data_5065 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5065 _Entry.Title ; Quail Cysteine and Glycine-rich Protein, NMR, 15 Minimized Model Structures ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-06-29 _Entry.Accession_date 2001-06-29 _Entry.Last_release_date 2001-11-14 _Entry.Original_release_date 2001-11-14 _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 Wolfgang Schuler . . . 5065 2 Karin Kloiber . . . 5065 3 Theresia Matt . . . 5065 4 Klaus Bister . . . 5065 5 Robert Konrat . . . 5065 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5065 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 231 5065 '15N chemical shifts' 56 5065 '1H chemical shifts' 336 5065 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 . . 2001-11-14 2001-06-29 original author . 5065 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1IBI 'BMRB Entry Tracking System' 5065 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5065 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21466850 _Citation.DOI . _Citation.PubMed_ID 11583159 _Citation.Full_citation . _Citation.Title ; Application of Cross-correlated NMR Spin Relaxation to the Zinc-finger Protein CRP2(LIM2): Evidence for Collective Motions in LIM Domains ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 40 _Citation.Journal_issue 32 _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 9596 _Citation.Page_last 9604 _Citation.Year 2001 _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 Wolfgang Schuler . . . 5065 1 2 Karin Kloiber . . . 5065 1 3 Theresia Matt . . . 5065 1 4 Klaus Bister . . . 5065 1 5 Robert Konrat . . . 5065 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'LIM domain containing proteins' 5065 1 'metal-binding protein' 5065 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5065 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9115265 _Citation.Full_citation ; Konrat R, Weiskirchen R, Krautler B, Bister K. Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2. J Biol Chem. 1997 May 2;272(18):12001-7. ; _Citation.Title 'Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 272 _Citation.Journal_issue 18 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9258 _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 12001 _Citation.Page_last 12007 _Citation.Year 1997 _Citation.Details ; Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3) are implicated in diverse processes linked to cellular differentiation and growth control. CRP proteins contain two LIM domains, each formed by two zinc-binding modules of the CCHC and CCCC type, respectively. The solution structure of the carboxyl-terminal LIM domain (LIM2) from recombinant quail CRP2 was determined by multidimensional homo- and heteronuclear magnetic resonance spectroscopy. The folding topology retains both independent zinc binding modules (CCHC and CCCC). Each module consists of two orthogonally arranged antiparallel beta-sheets, and the carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N magnetic relaxation data indicate that the modules differ in terms of conformational flexibility. They pack together via a hydrophobic core region. In addition, Arg122 in the CCHC module and Glu155 in the CCCC module are linked by an intermodular hydrogen bond and/or salt bridge. These residues are absolutely conserved in the CRP family of LIM proteins, and their interaction might contribute to the relative orientation of the two zinc-binding modules in CRP LIM2 domains. The global fold of quail CRP2 LIM2 is very similar to that of the carboxyl-terminal LIM domain of the related but functionally distinct CRP family member CRP1, analyzed recently. The carboxyl-terminal CCCC module is structurally related to the DNA-binding domain of the erythroid transcription factor GATA-1. In the two zinc-binding modules of quail CRP2 LIM2, flexible loop regions made up of conserved amino acid residues are located on the same side of the LIM2 domain and may cooperate in macromolecular recognition. ; 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 R Konrat R. . . 5065 2 2 R Weiskirchen R. . . 5065 2 3 B Krautler B. . . 5065 2 4 K Bister K. . . 5065 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5065 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9722554 _Citation.Full_citation ; Konrat R, Krautler B, Weiskirchen R, Bister K. Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. J Biol Chem. 1998 Sep 4;273(36):23233-40. ; _Citation.Title 'Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 273 _Citation.Journal_issue 36 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9258 _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 23233 _Citation.Page_last 23240 _Citation.Year 1998 _Citation.Details ; Members of the cysteine- and glycine-rich protein family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control, and pathogenesis. Here we report the solution structure of full-length recombinant quail CRP2 as determined by multi-dimensional triple-resonance NMR spectroscopy. The structural analysis revealed that the global fold of the two LIM domains in the context of the full-length protein is