data_5856 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5856 _Entry.Title ; Backbone Resonances Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-07-03 _Entry.Accession_date 2003-07-03 _Entry.Last_release_date 2004-02-11 _Entry.Original_release_date 2004-02-11 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Jonathan Lukin . A. . 5856 2 Georg Kontaxis . . . 5856 3 Virgil Simplaceanu . . . 5856 4 Yue Yuan . . . 5856 5 Ad Bax . . . 5856 6 Chien Ho . . . 5856 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5856 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 749 5856 '15N chemical shifts' 263 5856 '1H chemical shifts' 263 5856 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 . . 2004-02-11 2003-07-03 original author . 5856 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5856 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 14755170 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Backbone Resonance Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 28 _Citation.Journal_issue 2 _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 203 _Citation.Page_last 204 _Citation.Year 2004 _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 Jonathan Lukin . A. . 5856 1 2 Georg Kontaxis . . . 5856 1 3 Virgil Simplaceanu . . . 5856 1 4 Yue Yuan . . . 5856 1 5 Ad Bax . . . 5856 1 6 Chien Ho . . . 5856 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'backbone assignment' 5856 1 'Hb A in carbonmonoxy form (HbCO A)' 5856 1 'HbCO A' 5856 1 'human normnal adult hemoglobin (Hb A)' 5856 1 NMR 5856 1 recombinant 5856 1 stop_ save_ save_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode reference_1 _Citation.Entry_ID 5856 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8589602 _Citation.Full_citation ; Wishart, S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. M. "1H, 13C and 15N chemical shift referencing in biomolecular NMR", J. Biomol. NMR. 6, 135-140 (1995). ; _Citation.Title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 135 _Citation.Page_last 140 _Citation.Year 1995 _Citation.Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; 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 'D. S.' Wishart D. S. . 5856 2 2 'C. G.' Bigam C. G. . 5856 2 3 J. Yao J. . . 5856 2 4 F. Abildgaard F. . . 5856 2 5 'H. J.' Dyson H. J. . 5856 2 6 E. Oldfield E. . . 5856 2 7 'J. L.' Markley J. L. . 5856 2 8 'B. D.' Sykes B. D. . 5856 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HbCO_A _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HbCO_A _Assembly.Entry_ID 5856 _Assembly.ID 1 _Assembly.Name 'human normal adult hemoglobin carbonmonoxy form' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass 65336 _Assembly.Enzyme_commission_number . _Assembly.Details ; Tetrameric hemoglobin is a homodimer of heterodimers: (alpha-one, beta-one)(alpha-two, bea-two) with overall C2 symmetry. The two alpha subunits are magnetically equivalent and the two beta subunits are also magnetically eqivalent. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID tetramer 5856 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'globin subunit alpha, one' 1 $alpha_subunit . . . native . . . . . 5856 1 2 'globin subunit alpha, two' 1 $alpha_subunit . . . native . . . . . 5856 1 3 'globin subunit beta, one' 2 $beta_subunit . . . native . . . . . 5856 1 4 'globin subunit beta, two' 2 $beta_subunit . . . native . . . . . 5856 1 5 'heme unit, one' 3 $HEM . . . native . . . . . 5856 1 6 'heme unit, two' 3 $HEM . . . native . . . . . 5856 1 7 'carbon monoxide, one' 4 $CMO . . . native . . . . . 5856 1 8 'carbon monoxide, two' 4 $CMO . . . native . . . . . 5856 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 coordination single . 5 . 3 HEM 1 1 FE . 1 . 1 HIS 87 87 NE2 . . . . . . . . . . 5856 1 2 coordination single . 5 . 3 HEM 1 1 FE . 7 . 4 CMO 1 1 C . . . . . . . . . . 5856 1 3 coordination single . 6 . 3 HEM 1 1 FE . 2 . 1 HIS 87 87 NE2 . . . . . . . . . . 5856 1 4 coordination single . 6 . 3 HEM 1 1 FE . 8 . 4 CMO 1 1 C . . . . . . . . . . 5856 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1IRD . . . . . . 5856 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'HbCO A' abbreviation 5856 1 'human normal adult hemoglobin carbonmonoxy form' system 5856 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_alpha_subunit _Entity.Sf_category entity _Entity.Sf_framecode alpha_subunit _Entity.Entry_ID 5856 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'globin subunit 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 . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 141 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 . _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 . . . . 5856 1 2 no BMRB 1102 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 3 no BMRB 2006 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 4 no BMRB 2708 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 5 no BMRB 2710 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 6 no BMRB 6230 . bHb . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 7 no BMRB 6683 . human_normal_adult_hemoglobin_beta_chain_in_deoxy_form . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 8 no BMRB 7125 . globin_subunit_beta . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 9 no BMRB 908 . "hemoglobin A beta chain" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 10 no PDB 1A00 . "Hemoglobin (Val Beta1 Met, Trp Beta37 Tyr) Mutant" . . . . . 100.00 146 98.63 100.00 1.02e-99 . . . . 5856 1 11 no PDB 1A01 . "Hemoglobin (Val Beta1 Met, Trp Beta37 Ala) Mutant" . . . . . 100.00 146 98.63 99.32 4.99e-99 . . . . 5856 1 12 no PDB 1A0U . "Hemoglobin (Val Beta1 Met) Mutant" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 1 13 no PDB 1A0Z . "Hemoglobin (Val Beta1 Met) Mutant" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 1 14 no PDB 1A3N . "Deoxy Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 15 no PDB 1A3O . "Artificial Mutant (Alpha Y42h) Of Deoxy Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 16 no PDB 1ABW . "Deoxy Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 5856 1 17 no PDB 1ABY . "Cyanomet Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 5856 1 18 no PDB 1AJ9 . "R-State Human Carbonmonoxyhemoglobin Alpha-A53s" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 19 no PDB 1B86 . "Human Deoxyhaemoglobin-2,3-Diphosphoglycerate Complex" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 22 no PDB 1BIJ . "Crosslinked, Deoxy Human Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 23 no PDB 1BUW . "Crystal Structure Of S-Nitroso-Nitrosyl Human Hemoglobin A" . . . . . 100.00 146 99.32 99.32 1.91e-99 . . . . 5856 1 24 no PDB 1BZ0 . "Hemoglobin A (Human, Deoxy, High Salt)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 25 no PDB 1BZ1 . "Hemoglobin (Alpha + Met) Variant" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 26 no PDB 1BZZ . "Hemoglobin (Alpha V1m) Mutant" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 27 no PDB 1C7B . "Deoxy Rhb1.0 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 5856 1 28 no PDB 1C7C . "Deoxy Rhb1.1 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 5856 1 29 no PDB 1C7D . "Deoxy Rhb1.2 (Recombinant Hemoglobin)" . . . . . 100.00 146 98.63 99.32 1.23e-99 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 32 no PDB 1CLS . "Cross-Linked Human Hemoglobin Deoxy" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 35 no PDB 1DKE . "Ni Beta Heme Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 41 no PDB 1GBU . "Deoxy (Beta-(C93a,C112g)) Human Hemoglobin" . . . . . 100.00 146 98.63 98.63 3.20e-98 . . . . 5856 1 42 no PDB 1GBV . "(Alpha-Oxy, Beta-(C112g)deoxy) T-State Human Hemoglobin" . . . . . 100.00 146 99.32 99.32 2.92e-99 . . . . 5856 1 43 no PDB 1GLI . "Deoxyhemoglobin T38w (alpha Chains), V1g (alpha And Beta Chains)" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 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 . . . . 5856 1 45 no PDB 1HAB . "Crosslinked Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 46 no PDB 1HAC . "Crosslinked Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 55 no PDB 1HHO . "Structure Of Human Oxyhaemoglobin At 2.1 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 61 no PDB 1J7S . "Crystal Structure Of Deoxy Hbalphayq, A Mutant Of Hba" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 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 . . . . 5856 1 63 no PDB 1J7Y . "Crystal Structure Of Partially Ligated Mutant Of Hba" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 68 no PDB 1LFL . "Deoxy Hemoglobin (90% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 69 no PDB 1LFQ . "Oxy Hemoglobin (93% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 70 no PDB 1LFT . "Oxy Hemoglobin (90% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 71 no PDB 1LFV . "Oxy Hemoglobin (88% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 72 no PDB 1LFY . "Oxy Hemoglobin (84% Relative Humidity)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 73 no PDB 1LFZ . "Oxy Hemoglobin (25% Methanol)" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 78 no PDB 1NIH . "Structure Of Deoxy-Quaternary Haemoglobin With Liganded Beta Subunits" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 82 no PDB 1O1K . "Deoxy Hemoglobin (A,C:v1m; B,D:v1m,V67w)" . . . . . 100.00 146 98.63 99.32 2.89e-99 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 88 no PDB 1QI8 . "Deoxygenated Structure Of A Distal Pocket Hemoglobin Mutant" . . . . . 100.00 146 97.95 98.63 4.57e-99 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 99 no PDB 1RVW . "R State Human Hemoglobin [alpha V96w], Carbonmonoxy" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 100 no PDB 1SDK . "Cross-linked, Carbonmonoxy Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 101 no PDB 1SDL . "Cross-Linked, Carbonmonoxy Hemoglobin A" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 108 no PDB 1XZ2 . "Wild-Type Hemoglobin Deoxy No-Salt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 163 no PDB 1YZI . "A Novel Quaternary Structure Of Human Carbonmonoxy Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 169 no PDB 2DXM . "Neutron Structure Analysis Of Deoxy Human Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 170 no PDB 2H35 . "Solution Structure Of Human Normal Adult Hemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 175 no PDB 2HBS . "The High Resolution Crystal Structure Of Deoxyhemoglobin S" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 183 no PDB 2YRS . "Human Hemoglobin D Los Angeles: Crystal Structure" . . . . . 100.00 146 99.32 100.00 1.61e-100 . . . . 5856 1 184 no PDB 3B75 . "Crystal Structure Of Glycated Human Haemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 1 186 no PDB 3D7O . "Human Hemoglobin, Nitrogen Dioxide Anion Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 193 no PDB 3NL7 . "Human Hemoglobin A Mutant Beta H63w Carbonmonoxy-Form" . . . . . 100.00 146 99.32 99.32 2.27e-99 . . . . 5856 1 194 no PDB 3NMM . "Human Hemoglobin A Mutant Alpha H58w Deoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 1 196 no PDB 3ONZ . "Human Tetrameric Hemoglobin: Proximal Nitrite Ligand At Beta" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 197 no PDB 3OO4 . "R-State Human Hemoglobin: Nitriheme Modified At Alpha" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 198 no PDB 3OO5 . "R-State Human Hemoglobin: Nitriheme Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 199 no PDB 3P5Q . "Ferric R-State Human Aquomethemoglobin" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 200 no PDB 3QJB . "Human Hemoglobin A Mutant Alpha H58l Carbonmonoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 201 no PDB 3QJC . "Human Hemoglobin A Mutant Beta H63l Carbonmonoxy-Form" . . . . . 100.00 146 99.32 99.32 1.53e-99 . . . . 5856 1 202 no PDB 3QJD . "Human Hemoglobin A Mutant Alpha H58l Deoxy-Form" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 203 no PDB 3QJE . "Human Hemoglobin A Mutant Beta H63l Deoxy-Form" . . . . . 100.00 146 99.32 99.32 1.53e-99 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 208 no PDB 3W4U . "Human Zeta-2 Beta-2-s Hemoglobin" . . . . . 100.00 146 99.32 99.32 8.59e-100 . . . . 5856 1 209 no PDB 3WCP . "Deoxyhemoglobin Sh-drug Complex" . . . . . 100.00 146 99.32 99.32 1.91e-99 . . . . 5856 1 210 no PDB 3WHM . "Structure Of Hemoglobin Complex With 18-crown-6" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 215 no PDB 4M4A . "Human Hemoglobin Nitromethane Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 216 no PDB 4M4B . "Human Hemoglobin Nitroethane Modified" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 217 no PDB 4MQC . "Carbonmonoxy Structure Of Hemoglobin Evans Alphav62mbetawt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 218 no PDB 4MQG . "Structure Of Carbonmonoxy Adult Hemoglobin Bristol-alesha Alphawtbetav67m" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 1 219 no PDB 4MQH . "Structure Of Aquomet Hemoglobin Evans Alphav62mbetawt" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 220 no PDB 4MQI . "Structure Of Aquomet Hemoglobin Bristol-alesha Alphawtbetav67m" . . . . . 100.00 146 99.32 100.00 1.37e-100 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 224 no PDB 4N8T . "Human Hemoglobin Nitric Oxide Adduct" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 228 no PDB 6HBW . "Crystal Structure Of Deoxy-human Hemoglobin Beta6 Glu->trp" . . . . . 100.00 146 99.32 99.32 1.73e-99 . . . . 5856 1 229 no DBJ BAG34767 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 230 no EMBL CAA23756 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 231 no EMBL CAA23758 . "beta globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 232 no EMBL CAA23759 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 147 98.63 98.63 5.05e-99 . . . . 5856 1 233 no EMBL CAA43421 . "beta-globin [Gorilla gorilla]" . . . . . 82.19 121 99.17 100.00 4.37e-80 . . . . 5856 1 234 no EMBL CAG38767 . "HBB [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 235 no GB AAA16334 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 236 no GB AAA21100 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 237 no GB AAA21101 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 238 no GB AAA21102 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 239 no GB AAA21103 . "beta-globin [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 240 no PRF 0404170B . "hemoglobin beta" . . . . . 100.00 146 98.63 98.63 5.69e-99 . . . . 5856 1 241 no PRF 0907233B . "hemoglobin beta" . . . . . 100.00 146 100.00 100.00 6.17e-101 . . . . 5856 1 242 no REF NP_000509 . "hemoglobin subunit beta [Homo sapiens]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 243 no REF XP_002822173 . "PREDICTED: hemoglobin subunit beta isoform X2 [Pongo abelii]" . . . . . 100.00 147 98.63 98.63 5.39e-99 . . . . 5856 1 244 no REF XP_003819077 . "PREDICTED: hemoglobin subunit beta [Pan paniscus]" . . . . . 100.00 147 100.00 100.00 5.85e-101 . . . . 5856 1 245 no REF XP_004050595 . "PREDICTED: hemoglobin subunit beta [Gorilla gorilla gorilla]" . . . . . 95.21 143 99.28 100.00 4.51e-95 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 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 . . . . 5856 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'globin subunit alpha' abbreviation 5856 1 'globin subunit alpha' common 5856 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 . 5856 1 2 . LEU . 5856 1 3 . SER . 5856 1 4 . PRO . 5856 1 5 . ALA . 5856 1 6 . ASP . 5856 1 7 . LYS . 5856 1 8 . THR . 5856 1 9 . ASN . 5856 1 10 . VAL . 5856 1 11 . LYS . 5856 1 12 . ALA . 5856 1 13 . ALA . 5856 1 14 . TRP . 5856 1 15 . GLY . 5856 1 16 . LYS . 5856 1 17 . VAL . 5856 1 18 . GLY . 5856 1 19 . ALA . 5856 1 20 . HIS . 5856 1 21 . ALA . 5856 1 22 . GLY . 5856 1 23 . GLU . 5856 1 24 . TYR . 5856 1 25 . GLY . 5856 1 26 . ALA . 5856 1 27 . GLU . 5856 1 28 . ALA . 5856 1 29 . LEU . 5856 1 30 . GLU . 5856 1 31 . ARG . 5856 1 32 . MET . 5856 1 33 . PHE . 5856 1 34 . LEU . 5856 1 35 . SER . 5856 1 36 . PHE . 5856 1 37 . PRO . 5856 1 38 . THR . 