 . 1 1 114 114 PRO CA C 13 65.54 0.20 . 1 . . . . 114 PRO CA . 6683 1 428 . 1 1 114 114 PRO CB C 13 29.85 0.20 . 1 . . . . 114 PRO CB . 6683 1 429 . 1 1 115 115 ALA H H 1 8.16 0.03 . 1 . . . . 115 ALA H . 6683 1 430 . 1 1 115 115 ALA C C 13 179.86 0.20 . 1 . . . . 115 ALA C . 6683 1 431 . 1 1 115 115 ALA CA C 13 54.11 0.20 . 1 . . . . 115 ALA CA . 6683 1 432 . 1 1 115 115 ALA CB C 13 17.75 0.20 . 1 . . . . 115 ALA CB . 6683 1 433 . 1 1 115 115 ALA N N 15 119.68 0.30 . 1 . . . . 115 ALA N . 6683 1 434 . 1 1 116 116 GLU H H 1 7.80 0.03 . 1 . . . . 116 GLU H . 6683 1 435 . 1 1 116 116 GLU C C 13 178.01 0.20 . 1 . . . . 116 GLU C . 6683 1 436 . 1 1 116 116 GLU CA C 13 57.36 0.20 . 1 . . . . 116 GLU CA . 6683 1 437 . 1 1 116 116 GLU CB C 13 28.65 0.20 . 1 . . . . 116 GLU CB . 6683 1 438 . 1 1 116 116 GLU N N 15 115.79 0.30 . 1 . . . . 116 GLU N . 6683 1 439 . 1 1 117 117 PHE H H 1 7.67 0.03 . 1 . . . . 117 PHE H . 6683 1 440 . 1 1 117 117 PHE C C 13 175.63 0.20 . 1 . . . . 117 PHE C . 6683 1 441 . 1 1 117 117 PHE CA C 13 57.61 0.20 . 1 . . . . 117 PHE CA . 6683 1 442 . 1 1 117 117 PHE CB C 13 37.34 0.20 . 1 . . . . 117 PHE CB . 6683 1 443 . 1 1 117 117 PHE N N 15 123.71 0.30 . 1 . . . . 117 PHE N . 6683 1 444 . 1 1 118 118 THR H H 1 7.97 0.03 . 1 . . . . 118 THR H . 6683 1 445 . 1 1 118 118 THR CA C 13 60.50 0.20 . 1 . . . . 118 THR CA . 6683 1 446 . 1 1 118 118 THR CB C 13 67.44 0.20 . 1 . . . . 118 THR CB . 6683 1 447 . 1 1 118 118 THR N N 15 116.71 0.30 . 1 . . . . 118 THR N . 6683 1 448 . 1 1 119 119 PRO C C 13 177.09 0.20 . 1 . . . . 119 PRO C . 6683 1 449 . 1 1 119 119 PRO CA C 13 66.74 0.20 . 1 . . . . 119 PRO CA . 6683 1 450 . 1 1 119 119 PRO CB C 13 31.26 0.20 . 1 . . . . 119 PRO CB . 6683 1 451 . 1 1 120 120 ALA H H 1 8.41 0.03 . 1 . . . . 120 ALA H . 6683 1 452 . 1 1 120 120 ALA C C 13 180.72 0.20 . 1 . . . . 120 ALA C . 6683 1 453 . 1 1 120 120 ALA CA C 13 54.64 0.20 . 1 . . . . 120 ALA CA . 6683 1 454 . 1 1 120 120 ALA CB C 13 18.22 0.20 . 1 . . . . 120 ALA CB . 6683 1 455 . 1 1 120 120 ALA N N 15 117.51 0.30 . 1 . . . . 120 ALA N . 6683 1 456 . 1 1 121 121 VAL H H 1 7.26 0.03 . 1 . . . . 121 VAL H . 6683 1 457 . 1 1 121 121 VAL C C 13 177.37 0.20 . 1 . . . . 121 VAL C . 6683 1 458 . 1 1 121 121 VAL CA C 13 66.99 0.20 . 1 . . . . 121 VAL CA . 6683 1 459 . 1 1 121 121 VAL CB C 13 31.22 0.20 . 1 . . . . 121 VAL CB . 6683 1 460 . 1 1 121 121 VAL N N 15 121.28 0.30 . 1 . . . . 121 VAL N . 6683 1 461 . 1 1 122 122 HIS H H 1 8.47 0.03 . 1 . . . . 122 HIS H . 6683 1 462 . 1 1 122 122 HIS C C 13 177.98 0.20 . 1 . . . . 122 HIS C . 6683 1 463 . 1 1 122 122 HIS CA C 13 57.52 0.20 . 1 . . . . 122 HIS CA . 6683 1 464 . 1 1 122 122 HIS CB C 13 32.30 0.20 . 1 . . . . 122 HIS CB . 6683 1 465 . 1 1 122 122 HIS N N 15 123.24 0.30 . 1 . . . . 122 HIS N . 6683 1 466 . 1 1 123 123 ALA H H 1 7.96 0.03 . 1 . . . . 123 ALA H . 6683 1 467 . 1 1 123 123 ALA C C 13 180.04 0.20 . 1 . . . . 123 ALA C . 6683 1 468 . 1 1 123 123 ALA CA C 13 55.97 0.20 . 1 . . . . 123 ALA CA . 6683 1 469 . 1 1 123 123 ALA CB C 13 17.56 0.20 . 1 . . . . 123 ALA CB . 6683 1 470 . 1 1 123 123 ALA N N 15 121.87 0.30 . 1 . . . . 123 ALA N . 6683 1 471 . 1 1 124 124 SER H H 1 8.20 0.03 . 1 . . . . 124 SER H . 6683 1 472 . 1 1 124 124 SER C C 13 176.48 0.20 . 1 . . . . 124 SER C . 6683 1 473 . 1 1 124 124 SER CA C 13 62.80 0.20 . 1 . . . . 124 SER CA . 6683 1 474 . 1 1 124 124 SER N N 15 116.58 0.30 . 1 . . . . 124 SER N . 6683 1 475 . 1 1 125 125 LEU H H 1 9.27 0.03 . 1 . . . . 125 LEU H . 6683 1 476 . 1 1 125 125 LEU C C 13 179.04 0.20 . 1 . . . . 125 LEU C . 6683 1 477 . 1 1 125 125 LEU CA C 13 57.93 0.20 . 1 . . . . 125 LEU CA . 6683 1 478 . 1 1 125 125 LEU CB C 13 42.24 0.20 . 1 . . . . 125 LEU CB . 6683 1 479 . 1 1 125 125 LEU N N 15 122.79 0.30 . 1 . . . . 125 LEU N . 6683 1 480 . 1 1 126 126 ASP H H 1 8.62 0.03 . 1 . . . . 126 ASP H . 6683 1 481 . 1 1 126 126 ASP C C 13 180.18 0.20 . 1 . . . . 126 ASP C . 6683 1 482 . 1 1 126 126 ASP CA C 13 58.81 0.20 . 1 . . . . 126 ASP CA . 6683 1 483 . 1 1 126 126 ASP CB C 13 42.53 0.20 . 1 . . . . 126 ASP CB . 6683 1 484 . 1 1 126 126 ASP N N 15 121.87 0.30 . 1 . . . . 126 ASP N . 6683 1 485 . 1 1 127 127 LYS H H 1 8.21 0.03 . 1 . . . . 127 LYS H . 6683 1 486 . 1 1 127 127 LYS C C 13 180.40 0.20 . 1 . . . . 127 LYS C . 6683 1 487 . 1 1 127 127 LYS CA C 13 60.42 0.20 . 1 . . . . 127 LYS CA . 6683 1 488 . 1 1 127 127 LYS CB C 13 32.06 0.20 . 1 . . . . 127 LYS CB . 6683 1 489 . 1 1 127 127 LYS N N 15 119.30 0.30 . 1 . . . . 127 LYS N . 6683 1 490 . 1 1 128 128 PHE H H 1 8.99 0.03 . 1 . . . . 128 PHE H . 6683 1 491 . 1 1 128 128 PHE C C 13 176.84 0.20 . 1 . . . . 128 PHE C . 6683 1 492 . 1 1 128 128 PHE CA C 13 61.20 0.20 . 1 . . . . 128 PHE CA . 6683 1 493 . 1 1 128 128 PHE CB C 13 39.55 0.20 . 1 . . . . 128 PHE CB . 6683 1 494 . 1 1 128 128 PHE N N 15 123.73 0.30 . 1 . . . . 128 PHE N . 6683 1 495 . 1 1 129 129 LEU H H 1 8.89 0.03 . 1 . . . . 129 LEU H . 6683 1 496 . 1 1 129 129 LEU C C 13 180.72 0.20 . 1 . . . . 129 LEU C . 6683 1 497 . 1 1 129 129 LEU CA C 13 57.88 0.20 . 1 . . . . 129 LEU CA . 6683 1 498 . 1 1 129 129 LEU CB C 13 39.18 0.20 . 1 . . . . 129 LEU CB . 6683 1 499 . 1 1 129 129 LEU N N 15 122.40 0.30 . 1 . . . . 129 LEU N . 6683 1 500 . 1 1 130 130 ALA H H 1 8.30 0.03 . 1 . . . . 130 ALA H . 6683 1 501 . 1 1 130 130 ALA C C 13 180.89 0.20 . 1 . . . . 130 ALA C . 6683 1 502 . 1 1 130 130 ALA CA C 13 55.34 0.20 . 1 . . . . 130 ALA CA . 6683 1 503 . 1 1 130 130 ALA CB C 13 17.23 0.20 . 1 . . . . 130 ALA CB . 6683 1 504 . 1 1 130 130 ALA N N 15 125.68 0.30 . 1 . . . . 130 ALA N . 6683 1 505 . 1 1 131 131 SER H H 1 8.26 0.03 . 1 . . . . 131 SER H . 6683 1 506 . 1 1 131 131 SER C C 13 177.33 0.20 . 1 . . . . 131 SER C . 6683 1 507 . 1 1 131 131 SER CA C 13 62.62 0.20 . 1 . . . . 131 SER CA . 6683 1 508 . 1 1 131 131 SER N N 15 119.62 0.30 . 1 . . . . 131 SER N . 6683 1 509 . 1 1 132 132 VAL H H 1 8.37 0.03 . 1 . . . . 132 VAL H . 6683 1 510 . 1 1 132 132 VAL CA C 13 66.90 0.20 . 1 . . . . 132 VAL CA . 6683 1 511 . 1 1 132 132 VAL CB C 13 31.34 0.20 . 1 . . . . 132 VAL CB . 6683 1 512 . 1 1 132 132 VAL N N 15 124.30 0.30 . 1 . . . . 132 VAL N . 6683 1 513 . 1 1 133 133 SER C C 13 176.48 0.20 . 1 . . . . 133 SER C . 6683 1 514 . 