identical to the recently determined solution structures of the isolated individual LIM domains of quail CRP2. There is no preference in relative spatial orientation of the two domains. This supports the view that the two LIM domains are independent structural and presumably functional modules of CRP proteins. This is also reflected by the dynamic properties of CRP2 probed by 15N relaxation values (T1, T2, and nuclear Overhauser effect). A model-free analysis revealed local variations in mobility along the backbone of the two LIM domains in the native protein, similar to those observed for the isolated domains. Interestingly, fast and slow motions observed in the 58-amino acid linker region between the two LIM domains endow extensive motional freedom to CRP2. The dynamic analysis indicates independent backbone mobility of the two LIM domains and rules out correlated LIM domain motion in full-length CRP2. The finding that the LIM domains in a protein encompassing multiple LIM motifs are structurally and dynamically independent from each other supports the notion that these proteins may function as adaptor molecules arranging two or more protein constituents into a macromolecular complex. ; 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 R Konrat R. . . 5065 3 2 B Krautler B. . . 5065 3 3 R Weiskirchen R. . . 5065 3 4 K Bister K. . . 5065 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CRP2(LIM2) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CRP2(LIM2) _Assembly.Entry_ID 5065 _Assembly.ID 1 _Assembly.Name 'CYSTEINE-RICH PROTEIN 2' _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 other bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5065 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 'CYSTEINE-RICH PROTEIN' 1 $CRP2(LIM2) . . . native . . . . . 5065 1 2 'ZINC ION, I' 2 $ZN . . . native . . . . . 5065 1 3 'ZINC ION, II' 2 $ZN . . . native . . . . . 5065 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 'metal coordinate' single . 1 . 1 CYS 39 39 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 2 'metal coordinate' single . 1 . 1 CYS 42 42 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 3 'metal coordinate' single . 1 . 1 HIS 60 60 ND1 . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 4 'metal coordinate' single . 1 . 1 CYS 63 63 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 5 'metal coordinate' single . 1 . 1 CYS 66 66 SG . 3 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 6 'metal coordinate' single . 1 . 1 CYS 69 69 SG . 3 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 7 'metal coordinate' single . 1 . 1 CYS 87 87 SG . 3 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 1 8 'metal coordinate' single . 1 . 1 CYS 90 90 SG . 3 . 2 ZN 1 1 ZN . . . . . . . . . . 5065 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 1IBI . . . . . . 5065 1 yes PDB 1QLI . . . . . '1QLI: U-15N isotopical labelling but no U-13C isotopical labelling' 5065 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID CRP2(LIM2) abbreviation 5065 1 'CYSTEINE-RICH PROTEIN 2' system 5065 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CRP2(LIM2) _Entity.Sf_category entity _Entity.Sf_framecode CRP2(LIM2) _Entity.Entry_ID 5065 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'CYSTEINE-RICH PROTEIN CRP2(LIM2)' _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 ; MDRGERLGIKPESSPSPHRP TTNPNTSKFAQKFGGAEKCS RCGDSVYAAEKVIGAGKPWH KNCFRCAKCGKSLESTTLTE KEGEIYCKGCYAKNFGPKGF GYGQGAGALVHAQ ; _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 113 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all other bound' _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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . PDB 1QLI . 'Quail Cysteine And Glycine-Rich Protein, Nmr, Minimized Average Structure' . . . . . 100.00 113 100.00 100.00 6.49e-60 . . . . 5065 1 . . PDB 1IBI . 'Quail Cysteine And Glycine-Rich Protein, Nmr, 15 Minimized Model Structures' . . . . . 100.00 113 100.00 100.00 6.49e-60 . . . . 5065 1 . . PDB 1CXX . 'Mutant R122a Of Quail Cysteine And Glycine-Rich Protein, Nmr, Minimized Structure' . . . . . 100.00 113 99.12 99.12 3.94e-59 . . . . 5065 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID CRP2(LIM2) abbreviation 5065 1 'CYSTEINE-RICH PROTEIN CRP2(LIM2)' common 5065 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 82 MET . 5065 1 2 83 ASP . 5065 1 3 84 ARG . 5065 1 4 85 GLY . 5065 1 5 86 GLU . 5065 1 6 87 ARG . 5065 1 7 88 LEU . 5065 1 8 89 GLY . 5065 1 9 90 ILE . 5065 1 10 91 LYS . 5065 1 11 92 PRO . 5065 1 12 93 GLU . 5065 1 13 94 SER . 5065 1 14 95 SER . 5065 1 15 96 PRO . 5065 1 16 97 SER . 5065 1 17 98 PRO . 5065 1 18 99 HIS . 5065 1 19 100 ARG . 5065 1 20 101 PRO . 5065 1 21 102 THR . 5065 1 22 103 THR . 5065 1 23 104 ASN . 5065 1 24 105 PRO . 5065 1 25 106 ASN . 5065 1 26 107 THR . 5065 1 27 108 SER . 5065 1 28 109 LYS . 5065 1 29 110 PHE . 5065 1 30 111 ALA . 5065 1 31 112 GLN . 5065 1 32 113 LYS . 5065 1 33 114 PHE . 5065 1 34 115 GLY . 5065 1 35 116 GLY . 5065 1 36 117 ALA . 5065 1 37 118 GLU . 5065 1 38 119 LYS . 5065 1 39 120 CYS . 5065 1 40 121 SER . 