data_15969 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15969 _Entry.Title ; Heteronuclear NMR assignments for the dimeric human hepatitis B virus core protein under capsid dissociating conditions ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-10-01 _Entry.Accession_date 2008-10-01 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.116 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details ; 13C, 15N, 1H chemical shifts of the dimeric human hepatitis B virus core protein (residues 1 - 149) acquired at 298 K and pH 9.5 ; _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 Stefan Freund . M.V. . 15969 2 Christopher Johnson . M. . 15969 3 Agnes Jaulent . . . 15969 4 Neil Ferguson . . . 15969 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID . . 'UCD Conway Institute of Biomolecular and Biomedical Research' . 15969 1 . 'MRC Centre for Protein Engineering' . 15969 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15969 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 327 15969 '15N chemical shifts' 97 15969 '1H chemical shifts' 100 15969 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 2 . . 2009-03-20 2008-10-01 update BMRB 'update entry citation' 15969 1 . . 2009-02-16 2008-10-01 original author 'original release' 15969 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1qgt 'Crystal structure of recombinant T= 4 capsid like particles formed by human hepatitis virus core protein (strain cw)' 15969 PDB 2g33 'Crystal structure of recombinant T= 4 capsid like particles formed by human hepatitis virus core protein (sub-type adyw)' 15969 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15969 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18952101 _Citation.Full_citation . _Citation.Title 'Moving towards high resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 384 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1301 _Citation.Page_last 1303 _Citation.Year 2008 _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 Stefan Freund . M.V. . 15969 1 2 Christopher Johnson . M. . 15969 1 3 Agnes Jaulent . . . 15969 1 4 Neil Ferguson . . . 15969 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID allostery 15969 1 anti-viral 15969 1 'hepatitis B virus' 15969 1 'shift mapping' 15969 1 TROSY 15969 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15969 _Assembly.ID 1 _Assembly.Name 'Hepatitis B core protein homodimer' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 33540 _Assembly.Enzyme_commission_number . _Assembly.Details ; Homodimer formed by the human hepatitis B core protein (residues 1-149). The deposited assignments correspond to a homodimer where each monomer is magnetically equivalent. In nature, this homodimer self-associates into a complex of 120 homodimers to give a virus capsid complex. In the capsid form, for which a crystal structure exists, each homodimer contains a disulphide linkage connecting Cys61 of each monomer. However, under the conditions of our study, we deliberately used thiol reductants to reduce thiol linkages. Thus, it is not clear whether the disulphide linkage is present under the conditions of our study, nor is there NMR evidence to support/refute this. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'Hepatitis B virus coat protein monomer, chain 1' 1 $Hepatitis_B_virus_coat_protein A . yes native no no 1 'Core protein homodimers associate to from capsid cores' . 15969 1 2 'Hepatitis B virus coat protein monomer, chain 2' 1 $Hepatitis_B_virus_coat_protein A . yes native no no 1 'Core protein homodimers associate to from capsid cores' . 15969 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 1qgt . . X-ray 3.3 'ecombinant capsid like particle formed by core protein (residues 1-149) from strain CW' . 15969 1 yes PDB 2g33 . . X-ray 3.96 'Recombinant capsid like particle formed by core protein sequence but with point mutations present' 'Residues C48, C61 and C107 were mutated to alanine in this study. An additional residue (cysteine 150) was added to this sequence' 15969 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Homodimer formed by coat protein monomers are basic building block of hepatitis B nucleocapsid cores' 15969 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Hepatitis_B_virus_coat_protein _Entity.Sf_category entity _Entity.Sf_framecode Hepatitis_B_virus_coat_protein _Entity.Entry_ID 15969 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Hepatitis_B_virus_coat_protein _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 ; MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTAAALYRD ALESPEHCSPHHTALRQAIL CWGDLMTLATWVGTNLEDPA SRDLVVSYVNTNVGLKFRQL LWFHISCLTFGRETVLEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details ; The dimeric hepatitis core protein assignments deposited here correspond to residues 1-149 of the full length (183 residues) core protein. The C-terminal nucleic acid binding domain (residues 150-183) was truncated to simplify spectral assignment. Residues 1-149 of the core protein contain all structured regions reported to date and can form recombinant capsid like particles essentially identical to nucleocapsids isolated from patients infected with hepatitis B virus. ; _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 149 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state unknown _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 33540 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The dimeric coat protein corresponds to residues 1-149 fragment originating from the full length human hepatitis B core protein (183 residues in untruncated form) ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 yes UNP P03147 . "core antigen" . . . . . . . . . . . . . . 15969 1 2 no PDB 2G33 . "Human Hepatitis B Virus T4 Capsid, Strain Adyw" . . . . . 100.00 150 97.99 97.99 2.81e-100 . . . . 15969 1 3 no PDB 2G34 . "Human Hepatitis B Virus T4 Capsid Strain Adyw Complexed With Assembly Effector Hap1" . . . . . 100.00 150 97.99 97.99 2.81e-100 . . . . 15969 1 4 no PDB 2QIJ . "Hepatitis B Capsid Protein With An N-Terminal Extension Modelled Into 8.9 A Data" . . . . . 97.99 157 100.00 100.00 2.14e-101 . . . . 15969 1 5 no PDB 3KXS . "Crystal Structure Of Hbv Capsid Mutant Dimer (Oxy Form), Strain Adyw" . . . . . 95.97 143 99.30 99.30 3.23e-98 . . . . 15969 1 6 no PDB 3V6Z . "Crystal Structure Of Hepatitis B Virus E-antigen" . . . . . 100.00 159 97.99 97.99 5.27e-100 . . . . 15969 1 7 no PDB 4BMG . "Crystal Structure Of Hexameric Hbc149 Y132a" . . . . . 100.00 154 99.33 99.33 2.57e-102 . . . . 15969 1 8 no PDB 4G93 . "Crystal Structure Of The Human Hepatitis B Virus T = 4 Capsid, Adyw Strain, In Complex With The Phenylpropenamide Assembly Acce" . . . . . 100.00 150 97.99 97.99 2.81e-100 . . . . 15969 1 9 no DBJ BAA85372 . "core [Hepatitis B virus]" . . . . . 100.00 183 97.32 100.00 5.56e-102 . . . . 