1 1 133 133 SER CA C 13 63.85 0.20 . 1 . . . . 133 SER CA . 6683 1 515 . 1 1 133 133 SER CB C 13 62.58 0.20 . 1 . . . . 133 SER CB . 6683 1 516 . 1 1 134 134 THR H H 1 8.46 0.03 . 1 . . . . 134 THR H . 6683 1 517 . 1 1 134 134 THR C C 13 177.30 0.20 . 1 . . . . 134 THR C . 6683 1 518 . 1 1 134 134 THR CA C 13 66.75 0.20 . 1 . . . . 134 THR CA . 6683 1 519 . 1 1 134 134 THR CB C 13 68.42 0.20 . 1 . . . . 134 THR CB . 6683 1 520 . 1 1 134 134 THR N N 15 121.74 0.30 . 1 . . . . 134 THR N . 6683 1 521 . 1 1 135 135 VAL H H 1 8.16 0.03 . 1 . . . . 135 VAL H . 6683 1 522 . 1 1 135 135 VAL CA C 13 67.12 0.20 . 1 . . . . 135 VAL CA . 6683 1 523 . 1 1 135 135 VAL CB C 13 30.57 0.20 . 1 . . . . 135 VAL CB . 6683 1 524 . 1 1 135 135 VAL N N 15 123.53 0.30 . 1 . . . . 135 VAL N . 6683 1 525 . 1 1 136 136 LEU C C 13 178.47 0.20 . 1 . . . . 136 LEU C . 6683 1 526 . 1 1 137 137 THR H H 1 7.35 0.03 . 1 . . . . 137 THR H . 6683 1 527 . 1 1 137 137 THR C C 13 176.98 0.20 . 1 . . . . 137 THR C . 6683 1 528 . 1 1 137 137 THR CA C 13 60.82 0.20 . 1 . . . . 137 THR CA . 6683 1 529 . 1 1 137 137 THR CB C 13 69.09 0.20 . 1 . . . . 137 THR CB . 6683 1 530 . 1 1 137 137 THR N N 15 107.42 0.30 . 1 . . . . 137 THR N . 6683 1 531 . 1 1 138 138 SER H H 1 7.46 0.03 . 1 . . . . 138 SER H . 6683 1 532 . 1 1 138 138 SER C C 13 176.52 0.20 . 1 . . . . 138 SER C . 6683 1 533 . 1 1 138 138 SER CA C 13 61.88 0.20 . 1 . . . . 138 SER CA . 6683 1 534 . 1 1 138 138 SER CB C 13 63.32 0.20 . 1 . . . . 138 SER CB . 6683 1 535 . 1 1 138 138 SER N N 15 120.68 0.30 . 1 . . . . 138 SER N . 6683 1 536 . 1 1 139 139 LYS H H 1 8.71 0.03 . 1 . . . . 139 LYS H . 6683 1 537 . 1 1 139 139 LYS C C 13 176.16 0.20 . 1 . . . . 139 LYS C . 6683 1 538 . 1 1 139 139 LYS CA C 13 54.79 0.20 . 1 . . . . 139 LYS CA . 6683 1 539 . 1 1 139 139 LYS CB C 13 31.07 0.20 . 1 . . . . 139 LYS CB . 6683 1 540 . 1 1 139 139 LYS N N 15 122.63 0.30 . 1 . . . . 139 LYS N . 6683 1 541 . 1 1 140 140 TYR H H 1 7.39 0.03 . 1 . . . . 140 TYR H . 6683 1 542 . 1 1 140 140 TYR C C 13 176.20 0.20 . 1 . . . . 140 TYR C . 6683 1 543 . 1 1 140 140 TYR CA C 13 62.01 0.20 . 1 . . . . 140 TYR CA . 6683 1 544 . 1 1 140 140 TYR CB C 13 37.46 0.20 . 1 . . . . 140 TYR CB . 6683 1 545 . 1 1 140 140 TYR N N 15 122.33 0.30 . 1 . . . . 140 TYR N . 6683 1 546 . 1 1 141 141 ARG H H 1 7.43 0.03 . 1 . . . . 141 ARG H . 6683 1 547 . 1 1 141 141 ARG CA C 13 56.62 0.20 . 1 . . . . 141 ARG CA . 6683 1 548 . 1 1 141 141 ARG CB C 13 30.84 0.20 . 1 . . . . 141 ARG CB . 6683 1 549 . 1 1 141 141 ARG N N 15 115.51 0.30 . 1 . . . . 141 ARG N . 6683 1 550 . 3 2 2 2 HIS C C 13 174.40 0.20 . 1 . . . . 2 HIS C . 6683 1 551 . 3 2 2 2 HIS CA C 13 55.59 0.20 . 1 . . . . 2 HIS CA . 6683 1 552 . 3 2 2 2 HIS CB C 13 30.02 0.20 . 1 . . . . 2 HIS CB . 6683 1 553 . 3 2 3 3 LEU H H 1 8.28 0.03 . 1 . . . . 3 LEU H . 6683 1 554 . 3 2 3 3 LEU C C 13 177.78 0.20 . 1 . . . . 3 LEU C . 6683 1 555 . 3 2 3 3 LEU CA C 13 53.81 0.20 . 1 . . . . 3 LEU CA . 6683 1 556 . 3 2 3 3 LEU CB C 13 43.47 0.20 . 1 . . . . 3 LEU CB . 6683 1 557 . 3 2 3 3 LEU N N 15 126.95 0.30 . 1 . . . . 3 LEU N . 6683 1 558 . 3 2 4 4 THR H H 1 9.22 0.03 . 1 . . . . 4 THR H . 6683 1 559 . 3 2 4 4 THR CA C 13 60.49 0.20 . 1 . . . . 4 THR CA . 6683 1 560 . 3 2 4 4 THR CB C 13 67.79 0.20 . 1 . . . . 4 THR CB . 6683 1 561 . 3 2 4 4 THR N N 15 116.63 0.30 . 1 . . . . 4 THR N . 6683 1 562 . 3 2 5 5 PRO C C 13 180.03 0.20 . 1 . . . . 5 PRO C . 6683 1 563 . 3 2 5 5 PRO CA C 13 66.19 0.20 . 1 . . . . 5 PRO CA . 6683 1 564 . 3 2 5 5 PRO CB C 13 30.88 0.20 . 1 . . . . 5 PRO CB . 6683 1 565 . 3 2 6 6 GLU H H 1 8.63 0.03 . 1 . . . . 6 GLU H . 6683 1 566 . 3 2 6 6 GLU C C 13 180.37 0.20 . 1 . . . . 6 GLU C . 6683 1 567 . 3 2 6 6 GLU CA C 13 60.03 0.20 . 1 . . . . 6 GLU CA . 6683 1 568 . 3 2 6 6 GLU CB C 13 28.29 0.20 . 1 . . . . 6 GLU CB . 6683 1 569 . 3 2 6 6 GLU N N 15 118.61 0.30 . 1 . . . . 6 GLU N . 6683 1 570 . 3 2 7 7 GLU H H 1 7.75 0.03 . 1 . . . . 7 GLU H . 6683 1 571 . 3 2 7 7 GLU C C 13 178.92 0.20 . 1 . . . . 7 GLU C . 6683 1 572 . 3 2 7 7 GLU CA C 13 58.92 0.20 . 1 . . . . 7 GLU CA . 6683 1 573 . 3 2 7 7 GLU CB C 13 30.53 0.20 . 1 . . . . 7 GLU CB . 6683 1 574 . 3 2 7 7 GLU N N 15 122.93 0.30 . 1 . . . . 7 GLU N . 6683 1 575 . 3 2 8 8 LYS H H 1 8.55 0.03 . 1 . . . . 8 LYS H . 6683 1 576 . 3 2 8 8 LYS C C 13 179.60 0.20 . 1 . . . . 8 LYS C . 6683 1 577 . 3 2 8 8 LYS CA C 13 60.50 0.20 . 1 . . . . 8 LYS CA . 6683 1 578 . 3 2 8 8 LYS CB C 13 31.60 0.20 . 1 . . . . 8 LYS CB . 6683 1 579 . 3 2 8 8 LYS N N 15 119.85 0.30 . 1 . . . . 8 LYS N . 6683 1 580 . 3 2 9 9 SER H H 1 8.03 0.03 . 1 . . . . 9 SER H . 6683 1 581 . 3 2 9 9 SER C C 13 176.62 0.20 . 1 . . . . 9 SER C . 6683 1 582 . 3 2 9 9 SER CA C 13 61.40 0.20 . 1 . . . . 9 SER CA . 6683 1 583 . 3 2 9 9 SER CB C 13 62.40 0.20 . 1 . . . . 9 SER CB . 6683 1 584 . 3 2 9 9 SER N N 15 115.47 0.30 . 1 . . . . 9 SER N . 6683 1 585 . 3 2 10 10 ALA H H 1 7.65 0.03 . 1 . . . . 10 ALA H . 6683 1 586 . 3 2 10 10 ALA C C 13 181.31 0.20 . 1 . . . . 10 ALA C . 6683 1 587 . 3 2 10 10 ALA CA C 13 54.85 0.20 . 1 . . . . 10 ALA CA . 6683 1 588 . 3 2 10 10 ALA CB C 13 17.88 0.20 . 1 . . . . 10 ALA CB . 6683 1 589 . 3 2 10 10 ALA N N 15 124.94 0.30 . 1 . . . . 10 ALA N . 6683 1 590 . 3 2 11 11 VAL H H 1 8.14 0.03 . 1 . . . . 11 VAL H . 6683 1 591 . 3 2 11 11 VAL C C 13 180.36 0.20 . 1 . . . . 11 VAL C . 6683 1 592 . 3 2 11 11 VAL CA C 13 65.92 0.20 . 1 . . . . 11 VAL CA . 6683 1 593 . 3 2 11 11 VAL CB C 13 31.09 0.20 . 1 . . . . 11 VAL CB . 6683 1 594 . 3 2 11 11 VAL N N 15 117.55 0.30 . 1 . . . . 11 VAL N . 6683 1 595 . 3 2 12 12 THR H H 1 8.33 0.03 . 1 . . . . 12 THR H . 6683 1 596 . 3 2 12 12 THR C C 13 177.39 0.20 . 1 . . . . 12 THR C . 6683 1 597 . 3 2 12 12 THR CA C 13 65.88 0.20 . 1 . . . . 12 THR CA . 6683 1 598 . 3 2 12 12 THR CB C 13 68.46 0.20 . 1 . . . . 12 THR CB . 6683 1 599 . 3 2 12 12 THR N N 15 116.51 0.30 . 1 . . . . 12 THR N . 6683 1 600 . 3 2 13 13 ALA H H 1 8.35 0.03 . 1 . . . . 13 ALA H . 6683 1 601 . 3 2 13 13 ALA C C 13 181.08 0.20 . 1 . . . . 13 ALA C . 6683 1 602 . 3 2 13 13 ALA CA C 13 55.02 0.20 . 1 . . . . 13 ALA CA . 6683 1 603 . 3 2 13 13 ALA CB C 13 17.61 0.20 . 1 . . . . 13 ALA CB . 6683 1 604 . 3 2 13 13 ALA N N 15 126.62 0.30 . 1 . . . . 13 ALA N . 