5065 1 41 122 ARG . 5065 1 42 123 CYS . 5065 1 43 124 GLY . 5065 1 44 125 ASP . 5065 1 45 126 SER . 5065 1 46 127 VAL . 5065 1 47 128 TYR . 5065 1 48 129 ALA . 5065 1 49 130 ALA . 5065 1 50 131 GLU . 5065 1 51 132 LYS . 5065 1 52 133 VAL . 5065 1 53 134 ILE . 5065 1 54 135 GLY . 5065 1 55 136 ALA . 5065 1 56 137 GLY . 5065 1 57 138 LYS . 5065 1 58 139 PRO . 5065 1 59 140 TRP . 5065 1 60 141 HIS . 5065 1 61 142 LYS . 5065 1 62 143 ASN . 5065 1 63 144 CYS . 5065 1 64 145 PHE . 5065 1 65 146 ARG . 5065 1 66 147 CYS . 5065 1 67 148 ALA . 5065 1 68 149 LYS . 5065 1 69 150 CYS . 5065 1 70 151 GLY . 5065 1 71 152 LYS . 5065 1 72 153 SER . 5065 1 73 154 LEU . 5065 1 74 155 GLU . 5065 1 75 156 SER . 5065 1 76 157 THR . 5065 1 77 158 THR . 5065 1 78 159 LEU . 5065 1 79 160 THR . 5065 1 80 161 GLU . 5065 1 81 162 LYS . 5065 1 82 163 GLU . 5065 1 83 164 GLY . 5065 1 84 165 GLU . 5065 1 85 166 ILE . 5065 1 86 167 TYR . 5065 1 87 168 CYS . 5065 1 88 169 LYS . 5065 1 89 170 GLY . 5065 1 90 171 CYS . 5065 1 91 172 TYR . 5065 1 92 173 ALA . 5065 1 93 174 LYS . 5065 1 94 175 ASN . 5065 1 95 176 PHE . 5065 1 96 177 GLY . 5065 1 97 178 PRO . 5065 1 98 179 LYS . 5065 1 99 180 GLY . 5065 1 100 181 PHE . 5065 1 101 182 GLY . 5065 1 102 183 TYR . 5065 1 103 184 GLY . 5065 1 104 185 GLN . 5065 1 105 186 GLY . 5065 1 106 187 ALA . 5065 1 107 188 GLY . 5065 1 108 189 ALA . 5065 1 109 190 LEU . 5065 1 110 191 VAL . 5065 1 111 192 HIS . 5065 1 112 193 ALA . 5065 1 113 194 GLN . 5065 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 5065 1 . ASP 2 2 5065 1 . ARG 3 3 5065 1 . GLY 4 4 5065 1 . GLU 5 5 5065 1 . ARG 6 6 5065 1 . LEU 7 7 5065 1 . GLY 8 8 5065 1 . ILE 9 9 5065 1 . LYS 10 10 5065 1 . PRO 11 11 5065 1 . GLU 12 12 5065 1 . SER 13 13 5065 1 . SER 14 14 5065 1 . PRO 15 15 5065 1 . SER 16 16 5065 1 . PRO 17 17 5065 1 . HIS 18 18 5065 1 . ARG 19 19 5065 1 . PRO 20 20 5065 1 . THR 21 21 5065 1 . THR 22 22 5065 1 . ASN 23 23 5065 1 . PRO 24 24 5065 1 . ASN 25 25 5065 1 . THR 26 26 5065 1 . SER 27 27 5065 1 . LYS 28 28 5065 1 . PHE 29 29 5065 1 . ALA 30 30 5065 1 . GLN 31 31 5065 1 . LYS 32 32 5065 1 . PHE 33 33 5065 1 . GLY 34 34 5065 1 . GLY 35 35 5065 1 . ALA 36 36 5065 1 . GLU 37 37 5065 1 . LYS 38 38 5065 1 . CYS 39 39 5065 1 . SER 40 40 5065 1 . ARG 41 41 5065 1 . CYS 42 42 5065 1 . GLY 43 43 5065 1 . ASP 44 44 5065 1 . SER 45 45 5065 1 . VAL 46 46 5065 1 . TYR 47 47 5065 1 . ALA 48 48 5065 1 . ALA 49 49 5065 1 . GLU 50 50 5065 1 . LYS 51 51 5065 1 . VAL 52 52 5065 1 . ILE 53 53 5065 1 . GLY 54 54 5065 1 . ALA 55 55 5065 1 . GLY 56 56 5065 1 . LYS 57 57 5065 1 . PRO 58 58 5065 1 . TRP 59 59 5065 1 . HIS 60 60 5065 1 . LYS 61 61 5065 1 . ASN 62 62 5065 1 . CYS 63 63 5065 1 . PHE 64 64 5065 1 . ARG 65 65 5065 1 . CYS 66 66 5065 1 . ALA 67 67 5065 1 . LYS 68 68 5065 1 . CYS 69 69 5065 1 . GLY 70 70 5065 1 . LYS 71 71 5065 1 . SER 72 72 5065 1 . LEU 73 73 5065 1 . GLU 74 74 5065 1 . SER 75 75 5065 1 . THR 76 76 5065 1 . THR 77 77 5065 1 . LEU 78 78 5065 1 . THR 79 79 5065 1 . GLU 80 80 5065 1 . LYS 81 81 5065 1 . GLU 82 82 5065 1 . GLY 83 83 5065 1 . GLU 84 84 5065 1 . ILE 85 85 5065 1 . TYR 86 86 5065 1 . CYS 87 87 5065 1 . LYS 88 88 5065 1 . GLY 89 89 5065 1 . CYS 90 90 5065 1 . TYR 91 91 5065 1 . ALA 92 92 5065 1 . LYS 93 93 5065 1 . ASN 94 94 5065 1 . PHE 95 95 5065 1 . GLY 96 96 5065 1 . PRO 97 97 5065 1 . LYS 98 98 5065 1 . GLY 99 99 5065 1 . PHE 100 100 5065 1 . GLY 101 101 5065 1 . TYR 102 102 5065 1 . GLY 103 103 5065 1 . GLN 104 104 5065 1 . GLY 105 105 5065 1 . ALA 106 106 5065 1 . GLY 107 107 5065 1 . ALA 108 108 5065 1 . LEU 109 109 5065 1 . VAL 110 110 5065 1 . HIS 111 111 5065 1 . ALA 112 112 5065 1 . GLN 113 113 5065 1 stop_ save_ save_ZN _Entity.Sf_category entity _Entity.Sf_framecode ZN _Entity.Entry_ID 5065 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name ZN _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 ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _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 . _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 . ZN . 5065 2 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 5065 _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 $CRP2(LIM2) . 93934 organism . 'Coturnix japonica' 'Japanese Quail' . . Eukaryota Metazoa Coturnix japonica . . . . . . . . . . . . . . . . CSRP2 . . . . 5065 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 5065 _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 $CRP2(LIM2) . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3)PLYSS . . . . . . . . . . . . plasmid . . PET3D-QCRP2(LIM2) . . . . . . 