5856 1 39 . THR . 5856 1 40 . LYS . 5856 1 41 . THR . 5856 1 42 . TYR . 5856 1 43 . PHE . 5856 1 44 . PRO . 5856 1 45 . HIS . 5856 1 46 . PHE . 5856 1 47 . ASP . 5856 1 48 . LEU . 5856 1 49 . SER . 5856 1 50 . HIS . 5856 1 51 . GLY . 5856 1 52 . SER . 5856 1 53 . ALA . 5856 1 54 . GLN . 5856 1 55 . VAL . 5856 1 56 . LYS . 5856 1 57 . GLY . 5856 1 58 . HIS . 5856 1 59 . GLY . 5856 1 60 . LYS . 5856 1 61 . LYS . 5856 1 62 . VAL . 5856 1 63 . ALA . 5856 1 64 . ASP . 5856 1 65 . ALA . 5856 1 66 . LEU . 5856 1 67 . THR . 5856 1 68 . ASN . 5856 1 69 . ALA . 5856 1 70 . VAL . 5856 1 71 . ALA . 5856 1 72 . HIS . 5856 1 73 . VAL . 5856 1 74 . ASP . 5856 1 75 . ASP . 5856 1 76 . MET . 5856 1 77 . PRO . 5856 1 78 . ASN . 5856 1 79 . ALA . 5856 1 80 . LEU . 5856 1 81 . SER . 5856 1 82 . ALA . 5856 1 83 . LEU . 5856 1 84 . SER . 5856 1 85 . ASP . 5856 1 86 . LEU . 5856 1 87 . HIS . 5856 1 88 . ALA . 5856 1 89 . HIS . 5856 1 90 . LYS . 5856 1 91 . LEU . 5856 1 92 . ARG . 5856 1 93 . VAL . 5856 1 94 . ASP . 5856 1 95 . PRO . 5856 1 96 . VAL . 5856 1 97 . ASN . 5856 1 98 . PHE . 5856 1 99 . LYS . 5856 1 100 . LEU . 5856 1 101 . LEU . 5856 1 102 . SER . 5856 1 103 . HIS . 5856 1 104 . CYS . 5856 1 105 . LEU . 5856 1 106 . LEU . 5856 1 107 . VAL . 5856 1 108 . THR . 5856 1 109 . LEU . 5856 1 110 . ALA . 5856 1 111 . ALA . 5856 1 112 . HIS . 5856 1 113 . LEU . 5856 1 114 . PRO . 5856 1 115 . ALA . 5856 1 116 . GLU . 5856 1 117 . PHE . 5856 1 118 . THR . 5856 1 119 . PRO . 5856 1 120 . ALA . 5856 1 121 . VAL . 5856 1 122 . HIS . 5856 1 123 . ALA . 5856 1 124 . SER . 5856 1 125 . LEU . 5856 1 126 . ASP . 5856 1 127 . LYS . 5856 1 128 . PHE . 5856 1 129 . LEU . 5856 1 130 . ALA . 5856 1 131 . SER . 5856 1 132 . VAL . 5856 1 133 . SER . 5856 1 134 . THR . 5856 1 135 . VAL . 5856 1 136 . LEU . 5856 1 137 . THR . 5856 1 138 . SER . 5856 1 139 . LYS . 5856 1 140 . TYR . 5856 1 141 . ARG . 5856 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 5856 1 . LEU 2 2 5856 1 . SER 3 3 5856 1 . PRO 4 4 5856 1 . ALA 5 5 5856 1 . ASP 6 6 5856 1 . LYS 7 7 5856 1 . THR 8 8 5856 1 . ASN 9 9 5856 1 . VAL 10 10 5856 1 . LYS 11 11 5856 1 . ALA 12 12 5856 1 . ALA 13 13 5856 1 . TRP 14 14 5856 1 . GLY 15 15 5856 1 . LYS 16 16 5856 1 . VAL 17 17 5856 1 . GLY 18 18 5856 1 . ALA 19 19 5856 1 . HIS 20 20 5856 1 . ALA 21 21 5856 1 . GLY 22 22 5856 1 . GLU 23 23 5856 1 . TYR 24 24 5856 1 . GLY 25 25 5856 1 . ALA 26 26 5856 1 . GLU 27 27 5856 1 . ALA 28 28 5856 1 . LEU 29 29 5856 1 . GLU 30 30 5856 1 . ARG 31 31 5856 1 . MET 32 32 5856 1 . PHE 33 33 5856 1 . LEU 34 34 5856 1 . SER 35 35 5856 1 . PHE 36 36 5856 1 . PRO 37 37 5856 1 . THR 38 38 5856 1 . THR 39 39 5856 1 . LYS 40 40 5856 1 . THR 41 41 5856 1 . TYR 42 42 5856 1 . PHE 43 43 5856 1 . PRO 44 44 5856 1 . HIS 45 45 5856 1 . PHE 46 46 5856 1 . ASP 47 47 5856 1 . LEU 48 48 5856 1 . SER 49 49 5856 1 . HIS 50 50 5856 1 . GLY 51 51 5856 1 . SER 52 52 5856 1 . ALA 53 53 5856 1 . GLN 54 54 5856 1 . VAL 55 55 5856 1 . LYS 56 56 5856 1 . GLY 57 57 5856 1 . HIS 58 58 5856 1 . GLY 59 59 5856 1 . LYS 60 60 5856 1 . LYS 61 61 5856 1 . VAL 62 62 5856 1 . ALA 63 63 5856 1 . ASP 64 64 5856 1 . ALA 65 65 5856 1 . LEU 66 66 5856 1 . THR 67 67 5856 1 . ASN 68 68 5856 1 . ALA 69 69 5856 1 . VAL 70 70 5856 1 . ALA 71 71 5856 1 . HIS 72 72 5856 1 . VAL 73 73 5856 1 . ASP 74 74 5856 1 . ASP 75 75 5856 1 . MET 76 76 5856 1 . PRO 77 77 5856 1 . ASN 78 78 5856 1 . ALA 79 79 5856 1 . LEU 80 80 5856 1 . SER 81 81 5856 1 . ALA 82 82 5856 1 . LEU 83 83 5856 1 . SER 84 84 5856 1 . ASP 85 85 5856 1 . LEU 86 86 5856 1 . HIS 87 87 5856 1 . ALA 88 88 5856 1 . HIS 89 89 5856 1 . LYS 90 90 5856 1 . LEU 91 91 5856 1 . ARG 92 92 5856 1 . VAL 93 93 5856 1 . ASP 94 94 5856 1 . PRO 95 95 5856 1 . VAL 96 96 5856 1 . ASN 97 97 5856 1 . PHE 98 98 5856 1 . LYS 99 99 5856 1 . LEU 100 100 5856 1 . LEU 101 101 5856 1 . SER 102 102 5856 1 . HIS 103 103 5856 1 . CYS 104 104 5856 1 . LEU 105 105 5856 1 . LEU 106 106 5856 1 . VAL 107 107 5856 1 . THR 108 108 5856 1 . LEU 109 109 5856 1 . ALA 110 110 5856 1 . ALA 111 111 5856 1 . HIS 112 112 5856 1 . LEU 113 113 5856 1 . PRO 114 114 5856 1 . ALA 115 115 5856 1 . GLU 116 116 5856 1 . PHE 117 117 5856 1 . THR 118 118 5856 1 . PRO 119 119 5856 1 . ALA 120 120 5856 1 . VAL 121 121 5856 1 . HIS 122 122 5856 1 . ALA 123 123 5856 1 . SER 124 124 5856 1 . LEU 125 125 5856 1 . ASP 126 126 5856 1 . LYS 127 127 5856 1 . PHE 128 128 5856 1 . LEU 129 129 5856 1 . ALA 130 130 5856 1 . SER 131 131 5856 1 . VAL 132 132 5856 1 . SER 133 133 5856 1 . THR 134 134 5856 1 . VAL 135 135 5856 1 . LEU 136 136 5856 1 . THR 137 137 5856 1 . SER 138 138 5856 1 . LYS 139 139 5856 1 . TYR 140 140 5856 1 . ARG 141 141 5856 1 stop_ save_ save_beta_subunit _Entity.Sf_category entity _Entity.Sf_framecode beta_subunit _Entity.Entry_ID 5856 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'globin subunit 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 . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 146 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'globin subunit beta' abbreviation 5856 2 'globin subunit beta' common 5856 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 . 5856 2 2 . HIS . 5856 2 3 . LEU . 5856 2 4 . THR . 5856 2 5 . PRO . 5856 2 6 . GLU . 5856 2 7 . GLU . 5856 2 8 . LYS . 5856 2 9 . SER . 5856 2 10 . ALA . 5856 2 11 . VAL . 5856 2 12 . THR . 5856 2 13 . ALA . 5856 2 14 . LEU . 5856 2 15 . TRP . 5856 2 16 . GLY . 5856 2 17 . LYS . 5856 2 18 . VAL . 5856 2 19 . ASN . 5856 2 20 . VAL . 5856 2 21 . ASP . 5856 2 22 . GLU . 5856 2 23 . VAL . 5856 2 24 . GLY . 5856 2 25 . GLY . 5856 2 26 . GLU . 5856 2 27 . ALA . 5856 2 28 . LEU . 5856 2 29 . GLY . 5856 2 30 . ARG . 5856 2 31 . LEU . 5856 2 32 . LEU . 5856 2 33 . VAL . 5856 2 34 . VAL . 5856 2 35 . TYR . 5856 2 36 . PRO . 5856 2 37 . TRP . 5856 2 38 . THR . 5856 2 39 . GLN . 5856 2 40 . ARG . 5856 2 41 . PHE . 5856 2 42 . PHE . 5856 2 43 . GLU . 5856 2 44 . SER . 5856 2 45 . PHE . 5856 2 46 . GLY . 5856 2 47 . ASP . 5856 2 48 . LEU . 5856 2 49 . SER . 5856 2 50 . THR . 5856 2 51 . PRO . 5856 2 52 . ASP . 5856 2 53 . ALA . 5856 2 54 . VAL . 5856 2 55 . MET . 5856 2 56 . GLY . 5856 2 57 . ASN . 5856 2 58 . PRO . 5856 2 59 . LYS . 5856 2 60 . VAL . 5856 2 61 . LYS . 5856 2 62 . ALA . 5856 2 63 . HIS . 5856 2 64 . GLY . 5856 2 65 . LYS . 5856 2 66 . LYS . 5856 2 67 . VAL . 5856 2 68 . LEU . 5856 2 69 . GLY . 5856 2 70 . ALA . 5856 2 71 . PHE . 5856 2 72 . SER . 5856 2 73 . ASP . 5856 2 74 . GLY . 5856 2 75 . LEU . 5856 2 76 . ALA . 5856 2 77 . HIS . 5856 2 78 . LEU . 5856 2 79 . ASP . 5856 2 80 . ASN . 5856 2 81 . LEU . 5856 2 82 . LYS . 5856 2 83 . GLY . 5856 2 84 . THR . 5856 2 85 . PHE . 5856 2 86 . ALA . 5856 2 87 . THR . 5856 2 88 . LEU . 5856 2 89 . SER . 5856 2 90 . GLU . 5856 2 91 . LEU . 5856 2 92 . HIS . 5856 2 93 . CYS . 5856 2 94 . ASP . 5856 2 95 . LYS . 5856 2 96 . LEU . 5856 2 97 . HIS . 5856 2 98 . VAL . 5856 2 99 . ASP . 5856 2 100 . PRO . 5856 2 101 . GLU . 5856 2 102 . ASN . 5856 2 103 . PHE . 5856 2 104 . ARG . 5856 2 105 . LEU . 5856 2 106 . LEU . 5856 2 107 . GLY . 5856 2 108 . ASN . 5856 2 109 . VAL . 5856 2 110 . LEU . 5856 2 111 . VAL . 5856 2 112 . CYS . 5856 2 113 . VAL . 5856 2 114 . LEU . 5856 2 115 . ALA . 5856 2 116 . HIS . 5856 2 117 . HIS . 5856 2 118 . PHE . 5856 2 119 . GLY . 5856 2 120 . LYS . 5856 2 121 . GLU . 5856 2 122 . PHE . 5856 2 123 . THR . 5856 2 124 . PRO . 5856 2 125 . PRO . 5856 2 126 . VAL . 5856 2 127 . GLN . 5856 2 128 . ALA . 5856 2 129 . ALA . 5856 2 130 . TYR . 5856 2 131 . GLN . 5856 2 132 . LYS . 5856 2 133 . VAL . 5856 2 134 . VAL . 5856 2 135 . ALA . 5856 2 136 . GLY . 5856 2 137 . VAL . 5856 2 138 . ALA . 5856 2 139 . ASN . 5856 2 140 . ALA . 5856 2 141 . LEU . 5856 2 142 . ALA . 5856 2 143 . HIS . 5856 2 144 . LYS . 5856 2 145 . TYR . 5856 2 146 . HIS . 5856 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 5856 2 . HIS 2 2 5856 2 . LEU 3 3 5856 2 . THR 4 4 5856 2 . PRO 5 5 5856 2 . GLU 6 6 5856 2 . GLU 7 7 5856 2 . LYS 8 8 5856 2 . SER 9 9 5856 2 . ALA 10 10 5856 2 . VAL 11 11 5856 2 . THR 12 12 5856 2 . ALA 13 13 5856 2 . LEU 14 14 5856 2 . TRP 15 15 5856 2 . GLY 16 16 5856 2 . LYS 17 17 5856 2 . VAL 18 18 5856 2 . ASN 19 19 5856 2 . VAL 20 20 5856 2 . ASP 21 21 5856 2 . GLU 22 22 5856 2 . VAL 23 23 5856 2 . GLY 24 24 5856 2 . GLY 25 25 5856 2 . GLU 26 26 5856 2 . ALA 27 27 5856 2 . LEU 28 28 5856 2 . GLY 29 29 5856 2 . ARG 30 30 5856 2 . LEU 31 31 5856 2 . LEU 32 32 5856 2 . VAL 33 33 5856 2 . VAL 34 34 5856 2 . TYR 35 35 5856 2 . PRO 36 36 5856 2 . TRP 37 37 5856 2 . THR 38 38 5856 2 . GLN 39 39 5856 2 . ARG 40 40 5856 2 . PHE 41 41 5856 2 . PHE 42 42 5856 2 . GLU 43 43 5856 2 . SER 44 44 5856 2 . PHE 45 45 5856 2 . GLY 46 46 5856 2 . ASP 47 47 5856 2 . LEU 48 48 5856 2 . SER 49 49 5856 2 . THR 50 50 5856 2 . PRO 51 51 5856 2 . ASP 52 52 5856 2 . ALA 53 53 5856 2 . VAL 54 54 5856 2 . MET 55 55 5856 2 . GLY 56 56 5856 2 . ASN 57 57 5856 2 . PRO 58 58 5856 2 . LYS 59 59 5856 2 . VAL 60 60 5856 2 . LYS 61 61 5856 2 . ALA 62 62 5856 2 . HIS 63 63 5856 2 . GLY 64 64 5856 2 . LYS 65 65 5856 2 . LYS 66 66 5856 2 . VAL 67 67 5856 2 . LEU 68 68 5856 2 . GLY 69 69 5856 2 . ALA 70 70 5856 2 . PHE 71 71 5856 2 . SER 72 72 5856 2 . ASP 73 73 5856 2 . GLY 74 74 5856 2 . LEU 75 75 5856 2 . ALA 76 76 5856 2 . HIS 77 77 5856 2 . LEU 78 78 5856 2 . ASP 79 79 5856 2 . ASN 80 80 5856 2 . LEU 81 81 5856 2 . LYS 82 82 5856 2 . GLY 83 83 5856 2 . THR 84 84 5856 2 . PHE 85 85 5856 2 . ALA 86 86 5856 2 . THR 87 87 5856 2 . LEU 88 88 5856 2 . SER 89 89 5856 2 . GLU 90 90 5856 2 . LEU 91 91 5856 2 . HIS 92 92 5856 2 . CYS 93 93 5856 2 . ASP 94 94 5856 2 . LYS 95 95 5856 2 . LEU 96 96 5856 2 . HIS 97 97 5856 2 . VAL 98 98 5856 2 . ASP 99 99 5856 2 . PRO 100 100 5856 2 . GLU 101 101 5856 2 . ASN 102 102 5856 2 . PHE 103 103 5856 2 . ARG 104 104 5856 2 . LEU 105 105 5856 2 . LEU 106 106 5856 2 . GLY 107 107 5856 2 . ASN 108 108 5856 2 . VAL 109 109 5856 2 . LEU 110 110 5856 2 . VAL 111 111 5856 2 . CYS 112 112 5856 2 . VAL 113 113 5856 2 . LEU 114 114 5856 2 . ALA 115 115 5856 2 . HIS 116 116 5856 2 . HIS 117 117 5856 2 . PHE 118 118 5856 2 . GLY 119 119 5856 2 . LYS 120 120 5856 2 . GLU 121 121 5856 2 . PHE 122 122 5856 2 . THR 123 123 5856 2 . PRO 124 124 5856 2 . PRO 125 125 5856 2 . VAL 126 126 5856 2 . GLN 127 127 5856 2 . ALA 128 128 5856 2 . ALA 129 129 5856 2 . TYR 130 130 5856 2 . GLN 131 131 5856 2 . LYS 132 132 5856 2 . VAL 133 133 5856 2 . VAL 134 134 5856 2 . ALA 135 135 5856 2 . GLY 136 136 5856 2 . VAL 137 137 5856 2 . ALA 138 138 5856 2 . ASN 139 139 5856 2 . ALA 140 140 5856 2 . LEU 141 141 5856 2 . ALA 142 142 5856 2 . HIS 143 143 5856 2 . LYS 144 144 5856 2 . TYR 145 145 5856 2 . HIS 146 146 5856 2 stop_ save_ save_HEM _Entity.Sf_category entity _Entity.Sf_framecode HEM _Entity.Entry_ID 5856 _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 . 5856 3 stop_ save_ save_CMO _Entity.Sf_category entity _Entity.Sf_framecode CMO _Entity.Entry_ID 5856 _Entity.ID 4 _Entity.BMRB_code . _Entity.Name CMO _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 CMO _Entity.Nonpolymer_comp_label $chem_comp_CMO _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 4 _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 . CMO . 5856 4 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 5856 _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 $alpha_subunit . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . blood . . . 'red blood cell' . . . . . . . . . . . . . 5856 1 2 2 $beta_subunit . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . blood . . . 'red blood cell' . . . . . . . . . . . . . 5856 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 5856 _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 $alpha_subunit . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli JM109 . . . . . . . . . . . . plasmid . . pHE2 . . . . . . 5856 1 2 2 $beta_subunit . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli JM109 . . . . . . . . . . . . plasmid . . pHE2 . . . . . . 5856 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 5856 _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 Wed Jul 27 14:00:32 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 5856 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 5856 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 5856 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 5856 HEM FEDYMSUPMFCVOD-UJJXFSCMSA-N InChIKey InChI 1.02 5856 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 5856 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 5856 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 5856 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 5856 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 . 5856 HEM CHB . CHB . . C . . N 0 . . . . yes no . . . . 3.258 . -17.744 . 35.477 . 1.458 -3.419 0.306 2 . 5856 HEM CHC . CHC . . C . . N 0 . . . . yes no . . . . 1.703 . -21.900 . 33.637 . 4.701 0.169 -0.069 3 . 5856 HEM CHD . CHD . . C . . N 0 . . . . yes no . . . . 1.149 . -23.677 . 38.059 . 1.075 3.460 0.018 4 . 5856 HEM C1A . C1A . . C . . N 0 . . . . yes no . . . . 3.031 . -18.673 . 38.872 . -1.436 -1.305 0.380 5 . 5856 HEM C2A . C2A . . C . . N 0 . . . . yes no . . . . 3.578 . -17.325 . 39.013 . -2.015 -2.587 0.320 6 . 5856 HEM C3A . C3A . . C . . N 0 . . . . yes no . . . . 3.705 . -16.820 . 37.785 . -1.009 -3.500 0.270 7 . 5856 HEM C4A . C4A . . C . . N 0 . . . . yes no . . . . 3.256 . -17.863 . 36.862 . 0.216 -2.803 0.298 8 . 5856 HEM CMA . CMA . . C . . N 0 . . . . no no . . . . 4.227 . -15.469 . 37.393 . -1.175 -4.996 0.197 9 . 5856 HEM CAA . CAA . . C . . N 0 . . . . no no . . . . 3.945 . -16.670 . 40.296 . -3.490 -2.893 0.314 10 . 5856 HEM CBA . CBA . . C . . N 0 . . . . no no . . . . 5.391 . -17.138 . 40.581 . -3.998 -2.926 -1.129 11 . 5856 HEM CGA . CGA . . C . . N 0 . . . . no no . . . . 6.095 . -16.663 . 41.825 . -5.473 -3.232 -1.136 12 . 5856 HEM O1A . O1A . . O . . N 0 . . . . no no . . . . 7.098 . -15.928 . 41.683 . -6.059 -3.405 -0.094 13 . 5856 HEM O2A . O2A . . O . . N 0 . . . . no no . . . . 5.657 . -17.040 . 42.940 . -6.137 -3.311 -2.300 14 . 5856 HEM C1B . C1B . . C . . N 0 . . . . yes no . . . . 2.888 . -18.698 . 34.579 . 2.664 -2.707 0.308 15 . 5856 HEM C2B . C2B . . C . . N 0 . . . . yes no . . . . 2.933 . -18.535 . 33.146 . 3.937 -3.328 0.418 16 . 5856 HEM C3B . C3B . . C . . N 0 . . . . yes no . . . . 2.499 . -19.716 . 32.632 . 4.874 -2.341 0.314 17 . 5856 HEM C4B . C4B . . C . . N 0 . . . . yes no . . . . 2.187 . -20.580 . 33.743 . 4.117 -1.079 0.139 18 . 5856 HEM CMB . CMB . . C . . N 0 . . . . no no . . . . 3.391 . -17.290 . 32.422 . 4.203 -4.798 0.613 19 . 5856 HEM CAB . CAB . . C . . N 0 . . . . no no . . . . 2.345 . -20.140 . 31.217 . 6.339 -2.497 0.365 20 . 5856 HEM CBB . CBB . . C . . N 0 . . . . no no . . . . 1.755 . -19.492 . 30.233 . 6.935 -3.419 -0.385 21 . 5856 HEM C1C . C1C . . C . . N 0 . . . . yes no . . . . 1.395 . -22.786 . 34.659 . 3.964 1.345 -0.174 22 . 5856 HEM C2C . C2C . . C . . N 0 . . . . yes no . . . . 0.854 . -24.130 . 34.500 . 4.531 2.601 -0.445 23 . 5856 HEM C3C . C3C . . C . . N 0 . . . . yes no . . . . 0.689 . -24.626 . 35.757 . 3.510 3.536 -0.437 24 . 5856 HEM C4C . C4C . . C . . N 0 . . . . yes no . . . . 1.139 . -23.583 . 36.674 . 2.304 2.846 -0.139 25 . 5856 HEM CMC . CMC . . C . . N 0 . . . . no no . . . . 0.550 . -24.782 . 33.175 . 5.991 2.880 -0.697 26 . 5856 HEM CAC . CAC . . C . . N 0 . . . . no no . . . . 0.164 . -25.943 . 36.196 . 3.649 4.981 -0.692 27 . 5856 HEM CBC . CBC . . C . . N 0 . . . . no no . . . . 0.498 . -27.158 . 35.750 . 4.201 5.407 -1.823 28 . 5856 HEM C1D . C1D . . C . . N 0 . . . . yes no . . . . 1.550 . -22.718 . 38.980 . -0.102 2.753 0.298 29 . 5856 HEM C2D . C2D . . C . . N 0 . . . . yes no . . . . 1.513 . -22.879 . 40.415 . -1.382 3.388 0.641 30 . 5856 HEM C3D . C3D . . C . . N 0 . . . . yes no . . . . 1.951 . -21.691 . 40.929 . -2.283 2.389 0.774 31 . 5856 HEM C4D . C4D . . C . . N 0 . . . . yes no . . . . 2.277 . -20.826 . 39.811 . -1.561 1.137 0.511 32 . 5856 HEM CMD . CMD . . C . . N 0 . . . . no no . . . . 1.055 . -24.094 . 41.156 . -1.639 4.863 0.811 33 . 5856 HEM CAD . CAD . . C . . N 0 . . . . no no . . . . 