15969 1 10 no DBJ BAA85376 . "precore/core [Hepatitis B virus]" . . . . . 100.00 212 98.66 100.00 3.67e-102 . . . . 15969 1 11 no EMBL CAA59662 . "core [Hepatitis B virus]" . . . . . 100.00 183 97.32 99.33 4.01e-102 . . . . 15969 1 12 no EMBL CAM58608 . "precore protein [Hepatitis B virus]" . . . . . 100.00 212 97.32 99.33 6.33e-101 . . . . 15969 1 13 no EMBL CAM58609 . "core protein [Hepatitis B virus]" . . . . . 100.00 183 97.32 99.33 6.34e-102 . . . . 15969 1 14 no EMBL CAM58712 . "core protein [Hepatitis B virus]" . . . . . 100.00 183 97.32 99.33 6.34e-102 . . . . 15969 1 15 no EMBL CAM58713 . "core protein [Hepatitis B virus]" . . . . . 100.00 183 97.32 99.33 6.34e-102 . . . . 15969 1 16 no GB AAA02846 . "precore protein, partial [Hepatitis B virus]" . . . . . 55.03 111 98.78 100.00 2.09e-50 . . . . 15969 1 17 no GB AAA02847 . "core protein, partial [Hepatitis B virus]" . . . . . 55.03 82 98.78 100.00 1.03e-50 . . . . 15969 1 18 no GB AAA45486 . "core antigen [Hepatitis B virus]" . . . . . 100.00 183 100.00 100.00 4.71e-104 . . . . 15969 1 19 no GB AAL31811 . "core protein [Hepatitis B virus]" . . . . . 100.00 183 98.66 100.00 4.98e-103 . . . . 15969 1 20 no GB AAL31812 . "core protein [Hepatitis B virus]" . . . . . 100.00 183 98.66 100.00 4.98e-103 . . . . 15969 1 21 no SP P03147 . "RecName: Full=Capsid protein; AltName: Full=Core antigen; AltName: Full=Core protein; AltName: Full=HBcAg; AltName: Full=p21.5" . . . . . 100.00 183 100.00 100.00 4.71e-104 . . . . 15969 1 22 no SP Q9QMI2 . "RecName: Full=Capsid protein; AltName: Full=Core antigen; AltName: Full=Core protein; AltName: Full=HBcAg; AltName: Full=p21.5" . . . . . 100.00 183 97.32 100.00 5.56e-102 . . . . 15969 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Viral capsid core protein' 15969 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 . MET . 15969 1 2 . ASP . 15969 1 3 . ILE . 15969 1 4 . ASP . 15969 1 5 . PRO . 15969 1 6 . TYR . 15969 1 7 . LYS . 15969 1 8 . GLU . 15969 1 9 . PHE . 15969 1 10 . GLY . 15969 1 11 . ALA . 15969 1 12 . THR . 15969 1 13 . VAL . 15969 1 14 . GLU . 15969 1 15 . LEU . 15969 1 16 . LEU . 15969 1 17 . SER . 15969 1 18 . PHE . 15969 1 19 . LEU . 15969 1 20 . PRO . 15969 1 21 . SER . 15969 1 22 . ASP . 15969 1 23 . PHE . 15969 1 24 . PHE . 15969 1 25 . PRO . 15969 1 26 . SER . 15969 1 27 . VAL . 15969 1 28 . ARG . 15969 1 29 . ASP . 15969 1 30 . LEU . 15969 1 31 . LEU . 15969 1 32 . ASP . 15969 1 33 . THR . 15969 1 34 . ALA . 15969 1 35 . ALA . 15969 1 36 . ALA . 15969 1 37 . LEU . 15969 1 38 . TYR . 15969 1 39 . ARG . 15969 1 40 . ASP . 15969 1 41 . ALA . 15969 1 42 . LEU . 15969 1 43 . GLU . 15969 1 44 . SER . 15969 1 45 . PRO . 15969 1 46 . GLU . 15969 1 47 . HIS . 15969 1 48 . CYS . 15969 1 49 . SER . 15969 1 50 . PRO . 15969 1 51 . HIS . 15969 1 52 . HIS . 15969 1 53 . THR . 15969 1 54 . ALA . 15969 1 55 . LEU . 15969 1 56 . ARG . 15969 1 57 . GLN . 15969 1 58 . ALA . 15969 1 59 . ILE . 15969 1 60 . LEU . 15969 1 61 . CYS . 15969 1 62 . TRP . 15969 1 63 . GLY . 15969 1 64 . ASP . 15969 1 65 . LEU . 15969 1 66 . MET . 15969 1 67 . THR . 15969 1 68 . LEU . 15969 1 69 . ALA . 15969 1 70 . THR . 15969 1 71 . TRP . 15969 1 72 . VAL . 15969 1 73 . GLY . 15969 1 74 . THR . 15969 1 75 . ASN . 15969 1 76 . LEU . 15969 1 77 . GLU . 15969 1 78 . ASP . 15969 1 79 . PRO . 15969 1 80 . ALA . 15969 1 81 . SER . 15969 1 82 . ARG . 15969 1 83 . ASP . 15969 1 84 . LEU . 15969 1 85 . VAL . 15969 1 86 . VAL . 15969 1 87 . SER . 15969 1 88 . TYR . 15969 1 89 . VAL . 15969 1 90 . ASN . 15969 1 91 . THR . 15969 1 92 . ASN . 15969 1 93 . VAL . 15969 1 94 . GLY . 15969 1 95 . LEU . 15969 1 96 . LYS . 15969 1 97 . PHE . 15969 1 98 . ARG . 15969 1 99 . GLN . 15969 1 100 . LEU . 15969 1 101 . LEU . 15969 1 102 . TRP . 15969 1 103 . PHE . 15969 1 104 . HIS . 15969 1 105 . ILE . 15969 1 106 . SER . 15969 1 107 . CYS . 15969 1 108 . LEU . 15969 1 109 . THR . 15969 1 110 . PHE . 15969 1 111 . GLY . 15969 1 112 . ARG . 15969 1 113 . GLU . 15969 1 114 . THR . 15969 1 115 . VAL . 15969 1 116 . LEU . 15969 1 117 . GLU . 15969 1 118 . TYR . 15969 1 119 . LEU . 15969 1 120 . VAL . 15969 1 121 . SER . 15969 1 122 . PHE . 15969 1 123 . GLY . 15969 1 124 . VAL . 15969 1 125 . TRP . 15969 1 126 . ILE . 15969 1 127 . ARG . 15969 1 128 . THR . 15969 1 129 . PRO . 15969 1 130 . PRO . 15969 1 131 . ALA . 15969 1 132 . TYR . 15969 1 133 . ARG . 15969 1 134 . PRO . 15969 1 135 . PRO . 15969 1 136 . ASN . 15969 1 137 . ALA . 15969 1 138 . PRO . 15969 1 139 . ILE . 15969 1 140 . LEU . 15969 1 141 . SER . 15969 1 142 . THR . 15969 1 143 . LEU . 15969 1 144 . PRO . 15969 1 145 . GLU . 15969 1 146 . THR . 15969 1 147 . THR . 15969 1 148 . VAL . 15969 1 149 . VAL . 15969 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 15969 1 . ASP 2 2 15969 1 . ILE 3 3 15969 1 . ASP 4 4 15969 1 . PRO 5 5 15969 1 . TYR 6 6 15969 1 . LYS 7 7 15969 1 . GLU 8 8 15969 1 . PHE 9 9 15969 1 . GLY 10 10 15969 1 . ALA 11 11 15969 1 . THR 12 12 15969 1 . VAL 13 13 15969 1 . GLU 14 14 15969 1 . LEU 15 15 15969 1 . LEU 16 16 15969 1 . SER 17 17 15969 1 . PHE 18 18 15969 1 . LEU 19 19 15969 1 . PRO 20 20 15969 1 . SER 21 21 15969 1 . ASP 22 22 15969 1 . PHE 23 23 15969 1 . PHE 24 24 15969 1 . PRO 25 25 15969 1 . SER 26 26 15969 1 . VAL 27 27 15969 1 . ARG 28 28 15969 1 . ASP 29 29 15969 1 . LEU 30 30 15969 1 . LEU 31 31 15969 1 . ASP 32 32 15969 1 . THR 33 33 15969 1 . ALA 34 34 15969 1 . ALA 35 35 15969 1 . ALA 36 36 15969 1 . LEU 37 37 15969 1 . TYR 38 38 15969 1 . ARG 39 39 15969 1 . ASP 40 40 15969 1 . ALA 41 41 15969 1 . LEU 42 42 15969 1 . GLU 43 43 15969 1 . SER 44 44 15969 1 . PRO 45 45 15969 1 . GLU 46 46 15969 1 . HIS 47 47 15969 1 . CYS 48 48 15969 1 . SER 49 49 15969 1 . PRO 50 50 15969 1 . HIS 51 51 15969 1 . HIS 52 52 15969 1 . THR 53 53 15969 1 . ALA 54 54 15969 1 . LEU 55 55 15969 1 . ARG 56 56 15969 1 . GLN 57 57 15969 1 . ALA 58 58 15969 1 . ILE 59 59 15969 1 . LEU 60 60 15969 1 . CYS 61 61 15969 1 . TRP 62 62 15969 1 . GLY 63 63 15969 1 . ASP 64 64 15969 1 . LEU 65 65 15969 1 . MET 66 66 15969 1 . THR 67 67 15969 1 . LEU 68 68 15969 1 . ALA 69 69 15969 1 . THR 70 70 15969 1 . TRP 71 71 15969 1 . VAL 72 72 15969 1 . GLY 73 73 15969 1 . THR 74 74 15969 1 . ASN 75 75 15969 1 . LEU 76 76 15969 1 . GLU 77 77 15969 1 . ASP 78 78 15969 1 . PRO 79 79 15969 1 . ALA 80 80 15969 1 . SER 81 81 15969 1 . ARG 82 82 15969 1 . ASP 83 83 15969 1 . LEU 84 84 15969 1 . VAL 85 85 15969 1 . VAL 86 86 15969 1 . SER 87 87 15969 1 . TYR 88 88 15969 1 . VAL 89 89 15969 1 . ASN 90 90 15969 1 . THR 91 91 15969 1 . ASN 92 92 15969 1 . VAL 93 93 15969 1 . GLY 94 94 15969 1 . LEU 95 95 15969 1 . LYS 96 96 15969 1 . PHE 97 97 15969 1 . ARG 98 98 15969 1 . GLN 99 99 15969 1 . LEU 100 100 15969 1 . LEU 101 101 15969 1 . TRP 102 102 15969 1 . PHE 103 103 15969 1 . HIS 104 104 15969 1 . ILE 105 105 15969 1 . SER 106 106 15969 1 . CYS 107 107 15969 1 . LEU 108 108 15969 1 . THR 109 109 