6683 1 605 . 3 2 14 14 LEU H H 1 7.24 0.03 . 1 . . . . 14 LEU H . 6683 1 606 . 3 2 14 14 LEU C C 13 179.35 0.20 . 1 . . . . 14 LEU C . 6683 1 607 . 3 2 14 14 LEU CA C 13 57.80 0.20 . 1 . . . . 14 LEU CA . 6683 1 608 . 3 2 14 14 LEU CB C 13 40.83 0.20 . 1 . . . . 14 LEU CB . 6683 1 609 . 3 2 14 14 LEU N N 15 118.66 0.30 . 1 . . . . 14 LEU N . 6683 1 610 . 3 2 15 15 TRP H H 1 8.03 0.03 . 1 . . . . 15 TRP H . 6683 1 611 . 3 2 15 15 TRP C C 13 179.31 0.20 . 1 . . . . 15 TRP C . 6683 1 612 . 3 2 15 15 TRP CA C 13 59.95 0.20 . 1 . . . . 15 TRP CA . 6683 1 613 . 3 2 15 15 TRP CB C 13 28.38 0.20 . 1 . . . . 15 TRP CB . 6683 1 614 . 3 2 15 15 TRP N N 15 119.23 0.30 . 1 . . . . 15 TRP N . 6683 1 615 . 3 2 16 16 GLY H H 1 7.67 0.03 . 1 . . . . 16 GLY H . 6683 1 616 . 3 2 16 16 GLY C C 13 175.04 0.20 . 1 . . . . 16 GLY C . 6683 1 617 . 3 2 16 16 GLY CA C 13 46.16 0.20 . 1 . . . . 16 GLY CA . 6683 1 618 . 3 2 16 16 GLY N N 15 103.32 0.30 . 1 . . . . 16 GLY N . 6683 1 619 . 3 2 17 17 LYS H H 1 7.64 0.03 . 1 . . . . 17 LYS H . 6683 1 620 . 3 2 17 17 LYS C C 13 177.10 0.20 . 1 . . . . 17 LYS C . 6683 1 621 . 3 2 17 17 LYS CA C 13 55.84 0.20 . 1 . . . . 17 LYS CA . 6683 1 622 . 3 2 17 17 LYS CB C 13 32.77 0.20 . 1 . . . . 17 LYS CB . 6683 1 623 . 3 2 17 17 LYS N N 15 119.01 0.30 . 1 . . . . 17 LYS N . 6683 1 624 . 3 2 18 18 VAL H H 1 7.30 0.03 . 1 . . . . 18 VAL H . 6683 1 625 . 3 2 18 18 VAL C C 13 175.43 0.20 . 1 . . . . 18 VAL C . 6683 1 626 . 3 2 18 18 VAL CA C 13 62.80 0.20 . 1 . . . . 18 VAL CA . 6683 1 627 . 3 2 18 18 VAL CB C 13 31.43 0.20 . 1 . . . . 18 VAL CB . 6683 1 628 . 3 2 18 18 VAL N N 15 122.91 0.30 . 1 . . . . 18 VAL N . 6683 1 629 . 3 2 19 19 ASN H H 1 8.43 0.03 . 1 . . . . 19 ASN H . 6683 1 630 . 3 2 19 19 ASN C C 13 175.53 0.20 . 1 . . . . 19 ASN C . 6683 1 631 . 3 2 19 19 ASN CA C 13 51.54 0.20 . 1 . . . . 19 ASN CA . 6683 1 632 . 3 2 19 19 ASN CB C 13 36.94 0.20 . 1 . . . . 19 ASN CB . 6683 1 633 . 3 2 19 19 ASN N N 15 127.59 0.30 . 1 . . . . 19 ASN N . 6683 1 634 . 3 2 20 20 VAL H H 1 8.31 0.03 . 1 . . . . 20 VAL H . 6683 1 635 . 3 2 20 20 VAL C C 13 177.22 0.20 . 1 . . . . 20 VAL C . 6683 1 636 . 3 2 20 20 VAL CA C 13 66.10 0.20 . 1 . . . . 20 VAL CA . 6683 1 637 . 3 2 20 20 VAL CB C 13 31.14 0.20 . 1 . . . . 20 VAL CB . 6683 1 638 . 3 2 20 20 VAL N N 15 127.26 0.30 . 1 . . . . 20 VAL N . 6683 1 639 . 3 2 21 21 ASP H H 1 7.82 0.03 . 1 . . . . 21 ASP H . 6683 1 640 . 3 2 21 21 ASP C C 13 178.82 0.20 . 1 . . . . 21 ASP C . 6683 1 641 . 3 2 21 21 ASP CA C 13 57.18 0.20 . 1 . . . . 21 ASP CA . 6683 1 642 . 3 2 21 21 ASP CB C 13 39.84 0.20 . 1 . . . . 21 ASP CB . 6683 1 643 . 3 2 21 21 ASP N N 15 119.96 0.30 . 1 . . . . 21 ASP N . 6683 1 644 . 3 2 22 22 GLU H H 1 7.33 0.03 . 1 . . . . 22 GLU H . 6683 1 645 . 3 2 22 22 GLU C C 13 179.42 0.20 . 1 . . . . 22 GLU C . 6683 1 646 . 3 2 22 22 GLU CA C 13 58.18 0.20 . 1 . . . . 22 GLU CA . 6683 1 647 . 3 2 22 22 GLU CB C 13 30.05 0.20 . 1 . . . . 22 GLU CB . 6683 1 648 . 3 2 22 22 GLU N N 15 120.53 0.30 . 1 . . . . 22 GLU N . 6683 1 649 . 3 2 23 23 VAL H H 1 8.29 0.03 . 1 . . . . 23 VAL H . 6683 1 650 . 3 2 23 23 VAL C C 13 178.02 0.20 . 1 . . . . 23 VAL C . 6683 1 651 . 3 2 23 23 VAL CA C 13 65.92 0.20 . 1 . . . . 23 VAL CA . 6683 1 652 . 3 2 23 23 VAL CB C 13 31.02 0.20 . 1 . . . . 23 VAL CB . 6683 1 653 . 3 2 23 23 VAL N N 15 120.30 0.30 . 1 . . . . 23 VAL N . 6683 1 654 . 3 2 24 24 GLY H H 1 8.54 0.03 . 1 . . . . 24 GLY H . 6683 1 655 . 3 2 24 24 GLY C C 13 176.64 0.20 . 1 . . . . 24 GLY C . 6683 1 656 . 3 2 24 24 GLY CA C 13 48.06 0.20 . 1 . . . . 24 GLY CA . 6683 1 657 . 3 2 24 24 GLY N N 15 110.02 0.30 . 1 . . . . 24 GLY N . 6683 1 658 . 3 2 25 25 GLY H H 1 7.82 0.03 . 1 . . . . 25 GLY H . 6683 1 659 . 3 2 25 25 GLY C C 13 176.66 0.20 . 1 . . . . 25 GLY C . 6683 1 660 . 3 2 25 25 GLY CA C 13 47.91 0.20 . 1 . . . . 25 GLY CA . 6683 1 661 . 3 2 25 25 GLY N N 15 109.61 0.30 . 1 . . . . 25 GLY N . 6683 1 662 . 3 2 26 26 GLU H H 1 7.78 0.03 . 1 . . . . 26 GLU H . 6683 1 663 . 3 2 26 26 GLU C C 13 178.99 0.20 . 1 . . . . 26 GLU C . 6683 1 664 . 3 2 26 26 GLU CA C 13 59.08 0.20 . 1 . . . . 26 GLU CA . 6683 1 665 . 3 2 26 26 GLU CB C 13 29.55 0.20 . 1 . . . . 26 GLU CB . 6683 1 666 . 3 2 26 26 GLU N N 15 123.52 0.30 . 1 . . . . 26 GLU N . 6683 1 667 . 3 2 27 27 ALA H H 1 9.07 0.03 . 1 . . . . 27 ALA H . 6683 1 668 . 3 2 27 27 ALA CA C 13 55.37 0.20 . 1 . . . . 27 ALA CA . 6683 1 669 . 3 2 27 27 ALA CB C 13 17.51 0.20 . 1 . . . . 27 ALA CB . 6683 1 670 . 3 2 27 27 ALA N N 15 121.15 0.30 . 1 . . . . 27 ALA N . 6683 1 671 . 3 2 28 28 LEU C C 13 179.00 0.20 . 1 . . . . 28 LEU C . 6683 1 672 . 3 2 28 28 LEU CA C 13 57.66 0.20 . 1 . . . . 28 LEU CA . 6683 1 673 . 3 2 28 28 LEU CB C 13 41.12 0.20 . 1 . . . . 28 LEU CB . 6683 1 674 . 3 2 29 29 GLY H H 1 8.26 0.03 . 1 . . . . 29 GLY H . 6683 1 675 . 3 2 29 29 GLY C C 13 175.53 0.20 . 1 . . . . 29 GLY C . 6683 1 676 . 3 2 29 29 GLY CA C 13 47.90 0.20 . 1 . . . . 29 GLY CA . 6683 1 677 . 3 2 29 29 GLY N N 15 105.49 0.30 . 1 . . . . 29 GLY N . 6683 1 678 . 3 2 30 30 ARG H H 1 8.45 0.03 . 1 . . . . 30 ARG H . 6683 1 679 . 3 2 30 30 ARG C C 13 178.62 0.20 . 1 . . . . 30 ARG C . 6683 1 680 . 3 2 30 30 ARG CA C 13 60.83 0.20 . 1 . . . . 30 ARG CA . 6683 1 681 . 3 2 30 30 ARG CB C 13 30.06 0.20 . 1 . . . . 30 ARG CB . 6683 1 682 . 3 2 30 30 ARG N N 15 118.25 0.30 . 1 . . . . 30 ARG N . 6683 1 683 . 3 2 31 31 LEU H H 1 8.52 0.03 . 1 . . . . 31 LEU H . 6683 1 684 . 3 2 31 31 LEU C C 13 177.19 0.20 . 1 . . . . 31 LEU C . 6683 1 685 . 3 2 31 31 LEU CA C 13 60.28 0.20 . 1 . . . . 31 LEU CA . 6683 1 686 . 3 2 31 31 LEU CB C 13 41.97 0.20 . 1 . . . . 31 LEU CB . 6683 1 687 . 3 2 31 31 LEU N N 15 122.40 0.30 . 1 . . . . 31 LEU N . 6683 1 688 . 3 2 32 32 LEU H H 1 7.52 0.03 . 1 . . . . 32 LEU H . 6683 1 689 . 3 2 32 32 LEU C C 13 178.67 0.20 . 1 . . . . 32 LEU C . 6683 1 690 . 3 2 32 32 LEU CA C 13 57.07 0.20 . 1 . . . . 32 LEU CA . 6683 1 691 . 3 2 32 32 LEU CB C 13 41.80 0.20 . 1 . . . . 32 LEU CB . 6683 1 692 . 3 2 32 32 LEU N N 15 116.88 0.30 . 1 . . . . 32 LEU N . 6683 1 693 . 3 2 33 33 VAL H H 1 7.63 0.03 . 1 . . . . 33 VAL H . 6683 1 694 . 3 2 33 33 VAL C C 13 177.35 0.20 . 1 . . . . 33 VAL C . 6683 1 695 . 3 2 33 33 VAL CA C 13 64.54 0.20 . 1 . . . . 33 VAL CA . 