2.048 . -21.326 . 42.352 . -3.741 2.532 1.123 34 . 5856 HEM CBD . CBD . . C . . N 0 . . . . no no . . . . 0.741 . -20.498 . 42.530 . -4.573 2.563 -0.160 35 . 5856 HEM CGD . CGD . . C . . N 0 . . . . no no . . . . 0.578 . -19.987 . 43.892 . -6.032 2.706 0.189 36 . 5856 HEM O1D . O1D . . O . . N 0 . . . . no no . . . . 1.387 . -19.103 . 44.303 . -6.372 2.776 1.347 37 . 5856 HEM O2D . O2D . . O . . N 0 . . . . no no . . . . -0.401 . -20.468 . 44.537 . -6.954 2.755 -0.785 38 . 5856 HEM NA . NA . . N . . N 0 . . . . yes no . . . . 2.863 . -18.969 . 37.554 . -0.068 -1.456 0.321 39 . 5856 HEM NB . NB . . N . . N 0 . . . . yes no . . . . 2.439 . -19.944 . 34.911 . 2.820 -1.386 0.207 40 . 5856 HEM NC . NC . . N . . N 0 . . . . yes no . . . . 1.537 . -22.509 . 35.976 . 2.604 1.506 -0.033 41 . 5856 HEM ND . ND . . N . . N 0 . . . . yes no . . . . 2.008 . -21.465 . 38.663 . -0.276 1.431 0.298 42 . 5856 HEM FE . FE . . FE . . S 0 . . . . no no . . . . 2.196 . -20.749 . 36.814 . 1.010 0.157 -0.060 43 . 5856 HEM HHB . HHB . . H . . N 0 . . . . no no . . . . 3.587 . -16.798 . 35.072 . 1.498 -4.508 0.309 44 . 5856 HEM HHC . HHC . . H . . N 0 . . . . no no . . . . 1.553 . -22.268 . 32.633 . 5.786 0.229 -0.153 45 . 5856 HEM HHD . HHD . . H . . N 0 . . . . no no . . . . 0.802 . -24.613 . 38.472 . 1.018 4.543 -0.083 46 . 5856 HEM HMA . HMA . . H . . N 0 . . . . no no . . . . 5.316 . -15.524 . 37.249 . -1.220 -5.306 -0.847 47 . 5856 HEM HMAA . HMAA . . H . . N 0 . . . . no no . . . . 3.749 . -15.149 . 36.455 . -0.328 -5.480 0.683 48 . 5856 HEM HMAB . HMAB . . H . . N 0 . . . . no no . . . . 3.998 . -14.743 . 38.187 . -2.097 -5.285 0.702 49 . 5856 HEM HAA . HAA . . H . . N 0 . . . . no no . . . . 3.894 . -15.575 . 40.209 . -3.662 -3.862 0.782 50 . 5856 HEM HAAA . HAAA . . H . . N 0 . . . . no no . . . . 3.264 . -16.976 . 41.104 . -4.024 -2.121 0.869 51 . 5856 HEM HBA . HBA . . H . . N 0 . . . . no no . . . . 5.351 . -18.235 . 40.650 . -3.825 -1.956 -1.597 52 . 5856 HEM HBAA . HBAA . . H . . N 0 . . . . no no . . . . 5.999 . -16.792 . 39.732 . -3.464 -3.697 -1.684 53 . 5856 HEM HMB . HMB . . H . . N 0 . . . . no no . . . . 3.319 . -17.449 . 31.336 . 3.256 -5.336 0.660 54 . 5856 HEM HMBA . HMBA . . H . . N 0 . . . . no no . . . . 2.753 . -16.442 . 32.711 . 4.794 -5.175 -0.222 55 . 5856 HEM HMBB . HMBB . . H . . N 0 . . . . no no . . . . 4.435 . -17.072 . 32.692 . 4.752 -4.948 1.543 56 . 5856 HEM HAB . HAB . . H . . N 0 . . . . no no . . . . 2.770 . -21.100 . 30.963 . 6.927 -1.863 1.011 57 . 5856 HEM HBB . HBB . . H . . N 0 . . . . no no . . . . 1.719 . -19.927 . 29.245 . 7.994 -3.600 -0.277 58 . 5856 HEM HBBA . HBBA . . H . . N 0 . . . . no no . . . . 1.308 . -18.526 . 30.414 . 6.360 -3.987 -1.102 59 . 5856 HEM HMC . HMC . . H . . N 0 . . . . no no . . . . 1.438 . -25.328 . 32.822 . 6.554 1.949 -0.639 60 . 5856 HEM HMCA . HMCA . . H . . N 0 . . . . no no . . . . -0.288 . -25.484 . 33.296 . 6.110 3.316 -1.689 61 . 5856 HEM HMCB . HMCB . . H . . N 0 . . . . no no . . . . 0.278 . -24.010 . 32.440 . 6.362 3.578 0.053 62 . 5856 HEM HAC . HAC . . H . . N 0 . . . . no no . . . . -0.583 . -25.916 . 36.975 . 3.303 5.694 0.042 63 . 5856 HEM HBC . HBC . . H . . N 0 . . . . no no . . . . 0.027 . -28.035 . 36.169 . 4.614 4.696 -2.523 64 . 5856 HEM HBCA . HBCA . . H . . N 0 . . . . no no . . . . 1.239 . -27.263 . 34.971 . 4.235 6.464 -2.043 65 . 5856 HEM HMD . HMD . . H . . N 0 . . . . no no . . . . 1.142 . -23.919 . 42.238 . -0.715 5.415 0.639 66 . 5856 HEM HMDA . HMDA . . H . . N 0 . . . . no no . . . . 0.006 . -24.304 . 40.902 . -2.394 5.185 0.094 67 . 5856 HEM HMDB . HMDB . . H . . N 0 . . . . no no . . . . 1.680 . -24.954 . 40.872 . -1.994 5.055 1.824 68 . 5856 HEM HAD . HAD . . H . . N 0 . . . . no no . . . . 2.081 . -22.206 . 43.011 . -4.052 1.687 1.738 69 . 5856 HEM HADA . HADA . . H . . N 0 . . . . no no . . . . 2.951 . -20.739 . 42.575 . -3.893 3.459 1.677 70 . 5856 HEM HBD . HBD . . H . . N 0 . . . . no no . . . . 0.775 . -19.642 . 41.839 . -4.262 3.408 -0.775 71 . 5856 HEM HBDA . HBDA . . H . . N 0 . . . . no no . . . . -0.116 . -21.147 . 42.297 . -4.421 1.636 -0.714 72 . 5856 HEM H2A . H2A . . H . . N 0 . . . . no no . . . . 6.201 . -16.682 . 43.632 . -7.082 -3.510 -2.254 73 . 5856 HEM H2D . H2D . . H . . N 0 . . . . no no . . . . -0.445 . -20.063 . 45.395 . -7.877 2.847 -0.512 74 . 5856 HEM HHA . HHA . . H . . N 0 . . . . no no . . . . 2.913 . -19.150 . 40.893 . -3.246 -0.188 0.567 75 . 5856 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 . 5856 HEM 2 . DOUB CHA C4D yes N 2 . 5856 HEM 3 . SING CHA HHA no N 3 . 5856 HEM 4 . SING CHB C4A yes N 4 . 5856 HEM 5 . DOUB CHB C1B yes N 5 . 5856 HEM 6 . SING CHB HHB no N 6 . 5856 HEM 7 . SING CHC C4B yes N 7 . 5856 HEM 8 . DOUB CHC C1C yes N 8 . 5856 HEM 9 . SING CHC HHC no N 9 . 5856 HEM 10 . DOUB CHD C4C yes N 10 . 5856 HEM 11 . SING CHD C1D yes N 11 . 5856 HEM 12 . SING CHD HHD no N 12 . 5856 HEM 13 . DOUB C1A C2A yes N 13 . 5856 HEM 14 . SING C1A NA yes N 14 . 5856 HEM 15 . SING C2A C3A yes N 15 . 5856 HEM 16 . SING C2A CAA no N 16 . 5856 HEM 17 . DOUB C3A C4A yes N 17 . 5856 HEM 18 . SING C3A CMA no N 18 . 5856 HEM 19 . SING C4A NA yes N 19 . 5856 HEM 20 . SING CMA HMA no N 20 . 5856 HEM 21 . SING CMA HMAA no N 21 . 5856 HEM 22 . SING CMA HMAB no N 22 . 5856 HEM 23 . SING CAA CBA no N 23 . 5856 HEM 24 . SING CAA HAA no N 24 . 5856 HEM 25 . SING CAA HAAA no N 25 . 5856 HEM 26 . SING CBA CGA no N 26 . 5856 HEM 27 . SING CBA HBA no N 27 . 5856 HEM 28 . SING CBA HBAA no N 28 . 5856 HEM 29 . DOUB CGA O1A no N 29 . 5856 HEM 30 . SING CGA O2A no N 30 . 5856 HEM 31 . SING C1B C2B no N 31 . 5856 HEM 32 . SING C1B NB yes N 32 . 5856 HEM 33 . DOUB C2B C3B yes N 33 . 5856 HEM 34 . SING C2B CMB yes N 34 . 5856 HEM 35 . SING C3B C4B no N 35 . 5856 HEM 36 . SING C3B CAB yes N 36 . 5856 HEM 37 . DOUB C4B NB no N 37 . 5856 HEM 38 . SING CMB HMB yes N 38 . 5856 HEM 39 . SING CMB HMBA no N 39 . 5856 HEM 40 . SING CMB HMBB no N 40 . 5856 HEM 41 . DOUB CAB CBB no N 41 . 5856 HEM 42 . SING CAB HAB no N 42 . 5856 HEM 43 . SING CBB HBB no N 43 . 5856 HEM 44 . SING CBB HBBA no N 44 . 5856 HEM 45 . SING C1C C2C no N 45 . 5856 HEM 46 . SING C1C NC yes N 46 . 5856 HEM 47 . DOUB C2C C3C yes N 47 . 5856 HEM 48 . SING C2C CMC yes N 48 . 5856 HEM 49 . SING C3C C4C no N 49 . 5856 HEM 50 . SING C3C CAC yes N 50 . 5856 HEM 51 . SING C4C NC no N 51 . 5856 HEM 52 . SING CMC HMC yes N 52 . 5856 HEM 53 . SING CMC HMCA no N 53 . 5856 HEM 54 . SING CMC HMCB no N 54 . 5856 HEM 55 . DOUB CAC CBC no N 55 . 5856 HEM 56 . SING CAC HAC no N 56 . 5856 HEM 57 . SING CBC HBC no N 57 . 5856 HEM 58 . SING CBC HBCA no N 58 . 5856 HEM 59 . SING C1D C2D no N 59 . 5856 HEM 60 . DOUB C1D ND yes N 60 . 5856 HEM 61 . DOUB C2D C3D yes N 61 . 5856 HEM 62 . SING C2D CMD yes N 62 . 5856 HEM 63 . SING C3D C4D no N 63 . 5856 HEM 64 . SING C3D CAD yes N 64 . 5856 HEM 65 . SING C4D ND no N 65 . 5856 HEM 66 . SING CMD HMD yes N 66 . 5856 HEM 67 . SING CMD HMDA no N 67 . 5856 HEM 68 . SING CMD HMDB no N 68 . 5856 HEM 69 . SING CAD CBD no N 69 . 5856 HEM 70 . SING CAD HAD no N 70 . 5856 HEM 71 . SING CAD HADA no N 71 . 5856 HEM 72 . SING CBD CGD no N 72 . 5856 HEM 73 . SING CBD HBD no N 73 . 5856 HEM 74 . SING CBD HBDA no N 74 . 5856 HEM 75 . DOUB CGD O1D no N 75 . 5856 HEM 76 . SING CGD O2D no N 76 . 5856 HEM 77 . SING O2A H2A no N 77 . 5856 HEM 78 . SING O2D H2D no N 78 . 5856 HEM 79 . SING FE NA no N 79 . 5856 HEM 80 . SING FE NB no N 80 . 5856 HEM 81 . SING FE NC no N 81 . 5856 HEM 82 . SING FE ND no N 82 . 5856 HEM stop_ save_ save_chem_comp_CMO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CMO _Chem_comp.Entry_ID 5856 _Chem_comp.ID CMO _Chem_comp.Provenance . _Chem_comp.Name 'CARBON MONOXIDE' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CMO _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CMO _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 . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C O' _Chem_comp.Formula_weight 28.010 _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 no _Chem_comp.Model_coordinates_db_code 1BZR _Chem_comp.Processing_site PDBE _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 Wed Jul 27 14:02:43 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 [C-]#[O+] SMILES CACTVS 3.341 5856 CMO [C-]#[O+] SMILES 'OpenEye OEToolkits' 1.5.0 5856 CMO [C-]#[O+] SMILES_CANONICAL CACTVS 3.341 5856 CMO [C-]#[O+] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5856 CMO InChI=1S/CO/c1-2 InChI InChI 1.03 5856 CMO [O+]#[C-] SMILES ACDLabs 10.04 5856 CMO UGFAIRIUMAVXCW-UHFFFAOYSA-N InChIKey InChI 1.03 5856 CMO 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 'carbon monooxide' 'SYSTEMATIC NAME' ACDLabs 10.04 5856 CMO 'carbon monoxide' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5856 CMO 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 C . C . . C . . N -1 . . . . no no . . . . -0.296 . 8.526 . 17.112 . 0.607 0.000 0.000 1 . 5856 CMO O . O . . O . . N 1 . . . . no no . . . . 0.023 . 7.997 . 18.053 . -0.600 0.000 0.000 2 . 5856 CMO 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 . TRIP C O no N 1 . 5856 CMO stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 5856 _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 'globin subunit alpha' '[U-2H; U-13C; U-15N]' . . 1 $alpha_subunit . . 1.0 . . mM . . . . 5856 1 2 'globin subunit beta' '[U-2H; U-13C; U-15N]' . . 2 $beta_subunit . . 1.0 . . mM . . . . 5856 1 3 'Na phosphate' . . . . . . . 0.1 . . M . . . . 5856 1 4 H2O . . . . . . . 90 . . % . . . . 5856 1 5 D2O . . . . . . . 10 . . % . . . . 5856 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 5856 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'Aqueous phosphate buffer.' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.0 . n/a 5856 1 temperature 302.0 0.1 K 5856 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 5856 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 5856 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 5856 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 5856 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 5856 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5856 _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 internal indirect 0.251449530 . . . 2 $reference_1 . . . . 5856 1 H 1 H2O protons . . . . ppm 4.76 internal direct 1.0 . . . 2 $reference_1 . . . . 5856 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 internal indirect 0.101329150 . . . 2 $reference_1 . . . . 5856 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_chemical_shift_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_1 _Assigned_chem_shift_list.Entry_ID 5856 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 5856 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 57.250 0.100 . 1 . . . . . . . . 5856 1 2 . 1 1 1 1 VAL C C 13 178.050 0.100 . 1 . . . . . . . . 5856 1 3 . 1 1 2 2 LEU H H 1 7.010 0.030 . 1 . . . . . . . . 5856 1 4 . 1 1 2 2 LEU N N 15 116.590 0.050 . 1 . . . . . . . . 5856 1 5 . 1 1 2 2 LEU CA C 13 54.110 0.100 . 1 . . . . . . . . 5856 1 6 . 1 1 2 2 LEU CB C 13 40.250 0.100 . 1 . . . . . . . . 5856 1 7 . 1 1 2 2 LEU C C 13 176.470 0.100 . 1 . . . . . . . . 5856 1 8 . 1 1 3 3 SER H H 1 9.750 0.030 . 1 . . . . . . . . 5856 1 9 . 1 1 3 3 SER N N 15 122.080 0.050 . 1 . . . . . . . . 5856 1 10 . 1 1 3 3 SER CA C 13 56.270 0.100 . 1 . . . . . . . . 5856 1 11 . 1 1 3 3 SER C C 13 173.470 0.100 . 1 . . . . . . . . 5856 1 12 . 1 1 4 4 PRO CA C 13 65.840 0.100 . 1 . . . . . . . . 5856 1 13 . 1 1 4 4 PRO C C 13 179.440 0.100 . 1 . . . . . . . . 5856 1 14 . 1 1 5 5 ALA H H 1 7.900 0.030 . 1 . . . . . . . . 5856 1 15 . 1 1 5 5 ALA N N 15 119.940 0.050 . 1 . . . . . . . . 5856 1 16 . 1 1 5 5 ALA CA C 13 54.360 0.100 . 1 . . . . . . . . 5856 1 17 . 1 1 5 5 ALA C C 13 179.895 0.015 . 1 . . . . . . . . 5856 1 18 . 1 1 6 6 ASP H H 1 8.060 0.030 . 1 . . . . . . . . 5856 1 19 . 1 1 6 6 ASP N N 15 118.380 0.050 . 1 . . . . . . . . 5856 1 20 . 1 1 6 6 ASP CA C 13 57.040 0.070 . 1 . . . . . . . . 5856 1 21 . 1 1 6 6 ASP C C 13 178.720 0.100 . 1 . . . . . . . . 5856 1 22 . 1 1 7 7 LYS H H 1 8.080 0.030 . 1 . . . . . . . . 5856 1 23 . 1 1 7 7 LYS N N 15 119.050 0.050 . 1 . . . . . . . . 5856 1 24 . 1 1 7 7 LYS CA C 13 60.575 0.055 . 1 . . . . . . . . 5856 1 25 . 1 1 7 7 LYS CB C 13 31.240 0.010 . 1 . . . . . . . . 5856 1 26 . 1 1 7 7 LYS C C 13 178.410 0.030 . 1 . . . . . . . . 5856 1 27 . 1 1 8 8 THR H H 1 7.990 0.030 . 1 . . . . . . . . 5856 1 28 . 1 1 8 8 THR N N 15 116.110 0.050 . 1 . . . . . . . . 5856 1 29 . 1 1 8 8 THR CA C 13 66.190 0.000 . 1 . . . . . . . . 5856 1 30 . 1 1 8 8 THR CB C 13 68.050 0.100 . 1 . . . . . . . . 5856 1 31 . 1 1 8 8 THR C C 13 176.740 0.100 . 1 . . . . . . . . 5856 1 32 . 1 1 9 9 ASN H H 1 8.280 0.030 . 1 . . . . . . . . 5856 1 33 . 1 1 9 9 ASN N N 15 121.210 0.050 . 1 . . . . . . . . 5856 1 34 . 1 1 9 9 ASN CA C 13 55.090 0.100 . 1 . . . . . . . . 5856 1 35 . 1 1 9 9 ASN CB C 13 37.370 0.030 . 1 . . . . . . . . 5856 1 36 . 1 1 9 9 ASN C C 13 177.690 0.020 . 1 . . . . . . . . 5856 1 37 . 1 1 10 10 VAL H H 1 8.420 0.030 . 1 . . . . . . . . 5856 1 38 . 1 1 10 10 VAL N N 15 119.870 0.050 . 1 . . . . . . . . 5856 1 39 . 1 1 10 10 VAL CA C 13 66.475 0.025 . 1 . . . . . . . . 5856 1 40 . 1 1 10 10 VAL CB C 13 30.480 0.100 . 1 . . . . . . . . 5856 1 41 . 1 1 10 10 VAL C C 13 177.090 0.040 . 1 . . . . . . . . 5856 1 42 . 1 1 11 11 LYS H H 1 7.980 0.030 . 1 . . . . . . . . 5856 1 43 . 1 1 11 11 LYS N N 15 118.710 0.050 . 1 . . . . . . . . 5856 1 44 . 1 1 11 11 LYS CA C 13 59.700 0.020 . 1 . . . . . . . . 5856 1 45 . 1 1 11 11 LYS CB C 13 31.480 0.040 . 1 . . . . . . . . 5856 1 46 . 1 1 11 11 LYS C C 13 180.015 0.015 . 1 . . . . . . . . 5856 1 47 . 1 1 12 12 ALA H H 1 8.140 0.030 . 1 . . . . . . . . 5856 1 48 . 1 1 12 12 ALA N N 15 121.940 0.050 . 1 . . . . . . . . 5856 1 49 . 1 1 12 12 ALA CA C 13 54.300 0.010 . 1 . . . . . . . . 5856 1 50 . 1 1 12 12 ALA CB C 13 17.200 0.030 . 1 . . . . . . . . 5856 1 51 . 1 1 12 12 ALA C C 13 180.675 0.075 . 1 . . . . . . . . 5856 1 52 . 1 1 13 13 ALA H H 1 8.190 0.030 . 1 . . . . . . . . 5856 1 53 . 1 1 13 13 ALA N N 15 120.990 0.050 . 1 . . . . . . . . 5856 1 54 . 1 1 13 13 ALA CA C 13 54.860 0.000 . 1 . . . . . . . . 5856 1 55 . 1 1 13 13 ALA CB C 13 17.230 0.100 . 1 . . . . . . . . 5856 1 56 . 1 1 13 13 ALA C C 13 179.305 0.025 . 1 . . . . . . . . 5856 1 57 . 1 1 14 14 TRP H H 1 9.030 0.030 . 1 . . . . . . . . 5856 1 58 . 1 1 14 14 TRP N N 15 117.860 0.050 . 1 . . . . . . . . 5856 1 59 . 1 1 14 14 TRP CA C 13 59.360 0.050 . 1 . . . . . . . . 5856 1 60 . 1 1 14 14 TRP CB C 13 28.400 0.150 . 1 . . . . . . . . 5856 1 61 . 1 1 14 14 TRP C C 13 179.595 0.065 . 1 . . . . . . . . 5856 1 62 . 1 1 15 15 GLY H H 1 7.970 0.030 . 1 . . . . . . . . 5856 1 63 . 1 1 15 15 GLY N N 15 106.180 0.050 . 1 . . . . . . . . 5856 1 64 . 1 1 15 15 GLY CA C 13 46.200 0.020 . 1 . . . . . . . . 5856 1 65 . 1 1 15 15 GLY C C 13 175.980 0.010 . 1 . . . . . . . . 5856 1 66 . 1 1 16 16 LYS H H 1 7.250 0.030 . 1 . . . . . . . . 5856 1 67 . 1 1 16 16 LYS N N 15 120.260 0.050 . 1 . . . . . . . . 5856 1 68 . 1 1 16 16 LYS CA C 13 56.235 0.015 . 1 . . . . . . . . 5856 1 69 . 1 1 16 16 LYS CB C 13 30.785 0.055 . 1 . . . . . . . . 5856 1 70 . 1 1 16 16 LYS C C 13 178.490 0.030 . 1 . . . . . . . . 5856 1 71 . 1 1 17 17 VAL H H 1 7.440 0.030 . 1 . . . . . . . . 5856 1 72 . 1 1 17 17 VAL N N 15 121.220 0.050 . 1 . . . . . . . . 5856 1 73 . 1 1 17 17 VAL CA C 13 65.680 0.020 . 1 . . . . . . . . 5856 1 74 . 1 1 17 17 VAL CB C 13 29.855 0.005 . 1 . . . . . . . . 5856 1 75 . 1 1 17 17 VAL C C 13 177.470 0.030 . 1 . . . . . . . . 5856 1 76 . 1 1 18 18 GLY H H 1 7.110 0.030 . 1 . . . . . . . . 5856 1 77 . 1 1 18 18 GLY N N 15 103.020 0.050 . 1 . . . . . . . . 5856 1 78 . 1 1 18 18 GLY CA C 13 46.500 0.100 . 1 . . . . . . . . 5856 1 79 . 1 1 18 18 GLY C C 13 176.110 0.100 . 1 . . . . . . . . 5856 1 80 . 1 1 19 19 ALA CA C 13 52.740 0.100 . 1 . . . . . . . . 5856 1 81 . 1 1 19 19 ALA CB C 13 17.190 0.100 . 1 . . . . . . . . 5856 1 82 . 1 1 19 19 ALA C C 13 178.050 0.100 . 1 . . . . . . . . 5856 1 83 . 1 1 20 20 HIS H H 1 7.730 0.030 . 1 . . . . . . . . 5856 1 84 . 1 1 20 20 HIS N N 15 115.450 0.050 . 1 . . . . . . . . 