15969 1 . PHE 110 110 15969 1 . GLY 111 111 15969 1 . ARG 112 112 15969 1 . GLU 113 113 15969 1 . THR 114 114 15969 1 . VAL 115 115 15969 1 . LEU 116 116 15969 1 . GLU 117 117 15969 1 . TYR 118 118 15969 1 . LEU 119 119 15969 1 . VAL 120 120 15969 1 . SER 121 121 15969 1 . PHE 122 122 15969 1 . GLY 123 123 15969 1 . VAL 124 124 15969 1 . TRP 125 125 15969 1 . ILE 126 126 15969 1 . ARG 127 127 15969 1 . THR 128 128 15969 1 . PRO 129 129 15969 1 . PRO 130 130 15969 1 . ALA 131 131 15969 1 . TYR 132 132 15969 1 . ARG 133 133 15969 1 . PRO 134 134 15969 1 . PRO 135 135 15969 1 . ASN 136 136 15969 1 . ALA 137 137 15969 1 . PRO 138 138 15969 1 . ILE 139 139 15969 1 . LEU 140 140 15969 1 . SER 141 141 15969 1 . THR 142 142 15969 1 . LEU 143 143 15969 1 . PRO 144 144 15969 1 . GLU 145 145 15969 1 . THR 146 146 15969 1 . THR 147 147 15969 1 . VAL 148 148 15969 1 . VAL 149 149 15969 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 15969 _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 $Hepatitis_B_virus_coat_protein . 10407 virus . 'Orthohepadnavirus Hepatitis B virus' 'Hepatitis B virus' . . Viruses . Orthohepadnavirus 'Hepatitis B virus' 'sub type adyw' . . . . . . . . . . . . . . . . . . . . 15969 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 15969 _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 $Hepatitis_B_virus_coat_protein . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 (de3)' . . . . . . . . . . . . . . . pT7-SC . . . . . . 15969 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15969 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Hepatitis B virus coat protein monomer, chain 1' '[U-13C; U-15N; U-2H]' . . 1 $Hepatitis_B_virus_coat_protein . . 150 . . uM 3 . . . 15969 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 15969 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' '< 30' . mM 15969 1 pH 9.5 . pH 15969 1 pressure 1 . atm 15969 1 temperature 298 . K 15969 1 stop_ save_ ############################ # Computer software used # ############################ save_Felix _Software.Sf_category software _Software.Sf_framecode Felix _Software.Entry_ID 15969 _Software.ID 1 _Software.Name FELIX _Software.Version 2004 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Accelrys . . 15969 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15969 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_AV700 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode AV700 _NMR_spectrometer.Entry_ID 15969 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_AV900 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode AV900 _NMR_spectrometer.Entry_ID 15969 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 15969 _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 AV700 Bruker Avance . 700 . . . 15969 1 2 AV900 Bruker Avance . 900 . . . 15969 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 15969 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N TROSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 2 '3D TROSY_HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 3 '3D TROSY-HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 4 '3D TROSY-HN(CA)CB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 5 '3D TROSY-HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 6 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $AV900 . . . . . . . . . . . . . . . . 15969 1 7 '3D TROSY-HN(COCA)CB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 8 '3D TROSY-HN(CA)CO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 9 '2D 1H-15N TROSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $AV900 . . . . . . . . . . . . . . . . 15969 1 10 '3D HN(CACO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AV700 . . . . . . . . . . . . . . . . 15969 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 15969 _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 water protons . . . . ppm 4.75 internal indirect 0.25144953 . . . . . . . . . 15969 1 H 1 water protons . . . . ppm 4.75 internal direct 1.0 . . . . . . . . . 15969 1 N 15 water protons . . . . ppm 4.75 internal indirect 0.101329118 . . . . . . . . . 15969 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 15969 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.05 _Assigned_chem_shift_list.Chem_shift_13C_err 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N TROSY' . . . 15969 1 stop_ loop_ _Systematic_chem_shift_offset.Type _Systematic_chem_shift_offset.Atom_type _Systematic_chem_shift_offset.Atom_isotope_number _Systematic_chem_shift_offset.Val _Systematic_chem_shift_offset.Val_err _Systematic_chem_shift_offset.Entry_ID _Systematic_chem_shift_offset.Assigned_chem_shift_list_ID corrected . . . . 15969 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $Felix . . 15969 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 MET C C 13 179.04 0.3 . 1 . . . . 1 MET C . 15969 1 2 . 1 1 1 1 MET CA C 13 56.31 0.3 . 1 . . . . 1 MET CA . 15969 1 3 . 1 1 1 1 MET CB C 13 37.31 0.3 . 1 . . . . 1 MET CB . 15969 1 4 . 1 1 2 2 ASP H H 1 9.461 0.05 . 1 . . . . 2 ASP H . 15969 1 5 . 1 1 2 2 ASP CA C 13 52.69 0.3 . 1 . . . . 2 ASP CA . 15969 1 6 . 1 1 2 2 ASP CB C 13 40.67 0.3 . 1 . . . . 2 ASP CB . 15969 1 7 . 1 1 2 2 ASP N N 15 128.274 0.3 . 1 . . . . 2 ASP N . 15969 1 8 . 1 1 3 3 ILE H H 1 7.886 0.05 . 1 . . . . 3 ILE H . 15969 1 9 . 1 1 3 3 ILE C C 13 174.53 0.3 . 1 . . . . 3 ILE C . 15969 1 10 . 1 1 3 3 ILE CA C 13 59.36 0.3 . 1 . . . . 3 ILE CA . 15969 1 11 . 1 1 3 3 ILE CB C 13 39.07 0.3 . 1 . . . . 3 ILE CB . 15969 1 12 . 1 1 3 3 ILE N N 15 123.332 0.3 . 1 . . . . 3 ILE N . 15969 1 13 . 1 1 4 4 ASP H H 1 9.436 0.05 . 1 . . . . 4 ASP H . 15969 1 14 . 1 1 4 4 ASP CA C 13 49.73 0.3 . 1 . . . . 4 ASP CA . 15969 1 15 . 1 1 4 4 ASP CB C 13 42.4 0.3 . 1 . . . . 4 ASP CB . 15969 1 16 . 1 1 4 4 ASP N N 15 131.086 0.3 . 1 . . . . 4 ASP N . 15969 1 17 . 1 1 5 5 PRO C C 13 177.19 0.3 . 1 . . . . 5 PRO C . 15969 1 18 . 1 1 5 5 PRO CA C 13 63.19 0.3 . 1 . . . . 5 PRO CA . 15969 1 19 . 1 1 5 5 PRO CB C 13 30.72 0.3 . 1 . . . . 5 PRO CB . 15969 1 20 . 1 1 6 6 TYR H H 1 9.162 0.05 . 1 . . . . 6 TYR H . 15969 1 21 . 1 1 6 6 TYR C C 13 178.19 0.3 . 1 . . . . 6 TYR C . 15969 1 22 . 1 1 6 6 TYR CA C 13 59.12 0.3 . 1 . . . . 6 TYR CA . 15969 1 23 . 1 1 6 6 TYR CB C 13 37.7 0.3 . 1 . . . . 6 TYR CB . 15969 1 24 . 1 1 6 6 TYR N N 15 117.926 0.3 . 1 . . . . 6 TYR N . 15969 1 25 . 1 1 7 7 LYS H H 1 7.484 0.05 . 1 . . . . 7 LYS H . 15969 1 26 . 1 1 7 7 LYS C C 13 180.88 0.3 . 1 . . . . 7 LYS C . 15969 1 27 . 1 1 7 7 LYS CA C 13 60.07 0.3 . 1 . . . . 7 LYS CA . 15969 1 28 . 1 1 7 7 LYS CB C 13 32.14 0.3 . 1 . . . . 7 LYS CB . 15969 1 29 . 1 1 7 7 LYS N N 15 125.693 0.3 . 1 . . . . 7 LYS N . 15969 1 30 . 1 1 9 9 PHE C C 13 174.45 0.3 . 1 . . . . 9 PHE C . 15969 1 31 . 1 1 9 9 PHE CA C 13 57.39 0.3 . 1 . . . . 9 PHE CA . 15969 1 32 . 1 1 9 9 PHE CB C 13 40.55 0.3 . 1 . . . . 9 PHE CB . 15969 1 33 . 