5065 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 5065 _Chem_comp.ID ZN _Chem_comp.Provenance . _Chem_comp.Name 'ZINC ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ZN _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 ZN _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 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _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 . _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 20 15:35:03 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 InChI=1S/Zn/q+2 InChI InChI 1.03 5065 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 5065 ZN [Zn++] SMILES CACTVS 3.341 5065 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 5065 ZN [Zn+2] SMILES ACDLabs 10.04 5065 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 5065 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5065 ZN 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 zinc 'SYSTEMATIC NAME' ACDLabs 10.04 5065 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5065 ZN 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 ZN . ZN . . ZN . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5065 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5065 _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 'CYSTEINE-RICH PROTEIN CRP2(LIM2)' '[U-13C; U-15N]' . . 1 $CRP2(LIM2) . . . 1.0 2.0 mM . . . . 5065 1 2 H2O . . . . . . . 90 . . % . . . . 5065 1 3 D2O [U-2H] . . . . . . 10 . . % . . . . 5065 1 4 'potassium phosphate' . . . . . . . 20 . . mM . . . . 5065 1 5 KCl . . . . . . . 50 . . mM . . . . 5065 1 6 dithiothreitol . . . . . . . 0.5 . . mM . . . . 5065 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5065 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'CYSTEINE-RICH PROTEIN CRP2(LIM2)' [U-15N] . . 1 $CRP2(LIM2) . . . 1.0 2.0 mM . . . . 5065 2 2 H2O . . . . . . . 90 . . % . . . . 5065 2 3 D2O [U-2H] . . . . . . 10 . . % . . . . 5065 2 4 'potassium phosphate' . . . . . . . 20 . . mM . . . . 5065 2 5 KCl . . . . . . . 50 . . mM . . . . 5065 2 6 dithiothreitol . . . . . . . 0.5 . . mM . . . . 5065 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 5065 _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' 70.5 . mM 5065 1 pH 7.2 0.2 n/a 5065 1 pressure 1 . atm 5065 1 temperature 299 1 K 5065 1 stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Software.Sf_category software _Software.Sf_framecode VNMR _Software.Entry_ID 5065 _Software.ID 1 _Software.Name VNMR _Software.Version 'v6.1 Rev.B' _Software.Details 'Varian Associates, Inc.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 5065 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5065 _Software.ID 2 _Software.Name NMRPipe _Software.Version 'v1.8 Rev 2001.030.21.27' _Software.Details 'Delaglio, F.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 5065 2 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 5065 _Software.ID 3 _Software.Name ANSIG _Software.Version v3.3 _Software.Details 'Kraulis, P.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5065 3 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 5065 _Software.ID 4 _Software.Name CNS _Software.Version 1.0 _Software.Details 'Brunger, A.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 5065 4 stop_ save_ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 5065 _Software.ID 5 _Software.Name X-PLOR _Software.Version 3.851 _Software.Details 'Brunger, A.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 5065 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5065 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer VARIAN _NMR_spectrometer.Model UNITYPLUS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5065 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer VARIAN UNITYPLUS . 500 . . . 5065 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 5065 _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 15N-HSQC . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 2 '3D HNCA' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 3 '3D HNCACB' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 4 '3D HNCO' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 5 '3D CBCA(CO)NH' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 6 '3D HCCH-TOCSY' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 7 '3D CCH-TOCSY-NNH' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 8 '3D 13C-NOESY-HSQC (CA-centered)' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 9 '3D 13C-NOESY-HSQC (methyl-centered)' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 10 '3D 15N-NOESY-HSQC' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5065 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 15N-HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D HNCA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D HNCACB' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D HNCO' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D CBCA(CO)NH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D HCCH-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '3D CCH-TOCSY-NNH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name '3D 13C-NOESY-HSQC (CA-centered)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name '3D 13C-NOESY-HSQC (methyl-centered)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 5065 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name '3D 15N-NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_ref_1 _Chem_shift_reference.Entry_ID 5065 _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 . indirect 0.251449530 . . . . . . . . . 