6683 1 696 . 3 2 33 33 VAL CB C 13 32.48 0.20 . 1 . . . . 33 VAL CB . 6683 1 697 . 3 2 33 33 VAL N N 15 117.90 0.30 . 1 . . . . 33 VAL N . 6683 1 698 . 3 2 34 34 VAL H H 1 8.80 0.03 . 1 . . . . 34 VAL H . 6683 1 699 . 3 2 34 34 VAL C C 13 175.71 0.20 . 1 . . . . 34 VAL C . 6683 1 700 . 3 2 34 34 VAL CA C 13 65.71 0.20 . 1 . . . . 34 VAL CA . 6683 1 701 . 3 2 34 34 VAL CB C 13 31.44 0.20 . 1 . . . . 34 VAL CB . 6683 1 702 . 3 2 34 34 VAL N N 15 120.26 0.30 . 1 . . . . 34 VAL N . 6683 1 703 . 3 2 35 35 TYR H H 1 7.60 0.03 . 1 . . . . 35 TYR H . 6683 1 704 . 3 2 35 35 TYR CA C 13 53.00 0.20 . 1 . . . . 35 TYR CA . 6683 1 705 . 3 2 35 35 TYR CB C 13 36.48 0.20 . 1 . . . . 35 TYR CB . 6683 1 706 . 3 2 35 35 TYR N N 15 117.08 0.30 . 1 . . . . 35 TYR N . 6683 1 707 . 3 2 36 36 PRO C C 13 178.12 0.20 . 1 . . . . 36 PRO C . 6683 1 708 . 3 2 36 36 PRO CA C 13 65.35 0.20 . 1 . . . . 36 PRO CA . 6683 1 709 . 3 2 36 36 PRO CB C 13 31.32 0.20 . 1 . . . . 36 PRO CB . 6683 1 710 . 3 2 37 37 TRP H H 1 7.15 0.03 . 1 . . . . 37 TRP H . 6683 1 711 . 3 2 37 37 TRP C C 13 178.47 0.20 . 1 . . . . 37 TRP C . 6683 1 712 . 3 2 37 37 TRP CA C 13 60.25 0.20 . 1 . . . . 37 TRP CA . 6683 1 713 . 3 2 37 37 TRP CB C 13 25.53 0.20 . 1 . . . . 37 TRP CB . 6683 1 714 . 3 2 37 37 TRP N N 15 119.04 0.30 . 1 . . . . 37 TRP N . 6683 1 715 . 3 2 38 38 THR H H 1 8.06 0.03 . 1 . . . . 38 THR H . 6683 1 716 . 3 2 38 38 THR C C 13 175.56 0.20 . 1 . . . . 38 THR C . 6683 1 717 . 3 2 38 38 THR CA C 13 65.37 0.20 . 1 . . . . 38 THR CA . 6683 1 718 . 3 2 38 38 THR CB C 13 70.01 0.20 . 1 . . . . 38 THR CB . 6683 1 719 . 3 2 38 38 THR N N 15 116.18 0.30 . 1 . . . . 38 THR N . 6683 1 720 . 3 2 39 39 GLN H H 1 7.34 0.03 . 1 . . . . 39 GLN H . 6683 1 721 . 3 2 39 39 GLN C C 13 178.02 0.20 . 1 . . . . 39 GLN C . 6683 1 722 . 3 2 39 39 GLN CA C 13 57.50 0.20 . 1 . . . . 39 GLN CA . 6683 1 723 . 3 2 39 39 GLN CB C 13 27.27 0.20 . 1 . . . . 39 GLN CB . 6683 1 724 . 3 2 39 39 GLN N N 15 117.09 0.30 . 1 . . . . 39 GLN N . 6683 1 725 . 3 2 40 40 ARG H H 1 6.86 0.03 . 1 . . . . 40 ARG H . 6683 1 726 . 3 2 40 40 ARG CA C 13 57.21 0.20 . 1 . . . . 40 ARG CA . 6683 1 727 . 3 2 40 40 ARG CB C 13 27.66 0.20 . 1 . . . . 40 ARG CB . 6683 1 728 . 3 2 40 40 ARG N N 15 118.20 0.30 . 1 . . . . 40 ARG N . 6683 1 729 . 3 2 41 41 PHE C C 13 174.70 0.20 . 1 . . . . 41 PHE C . 6683 1 730 . 3 2 41 41 PHE CA C 13 57.26 0.20 . 1 . . . . 41 PHE CA . 6683 1 731 . 3 2 41 41 PHE CB C 13 36.70 0.20 . 1 . . . . 41 PHE CB . 6683 1 732 . 3 2 42 42 PHE H H 1 6.71 0.03 . 1 . . . . 42 PHE H . 6683 1 733 . 3 2 42 42 PHE C C 13 175.71 0.20 . 1 . . . . 42 PHE C . 6683 1 734 . 3 2 42 42 PHE CA C 13 55.70 0.20 . 1 . . . . 42 PHE CA . 6683 1 735 . 3 2 42 42 PHE CB C 13 38.78 0.20 . 1 . . . . 42 PHE CB . 6683 1 736 . 3 2 42 42 PHE N N 15 116.26 0.30 . 1 . . . . 42 PHE N . 6683 1 737 . 3 2 43 43 GLU H H 1 7.29 0.03 . 1 . . . . 43 GLU H . 6683 1 738 . 3 2 43 43 GLU CA C 13 59.11 0.20 . 1 . . . . 43 GLU CA . 6683 1 739 . 3 2 43 43 GLU CB C 13 28.35 0.20 . 1 . . . . 43 GLU CB . 6683 1 740 . 3 2 43 43 GLU N N 15 122.40 0.30 . 1 . . . . 43 GLU N . 6683 1 741 . 3 2 44 44 SER C C 13 175.82 0.20 . 1 . . . . 44 SER C . 6683 1 742 . 3 2 44 44 SER CA C 13 59.39 0.20 . 1 . . . . 44 SER CA . 6683 1 743 . 3 2 44 44 SER CB C 13 62.66 0.20 . 1 . . . . 44 SER CB . 6683 1 744 . 3 2 45 45 PHE H H 1 7.88 0.03 . 1 . . . . 45 PHE H . 6683 1 745 . 3 2 45 45 PHE C C 13 175.94 0.20 . 1 . . . . 45 PHE C . 6683 1 746 . 3 2 45 45 PHE CA C 13 56.24 0.20 . 1 . . . . 45 PHE CA . 6683 1 747 . 3 2 45 45 PHE CB C 13 35.62 0.20 . 1 . . . . 45 PHE CB . 6683 1 748 . 3 2 45 45 PHE N N 15 122.73 0.30 . 1 . . . . 45 PHE N . 6683 1 749 . 3 2 46 46 GLY H H 1 7.31 0.03 . 1 . . . . 46 GLY H . 6683 1 750 . 3 2 46 46 GLY C C 13 172.83 0.20 . 1 . . . . 46 GLY C . 6683 1 751 . 3 2 46 46 GLY CA C 13 44.12 0.20 . 1 . . . . 46 GLY CA . 6683 1 752 . 3 2 46 46 GLY N N 15 108.92 0.30 . 1 . . . . 46 GLY N . 6683 1 753 . 3 2 47 47 ASP H H 1 8.16 0.03 . 1 . . . . 47 ASP H . 6683 1 754 . 3 2 47 47 ASP C C 13 175.97 0.20 . 1 . . . . 47 ASP C . 6683 1 755 . 3 2 47 47 ASP CA C 13 55.34 0.20 . 1 . . . . 47 ASP CA . 6683 1 756 . 3 2 47 47 ASP CB C 13 40.04 0.20 . 1 . . . . 47 ASP CB . 6683 1 757 . 3 2 47 47 ASP N N 15 122.96 0.30 . 1 . . . . 47 ASP N . 6683 1 758 . 3 2 48 48 LEU H H 1 8.25 0.03 . 1 . . . . 48 LEU H . 6683 1 759 . 3 2 48 48 LEU C C 13 178.14 0.20 . 1 . . . . 48 LEU C . 6683 1 760 . 3 2 48 48 LEU CA C 13 52.57 0.20 . 1 . . . . 48 LEU CA . 6683 1 761 . 3 2 48 48 LEU CB C 13 40.36 0.20 . 1 . . . . 48 LEU CB . 6683 1 762 . 3 2 48 48 LEU N N 15 129.36 0.30 . 1 . . . . 48 LEU N . 6683 1 763 . 3 2 49 49 SER H H 1 8.04 0.03 . 1 . . . . 49 SER H . 6683 1 764 . 3 2 49 49 SER CA C 13 61.96 0.20 . 1 . . . . 49 SER CA . 6683 1 765 . 3 2 49 49 SER CB C 13 63.83 0.20 . 1 . . . . 49 SER CB . 6683 1 766 . 3 2 49 49 SER N N 15 113.96 0.30 . 1 . . . . 49 SER N . 6683 1 767 . 3 2 50 50 THR H H 1 6.96 0.03 . 1 . . . . 50 THR H . 6683 1 768 . 3 2 50 50 THR C C 13 175.23 0.20 . 1 . . . . 50 THR C . 6683 1 769 . 3 2 50 50 THR CA C 13 58.17 0.20 . 1 . . . . 50 THR CA . 6683 1 770 . 3 2 50 50 THR CB C 13 70.26 0.20 . 1 . . . . 50 THR CB . 6683 1 771 . 3 2 50 50 THR N N 15 112.27 0.30 . 1 . . . . 50 THR N . 6683 1 772 . 3 2 52 52 ASP C C 13 179.48 0.20 . 1 . . . . 52 ASP C . 6683 1 773 . 3 2 52 52 ASP CA C 13 56.99 0.20 . 1 . . . . 52 ASP CA . 6683 1 774 . 3 2 52 52 ASP CB C 13 39.87 0.20 . 1 . . . . 52 ASP CB . 6683 1 775 . 3 2 53 53 ALA H H 1 7.68 0.03 . 1 . . . . 53 ALA H . 6683 1 776 . 3 2 53 53 ALA C C 13 180.61 0.20 . 1 . . . . 53 ALA C . 6683 1 777 . 3 2 53 53 ALA CA C 13 54.62 0.20 . 1 . . . . 53 ALA CA . 6683 1 778 . 3 2 53 53 ALA CB C 13 17.86 0.20 . 1 . . . . 53 ALA CB . 6683 1 779 . 3 2 53 53 ALA N N 15 124.76 0.30 . 1 . . . . 53 ALA N . 6683 1 780 . 3 2 54 54 VAL H H 1 7.78 0.03 . 1 . . . . 54 VAL H . 6683 1 781 . 3 2 54 54 VAL C C 13 178.62 0.20 . 1 . . . . 54 VAL C . 6683 1 782 . 3 2 54 54 VAL CA C 13 66.76 0.20 . 1 . . . . 54 VAL CA . 6683 1 783 . 3 2 54 54 VAL CB C 13 31.26 0.20 . 1 . . . . 54 VAL CB . 6683 1 784 . 3 2 54 54 VAL N N 15 117.84 0.30 . 1 . . . . 54 VAL N . 6683 1 785 . 3 2 55 55 MET H H 1 7.96 0.03 . 1 . . . . 55 MET H . 6683 1 786 . 3 2 55 55 MET C C 13 178.85 0.20 . 1 . . . . 