1 1 10 10 GLY H H 1 7.560 0.05 . 1 . . . . 10 GLY H . 15969 1 34 . 1 1 10 10 GLY C C 13 173.65 0.3 . 1 . . . . 10 GLY C . 15969 1 35 . 1 1 10 10 GLY CA C 13 45.34 0.3 . 1 . . . . 10 GLY CA . 15969 1 36 . 1 1 10 10 GLY N N 15 103.764 0.3 . 1 . . . . 10 GLY N . 15969 1 37 . 1 1 11 11 ALA H H 1 7.641 0.05 . 1 . . . . 11 ALA H . 15969 1 38 . 1 1 11 11 ALA C C 13 173.46 0.3 . 1 . . . . 11 ALA C . 15969 1 39 . 1 1 11 11 ALA CA C 13 48.38 0.3 . 1 . . . . 11 ALA CA . 15969 1 40 . 1 1 11 11 ALA CB C 13 21.23 0.3 . 1 . . . . 11 ALA CB . 15969 1 41 . 1 1 11 11 ALA N N 15 121.378 0.3 . 1 . . . . 11 ALA N . 15969 1 42 . 1 1 12 12 THR H H 1 6.419 0.05 . 1 . . . . 12 THR H . 15969 1 43 . 1 1 12 12 THR C C 13 175 0.3 . 1 . . . . 12 THR C . 15969 1 44 . 1 1 12 12 THR CA C 13 58.85 0.3 . 1 . . . . 12 THR CA . 15969 1 45 . 1 1 12 12 THR CB C 13 73.9 0.3 . 1 . . . . 12 THR CB . 15969 1 46 . 1 1 12 12 THR N N 15 105.252 0.3 . 1 . . . . 12 THR N . 15969 1 47 . 1 1 13 13 VAL H H 1 10.407 0.05 . 1 . . . . 13 VAL H . 15969 1 48 . 1 1 13 13 VAL C C 13 178.93 0.3 . 1 . . . . 13 VAL C . 15969 1 49 . 1 1 13 13 VAL CA C 13 65.76 0.3 . 1 . . . . 13 VAL CA . 15969 1 50 . 1 1 13 13 VAL CB C 13 31.3 0.3 . 1 . . . . 13 VAL CB . 15969 1 51 . 1 1 13 13 VAL N N 15 123.148 0.3 . 1 . . . . 13 VAL N . 15969 1 52 . 1 1 14 14 GLU C C 13 178.81 0.3 . 1 . . . . 14 GLU C . 15969 1 53 . 1 1 14 14 GLU CA C 13 58.98 0.3 . 1 . . . . 14 GLU CA . 15969 1 54 . 1 1 14 14 GLU CB C 13 28.67 0.3 . 1 . . . . 14 GLU CB . 15969 1 55 . 1 1 15 15 LEU H H 1 7.736 0.05 . 1 . . . . 15 LEU H . 15969 1 56 . 1 1 15 15 LEU C C 13 178.7 0.3 . 1 . . . . 15 LEU C . 15969 1 57 . 1 1 15 15 LEU CA C 13 57.22 0.3 . 1 . . . . 15 LEU CA . 15969 1 58 . 1 1 15 15 LEU CB C 13 41.5 0.3 . 1 . . . . 15 LEU CB . 15969 1 59 . 1 1 15 15 LEU N N 15 120.375 0.3 . 1 . . . . 15 LEU N . 15969 1 60 . 1 1 16 16 LEU H H 1 6.816 0.05 . 1 . . . . 16 LEU H . 15969 1 61 . 1 1 16 16 LEU C C 13 179.16 0.3 . 1 . . . . 16 LEU C . 15969 1 62 . 1 1 16 16 LEU CA C 13 55.1 0.3 . 1 . . . . 16 LEU CA . 15969 1 63 . 1 1 16 16 LEU CB C 13 39.88 0.3 . 1 . . . . 16 LEU CB . 15969 1 64 . 1 1 16 16 LEU N N 15 119.000 0.3 . 1 . . . . 16 LEU N . 15969 1 65 . 1 1 17 17 SER H H 1 7.668 0.05 . 1 . . . . 17 SER H . 15969 1 66 . 1 1 17 17 SER C C 13 174.38 0.3 . 1 . . . . 17 SER C . 15969 1 67 . 1 1 17 17 SER CA C 13 60.39 0.3 . 1 . . . . 17 SER CA . 15969 1 68 . 1 1 17 17 SER CB C 13 62.72 0.3 . 1 . . . . 17 SER CB . 15969 1 69 . 1 1 17 17 SER N N 15 114.259 0.3 . 1 . . . . 17 SER N . 15969 1 70 . 1 1 18 18 PHE H H 1 6.815 0.05 . 1 . . . . 18 PHE H . 15969 1 71 . 1 1 18 18 PHE C C 13 176.38 0.3 . 1 . . . . 18 PHE C . 15969 1 72 . 1 1 18 18 PHE CA C 13 58.88 0.3 . 1 . . . . 18 PHE CA . 15969 1 73 . 1 1 18 18 PHE CB C 13 38.39 0.3 . 1 . . . . 18 PHE CB . 15969 1 74 . 1 1 18 18 PHE N N 15 118.085 0.3 . 1 . . . . 18 PHE N . 15969 1 75 . 1 1 19 19 LEU H H 1 6.986 0.05 . 1 . . . . 19 LEU H . 15969 1 76 . 1 1 19 19 LEU C C 13 174.5 0.3 . 1 . . . . 19 LEU C . 15969 1 77 . 1 1 19 19 LEU CA C 13 52.91 0.3 . 1 . . . . 19 LEU CA . 15969 1 78 . 1 1 19 19 LEU CB C 13 39.3 0.3 . 1 . . . . 19 LEU CB . 15969 1 79 . 1 1 19 19 LEU N N 15 120.312 0.3 . 1 . . . . 19 LEU N . 15969 1 80 . 1 1 21 21 SER C C 13 175.22 0.3 . 1 . . . . 21 SER C . 15969 1 81 . 1 1 21 21 SER CA C 13 62.9 0.3 . 1 . . . . 21 SER CA . 15969 1 82 . 1 1 21 21 SER CB C 13 69.68 0.3 . 1 . . . . 21 SER CB . 15969 1 83 . 1 1 22 22 ASP H H 1 7.490 0.05 . 1 . . . . 22 ASP H . 15969 1 84 . 1 1 22 22 ASP C C 13 174.3 0.3 . 1 . . . . 22 ASP C . 15969 1 85 . 1 1 22 22 ASP CA C 13 54.68 0.3 . 1 . . . . 22 ASP CA . 15969 1 86 . 1 1 22 22 ASP CB C 13 39.08 0.3 . 1 . . . . 22 ASP CB . 15969 1 87 . 1 1 22 22 ASP N N 15 117.192 0.3 . 1 . . . . 22 ASP N . 15969 1 88 . 1 1 23 23 PHE H H 1 7.527 0.05 . 1 . . . . 23 PHE H . 15969 1 89 . 1 1 23 23 PHE C C 13 176.64 0.3 . 1 . . . . 23 PHE C . 15969 1 90 . 1 1 23 23 PHE CA C 13 54.64 0.3 . 1 . . . . 23 PHE CA . 15969 1 91 . 1 1 23 23 PHE CB C 13 40.46 0.3 . 1 . . . . 23 PHE CB . 15969 1 92 . 1 1 23 23 PHE N N 15 119.546 0.3 . 1 . . . . 23 PHE N . 15969 1 93 . 1 1 25 25 PRO C C 13 174.78 0.3 . 1 . . . . 25 PRO C . 15969 1 94 . 1 1 25 25 PRO CA C 13 61.7 0.3 . 1 . . . . 25 PRO CA . 15969 1 95 . 1 1 25 25 PRO CB C 13 31.76 0.3 . 1 . . . . 25 PRO CB . 15969 1 96 . 1 1 26 26 SER H H 1 8.745 0.05 . 1 . . . . 26 SER H . 15969 1 97 . 1 1 26 26 SER C C 13 174.18 0.3 . 1 . . . . 26 SER C . 15969 1 98 . 1 1 26 26 SER CA C 13 57.2 0.3 . 1 . . . . 26 SER CA . 15969 1 99 . 1 1 26 26 SER CB C 13 64.05 0.3 . 1 . . . . 26 SER CB . 15969 1 100 . 1 1 26 26 SER N N 15 115.59 0.3 . 1 . . . . 26 SER N . 15969 1 101 . 1 1 27 27 VAL H H 1 8.695 0.05 . 1 . . . . 27 VAL H . 15969 1 102 . 1 1 27 27 VAL C C 13 177.41 0.3 . 1 . . . . 27 VAL C . 15969 1 103 . 1 1 27 27 VAL CA C 13 67.02 0.3 . 1 . . . . 27 VAL CA . 15969 1 104 . 1 1 27 27 VAL CB C 13 30.43 0.3 . 1 . . . . 27 VAL CB . 15969 1 105 . 1 1 27 27 VAL N N 15 120.748 0.3 . 1 . . . . 27 VAL N . 15969 1 106 . 1 1 28 28 ARG H H 1 8.078 0.05 . 1 . . . . 28 ARG H . 15969 1 107 . 1 1 28 28 ARG C C 13 178.01 0.3 . 1 . . . . 28 ARG C . 15969 1 108 . 1 1 28 28 ARG CA C 13 58.42 0.3 . 1 . . . . 28 ARG CA . 15969 1 109 . 1 1 28 28 ARG CB C 13 29.62 0.3 . 1 . . . . 28 ARG CB . 15969 1 110 . 1 1 28 28 ARG N N 15 118.378 0.3 . 1 . . . . 28 ARG N . 15969 1 111 . 1 1 29 29 ASP H H 1 7.743 0.05 . 1 . . . . 29 ASP H . 15969 1 112 . 1 1 29 29 ASP C C 13 179.72 0.3 . 1 . . . . 29 ASP C . 15969 1 113 . 1 1 29 29 ASP CA C 13 57.23 0.3 . 1 . . . . 29 ASP CA . 15969 1 114 . 1 1 29 29 ASP CB C 13 39.54 0.3 . 1 . . . . 29 ASP CB . 15969 1 115 . 1 1 29 29 ASP N N 15 119.647 0.3 . 1 . . . . 29 ASP N . 15969 1 116 . 1 1 30 30 LEU H H 1 8.126 0.05 . 1 . . . . 30 LEU H . 15969 1 117 . 1 1 30 30 LEU C C 13 178.9 0.3 . 1 . . . . 30 LEU C . 15969 1 118 . 1 1 30 30 LEU CA C 13 58.05 0.3 . 1 . . . . 30 LEU CA . 15969 1 119 . 1 1 30 30 LEU CB C 13 41.69 0.3 . 1 . . . . 30 LEU CB . 15969 1 120 . 1 1 30 30 LEU N N 15 123.049 0.3 . 1 . . . . 30 LEU N . 15969 1 121 . 1 1 31 31 LEU H H 1 8.803 0.05 . 1 . . . . 31 LEU H . 15969 1 122 . 1 1 31 31 LEU C C 13 180.47 0.3 . 1 . . . . 31 LEU C . 15969 1 123 . 1 1 31 31 LEU CA C 13 56.88 0.3 . 1 . . . . 31 LEU CA . 15969 1 124 . 1 1 31 31 LEU CB C 13 40.33 0.3 . 1 . . . . 31 LEU CB . 15969 1 125 . 1 1 31 31 LEU N N 15 120.445 0.3 . 1 . . . . 31 LEU N . 15969 1 126 . 1 1 32 32 ASP H H 1 8.436 0.05 . 1 . . . . 32 ASP H . 15969 1 127 . 1 1 32 32 ASP C C 13 179.76 0.3 . 1 . . . . 32 ASP C . 15969 1 128 . 1 1 32 32 ASP CA C 13 56.33 0.3 . 1 . . . . 32 ASP CA . 15969 1 129 . 1 1 32 32 ASP CB C 13 39.29 0.3 . 1 . . . . 32 ASP CB . 15969 1 130 . 1 1 32 32 ASP N N 15 121.567 0.3 . 1 . . . . 32 ASP N . 15969 1 131 . 1 1 33 33 THR H H 1 8.274 0.05 . 1 . . . . 33 THR H . 15969 1 132 . 1 1 33 33 THR C C 13 175.57 0.3 . 1 . . . . 33 THR C . 15969 1 133 . 1 1 33 33 THR CA C 13 66.73 0.3 . 1 . . . . 