5856 1 85 . 1 1 20 20 HIS CA C 13 55.120 0.010 . 1 . . . . . . . . 5856 1 86 . 1 1 20 20 HIS CB C 13 28.075 0.015 . 1 . . . . . . . . 5856 1 87 . 1 1 20 20 HIS C C 13 173.705 0.015 . 1 . . . . . . . . 5856 1 88 . 1 1 21 21 ALA H H 1 6.940 0.030 . 1 . . . . . . . . 5856 1 89 . 1 1 21 21 ALA N N 15 122.020 0.050 . 1 . . . . . . . . 5856 1 90 . 1 1 21 21 ALA CA C 13 55.860 0.050 . 1 . . . . . . . . 5856 1 91 . 1 1 21 21 ALA CB C 13 17.540 0.100 . 1 . . . . . . . . 5856 1 92 . 1 1 21 21 ALA C C 13 178.135 0.005 . 1 . . . . . . . . 5856 1 93 . 1 1 22 22 GLY H H 1 8.410 0.030 . 1 . . . . . . . . 5856 1 94 . 1 1 22 22 GLY N N 15 104.690 0.050 . 1 . . . . . . . . 5856 1 95 . 1 1 22 22 GLY CA C 13 46.920 0.010 . 1 . . . . . . . . 5856 1 96 . 1 1 22 22 GLY C C 13 176.330 0.030 . 1 . . . . . . . . 5856 1 97 . 1 1 23 23 GLU H H 1 7.690 0.030 . 1 . . . . . . . . 5856 1 98 . 1 1 23 23 GLU N N 15 124.370 0.050 . 1 . . . . . . . . 5856 1 99 . 1 1 23 23 GLU CA C 13 58.425 0.025 . 1 . . . . . . . . 5856 1 100 . 1 1 23 23 GLU CB C 13 27.925 0.005 . 1 . . . . . . . . 5856 1 101 . 1 1 23 23 GLU C C 13 179.650 0.010 . 1 . . . . . . . . 5856 1 102 . 1 1 24 24 TYR H H 1 7.950 0.030 . 1 . . . . . . . . 5856 1 103 . 1 1 24 24 TYR N N 15 121.080 0.050 . 1 . . . . . . . . 5856 1 104 . 1 1 24 24 TYR CA C 13 56.680 0.020 . 1 . . . . . . . . 5856 1 105 . 1 1 24 24 TYR CB C 13 33.950 0.000 . 1 . . . . . . . . 5856 1 106 . 1 1 24 24 TYR C C 13 178.410 0.030 . 1 . . . . . . . . 5856 1 107 . 1 1 25 25 GLY H H 1 8.760 0.030 . 1 . . . . . . . . 5856 1 108 . 1 1 25 25 GLY N N 15 107.830 0.050 . 1 . . . . . . . . 5856 1 109 . 1 1 25 25 GLY CA C 13 46.120 0.030 . 1 . . . . . . . . 5856 1 110 . 1 1 25 25 GLY C C 13 174.330 0.000 . 1 . . . . . . . . 5856 1 111 . 1 1 26 26 ALA H H 1 7.700 0.030 . 1 . . . . . . . . 5856 1 112 . 1 1 26 26 ALA N N 15 121.460 0.050 . 1 . . . . . . . . 5856 1 113 . 1 1 26 26 ALA CA C 13 54.245 0.005 . 1 . . . . . . . . 5856 1 114 . 1 1 26 26 ALA CB C 13 18.160 0.030 . 1 . . . . . . . . 5856 1 115 . 1 1 26 26 ALA C C 13 178.340 0.040 . 1 . . . . . . . . 5856 1 116 . 1 1 27 27 GLU H H 1 7.820 0.030 . 1 . . . . . . . . 5856 1 117 . 1 1 27 27 GLU N N 15 119.690 0.050 . 1 . . . . . . . . 5856 1 118 . 1 1 27 27 GLU CA C 13 58.480 0.010 . 1 . . . . . . . . 5856 1 119 . 1 1 27 27 GLU CB C 13 28.410 0.040 . 1 . . . . . . . . 5856 1 120 . 1 1 27 27 GLU C C 13 177.915 0.005 . 1 . . . . . . . . 5856 1 121 . 1 1 28 28 ALA H H 1 8.290 0.030 . 1 . . . . . . . . 5856 1 122 . 1 1 28 28 ALA N N 15 121.890 0.050 . 1 . . . . . . . . 5856 1 123 . 1 1 28 28 ALA CA C 13 55.210 0.010 . 1 . . . . . . . . 5856 1 124 . 1 1 28 28 ALA CB C 13 16.630 0.100 . 1 . . . . . . . . 5856 1 125 . 1 1 28 28 ALA C C 13 179.010 0.070 . 1 . . . . . . . . 5856 1 126 . 1 1 29 29 LEU H H 1 7.000 0.030 . 1 . . . . . . . . 5856 1 127 . 1 1 29 29 LEU N N 15 115.810 0.050 . 1 . . . . . . . . 5856 1 128 . 1 1 29 29 LEU CA C 13 56.835 0.045 . 1 . . . . . . . . 5856 1 129 . 1 1 29 29 LEU CB C 13 39.335 0.065 . 1 . . . . . . . . 5856 1 130 . 1 1 29 29 LEU C C 13 176.175 0.045 . 1 . . . . . . . . 5856 1 131 . 1 1 30 30 GLU H H 1 7.760 0.030 . 1 . . . . . . . . 5856 1 132 . 1 1 30 30 GLU N N 15 118.270 0.050 . 1 . . . . . . . . 5856 1 133 . 1 1 30 30 GLU CA C 13 59.690 0.010 . 1 . . . . . . . . 5856 1 134 . 1 1 30 30 GLU CB C 13 28.480 0.100 . 1 . . . . . . . . 5856 1 135 . 1 1 30 30 GLU C C 13 179.470 0.000 . 1 . . . . . . . . 5856 1 136 . 1 1 31 31 ARG H H 1 8.630 0.030 . 1 . . . . . . . . 5856 1 137 . 1 1 31 31 ARG N N 15 116.430 0.050 . 1 . . . . . . . . 5856 1 138 . 1 1 31 31 ARG CA C 13 59.895 0.055 . 1 . . . . . . . . 5856 1 139 . 1 1 31 31 ARG CB C 13 28.370 0.100 . 1 . . . . . . . . 5856 1 140 . 1 1 31 31 ARG C C 13 178.220 0.000 . 1 . . . . . . . . 5856 1 141 . 1 1 32 32 MET H H 1 7.900 0.030 . 1 . . . . . . . . 5856 1 142 . 1 1 32 32 MET N N 15 123.270 0.050 . 1 . . . . . . . . 5856 1 143 . 1 1 32 32 MET CA C 13 59.805 0.055 . 1 . . . . . . . . 5856 1 144 . 1 1 32 32 MET CB C 13 31.440 0.100 . 1 . . . . . . . . 5856 1 145 . 1 1 32 32 MET C C 13 177.145 0.065 . 1 . . . . . . . . 5856 1 146 . 1 1 33 33 PHE H H 1 8.360 0.030 . 1 . . . . . . . . 5856 1 147 . 1 1 33 33 PHE N N 15 118.510 0.050 . 1 . . . . . . . . 5856 1 148 . 1 1 33 33 PHE CA C 13 57.970 0.000 . 1 . . . . . . . . 5856 1 149 . 1 1 33 33 PHE CB C 13 37.180 0.100 . 1 . . . . . . . . 5856 1 150 . 1 1 33 33 PHE C C 13 178.120 0.020 . 1 . . . . . . . . 5856 1 151 . 1 1 34 34 LEU H H 1 7.610 0.030 . 1 . . . . . . . . 5856 1 152 . 1 1 34 34 LEU N N 15 114.110 0.050 . 1 . . . . . . . . 5856 1 153 . 1 1 34 34 LEU CA C 13 56.050 0.030 . 1 . . . . . . . . 5856 1 154 . 1 1 34 34 LEU CB C 13 41.950 0.100 . 1 . . . . . . . . 5856 1 155 . 1 1 34 34 LEU C C 13 179.020 0.100 . 1 . . . . . . . . 5856 1 156 . 1 1 35 35 SER H H 1 7.900 0.030 . 1 . . . . . . . . 5856 1 157 . 1 1 35 35 SER N N 15 113.110 0.050 . 1 . . . . . . . . 5856 1 158 . 1 1 35 35 SER CA C 13 62.350 0.060 . 1 . . . . . . . . 5856 1 159 . 1 1 35 35 SER CB C 13 63.490 0.100 . 1 . . . . . . . . 5856 1 160 . 1 1 35 35 SER C C 13 173.360 0.100 . 1 . . . . . . . . 5856 1 161 . 1 1 36 36 PHE H H 1 8.310 0.030 . 1 . . . . . . . . 5856 1 162 . 1 1 36 36 PHE N N 15 117.910 0.050 . 1 . . . . . . . . 5856 1 163 . 1 1 36 36 PHE CA C 13 53.930 0.100 . 1 . . . . . . . . 5856 1 164 . 1 1 36 36 PHE CB C 13 38.400 0.100 . 1 . . . . . . . . 5856 1 165 . 1 1 37 37 PRO CA C 13 64.940 0.100 . 1 . . . . . . . . 5856 1 166 . 1 1 37 37 PRO C C 13 179.660 0.100 . 1 . . . . . . . . 5856 1 167 . 1 1 38 38 THR H H 1 8.300 0.030 . 1 . . . . . . . . 5856 1 168 . 1 1 38 38 THR N N 15 113.010 0.050 . 1 . . . . . . . . 5856 1 169 . 1 1 38 38 THR CA C 13 65.205 0.025 . 1 . . . . . . . . 5856 1 170 . 1 1 38 38 THR C C 13 178.020 0.100 . 1 . . . . . . . . 5856 1 171 . 1 1 39 39 THR H H 1 8.810 0.030 . 1 . . . . . . . . 5856 1 172 . 1 1 39 39 THR N N 15 115.110 0.050 . 1 . . . . . . . . 5856 1 173 . 1 1 39 39 THR CA C 13 66.040 0.000 . 1 . . . . . . . . 5856 1 174 . 1 1 39 39 THR CB C 13 70.190 0.100 . 1 . . . . . . . . 5856 1 175 . 1 1 39 39 THR C C 13 177.050 0.100 . 1 . . . . . . . . 5856 1 176 . 1 1 40 40 LYS H H 1 7.690 0.030 . 1 . . . . . . . . 5856 1 177 . 1 1 40 40 LYS N N 15 118.460 0.050 . 1 . . . . . . . . 5856 1 178 . 1 1 40 40 LYS CA C 13 59.085 0.065 . 1 . . . . . . . . 5856 1 179 . 1 1 40 40 LYS CB C 13 31.000 0.100 . 1 . . . . . . . . 5856 1 180 . 1 1 40 40 LYS C C 13 179.875 0.015 . 1 . . . . . . . . 5856 1 181 . 1 1 41 41 THR H H 1 7.730 0.030 . 1 . . . . . . . . 5856 1 182 . 1 1 41 41 THR N N 15 111.200 0.050 . 1 . . . . . . . . 5856 1 183 . 1 1 41 41 THR CA C 13 63.890 0.010 . 1 . . . . . . . . 5856 1 184 . 1 1 41 41 THR C C 13 175.220 0.000 . 1 . . . . . . . . 5856 1 185 . 1 1 42 42 TYR H H 1 7.420 0.030 . 1 . . . . . . . . 5856 1 186 . 1 1 42 42 TYR N N 15 117.120 0.050 . 1 . . . . . . . . 5856 1 187 . 1 1 42 42 TYR CA C 13 59.940 0.010 . 1 . . . . . . . . 5856 1 188 . 1 1 42 42 TYR CB C 13 38.610 0.100 . 1 . . . . . . . . 5856 1 189 . 1 1 42 42 TYR C C 13 173.855 0.025 . 1 . . . . . . . . 5856 1 190 . 1 1 43 43 PHE H H 1 7.760 0.030 . 1 . . . . . . . . 5856 1 191 . 1 1 43 43 PHE N N 15 117.090 0.050 . 1 . . . . . . . . 5856 1 192 . 1 1 43 43 PHE CA C 13 54.680 0.100 . 1 . . . . . . . . 5856 1 193 . 1 1 43 43 PHE CB C 13 39.060 0.100 . 1 . . . . . . . . 5856 1 194 . 1 1 43 43 PHE C C 13 173.960 0.100 . 1 . . . . . . . . 5856 1 195 . 1 1 44 44 PRO CA C 13 64.830 0.100 . 1 . . . . . . . . 5856 1 196 . 1 1 44 44 PRO CB C 13 30.360 0.100 . 1 . . . . . . . . 5856 1 197 . 1 1 44 44 PRO C C 13 177.270 0.100 . 1 . . . . . . . . 5856 1 198 . 1 1 45 45 HIS H H 1 9.470 0.030 . 1 . . . . . . . . 5856 1 199 . 1 1 45 45 HIS N N 15 116.840 0.050 . 1 . . . . . . . . 5856 1 200 . 1 1 45 45 HIS CA C 13 54.915 0.015 . 1 . . . . . . . . 5856 1 201 . 1 1 45 45 HIS CB C 13 29.065 0.055 . 1 . . . . . . . . 5856 1 202 . 1 1 45 45 HIS C C 13 175.480 0.040 . 1 . . . . . . . . 5856 1 203 . 1 1 46 46 PHE H H 1 7.440 0.030 . 1 . . . . . . . . 5856 1 204 . 1 1 46 46 PHE N N 15 122.760 0.050 . 1 . . . . . . . . 5856 1 205 . 1 1 46 46 PHE CA C 13 55.280 0.010 . 1 . . . . . . . . 5856 1 206 . 1 1 46 46 PHE CB C 13 39.340 0.000 . 1 . . . . . . . . 5856 1 207 . 1 1 46 46 PHE C C 13 175.700 0.040 . 1 . . . . . . . . 5856 1 208 . 1 1 47 47 ASP H H 1 7.830 0.030 . 1 . . . . . . . . 5856 1 209 . 1 1 47 47 ASP N N 15 119.400 0.050 . 1 . . . . . . . . 5856 1 210 . 1 1 47 47 ASP CA C 13 52.985 0.035 . 1 . . . . . . . . 5856 1 211 . 1 1 47 47 ASP CB C 13 39.255 0.015 . 1 . . . . . . . . 5856 1 212 . 1 1 47 47 ASP C C 13 176.300 0.050 . 1 . . . . . . . . 5856 1 213 . 1 1 48 48 LEU H H 1 8.470 0.030 . 1 . . . . . . . . 5856 1 214 . 1 1 48 48 LEU N N 15 128.220 0.050 . 1 . . . . . . . . 5856 1 215 . 1 1 48 48 LEU CA C 13 52.950 0.020 . 1 . . . . . . . . 5856 1 216 . 1 1 48 48 LEU CB C 13 39.460 0.170 . 1 . . . . . . . . 5856 1 217 . 1 1 48 48 LEU C C 13 177.045 0.025 . 1 . . . . . . . . 5856 1 218 . 1 1 49 49 SER H H 1 8.110 0.030 . 1 . . . . . . . . 5856 1 219 . 1 1 49 49 SER N N 15 117.430 0.050 . 1 . . . . . . . . 5856 1 220 . 1 1 49 49 SER CA C 13 58.630 0.100 . 1 . . . . . . . . 5856 1 221 . 1 1 49 49 SER CB C 13 63.360 0.100 . 1 . . . . . . . . 5856 1 222 . 1 1 49 49 SER C C 13 174.325 0.055 . 1 . . . . . . . . 5856 1 223 . 1 1 50 50 HIS H H 1 8.570 0.030 . 1 . . . . . . . . 5856 1 224 . 1 1 50 50 HIS N N 15 121.580 0.050 . 1 . . . . . . . . 5856 1 225 . 1 1 50 50 HIS CA C 13 57.275 0.055 . 1 . . . . . . . . 5856 1 226 . 1 1 50 50 HIS CB C 13 27.760 0.100 . 1 . . . . . . . . 5856 1 227 . 1 1 50 50 HIS C C 13 176.990 0.100 . 1 . . . . . . . . 5856 1 228 . 1 1 51 51 GLY H H 1 8.920 0.030 . 1 . . . . . . . . 5856 1 229 . 1 1 51 51 GLY N N 15 116.290 0.050 . 1 . . . . . . . . 5856 1 230 . 1 1 51 51 GLY CA C 13 44.630 0.050 . 1 . . . . . . . . 5856 1 231 . 1 1 51 51 GLY C C 13 174.130 0.030 . 1 . . . . . . . . 5856 1 232 . 1 1 52 52 SER H H 1 7.370 0.030 . 1 . . . . . . . . 5856 1 233 . 1 1 52 52 SER N N 15 114.730 0.050 . 1 . . . . . . . . 5856 1 234 . 1 1 52 52 SER CA C 13 56.520 0.100 . 1 . . . . . . . . 5856 1 235 . 1 1 52 52 SER CB C 13 64.010 0.100 . 1 . . . . . . . . 5856 1 236 . 1 1 52 52 SER C C 13 176.430 0.010 . 1 . . . . . . . . 5856 1 237 . 1 1 53 53 ALA H H 1 9.010 0.030 . 1 . . . . . . . . 5856 1 238 . 1 1 53 53 ALA N N 15 131.580 0.050 . 1 . . . . . . . . 5856 1 239 . 1 1 53 53 ALA CA C 13 54.180 0.100 . 1 . . . . . . . . 5856 1 240 . 1 1 53 53 ALA C C 13 180.800 0.100 . 1 . . . . . . . . 5856 1 241 . 1 1 54 54 GLN H H 1 8.210 0.030 . 1 . . . . . . . . 5856 1 242 . 1 1 54 54 GLN N N 15 120.070 0.050 . 1 . . . . . . . . 5856 1 243 . 1 1 54 54 GLN CA C 13 58.220 0.100 . 1 . . . . . . . . 5856 1 244 . 1 1 54 54 GLN CB C 13 27.740 0.110 . 1 . . . . . . . . 5856 1 245 . 1 1 54 54 GLN C C 13 179.300 0.000 . 1 . . . . . . . . 5856 1 246 . 1 1 55 55 VAL H H 1 7.450 0.030 . 1 . . . . . . . . 5856 1 247 . 1 1 55 55 VAL N N 15 121.980 0.050 . 1 . . . . . . . . 5856 1 248 . 1 1 55 55 VAL CA C 13 66.585 0.075 . 1 . . . . . . . . 5856 1 249 . 1 1 55 55 VAL CB C 13 30.705 0.065 . 1 . . . . . . . . 5856 1 250 . 1 1 55 55 VAL C C 13 177.480 0.020 . 1 . . . . . . . . 5856 1 251 . 1 1 56 56 LYS H H 1 7.660 0.030 . 1 . . . . . . . . 5856 1 252 . 1 1 56 56 LYS N N 15 120.220 0.050 . 1 . . . . . . . . 5856 1 253 . 1 1 56 56 LYS CA C 13 59.270 0.110 . 1 . . . . . . . . 5856 1 254 . 1 1 56 56 LYS CB C 13 30.905 0.045 . 1 . . . . . . . . 5856 1 255 . 1 1 56 56 LYS C C 13 180.230 0.040 . 1 . . . . . . . . 5856 1 256 . 1 1 57 57 GLY H H 1 8.170 0.030 . 1 . . . . . . . . 5856 1 257 . 1 1 57 57 GLY N N 15 106.200 0.050 . 1 . . . . . . . . 5856 1 258 . 1 1 57 57 GLY CA C 13 46.220 0.020 . 1 . . . . . . . . 5856 1 259 . 1 1 57 57 GLY C C 13 176.625 0.015 . 1 . . . . . . . . 5856 1 260 . 1 1 58 58 HIS H H 1 8.090 0.030 . 1 . . . . . . . . 5856 1 261 . 1 1 58 58 HIS N N 15 124.610 0.050 . 1 . . . . . . . . 5856 1 262 . 1 1 58 58 HIS CA C 13 59.465 0.035 . 1 . . . . . . . . 5856 1 263 . 1 1 58 58 HIS CB C 13 30.365 0.005 . 1 . . . . . . . . 5856 1 264 . 1 1 58 58 HIS C C 13 177.190 0.020 . 1 . . . . . . . . 5856 1 265 . 1 1 59 59 GLY H H 1 8.480 0.030 . 1 . . . . . . . . 5856 1 266 . 1 1 59 59 GLY N N 15 105.800 0.050 . 1 . . . . . . . . 5856 1 267 . 1 1 59 59 GLY CA C 13 45.815 0.025 . 1 . . . . . . . . 5856 1 268 . 1 1 59 59 GLY C C 13 174.925 0.015 . 1 . . . . . . . . 5856 1 269 . 1 1 60 60 LYS H H 1 7.000 0.030 . 1 . . . . . . . . 5856 1 270 . 1 1 60 60 LYS N N 15 120.280 0.050 . 1 . . . . . . . . 5856 1 271 . 1 1 60 60 LYS CA C 13 58.880 0.050 . 1 . . . . . . . . 5856 1 272 . 1 1 60 60 LYS CB C 13 31.005 0.105 . 1 . . . . . . . . 5856 1 273 . 1 1 60 60 LYS C C 13 177.320 0.000 . 1 . . . . . . . . 5856 1 274 . 1 1 61 61 LYS H H 1 6.890 0.030 . 1 . . . . . . . . 5856 1 275 . 1 1 61 61 LYS N N 15 118.490 0.050 . 1 . . . . . . . . 5856 1 276 . 1 1 61 61 LYS CA C 13 59.575 0.055 . 1 . . . . . . . . 5856 1 277 . 1 1 61 61 LYS CB C 13 30.930 0.100 . 1 . . . . . . . . 5856 1 278 . 1 1 61 61 LYS C C 13 180.385 0.055 . 1 . . . . . . . . 5856 1 279 . 1 1 62 62 VAL H H 1 7.660 0.030 . 1 . . . . . . . . 5856 1 280 . 1 1 62 62 VAL N N 15 120.500 0.050 . 1 . . . . . . . . 5856 1 281 . 1 1 62 62 VAL CA C 13 66.280 0.020 . 1 . . . . . . . . 5856 1 282 . 1 1 62 62 VAL CB C 13 30.310 0.100 . 1 . . . . . . . . 5856 1 283 . 1 1 62 62 VAL C C 13 177.460 0.040 . 1 . . . . . . . . 5856 1 284 . 1 1 63 63 ALA H H 1 8.080 0.030 . 1 . . . . . . . . 5856 1 285 . 1 1 63 63 ALA N N 15 120.930 0.050 . 1 . . . . . . . . 5856 1 286 . 1 1 63 63 ALA CA C 13 55.240 0.000 . 1 . . . . . . . . 5856 1 287 . 1 1 63 63 ALA CB C 13 18.325 0.055 . 1 . . . . . . . . 5856 1 288 . 1 1 63 63 ALA C C 13 179.875 0.045 . 1 . . . . . . . . 5856 1 289 . 1 1 64 64 ASP H H 1 8.820 0.030 . 1 . . . . . . . . 5856 1 290 . 1 1 64 64 ASP N N 15 119.910 0.050 . 1 . . . . . . . . 5856 1 291 . 1 1 64 64 ASP CA C 13 57.065 0.025 . 1 . . . . . . . . 5856 1 292 . 1 1 64 64 ASP CB C 13 39.085 0.025 . 1 . . . . . . . . 5856 1 293 . 1 1 64 64 ASP C C 13 179.730 0.070 . 1 . . . . . . . . 5856 1 294 . 1 1 65 65 ALA H H 1 8.250 0.030 . 1 . . . . . . . . 5856 1 295 . 1 1 65 65 ALA N N 15 124.610 0.050 . 1 . . . . . . . . 5856 1 296 . 1 1 65 65 ALA CA C 13 54.850 0.010 . 1 . . . . . . . . 5856 1 297 . 1 1 65 65 ALA CB C 13 19.030 0.080 . 1 . . . . . . . . 5856 1 298 . 1 1 65 65 ALA C C 13 180.520 0.050 . 1 . . . . . . . . 5856 1 299 . 1 1 66 66 LEU H H 1 8.400 0.030 . 1 . . . . . . . . 5856 1 300 . 1 1 66 66 LEU N N 15 119.480 0.050 . 1 . . . . . . . . 5856 1 301 . 1 1 66 66 LEU CA C 13 57.565 0.065 . 1 . . . . . . . . 5856 1 302 . 1 1 66 66 LEU CB C 13 40.290 0.040 . 1 . . . . . . . . 5856 1 303 . 1 1 66 66 LEU C C 13 178.565 0.035 . 1 . . . . . . . . 5856 1 304 . 1 1 67 67 THR H H 1 9.060 0.030 . 1 . . . . . . . . 5856 1 305 . 1 1 67 67 THR N N 15 118.340 0.050 . 1 . . . . . . . . 5856 1 306 . 1 1 67 67 THR CA C 13 66.580 0.030 . 1 . . . . . . . . 5856 1 307 . 1 1 67 67 THR CB C 13 68.025 0.015 . 1 . . . . . . . . 5856 1 308 . 1 1 67 67 THR C C 13 176.940 0.100 . 1 . . . . . . . . 5856 1 309 . 1 1 68 68 ASN H H 1 8.060 0.030 . 1 . . . . . . . . 5856 1 310 . 1 1 68 68 ASN N N 15 121.440 0.050 . 1 . . . . . . . . 5856 1 311 . 1 1 68 68 ASN CA C 13 56.005 0.015 . 1 . . . . . . . . 5856 1 312 . 1 1 68 68 ASN CB C 13 38.075 0.035 . 1 . . . . . . . . 5856 1 313 . 1 1 68 68 ASN C C 13 177.240 0.030 . 1 . . . . . . . . 5856 1 314 . 1 1 69 69 ALA H H 1 8.470 0.030 . 1 . . . . . . . . 5856 1 315 . 1 1 69 69 ALA N N 15 123.330 0.050 . 1 . . . . . . . . 5856 1 316 . 1 1 69 69 ALA CA C 13 55.405 0.065 . 1 . . . . . . . . 5856 1 317 . 1 1 69 69 ALA CB C 13 17.230 0.020 . 1 . . . . . . . . 5856 1 318 . 1 1 69 69 ALA C C 13 178.115 0.015 . 1 . . . . . . . . 5856 1 319 . 1 1 70 70 VAL H H 1 8.160 0.030 . 1 . . . . . . . . 5856 1 320 . 1 1 70 70 VAL N N 15 116.870 0.050 . 1 . . . . . . . . 5856 1 321 . 1 1 70 70 VAL CA C 13 66.295 0.035 . 1 . . . . . . . . 5856 1 322 . 1 1 70 70 VAL CB C 13 30.950 0.100 . 1 . . . . . . . . 5856 1 323 . 1 1 70 70 VAL C C 13 178.550 0.030 . 1 . . . . . . . . 5856 1 324 . 1 1 71 71 ALA H H 1 7.630 0.030 . 1 . . . . . . . . 5856 1 325 . 1 1 71 71 ALA N N 15 120.300 0.050 . 