55 MET C . 6683 1 787 . 3 2 55 55 MET CA C 13 55.19 0.20 . 1 . . . . 55 MET CA . 6683 1 788 . 3 2 55 55 MET CB C 13 28.13 0.20 . 1 . . . . 55 MET CB . 6683 1 789 . 3 2 55 55 MET N N 15 112.91 0.30 . 1 . . . . 55 MET N . 6683 1 790 . 3 2 56 56 GLY H H 1 7.31 0.03 . 1 . . . . 56 GLY H . 6683 1 791 . 3 2 56 56 GLY C C 13 174.25 0.20 . 1 . . . . 56 GLY C . 6683 1 792 . 3 2 56 56 GLY CA C 13 44.08 0.20 . 1 . . . . 56 GLY CA . 6683 1 793 . 3 2 56 56 GLY N N 15 103.98 0.30 . 1 . . . . 56 GLY N . 6683 1 794 . 3 2 57 57 ASN H H 1 7.13 0.03 . 1 . . . . 57 ASN H . 6683 1 795 . 3 2 57 57 ASN CA C 13 51.80 0.20 . 1 . . . . 57 ASN CA . 6683 1 796 . 3 2 57 57 ASN CB C 13 38.54 0.20 . 1 . . . . 57 ASN CB . 6683 1 797 . 3 2 57 57 ASN N N 15 124.68 0.30 . 1 . . . . 57 ASN N . 6683 1 798 . 3 2 58 58 PRO C C 13 179.83 0.20 . 1 . . . . 58 PRO C . 6683 1 799 . 3 2 58 58 PRO CA C 13 64.70 0.20 . 1 . . . . 58 PRO CA . 6683 1 800 . 3 2 58 58 PRO CB C 13 31.42 0.20 . 1 . . . . 58 PRO CB . 6683 1 801 . 3 2 59 59 LYS H H 1 7.76 0.03 . 1 . . . . 59 LYS H . 6683 1 802 . 3 2 59 59 LYS C C 13 179.42 0.20 . 1 . . . . 59 LYS C . 6683 1 803 . 3 2 59 59 LYS CA C 13 58.68 0.20 . 1 . . . . 59 LYS CA . 6683 1 804 . 3 2 59 59 LYS CB C 13 29.42 0.20 . 1 . . . . 59 LYS CB . 6683 1 805 . 3 2 59 59 LYS N N 15 120.38 0.30 . 1 . . . . 59 LYS N . 6683 1 806 . 3 2 60 60 VAL H H 1 7.31 0.03 . 1 . . . . 60 VAL H . 6683 1 807 . 3 2 60 60 VAL C C 13 178.21 0.20 . 1 . . . . 60 VAL C . 6683 1 808 . 3 2 60 60 VAL CA C 13 66.09 0.20 . 1 . . . . 60 VAL CA . 6683 1 809 . 3 2 60 60 VAL CB C 13 30.98 0.20 . 1 . . . . 60 VAL CB . 6683 1 810 . 3 2 60 60 VAL N N 15 123.64 0.30 . 1 . . . . 60 VAL N . 6683 1 811 . 3 2 61 61 LYS H H 1 7.24 0.03 . 1 . . . . 61 LYS H . 6683 1 812 . 3 2 61 61 LYS C C 13 179.56 0.20 . 1 . . . . 61 LYS C . 6683 1 813 . 3 2 61 61 LYS CA C 13 60.16 0.20 . 1 . . . . 61 LYS CA . 6683 1 814 . 3 2 61 61 LYS CB C 13 31.33 0.20 . 1 . . . . 61 LYS CB . 6683 1 815 . 3 2 61 61 LYS N N 15 119.24 0.30 . 1 . . . . 61 LYS N . 6683 1 816 . 3 2 62 62 ALA H H 1 7.58 0.03 . 1 . . . . 62 ALA H . 6683 1 817 . 3 2 62 62 ALA CA C 13 54.51 0.20 . 1 . . . . 62 ALA CA . 6683 1 818 . 3 2 62 62 ALA CB C 13 17.46 0.20 . 1 . . . . 62 ALA CB . 6683 1 819 . 3 2 62 62 ALA N N 15 121.65 0.30 . 1 . . . . 62 ALA N . 6683 1 820 . 3 2 64 64 GLY C C 13 175.56 0.20 . 1 . . . . 64 GLY C . 6683 1 821 . 3 2 64 64 GLY CA C 13 46.84 0.20 . 1 . . . . 64 GLY CA . 6683 1 822 . 3 2 65 65 LYS H H 1 7.14 0.03 . 1 . . . . 65 LYS H . 6683 1 823 . 3 2 65 65 LYS CA C 13 59.36 0.20 . 1 . . . . 65 LYS CA . 6683 1 824 . 3 2 65 65 LYS CB C 13 31.41 0.20 . 1 . . . . 65 LYS CB . 6683 1 825 . 3 2 65 65 LYS N N 15 121.62 0.30 . 1 . . . . 65 LYS N . 6683 1 826 . 3 2 68 68 LEU CA C 13 56.29 0.20 . 1 . . . . 68 LEU CA . 6683 1 827 . 3 2 68 68 LEU CB C 13 35.80 0.20 . 1 . . . . 68 LEU CB . 6683 1 828 . 3 2 69 69 GLY H H 1 7.39 0.03 . 1 . . . . 69 GLY H . 6683 1 829 . 3 2 69 69 GLY CA C 13 44.23 0.20 . 1 . . . . 69 GLY CA . 6683 1 830 . 3 2 69 69 GLY N N 15 109.16 0.30 . 1 . . . . 69 GLY N . 6683 1 831 . 3 2 71 71 PHE C C 13 176.64 0.20 . 1 . . . . 71 PHE C . 6683 1 832 . 3 2 71 71 PHE CA C 13 61.95 0.20 . 1 . . . . 71 PHE CA . 6683 1 833 . 3 2 71 71 PHE CB C 13 40.02 0.20 . 1 . . . . 71 PHE CB . 6683 1 834 . 3 2 72 72 SER H H 1 8.37 0.03 . 1 . . . . 72 SER H . 6683 1 835 . 3 2 72 72 SER C C 13 177.65 0.20 . 1 . . . . 72 SER C . 6683 1 836 . 3 2 72 72 SER CA C 13 61.38 0.20 . 1 . . . . 72 SER CA . 6683 1 837 . 3 2 72 72 SER CB C 13 62.81 0.20 . 1 . . . . 72 SER CB . 6683 1 838 . 3 2 72 72 SER N N 15 114.21 0.30 . 1 . . . . 72 SER N . 6683 1 839 . 3 2 73 73 ASP H H 1 7.32 0.03 . 1 . . . . 73 ASP H . 6683 1 840 . 3 2 73 73 ASP C C 13 179.22 0.20 . 1 . . . . 73 ASP C . 6683 1 841 . 3 2 73 73 ASP CA C 13 56.92 0.20 . 1 . . . . 73 ASP CA . 6683 1 842 . 3 2 73 73 ASP CB C 13 39.64 0.20 . 1 . . . . 73 ASP CB . 6683 1 843 . 3 2 73 73 ASP N N 15 122.33 0.30 . 1 . . . . 73 ASP N . 6683 1 844 . 3 2 74 74 GLY H H 1 7.37 0.03 . 1 . . . . 74 GLY H . 6683 1 845 . 3 2 74 74 GLY C C 13 174.65 0.20 . 1 . . . . 74 GLY C . 6683 1 846 . 3 2 74 74 GLY CA C 13 46.75 0.20 . 1 . . . . 74 GLY CA . 6683 1 847 . 3 2 74 74 GLY N N 15 107.83 0.30 . 1 . . . . 74 GLY N . 6683 1 848 . 3 2 75 75 LEU H H 1 6.99 0.03 . 1 . . . . 75 LEU H . 6683 1 849 . 3 2 75 75 LEU C C 13 178.01 0.20 . 1 . . . . 75 LEU C . 6683 1 850 . 3 2 75 75 LEU CA C 13 56.52 0.20 . 1 . . . . 75 LEU CA . 6683 1 851 . 3 2 75 75 LEU CB C 13 39.59 0.20 . 1 . . . . 75 LEU CB . 6683 1 852 . 3 2 75 75 LEU N N 15 119.88 0.30 . 1 . . . . 75 LEU N . 6683 1 853 . 3 2 76 76 ALA H H 1 6.82 0.03 . 1 . . . . 76 ALA H . 6683 1 854 . 3 2 76 76 ALA C C 13 177.40 0.20 . 1 . . . . 76 ALA C . 6683 1 855 . 3 2 76 76 ALA CA C 13 52.19 0.20 . 1 . . . . 76 ALA CA . 6683 1 856 . 3 2 76 76 ALA CB C 13 17.97 0.20 . 1 . . . . 76 ALA CB . 6683 1 857 . 3 2 76 76 ALA N N 15 119.64 0.30 . 1 . . . . 76 ALA N . 6683 1 858 . 3 2 77 77 HIS H H 1 7.38 0.03 . 1 . . . . 77 HIS H . 6683 1 859 . 3 2 77 77 HIS C C 13 176.00 0.20 . 1 . . . . 77 HIS C . 6683 1 860 . 3 2 77 77 HIS CA C 13 53.88 0.20 . 1 . . . . 77 HIS CA . 6683 1 861 . 3 2 77 77 HIS CB C 13 29.43 0.20 . 1 . . . . 77 HIS CB . 6683 1 862 . 3 2 77 77 HIS N N 15 119.64 0.30 . 1 . . . . 77 HIS N . 6683 1 863 . 3 2 78 78 LEU H H 1 7.53 0.03 . 1 . . . . 78 LEU H . 6683 1 864 . 3 2 78 78 LEU C C 13 177.86 0.20 . 1 . . . . 78 LEU C . 6683 1 865 . 3 2 78 78 LEU CA C 13 57.75 0.20 . 1 . . . . 78 LEU CA . 6683 1 866 . 3 2 78 78 LEU CB C 13 41.20 0.20 . 1 . . . . 78 LEU CB . 6683 1 867 . 3 2 78 78 LEU N N 15 120.95 0.30 . 1 . . . . 78 LEU N . 6683 1 868 . 3 2 79 79 ASP H H 1 8.32 0.03 . 1 . . . . 79 ASP H . 6683 1 869 . 3 2 79 79 ASP C C 13 176.21 0.20 . 1 . . . . 79 ASP C . 6683 1 870 . 3 2 79 79 ASP CA C 13 54.29 0.20 . 1 . . . . 79 ASP CA . 6683 1 871 . 3 2 79 79 ASP CB C 13 39.96 0.20 . 1 . . . . 79 ASP CB . 6683 1 872 . 3 2 79 79 ASP N N 15 116.27 0.30 . 1 . . . . 79 ASP N . 6683 1 873 . 3 2 80 80 ASN H H 1 7.88 0.03 . 1 . . . . 80 ASN H . 6683 1 874 . 3 2 80 80 ASN C C 13 176.39 0.20 . 1 . . . . 80 ASN C . 6683 1 875 . 3 2 80 80 ASN CA C 13 51.69 0.20 . 1 . . . . 80 ASN CA . 6683 1 876 . 3 2 80 80 ASN CB C 13 37.73 0.20 . 1 . . . . 80 ASN CB . 6683 1 877 . 3 2 80 80 ASN N N 15 120.23 0.30 . 