33 THR CA . 15969 1 134 . 1 1 33 33 THR CB C 13 67.99 0.3 . 1 . . . . 33 THR CB . 15969 1 135 . 1 1 33 33 THR N N 15 120.882 0.3 . 1 . . . . 33 THR N . 15969 1 136 . 1 1 34 34 ALA H H 1 8.667 0.05 . 1 . . . . 34 ALA H . 15969 1 137 . 1 1 34 34 ALA C C 13 178.93 0.3 . 1 . . . . 34 ALA C . 15969 1 138 . 1 1 34 34 ALA CA C 13 55.2 0.3 . 1 . . . . 34 ALA CA . 15969 1 139 . 1 1 34 34 ALA CB C 13 16.05 0.3 . 1 . . . . 34 ALA CB . 15969 1 140 . 1 1 34 34 ALA N N 15 123.066 0.3 . 1 . . . . 34 ALA N . 15969 1 141 . 1 1 35 35 ALA H H 1 8.028 0.05 . 1 . . . . 35 ALA H . 15969 1 142 . 1 1 35 35 ALA C C 13 179.32 0.3 . 1 . . . . 35 ALA C . 15969 1 143 . 1 1 35 35 ALA CA C 13 54.14 0.3 . 1 . . . . 35 ALA CA . 15969 1 144 . 1 1 35 35 ALA CB C 13 17.87 0.3 . 1 . . . . 35 ALA CB . 15969 1 145 . 1 1 35 35 ALA N N 15 117.980 0.3 . 1 . . . . 35 ALA N . 15969 1 146 . 1 1 36 36 ALA H H 1 8.102 0.05 . 1 . . . . 36 ALA H . 15969 1 147 . 1 1 36 36 ALA C C 13 179.99 0.3 . 1 . . . . 36 ALA C . 15969 1 148 . 1 1 36 36 ALA CA C 13 54.31 0.3 . 1 . . . . 36 ALA CA . 15969 1 149 . 1 1 36 36 ALA CB C 13 17.87 0.3 . 1 . . . . 36 ALA CB . 15969 1 150 . 1 1 36 36 ALA N N 15 120.619 0.3 . 1 . . . . 36 ALA N . 15969 1 151 . 1 1 37 37 LEU H H 1 7.861 0.05 . 1 . . . . 37 LEU H . 15969 1 152 . 1 1 37 37 LEU C C 13 179.36 0.3 . 1 . . . . 37 LEU C . 15969 1 153 . 1 1 37 37 LEU CA C 13 55.64 0.3 . 1 . . . . 37 LEU CA . 15969 1 154 . 1 1 37 37 LEU CB C 13 42.01 0.3 . 1 . . . . 37 LEU CB . 15969 1 155 . 1 1 37 37 LEU N N 15 113.596 0.3 . 1 . . . . 37 LEU N . 15969 1 156 . 1 1 38 38 TYR H H 1 7.735 0.05 . 1 . . . . 38 TYR H . 15969 1 157 . 1 1 38 38 TYR C C 13 176.23 0.3 . 1 . . . . 38 TYR C . 15969 1 158 . 1 1 38 38 TYR CA C 13 56.67 0.3 . 1 . . . . 38 TYR CA . 15969 1 159 . 1 1 38 38 TYR CB C 13 38.96 0.3 . 1 . . . . 38 TYR CB . 15969 1 160 . 1 1 38 38 TYR N N 15 113.763 0.3 . 1 . . . . 38 TYR N . 15969 1 161 . 1 1 39 39 ARG H H 1 7.535 0.05 . 1 . . . . 39 ARG H . 15969 1 162 . 1 1 39 39 ARG C C 13 177.02 0.3 . 1 . . . . 39 ARG C . 15969 1 163 . 1 1 39 39 ARG CA C 13 61.44 0.3 . 1 . . . . 39 ARG CA . 15969 1 164 . 1 1 39 39 ARG CB C 13 29.7 0.3 . 1 . . . . 39 ARG CB . 15969 1 165 . 1 1 39 39 ARG N N 15 121.806 0.3 . 1 . . . . 39 ARG N . 15969 1 166 . 1 1 41 41 ALA C C 13 181.84 0.3 . 1 . . . . 41 ALA C . 15969 1 167 . 1 1 41 41 ALA CA C 13 54.21 0.3 . 1 . . . . 41 ALA CA . 15969 1 168 . 1 1 41 41 ALA CB C 13 18.81 0.3 . 1 . . . . 41 ALA CB . 15969 1 169 . 1 1 42 42 LEU H H 1 9.145 0.05 . 1 . . . . 42 LEU H . 15969 1 170 . 1 1 42 42 LEU C C 13 179.81 0.3 . 1 . . . . 42 LEU C . 15969 1 171 . 1 1 42 42 LEU CA C 13 57.81 0.3 . 1 . . . . 42 LEU CA . 15969 1 172 . 1 1 42 42 LEU CB C 13 39.14 0.3 . 1 . . . . 42 LEU CB . 15969 1 173 . 1 1 42 42 LEU N N 15 119.081 0.3 . 1 . . . . 42 LEU N . 15969 1 174 . 1 1 43 43 GLU H H 1 8.455 0.05 . 1 . . . . 43 GLU H . 15969 1 175 . 1 1 43 43 GLU C C 13 175.11 0.3 . 1 . . . . 43 GLU C . 15969 1 176 . 1 1 43 43 GLU CA C 13 57.22 0.3 . 1 . . . . 43 GLU CA . 15969 1 177 . 1 1 43 43 GLU CB C 13 29.69 0.3 . 1 . . . . 43 GLU CB . 15969 1 178 . 1 1 43 43 GLU N N 15 118.648 0.3 . 1 . . . . 43 GLU N . 15969 1 179 . 1 1 44 44 SER H H 1 7.082 0.05 . 1 . . . . 44 SER H . 15969 1 180 . 1 1 44 44 SER C C 13 173.3 0.3 . 1 . . . . 44 SER C . 15969 1 181 . 1 1 44 44 SER CA C 13 57.42 0.3 . 1 . . . . 44 SER CA . 15969 1 182 . 1 1 44 44 SER CB C 13 63.44 0.3 . 1 . . . . 44 SER CB . 15969 1 183 . 1 1 44 44 SER N N 15 115.838 0.3 . 1 . . . . 44 SER N . 15969 1 184 . 1 1 50 50 PRO C C 13 179.25 0.3 . 1 . . . . 50 PRO C . 15969 1 185 . 1 1 50 50 PRO CA C 13 64.89 0.3 . 1 . . . . 50 PRO CA . 15969 1 186 . 1 1 51 51 HIS H H 1 7.312 0.05 . 1 . . . . 51 HIS H . 15969 1 187 . 1 1 51 51 HIS C C 13 177.41 0.3 . 1 . . . . 51 HIS C . 15969 1 188 . 1 1 51 51 HIS CA C 13 59.5 0.3 . 1 . . . . 51 HIS CA . 15969 1 189 . 1 1 51 51 HIS CB C 13 28.76 0.3 . 1 . . . . 51 HIS CB . 15969 1 190 . 1 1 51 51 HIS N N 15 112.910 0.3 . 1 . . . . 51 HIS N . 15969 1 191 . 1 1 52 52 HIS H H 1 7.919 0.05 . 1 . . . . 52 HIS H . 15969 1 192 . 1 1 52 52 HIS C C 13 177.88 0.3 . 1 . . . . 52 HIS C . 15969 1 193 . 1 1 52 52 HIS CA C 13 61.91 0.3 . 1 . . . . 52 HIS CA . 15969 1 194 . 1 1 52 52 HIS CB C 13 29.27 0.3 . 1 . . . . 52 HIS CB . 15969 1 195 . 1 1 52 52 HIS N N 15 119.591 0.3 . 1 . . . . 52 HIS N . 15969 1 196 . 1 1 53 53 THR H H 1 8.238 0.05 . 1 . . . . 53 THR H . 15969 1 197 . 1 1 53 53 THR CA C 13 66.69 0.3 . 1 . . . . 53 THR CA . 15969 1 198 . 1 1 53 53 THR CB C 13 68.3 0.3 . 1 . . . . 53 THR CB . 15969 1 199 . 1 1 53 53 THR N N 15 117.424 0.3 . 1 . . . . 53 THR N . 15969 1 200 . 1 1 54 54 ALA H H 1 8.187 0.05 . 1 . . . . 54 ALA H . 15969 1 201 . 1 1 54 54 ALA C C 13 179.07 0.3 . 1 . . . . 54 ALA C . 15969 1 202 . 1 1 54 54 ALA CA C 13 55.86 0.3 . 1 . . . . 54 ALA CA . 15969 1 203 . 1 1 54 54 ALA CB C 13 17.23 0.3 . 1 . . . . 54 ALA CB . 15969 1 204 . 1 1 54 54 ALA N N 15 122.235 0.3 . 1 . . . . 54 ALA N . 15969 1 205 . 1 1 55 55 LEU H H 1 8.203 0.05 . 1 . . . . 55 LEU H . 15969 1 206 . 1 1 55 55 LEU C C 13 178.44 0.3 . 1 . . . . 55 LEU C . 15969 1 207 . 1 1 55 55 LEU CA C 13 57.56 0.3 . 1 . . . . 55 LEU CA . 15969 1 208 . 1 1 55 55 LEU CB C 13 41.43 0.3 . 1 . . . . 55 LEU CB . 15969 1 209 . 1 1 55 55 LEU N N 15 119.627 0.3 . 1 . . . . 55 LEU N . 15969 1 210 . 1 1 56 56 ARG H H 1 8.558 0.05 . 1 . . . . 56 ARG H . 15969 1 211 . 1 1 56 56 ARG C C 13 177.54 0.3 . 1 . . . . 56 ARG C . 15969 1 212 . 1 1 56 56 ARG CA C 13 60.32 0.3 . 1 . . . . 56 ARG CA . 15969 1 213 . 1 1 56 56 ARG CB C 13 30.32 0.3 . 1 . . . . 56 ARG CB . 15969 1 214 . 1 1 56 56 ARG N N 15 117.051 0.3 . 1 . . . . 56 ARG N . 15969 1 215 . 1 1 57 57 GLN H H 1 7.196 0.05 . 1 . . . . 57 GLN H . 15969 1 216 . 1 1 57 57 GLN C C 13 179.28 0.3 . 1 . . . . 57 GLN C . 15969 1 217 . 1 1 57 57 GLN CA C 13 56.79 0.3 . 1 . . . . 57 GLN CA . 15969 1 218 . 1 1 58 58 ALA H H 1 8.449 0.05 . 1 . . . . 58 ALA H . 15969 1 219 . 1 1 58 58 ALA C C 13 179.51 0.3 . 1 . . . . 58 ALA C . 15969 1 220 . 1 1 58 58 ALA CA C 13 55.15 0.3 . 1 . . . . 58 ALA CA . 15969 1 221 . 1 1 58 58 ALA CB C 13 17.46 0.3 . 1 . . . . 58 ALA CB . 15969 1 222 . 1 1 58 58 ALA N N 15 123.232 0.3 . 1 . . . . 58 ALA N . 15969 1 223 . 1 1 59 59 ILE H H 1 8.523 0.05 . 1 . . . . 59 ILE H . 15969 1 224 . 1 1 59 59 ILE C C 13 179.37 0.3 . 1 . . . . 59 ILE C . 15969 1 225 . 1 1 59 59 ILE CA C 13 65.91 0.3 . 1 . . . . 59 ILE CA . 15969 1 226 . 1 1 59 59 ILE CB C 13 37.78 0.3 . 1 . . . . 59 ILE CB . 15969 1 227 . 1 1 59 59 ILE N N 15 118.539 0.3 . 1 . . . . 59 ILE N . 15969 1 228 . 1 1 60 60 LEU H H 1 7.688 0.05 . 1 . . . . 60 LEU H . 15969 1 229 . 1 1 60 60 LEU CA C 13 57.37 0.3 . 1 . . . . 60 LEU CA . 15969 1 230 . 1 1 60 60 LEU CB C 13 40.39 0.3 . 1 . . . . 60 LEU CB . 15969 1 231 . 1 1 60 60 LEU N N 15 121.030 0.3 . 1 . . . . 60 LEU N . 15969 1 232 . 1 1 61 61 CYS H H 1 8.755 0.05 . 1 . . . . 61 CYS H . 15969 1 233 . 