1 . . . . . . . . 5856 1 326 . 1 1 71 71 ALA CA C 13 53.555 0.055 . 1 . . . . . . . . 5856 1 327 . 1 1 71 71 ALA CB C 13 17.200 0.070 . 1 . . . . . . . . 5856 1 328 . 1 1 71 71 ALA C C 13 178.520 0.030 . 1 . . . . . . . . 5856 1 329 . 1 1 72 72 HIS H H 1 7.620 0.030 . 1 . . . . . . . . 5856 1 330 . 1 1 72 72 HIS N N 15 116.240 0.050 . 1 . . . . . . . . 5856 1 331 . 1 1 72 72 HIS CA C 13 54.500 0.000 . 1 . . . . . . . . 5856 1 332 . 1 1 72 72 HIS CB C 13 27.740 0.050 . 1 . . . . . . . . 5856 1 333 . 1 1 72 72 HIS C C 13 176.390 0.000 . 1 . . . . . . . . 5856 1 334 . 1 1 73 73 VAL H H 1 6.600 0.030 . 1 . . . . . . . . 5856 1 335 . 1 1 73 73 VAL N N 15 120.120 0.050 . 1 . . . . . . . . 5856 1 336 . 1 1 73 73 VAL CA C 13 64.675 0.015 . 1 . . . . . . . . 5856 1 337 . 1 1 73 73 VAL CB C 13 30.970 0.070 . 1 . . . . . . . . 5856 1 338 . 1 1 73 73 VAL C C 13 176.290 0.040 . 1 . . . . . . . . 5856 1 339 . 1 1 74 74 ASP H H 1 8.190 0.030 . 1 . . . . . . . . 5856 1 340 . 1 1 74 74 ASP N N 15 119.670 0.050 . 1 . . . . . . . . 5856 1 341 . 1 1 74 74 ASP CA C 13 54.770 0.000 . 1 . . . . . . . . 5856 1 342 . 1 1 74 74 ASP CB C 13 40.395 0.035 . 1 . . . . . . . . 5856 1 343 . 1 1 74 74 ASP C C 13 175.655 0.015 . 1 . . . . . . . . 5856 1 344 . 1 1 75 75 ASP H H 1 8.270 0.030 . 1 . . . . . . . . 5856 1 345 . 1 1 75 75 ASP N N 15 122.600 0.050 . 1 . . . . . . . . 5856 1 346 . 1 1 75 75 ASP CA C 13 52.540 0.020 . 1 . . . . . . . . 5856 1 347 . 1 1 75 75 ASP CB C 13 40.760 0.010 . 1 . . . . . . . . 5856 1 348 . 1 1 75 75 ASP C C 13 175.870 0.040 . 1 . . . . . . . . 5856 1 349 . 1 1 76 76 MET H H 1 8.600 0.030 . 1 . . . . . . . . 5856 1 350 . 1 1 76 76 MET N N 15 122.000 0.050 . 1 . . . . . . . . 5856 1 351 . 1 1 76 76 MET CA C 13 61.310 0.100 . 1 . . . . . . . . 5856 1 352 . 1 1 76 76 MET CB C 13 31.780 0.100 . 1 . . . . . . . . 5856 1 353 . 1 1 76 76 MET C C 13 174.960 0.100 . 1 . . . . . . . . 5856 1 354 . 1 1 77 77 PRO CA C 13 65.550 0.100 . 1 . . . . . . . . 5856 1 355 . 1 1 77 77 PRO C C 13 178.830 0.100 . 1 . . . . . . . . 5856 1 356 . 1 1 78 78 ASN H H 1 7.360 0.030 . 1 . . . . . . . . 5856 1 357 . 1 1 78 78 ASN N N 15 113.160 0.050 . 1 . . . . . . . . 5856 1 358 . 1 1 78 78 ASN CA C 13 55.160 0.000 . 1 . . . . . . . . 5856 1 359 . 1 1 78 78 ASN CB C 13 38.075 0.055 . 1 . . . . . . . . 5856 1 360 . 1 1 78 78 ASN C C 13 177.500 0.080 . 1 . . . . . . . . 5856 1 361 . 1 1 79 79 ALA H H 1 7.840 0.030 . 1 . . . . . . . . 5856 1 362 . 1 1 79 79 ALA N N 15 122.150 0.050 . 1 . . . . . . . . 5856 1 363 . 1 1 79 79 ALA CA C 13 54.245 0.005 . 1 . . . . . . . . 5856 1 364 . 1 1 79 79 ALA CB C 13 17.530 0.100 . 1 . . . . . . . . 5856 1 365 . 1 1 79 79 ALA C C 13 179.255 0.045 . 1 . . . . . . . . 5856 1 366 . 1 1 80 80 LEU H H 1 8.010 0.030 . 1 . . . . . . . . 5856 1 367 . 1 1 80 80 LEU N N 15 113.820 0.050 . 1 . . . . . . . . 5856 1 368 . 1 1 80 80 LEU CA C 13 53.310 0.020 . 1 . . . . . . . . 5856 1 369 . 1 1 80 80 LEU CB C 13 40.165 0.035 . 1 . . . . . . . . 5856 1 370 . 1 1 80 80 LEU C C 13 177.255 0.015 . 1 . . . . . . . . 5856 1 371 . 1 1 81 81 SER H H 1 7.030 0.030 . 1 . . . . . . . . 5856 1 372 . 1 1 81 81 SER N N 15 116.780 0.050 . 1 . . . . . . . . 5856 1 373 . 1 1 81 81 SER CA C 13 61.770 0.100 . 1 . . . . . . . . 5856 1 374 . 1 1 81 81 SER C C 13 175.860 0.100 . 1 . . . . . . . . 5856 1 375 . 1 1 82 82 ALA H H 1 8.550 0.030 . 1 . . . . . . . . 5856 1 376 . 1 1 82 82 ALA N N 15 122.360 0.050 . 1 . . . . . . . . 5856 1 377 . 1 1 82 82 ALA CA C 13 54.490 0.100 . 1 . . . . . . . . 5856 1 378 . 1 1 82 82 ALA C C 13 180.910 0.100 . 1 . . . . . . . . 5856 1 379 . 1 1 83 83 LEU H H 1 7.450 0.030 . 1 . . . . . . . . 5856 1 380 . 1 1 83 83 LEU N N 15 118.040 0.050 . 1 . . . . . . . . 5856 1 381 . 1 1 83 83 LEU CA C 13 55.540 0.020 . 1 . . . . . . . . 5856 1 382 . 1 1 83 83 LEU CB C 13 40.590 0.100 . 1 . . . . . . . . 5856 1 383 . 1 1 83 83 LEU C C 13 180.440 0.100 . 1 . . . . . . . . 5856 1 384 . 1 1 84 84 SER H H 1 8.170 0.030 . 1 . . . . . . . . 5856 1 385 . 1 1 84 84 SER N N 15 121.460 0.050 . 1 . . . . . . . . 5856 1 386 . 1 1 84 84 SER CA C 13 60.190 0.010 . 1 . . . . . . . . 5856 1 387 . 1 1 84 84 SER C C 13 175.800 0.100 . 1 . . . . . . . . 5856 1 388 . 1 1 85 85 ASP H H 1 7.510 0.030 . 1 . . . . . . . . 5856 1 389 . 1 1 85 85 ASP N N 15 121.710 0.050 . 1 . . . . . . . . 5856 1 390 . 1 1 85 85 ASP CA C 13 57.055 0.215 . 1 . . . . . . . . 5856 1 391 . 1 1 85 85 ASP C C 13 174.660 0.100 . 1 . . . . . . . . 5856 1 392 . 1 1 86 86 LEU H H 1 7.310 0.030 . 1 . . . . . . . . 5856 1 393 . 1 1 86 86 LEU N N 15 125.290 0.050 . 1 . . . . . . . . 5856 1 394 . 1 1 86 86 LEU CA C 13 57.015 0.045 . 1 . . . . . . . . 5856 1 395 . 1 1 86 86 LEU C C 13 177.140 0.100 . 1 . . . . . . . . 5856 1 396 . 1 1 87 87 HIS H H 1 7.120 0.030 . 1 . . . . . . . . 5856 1 397 . 1 1 87 87 HIS N N 15 112.120 0.050 . 1 . . . . . . . . 5856 1 398 . 1 1 87 87 HIS CA C 13 60.470 0.100 . 1 . . . . . . . . 5856 1 399 . 1 1 87 87 HIS C C 13 174.390 0.100 . 1 . . . . . . . . 5856 1 400 . 1 1 88 88 ALA CA C 13 52.770 0.100 . 1 . . . . . . . . 5856 1 401 . 1 1 88 88 ALA C C 13 177.970 0.100 . 1 . . . . . . . . 5856 1 402 . 1 1 89 89 HIS H H 1 7.140 0.030 . 1 . . . . . . . . 5856 1 403 . 1 1 89 89 HIS N N 15 115.100 0.050 . 1 . . . . . . . . 5856 1 404 . 1 1 89 89 HIS CA C 13 57.540 0.020 . 1 . . . . . . . . 5856 1 405 . 1 1 89 89 HIS CB C 13 30.250 0.100 . 1 . . . . . . . . 5856 1 406 . 1 1 89 89 HIS C C 13 176.050 0.020 . 1 . . . . . . . . 5856 1 407 . 1 1 90 90 LYS H H 1 7.320 0.030 . 1 . . . . . . . . 5856 1 408 . 1 1 90 90 LYS N N 15 117.260 0.050 . 1 . . . . . . . . 5856 1 409 . 1 1 90 90 LYS CA C 13 58.150 0.100 . 1 . . . . . . . . 5856 1 410 . 1 1 90 90 LYS CB C 13 31.320 0.100 . 1 . . . . . . . . 5856 1 411 . 1 1 90 90 LYS C C 13 178.380 0.100 . 1 . . . . . . . . 5856 1 412 . 1 1 91 91 LEU CA C 13 55.200 0.100 . 1 . . . . . . . . 5856 1 413 . 1 1 91 91 LEU C C 13 176.910 0.100 . 1 . . . . . . . . 5856 1 414 . 1 1 92 92 ARG H H 1 6.420 0.030 . 1 . . . . . . . . 5856 1 415 . 1 1 92 92 ARG N N 15 112.030 0.050 . 1 . . . . . . . . 5856 1 416 . 1 1 92 92 ARG CA C 13 56.550 0.010 . 1 . . . . . . . . 5856 1 417 . 1 1 92 92 ARG CB C 13 27.970 0.100 . 1 . . . . . . . . 5856 1 418 . 1 1 92 92 ARG C C 13 174.340 0.010 . 1 . . . . . . . . 5856 1 419 . 1 1 93 93 VAL H H 1 7.500 0.030 . 1 . . . . . . . . 5856 1 420 . 1 1 93 93 VAL N N 15 116.070 0.050 . 1 . . . . . . . . 5856 1 421 . 1 1 93 93 VAL CA C 13 62.870 0.010 . 1 . . . . . . . . 5856 1 422 . 1 1 93 93 VAL CB C 13 27.350 0.100 . 1 . . . . . . . . 5856 1 423 . 1 1 93 93 VAL C C 13 176.940 0.000 . 1 . . . . . . . . 5856 1 424 . 1 1 94 94 ASP H H 1 7.670 0.030 . 1 . . . . . . . . 5856 1 425 . 1 1 94 94 ASP N N 15 129.790 0.050 . 1 . . . . . . . . 5856 1 426 . 1 1 94 94 ASP CA C 13 52.240 0.100 . 1 . . . . . . . . 5856 1 427 . 1 1 95 95 PRO CA C 13 64.370 0.100 . 1 . . . . . . . . 5856 1 428 . 1 1 95 95 PRO C C 13 179.860 0.100 . 1 . . . . . . . . 5856 1 429 . 1 1 96 96 VAL H H 1 8.820 0.030 . 1 . . . . . . . . 5856 1 430 . 1 1 96 96 VAL N N 15 119.920 0.050 . 1 . . . . . . . . 5856 1 431 . 1 1 96 96 VAL CA C 13 65.355 0.015 . 1 . . . . . . . . 5856 1 432 . 1 1 96 96 VAL C C 13 178.660 0.050 . 1 . . . . . . . . 5856 1 433 . 1 1 97 97 ASN H H 1 8.260 0.030 . 1 . . . . . . . . 5856 1 434 . 1 1 97 97 ASN N N 15 116.530 0.050 . 1 . . . . . . . . 5856 1 435 . 1 1 97 97 ASN CA C 13 56.170 0.080 . 1 . . . . . . . . 5856 1 436 . 1 1 97 97 ASN CB C 13 39.700 0.100 . 1 . . . . . . . . 5856 1 437 . 1 1 97 97 ASN C C 13 177.680 0.040 . 1 . . . . . . . . 5856 1 438 . 1 1 98 98 PHE H H 1 7.800 0.030 . 1 . . . . . . . . 5856 1 439 . 1 1 98 98 PHE N N 15 118.590 0.050 . 1 . . . . . . . . 5856 1 440 . 1 1 98 98 PHE CA C 13 62.345 0.035 . 1 . . . . . . . . 5856 1 441 . 1 1 98 98 PHE CB C 13 36.590 0.100 . 1 . . . . . . . . 5856 1 442 . 1 1 98 98 PHE C C 13 179.520 0.050 . 1 . . . . . . . . 5856 1 443 . 1 1 99 99 LYS H H 1 7.390 0.030 . 1 . . . . . . . . 5856 1 444 . 1 1 99 99 LYS N N 15 121.140 0.050 . 1 . . . . . . . . 5856 1 445 . 1 1 99 99 LYS CA C 13 58.840 0.070 . 1 . . . . . . . . 5856 1 446 . 1 1 99 99 LYS CB C 13 30.770 0.100 . 1 . . . . . . . . 5856 1 447 . 1 1 99 99 LYS C C 13 179.815 0.065 . 1 . . . . . . . . 5856 1 448 . 1 1 100 100 LEU H H 1 7.260 0.030 . 1 . . . . . . . . 5856 1 449 . 1 1 100 100 LEU N N 15 119.620 0.050 . 1 . . . . . . . . 5856 1 450 . 1 1 100 100 LEU CA C 13 57.075 0.015 . 1 . . . . . . . . 5856 1 451 . 1 1 100 100 LEU CB C 13 38.085 0.135 . 1 . . . . . . . . 5856 1 452 . 1 1 100 100 LEU C C 13 179.360 0.030 . 1 . . . . . . . . 5856 1 453 . 1 1 101 101 LEU H H 1 8.110 0.030 . 1 . . . . . . . . 5856 1 454 . 1 1 101 101 LEU N N 15 120.870 0.050 . 1 . . . . . . . . 5856 1 455 . 1 1 101 101 LEU CA C 13 58.140 0.060 . 1 . . . . . . . . 5856 1 456 . 1 1 101 101 LEU CB C 13 39.930 0.100 . 1 . . . . . . . . 5856 1 457 . 1 1 101 101 LEU C C 13 178.910 0.050 . 1 . . . . . . . . 5856 1 458 . 1 1 102 102 SER H H 1 8.280 0.030 . 1 . . . . . . . . 5856 1 459 . 1 1 102 102 SER N N 15 114.970 0.050 . 1 . . . . . . . . 5856 1 460 . 1 1 102 102 SER CA C 13 63.335 0.045 . 1 . . . . . . . . 5856 1 461 . 1 1 102 102 SER C C 13 175.000 0.100 . 1 . . . . . . . . 5856 1 462 . 1 1 103 103 HIS H H 1 7.720 0.030 . 1 . . . . . . . . 5856 1 463 . 1 1 103 103 HIS N N 15 119.850 0.050 . 1 . . . . . . . . 5856 1 464 . 1 1 103 103 HIS CA C 13 59.385 0.045 . 1 . . . . . . . . 5856 1 465 . 1 1 103 103 HIS CB C 13 30.320 0.100 . 1 . . . . . . . . 5856 1 466 . 1 1 103 103 HIS C C 13 176.495 0.005 . 1 . . . . . . . . 5856 1 467 . 1 1 104 104 CYS H H 1 7.800 0.030 . 1 . . . . . . . . 5856 1 468 . 1 1 104 104 CYS N N 15 114.970 0.050 . 1 . . . . . . . . 5856 1 469 . 1 1 104 104 CYS CA C 13 65.285 0.025 . 1 . . . . . . . . 5856 1 470 . 1 1 104 104 CYS CB C 13 27.300 0.100 . 1 . . . . . . . . 5856 1 471 . 1 1 104 104 CYS C C 13 177.590 0.040 . 1 . . . . . . . . 5856 1 472 . 1 1 105 105 LEU H H 1 8.830 0.030 . 1 . . . . . . . . 5856 1 473 . 1 1 105 105 LEU N N 15 125.180 0.050 . 1 . . . . . . . . 5856 1 474 . 1 1 105 105 LEU CA C 13 58.020 0.100 . 1 . . . . . . . . 5856 1 475 . 1 1 105 105 LEU C C 13 177.440 0.100 . 1 . . . . . . . . 5856 1 476 . 1 1 106 106 LEU CA C 13 58.470 0.100 . 1 . . . . . . . . 5856 1 477 . 1 1 106 106 LEU C C 13 177.890 0.100 . 1 . . . . . . . . 5856 1 478 . 1 1 107 107 VAL H H 1 8.140 0.030 . 1 . . . . . . . . 5856 1 479 . 1 1 107 107 VAL N N 15 117.650 0.050 . 1 . . . . . . . . 5856 1 480 . 1 1 107 107 VAL CA C 13 66.205 0.025 . 1 . . . . . . . . 5856 1 481 . 1 1 107 107 VAL CB C 13 31.060 0.100 . 1 . . . . . . . . 5856 1 482 . 1 1 107 107 VAL C C 13 176.215 0.005 . 1 . . . . . . . . 5856 1 483 . 1 1 108 108 THR H H 1 7.090 0.030 . 1 . . . . . . . . 5856 1 484 . 1 1 108 108 THR N N 15 115.000 0.050 . 1 . . . . . . . . 5856 1 485 . 1 1 108 108 THR CA C 13 67.245 0.055 . 1 . . . . . . . . 5856 1 486 . 1 1 108 108 THR CB C 13 68.370 0.100 . 1 . . . . . . . . 5856 1 487 . 1 1 108 108 THR C C 13 175.940 0.100 . 1 . . . . . . . . 5856 1 488 . 1 1 109 109 LEU H H 1 7.950 0.030 . 1 . . . . . . . . 5856 1 489 . 1 1 109 109 LEU N N 15 120.510 0.050 . 1 . . . . . . . . 5856 1 490 . 1 1 109 109 LEU CA C 13 57.870 0.080 . 1 . . . . . . . . 5856 1 491 . 1 1 109 109 LEU CB C 13 39.890 0.100 . 1 . . . . . . . . 5856 1 492 . 1 1 109 109 LEU C C 13 177.550 0.100 . 1 . . . . . . . . 5856 1 493 . 1 1 110 110 ALA H H 1 7.800 0.030 . 1 . . . . . . . . 5856 1 494 . 1 1 110 110 ALA N N 15 121.870 0.050 . 1 . . . . . . . . 5856 1 495 . 1 1 110 110 ALA CA C 13 54.555 0.035 . 1 . . . . . . . . 5856 1 496 . 1 1 110 110 ALA CB C 13 17.120 0.100 . 1 . . . . . . . . 5856 1 497 . 1 1 110 110 ALA C C 13 177.995 0.025 . 1 . . . . . . . . 5856 1 498 . 1 1 111 111 ALA H H 1 7.360 0.030 . 1 . . . . . . . . 5856 1 499 . 1 1 111 111 ALA N N 15 113.540 0.050 . 1 . . . . . . . . 5856 1 500 . 1 1 111 111 ALA CA C 13 52.710 0.010 . 1 . . . . . . . . 5856 1 501 . 1 1 111 111 ALA CB C 13 16.785 0.095 . 1 . . . . . . . . 5856 1 502 . 1 1 111 111 ALA C C 13 179.555 0.025 . 1 . . . . . . . . 5856 1 503 . 1 1 112 112 HIS H H 1 7.160 0.030 . 1 . . . . . . . . 5856 1 504 . 1 1 112 112 HIS N N 15 112.490 0.050 . 1 . . . . . . . . 5856 1 505 . 1 1 112 112 HIS CA C 13 56.710 0.010 . 1 . . . . . . . . 5856 1 506 . 1 1 112 112 HIS CB C 13 30.230 0.020 . 1 . . . . . . . . 5856 1 507 . 1 1 112 112 HIS C C 13 174.760 0.010 . 1 . . . . . . . . 5856 1 508 . 1 1 113 113 LEU H H 1 8.140 0.030 . 1 . . . . . . . . 5856 1 509 . 1 1 113 113 LEU N N 15 121.270 0.050 . 1 . . . . . . . . 5856 1 510 . 1 1 113 113 LEU CA C 13 51.860 0.100 . 1 . . . . . . . . 5856 1 511 . 1 1 113 113 LEU C C 13 173.600 0.100 . 1 . . . . . . . . 5856 1 512 . 1 1 114 114 PRO CA C 13 65.160 0.100 . 1 . . . . . . . . 5856 1 513 . 1 1 114 114 PRO CB C 13 29.480 0.100 . 1 . . . . . . . . 5856 1 514 . 1 1 114 114 PRO C C 13 180.250 0.100 . 1 . . . . . . . . 5856 1 515 . 1 1 115 115 ALA H H 1 8.250 0.030 . 1 . . . . . . . . 5856 1 516 . 1 1 115 115 ALA N N 15 118.860 0.050 . 1 . . . . . . . . 5856 1 517 . 1 1 115 115 ALA CA C 13 53.770 0.000 . 1 . . . . . . . . 5856 1 518 . 1 1 115 115 ALA CB C 13 17.450 0.100 . 1 . . . . . . . . 5856 1 519 . 1 1 115 115 ALA C C 13 179.270 0.080 . 1 . . . . . . . . 5856 1 520 . 1 1 116 116 GLU H H 1 7.650 0.030 . 1 . . . . . . . . 5856 1 521 . 1 1 116 116 GLU N N 15 114.050 0.050 . 1 . . . . . . . . 5856 1 522 . 1 1 116 116 GLU CA C 13 56.145 0.035 . 1 . . . . . . . . 5856 1 523 . 1 1 116 116 GLU CB C 13 28.385 0.035 . 1 . . . . . . . . 5856 1 524 . 1 1 116 116 GLU C C 13 177.575 0.025 . 1 . . . . . . . . 5856 1 525 . 1 1 117 117 PHE H H 1 7.570 0.030 . 1 . . . . . . . . 5856 1 526 . 1 1 117 117 PHE N N 15 123.000 0.050 . 1 . . . . . . . . 5856 1 527 . 1 1 117 117 PHE CA C 13 57.085 0.045 . 1 . . . . . . . . 5856 1 528 . 1 1 117 117 PHE CB C 13 36.880 0.020 . 1 . . . . . . . . 5856 1 529 . 1 1 117 117 PHE C C 13 175.190 0.030 . 1 . . . . . . . . 5856 1 530 . 1 1 118 118 THR H H 1 7.820 0.030 . 1 . . . . . . . . 5856 1 531 . 1 1 118 118 THR N N 15 115.010 0.050 . 1 . . . . . . . . 5856 1 532 . 1 1 118 118 THR CA C 13 59.880 0.100 . 1 . . . . . . . . 5856 1 533 . 1 1 118 118 THR CB C 13 67.050 0.100 . 1 . . . . . . . . 5856 1 534 . 1 1 118 118 THR C C 13 173.360 0.100 . 1 . . . . . . . . 5856 1 535 . 1 1 119 119 PRO CA C 13 66.180 0.100 . 1 . . . . . . . . 5856 1 536 . 1 1 119 119 PRO CB C 13 30.690 0.100 . 1 . . . . . . . . 5856 1 537 . 1 1 119 119 PRO C C 13 176.600 0.100 . 1 . . . . . . . . 5856 1 538 . 1 1 120 120 ALA H H 1 8.280 0.030 . 1 . . . . . . . . 5856 1 539 . 1 1 120 120 ALA N N 15 116.230 0.050 . 1 . . . . . . . . 5856 1 540 . 1 1 120 120 ALA CA C 13 54.210 0.010 . 1 . . . . . . . . 5856 1 541 . 1 1 120 120 ALA CB C 13 17.700 0.030 . 1 . . . . . . . . 5856 1 542 . 1 1 120 120 ALA C C 13 180.275 0.055 . 1 . . . . . . . . 5856 1 543 . 1 1 121 121 VAL H H 1 7.210 0.030 . 1 . . . . . . . . 5856 1 544 . 1 1 121 121 VAL N N 15 120.100 0.050 . 1 . . . . . . . . 5856 1 545 . 1 1 121 121 VAL CA C 13 66.610 0.020 . 1 . . . . . . . . 5856 1 546 . 1 1 121 121 VAL CB C 13 30.760 0.100 . 1 . . . . . . . . 5856 1 547 . 1 1 121 121 VAL C C 13 176.985 0.015 . 1 . . . . . . . . 5856 1 548 . 1 1 122 122 HIS H H 1 8.360 0.030 . 1 . . . . . . . . 5856 1 549 . 1 1 122 122 HIS N N 15 121.830 0.050 . 1 . . . . . . . . 5856 1 550 . 1 1 122 122 HIS CA C 13 57.055 0.035 . 1 . . . . . . . . 5856 1 551 . 1 1 122 122 HIS CB C 13 31.715 0.005 . 1 . . . . . . . . 5856 1 552 . 1 1 122 122 HIS C C 13 177.390 0.100 . 1 . . . . . . . . 5856 1 553 . 1 1 123 123 ALA H H 1 7.880 0.030 . 1 . . . . . . . . 5856 1 554 . 1 1 123 123 ALA N N 15 120.310 0.050 . 1 . . . . . . . . 5856 1 555 . 1 1 123 123 ALA CA C 13 55.110 0.000 . 1 . . . . . . . . 5856 1 556 . 1 1 123 123 ALA CB C 13 17.200 0.100 . 1 . . . . . . . . 5856 1 557 . 1 1 123 123 ALA C C 13 179.645 0.015 . 1 . . . . . . . . 5856 1 558 . 1 1 124 124 SER H H 1 8.040 0.030 . 1 . . . . . . . . 5856 1 559 . 1 1 124 124 SER N N 15 115.620 0.050 . 1 . . . . . . . . 5856 1 560 . 1 1 124 124 SER CA C 13 62.485 0.015 . 1 . . . . . . . . 5856 1 561 . 1 1 124 124 SER C C 13 175.910 0.100 . 1 . . . . . . . . 5856 1 562 . 1 1 125 125 LEU H H 1 9.080 0.030 . 1 . . . . . . . . 