1 . . . . 80 ASN N . 6683 1 878 . 3 2 81 81 LEU H H 1 8.62 0.03 . 1 . . . . 81 LEU H . 6683 1 879 . 3 2 81 81 LEU C C 13 179.62 0.20 . 1 . . . . 81 LEU C . 6683 1 880 . 3 2 81 81 LEU CA C 13 58.16 0.20 . 1 . . . . 81 LEU CA . 6683 1 881 . 3 2 81 81 LEU CB C 13 41.81 0.20 . 1 . . . . 81 LEU CB . 6683 1 882 . 3 2 81 81 LEU N N 15 126.84 0.30 . 1 . . . . 81 LEU N . 6683 1 883 . 3 2 82 82 LYS H H 1 8.52 0.03 . 1 . . . . 82 LYS H . 6683 1 884 . 3 2 82 82 LYS C C 13 179.02 0.20 . 1 . . . . 82 LYS C . 6683 1 885 . 3 2 82 82 LYS CA C 13 60.88 0.20 . 1 . . . . 82 LYS CA . 6683 1 886 . 3 2 82 82 LYS CB C 13 30.79 0.20 . 1 . . . . 82 LYS CB . 6683 1 887 . 3 2 82 82 LYS N N 15 118.99 0.30 . 1 . . . . 82 LYS N . 6683 1 888 . 3 2 83 83 GLY H H 1 7.30 0.03 . 1 . . . . 83 GLY H . 6683 1 889 . 3 2 83 83 GLY C C 13 177.04 0.20 . 1 . . . . 83 GLY C . 6683 1 890 . 3 2 83 83 GLY CA C 13 46.70 0.20 . 1 . . . . 83 GLY CA . 6683 1 891 . 3 2 83 83 GLY N N 15 105.16 0.30 . 1 . . . . 83 GLY N . 6683 1 892 . 3 2 84 84 THR H H 1 7.28 0.03 . 1 . . . . 84 THR H . 6683 1 893 . 3 2 84 84 THR C C 13 175.89 0.20 . 1 . . . . 84 THR C . 6683 1 894 . 3 2 84 84 THR CA C 13 65.91 0.20 . 1 . . . . 84 THR CA . 6683 1 895 . 3 2 84 84 THR CB C 13 68.21 0.20 . 1 . . . . 84 THR CB . 6683 1 896 . 3 2 84 84 THR N N 15 118.67 0.30 . 1 . . . . 84 THR N . 6683 1 897 . 3 2 85 85 PHE H H 1 7.24 0.03 . 1 . . . . 85 PHE H . 6683 1 898 . 3 2 85 85 PHE C C 13 174.79 0.20 . 1 . . . . 85 PHE C . 6683 1 899 . 3 2 85 85 PHE CA C 13 58.39 0.20 . 1 . . . . 85 PHE CA . 6683 1 900 . 3 2 85 85 PHE CB C 13 37.27 0.20 . 1 . . . . 85 PHE CB . 6683 1 901 . 3 2 85 85 PHE N N 15 116.25 0.30 . 1 . . . . 85 PHE N . 6683 1 902 . 3 2 86 86 ALA H H 1 6.96 0.03 . 1 . . . . 86 ALA H . 6683 1 903 . 3 2 86 86 ALA C C 13 179.73 0.20 . 1 . . . . 86 ALA C . 6683 1 904 . 3 2 86 86 ALA CA C 13 56.85 0.20 . 1 . . . . 86 ALA CA . 6683 1 905 . 3 2 86 86 ALA CB C 13 17.82 0.20 . 1 . . . . 86 ALA CB . 6683 1 906 . 3 2 86 86 ALA N N 15 125.47 0.30 . 1 . . . . 86 ALA N . 6683 1 907 . 3 2 87 87 THR H H 1 8.43 0.03 . 1 . . . . 87 THR H . 6683 1 908 . 3 2 87 87 THR CA C 13 66.62 0.20 . 1 . . . . 87 THR CA . 6683 1 909 . 3 2 87 87 THR CB C 13 68.06 0.20 . 1 . . . . 87 THR CB . 6683 1 910 . 3 2 87 87 THR N N 15 115.31 0.30 . 1 . . . . 87 THR N . 6683 1 911 . 3 2 93 93 CYS C C 13 176.73 0.20 . 1 . . . . 93 CYS C . 6683 1 912 . 3 2 93 93 CYS CA C 13 63.11 0.20 . 1 . . . . 93 CYS CA . 6683 1 913 . 3 2 93 93 CYS CB C 13 25.58 0.20 . 1 . . . . 93 CYS CB . 6683 1 914 . 3 2 94 94 ASP H H 1 8.93 0.03 . 1 . . . . 94 ASP H . 6683 1 915 . 3 2 94 94 ASP C C 13 177.10 0.20 . 1 . . . . 94 ASP C . 6683 1 916 . 3 2 94 94 ASP CA C 13 57.46 0.20 . 1 . . . . 94 ASP CA . 6683 1 917 . 3 2 94 94 ASP CB C 13 40.78 0.20 . 1 . . . . 94 ASP CB . 6683 1 918 . 3 2 94 94 ASP N N 15 117.16 0.30 . 1 . . . . 94 ASP N . 6683 1 919 . 3 2 95 95 LYS H H 1 8.16 0.03 . 1 . . . . 95 LYS H . 6683 1 920 . 3 2 95 95 LYS CA C 13 57.16 0.20 . 1 . . . . 95 LYS CA . 6683 1 921 . 3 2 95 95 LYS N N 15 117.20 0.30 . 1 . . . . 95 LYS N . 6683 1 922 . 3 2 98 98 VAL CA C 13 68.00 0.20 . 1 . . . . 98 VAL CA . 6683 1 923 . 3 2 98 98 VAL CB C 13 31.53 0.20 . 1 . . . . 98 VAL CB . 6683 1 924 . 3 2 99 99 ASP N N 15 123.08 0.30 . 1 . . . . 99 ASP N . 6683 1 925 . 3 2 99 99 ASP CA C 13 58.50 0.20 . 1 . . . . 99 ASP CA . 6683 1 926 . 3 2 99 99 ASP CB C 13 40.99 0.20 . 1 . . . . 99 ASP CB . 6683 1 927 . 3 2 99 99 ASP H H 1 10.05 0.03 . 1 . . . . 99 ASP H . 6683 1 928 . 3 2 100 100 PRO C C 13 178.38 0.20 . 1 . . . . 100 PRO C . 6683 1 929 . 3 2 100 100 PRO CA C 13 63.37 0.20 . 1 . . . . 100 PRO CA . 6683 1 930 . 3 2 100 100 PRO CB C 13 31.01 0.20 . 1 . . . . 100 PRO CB . 6683 1 931 . 3 2 101 101 GLU H H 1 8.17 0.03 . 1 . . . . 101 GLU H . 6683 1 932 . 3 2 101 101 GLU CA C 13 59.08 0.20 . 1 . . . . 101 GLU CA . 6683 1 933 . 3 2 101 101 GLU CB C 13 28.41 0.20 . 1 . . . . 101 GLU CB . 6683 1 934 . 3 2 101 101 GLU N N 15 124.40 0.30 . 1 . . . . 101 GLU N . 6683 1 935 . 3 2 103 103 PHE C C 13 180.25 0.20 . 1 . . . . 103 PHE C . 6683 1 936 . 3 2 103 103 PHE CA C 13 59.21 0.20 . 1 . . . . 103 PHE CA . 6683 1 937 . 3 2 103 103 PHE CB C 13 38.26 0.20 . 1 . . . . 103 PHE CB . 6683 1 938 . 3 2 104 104 ARG H H 1 7.66 0.03 . 1 . . . . 104 ARG H . 6683 1 939 . 3 2 104 104 ARG C C 13 180.23 0.20 . 1 . . . . 104 ARG C . 6683 1 940 . 3 2 104 104 ARG CA C 13 59.62 0.20 . 1 . . . . 104 ARG CA . 6683 1 941 . 3 2 104 104 ARG CB C 13 29.12 0.20 . 1 . . . . 104 ARG CB . 6683 1 942 . 3 2 104 104 ARG N N 15 122.18 0.30 . 1 . . . . 104 ARG N . 6683 1 943 . 3 2 105 105 LEU H H 1 8.39 0.03 . 1 . . . . 105 LEU H . 6683 1 944 . 3 2 105 105 LEU C C 13 180.75 0.20 . 1 . . . . 105 LEU C . 6683 1 945 . 3 2 105 105 LEU CA C 13 58.64 0.20 . 1 . . . . 105 LEU CA . 6683 1 946 . 3 2 105 105 LEU CB C 13 43.29 0.20 . 1 . . . . 105 LEU CB . 6683 1 947 . 3 2 105 105 LEU N N 15 121.33 0.30 . 1 . . . . 105 LEU N . 6683 1 948 . 3 2 106 106 LEU H H 1 9.66 0.03 . 1 . . . . 106 LEU H . 6683 1 949 . 3 2 106 106 LEU C C 13 179.90 0.20 . 1 . . . . 106 LEU C . 6683 1 950 . 3 2 106 106 LEU CA C 13 59.34 0.20 . 1 . . . . 106 LEU CA . 6683 1 951 . 3 2 106 106 LEU CB C 13 42.58 0.20 . 1 . . . . 106 LEU CB . 6683 1 952 . 3 2 106 106 LEU N N 15 119.81 0.30 . 1 . . . . 106 LEU N . 6683 1 953 . 3 2 107 107 GLY H H 1 8.99 0.03 . 1 . . . . 107 GLY H . 6683 1 954 . 3 2 107 107 GLY C C 13 175.70 0.20 . 1 . . . . 107 GLY C . 6683 1 955 . 3 2 107 107 GLY CA C 13 48.52 0.20 . 1 . . . . 107 GLY CA . 6683 1 956 . 3 2 107 107 GLY N N 15 108.06 0.30 . 1 . . . . 107 GLY N . 6683 1 957 . 3 2 108 108 ASN H H 1 8.13 0.03 . 1 . . . . 108 ASN H . 6683 1 958 . 3 2 108 108 ASN C C 13 179.85 0.20 . 1 . . . . 108 ASN C . 6683 1 959 . 3 2 108 108 ASN CA C 13 56.20 0.20 . 1 . . . . 108 ASN CA . 6683 1 960 . 3 2 108 108 ASN CB C 13 37.52 0.20 . 1 . . . . 108 ASN CB . 6683 1 961 . 3 2 108 108 ASN N N 15 121.33 0.30 . 1 . . . . 108 ASN N . 6683 1 962 . 3 2 109 109 VAL H H 1 9.06 0.03 . 1 . . . . 109 VAL H . 6683 1 963 . 3 2 109 109 VAL C C 13 179.02 0.20 . 1 . . . . 109 VAL C . 6683 1 964 . 3 2 109 109 VAL CA C 13 68.24 0.20 . 1 . . . . 109 VAL CA . 6683 1 965 . 3 2 109 109 VAL CB C 13 31.76 0.20 . 1 . . . . 109 VAL CB . 6683 1 966 . 3 2 109 109 VAL N N 15 123.30 0.30 . 1 . . . . 