1 1 61 61 CYS C C 13 176.58 0.3 . 1 . . . . 61 CYS C . 15969 1 234 . 1 1 61 61 CYS CA C 13 59.8 0.3 . 1 . . . . 61 CYS CA . 15969 1 235 . 1 1 61 61 CYS CB C 13 42.18 0.3 . 1 . . . . 61 CYS CB . 15969 1 236 . 1 1 61 61 CYS N N 15 121.982 0.3 . 1 . . . . 61 CYS N . 15969 1 237 . 1 1 62 62 TRP H H 1 8.415 0.05 . 1 . . . . 62 TRP H . 15969 1 238 . 1 1 62 62 TRP C C 13 177.72 0.3 . 1 . . . . 62 TRP C . 15969 1 239 . 1 1 62 62 TRP CA C 13 59.59 0.3 . 1 . . . . 62 TRP CA . 15969 1 240 . 1 1 62 62 TRP CB C 13 28.04 0.3 . 1 . . . . 62 TRP CB . 15969 1 241 . 1 1 62 62 TRP N N 15 119.193 0.3 . 1 . . . . 62 TRP N . 15969 1 242 . 1 1 63 63 GLY H H 1 8.051 0.05 . 1 . . . . 63 GLY H . 15969 1 243 . 1 1 63 63 GLY C C 13 177.06 0.3 . 1 . . . . 63 GLY C . 15969 1 244 . 1 1 63 63 GLY CA C 13 47.05 0.3 . 1 . . . . 63 GLY CA . 15969 1 245 . 1 1 63 63 GLY N N 15 104.569 0.3 . 1 . . . . 63 GLY N . 15969 1 246 . 1 1 64 64 ASP H H 1 8.171 0.05 . 1 . . . . 64 ASP H . 15969 1 247 . 1 1 64 64 ASP C C 13 179.83 0.3 . 1 . . . . 64 ASP C . 15969 1 248 . 1 1 64 64 ASP CA C 13 58.02 0.3 . 1 . . . . 64 ASP CA . 15969 1 249 . 1 1 64 64 ASP CB C 13 40.13 0.3 . 1 . . . . 64 ASP CB . 15969 1 250 . 1 1 64 64 ASP N N 15 125.074 0.3 . 1 . . . . 64 ASP N . 15969 1 251 . 1 1 65 65 LEU H H 1 8.136 0.05 . 1 . . . . 65 LEU H . 15969 1 252 . 1 1 65 65 LEU C C 13 178.52 0.3 . 1 . . . . 65 LEU C . 15969 1 253 . 1 1 65 65 LEU CA C 13 57.89 0.3 . 1 . . . . 65 LEU CA . 15969 1 254 . 1 1 65 65 LEU CB C 13 39.97 0.3 . 1 . . . . 65 LEU CB . 15969 1 255 . 1 1 65 65 LEU N N 15 124.609 0.3 . 1 . . . . 65 LEU N . 15969 1 256 . 1 1 66 66 MET H H 1 8.457 0.05 . 1 . . . . 66 MET H . 15969 1 257 . 1 1 66 66 MET C C 13 180.29 0.3 . 1 . . . . 66 MET C . 15969 1 258 . 1 1 66 66 MET CA C 13 56.32 0.3 . 1 . . . . 66 MET CA . 15969 1 259 . 1 1 66 66 MET N N 15 118.791 0.3 . 1 . . . . 66 MET N . 15969 1 260 . 1 1 67 67 THR H H 1 8.680 0.05 . 1 . . . . 67 THR H . 15969 1 261 . 1 1 67 67 THR CA C 13 66.73 0.3 . 1 . . . . 67 THR CA . 15969 1 262 . 1 1 67 67 THR CB C 13 67.85 0.3 . 1 . . . . 67 THR CB . 15969 1 263 . 1 1 67 67 THR N N 15 121.332 0.3 . 1 . . . . 67 THR N . 15969 1 264 . 1 1 68 68 LEU H H 1 7.907 0.05 . 1 . . . . 68 LEU H . 15969 1 265 . 1 1 68 68 LEU C C 13 178.03 0.3 . 1 . . . . 68 LEU C . 15969 1 266 . 1 1 68 68 LEU CA C 13 58.66 0.3 . 1 . . . . 68 LEU CA . 15969 1 267 . 1 1 68 68 LEU CB C 13 40.41 0.3 . 1 . . . . 68 LEU CB . 15969 1 268 . 1 1 68 68 LEU N N 15 124.876 0.3 . 1 . . . . 68 LEU N . 15969 1 269 . 1 1 69 69 ALA H H 1 8.464 0.05 . 1 . . . . 69 ALA H . 15969 1 270 . 1 1 69 69 ALA C C 13 180.2 0.3 . 1 . . . . 69 ALA C . 15969 1 271 . 1 1 69 69 ALA CA C 13 55.31 0.3 . 1 . . . . 69 ALA CA . 15969 1 272 . 1 1 69 69 ALA CB C 13 17.06 0.3 . 1 . . . . 69 ALA CB . 15969 1 273 . 1 1 69 69 ALA N N 15 122.041 0.3 . 1 . . . . 69 ALA N . 15969 1 274 . 1 1 70 70 THR H H 1 8.497 0.05 . 1 . . . . 70 THR H . 15969 1 275 . 1 1 70 70 THR C C 13 176.5 0.3 . 1 . . . . 70 THR C . 15969 1 276 . 1 1 70 70 THR CA C 13 65.99 0.3 . 1 . . . . 70 THR CA . 15969 1 277 . 1 1 70 70 THR CB C 13 68.47 0.3 . 1 . . . . 70 THR CB . 15969 1 278 . 1 1 70 70 THR N N 15 116.854 0.3 . 1 . . . . 70 THR N . 15969 1 279 . 1 1 71 71 TRP H H 1 8.748 0.05 . 1 . . . . 71 TRP H . 15969 1 280 . 1 1 71 71 TRP C C 13 180.27 0.3 . 1 . . . . 71 TRP C . 15969 1 281 . 1 1 71 71 TRP CA C 13 62.27 0.3 . 1 . . . . 71 TRP CA . 15969 1 282 . 1 1 71 71 TRP CB C 13 28 0.3 . 1 . . . . 71 TRP CB . 15969 1 283 . 1 1 71 71 TRP N N 15 126.853 0.3 . 1 . . . . 71 TRP N . 15969 1 284 . 1 1 72 72 VAL H H 1 8.956 0.05 . 1 . . . . 72 VAL H . 15969 1 285 . 1 1 72 72 VAL C C 13 177.42 0.3 . 1 . . . . 72 VAL C . 15969 1 286 . 1 1 72 72 VAL CA C 13 65.75 0.3 . 1 . . . . 72 VAL CA . 15969 1 287 . 1 1 72 72 VAL CB C 13 30.76 0.3 . 1 . . . . 72 VAL CB . 15969 1 288 . 1 1 72 72 VAL N N 15 119.100 0.3 . 1 . . . . 72 VAL N . 15969 1 289 . 1 1 73 73 GLY H H 1 7.707 0.05 . 1 . . . . 73 GLY H . 15969 1 290 . 1 1 73 73 GLY C C 13 174.81 0.3 . 1 . . . . 73 GLY C . 15969 1 291 . 1 1 73 73 GLY CA C 13 46.45 0.3 . 1 . . . . 73 GLY CA . 15969 1 292 . 1 1 73 73 GLY N N 15 104.816 0.3 . 1 . . . . 73 GLY N . 15969 1 293 . 1 1 75 75 ASN H H 1 7.828 0.05 . 1 . . . . 75 ASN H . 15969 1 294 . 1 1 75 75 ASN C C 13 175.97 0.3 . 1 . . . . 75 ASN C . 15969 1 295 . 1 1 75 75 ASN CA C 13 58.94 0.3 . 1 . . . . 75 ASN CA . 15969 1 296 . 1 1 75 75 ASN CB C 13 38.63 0.3 . 1 . . . . 75 ASN CB . 15969 1 297 . 1 1 76 76 LEU H H 1 6.676 0.05 . 1 . . . . 76 LEU H . 15969 1 298 . 1 1 76 76 LEU C C 13 174.51 0.3 . 1 . . . . 76 LEU C . 15969 1 299 . 1 1 76 76 LEU CA C 13 55.91 0.3 . 1 . . . . 76 LEU CA . 15969 1 300 . 1 1 76 76 LEU CB C 13 38.48 0.3 . 1 . . . . 76 LEU CB . 15969 1 301 . 1 1 76 76 LEU N N 15 115.387 0.3 . 1 . . . . 76 LEU N . 15969 1 302 . 1 1 80 80 ALA C C 13 181.07 0.3 . 1 . . . . 80 ALA C . 15969 1 303 . 1 1 80 80 ALA CA C 13 54.61 0.3 . 1 . . . . 80 ALA CA . 15969 1 304 . 1 1 80 80 ALA CB C 13 17.52 0.3 . 1 . . . . 80 ALA CB . 15969 1 305 . 1 1 81 81 SER H H 1 7.758 0.05 . 1 . . . . 81 SER H . 15969 1 306 . 1 1 81 81 SER C C 13 180 0.3 . 1 . . . . 81 SER C . 15969 1 307 . 1 1 81 81 SER CA C 13 62.06 0.3 . 1 . . . . 81 SER CA . 15969 1 308 . 1 1 81 81 SER CB C 13 62.74 0.3 . 1 . . . . 81 SER CB . 15969 1 309 . 1 1 81 81 SER N N 15 115.109 0.3 . 1 . . . . 81 SER N . 15969 1 310 . 1 1 83 83 ASP C C 13 179.38 0.3 . 1 . . . . 83 ASP C . 15969 1 311 . 1 1 83 83 ASP CA C 13 56.76 0.3 . 1 . . . . 83 ASP CA . 15969 1 312 . 1 1 83 83 ASP CB C 13 39.7 0.3 . 1 . . . . 83 ASP CB . 15969 1 313 . 1 1 84 84 LEU H H 1 8.021 0.05 . 1 . . . . 84 LEU H . 15969 1 314 . 1 1 84 84 LEU C C 13 179.85 0.3 . 1 . . . . 84 LEU C . 15969 1 315 . 1 1 84 84 LEU CA C 13 58.01 0.3 . 1 . . . . 84 LEU CA . 15969 1 316 . 1 1 84 84 LEU CB C 13 42 0.3 . 1 . . . . 84 LEU CB . 15969 1 317 . 1 1 84 84 LEU N N 15 121.615 0.3 . 1 . . . . 84 LEU N . 15969 1 318 . 1 1 85 85 VAL H H 1 7.879 0.05 . 1 . . . . 85 VAL H . 15969 1 319 . 1 1 85 85 VAL C C 13 177.35 0.3 . 1 . . . . 85 VAL C . 15969 1 320 . 1 1 85 85 VAL CA C 13 66.41 0.3 . 1 . . . . 85 VAL CA . 15969 1 321 . 1 1 85 85 VAL CB C 13 30.99 0.3 . 1 . . . . 85 VAL CB . 15969 1 322 . 1 1 85 85 VAL N N 15 118.404 0.3 . 1 . . . . 85 VAL N . 15969 1 323 . 1 1 86 86 VAL H H 1 8.176 0.05 . 1 . . . . 86 VAL H . 15969 1 324 . 1 1 86 86 VAL C C 13 178.61 0.3 . 1 . . . . 86 VAL C . 15969 1 325 . 1 1 86 86 VAL CA C 13 67.27 0.3 . 1 . . . . 86 VAL CA . 15969 1 326 . 1 1 86 86 VAL N N 15 119.846 0.3 . 1 . . . . 86 VAL N . 15969 1 327 . 1 1 87 87 SER H H 1 8.320 0.05 . 1 . . . . 87 SER H . 15969 1 328 . 1 1 87 87 SER CA C 13 61.37 0.3 . 1 . . . . 87 SER CA . 15969 1 329 . 1 1 87 87 SER CB C 13 62.38 0.3 . 1 . . . . 87 SER CB . 15969 1 330 . 1 1 87 87 SER N N 15 114.606 0.3 . 1 . . . . 87 SER N . 15969 1 331 . 1 1 88 88 TYR H H 1 7.972 0.05 . 1 . . . . 88 TYR H . 15969 1 332 . 1 1 88 88 TYR C C 13 178.39 0.3 . 1 . . . . 88 TYR C . 