5856 1 563 . 1 1 125 125 LEU N N 15 121.470 0.050 . 1 . . . . . . . . 5856 1 564 . 1 1 125 125 LEU CA C 13 57.605 0.045 . 1 . . . . . . . . 5856 1 565 . 1 1 125 125 LEU CB C 13 41.825 0.125 . 1 . . . . . . . . 5856 1 566 . 1 1 125 125 LEU C C 13 178.750 0.030 . 1 . . . . . . . . 5856 1 567 . 1 1 126 126 ASP H H 1 8.580 0.030 . 1 . . . . . . . . 5856 1 568 . 1 1 126 126 ASP N N 15 120.750 0.050 . 1 . . . . . . . . 5856 1 569 . 1 1 126 126 ASP CA C 13 58.390 0.060 . 1 . . . . . . . . 5856 1 570 . 1 1 126 126 ASP CB C 13 42.490 0.100 . 1 . . . . . . . . 5856 1 571 . 1 1 126 126 ASP C C 13 178.980 0.040 . 1 . . . . . . . . 5856 1 572 . 1 1 127 127 LYS H H 1 7.910 0.030 . 1 . . . . . . . . 5856 1 573 . 1 1 127 127 LYS N N 15 118.470 0.050 . 1 . . . . . . . . 5856 1 574 . 1 1 127 127 LYS CA C 13 59.230 0.080 . 1 . . . . . . . . 5856 1 575 . 1 1 127 127 LYS C C 13 180.245 0.085 . 1 . . . . . . . . 5856 1 576 . 1 1 128 128 PHE H H 1 8.810 0.030 . 1 . . . . . . . . 5856 1 577 . 1 1 128 128 PHE N N 15 122.290 0.050 . 1 . . . . . . . . 5856 1 578 . 1 1 128 128 PHE CA C 13 60.700 0.020 . 1 . . . . . . . . 5856 1 579 . 1 1 128 128 PHE CB C 13 39.340 0.100 . 1 . . . . . . . . 5856 1 580 . 1 1 128 128 PHE C C 13 176.590 0.020 . 1 . . . . . . . . 5856 1 581 . 1 1 129 129 LEU H H 1 8.920 0.030 . 1 . . . . . . . . 5856 1 582 . 1 1 129 129 LEU N N 15 121.110 0.050 . 1 . . . . . . . . 5856 1 583 . 1 1 129 129 LEU CA C 13 57.450 0.050 . 1 . . . . . . . . 5856 1 584 . 1 1 129 129 LEU CB C 13 38.860 0.100 . 1 . . . . . . . . 5856 1 585 . 1 1 129 129 LEU C C 13 180.350 0.110 . 1 . . . . . . . . 5856 1 586 . 1 1 130 130 ALA H H 1 8.500 0.030 . 1 . . . . . . . . 5856 1 587 . 1 1 130 130 ALA N N 15 125.530 0.050 . 1 . . . . . . . . 5856 1 588 . 1 1 130 130 ALA CA C 13 54.895 0.015 . 1 . . . . . . . . 5856 1 589 . 1 1 130 130 ALA CB C 13 16.950 0.100 . 1 . . . . . . . . 5856 1 590 . 1 1 130 130 ALA C C 13 180.465 0.055 . 1 . . . . . . . . 5856 1 591 . 1 1 131 131 SER H H 1 8.110 0.030 . 1 . . . . . . . . 5856 1 592 . 1 1 131 131 SER N N 15 118.400 0.050 . 1 . . . . . . . . 5856 1 593 . 1 1 131 131 SER CA C 13 62.270 0.000 . 1 . . . . . . . . 5856 1 594 . 1 1 131 131 SER C C 13 176.860 0.100 . 1 . . . . . . . . 5856 1 595 . 1 1 132 132 VAL H H 1 8.140 0.030 . 1 . . . . . . . . 5856 1 596 . 1 1 132 132 VAL N N 15 123.100 0.050 . 1 . . . . . . . . 5856 1 597 . 1 1 132 132 VAL CA C 13 66.195 0.035 . 1 . . . . . . . . 5856 1 598 . 1 1 132 132 VAL CB C 13 31.060 0.100 . 1 . . . . . . . . 5856 1 599 . 1 1 132 132 VAL C C 13 177.800 0.000 . 1 . . . . . . . . 5856 1 600 . 1 1 133 133 SER H H 1 8.130 0.030 . 1 . . . . . . . . 5856 1 601 . 1 1 133 133 SER N N 15 115.260 0.050 . 1 . . . . . . . . 5856 1 602 . 1 1 133 133 SER CA C 13 62.645 0.015 . 1 . . . . . . . . 5856 1 603 . 1 1 133 133 SER C C 13 175.690 0.100 . 1 . . . . . . . . 5856 1 604 . 1 1 134 134 THR H H 1 8.070 0.030 . 1 . . . . . . . . 5856 1 605 . 1 1 134 134 THR N N 15 119.820 0.050 . 1 . . . . . . . . 5856 1 606 . 1 1 134 134 THR CA C 13 66.105 0.025 . 1 . . . . . . . . 5856 1 607 . 1 1 134 134 THR CB C 13 67.900 0.100 . 1 . . . . . . . . 5856 1 608 . 1 1 134 134 THR C C 13 176.030 0.100 . 1 . . . . . . . . 5856 1 609 . 1 1 135 135 VAL H H 1 7.380 0.030 . 1 . . . . . . . . 5856 1 610 . 1 1 135 135 VAL N N 15 122.480 0.050 . 1 . . . . . . . . 5856 1 611 . 1 1 135 135 VAL CA C 13 66.200 0.100 . 1 . . . . . . . . 5856 1 612 . 1 1 135 135 VAL C C 13 178.550 0.100 . 1 . . . . . . . . 5856 1 613 . 1 1 136 136 LEU C C 13 175.270 0.100 . 1 . . . . . . . . 5856 1 614 . 1 1 137 137 THR H H 1 6.670 0.030 . 1 . . . . . . . . 5856 1 615 . 1 1 137 137 THR N N 15 102.520 0.050 . 1 . . . . . . . . 5856 1 616 . 1 1 137 137 THR CA C 13 59.970 0.000 . 1 . . . . . . . . 5856 1 617 . 1 1 137 137 THR C C 13 175.190 0.100 . 1 . . . . . . . . 5856 1 618 . 1 1 138 138 SER H H 1 7.110 0.030 . 1 . . . . . . . . 5856 1 619 . 1 1 138 138 SER N N 15 118.180 0.050 . 1 . . . . . . . . 5856 1 620 . 1 1 138 138 SER CA C 13 59.180 0.100 . 1 . . . . . . . . 5856 1 621 . 1 1 138 138 SER C C 13 180.660 0.100 . 1 . . . . . . . . 5856 1 stop_ save_ save_chemical_shift_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_2 _Assigned_chem_shift_list.Entry_ID 5856 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 5856 2 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 . 3 2 1 1 VAL CA C 13 58.330 0.100 . 1 . . . . . . . . 5856 2 2 . 3 2 2 2 HIS H H 1 7.550 0.030 . 1 . . . . . . . . 5856 2 3 . 3 2 2 2 HIS N N 15 118.530 0.050 . 1 . . . . . . . . 5856 2 4 . 3 2 2 2 HIS CA C 13 55.220 0.100 . 1 . . . . . . . . 5856 2 5 . 3 2 2 2 HIS C C 13 174.020 0.100 . 1 . . . . . . . . 5856 2 6 . 3 2 3 3 LEU H H 1 8.100 0.030 . 1 . . . . . . . . 5856 2 7 . 3 2 3 3 LEU N N 15 126.090 0.050 . 1 . . . . . . . . 5856 2 8 . 3 2 3 3 LEU CA C 13 53.020 0.020 . 1 . . . . . . . . 5856 2 9 . 3 2 3 3 LEU CB C 13 42.950 0.100 . 1 . . . . . . . . 5856 2 10 . 3 2 3 3 LEU C C 13 177.240 0.030 . 1 . . . . . . . . 5856 2 11 . 3 2 4 4 THR H H 1 9.140 0.030 . 1 . . . . . . . . 5856 2 12 . 3 2 4 4 THR N N 15 115.420 0.050 . 1 . . . . . . . . 5856 2 13 . 3 2 4 4 THR CA C 13 60.200 0.100 . 1 . . . . . . . . 5856 2 14 . 3 2 4 4 THR CB C 13 67.260 0.100 . 1 . . . . . . . . 5856 2 15 . 3 2 4 4 THR C C 13 173.320 0.100 . 1 . . . . . . . . 5856 2 16 . 3 2 5 5 PRO CA C 13 65.800 0.100 . 1 . . . . . . . . 5856 2 17 . 3 2 5 5 PRO CB C 13 30.720 0.100 . 1 . . . . . . . . 5856 2 18 . 3 2 5 5 PRO C C 13 179.630 0.100 . 1 . . . . . . . . 5856 2 19 . 3 2 6 6 GLU H H 1 8.590 0.030 . 1 . . . . . . . . 5856 2 20 . 3 2 6 6 GLU N N 15 117.560 0.050 . 1 . . . . . . . . 5856 2 21 . 3 2 6 6 GLU CA C 13 59.495 0.025 . 1 . . . . . . . . 5856 2 22 . 3 2 6 6 GLU CB C 13 28.135 0.095 . 1 . . . . . . . . 5856 2 23 . 3 2 6 6 GLU C C 13 179.900 0.040 . 1 . . . . . . . . 5856 2 24 . 3 2 7 7 GLU H H 1 7.680 0.030 . 1 . . . . . . . . 5856 2 25 . 3 2 7 7 GLU N N 15 121.740 0.050 . 1 . . . . . . . . 5856 2 26 . 3 2 7 7 GLU CA C 13 58.505 0.015 . 1 . . . . . . . . 5856 2 27 . 3 2 7 7 GLU CB C 13 30.475 0.025 . 1 . . . . . . . . 5856 2 28 . 3 2 7 7 GLU C C 13 178.355 0.025 . 1 . . . . . . . . 5856 2 29 . 3 2 8 8 LYS H H 1 8.710 0.030 . 1 . . . . . . . . 5856 2 30 . 3 2 8 8 LYS N N 15 119.170 0.050 . 1 . . . . . . . . 5856 2 31 . 3 2 8 8 LYS CA C 13 59.645 0.035 . 1 . . . . . . . . 5856 2 32 . 3 2 8 8 LYS CB C 13 31.145 0.055 . 1 . . . . . . . . 5856 2 33 . 3 2 8 8 LYS C C 13 179.400 0.010 . 1 . . . . . . . . 5856 2 34 . 3 2 9 9 SER H H 1 8.080 0.030 . 1 . . . . . . . . 5856 2 35 . 3 2 9 9 SER N N 15 115.200 0.050 . 1 . . . . . . . . 5856 2 36 . 3 2 9 9 SER CA C 13 61.120 0.010 . 1 . . . . . . . . 5856 2 37 . 3 2 9 9 SER CB C 13 62.025 0.055 . 1 . . . . . . . . 5856 2 38 . 3 2 9 9 SER C C 13 176.270 0.100 . 1 . . . . . . . . 5856 2 39 . 3 2 10 10 ALA H H 1 7.570 0.030 . 1 . . . . . . . . 5856 2 40 . 3 2 10 10 ALA N N 15 123.950 0.050 . 1 . . . . . . . . 5856 2 41 . 3 2 10 10 ALA CA C 13 54.495 0.025 . 1 . . . . . . . . 5856 2 42 . 3 2 10 10 ALA CB C 13 17.540 0.100 . 1 . . . . . . . . 5856 2 43 . 3 2 10 10 ALA C C 13 180.900 0.040 . 1 . . . . . . . . 5856 2 44 . 3 2 11 11 VAL H H 1 8.330 0.030 . 1 . . . . . . . . 5856 2 45 . 3 2 11 11 VAL N N 15 115.940 0.050 . 1 . . . . . . . . 5856 2 46 . 3 2 11 11 VAL CA C 13 65.365 0.005 . 1 . . . . . . . . 5856 2 47 . 3 2 11 11 VAL CB C 13 30.800 0.100 . 1 . . . . . . . . 5856 2 48 . 3 2 11 11 VAL C C 13 179.910 0.030 . 1 . . . . . . . . 5856 2 49 . 3 2 12 12 THR H H 1 8.300 0.030 . 1 . . . . . . . . 5856 2 50 . 3 2 12 12 THR N N 15 115.680 0.050 . 1 . . . . . . . . 5856 2 51 . 3 2 12 12 THR CA C 13 65.790 0.100 . 1 . . . . . . . . 5856 2 52 . 3 2 12 12 THR CB C 13 68.060 0.100 . 1 . . . . . . . . 5856 2 53 . 3 2 12 12 THR C C 13 176.940 0.100 . 1 . . . . . . . . 5856 2 54 . 3 2 13 13 ALA H H 1 8.170 0.030 . 1 . . . . . . . . 5856 2 55 . 3 2 13 13 ALA N N 15 125.790 0.050 . 1 . . . . . . . . 5856 2 56 . 3 2 13 13 ALA CA C 13 54.600 0.010 . 1 . . . . . . . . 5856 2 57 . 3 2 13 13 ALA CB C 13 17.245 0.045 . 1 . . . . . . . . 5856 2 58 . 3 2 13 13 ALA C C 13 180.495 0.055 . 1 . . . . . . . . 5856 2 59 . 3 2 14 14 LEU H H 1 7.140 0.030 . 1 . . . . . . . . 5856 2 60 . 3 2 14 14 LEU N N 15 117.210 0.050 . 1 . . . . . . . . 5856 2 61 . 3 2 14 14 LEU CA C 13 57.340 0.100 . 1 . . . . . . . . 5856 2 62 . 3 2 14 14 LEU CB C 13 40.400 0.100 . 1 . . . . . . . . 5856 2 63 . 3 2 14 14 LEU C C 13 178.900 0.010 . 1 . . . . . . . . 5856 2 64 . 3 2 15 15 TRP H H 1 8.060 0.030 . 1 . . . . . . . . 5856 2 65 . 3 2 15 15 TRP N N 15 119.190 0.050 . 1 . . . . . . . . 5856 2 66 . 3 2 15 15 TRP CA C 13 59.530 0.030 . 1 . . . . . . . . 5856 2 67 . 3 2 15 15 TRP C C 13 179.190 0.000 . 1 . . . . . . . . 5856 2 68 . 3 2 16 16 GLY H H 1 7.720 0.030 . 1 . . . . . . . . 5856 2 69 . 3 2 16 16 GLY N N 15 101.630 0.050 . 1 . . . . . . . . 5856 2 70 . 3 2 16 16 GLY CA C 13 45.750 0.000 . 1 . . . . . . . . 5856 2 71 . 3 2 16 16 GLY C C 13 174.730 0.010 . 1 . . . . . . . . 5856 2 72 . 3 2 17 17 LYS H H 1 7.640 0.030 . 1 . . . . . . . . 5856 2 73 . 3 2 17 17 LYS N N 15 118.380 0.050 . 1 . . . . . . . . 5856 2 74 . 3 2 17 17 LYS CA C 13 55.500 0.000 . 1 . . . . . . . . 5856 2 75 . 3 2 17 17 LYS CB C 13 32.600 0.010 . 1 . . . . . . . . 5856 2 76 . 3 2 17 17 LYS C C 13 176.820 0.100 . 1 . . . . . . . . 5856 2 77 . 3 2 18 18 VAL H H 1 7.150 0.030 . 1 . . . . . . . . 5856 2 78 . 3 2 18 18 VAL N N 15 121.770 0.050 . 1 . . . . . . . . 5856 2 79 . 3 2 18 18 VAL CA C 13 62.770 0.020 . 1 . . . . . . . . 5856 2 80 . 3 2 18 18 VAL CB C 13 31.260 0.010 . 1 . . . . . . . . 5856 2 81 . 3 2 18 18 VAL C C 13 175.250 0.000 . 1 . . . . . . . . 5856 2 82 . 3 2 19 19 ASN H H 1 8.270 0.030 . 1 . . . . . . . . 5856 2 83 . 3 2 19 19 ASN N N 15 124.850 0.050 . 1 . . . . . . . . 5856 2 84 . 3 2 19 19 ASN CA C 13 51.770 0.020 . 1 . . . . . . . . 5856 2 85 . 3 2 19 19 ASN CB C 13 36.360 0.020 . 1 . . . . . . . . 5856 2 86 . 3 2 19 19 ASN C C 13 176.070 0.000 . 1 . . . . . . . . 5856 2 87 . 3 2 20 20 VAL H H 1 8.070 0.030 . 1 . . . . . . . . 5856 2 88 . 3 2 20 20 VAL N N 15 124.210 0.050 . 1 . . . . . . . . 5856 2 89 . 3 2 20 20 VAL CA C 13 63.510 0.010 . 1 . . . . . . . . 5856 2 90 . 3 2 20 20 VAL CB C 13 30.295 0.045 . 1 . . . . . . . . 5856 2 91 . 3 2 20 20 VAL C C 13 176.840 0.010 . 1 . . . . . . . . 5856 2 92 . 3 2 21 21 ASP H H 1 7.850 0.030 . 1 . . . . . . . . 5856 2 93 . 3 2 21 21 ASP N N 15 119.270 0.050 . 1 . . . . . . . . 5856 2 94 . 3 2 21 21 ASP CA C 13 55.940 0.010 . 1 . . . . . . . . 5856 2 95 . 3 2 21 21 ASP CB C 13 40.605 0.025 . 1 . . . . . . . . 5856 2 96 . 3 2 21 21 ASP C C 13 177.425 0.045 . 1 . . . . . . . . 5856 2 97 . 3 2 22 22 GLU H H 1 7.120 0.030 . 1 . . . . . . . . 5856 2 98 . 3 2 22 22 GLU N N 15 117.370 0.050 . 1 . . . . . . . . 5856 2 99 . 3 2 22 22 GLU CA C 13 56.650 0.090 . 1 . . . . . . . . 5856 2 100 . 3 2 22 22 GLU CB C 13 31.825 0.015 . 1 . . . . . . . . 5856 2 101 . 3 2 22 22 GLU C C 13 177.990 0.100 . 1 . . . . . . . . 5856 2 102 . 3 2 23 23 VAL H H 1 7.680 0.030 . 1 . . . . . . . . 5856 2 103 . 3 2 23 23 VAL N N 15 118.270 0.050 . 1 . . . . . . . . 5856 2 104 . 3 2 23 23 VAL CA C 13 66.345 0.015 . 1 . . . . . . . . 5856 2 105 . 3 2 23 23 VAL C C 13 176.860 0.100 . 1 . . . . . . . . 5856 2 106 . 3 2 24 24 GLY H H 1 8.500 0.030 . 1 . . . . . . . . 5856 2 107 . 3 2 24 24 GLY N N 15 108.610 0.050 . 1 . . . . . . . . 5856 2 108 . 3 2 24 24 GLY CA C 13 46.825 0.015 . 1 . . . . . . . . 5856 2 109 . 3 2 24 24 GLY C C 13 175.795 0.025 . 1 . . . . . . . . 5856 2 110 . 3 2 25 25 GLY H H 1 7.380 0.030 . 1 . . . . . . . . 5856 2 111 . 3 2 25 25 GLY N N 15 108.930 0.050 . 1 . . . . . . . . 5856 2 112 . 3 2 25 25 GLY CA C 13 46.905 0.025 . 1 . . . . . . . . 5856 2 113 . 3 2 25 25 GLY C C 13 175.795 0.025 . 1 . . . . . . . . 5856 2 114 . 3 2 26 26 GLU H H 1 7.520 0.030 . 1 . . . . . . . . 5856 2 115 . 3 2 26 26 GLU N N 15 122.020 0.050 . 1 . . . . . . . . 5856 2 116 . 3 2 26 26 GLU CA C 13 58.460 0.010 . 1 . . . . . . . . 5856 2 117 . 3 2 26 26 GLU CB C 13 28.720 0.100 . 1 . . . . . . . . 5856 2 118 . 3 2 26 26 GLU C C 13 178.200 0.010 . 1 . . . . . . . . 5856 2 119 . 3 2 27 27 ALA H H 1 7.930 0.030 . 1 . . . . . . . . 5856 2 120 . 3 2 27 27 ALA N N 15 119.980 0.050 . 1 . . . . . . . . 5856 2 121 . 3 2 27 27 ALA CA C 13 54.110 0.020 . 1 . . . . . . . . 5856 2 122 . 3 2 27 27 ALA CB C 13 15.960 0.020 . 1 . . . . . . . . 5856 2 123 . 3 2 27 27 ALA C C 13 177.220 0.030 . 1 . . . . . . . . 5856 2 124 . 3 2 28 28 LEU H H 1 7.760 0.030 . 1 . . . . . . . . 5856 2 125 . 3 2 28 28 LEU N N 15 116.510 0.050 . 1 . . . . . . . . 5856 2 126 . 3 2 28 28 LEU CA C 13 56.260 0.010 . 1 . . . . . . . . 5856 2 127 . 3 2 28 28 LEU CB C 13 40.450 0.050 . 1 . . . . . . . . 5856 2 128 . 3 2 28 28 LEU C C 13 177.260 0.040 . 1 . . . . . . . . 5856 2 129 . 3 2 29 29 GLY H H 1 7.960 0.030 . 1 . . . . . . . . 5856 2 130 . 3 2 29 29 GLY N N 15 104.270 0.050 . 1 . . . . . . . . 5856 2 131 . 3 2 29 29 GLY CA C 13 46.835 0.005 . 1 . . . . . . . . 5856 2 132 . 3 2 29 29 GLY C C 13 174.860 0.000 . 1 . . . . . . . . 5856 2 133 . 3 2 30 30 ARG H H 1 7.790 0.030 . 1 . . . . . . . . 5856 2 134 . 3 2 30 30 ARG N N 15 117.090 0.050 . 1 . . . . . . . . 5856 2 135 . 3 2 30 30 ARG CA C 13 60.030 0.010 . 1 . . . . . . . . 5856 2 136 . 3 2 30 30 ARG CB C 13 29.120 0.100 . 1 . . . . . . . . 5856 2 137 . 3 2 30 30 ARG C C 13 177.610 0.030 . 1 . . . . . . . . 5856 2 138 . 3 2 31 31 LEU H H 1 7.660 0.030 . 1 . . . . . . . . 5856 2 139 . 3 2 31 31 LEU N N 15 121.110 0.050 . 1 . . . . . . . . 5856 2 140 . 3 2 31 31 LEU CA C 13 58.985 0.055 . 1 . . . . . . . . 5856 2 141 . 3 2 31 31 LEU C C 13 176.410 0.100 . 1 . . . . . . . . 5856 2 142 . 3 2 32 32 LEU H H 1 6.950 0.030 . 1 . . . . . . . . 5856 2 143 . 3 2 32 32 LEU N N 15 115.460 0.050 . 1 . . . . . . . . 5856 2 144 . 3 2 32 32 LEU CA C 13 56.325 0.015 . 1 . . . . . . . . 5856 2 145 . 3 2 32 32 LEU C C 13 178.250 0.100 . 1 . . . . . . . . 5856 2 146 . 3 2 33 33 VAL H H 1 7.390 0.030 . 1 . . . . . . . . 5856 2 147 . 3 2 33 33 VAL N N 15 116.360 0.050 . 1 . . . . . . . . 5856 2 148 . 3 2 33 33 VAL CA C 13 64.085 0.065 . 1 . . . . . . . . 5856 2 149 . 3 2 33 33 VAL C C 13 176.785 0.015 . 1 . . . . . . . . 5856 2 150 . 3 2 34 34 VAL H H 1 8.480 0.030 . 1 . . . . . . . . 5856 2 151 . 3 2 34 34 VAL N N 15 119.240 0.050 . 1 . . . . . . . . 5856 2 152 . 3 2 34 34 VAL CA C 13 64.560 0.060 . 1 . . . . . . . . 5856 2 153 . 3 2 34 34 VAL C C 13 175.070 0.000 . 1 . . . . . . . . 5856 2 154 . 3 2 35 35 TYR H H 1 7.380 0.030 . 1 . . . . . . . . 5856 2 155 . 3 2 35 35 TYR N N 15 117.750 0.050 . 1 . . . . . . . . 5856 2 156 . 3 2 35 35 TYR CA C 13 52.770 0.100 . 1 . . . . . . . . 5856 2 157 . 3 2 36 36 PRO CA C 13 65.190 0.100 . 1 . . . . . . . . 5856 2 158 . 3 2 36 36 PRO C C 13 178.550 0.100 . 1 . . . . . . . . 5856 2 159 . 3 2 37 37 TRP H H 1 7.000 0.030 . 1 . . . . . . . . 5856 2 160 . 3 2 37 37 TRP N N 15 117.270 0.050 . 1 . . . . . . . . 5856 2 161 . 3 2 37 37 TRP CA C 13 60.680 0.000 . 1 . . . . . . . . 5856 2 162 . 3 2 37 37 TRP C C 13 179.970 0.100 . 1 . . . . . . . . 5856 2 163 . 3 2 38 38 THR H H 1 8.120 0.030 . 1 . . . . . . . . 5856 2 164 . 3 2 38 38 THR N N 15 117.410 0.050 . 1 . . . . . . . . 5856 2 165 . 3 2 38 38 THR CA C 13 65.410 0.000 . 1 . . . . . . . . 5856 2 166 . 3 2 38 38 THR C C 13 176.570 0.100 . 1 . . . . . . . . 5856 2 167 . 3 2 39 39 GLN H H 1 7.640 0.030 . 1 . . . . . . . . 5856 2 168 . 3 2 39 39 GLN N N 15 118.050 0.050 . 1 . . . . . . . . 5856 2 169 . 3 2 39 39 GLN CA C 13 58.200 0.100 . 1 . . . . . . . . 5856 2 170 . 3 2 39 39 GLN CB C 13 27.700 0.000 . 1 . . . . . . . . 5856 2 171 . 3 2 39 39 GLN C C 13 178.750 0.000 . 1 . . . . . . . . 5856 2 172 . 3 2 40 40 ARG H H 1 7.670 0.030 . 1 . . . . . . . . 5856 2 173 . 3 2 40 40 ARG N N 15 118.450 0.050 . 1 . . . . . . . . 5856 2 174 . 3 2 40 40 ARG CA C 13 58.590 0.100 . 1 . . . . . . . . 5856 2 175 . 3 2 40 40 ARG C C 13 177.440 0.100 . 1 . . . . . . . . 5856 2 176 . 3 2 41 41 PHE H H 1 7.400 0.030 . 1 . . . . . . . . 5856 2 177 . 3 2 41 41 PHE N N 15 112.450 0.050 . 1 . . . . . . . . 5856 2 178 . 3 2 41 41 PHE CA C 13 59.760 0.010 . 1 . . . . . . . . 5856 2 179 . 3 2 41 41 PHE CB C 13 39.520 0.100 . 1 . . . . . . . . 