5065 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5065 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5065 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_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 5065 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_ref_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 5065 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 37 37 GLU HA H 1 4.24 0.03 . 1 . . . . . . . . 5065 1 2 . 1 1 37 37 GLU HB2 H 1 1.80 0.03 . 2 . . . . . . . . 5065 1 3 . 1 1 37 37 GLU HB3 H 1 1.59 0.03 . 2 . . . . . . . . 5065 1 4 . 1 1 37 37 GLU HG2 H 1 2.13 0.03 . 2 . . . . . . . . 5065 1 5 . 1 1 37 37 GLU HG3 H 1 2.05 0.03 . 2 . . . . . . . . 5065 1 6 . 1 1 37 37 GLU CA C 13 55.58 0.50 . 1 . . . . . . . . 5065 1 7 . 1 1 37 37 GLU CB C 13 31.50 0.50 . 1 . . . . . . . . 5065 1 8 . 1 1 37 37 GLU CG C 13 37.05 0.50 . 1 . . . . . . . . 5065 1 9 . 1 1 38 38 LYS H H 1 8.27 0.03 . 1 . . . . . . . . 5065 1 10 . 1 1 38 38 LYS HA H 1 4.23 0.03 . 1 . . . . . . . . 5065 1 11 . 1 1 38 38 LYS HB2 H 1 1.46 0.03 . 2 . . . . . . . . 5065 1 12 . 1 1 38 38 LYS HB3 H 1 1.30 0.03 . 2 . . . . . . . . 5065 1 13 . 1 1 38 38 LYS HG2 H 1 1.50 0.03 . 2 . . . . . . . . 5065 1 14 . 1 1 38 38 LYS HG3 H 1 1.22 0.03 . 2 . . . . . . . . 5065 1 15 . 1 1 38 38 LYS HD2 H 1 1.50 0.03 . 1 . . . . . . . . 5065 1 16 . 1 1 38 38 LYS HD3 H 1 1.50 0.03 . 1 . . . . . . . . 5065 1 17 . 1 1 38 38 LYS HE2 H 1 2.94 0.03 . 1 . . . . . . . . 5065 1 18 . 1 1 38 38 LYS HE3 H 1 2.94 0.03 . 1 . . . . . . . . 5065 1 19 . 1 1 38 38 LYS CA C 13 54.02 0.50 . 1 . . . . . . . . 5065 1 20 . 1 1 38 38 LYS C C 13 175.11 0.50 . 1 . . . . . . . . 5065 1 21 . 1 1 38 38 LYS CB C 13 33.38 0.50 . 1 . . . . . . . . 5065 1 22 . 1 1 38 38 LYS CG C 13 24.32 0.50 . 1 . . . . . . . . 5065 1 23 . 1 1 38 38 LYS CD C 13 28.34 0.50 . 1 . . . . . . . . 5065 1 24 . 1 1 38 38 LYS CE C 13 42.14 0.50 . 1 . . . . . . . . 5065 1 25 . 1 1 38 38 LYS N N 15 121.06 0.25 . 1 . . . . . . . . 5065 1 26 . 1 1 39 39 CYS H H 1 8.33 0.03 . 1 . . . . . . . . 5065 1 27 . 1 1 39 39 CYS HA H 1 3.60 0.03 . 1 . . . . . . . . 5065 1 28 . 1 1 39 39 CYS HB2 H 1 3.32 0.03 . 2 . . . . . . . . 5065 1 29 . 1 1 39 39 CYS HB3 H 1 2.05 0.03 . 2 . . . . . . . . 5065 1 30 . 1 1 39 39 CYS CA C 13 59.05 0.50 . 1 . . . . . . . . 5065 1 31 . 1 1 39 39 CYS C C 13 177.71 0.50 . 1 . . . . . . . . 5065 1 32 . 1 1 39 39 CYS CB C 13 31.06 0.50 . 1 . . . . . . . . 5065 1 33 . 1 1 39 39 CYS N N 15 124.88 0.25 . 1 . . . . . . . . 5065 1 34 . 1 1 40 40 SER H H 1 8.09 0.03 . 1 . . . . . . . . 5065 1 35 . 1 1 40 40 SER HA H 1 3.84 0.03 . 1 . . . . . . . . 5065 1 36 . 1 1 40 40 SER HB2 H 1 2.81 0.03 . 2 . . . . . . . . 5065 1 37 . 1 1 40 40 SER HB3 H 1 1.62 0.03 . 2 . . . . . . . . 5065 1 38 . 1 1 40 40 SER CA C 13 61.34 0.50 . 1 . . . . . . . . 5065 1 39 . 1 1 40 40 SER C C 13 172.43 0.50 . 1 . . . . . . . . 5065 1 40 . 1 1 40 40 SER CB C 13 61.76 0.50 . 1 . . . . . . . . 5065 1 41 . 1 1 40 40 SER N N 15 125.83 0.25 . 1 . . . . . . . . 5065 1 42 . 1 1 41 41 ARG H H 1 8.97 0.03 . 1 . . . . . . . . 5065 1 43 . 1 1 41 41 ARG HA H 1 4.78 0.03 . 1 . . . . . . . . 5065 1 44 . 1 1 41 41 ARG HB2 H 1 2.62 0.03 . 2 . . . . . . . . 5065 1 45 . 1 1 41 41 ARG HB3 H 1 2.38 0.03 . 2 . . . . . . . . 5065 1 46 . 1 1 41 41 ARG HG2 H 1 2.25 0.03 . 2 . . . . . . . . 5065 1 47 . 1 1 41 41 ARG HG3 H 1 1.63 0.03 . 2 . . . . . . . . 5065 1 48 . 1 1 41 41 ARG HD2 H 1 3.51 0.03 . 1 . . . . . . . . 5065 1 49 . 1 1 41 41 ARG HD3 H 1 3.51 0.03 . 1 . . . . . . . . 5065 1 50 . 1 1 41 41 ARG CA C 13 56.26 0.50 . 1 . . . . . . . . 5065 1 51 . 1 1 41 41 ARG C C 13 176.09 0.50 . 1 . . . . . . . . 5065 1 52 . 1 1 41 41 ARG CB C 13 29.82 0.50 . 1 . . . . . . . . 5065 1 53 . 1 1 41 41 ARG CG C 13 25.08 0.50 . 1 . . . . . . . . 5065 1 54 . 1 1 41 41 ARG CD C 13 40.62 0.50 . 1 . . . . . . . . 5065 1 55 . 1 1 41 41 ARG N N 15 123.64 0.25 . 1 . . . . . . . . 5065 1 56 . 1 1 42 42 CYS H H 1 7.99 0.03 . 1 . . . . . . . . 5065 1 57 . 1 1 42 42 CYS HA H 1 4.94 0.03 . 1 . . . . . . . . 5065 1 58 . 1 1 42 42 CYS HB2 H 1 3.40 0.03 . 2 . . . . . . . . 5065 1 59 . 1 1 42 42 CYS HB3 H 1 3.02 0.03 . 2 . . . . . . . . 5065 1 60 . 1 1 42 42 CYS CA C 13 58.77 0.50 . 1 . . . . . . . . 5065 1 61 . 1 1 42 42 CYS C C 13 176.60 0.50 . 1 . . . . . . . . 5065 1 62 . 1 1 42 42 CYS CB C 13 31.90 0.50 . 1 . . . . . . . . 5065 1 63 . 1 1 42 42 CYS N N 15 116.18 0.25 . 1 . . . . . . . . 5065 1 64 . 1 1 43 43 GLY H H 1 7.73 0.03 . 1 . . . . . . . . 5065 1 65 . 1 1 43 43 GLY HA2 H 1 4.22 0.03 . 2 . . . . . . . . 5065 1 66 . 1 1 43 43 GLY HA3 H 1 3.74 0.03 . 2 . . . . . . . . 5065 1 67 . 1 1 43 43 GLY CA C 13 46.19 0.50 . 1 . . . . . . . . 5065 1 68 . 1 1 43 43 GLY C C 13 172.61 0.50 . 1 . . . . . . . . 5065 1 69 . 1 1 43 43 GLY N N 15 112.49 0.25 . 1 . . . . . . . . 5065 1 70 . 1 1 44 44 ASP H H 1 8.43 0.03 . 1 . . . . . . . . 5065 1 71 . 1 1 44 44 ASP HA H 1 5.12 0.03 . 1 . . . . . . . . 5065 1 72 . 1 1 44 44 ASP HB2 H 1 2.99 0.03 . 2 . . . . . . . . 5065 1 73 . 1 1 44 44 ASP HB3 H 1 2.90 0.03 . 2 . . . . . . . . 5065 1 74 . 1 1 44 44 ASP CA C 13 52.97 0.50 . 1 . . . . . . . . 5065 1 75 . 1 1 44 44 ASP C C 13 176.35 0.50 . 1 . . . . . . . . 5065 1 76 . 1 1 44 44 ASP CB C 13 42.42 0.50 . 1 . . . . . . . . 5065 1 77 . 