15969 1 333 . 1 1 88 88 TYR CA C 13 61.32 0.3 . 1 . . . . 88 TYR CA . 15969 1 334 . 1 1 88 88 TYR CB C 13 37.17 0.3 . 1 . . . . 88 TYR CB . 15969 1 335 . 1 1 88 88 TYR N N 15 124.866 0.3 . 1 . . . . 88 TYR N . 15969 1 336 . 1 1 89 89 VAL H H 1 8.141 0.05 . 1 . . . . 89 VAL H . 15969 1 337 . 1 1 89 89 VAL C C 13 177.29 0.3 . 1 . . . . 89 VAL C . 15969 1 338 . 1 1 89 89 VAL CA C 13 66.38 0.3 . 1 . . . . 89 VAL CA . 15969 1 339 . 1 1 89 89 VAL CB C 13 30.92 0.3 . 1 . . . . 89 VAL CB . 15969 1 340 . 1 1 89 89 VAL N N 15 119.224 0.3 . 1 . . . . 89 VAL N . 15969 1 341 . 1 1 93 93 VAL H H 1 7.579 0.05 . 1 . . . . 93 VAL H . 15969 1 342 . 1 1 93 93 VAL C C 13 175.77 0.3 . 1 . . . . 93 VAL C . 15969 1 343 . 1 1 93 93 VAL CA C 13 64.32 0.3 . 1 . . . . 93 VAL CA . 15969 1 344 . 1 1 93 93 VAL CB C 13 30.65 0.3 . 1 . . . . 93 VAL CB . 15969 1 345 . 1 1 93 93 VAL N N 15 119.019 0.3 . 1 . . . . 93 VAL N . 15969 1 346 . 1 1 94 94 GLY H H 1 7.976 0.05 . 1 . . . . 94 GLY H . 15969 1 347 . 1 1 94 94 GLY C C 13 175.59 0.3 . 1 . . . . 94 GLY C . 15969 1 348 . 1 1 94 94 GLY CA C 13 47.76 0.3 . 1 . . . . 94 GLY CA . 15969 1 349 . 1 1 94 94 GLY N N 15 106.594 0.3 . 1 . . . . 94 GLY N . 15969 1 350 . 1 1 95 95 LEU C C 13 177.97 0.3 . 1 . . . . 95 LEU C . 15969 1 351 . 1 1 95 95 LEU CA C 13 58.24 0.3 . 1 . . . . 95 LEU CA . 15969 1 352 . 1 1 95 95 LEU CB C 13 39.8 0.3 . 1 . . . . 95 LEU CB . 15969 1 353 . 1 1 96 96 LYS H H 1 7.299 0.05 . 1 . . . . 96 LYS H . 15969 1 354 . 1 1 96 96 LYS C C 13 179.86 0.3 . 1 . . . . 96 LYS C . 15969 1 355 . 1 1 96 96 LYS CA C 13 58.7 0.3 . 1 . . . . 96 LYS CA . 15969 1 356 . 1 1 96 96 LYS CB C 13 30.21 0.3 . 1 . . . . 96 LYS CB . 15969 1 357 . 1 1 96 96 LYS N N 15 117.492 0.3 . 1 . . . . 96 LYS N . 15969 1 358 . 1 1 97 97 PHE H H 1 7.668 0.05 . 1 . . . . 97 PHE H . 15969 1 359 . 1 1 97 97 PHE C C 13 177.39 0.3 . 1 . . . . 97 PHE C . 15969 1 360 . 1 1 97 97 PHE CA C 13 62.57 0.3 . 1 . . . . 97 PHE CA . 15969 1 361 . 1 1 97 97 PHE CB C 13 38.93 0.3 . 1 . . . . 97 PHE CB . 15969 1 362 . 1 1 97 97 PHE N N 15 117.825 0.3 . 1 . . . . 97 PHE N . 15969 1 363 . 1 1 98 98 ARG C C 13 177.66 0.3 . 1 . . . . 98 ARG C . 15969 1 364 . 1 1 98 98 ARG CA C 13 59.43 0.3 . 1 . . . . 98 ARG CA . 15969 1 365 . 1 1 98 98 ARG CB C 13 29.59 0.3 . 1 . . . . 98 ARG CB . 15969 1 366 . 1 1 99 99 GLN H H 1 7.358 0.05 . 1 . . . . 99 GLN H . 15969 1 367 . 1 1 99 99 GLN C C 13 177.08 0.3 . 1 . . . . 99 GLN C . 15969 1 368 . 1 1 99 99 GLN CA C 13 58.47 0.3 . 1 . . . . 99 GLN CA . 15969 1 369 . 1 1 99 99 GLN CB C 13 27.62 0.3 . 1 . . . . 99 GLN CB . 15969 1 370 . 1 1 100 100 LEU H H 1 7.326 0.05 . 1 . . . . 100 LEU H . 15969 1 371 . 1 1 100 100 LEU C C 13 179.61 0.3 . 1 . . . . 100 LEU C . 15969 1 372 . 1 1 100 100 LEU CA C 13 58.22 0.3 . 1 . . . . 100 LEU CA . 15969 1 373 . 1 1 100 100 LEU CB C 13 43.52 0.3 . 1 . . . . 100 LEU CB . 15969 1 374 . 1 1 100 100 LEU N N 15 119.998 0.3 . 1 . . . . 100 LEU N . 15969 1 375 . 1 1 101 101 LEU H H 1 8.838 0.05 . 1 . . . . 101 LEU H . 15969 1 376 . 1 1 101 101 LEU C C 13 178.88 0.3 . 1 . . . . 101 LEU C . 15969 1 377 . 1 1 101 101 LEU CA C 13 58.06 0.3 . 1 . . . . 101 LEU CA . 15969 1 378 . 1 1 101 101 LEU CB C 13 41.62 0.3 . 1 . . . . 101 LEU CB . 15969 1 379 . 1 1 101 101 LEU N N 15 117.329 0.3 . 1 . . . . 101 LEU N . 15969 1 380 . 1 1 102 102 TRP H H 1 8.402 0.05 . 1 . . . . 102 TRP H . 15969 1 381 . 1 1 102 102 TRP C C 13 179.08 0.3 . 1 . . . . 102 TRP C . 15969 1 382 . 1 1 102 102 TRP CA C 13 62.84 0.3 . 1 . . . . 102 TRP CA . 15969 1 383 . 1 1 102 102 TRP CB C 13 28.71 0.3 . 1 . . . . 102 TRP CB . 15969 1 384 . 1 1 102 102 TRP N N 15 118.549 0.3 . 1 . . . . 102 TRP N . 15969 1 385 . 1 1 103 103 PHE H H 1 9.196 0.05 . 1 . . . . 103 PHE H . 15969 1 386 . 1 1 103 103 PHE C C 13 177.18 0.3 . 1 . . . . 103 PHE C . 15969 1 387 . 1 1 103 103 PHE CA C 13 62.16 0.3 . 1 . . . . 103 PHE CA . 15969 1 388 . 1 1 103 103 PHE CB C 13 39.15 0.3 . 1 . . . . 103 PHE CB . 15969 1 389 . 1 1 103 103 PHE N N 15 122.655 0.3 . 1 . . . . 103 PHE N . 15969 1 390 . 1 1 104 104 HIS H H 1 8.064 0.05 . 1 . . . . 104 HIS H . 15969 1 391 . 1 1 104 104 HIS C C 13 178 0.3 . 1 . . . . 104 HIS C . 15969 1 392 . 1 1 104 104 HIS CA C 13 61.1 0.3 . 1 . . . . 104 HIS CA . 15969 1 393 . 1 1 104 104 HIS CB C 13 31.83 0.3 . 1 . . . . 104 HIS CB . 15969 1 394 . 1 1 104 104 HIS N N 15 118.280 0.3 . 1 . . . . 104 HIS N . 15969 1 395 . 1 1 105 105 ILE H H 1 8.596 0.05 . 1 . . . . 105 ILE H . 15969 1 396 . 1 1 105 105 ILE C C 13 178.87 0.3 . 1 . . . . 105 ILE C . 15969 1 397 . 1 1 105 105 ILE CA C 13 65.47 0.3 . 1 . . . . 105 ILE CA . 15969 1 398 . 1 1 105 105 ILE CB C 13 37.15 0.3 . 1 . . . . 105 ILE CB . 15969 1 399 . 1 1 105 105 ILE N N 15 118.720 0.3 . 1 . . . . 105 ILE N . 15969 1 400 . 1 1 106 106 SER H H 1 8.290 0.05 . 1 . . . . 106 SER H . 15969 1 401 . 1 1 106 106 SER CA C 13 61.81 0.3 . 1 . . . . 106 SER CA . 15969 1 402 . 1 1 106 106 SER CB C 13 61.14 0.3 . 1 . . . . 106 SER CB . 15969 1 403 . 1 1 106 106 SER N N 15 117.520 0.3 . 1 . . . . 106 SER N . 15969 1 404 . 1 1 107 107 CYS H H 1 7.915 0.05 . 1 . . . . 107 CYS H . 15969 1 405 . 1 1 107 107 CYS C C 13 177.83 0.3 . 1 . . . . 107 CYS C . 15969 1 406 . 1 1 107 107 CYS CA C 13 63.98 0.3 . 1 . . . . 107 CYS CA . 15969 1 407 . 1 1 107 107 CYS CB C 13 25.44 0.3 . 1 . . . . 107 CYS CB . 15969 1 408 . 1 1 107 107 CYS N N 15 121.918 0.3 . 1 . . . . 107 CYS N . 15969 1 409 . 1 1 108 108 LEU H H 1 7.378 0.05 . 1 . . . . 108 LEU H . 15969 1 410 . 1 1 108 108 LEU C C 13 178.23 0.3 . 1 . . . . 108 LEU C . 15969 1 411 . 1 1 108 108 LEU CA C 13 57.18 0.3 . 1 . . . . 108 LEU CA . 15969 1 412 . 1 1 108 108 LEU CB C 13 41 0.3 . 1 . . . . 108 LEU CB . 15969 1 413 . 1 1 108 108 LEU N N 15 119.581 0.3 . 1 . . . . 108 LEU N . 15969 1 414 . 1 1 109 109 THR H H 1 7.627 0.05 . 1 . . . . 109 THR H . 15969 1 415 . 1 1 109 109 THR C C 13 175.22 0.3 . 1 . . . . 109 THR C . 15969 1 416 . 1 1 109 109 THR CA C 13 64.99 0.3 . 1 . . . . 109 THR CA . 15969 1 417 . 1 1 109 109 THR CB C 13 69.22 0.3 . 1 . . . . 109 THR CB . 15969 1 418 . 1 1 109 109 THR N N 15 115.552 0.3 . 1 . . . . 109 THR N . 15969 1 419 . 1 1 110 110 PHE H H 1 8.469 0.05 . 1 . . . . 110 PHE H . 15969 1 420 . 1 1 110 110 PHE C C 13 176.31 0.3 . 1 . . . . 110 PHE C . 15969 1 421 . 1 1 110 110 PHE CA C 13 58.26 0.3 . 1 . . . . 110 PHE CA . 15969 1 422 . 1 1 110 110 PHE CB C 13 40.06 0.3 . 1 . . . . 110 PHE CB . 15969 1 423 . 1 1 110 110 PHE N N 15 116.690 0.3 . 1 . . . . 110 PHE N . 15969 1 424 . 1 1 111 111 GLY H H 1 7.201 0.05 . 1 . . . . 111 GLY H . 15969 1 425 . 1 1 111 111 GLY C C 13 174.28 0.3 . 1 . . . . 111 GLY C . 15969 1 426 . 1 1 111 111 GLY CA C 13 44.04 0.3 . 1 . . . . 111 GLY CA . 15969 1 427 . 1 1 111 111 GLY N N 15 110.391 0.3 . 1 . . . . 111 GLY N . 15969 1 428 . 1 1 114 114 THR C C 13 177.07 0.3 . 1 . . . . 114 THR C . 15969 1 429 . 1 1 114 114 THR CA C 13 65.57 0.3 . 1 . . . . 