109 VAL N . 6683 1 967 . 3 2 110 110 LEU H H 1 10.03 0.03 . 1 . . . . 110 LEU H . 6683 1 968 . 3 2 110 110 LEU C C 13 178.79 0.20 . 1 . . . . 110 LEU C . 6683 1 969 . 3 2 110 110 LEU CA C 13 58.86 0.20 . 1 . . . . 110 LEU CA . 6683 1 970 . 3 2 110 110 LEU CB C 13 41.34 0.20 . 1 . . . . 110 LEU CB . 6683 1 971 . 3 2 110 110 LEU N N 15 123.01 0.30 . 1 . . . . 110 LEU N . 6683 1 972 . 3 2 111 111 VAL H H 1 8.33 0.03 . 1 . . . . 111 VAL H . 6683 1 973 . 3 2 111 111 VAL C C 13 177.66 0.20 . 1 . . . . 111 VAL C . 6683 1 974 . 3 2 111 111 VAL CA C 13 68.46 0.20 . 1 . . . . 111 VAL CA . 6683 1 975 . 3 2 111 111 VAL CB C 13 31.15 0.20 . 1 . . . . 111 VAL CB . 6683 1 976 . 3 2 111 111 VAL N N 15 119.72 0.30 . 1 . . . . 111 VAL N . 6683 1 977 . 3 2 112 112 CYS H H 1 7.92 0.03 . 1 . . . . 112 CYS H . 6683 1 978 . 3 2 112 112 CYS C C 13 176.94 0.20 . 1 . . . . 112 CYS C . 6683 1 979 . 3 2 112 112 CYS CA C 13 65.20 0.20 . 1 . . . . 112 CYS CA . 6683 1 980 . 3 2 112 112 CYS CB C 13 26.76 0.20 . 1 . . . . 112 CYS CB . 6683 1 981 . 3 2 112 112 CYS N N 15 117.90 0.30 . 1 . . . . 112 CYS N . 6683 1 982 . 3 2 113 113 VAL H H 1 8.77 0.03 . 1 . . . . 113 VAL H . 6683 1 983 . 3 2 113 113 VAL C C 13 178.30 0.20 . 1 . . . . 113 VAL C . 6683 1 984 . 3 2 113 113 VAL CA C 13 66.66 0.20 . 1 . . . . 113 VAL CA . 6683 1 985 . 3 2 113 113 VAL CB C 13 31.10 0.20 . 1 . . . . 113 VAL CB . 6683 1 986 . 3 2 113 113 VAL N N 15 121.72 0.30 . 1 . . . . 113 VAL N . 6683 1 987 . 3 2 114 114 LEU H H 1 8.62 0.03 . 1 . . . . 114 LEU H . 6683 1 988 . 3 2 114 114 LEU C C 13 178.90 0.20 . 1 . . . . 114 LEU C . 6683 1 989 . 3 2 114 114 LEU CA C 13 57.84 0.20 . 1 . . . . 114 LEU CA . 6683 1 990 . 3 2 114 114 LEU CB C 13 40.80 0.20 . 1 . . . . 114 LEU CB . 6683 1 991 . 3 2 114 114 LEU N N 15 122.18 0.30 . 1 . . . . 114 LEU N . 6683 1 992 . 3 2 115 115 ALA H H 1 7.38 0.03 . 1 . . . . 115 ALA H . 6683 1 993 . 3 2 115 115 ALA C C 13 178.64 0.20 . 1 . . . . 115 ALA C . 6683 1 994 . 3 2 115 115 ALA CA C 13 54.94 0.20 . 1 . . . . 115 ALA CA . 6683 1 995 . 3 2 115 115 ALA CB C 13 19.44 0.20 . 1 . . . . 115 ALA CB . 6683 1 996 . 3 2 115 115 ALA N N 15 122.86 0.30 . 1 . . . . 115 ALA N . 6683 1 997 . 3 2 116 116 HIS H H 1 8.00 0.03 . 1 . . . . 116 HIS H . 6683 1 998 . 3 2 116 116 HIS C C 13 178.56 0.20 . 1 . . . . 116 HIS C . 6683 1 999 . 3 2 116 116 HIS CA C 13 57.93 0.20 . 1 . . . . 116 HIS CA . 6683 1 1000 . 3 2 116 116 HIS CB C 13 30.86 0.20 . 1 . . . . 116 HIS CB . 6683 1 1001 . 3 2 116 116 HIS N N 15 118.05 0.30 . 1 . . . . 116 HIS N . 6683 1 1002 . 3 2 117 117 HIS H H 1 8.35 0.03 . 1 . . . . 117 HIS H . 6683 1 1003 . 3 2 117 117 HIS C C 13 177.32 0.20 . 1 . . . . 117 HIS C . 6683 1 1004 . 3 2 117 117 HIS CA C 13 58.73 0.20 . 1 . . . . 117 HIS CA . 6683 1 1005 . 3 2 117 117 HIS CB C 13 29.78 0.20 . 1 . . . . 117 HIS CB . 6683 1 1006 . 3 2 117 117 HIS N N 15 117.47 0.30 . 1 . . . . 117 HIS N . 6683 1 1007 . 3 2 118 118 PHE H H 1 8.33 0.03 . 1 . . . . 118 PHE H . 6683 1 1008 . 3 2 118 118 PHE C C 13 177.84 0.20 . 1 . . . . 118 PHE C . 6683 1 1009 . 3 2 118 118 PHE CA C 13 59.56 0.20 . 1 . . . . 118 PHE CA . 6683 1 1010 . 3 2 118 118 PHE CB C 13 39.21 0.20 . 1 . . . . 118 PHE CB . 6683 1 1011 . 3 2 118 118 PHE N N 15 115.33 0.30 . 1 . . . . 118 PHE N . 6683 1 1012 . 3 2 119 119 GLY H H 1 8.41 0.03 . 1 . . . . 119 GLY H . 6683 1 1013 . 3 2 119 119 GLY C C 13 176.43 0.20 . 1 . . . . 119 GLY C . 6683 1 1014 . 3 2 119 119 GLY CA C 13 47.69 0.20 . 1 . . . . 119 GLY CA . 6683 1 1015 . 3 2 119 119 GLY N N 15 114.92 0.30 . 1 . . . . 119 GLY N . 6683 1 1016 . 3 2 120 120 LYS H H 1 8.62 0.03 . 1 . . . . 120 LYS H . 6683 1 1017 . 3 2 120 120 LYS C C 13 178.36 0.20 . 1 . . . . 120 LYS C . 6683 1 1018 . 3 2 120 120 LYS CA C 13 57.99 0.20 . 1 . . . . 120 LYS CA . 6683 1 1019 . 3 2 120 120 LYS CB C 13 31.27 0.20 . 1 . . . . 120 LYS CB . 6683 1 1020 . 3 2 120 120 LYS N N 15 126.33 0.30 . 1 . . . . 120 LYS N . 6683 1 1021 . 3 2 121 121 GLU H H 1 7.69 0.03 . 1 . . . . 121 GLU H . 6683 1 1022 . 3 2 121 121 GLU C C 13 177.73 0.20 . 1 . . . . 121 GLU C . 6683 1 1023 . 3 2 121 121 GLU CA C 13 57.47 0.20 . 1 . . . . 121 GLU CA . 6683 1 1024 . 3 2 121 121 GLU CB C 13 29.69 0.20 . 1 . . . . 121 GLU CB . 6683 1 1025 . 3 2 121 121 GLU N N 15 117.93 0.30 . 1 . . . . 121 GLU N . 6683 1 1026 . 3 2 122 122 PHE H H 1 8.47 0.03 . 1 . . . . 122 PHE H . 6683 1 1027 . 3 2 122 122 PHE C C 13 174.83 0.20 . 1 . . . . 122 PHE C . 6683 1 1028 . 3 2 122 122 PHE CA C 13 56.55 0.20 . 1 . . . . 122 PHE CA . 6683 1 1029 . 3 2 122 122 PHE CB C 13 37.30 0.20 . 1 . . . . 122 PHE CB . 6683 1 1030 . 3 2 122 122 PHE N N 15 127.15 0.30 . 1 . . . . 122 PHE N . 6683 1 1031 . 3 2 123 123 THR H H 1 6.99 0.03 . 1 . . . . 123 THR H . 6683 1 1032 . 3 2 123 123 THR CA C 13 60.49 0.20 . 1 . . . . 123 THR CA . 6683 1 1033 . 3 2 123 123 THR CB C 13 66.98 0.20 . 1 . . . . 123 THR CB . 6683 1 1034 . 3 2 123 123 THR N N 15 114.46 0.30 . 1 . . . . 123 THR N . 6683 1 1035 . 3 2 125 125 PRO C C 13 180.30 0.20 . 1 . . . . 125 PRO C . 6683 1 1036 . 3 2 125 125 PRO CA C 13 65.88 0.20 . 1 . . . . 125 PRO CA . 6683 1 1037 . 3 2 125 125 PRO CB C 13 30.74 0.20 . 1 . . . . 125 PRO CB . 6683 1 1038 . 3 2 126 126 VAL H H 1 6.92 0.03 . 1 . . . . 126 VAL H . 6683 1 1039 . 3 2 126 126 VAL C C 13 178.35 0.20 . 1 . . . . 126 VAL C . 6683 1 1040 . 3 2 126 126 VAL CA C 13 66.73 0.20 . 1 . . . . 126 VAL CA . 6683 1 1041 . 3 2 126 126 VAL CB C 13 30.32 0.20 . 1 . . . . 126 VAL CB . 6683 1 1042 . 3 2 126 126 VAL N N 15 122.60 0.30 . 1 . . . . 126 VAL N . 6683 1 1043 . 3 2 127 127 GLN H H 1 8.32 0.03 . 1 . . . . 127 GLN H . 6683 1 1044 . 3 2 127 127 GLN C C 13 178.21 0.20 . 1 . . . . 127 GLN C . 6683 1 1045 . 3 2 127 127 GLN CA C 13 58.97 0.20 . 1 . . . . 127 GLN CA . 6683 1 1046 . 3 2 127 127 GLN CB C 13 25.26 0.20 . 1 . . . . 127 GLN CB . 6683 1 1047 . 3 2 127 127 GLN N N 15 120.85 0.30 . 1 . . . . 127 GLN N . 6683 1 1048 . 3 2 128 128 ALA H H 1 8.03 0.03 . 1 . . . . 128 ALA H . 6683 1 1049 . 3 2 128 128 ALA C C 13 180.28 0.20 . 1 . . . . 128 ALA C . 6683 1 1050 . 3 2 128 128 ALA CA C 13 55.55 0.20 . 1 . . . . 128 ALA CA . 6683 1 1051 . 3 2 128 128 ALA CB C 13 17.25 0.20 . 1 . . . . 128 ALA CB . 6683 1 1052 . 3 2 128 128 ALA N N 15 122.78 0.30 . 1 . . . . 128 ALA N . 6683 1 1053 . 