5856 2 180 . 3 2 41 41 PHE C C 13 175.125 0.015 . 1 . . . . . . . . 5856 2 181 . 3 2 42 42 PHE H H 1 7.490 0.030 . 1 . . . . . . . . 5856 2 182 . 3 2 42 42 PHE N N 15 116.500 0.050 . 1 . . . . . . . . 5856 2 183 . 3 2 42 42 PHE CA C 13 56.675 0.025 . 1 . . . . . . . . 5856 2 184 . 3 2 42 42 PHE CB C 13 39.010 0.080 . 1 . . . . . . . . 5856 2 185 . 3 2 42 42 PHE C C 13 175.520 0.030 . 1 . . . . . . . . 5856 2 186 . 3 2 43 43 GLU H H 1 7.330 0.030 . 1 . . . . . . . . 5856 2 187 . 3 2 43 43 GLU N N 15 121.240 0.050 . 1 . . . . . . . . 5856 2 188 . 3 2 43 43 GLU CA C 13 59.090 0.100 . 1 . . . . . . . . 5856 2 189 . 3 2 43 43 GLU CB C 13 29.030 0.100 . 1 . . . . . . . . 5856 2 190 . 3 2 43 43 GLU C C 13 178.500 0.100 . 1 . . . . . . . . 5856 2 191 . 3 2 44 44 SER H H 1 8.680 0.030 . 1 . . . . . . . . 5856 2 192 . 3 2 44 44 SER N N 15 113.770 0.050 . 1 . . . . . . . . 5856 2 193 . 3 2 44 44 SER CA C 13 59.560 0.100 . 1 . . . . . . . . 5856 2 194 . 3 2 44 44 SER CB C 13 62.450 0.100 . 1 . . . . . . . . 5856 2 195 . 3 2 44 44 SER C C 13 175.780 0.100 . 1 . . . . . . . . 5856 2 196 . 3 2 45 45 PHE H H 1 8.470 0.030 . 1 . . . . . . . . 5856 2 197 . 3 2 45 45 PHE N N 15 122.270 0.050 . 1 . . . . . . . . 5856 2 198 . 3 2 45 45 PHE CA C 13 56.440 0.010 . 1 . . . . . . . . 5856 2 199 . 3 2 45 45 PHE CB C 13 35.890 0.010 . 1 . . . . . . . . 5856 2 200 . 3 2 45 45 PHE C C 13 175.685 0.025 . 1 . . . . . . . . 5856 2 201 . 3 2 46 46 GLY H H 1 7.660 0.030 . 1 . . . . . . . . 5856 2 202 . 3 2 46 46 GLY N N 15 108.230 0.050 . 1 . . . . . . . . 5856 2 203 . 3 2 46 46 GLY CA C 13 44.290 0.020 . 1 . . . . . . . . 5856 2 204 . 3 2 46 46 GLY C C 13 172.760 0.010 . 1 . . . . . . . . 5856 2 205 . 3 2 47 47 ASP H H 1 8.360 0.030 . 1 . . . . . . . . 5856 2 206 . 3 2 47 47 ASP N N 15 122.540 0.050 . 1 . . . . . . . . 5856 2 207 . 3 2 47 47 ASP CA C 13 55.120 0.010 . 1 . . . . . . . . 5856 2 208 . 3 2 47 47 ASP CB C 13 39.765 0.065 . 1 . . . . . . . . 5856 2 209 . 3 2 47 47 ASP C C 13 175.705 0.015 . 1 . . . . . . . . 5856 2 210 . 3 2 48 48 LEU H H 1 8.320 0.030 . 1 . . . . . . . . 5856 2 211 . 3 2 48 48 LEU N N 15 128.530 0.050 . 1 . . . . . . . . 5856 2 212 . 3 2 48 48 LEU CA C 13 52.190 0.010 . 1 . . . . . . . . 5856 2 213 . 3 2 48 48 LEU CB C 13 40.200 0.100 . 1 . . . . . . . . 5856 2 214 . 3 2 48 48 LEU C C 13 177.830 0.030 . 1 . . . . . . . . 5856 2 215 . 3 2 49 49 SER H H 1 8.100 0.030 . 1 . . . . . . . . 5856 2 216 . 3 2 49 49 SER N N 15 112.870 0.050 . 1 . . . . . . . . 5856 2 217 . 3 2 49 49 SER CA C 13 61.630 0.020 . 1 . . . . . . . . 5856 2 218 . 3 2 49 49 SER CB C 13 63.470 0.160 . 1 . . . . . . . . 5856 2 219 . 3 2 49 49 SER C C 13 175.090 0.020 . 1 . . . . . . . . 5856 2 220 . 3 2 50 50 THR H H 1 7.020 0.030 . 1 . . . . . . . . 5856 2 221 . 3 2 50 50 THR N N 15 111.610 0.050 . 1 . . . . . . . . 5856 2 222 . 3 2 50 50 THR CA C 13 57.840 0.100 . 1 . . . . . . . . 5856 2 223 . 3 2 50 50 THR CB C 13 69.970 0.100 . 1 . . . . . . . . 5856 2 224 . 3 2 50 50 THR C C 13 173.070 0.100 . 1 . . . . . . . . 5856 2 225 . 3 2 51 51 PRO CA C 13 65.200 0.100 . 1 . . . . . . . . 5856 2 226 . 3 2 51 51 PRO CB C 13 30.480 0.100 . 1 . . . . . . . . 5856 2 227 . 3 2 51 51 PRO C C 13 177.610 0.100 . 1 . . . . . . . . 5856 2 228 . 3 2 52 52 ASP H H 1 7.890 0.030 . 1 . . . . . . . . 5856 2 229 . 3 2 52 52 ASP N N 15 114.660 0.050 . 1 . . . . . . . . 5856 2 230 . 3 2 52 52 ASP CA C 13 56.580 0.000 . 1 . . . . . . . . 5856 2 231 . 3 2 52 52 ASP CB C 13 39.500 0.000 . 1 . . . . . . . . 5856 2 232 . 3 2 52 52 ASP C C 13 178.940 0.060 . 1 . . . . . . . . 5856 2 233 . 3 2 53 53 ALA H H 1 7.720 0.030 . 1 . . . . . . . . 5856 2 234 . 3 2 53 53 ALA N N 15 123.860 0.050 . 1 . . . . . . . . 5856 2 235 . 3 2 53 53 ALA CA C 13 54.120 0.010 . 1 . . . . . . . . 5856 2 236 . 3 2 53 53 ALA CB C 13 17.470 0.010 . 1 . . . . . . . . 5856 2 237 . 3 2 53 53 ALA C C 13 180.190 0.030 . 1 . . . . . . . . 5856 2 238 . 3 2 54 54 VAL H H 1 7.750 0.030 . 1 . . . . . . . . 5856 2 239 . 3 2 54 54 VAL N N 15 116.880 0.050 . 1 . . . . . . . . 5856 2 240 . 3 2 54 54 VAL CA C 13 66.315 0.015 . 1 . . . . . . . . 5856 2 241 . 3 2 54 54 VAL CB C 13 31.060 0.030 . 1 . . . . . . . . 5856 2 242 . 3 2 54 54 VAL C C 13 178.035 0.035 . 1 . . . . . . . . 5856 2 243 . 3 2 55 55 MET H H 1 7.830 0.030 . 1 . . . . . . . . 5856 2 244 . 3 2 55 55 MET N N 15 111.990 0.050 . 1 . . . . . . . . 5856 2 245 . 3 2 55 55 MET CA C 13 54.810 0.020 . 1 . . . . . . . . 5856 2 246 . 3 2 55 55 MET CB C 13 27.875 0.005 . 1 . . . . . . . . 5856 2 247 . 3 2 55 55 MET C C 13 178.425 0.015 . 1 . . . . . . . . 5856 2 248 . 3 2 56 56 GLY H H 1 7.310 0.030 . 1 . . . . . . . . 5856 2 249 . 3 2 56 56 GLY N N 15 103.510 0.050 . 1 . . . . . . . . 5856 2 250 . 3 2 56 56 GLY CA C 13 43.770 0.020 . 1 . . . . . . . . 5856 2 251 . 3 2 56 56 GLY C C 13 173.785 0.015 . 1 . . . . . . . . 5856 2 252 . 3 2 57 57 ASN H H 1 7.090 0.030 . 1 . . . . . . . . 5856 2 253 . 3 2 57 57 ASN N N 15 123.580 0.050 . 1 . . . . . . . . 5856 2 254 . 3 2 57 57 ASN CA C 13 51.340 0.100 . 1 . . . . . . . . 5856 2 255 . 3 2 57 57 ASN CB C 13 38.220 0.100 . 1 . . . . . . . . 5856 2 256 . 3 2 57 57 ASN C C 13 174.960 0.100 . 1 . . . . . . . . 5856 2 257 . 3 2 58 58 PRO CA C 13 64.430 0.100 . 1 . . . . . . . . 5856 2 258 . 3 2 58 58 PRO CB C 13 31.260 0.100 . 1 . . . . . . . . 5856 2 259 . 3 2 58 58 PRO C C 13 179.630 0.100 . 1 . . . . . . . . 5856 2 260 . 3 2 59 59 LYS H H 1 8.010 0.030 . 1 . . . . . . . . 5856 2 261 . 3 2 59 59 LYS N N 15 119.360 0.050 . 1 . . . . . . . . 5856 2 262 . 3 2 59 59 LYS CA C 13 58.610 0.020 . 1 . . . . . . . . 5856 2 263 . 3 2 59 59 LYS CB C 13 29.950 0.100 . 1 . . . . . . . . 5856 2 264 . 3 2 59 59 LYS C C 13 179.430 0.040 . 1 . . . . . . . . 5856 2 265 . 3 2 60 60 VAL H H 1 7.400 0.030 . 1 . . . . . . . . 5856 2 266 . 3 2 60 60 VAL N N 15 122.540 0.050 . 1 . . . . . . . . 5856 2 267 . 3 2 60 60 VAL CA C 13 65.695 0.005 . 1 . . . . . . . . 5856 2 268 . 3 2 60 60 VAL CB C 13 30.540 0.000 . 1 . . . . . . . . 5856 2 269 . 3 2 60 60 VAL C C 13 177.785 0.015 . 1 . . . . . . . . 5856 2 270 . 3 2 61 61 LYS H H 1 7.240 0.030 . 1 . . . . . . . . 5856 2 271 . 3 2 61 61 LYS N N 15 118.730 0.050 . 1 . . . . . . . . 5856 2 272 . 3 2 61 61 LYS CA C 13 59.725 0.025 . 1 . . . . . . . . 5856 2 273 . 3 2 61 61 LYS CB C 13 31.065 0.025 . 1 . . . . . . . . 5856 2 274 . 3 2 61 61 LYS C C 13 179.435 0.025 . 1 . . . . . . . . 5856 2 275 . 3 2 62 62 ALA H H 1 7.760 0.030 . 1 . . . . . . . . 5856 2 276 . 3 2 62 62 ALA N N 15 120.840 0.050 . 1 . . . . . . . . 5856 2 277 . 3 2 62 62 ALA CA C 13 54.400 0.000 . 1 . . . . . . . . 5856 2 278 . 3 2 62 62 ALA CB C 13 17.435 0.015 . 1 . . . . . . . . 5856 2 279 . 3 2 62 62 ALA C C 13 180.765 0.055 . 1 . . . . . . . . 5856 2 280 . 3 2 63 63 HIS H H 1 8.250 0.030 . 1 . . . . . . . . 5856 2 281 . 3 2 63 63 HIS N N 15 120.610 0.050 . 1 . . . . . . . . 5856 2 282 . 3 2 63 63 HIS CA C 13 59.370 0.030 . 1 . . . . . . . . 5856 2 283 . 3 2 63 63 HIS CB C 13 30.590 0.020 . 1 . . . . . . . . 5856 2 284 . 3 2 63 63 HIS C C 13 177.790 0.010 . 1 . . . . . . . . 5856 2 285 . 3 2 64 64 GLY H H 1 8.120 0.030 . 1 . . . . . . . . 5856 2 286 . 3 2 64 64 GLY N N 15 105.650 0.050 . 1 . . . . . . . . 5856 2 287 . 3 2 64 64 GLY CA C 13 45.460 0.010 . 1 . . . . . . . . 5856 2 288 . 3 2 64 64 GLY C C 13 174.850 0.100 . 1 . . . . . . . . 5856 2 289 . 3 2 65 65 LYS H H 1 6.990 0.030 . 1 . . . . . . . . 5856 2 290 . 3 2 65 65 LYS N N 15 120.930 0.050 . 1 . . . . . . . . 5856 2 291 . 3 2 65 65 LYS CA C 13 59.550 0.030 . 1 . . . . . . . . 5856 2 292 . 3 2 65 65 LYS CB C 13 31.310 0.100 . 1 . . . . . . . . 5856 2 293 . 3 2 65 65 LYS C C 13 179.660 0.000 . 1 . . . . . . . . 5856 2 294 . 3 2 66 66 LYS H H 1 6.860 0.030 . 1 . . . . . . . . 5856 2 295 . 3 2 66 66 LYS N N 15 120.260 0.050 . 1 . . . . . . . . 5856 2 296 . 3 2 66 66 LYS CA C 13 58.985 0.035 . 1 . . . . . . . . 5856 2 297 . 3 2 66 66 LYS CB C 13 30.730 0.100 . 1 . . . . . . . . 5856 2 298 . 3 2 66 66 LYS C C 13 180.035 0.095 . 1 . . . . . . . . 5856 2 299 . 3 2 67 67 VAL H H 1 7.220 0.030 . 1 . . . . . . . . 5856 2 300 . 3 2 67 67 VAL N N 15 121.160 0.050 . 1 . . . . . . . . 5856 2 301 . 3 2 67 67 VAL CA C 13 66.000 0.000 . 1 . . . . . . . . 5856 2 302 . 3 2 67 67 VAL CB C 13 29.810 0.100 . 1 . . . . . . . . 5856 2 303 . 3 2 67 67 VAL C C 13 178.220 0.000 . 1 . . . . . . . . 5856 2 304 . 3 2 68 68 LEU H H 1 8.110 0.030 . 1 . . . . . . . . 5856 2 305 . 3 2 68 68 LEU N N 15 119.680 0.050 . 1 . . . . . . . . 5856 2 306 . 3 2 68 68 LEU CA C 13 57.725 0.025 . 1 . . . . . . . . 5856 2 307 . 3 2 68 68 LEU CB C 13 40.235 0.035 . 1 . . . . . . . . 5856 2 308 . 3 2 68 68 LEU C C 13 179.750 0.030 . 1 . . . . . . . . 5856 2 309 . 3 2 69 69 GLY H H 1 8.260 0.030 . 1 . . . . . . . . 5856 2 310 . 3 2 69 69 GLY N N 15 107.850 0.050 . 1 . . . . . . . . 5856 2 311 . 3 2 69 69 GLY CA C 13 46.900 0.000 . 1 . . . . . . . . 5856 2 312 . 3 2 69 69 GLY C C 13 176.050 0.000 . 1 . . . . . . . . 5856 2 313 . 3 2 70 70 ALA H H 1 8.050 0.030 . 1 . . . . . . . . 5856 2 314 . 3 2 70 70 ALA N N 15 125.230 0.050 . 1 . . . . . . . . 5856 2 315 . 3 2 70 70 ALA CA C 13 54.780 0.010 . 1 . . . . . . . . 5856 2 316 . 3 2 70 70 ALA CB C 13 18.500 0.100 . 1 . . . . . . . . 5856 2 317 . 3 2 70 70 ALA C C 13 180.675 0.065 . 1 . . . . . . . . 5856 2 318 . 3 2 71 71 PHE H H 1 8.450 0.030 . 1 . . . . . . . . 5856 2 319 . 3 2 71 71 PHE N N 15 118.290 0.050 . 1 . . . . . . . . 5856 2 320 . 3 2 71 71 PHE CA C 13 64.135 0.045 . 1 . . . . . . . . 5856 2 321 . 3 2 71 71 PHE CB C 13 39.110 0.100 . 1 . . . . . . . . 5856 2 322 . 3 2 71 71 PHE C C 13 178.230 0.020 . 1 . . . . . . . . 5856 2 323 . 3 2 72 72 SER H H 1 9.090 0.030 . 1 . . . . . . . . 5856 2 324 . 3 2 72 72 SER N N 15 116.250 0.050 . 1 . . . . . . . . 5856 2 325 . 3 2 72 72 SER CA C 13 62.045 0.045 . 1 . . . . . . . . 5856 2 326 . 3 2 72 72 SER C C 13 177.070 0.100 . 1 . . . . . . . . 5856 2 327 . 3 2 73 73 ASP H H 1 8.200 0.030 . 1 . . . . . . . . 5856 2 328 . 3 2 73 73 ASP N N 15 123.840 0.050 . 1 . . . . . . . . 5856 2 329 . 3 2 73 73 ASP CA C 13 56.930 0.000 . 1 . . . . . . . . 5856 2 330 . 3 2 73 73 ASP CB C 13 39.650 0.000 . 1 . . . . . . . . 5856 2 331 . 3 2 73 73 ASP C C 13 179.280 0.070 . 1 . . . . . . . . 5856 2 332 . 3 2 74 74 GLY H H 1 8.470 0.030 . 1 . . . . . . . . 5856 2 333 . 3 2 74 74 GLY N N 15 108.290 0.050 . 1 . . . . . . . . 5856 2 334 . 3 2 74 74 GLY CA C 13 47.335 0.005 . 1 . . . . . . . . 5856 2 335 . 3 2 74 74 GLY C C 13 174.520 0.000 . 1 . . . . . . . . 5856 2 336 . 3 2 75 75 LEU H H 1 7.980 0.030 . 1 . . . . . . . . 5856 2 337 . 3 2 75 75 LEU N N 15 119.850 0.050 . 1 . . . . . . . . 5856 2 338 . 3 2 75 75 LEU CA C 13 57.115 0.035 . 1 . . . . . . . . 5856 2 339 . 3 2 75 75 LEU CB C 13 40.495 0.045 . 1 . . . . . . . . 5856 2 340 . 3 2 75 75 LEU C C 13 178.230 0.040 . 1 . . . . . . . . 5856 2 341 . 3 2 76 76 ALA H H 1 7.270 0.030 . 1 . . . . . . . . 5856 2 342 . 3 2 76 76 ALA N N 15 118.740 0.050 . 1 . . . . . . . . 5856 2 343 . 3 2 76 76 ALA CA C 13 52.110 0.020 . 1 . . . . . . . . 5856 2 344 . 3 2 76 76 ALA CB C 13 18.220 0.100 . 1 . . . . . . . . 5856 2 345 . 3 2 76 76 ALA C C 13 177.370 0.010 . 1 . . . . . . . . 5856 2 346 . 3 2 77 77 HIS H H 1 7.540 0.030 . 1 . . . . . . . . 5856 2 347 . 3 2 77 77 HIS N N 15 118.580 0.050 . 1 . . . . . . . . 5856 2 348 . 3 2 77 77 HIS CA C 13 54.020 0.020 . 1 . . . . . . . . 5856 2 349 . 3 2 77 77 HIS CB C 13 28.980 0.100 . 1 . . . . . . . . 5856 2 350 . 3 2 77 77 HIS C C 13 175.465 0.005 . 1 . . . . . . . . 5856 2 351 . 3 2 78 78 LEU H H 1 7.710 0.030 . 1 . . . . . . . . 5856 2 352 . 3 2 78 78 LEU N N 15 121.040 0.050 . 1 . . . . . . . . 5856 2 353 . 3 2 78 78 LEU CA C 13 57.565 0.025 . 1 . . . . . . . . 5856 2 354 . 3 2 78 78 LEU CB C 13 40.970 0.100 . 1 . . . . . . . . 5856 2 355 . 3 2 78 78 LEU C C 13 177.620 0.010 . 1 . . . . . . . . 5856 2 356 . 3 2 79 79 ASP H H 1 8.490 0.030 . 1 . . . . . . . . 5856 2 357 . 3 2 79 79 ASP N N 15 114.660 0.050 . 1 . . . . . . . . 5856 2 358 . 3 2 79 79 ASP CA C 13 53.665 0.015 . 1 . . . . . . . . 5856 2 359 . 3 2 79 79 ASP CB C 13 39.585 0.045 . 1 . . . . . . . . 5856 2 360 . 3 2 79 79 ASP C C 13 176.135 0.025 . 1 . . . . . . . . 5856 2 361 . 3 2 80 80 ASN H H 1 8.010 0.030 . 1 . . . . . . . . 5856 2 362 . 3 2 80 80 ASN N N 15 119.340 0.050 . 1 . . . . . . . . 5856 2 363 . 3 2 80 80 ASN CA C 13 51.470 0.100 . 1 . . . . . . . . 5856 2 364 . 3 2 80 80 ASN CB C 13 37.450 0.100 . 1 . . . . . . . . 5856 2 365 . 3 2 81 81 LEU H H 1 8.850 0.030 . 1 . . . . . . . . 5856 2 366 . 3 2 81 81 LEU N N 15 126.050 0.050 . 1 . . . . . . . . 5856 2 367 . 3 2 81 81 LEU CA C 13 57.940 0.010 . 1 . . . . . . . . 5856 2 368 . 3 2 81 81 LEU C C 13 179.050 0.100 . 1 . . . . . . . . 5856 2 369 . 3 2 82 82 LYS H H 1 8.600 0.030 . 1 . . . . . . . . 5856 2 370 . 3 2 82 82 LYS N N 15 118.690 0.050 . 1 . . . . . . . . 5856 2 371 . 3 2 82 82 LYS CA C 13 60.245 0.005 . 1 . . . . . . . . 5856 2 372 . 3 2 82 82 LYS CB C 13 30.480 0.100 . 1 . . . . . . . . 5856 2 373 . 3 2 82 82 LYS C C 13 178.790 0.010 . 1 . . . . . . . . 5856 2 374 . 3 2 83 83 GLY H H 1 7.440 0.030 . 1 . . . . . . . . 5856 2 375 . 3 2 83 83 GLY N N 15 104.110 0.050 . 1 . . . . . . . . 5856 2 376 . 3 2 83 83 GLY CA C 13 46.370 0.010 . 1 . . . . . . . . 5856 2 377 . 3 2 83 83 GLY C C 13 176.895 0.015 . 1 . . . . . . . . 5856 2 378 . 3 2 84 84 THR H H 1 7.500 0.030 . 1 . . . . . . . . 5856 2 379 . 3 2 84 84 THR N N 15 118.470 0.050 . 1 . . . . . . . . 5856 2 380 . 3 2 84 84 THR CA C 13 65.845 0.015 . 1 . . . . . . . . 5856 2 381 . 3 2 84 84 THR C C 13 175.720 0.100 . 1 . . . . . . . . 5856 2 382 . 3 2 85 85 PHE H H 1 7.630 0.030 . 1 . . . . . . . . 5856 2 383 . 3 2 85 85 PHE N N 15 115.850 0.050 . 1 . . . . . . . . 5856 2 384 . 3 2 85 85 PHE CA C 13 57.765 0.045 . 1 . . . . . . . . 5856 2 385 . 3 2 85 85 PHE CB C 13 37.650 0.100 . 1 . . . . . . . . 5856 2 386 . 3 2 85 85 PHE C C 13 174.880 0.000 . 1 . . . . . . . . 5856 2 387 . 3 2 86 86 ALA H H 1 7.020 0.030 . 1 . . . . . . . . 5856 2 388 . 3 2 86 86 ALA N N 15 125.020 0.050 . 1 . . . . . . . . 5856 2 389 . 3 2 86 86 ALA CA C 13 56.700 0.020 . 1 . . . . . . . . 5856 2 390 . 3 2 86 86 ALA CB C 13 17.530 0.100 . 1 . . . . . . . . 5856 2 391 . 3 2 86 86 ALA C C 13 180.050 0.000 . 1 . . . . . . . . 5856 2 392 . 3 2 87 87 THR H H 1 8.310 0.030 . 1 . . . . . . . . 5856 2 393 . 3 2 87 87 THR N N 15 114.460 0.050 . 1 . . . . . . . . 5856 2 394 . 3 2 87 87 THR CA C 13 65.600 0.020 . 1 . . . . . . . . 5856 2 395 . 3 2 87 87 THR C C 13 177.520 0.100 . 1 . . . . . . . . 5856 2 396 . 3 2 88 88 LEU H H 1 7.770 0.030 . 1 . . . . . . . . 5856 2 397 . 3 2 88 88 LEU N N 15 123.480 0.050 . 1 . . . . . . . . 5856 2 398 . 3 2 88 88 LEU CA C 13 56.180 0.000 . 1 . . . . . . . . 5856 2 399 . 3 2 88 88 LEU CB C 13 40.790 0.100 . 1 . . . . . . . . 5856 2 400 . 3 2 88 88 LEU C C 13 179.975 0.015 . 1 . . . . . . . . 5856 2 401 . 3 2 89 89 SER H H 1 8.900 0.030 . 1 . . . . . . . . 5856 2 402 . 3 2 89 89 SER N N 15 119.970 0.050 . 1 . . . . . . . . 5856 2 403 . 3 2 89 89 SER CA C 13 60.300 0.010 . 1 . . . . . . . . 5856 2 404 . 3 2 89 89 SER C C 13 176.610 0.100 . 1 . . . . . . . . 5856 2 405 . 3 2 90 90 GLU H H 1 7.460 0.030 . 1 . . . . . . . . 5856 2 406 . 3 2 90 90 GLU N N 15 120.170 0.050 . 1 . . . . . . . . 5856 2 407 . 3 2 90 90 GLU CA C 13 59.425 0.045 . 1 . . . . . . . . 5856 2 408 . 3 2 90 90 GLU CB C 13 28.100 0.100 . 1 . . . . . . . . 5856 2 409 . 3 2 90 90 GLU C C 13 178.060 0.010 . 1 . . . . . . . . 5856 2 410 . 3 2 91 91 LEU H H 1 7.140 0.030 . 1 . . . . . . . . 5856 2 411 . 3 2 91 91 LEU N N 15 117.450 0.050 . 1 . . . . . . . . 5856 2 412 . 3 2 91 91 LEU CA C 13 57.190 0.010 . 1 . . . . . . . . 5856 2 413 . 3 2 91 91 LEU C C 13 177.640 0.100 . 1 . . . . . . . . 5856 2 414 . 3 2 92 92 HIS H H 1 7.000 0.030 . 1 . . . . . . . . 5856 2 415 . 3 2 92 92 HIS N N 15 112.170 0.050 . 1 . . . . . . . . 5856 2 416 . 3 2 92 92 HIS CA C 13 59.935 0.035 . 1 . . . . . . . . 5856 2 417 . 3 2 92 92 HIS C C 13 174.070 0.000 . 1 . . . . . . . . 5856 2 418 . 3 2 93 93 CYS H H 1 7.810 0.030 . 1 . . . . . . . . 5856 2 419 . 3 2 93 93 CYS N N 15 115.000 0.050 . 1 . . . . . . . . 5856 2 420 . 3 2 93 93 CYS CA C 13 59.735 0.145 . 