114 THR CA . 15969 1 430 . 1 1 114 114 THR CB C 13 68.15 0.3 . 1 . . . . 114 THR CB . 15969 1 431 . 1 1 115 115 VAL H H 1 7.574 0.05 . 1 . . . . 115 VAL H . 15969 1 432 . 1 1 115 115 VAL C C 13 177.78 0.3 . 1 . . . . 115 VAL C . 15969 1 433 . 1 1 115 115 VAL CA C 13 66.65 0.3 . 1 . . . . 115 VAL CA . 15969 1 434 . 1 1 115 115 VAL CB C 13 30.57 0.3 . 1 . . . . 115 VAL CB . 15969 1 435 . 1 1 115 115 VAL N N 15 123.776 0.3 . 1 . . . . 115 VAL N . 15969 1 436 . 1 1 116 116 LEU H H 1 8.786 0.05 . 1 . . . . 116 LEU H . 15969 1 437 . 1 1 116 116 LEU C C 13 179.14 0.3 . 1 . . . . 116 LEU C . 15969 1 438 . 1 1 116 116 LEU CA C 13 57.72 0.3 . 1 . . . . 116 LEU CA . 15969 1 439 . 1 1 116 116 LEU CB C 13 40.22 0.3 . 1 . . . . 116 LEU CB . 15969 1 440 . 1 1 116 116 LEU N N 15 119.832 0.3 . 1 . . . . 116 LEU N . 15969 1 441 . 1 1 117 117 GLU H H 1 8.137 0.05 . 1 . . . . 117 GLU H . 15969 1 442 . 1 1 117 117 GLU C C 13 179.5 0.3 . 1 . . . . 117 GLU C . 15969 1 443 . 1 1 117 117 GLU CA C 13 59.09 0.3 . 1 . . . . 117 GLU CA . 15969 1 444 . 1 1 117 117 GLU CB C 13 28.72 0.3 . 1 . . . . 117 GLU CB . 15969 1 445 . 1 1 117 117 GLU N N 15 118.256 0.3 . 1 . . . . 117 GLU N . 15969 1 446 . 1 1 118 118 TYR H H 1 7.873 0.05 . 1 . . . . 118 TYR H . 15969 1 447 . 1 1 118 118 TYR C C 13 176.68 0.3 . 1 . . . . 118 TYR C . 15969 1 448 . 1 1 118 118 TYR CA C 13 60.61 0.3 . 1 . . . . 118 TYR CA . 15969 1 449 . 1 1 118 118 TYR CB C 13 37.82 0.3 . 1 . . . . 118 TYR CB . 15969 1 450 . 1 1 118 118 TYR N N 15 121.829 0.3 . 1 . . . . 118 TYR N . 15969 1 451 . 1 1 119 119 LEU H H 1 8.801 0.05 . 1 . . . . 119 LEU H . 15969 1 452 . 1 1 119 119 LEU C C 13 180.59 0.3 . 1 . . . . 119 LEU C . 15969 1 453 . 1 1 119 119 LEU CA C 13 58.27 0.3 . 1 . . . . 119 LEU CA . 15969 1 454 . 1 1 119 119 LEU CB C 13 40.82 0.3 . 1 . . . . 119 LEU CB . 15969 1 455 . 1 1 119 119 LEU N N 15 119.859 0.3 . 1 . . . . 119 LEU N . 15969 1 456 . 1 1 120 120 VAL H H 1 8.417 0.05 . 1 . . . . 120 VAL H . 15969 1 457 . 1 1 120 120 VAL C C 13 179.56 0.3 . 1 . . . . 120 VAL C . 15969 1 458 . 1 1 120 120 VAL CA C 13 66.08 0.3 . 1 . . . . 120 VAL CA . 15969 1 459 . 1 1 120 120 VAL CB C 13 31.2 0.3 . 1 . . . . 120 VAL CB . 15969 1 460 . 1 1 120 120 VAL N N 15 120.120 0.3 . 1 . . . . 120 VAL N . 15969 1 461 . 1 1 121 121 SER H H 1 8.453 0.05 . 1 . . . . 121 SER H . 15969 1 462 . 1 1 121 121 SER C C 13 181.62 0.3 . 1 . . . . 121 SER C . 15969 1 463 . 1 1 121 121 SER CA C 13 61.47 0.3 . 1 . . . . 121 SER CA . 15969 1 464 . 1 1 121 121 SER CB C 13 62.12 0.3 . 1 . . . . 121 SER CB . 15969 1 465 . 1 1 121 121 SER N N 15 117.387 0.3 . 1 . . . . 121 SER N . 15969 1 466 . 1 1 122 122 PHE H H 1 9.478 0.05 . 1 . . . . 122 PHE H . 15969 1 467 . 1 1 122 122 PHE C C 13 177.17 0.3 . 1 . . . . 122 PHE C . 15969 1 468 . 1 1 122 122 PHE CA C 13 61.87 0.3 . 1 . . . . 122 PHE CA . 15969 1 469 . 1 1 122 122 PHE CB C 13 37.94 0.3 . 1 . . . . 122 PHE CB . 15969 1 470 . 1 1 122 122 PHE N N 15 127.077 0.3 . 1 . . . . 122 PHE N . 15969 1 471 . 1 1 123 123 GLY H H 1 7.915 0.05 . 1 . . . . 123 GLY H . 15969 1 472 . 1 1 123 123 GLY C C 13 175.16 0.3 . 1 . . . . 123 GLY C . 15969 1 473 . 1 1 123 123 GLY CA C 13 46.8 0.3 . 1 . . . . 123 GLY CA . 15969 1 474 . 1 1 123 123 GLY N N 15 106.058 0.3 . 1 . . . . 123 GLY N . 15969 1 475 . 1 1 124 124 VAL H H 1 7.602 0.05 . 1 . . . . 124 VAL H . 15969 1 476 . 1 1 124 124 VAL C C 13 178.88 0.3 . 1 . . . . 124 VAL C . 15969 1 477 . 1 1 124 124 VAL CA C 13 65.77 0.3 . 1 . . . . 124 VAL CA . 15969 1 478 . 1 1 124 124 VAL CB C 13 31.09 0.3 . 1 . . . . 124 VAL CB . 15969 1 479 . 1 1 124 124 VAL N N 15 120.580 0.3 . 1 . . . . 124 VAL N . 15969 1 480 . 1 1 125 125 TRP H H 1 7.894 0.05 . 1 . . . . 125 TRP H . 15969 1 481 . 1 1 125 125 TRP C C 13 178.28 0.3 . 1 . . . . 125 TRP C . 15969 1 482 . 1 1 125 125 TRP CA C 13 62.86 0.3 . 1 . . . . 125 TRP CA . 15969 1 483 . 1 1 125 125 TRP CB C 13 28.18 0.3 . 1 . . . . 125 TRP CB . 15969 1 484 . 1 1 125 125 TRP N N 15 123.340 0.3 . 1 . . . . 125 TRP N . 15969 1 485 . 1 1 126 126 ILE H H 1 8.638 0.05 . 1 . . . . 126 ILE H . 15969 1 486 . 1 1 126 126 ILE C C 13 177.15 0.3 . 1 . . . . 126 ILE C . 15969 1 487 . 1 1 126 126 ILE CA C 13 61.49 0.3 . 1 . . . . 126 ILE CA . 15969 1 488 . 1 1 126 126 ILE CB C 13 37.1 0.3 . 1 . . . . 126 ILE CB . 15969 1 489 . 1 1 126 126 ILE N N 15 117.741 0.3 . 1 . . . . 126 ILE N . 15969 1 490 . 1 1 127 127 ARG H H 1 7.205 0.05 . 1 . . . . 127 ARG H . 15969 1 491 . 1 1 127 127 ARG C C 13 177.01 0.3 . 1 . . . . 127 ARG C . 15969 1 492 . 1 1 127 127 ARG CA C 13 56.48 0.3 . 1 . . . . 127 ARG CA . 15969 1 493 . 1 1 127 127 ARG CB C 13 30.18 0.3 . 1 . . . . 127 ARG CB . 15969 1 494 . 1 1 127 127 ARG N N 15 118.334 0.3 . 1 . . . . 127 ARG N . 15969 1 495 . 1 1 128 128 THR H H 1 7.476 0.05 . 1 . . . . 128 THR H . 15969 1 496 . 1 1 128 128 THR C C 13 181.53 0.3 . 1 . . . . 128 THR C . 15969 1 497 . 1 1 128 128 THR CA C 13 61.34 0.3 . 1 . . . . 128 THR CA . 15969 1 498 . 1 1 128 128 THR CB C 13 69.34 0.3 . 1 . . . . 128 THR CB . 15969 1 499 . 1 1 128 128 THR N N 15 121.718 0.3 . 1 . . . . 128 THR N . 15969 1 500 . 1 1 131 131 ALA C C 13 178.17 0.3 . 1 . . . . 131 ALA C . 15969 1 501 . 1 1 131 131 ALA CA C 13 53.65 0.3 . 1 . . . . 131 ALA CA . 15969 1 502 . 1 1 131 131 ALA CB C 13 17.42 0.3 . 1 . . . . 131 ALA CB . 15969 1 503 . 1 1 132 132 TYR H H 1 7.654 0.05 . 1 . . . . 132 TYR H . 15969 1 504 . 1 1 132 132 TYR C C 13 174.76 0.3 . 1 . . . . 132 TYR C . 15969 1 505 . 1 1 132 132 TYR CA C 13 55.45 0.3 . 1 . . . . 132 TYR CA . 15969 1 506 . 1 1 132 132 TYR CB C 13 38.58 0.3 . 1 . . . . 132 TYR CB . 15969 1 507 . 1 1 132 132 TYR N N 15 113.663 0.3 . 1 . . . . 132 TYR N . 15969 1 508 . 1 1 133 133 ARG H H 1 7.141 0.05 . 1 . . . . 133 ARG H . 15969 1 509 . 1 1 133 133 ARG C C 13 173.63 0.3 . 1 . . . . 133 ARG C . 15969 1 510 . 1 1 133 133 ARG CA C 13 53.75 0.3 . 1 . . . . 133 ARG CA . 15969 1 511 . 1 1 133 133 ARG CB C 13 30.37 0.3 . 1 . . . . 133 ARG CB . 15969 1 512 . 1 1 133 133 ARG N N 15 122.695 0.3 . 1 . . . . 133 ARG N . 15969 1 513 . 1 1 138 138 PRO C C 13 174.89 0.3 . 1 . . . . 138 PRO C . 15969 1 514 . 1 1 138 138 PRO CA C 13 62.47 0.3 . 1 . . . . 138 PRO CA . 15969 1 515 . 1 1 138 138 PRO CB C 13 31.44 0.3 . 1 . . . . 138 PRO CB . 15969 1 516 . 1 1 139 139 ILE H H 1 8.242 0.05 . 1 . . . . 139 ILE H . 15969 1 517 . 1 1 139 139 ILE C C 13 175.08 0.3 . 1 . . . . 139 ILE C . 15969 1 518 . 1 1 139 139 ILE CA C 13 59.35 0.3 . 1 . . . . 139 ILE CA . 15969 1 519 . 1 1 139 139 ILE CB C 13 41.04 0.3 . 1 . . . . 139 ILE CB . 15969 1 520 . 1 1 139 139 ILE N N 15 118.923 0.3 . 1 . . . . 139 ILE N . 15969 1 521 . 1 1 140 140 LEU H H 1 7.986 0.05 . 1 . . . . 140 LEU H . 15969 1 522 . 1 1 140 140 LEU CA C 13 54.08 0.3 . 1 . . . . 140 LEU CA . 15969 1 523 . 1 1 140 140 LEU CB C 13 39.75 0.3 . 1 . . . . 140 LEU CB . 15969 1 524 . 1 1 140 140 LEU N N 15 128.177 0.3 . 1 . . . . 140 LEU N . 15969 1 stop_ save_