3 2 129 129 ALA H H 1 7.35 0.03 . 1 . . . . 129 ALA H . 6683 1 1054 . 3 2 129 129 ALA C C 13 179.98 0.20 . 1 . . . . 129 ALA C . 6683 1 1055 . 3 2 129 129 ALA CA C 13 55.25 0.20 . 1 . . . . 129 ALA CA . 6683 1 1056 . 3 2 129 129 ALA CB C 13 17.66 0.20 . 1 . . . . 129 ALA CB . 6683 1 1057 . 3 2 129 129 ALA N N 15 121.14 0.30 . 1 . . . . 129 ALA N . 6683 1 1058 . 3 2 130 130 TYR H H 1 8.34 0.03 . 1 . . . . 130 TYR H . 6683 1 1059 . 3 2 130 130 TYR C C 13 179.59 0.20 . 1 . . . . 130 TYR C . 6683 1 1060 . 3 2 130 130 TYR CA C 13 64.70 0.20 . 1 . . . . 130 TYR CA . 6683 1 1061 . 3 2 130 130 TYR CB C 13 38.60 0.20 . 1 . . . . 130 TYR CB . 6683 1 1062 . 3 2 130 130 TYR N N 15 117.16 0.30 . 1 . . . . 130 TYR N . 6683 1 1063 . 3 2 131 131 GLN H H 1 9.60 0.03 . 1 . . . . 131 GLN H . 6683 1 1064 . 3 2 131 131 GLN C C 13 180.01 0.20 . 1 . . . . 131 GLN C . 6683 1 1065 . 3 2 131 131 GLN CA C 13 58.71 0.20 . 1 . . . . 131 GLN CA . 6683 1 1066 . 3 2 131 131 GLN CB C 13 25.78 0.20 . 1 . . . . 131 GLN CB . 6683 1 1067 . 3 2 131 131 GLN N N 15 121.43 0.30 . 1 . . . . 131 GLN N . 6683 1 1068 . 3 2 132 132 LYS H H 1 7.64 0.03 . 1 . . . . 132 LYS H . 6683 1 1069 . 3 2 132 132 LYS C C 13 180.41 0.20 . 1 . . . . 132 LYS C . 6683 1 1070 . 3 2 132 132 LYS CA C 13 60.28 0.20 . 1 . . . . 132 LYS CA . 6683 1 1071 . 3 2 132 132 LYS N N 15 121.93 0.30 . 1 . . . . 132 LYS N . 6683 1 1072 . 3 2 133 133 VAL H H 1 7.82 0.03 . 1 . . . . 133 VAL H . 6683 1 1073 . 3 2 133 133 VAL C C 13 178.40 0.20 . 1 . . . . 133 VAL C . 6683 1 1074 . 3 2 133 133 VAL CA C 13 67.55 0.20 . 1 . . . . 133 VAL CA . 6683 1 1075 . 3 2 133 133 VAL CB C 13 31.09 0.20 . 1 . . . . 133 VAL CB . 6683 1 1076 . 3 2 133 133 VAL N N 15 120.94 0.30 . 1 . . . . 133 VAL N . 6683 1 1077 . 3 2 134 134 VAL H H 1 9.25 0.03 . 1 . . . . 134 VAL H . 6683 1 1078 . 3 2 134 134 VAL C C 13 179.91 0.20 . 1 . . . . 134 VAL C . 6683 1 1079 . 3 2 134 134 VAL CA C 13 66.60 0.20 . 1 . . . . 134 VAL CA . 6683 1 1080 . 3 2 134 134 VAL CB C 13 30.73 0.20 . 1 . . . . 134 VAL CB . 6683 1 1081 . 3 2 134 134 VAL N N 15 115.12 0.30 . 1 . . . . 134 VAL N . 6683 1 1082 . 3 2 135 135 ALA H H 1 7.92 0.03 . 1 . . . . 135 ALA H . 6683 1 1083 . 3 2 135 135 ALA C C 13 180.36 0.20 . 1 . . . . 135 ALA C . 6683 1 1084 . 3 2 135 135 ALA CA C 13 55.07 0.20 . 1 . . . . 135 ALA CA . 6683 1 1085 . 3 2 135 135 ALA CB C 13 17.88 0.20 . 1 . . . . 135 ALA CB . 6683 1 1086 . 3 2 135 135 ALA N N 15 126.10 0.30 . 1 . . . . 135 ALA N . 6683 1 1087 . 3 2 136 136 GLY H H 1 8.16 0.03 . 1 . . . . 136 GLY H . 6683 1 1088 . 3 2 136 136 GLY C C 13 177.55 0.20 . 1 . . . . 136 GLY C . 6683 1 1089 . 3 2 136 136 GLY CA C 13 46.89 0.20 . 1 . . . . 136 GLY CA . 6683 1 1090 . 3 2 136 136 GLY N N 15 108.66 0.30 . 1 . . . . 136 GLY N . 6683 1 1091 . 3 2 137 137 VAL H H 1 8.75 0.03 . 1 . . . . 137 VAL H . 6683 1 1092 . 3 2 137 137 VAL C C 13 176.74 0.20 . 1 . . . . 137 VAL C . 6683 1 1093 . 3 2 137 137 VAL CA C 13 66.94 0.20 . 1 . . . . 137 VAL CA . 6683 1 1094 . 3 2 137 137 VAL CB C 13 30.74 0.20 . 1 . . . . 137 VAL CB . 6683 1 1095 . 3 2 137 137 VAL N N 15 125.72 0.30 . 1 . . . . 137 VAL N . 6683 1 1096 . 3 2 138 138 ALA H H 1 7.92 0.03 . 1 . . . . 138 ALA H . 6683 1 1097 . 3 2 138 138 ALA C C 13 179.33 0.20 . 1 . . . . 138 ALA C . 6683 1 1098 . 3 2 138 138 ALA CA C 13 55.55 0.20 . 1 . . . . 138 ALA CA . 6683 1 1099 . 3 2 138 138 ALA CB C 13 17.42 0.20 . 1 . . . . 138 ALA CB . 6683 1 1100 . 3 2 138 138 ALA N N 15 122.43 0.30 . 1 . . . . 138 ALA N . 6683 1 1101 . 3 2 139 139 ASN H H 1 8.16 0.03 . 1 . . . . 139 ASN H . 6683 1 1102 . 3 2 139 139 ASN C C 13 178.60 0.20 . 1 . . . . 139 ASN C . 6683 1 1103 . 3 2 139 139 ASN CA C 13 55.60 0.20 . 1 . . . . 139 ASN CA . 6683 1 1104 . 3 2 139 139 ASN CB C 13 37.91 0.20 . 1 . . . . 139 ASN CB . 6683 1 1105 . 3 2 139 139 ASN N N 15 115.97 0.30 . 1 . . . . 139 ASN N . 6683 1 1106 . 3 2 140 140 ALA H H 1 7.77 0.03 . 1 . . . . 140 ALA H . 6683 1 1107 . 3 2 140 140 ALA C C 13 180.66 0.20 . 1 . . . . 140 ALA C . 6683 1 1108 . 3 2 140 140 ALA CA C 13 54.48 0.20 . 1 . . . . 140 ALA CA . 6683 1 1109 . 3 2 140 140 ALA CB C 13 17.86 0.20 . 1 . . . . 140 ALA CB . 6683 1 1110 . 3 2 140 140 ALA N N 15 124.34 0.30 . 1 . . . . 140 ALA N . 6683 1 1111 . 3 2 141 141 LEU H H 1 7.71 0.03 . 1 . . . . 141 LEU H . 6683 1 1112 . 3 2 141 141 LEU C C 13 178.74 0.20 . 1 . . . . 141 LEU C . 6683 1 1113 . 3 2 141 141 LEU CA C 13 55.71 0.20 . 1 . . . . 141 LEU CA . 6683 1 1114 . 3 2 141 141 LEU N N 15 120.82 0.30 . 1 . . . . 141 LEU N . 6683 1 1115 . 3 2 142 142 ALA H H 1 7.29 0.03 . 1 . . . . 142 ALA H . 6683 1 1116 . 3 2 142 142 ALA C C 13 180.65 0.20 . 1 . . . . 142 ALA C . 6683 1 1117 . 3 2 142 142 ALA CA C 13 51.90 0.20 . 1 . . . . 142 ALA CA . 6683 1 1118 . 3 2 142 142 ALA CB C 13 18.90 0.20 . 1 . . . . 142 ALA CB . 6683 1 1119 . 3 2 142 142 ALA N N 15 121.68 0.30 . 1 . . . . 142 ALA N . 6683 1 1120 . 3 2 143 143 HIS H H 1 7.12 0.03 . 1 . . . . 143 HIS H . 6683 1 1121 . 3 2 143 143 HIS C C 13 176.79 0.20 . 1 . . . . 143 HIS C . 6683 1 1122 . 3 2 143 143 HIS CA C 13 60.98 0.20 . 1 . . . . 143 HIS CA . 6683 1 1123 . 3 2 143 143 HIS CB C 13 29.45 0.20 . 1 . . . . 143 HIS CB . 6683 1 1124 . 3 2 143 143 HIS N N 15 120.13 0.30 . 1 . . . . 143 HIS N . 6683 1 1125 . 3 2 144 144 LYS H H 1 7.93 0.03 . 1 . . . . 144 LYS H . 6683 1 1126 . 3 2 144 144 LYS C C 13 176.79 0.20 . 1 . . . . 144 LYS C . 6683 1 1127 . 3 2 144 144 LYS CA C 13 53.54 0.20 . 1 . . . . 144 LYS CA . 6683 1 1128 . 3 2 144 144 LYS CB C 13 28.60 0.20 . 1 . . . . 144 LYS CB . 6683 1 1129 . 3 2 144 144 LYS N N 15 115.75 0.30 . 1 . . . . 144 LYS N . 6683 1 1130 . 3 2 145 145 TYR H H 1 7.30 0.03 . 1 . . . . 145 TYR H . 6683 1 1131 . 3 2 145 145 TYR C C 13 175.77 0.20 . 1 . . . . 145 TYR C . 6683 1 1132 . 3 2 145 145 TYR CA C 13 60.20 0.20 . 1 . . . . 145 TYR CA . 6683 1 1133 . 3 2 145 145 TYR CB C 13 37.29 0.20 . 1 . . . . 145 TYR CB . 6683 1 1134 . 3 2 145 145 TYR N N 15 121.54 0.30 . 1 . . . . 145 TYR N . 6683 1 1135 . 3 2 146 146 HIS H H 1 7.17 0.03 . 1 . . . . 146 HIS H . 6683 1 1136 . 3 2 146 146 HIS CA C 13 55.35 0.20 . 1 . . . . 146 HIS CA . 6683 1 1137 . 3 2 146 146 HIS CB C 13 30.49 0.20 . 1 . . . . 146 HIS CB . 6683 1 1138 . 3 2 146 146 HIS N N 15 122.98 0.30 . 1 . . . . 146 HIS N . 6683 1 stop_ save_