1 1 44 44 ASP N N 15 122.75 0.25 . 1 . . . . . . . . 5065 1 78 . 1 1 45 45 SER H H 1 8.75 0.03 . 1 . . . . . . . . 5065 1 79 . 1 1 45 45 SER HA H 1 4.38 0.03 . 1 . . . . . . . . 5065 1 80 . 1 1 45 45 SER HB2 H 1 3.64 0.03 . 2 . . . . . . . . 5065 1 81 . 1 1 45 45 SER HB3 H 1 3.42 0.03 . 2 . . . . . . . . 5065 1 82 . 1 1 45 45 SER CA C 13 59.85 0.50 . 1 . . . . . . . . 5065 1 83 . 1 1 45 45 SER C C 13 173.29 0.50 . 1 . . . . . . . . 5065 1 84 . 1 1 45 45 SER CB C 13 63.93 0.50 . 1 . . . . . . . . 5065 1 85 . 1 1 45 45 SER N N 15 117.24 0.25 . 1 . . . . . . . . 5065 1 86 . 1 1 46 46 VAL H H 1 8.65 0.03 . 1 . . . . . . . . 5065 1 87 . 1 1 46 46 VAL HA H 1 4.31 0.03 . 1 . . . . . . . . 5065 1 88 . 1 1 46 46 VAL HB H 1 0.92 0.03 . 1 . . . . . . . . 5065 1 89 . 1 1 46 46 VAL HG11 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 90 . 1 1 46 46 VAL HG12 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 91 . 1 1 46 46 VAL HG13 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 92 . 1 1 46 46 VAL HG21 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 93 . 1 1 46 46 VAL HG22 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 94 . 1 1 46 46 VAL HG23 H 1 0.42 0.03 . 1 . . . . . . . . 5065 1 95 . 1 1 46 46 VAL CA C 13 58.75 0.50 . 1 . . . . . . . . 5065 1 96 . 1 1 46 46 VAL C C 13 173.48 0.50 . 1 . . . . . . . . 5065 1 97 . 1 1 46 46 VAL CB C 13 33.83 0.50 . 1 . . . . . . . . 5065 1 98 . 1 1 46 46 VAL CG1 C 13 19.36 0.50 . 2 . . . . . . . . 5065 1 99 . 1 1 46 46 VAL CG2 C 13 21.51 0.50 . 2 . . . . . . . . 5065 1 100 . 1 1 46 46 VAL N N 15 124.55 0.25 . 1 . . . . . . . . 5065 1 101 . 1 1 47 47 TYR H H 1 8.97 0.03 . 1 . . . . . . . . 5065 1 102 . 1 1 47 47 TYR HA H 1 4.62 0.03 . 1 . . . . . . . . 5065 1 103 . 1 1 47 47 TYR HB2 H 1 3.32 0.03 . 2 . . . . . . . . 5065 1 104 . 1 1 47 47 TYR HB3 H 1 2.88 0.03 . 2 . . . . . . . . 5065 1 105 . 1 1 47 47 TYR HD1 H 1 7.23 0.03 . 1 . . . . . . . . 5065 1 106 . 1 1 47 47 TYR HD2 H 1 7.23 0.03 . 1 . . . . . . . . 5065 1 107 . 1 1 47 47 TYR HE1 H 1 6.82 0.03 . 1 . . . . . . . . 5065 1 108 . 1 1 47 47 TYR HE2 H 1 6.82 0.03 . 1 . . . . . . . . 5065 1 109 . 1 1 47 47 TYR CA C 13 57.37 0.50 . 1 . . . . . . . . 5065 1 110 . 1 1 47 47 TYR C C 13 176.67 0.50 . 1 . . . . . . . . 5065 1 111 . 1 1 47 47 TYR CB C 13 38.71 0.50 . 1 . . . . . . . . 5065 1 112 . 1 1 47 47 TYR CD1 C 13 133.15 0.50 . 1 . . . . . . . . 5065 1 113 . 1 1 47 47 TYR CD2 C 13 133.15 0.50 . 1 . . . . . . . . 5065 1 114 . 1 1 47 47 TYR CE1 C 13 118.22 0.50 . 1 . . . . . . . . 5065 1 115 . 1 1 47 47 TYR CE2 C 13 118.22 0.50 . 1 . . . . . . . . 5065 1 116 . 1 1 47 47 TYR N N 15 129.18 0.25 . 1 . . . . . . . . 5065 1 117 . 1 1 48 48 ALA H H 1 8.58 0.03 . 1 . . . . . . . . 5065 1 118 . 1 1 48 48 ALA HA H 1 3.87 0.03 . 1 . . . . . . . . 5065 1 119 . 1 1 48 48 ALA HB1 H 1 1.50 0.03 . 1 . . . . . . . . 5065 1 120 . 1 1 48 48 ALA HB2 H 1 1.50 0.03 . 1 . . . . . . . . 5065 1 121 . 1 1 48 48 ALA HB3 H 1 1.50 0.03 . 1 . . . . . . . . 5065 1 122 . 1 1 48 48 ALA CA C 13 56.21 0.50 . 1 . . . . . . . . 5065 1 123 . 1 1 48 48 ALA C C 13 179.74 0.50 . 1 . . . . . . . . 5065 1 124 . 1 1 48 48 ALA CB C 13 18.60 0.50 . 1 . . . . . . . . 5065 1 125 . 1 1 48 48 ALA N N 15 123.50 0.25 . 1 . . . . . . . . 5065 1 126 . 1 1 49 49 ALA H H 1 8.43 0.03 . 1 . . . . . . . . 5065 1 127 . 1 1 49 49 ALA HA H 1 4.21 0.03 . 1 . . . . . . . . 5065 1 128 . 1 1 49 49 ALA HB1 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 129 . 1 1 49 49 ALA HB2 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 130 . 1 1 49 49 ALA HB3 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 131 . 1 1 49 49 ALA CA C 13 54.27 0.50 . 1 . . . . . . . . 5065 1 132 . 1 1 49 49 ALA C C 13 178.28 0.50 . 1 . . . . . . . . 5065 1 133 . 1 1 49 49 ALA CB C 13 18.52 0.50 . 1 . . . . . . . . 5065 1 134 . 1 1 49 49 ALA N N 15 117.46 0.25 . 1 . . . . . . . . 5065 1 135 . 1 1 50 50 GLU H H 1 7.67 0.03 . 1 . . . . . . . . 5065 1 136 . 1 1 50 50 GLU HA H 1 4.58 0.03 . 1 . . . . . . . . 5065 1 137 . 1 1 50 50 GLU HB2 H 1 2.55 0.03 . 2 . . . . . . . . 5065 1 138 . 1 1 50 50 GLU HB3 H 1 2.30 0.03 . 2 . . . . . . . . 5065 1 139 . 1 1 50 50 GLU HG2 H 1 2.44 0.03 . 2 . . . . . . . . 5065 1 140 . 1 1 50 50 GLU HG3 H 1 2.38 0.03 . 2 . . . . . . . . 5065 1 141 . 1 1 50 50 GLU CA C 13 55.35 0.50 . 1 . . . . . . . . 5065 1 142 . 1 1 50 50 GLU C C 13 174.46 0.50 . 1 . . . . . . . . 5065 1 143 . 1 1 50 50 GLU CB C 13 30.96 0.50 . 1 . . . . . . . . 5065 1 144 . 1 1 50 50 GLU CG C 13 36.70 0.50 . 1 . . . . . . . . 5065 1 145 . 1 1 50 50 GLU N N 15 114.73 0.25 . 1 . . . . . . . . 5065 1 146 . 1 1 51 51 LYS H H 1 7.13 0.03 . 1 . . . . . . . . 5065 1 147 . 1 1 51 51 LYS HA H 1 4.37 0.03 . 1 . . . . . . . . 5065 1 148 . 1 1 51 51 LYS HB2 H 1 1.77 0.03 . 2 . . . . . . . . 5065 1 149 . 1 1 51 51 LYS HB3 H 1 1.56 0.03 . 2 . . . . . . . . 5065 1 150 . 1 1 51 51 LYS HD2 H 1 1.55 0.03 . 2 . . . . . . . . 5065 1 151 . 1 1 51 51 LYS HD3 H 1 1.46 0.03 . 2 . . . . . . . . 5065 1 152 . 1 1 51 51 LYS HE2 H 1 2.75 0.03 . 2 . . . . . . . . 5065 1 153 . 1 1 51 51 LYS HE3 H 1 2.65 0.03 . 2 . . . . . . . . 5065 1 154 . 1 1 51 51 LYS HG2 H 1 1.10 0.03 . 