1 . . . . . . . . 5856 2 421 . 3 2 93 93 CYS C C 13 175.310 0.010 . 1 . . . . . . . . 5856 2 422 . 3 2 94 94 ASP H H 1 7.230 0.030 . 1 . . . . . . . . 5856 2 423 . 3 2 94 94 ASP N N 15 116.860 0.050 . 1 . . . . . . . . 5856 2 424 . 3 2 94 94 ASP CA C 13 56.020 0.000 . 1 . . . . . . . . 5856 2 425 . 3 2 94 94 ASP CB C 13 40.270 0.100 . 1 . . . . . . . . 5856 2 426 . 3 2 94 94 ASP C C 13 176.420 0.000 . 1 . . . . . . . . 5856 2 427 . 3 2 95 95 LYS H H 1 6.730 0.030 . 1 . . . . . . . . 5856 2 428 . 3 2 95 95 LYS N N 15 115.230 0.050 . 1 . . . . . . . . 5856 2 429 . 3 2 95 95 LYS CA C 13 56.875 0.035 . 1 . . . . . . . . 5856 2 430 . 3 2 95 95 LYS CB C 13 30.770 0.090 . 1 . . . . . . . . 5856 2 431 . 3 2 95 95 LYS C C 13 178.040 0.010 . 1 . . . . . . . . 5856 2 432 . 3 2 96 96 LEU H H 1 7.130 0.030 . 1 . . . . . . . . 5856 2 433 . 3 2 96 96 LEU N N 15 114.440 0.050 . 1 . . . . . . . . 5856 2 434 . 3 2 96 96 LEU CA C 13 54.690 0.010 . 1 . . . . . . . . 5856 2 435 . 3 2 96 96 LEU CB C 13 42.520 0.100 . 1 . . . . . . . . 5856 2 436 . 3 2 96 96 LEU C C 13 176.800 0.100 . 1 . . . . . . . . 5856 2 437 . 3 2 97 97 HIS H H 1 6.300 0.030 . 1 . . . . . . . . 5856 2 438 . 3 2 97 97 HIS N N 15 111.190 0.050 . 1 . . . . . . . . 5856 2 439 . 3 2 97 97 HIS CA C 13 55.760 0.010 . 1 . . . . . . . . 5856 2 440 . 3 2 97 97 HIS CB C 13 26.040 0.100 . 1 . . . . . . . . 5856 2 441 . 3 2 97 97 HIS C C 13 174.790 0.040 . 1 . . . . . . . . 5856 2 442 . 3 2 98 98 VAL H H 1 7.920 0.030 . 1 . . . . . . . . 5856 2 443 . 3 2 98 98 VAL N N 15 119.410 0.050 . 1 . . . . . . . . 5856 2 444 . 3 2 98 98 VAL CA C 13 62.020 0.110 . 1 . . . . . . . . 5856 2 445 . 3 2 98 98 VAL CB C 13 30.370 0.100 . 1 . . . . . . . . 5856 2 446 . 3 2 98 98 VAL C C 13 177.345 0.015 . 1 . . . . . . . . 5856 2 447 . 3 2 99 99 ASP H H 1 9.160 0.030 . 1 . . . . . . . . 5856 2 448 . 3 2 99 99 ASP N N 15 130.720 0.050 . 1 . . . . . . . . 5856 2 449 . 3 2 99 99 ASP CA C 13 53.740 0.100 . 1 . . . . . . . . 5856 2 450 . 3 2 99 99 ASP C C 13 177.220 0.100 . 1 . . . . . . . . 5856 2 451 . 3 2 100 100 PRO CA C 13 63.540 0.100 . 1 . . . . . . . . 5856 2 452 . 3 2 100 100 PRO C C 13 178.750 0.100 . 1 . . . . . . . . 5856 2 453 . 3 2 101 101 GLU H H 1 9.060 0.030 . 1 . . . . . . . . 5856 2 454 . 3 2 101 101 GLU N N 15 123.890 0.050 . 1 . . . . . . . . 5856 2 455 . 3 2 101 101 GLU CA C 13 58.825 0.015 . 1 . . . . . . . . 5856 2 456 . 3 2 101 101 GLU C C 13 179.785 0.015 . 1 . . . . . . . . 5856 2 457 . 3 2 102 102 ASN H H 1 8.120 0.030 . 1 . . . . . . . . 5856 2 458 . 3 2 102 102 ASN N N 15 112.380 0.050 . 1 . . . . . . . . 5856 2 459 . 3 2 102 102 ASN CA C 13 56.230 0.010 . 1 . . . . . . . . 5856 2 460 . 3 2 102 102 ASN CB C 13 39.900 0.100 . 1 . . . . . . . . 5856 2 461 . 3 2 102 102 ASN C C 13 177.810 0.040 . 1 . . . . . . . . 5856 2 462 . 3 2 103 103 PHE H H 1 7.550 0.030 . 1 . . . . . . . . 5856 2 463 . 3 2 103 103 PHE N N 15 118.150 0.050 . 1 . . . . . . . . 5856 2 464 . 3 2 103 103 PHE CA C 13 58.370 0.030 . 1 . . . . . . . . 5856 2 465 . 3 2 103 103 PHE C C 13 179.080 0.000 . 1 . . . . . . . . 5856 2 466 . 3 2 104 104 ARG H H 1 7.250 0.030 . 1 . . . . . . . . 5856 2 467 . 3 2 104 104 ARG N N 15 119.670 0.050 . 1 . . . . . . . . 5856 2 468 . 3 2 104 104 ARG CA C 13 58.660 0.100 . 1 . . . . . . . . 5856 2 469 . 3 2 104 104 ARG C C 13 177.890 0.100 . 1 . . . . . . . . 5856 2 470 . 3 2 105 105 LEU H H 1 7.870 0.030 . 1 . . . . . . . . 5856 2 471 . 3 2 105 105 LEU N N 15 118.580 0.050 . 1 . . . . . . . . 5856 2 472 . 3 2 105 105 LEU CA C 13 57.700 0.020 . 1 . . . . . . . . 5856 2 473 . 3 2 105 105 LEU CB C 13 39.500 0.100 . 1 . . . . . . . . 5856 2 474 . 3 2 105 105 LEU C C 13 179.330 0.100 . 1 . . . . . . . . 5856 2 475 . 3 2 106 106 LEU H H 1 8.180 0.030 . 1 . . . . . . . . 5856 2 476 . 3 2 106 106 LEU N N 15 118.370 0.050 . 1 . . . . . . . . 5856 2 477 . 3 2 106 106 LEU CA C 13 58.340 0.100 . 1 . . . . . . . . 5856 2 478 . 3 2 106 106 LEU CB C 13 39.400 0.100 . 1 . . . . . . . . 5856 2 479 . 3 2 106 106 LEU C C 13 178.585 0.055 . 1 . . . . . . . . 5856 2 480 . 3 2 107 107 GLY H H 1 8.070 0.030 . 1 . . . . . . . . 5856 2 481 . 3 2 107 107 GLY N N 15 105.480 0.050 . 1 . . . . . . . . 5856 2 482 . 3 2 107 107 GLY CA C 13 47.610 0.020 . 1 . . . . . . . . 5856 2 483 . 3 2 107 107 GLY C C 13 174.800 0.020 . 1 . . . . . . . . 5856 2 484 . 3 2 108 108 ASN H H 1 8.050 0.030 . 1 . . . . . . . . 5856 2 485 . 3 2 108 108 ASN N N 15 120.460 0.050 . 1 . . . . . . . . 5856 2 486 . 3 2 108 108 ASN CA C 13 54.790 0.020 . 1 . . . . . . . . 5856 2 487 . 3 2 108 108 ASN CB C 13 36.360 0.100 . 1 . . . . . . . . 5856 2 488 . 3 2 108 108 ASN C C 13 179.285 0.015 . 1 . . . . . . . . 5856 2 489 . 3 2 109 109 VAL H H 1 8.850 0.030 . 1 . . . . . . . . 5856 2 490 . 3 2 109 109 VAL N N 15 123.490 0.050 . 1 . . . . . . . . 5856 2 491 . 3 2 109 109 VAL CA C 13 67.495 0.015 . 1 . . . . . . . . 5856 2 492 . 3 2 109 109 VAL CB C 13 30.450 0.100 . 1 . . . . . . . . 5856 2 493 . 3 2 109 109 VAL C C 13 178.105 0.025 . 1 . . . . . . . . 5856 2 494 . 3 2 110 110 LEU H H 1 8.660 0.030 . 1 . . . . . . . . 5856 2 495 . 3 2 110 110 LEU N N 15 121.160 0.050 . 1 . . . . . . . . 5856 2 496 . 3 2 110 110 LEU CA C 13 58.320 0.010 . 1 . . . . . . . . 5856 2 497 . 3 2 110 110 LEU C C 13 179.190 0.100 . 1 . . . . . . . . 5856 2 498 . 3 2 111 111 VAL H H 1 7.880 0.030 . 1 . . . . . . . . 5856 2 499 . 3 2 111 111 VAL N N 15 118.610 0.050 . 1 . . . . . . . . 5856 2 500 . 3 2 111 111 VAL CA C 13 67.710 0.020 . 1 . . . . . . . . 5856 2 501 . 3 2 111 111 VAL CB C 13 30.500 0.100 . 1 . . . . . . . . 5856 2 502 . 3 2 111 111 VAL C C 13 176.840 0.040 . 1 . . . . . . . . 5856 2 503 . 3 2 112 112 CYS H H 1 7.980 0.030 . 1 . . . . . . . . 5856 2 504 . 3 2 112 112 CYS N N 15 117.340 0.050 . 1 . . . . . . . . 5856 2 505 . 3 2 112 112 CYS CA C 13 64.650 0.000 . 1 . . . . . . . . 5856 2 506 . 3 2 112 112 CYS C C 13 176.275 0.025 . 1 . . . . . . . . 5856 2 507 . 3 2 113 113 VAL H H 1 8.330 0.030 . 1 . . . . . . . . 5856 2 508 . 3 2 113 113 VAL N N 15 120.330 0.050 . 1 . . . . . . . . 5856 2 509 . 3 2 113 113 VAL CA C 13 66.020 0.100 . 1 . . . . . . . . 5856 2 510 . 3 2 113 113 VAL C C 13 177.675 0.015 . 1 . . . . . . . . 5856 2 511 . 3 2 114 114 LEU H H 1 8.300 0.030 . 1 . . . . . . . . 5856 2 512 . 3 2 114 114 LEU N N 15 121.110 0.050 . 1 . . . . . . . . 5856 2 513 . 3 2 114 114 LEU CA C 13 57.360 0.020 . 1 . . . . . . . . 5856 2 514 . 3 2 114 114 LEU C C 13 178.470 0.100 . 1 . . . . . . . . 5856 2 515 . 3 2 115 115 ALA H H 1 7.330 0.030 . 1 . . . . . . . . 5856 2 516 . 3 2 115 115 ALA N N 15 121.770 0.050 . 1 . . . . . . . . 5856 2 517 . 3 2 115 115 ALA CA C 13 54.485 0.035 . 1 . . . . . . . . 5856 2 518 . 3 2 115 115 ALA CB C 13 18.730 0.100 . 1 . . . . . . . . 5856 2 519 . 3 2 115 115 ALA C C 13 178.160 0.030 . 1 . . . . . . . . 5856 2 520 . 3 2 116 116 HIS H H 1 7.880 0.030 . 1 . . . . . . . . 5856 2 521 . 3 2 116 116 HIS N N 15 117.390 0.050 . 1 . . . . . . . . 5856 2 522 . 3 2 116 116 HIS CA C 13 57.405 0.025 . 1 . . . . . . . . 5856 2 523 . 3 2 116 116 HIS CB C 13 30.560 0.010 . 1 . . . . . . . . 5856 2 524 . 3 2 116 116 HIS C C 13 178.260 0.040 . 1 . . . . . . . . 5856 2 525 . 3 2 117 117 HIS H H 1 8.140 0.030 . 1 . . . . . . . . 5856 2 526 . 3 2 117 117 HIS N N 15 116.140 0.050 . 1 . . . . . . . . 5856 2 527 . 3 2 117 117 HIS CA C 13 58.620 0.010 . 1 . . . . . . . . 5856 2 528 . 3 2 117 117 HIS CB C 13 29.940 0.100 . 1 . . . . . . . . 5856 2 529 . 3 2 117 117 HIS C C 13 177.150 0.040 . 1 . . . . . . . . 5856 2 530 . 3 2 118 118 PHE H H 1 8.290 0.030 . 1 . . . . . . . . 5856 2 531 . 3 2 118 118 PHE N N 15 114.810 0.050 . 1 . . . . . . . . 5856 2 532 . 3 2 118 118 PHE CA C 13 58.905 0.025 . 1 . . . . . . . . 5856 2 533 . 3 2 118 118 PHE CB C 13 38.920 0.010 . 1 . . . . . . . . 5856 2 534 . 3 2 118 118 PHE C C 13 177.415 0.055 . 1 . . . . . . . . 5856 2 535 . 3 2 119 119 GLY H H 1 8.440 0.030 . 1 . . . . . . . . 5856 2 536 . 3 2 119 119 GLY N N 15 114.050 0.050 . 1 . . . . . . . . 5856 2 537 . 3 2 119 119 GLY CA C 13 47.380 0.020 . 1 . . . . . . . . 5856 2 538 . 3 2 119 119 GLY C C 13 176.120 0.010 . 1 . . . . . . . . 5856 2 539 . 3 2 120 120 LYS H H 1 8.620 0.030 . 1 . . . . . . . . 5856 2 540 . 3 2 120 120 LYS N N 15 125.240 0.050 . 1 . . . . . . . . 5856 2 541 . 3 2 120 120 LYS CA C 13 57.565 0.025 . 1 . . . . . . . . 5856 2 542 . 3 2 120 120 LYS CB C 13 30.925 0.025 . 1 . . . . . . . . 5856 2 543 . 3 2 120 120 LYS C C 13 177.910 0.030 . 1 . . . . . . . . 5856 2 544 . 3 2 121 121 GLU H H 1 7.680 0.030 . 1 . . . . . . . . 5856 2 545 . 3 2 121 121 GLU N N 15 116.850 0.050 . 1 . . . . . . . . 5856 2 546 . 3 2 121 121 GLU CA C 13 57.065 0.045 . 1 . . . . . . . . 5856 2 547 . 3 2 121 121 GLU CB C 13 29.430 0.010 . 1 . . . . . . . . 5856 2 548 . 3 2 121 121 GLU C C 13 177.190 0.060 . 1 . . . . . . . . 5856 2 549 . 3 2 122 122 PHE H H 1 8.450 0.030 . 1 . . . . . . . . 5856 2 550 . 3 2 122 122 PHE N N 15 126.340 0.050 . 1 . . . . . . . . 5856 2 551 . 3 2 122 122 PHE CA C 13 56.290 0.020 . 1 . . . . . . . . 5856 2 552 . 3 2 122 122 PHE CB C 13 36.880 0.050 . 1 . . . . . . . . 5856 2 553 . 3 2 122 122 PHE C C 13 174.400 0.010 . 1 . . . . . . . . 5856 2 554 . 3 2 123 123 THR H H 1 7.040 0.030 . 1 . . . . . . . . 5856 2 555 . 3 2 123 123 THR N N 15 113.520 0.050 . 1 . . . . . . . . 5856 2 556 . 3 2 123 123 THR CA C 13 60.250 0.100 . 1 . . . . . . . . 5856 2 557 . 3 2 123 123 THR CB C 13 66.700 0.100 . 1 . . . . . . . . 5856 2 558 . 3 2 123 123 THR C C 13 172.970 0.100 . 1 . . . . . . . . 5856 2 559 . 3 2 125 125 PRO CA C 13 65.480 0.100 . 1 . . . . . . . . 5856 2 560 . 3 2 125 125 PRO CB C 13 30.370 0.100 . 1 . . . . . . . . 5856 2 561 . 3 2 125 125 PRO C C 13 179.800 0.100 . 1 . . . . . . . . 5856 2 562 . 3 2 126 126 VAL H H 1 6.830 0.030 . 1 . . . . . . . . 5856 2 563 . 3 2 126 126 VAL N N 15 121.150 0.050 . 1 . . . . . . . . 5856 2 564 . 3 2 126 126 VAL CA C 13 66.120 0.000 . 1 . . . . . . . . 5856 2 565 . 3 2 126 126 VAL CB C 13 30.285 0.085 . 1 . . . . . . . . 5856 2 566 . 3 2 126 126 VAL C C 13 177.855 0.025 . 1 . . . . . . . . 5856 2 567 . 3 2 127 127 GLN H H 1 8.220 0.030 . 1 . . . . . . . . 5856 2 568 . 3 2 127 127 GLN N N 15 119.850 0.050 . 1 . . . . . . . . 5856 2 569 . 3 2 127 127 GLN CA C 13 58.605 0.025 . 1 . . . . . . . . 5856 2 570 . 3 2 127 127 GLN CB C 13 24.980 0.030 . 1 . . . . . . . . 5856 2 571 . 3 2 127 127 GLN C C 13 177.800 0.020 . 1 . . . . . . . . 5856 2 572 . 3 2 128 128 ALA H H 1 8.040 0.030 . 1 . . . . . . . . 5856 2 573 . 3 2 128 128 ALA N N 15 121.660 0.050 . 1 . . . . . . . . 5856 2 574 . 3 2 128 128 ALA CA C 13 55.095 0.015 . 1 . . . . . . . . 5856 2 575 . 3 2 128 128 ALA CB C 13 16.920 0.100 . 1 . . . . . . . . 5856 2 576 . 3 2 128 128 ALA C C 13 179.795 0.025 . 1 . . . . . . . . 5856 2 577 . 3 2 129 129 ALA H H 1 7.170 0.030 . 1 . . . . . . . . 5856 2 578 . 3 2 129 129 ALA N N 15 120.010 0.050 . 1 . . . . . . . . 5856 2 579 . 3 2 129 129 ALA CA C 13 54.780 0.010 . 1 . . . . . . . . 5856 2 580 . 3 2 129 129 ALA CB C 13 17.470 0.100 . 1 . . . . . . . . 5856 2 581 . 3 2 129 129 ALA C C 13 179.495 0.005 . 1 . . . . . . . . 5856 2 582 . 3 2 130 130 TYR H H 1 8.180 0.030 . 1 . . . . . . . . 5856 2 583 . 3 2 130 130 TYR N N 15 116.300 0.050 . 1 . . . . . . . . 5856 2 584 . 3 2 130 130 TYR CA C 13 64.305 0.105 . 1 . . . . . . . . 5856 2 585 . 3 2 130 130 TYR C C 13 179.360 0.100 . 1 . . . . . . . . 5856 2 586 . 3 2 131 131 GLN H H 1 9.420 0.030 . 1 . . . . . . . . 5856 2 587 . 3 2 131 131 GLN N N 15 119.160 0.050 . 1 . . . . . . . . 5856 2 588 . 3 2 131 131 GLN CA C 13 57.780 0.060 . 1 . . . . . . . . 5856 2 589 . 3 2 131 131 GLN CB C 13 24.970 0.210 . 1 . . . . . . . . 5856 2 590 . 3 2 131 131 GLN C C 13 179.630 0.030 . 1 . . . . . . . . 5856 2 591 . 3 2 132 132 LYS H H 1 7.500 0.030 . 1 . . . . . . . . 5856 2 592 . 3 2 132 132 LYS N N 15 121.110 0.050 . 1 . . . . . . . . 5856 2 593 . 3 2 132 132 LYS CA C 13 59.810 0.020 . 1 . . . . . . . . 5856 2 594 . 3 2 132 132 LYS CB C 13 31.670 0.100 . 1 . . . . . . . . 5856 2 595 . 3 2 132 132 LYS C C 13 179.755 0.045 . 1 . . . . . . . . 5856 2 596 . 3 2 133 133 VAL H H 1 7.470 0.030 . 1 . . . . . . . . 5856 2 597 . 3 2 133 133 VAL N N 15 119.320 0.050 . 1 . . . . . . . . 5856 2 598 . 3 2 133 133 VAL CA C 13 67.000 0.020 . 1 . . . . . . . . 5856 2 599 . 3 2 133 133 VAL C C 13 177.990 0.080 . 1 . . . . . . . . 5856 2 600 . 3 2 134 134 VAL H H 1 9.010 0.030 . 1 . . . . . . . . 5856 2 601 . 3 2 134 134 VAL N N 15 113.810 0.050 . 1 . . . . . . . . 5856 2 602 . 3 2 134 134 VAL CA C 13 66.225 0.035 . 1 . . . . . . . . 5856 2 603 . 3 2 134 134 VAL CB C 13 30.460 0.100 . 1 . . . . . . . . 5856 2 604 . 3 2 134 134 VAL C C 13 179.050 0.000 . 1 . . . . . . . . 5856 2 605 . 3 2 135 135 ALA H H 1 8.010 0.030 . 1 . . . . . . . . 5856 2 606 . 3 2 135 135 ALA N N 15 124.680 0.050 . 1 . . . . . . . . 5856 2 607 . 3 2 135 135 ALA CA C 13 54.665 0.035 . 1 . . . . . . . . 5856 2 608 . 3 2 135 135 ALA CB C 13 17.450 0.100 . 1 . . . . . . . . 5856 2 609 . 3 2 135 135 ALA C C 13 180.095 0.045 . 1 . . . . . . . . 5856 2 610 . 3 2 136 136 GLY H H 1 7.930 0.030 . 1 . . . . . . . . 5856 2 611 . 3 2 136 136 GLY N N 15 107.110 0.050 . 1 . . . . . . . . 5856 2 612 . 3 2 136 136 GLY CA C 13 46.640 0.010 . 1 . . . . . . . . 5856 2 613 . 3 2 136 136 GLY C C 13 177.150 0.010 . 1 . . . . . . . . 5856 2 614 . 3 2 137 137 VAL H H 1 8.580 0.030 . 1 . . . . . . . . 5856 2 615 . 3 2 137 137 VAL N N 15 124.370 0.050 . 1 . . . . . . . . 5856 2 616 . 3 2 137 137 VAL CA C 13 66.695 0.035 . 1 . . . . . . . . 5856 2 617 . 3 2 137 137 VAL C C 13 176.495 0.005 . 1 . . . . . . . . 5856 2 618 . 3 2 138 138 ALA H H 1 8.220 0.030 . 1 . . . . . . . . 5856 2 619 . 3 2 138 138 ALA N N 15 121.110 0.050 . 1 . . . . . . . . 5856 2 620 . 3 2 138 138 ALA CA C 13 55.440 0.010 . 1 . . . . . . . . 5856 2 621 . 3 2 138 138 ALA C C 13 179.195 0.025 . 1 . . . . . . . . 5856 2 622 . 3 2 139 139 ASN H H 1 8.160 0.030 . 1 . . . . . . . . 5856 2 623 . 3 2 139 139 ASN N N 15 114.960 0.050 . 1 . . . . . . . . 5856 2 624 . 3 2 139 139 ASN CA C 13 55.585 0.025 . 1 . . . . . . . . 5856 2 625 . 3 2 139 139 ASN C C 13 177.650 0.040 . 1 . . . . . . . . 5856 2 626 . 3 2 140 140 ALA H H 1 7.800 0.030 . 1 . . . . . . . . 5856 2 627 . 3 2 140 140 ALA N N 15 122.660 0.050 . 1 . . . . . . . . 5856 2 628 . 3 2 140 140 ALA CA C 13 54.155 0.045 . 1 . . . . . . . . 5856 2 629 . 3 2 140 140 ALA C C 13 180.395 0.045 . 1 . . . . . . . . 5856 2 630 . 3 2 141 141 LEU H H 1 8.030 0.030 . 1 . . . . . . . . 5856 2 631 . 3 2 141 141 LEU N N 15 120.520 0.050 . 1 . . . . . . . . 5856 2 632 . 3 2 141 141 LEU CA C 13 55.800 0.010 . 1 . . . . . . . . 5856 2 633 . 3 2 141 141 LEU C C 13 178.120 0.040 . 1 . . . . . . . . 5856 2 634 . 3 2 142 142 ALA H H 1 7.280 0.030 . 1 . . . . . . . . 5856 2 635 . 3 2 142 142 ALA N N 15 118.940 0.050 . 1 . . . . . . . . 5856 2 636 . 3 2 142 142 ALA CA C 13 51.710 0.130 . 1 . . . . . . . . 5856 2 637 . 3 2 142 142 ALA C C 13 177.670 0.040 . 1 . . . . . . . . 5856 2 638 . 3 2 143 143 HIS H H 1 7.050 0.030 . 1 . . . . . . . . 5856 2 639 . 3 2 143 143 HIS N N 15 118.400 0.050 . 1 . . . . . . . . 5856 2 640 . 3 2 143 143 HIS CA C 13 59.815 0.095 . 1 . . . . . . . . 5856 2 641 . 3 2 143 143 HIS CB C 13 25.770 0.100 . 1 . . . . . . . . 5856 2 642 . 3 2 143 143 HIS C C 13 176.965 0.005 . 1 . . . . . . . . 5856 2 643 . 3 2 144 144 LYS H H 1 7.040 0.030 . 1 . . . . . . . . 5856 2 644 . 3 2 144 144 LYS N N 15 115.620 0.050 . 1 . . . . . . . . 5856 2 645 . 3 2 144 144 LYS CA C 13 55.610 0.050 . 1 . . . . . . . . 5856 2 646 . 3 2 144 144 LYS C C 13 177.025 0.025 . 1 . . . . . . . . 5856 2 647 . 3 2 145 145 TYR H H 1 7.660 0.030 . 1 . . . . . . . . 5856 2 648 . 3 2 145 145 TYR N N 15 118.270 0.050 . 1 . . . . . . . . 5856 2 649 . 3 2 145 145 TYR CA C 13 58.355 0.045 . 1 . . . . . . . . 5856 2 650 . 3 2 145 145 TYR C C 13 175.910 0.030 . 1 . . . . . . . . 5856 2 651 . 3 2 146 146 HIS H H 1 7.410 0.030 . 1 . . . . . . . . 5856 2 652 . 3 2 146 146 HIS N N 15 124.460 0.050 . 1 . . . . . . . . 5856 2 653 . 3 2 146 146 HIS CA C 13 57.275 1.035 . 1 . . . . . . . . 5856 2 654 . 3 2 146 146 HIS C C 13 177.845 1.905 . 1 . . . . . . . . 5856 2 stop_ save_