1 . . . . . . . . 5065 1 155 . 1 1 51 51 LYS HG3 H 1 1.10 0.03 . 1 . . . . . . . . 5065 1 156 . 1 1 51 51 LYS CA C 13 57.05 0.50 . 1 . . . . . . . . 5065 1 157 . 1 1 51 51 LYS C C 13 175.60 0.50 . 1 . . . . . . . . 5065 1 158 . 1 1 51 51 LYS CB C 13 33.89 0.50 . 1 . . . . . . . . 5065 1 159 . 1 1 51 51 LYS CG C 13 24.65 0.50 . 1 . . . . . . . . 5065 1 160 . 1 1 51 51 LYS CD C 13 29.54 0.50 . 1 . . . . . . . . 5065 1 161 . 1 1 51 51 LYS CE C 13 41.37 0.50 . 1 . . . . . . . . 5065 1 162 . 1 1 51 51 LYS N N 15 121.56 0.25 . 1 . . . . . . . . 5065 1 163 . 1 1 52 52 VAL H H 1 8.97 0.03 . 1 . . . . . . . . 5065 1 164 . 1 1 52 52 VAL HA H 1 4.29 0.03 . 1 . . . . . . . . 5065 1 165 . 1 1 52 52 VAL HB H 1 1.55 0.03 . 1 . . . . . . . . 5065 1 166 . 1 1 52 52 VAL HG11 H 1 0.33 0.03 . 2 . . . . . . . . 5065 1 167 . 1 1 52 52 VAL HG12 H 1 0.33 0.03 . 2 . . . . . . . . 5065 1 168 . 1 1 52 52 VAL HG13 H 1 0.33 0.03 . 2 . . . . . . . . 5065 1 169 . 1 1 52 52 VAL HG21 H 1 0.44 0.03 . 2 . . . . . . . . 5065 1 170 . 1 1 52 52 VAL HG22 H 1 0.44 0.03 . 2 . . . . . . . . 5065 1 171 . 1 1 52 52 VAL HG23 H 1 0.44 0.03 . 2 . . . . . . . . 5065 1 172 . 1 1 52 52 VAL CA C 13 60.10 0.50 . 1 . . . . . . . . 5065 1 173 . 1 1 52 52 VAL C C 13 173.18 0.50 . 1 . . . . . . . . 5065 1 174 . 1 1 52 52 VAL CB C 13 34.88 0.50 . 1 . . . . . . . . 5065 1 175 . 1 1 52 52 VAL CG1 C 13 20.40 0.50 . 2 . . . . . . . . 5065 1 176 . 1 1 52 52 VAL CG2 C 13 20.30 0.50 . 2 . . . . . . . . 5065 1 177 . 1 1 52 52 VAL N N 15 125.47 0.25 . 1 . . . . . . . . 5065 1 178 . 1 1 53 53 ILE H H 1 8.16 0.03 . 1 . . . . . . . . 5065 1 179 . 1 1 53 53 ILE HA H 1 5.00 0.03 . 1 . . . . . . . . 5065 1 180 . 1 1 53 53 ILE HB H 1 1.78 0.03 . 1 . . . . . . . . 5065 1 181 . 1 1 53 53 ILE HG12 H 1 1.35 0.03 . 1 . . . . . . . . 5065 1 182 . 1 1 53 53 ILE HG13 H 1 1.16 0.03 . 1 . . . . . . . . 5065 1 183 . 1 1 53 53 ILE HG21 H 1 0.73 0.03 . 1 . . . . . . . . 5065 1 184 . 1 1 53 53 ILE HG22 H 1 0.73 0.03 . 1 . . . . . . . . 5065 1 185 . 1 1 53 53 ILE HG23 H 1 0.73 0.03 . 1 . . . . . . . . 5065 1 186 . 1 1 53 53 ILE HD11 H 1 0.65 0.03 . 1 . . . . . . . . 5065 1 187 . 1 1 53 53 ILE HD12 H 1 0.65 0.03 . 1 . . . . . . . . 5065 1 188 . 1 1 53 53 ILE HD13 H 1 0.65 0.03 . 1 . . . . . . . . 5065 1 189 . 1 1 53 53 ILE CA C 13 58.35 0.50 . 1 . . . . . . . . 5065 1 190 . 1 1 53 53 ILE C C 13 176.42 0.50 . 1 . . . . . . . . 5065 1 191 . 1 1 53 53 ILE CB C 13 37.58 0.50 . 1 . . . . . . . . 5065 1 192 . 1 1 53 53 ILE CG1 C 13 26.83 0.50 . 1 . . . . . . . . 5065 1 193 . 1 1 53 53 ILE CG2 C 13 16.75 0.50 . 1 . . . . . . . . 5065 1 194 . 1 1 53 53 ILE CD1 C 13 10.99 0.50 . 1 . . . . . . . . 5065 1 195 . 1 1 53 53 ILE N N 15 124.94 0.25 . 1 . . . . . . . . 5065 1 196 . 1 1 54 54 GLY H H 1 9.01 0.03 . 1 . . . . . . . . 5065 1 197 . 1 1 54 54 GLY CA C 13 45.33 0.50 . 1 . . . . . . . . 5065 1 198 . 1 1 54 54 GLY C C 13 173.35 0.50 . 1 . . . . . . . . 5065 1 199 . 1 1 54 54 GLY N N 15 112.72 0.25 . 1 . . . . . . . . 5065 1 200 . 1 1 55 55 ALA H H 1 9.79 0.03 . 1 . . . . . . . . 5065 1 201 . 1 1 55 55 ALA HA H 1 4.13 0.03 . 1 . . . . . . . . 5065 1 202 . 1 1 55 55 ALA HB1 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 203 . 1 1 55 55 ALA HB2 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 204 . 1 1 55 55 ALA HB3 H 1 1.49 0.03 . 1 . . . . . . . . 5065 1 205 . 1 1 55 55 ALA CA C 13 53.00 0.50 . 1 . . . . . . . . 5065 1 206 . 1 1 55 55 ALA C C 13 176.81 0.50 . 1 . . . . . . . . 5065 1 207 . 1 1 55 55 ALA CB C 13 16.78 0.50 . 1 . . . . . . . . 5065 1 208 . 1 1 55 55 ALA N N 15 129.68 0.25 . 1 . . . . . . . . 5065 1 209 . 1 1 56 56 GLY H H 1 8.67 0.03 . 1 . . . . . . . . 5065 1 210 . 1 1 56 56 GLY HA2 H 1 4.06 0.03 . 2 . . . . . . . . 5065 1 211 . 1 1 56 56 GLY HA3 H 1 3.59 0.03 . 2 . . . . . . . . 5065 1 212 . 1 1 56 56 GLY CA C 13 45.02 0.50 . 1 . . . . . . . . 5065 1 213 . 1 1 56 56 GLY C C 13 173.70 0.50 . 1 . . . . . . . . 5065 1 214 . 1 1 56 56 GLY N N 15 103.14 0.25 . 1 . . . . . . . . 5065 1 215 . 1 1 57 57 LYS H H 1 8.01 0.03 . 1 . . . . . . . . 5065 1 216 . 1 1 57 57 LYS CA C 13 52.29 0.50 . 1 . . . . . . . . 5065 1 217 . 1 1 57 57 LYS C C 13 177.47 0.50 . 1 . . . . . . . . 5065 1 218 . 1 1 57 57 LYS N N 15 123.93 0.25 . 1 . . . . . . . . 5065 1 219 . 1 1 58 58 PRO HA H 1 5.08 0.03 . 1 . . . . . . . . 5065 1 220 . 1 1 58 58 PRO HB2 H 1 1.80 0.03 . 2 . . . . . . . . 5065 1 221 . 1 1 58 58 PRO HB3 H 1 1.29 0.03 . 2 . . . . . . . . 5065 1 222 . 1 1 58 58 PRO HG2 H 1 2.12 0.03 . 2 . . . . . . . . 5065 1 223 . 1 1 58 58 PRO HG3 H 1 1.83 0.03 . 2 . . . . . . . . 5065 1 224 . 1 1 58 58 PRO HD2 H 1 3.59 0.03 . 2 . . . . . . . . 5065 1 225 . 1 1 58 58 PRO HD3 H 1 3.46 0.03 . 2 . . . . . . . . 5065 1 226 . 1 1 58 58 PRO CA C 13 61.63 0.50 . 1 . . . . . . . . 5065 1 227 . 1 1 58 58 PRO C C 13 176.74 0.50 . 1 . . . . . . . . 5065 1 228 . 1 1 58 58 PRO CB C 13 32.86 0.50 . 1 . . . . . . . . 5065 1 229 . 1 1 58 58 PRO CG C 13 26.04 0.50 . 1 . . . . . . . . 5065 1 230 . 1 1 58 58 PRO CD C 13 49.79 0.50 . 1 . . . . . . . . 5065 1 231 . 1 1 59 59 TRP H H 1 8.75 0.03 . 1 . . . . . . . . 5065 1 232 . 1 1 59 59 TRP HA H 1 5.41 0.03 . 1 . . . . . . . . 5065 1 233 . 1 1 59 59 TRP HB2 H 1 3.32 0.03 . 2 . . . . . . . . 5065 1 234 . 1 1 59 59 TRP HB3 H 1 2.55 0.03 . 2 . . . . . . . . 5065 1 235 . 1 1 59 59 TRP HD1 H 1 7.30 0.03 . 1 . . . . . . . . 5065 1 236 . 1 1 59 59 TRP HE1 H 1 10.17 0.03 . 1 . . . . . . . . 5065 1 237 . 1 1 59 59 TRP HE3 H 1 7.46 0.03 . 1 . . . . . . . . 5065 1 238 . 1 1 59 59 TRP HZ2 H 1 7.10 0.03 . 1 . . . . . . . . 5065 1 239 . 1 1 59 59 TRP HZ3 H 1 7.01 0.03 . 1 . . . . . . . . 5065 1 240 . 1 1 59 59 TRP HH2 H 1 7.26 0.03 . 1 . . . . . . . . 5065 1 241 . 1 1 59 59 TRP CA C 13 54.89 0.50 . 1 . . . . . . . . 5065 1 242 . 1 1 59 59 TRP C C 13 177.20 0.50 . 1 . . . . . . . . 5065 1 243 . 1 1 59 59 TRP CB C 13 31.96 0.50 . 1 . . . . . . . . 5065 1 244 . 1 1 59 59 TRP CD1 C 13 130.43 0.50 . 1 . . . . . . . . 5065 1 245 . 1 1 59 59 TRP CE3 C 13 119.67 0.50 . 1 . . . . . . . . 5065 1 246 . 1 1 59 59 TRP CZ2 C 13 113.81 0.50 . 1 . . . . . . . . 5065 1 247 . 1 1 59 59 TRP CZ3 C 13 121.86 0.50 . 1 . . . . . . . . 5065 1 248 . 1 1 59 59 TRP CH2 C 13 124.56 0.50 . 1 . . . . . . . . 5065 1 249 . 1 1 59 59 TRP N N 15 119.21 0.25 . 1 . . . . . . . . 5065 1 250 . 1 1 59 59 TRP NE1 N 15 131.22 0.25 . 1 . . . . . . . . 5065 1 251 . 1 1 60 60 HIS H H 1 8.90 0.03 . 1 . . . . . . . . 5065 1 252 . 1 1 60 60 HIS HA H 1 4.81 0.03 . 1 . . . . . . . . 5065 1 253 . 1 1 60 60 HIS HB2 H 1 3.73 0.03 . 2 . . . . . . . . 5065 1 254 . 1 1 60 60 HIS HB3 H 1 3.60 0.03 . 2 . . . . . . . . 5065 1 255 . 1 1 60 60 HIS HD2 H 1 7.44 0.03 . 1 . . . . . . . . 5065 1 256 . 1 1 60 60 HIS HE1 H 1 7.20 0.03 . 1 . . . . . . . . 5065 1 257 . 1 1 60 60 HIS CA C 13 59.19 0.50 . 1 . . . . . . . . 5065 1 258 . 1 1 60 60 HIS C C 13 178.77 0.50 . 1 . . . . . . . . 5065 1 259 . 1 1 60 60 HIS CB C 13 30.51 0.50 . 1 . . . . . . . . 5065 1 260 . 1 1 60 60 HIS CD2 C 13 118.82 0.50 . 1 . . . . . . . . 5065 1 261 . 1 1 60 60 HIS N N 15 120.56 0.25 . 1 . . . . . . . . 5065 1 262 . 1 1 61 61 LYS H H 1 9.32 0.03 . 1 . . . . . . . . 5065 1 263 . 1 1 61 61 LYS HA H 1 3.95 0.03 . 1 . . . . . . . . 5065 1 264 . 1 1 61 61 LYS HB2 H 1 1.96 0.03 . 2 . . . . . . . . 5065 1 265 . 1 1 61 61 LYS HB3 H 1 1.86 0.03 . 2 . . . . . . . . 5065 1 266 . 1 1 61 61 LYS HG2 H 1 1.43 0.03 . 1 . . . . . . . . 5065 1 267 . 1 1 61 61 LYS HG3 H 1 1.43 0.03 . 1 . . . . . . . . 5065 1 268 . 1 1 61 61 LYS HE2 H 1 2.97 0.03 . 1 . . . . . . . . 5065 1 269 . 1 1 61 61 LYS HE3 H 1 2.97 0.03 . 1 . . . . . . . . 5065 1 270 . 1 1 61 61 LYS CA C 13 60.88 0.50 . 1 . . . . . . . . 5065 1 271 . 1 1 61 61 LYS C C 13 179.95 0.50 . 1 . . . . . . . . 5065 1 272 . 1 1 61 61 LYS CB C 13 31.83 0.50 . 1 . . . . . . . . 5065 1 273 . 1 1 61 61 LYS CG C 13 25.66 0.50 . 1 . . . . . . . . 5065 1 274 . 1 1 61 61 LYS CD C 13 29.39 0.50 . 1 . . . . . . . . 5065 1 275 . 1 1 61 61 LYS CE C 13 42.14 0.50 . 1 . . . . . . . . 5065 1 276 . 1 1 61 61 LYS N N 15 127.13 0.25 . 1 . . . . . . . . 5065 1 277 . 1 1 62 62 ASN H H 1 9.26 0.03 . 1 . . . . . . . . 5065 1 278 . 1 1 62 62 ASN HA H 1 4.70 0.03 . 1 . . . . . . . . 5065 1 279 . 1 1 62 62 ASN HB2 H 1 2.94 0.03 . 2 . . . . . . . . 5065 1 280 . 1 1 62 62 ASN HB3 H 1 2.86 0.03 . 2 . . . . . . . . 5065 1 281 . 1 1 62 62 ASN CA C 13 54.72 0.50 . 1 . . . . . . . . 5065 1 282 . 1 1 62 62 ASN C C 13 175.97 0.50 . 1 . . . . . . . . 5065 1 283 . 1 1 62 62 ASN CB C 13 38.19 0.50 . 1 . . . . . . . . 5065 1 284 . 1 1 62 62 ASN N N 15 114.66 0.25 . 1 . . . . . . . . 5065 1 285 . 1 1 63 63 CYS H H 1 7.70 0.03 . 1 . . . . . . . . 5065 1 286 . 1 1 63 63 CYS HA H 1 4.43 0.03 . 1 . . . . . . . . 5065 1 287 . 1 1 63 63 CYS HB2 H 1 3.55 0.03 . 2 . . . . . . . . 5065 1 288 . 1 1 63 63 CYS HB3 H 1 3.33 0.03 . 2 . . . . . . . . 5065 1 289 . 1 1 63 63 CYS CA C 13 60.15 0.50 . 1 . . . . . . . . 5065 1 290 . 1 1 63 63 CYS C C 13 173.58 0.50 . 1 . . . . . . . . 5065 1 291 . 1 1 63 63 CYS CB C 13 31.64 0.50 . 1 . . . . . . . . 5065 1 292 . 1 1 63 63 CYS N N 15 117.31 0.25 . 1 . . . . . . . . 5065 1 293 . 1 1 64 64 PHE H H 1 7.35 0.03 . 1 . . . . . . . . 5065 1 294 . 1 1 64 64 PHE HA H 1 4.13 0.03 . 1 . . . . . . . . 5065 1 295 . 1 1 64 64 PHE HB2 H 1 3.31 0.03 . 2 . . . . . . . . 5065 1 296 . 1 1 64 64 PHE HB3 H 1 2.60 0.03 . 2 . . . . . . . . 5065 1 297 . 1 1 64 64 PHE HD1 H 1 6.38 0.03 . 1 . . . . . . . . 5065 1 298 . 1 1 64 64 PHE HD2 H 1 6.38 0.03 . 1 . . . . . . . . 5065 1 299 . 1 1 64 64 PHE CA C 13 56.49 0.50 . 1 . . . . . . . . 5065 1 300 . 1 1 64 64 PHE HE1 H 1 6.64 0.03 . 1 . . . . . . . . 5065 1 301 . 1 1 64 64 PHE HE2 H 1 6.64 0.03 . 1 . . . . . . . . 5065 1 302 . 1 1 64 64 PHE C C 13 173.23 0.50 . 1 . . . . . . . . 5065 1 303 . 1 1 64 64 PHE CB C 13 36.67 0.50 . 1 . . . . . . . . 5065 1 304 . 1 1 64 64 PHE CD1 C 13 132.35 0.50 . 1 . . . . . . . . 5065 1 305 . 1 1 64 64 PHE CD2 C 13 132.35 0.50 . 1 . . . . . . . . 5065 1 306 . 1 1 64 64 PHE N N 15 124.01 0.25 . 1 . . . . . . . . 5065 1 307 . 1 1 65 65 ARG H H 1 7.63 0.03 . 1 . . . . . . . . 5065 1 308 . 1 1 65 65 ARG HA H 1 4.73 0.03 . 1 . . . . . . . . 5065 1 309 . 1 1 65 65 ARG HB2 H 1 1.26 0.03 . 2 . . . . . . . . 5065 1 310 . 1 1 65 65 ARG HB3 H 1 1.07 0.03 . 2 . . . . . . . . 5065 1 311 . 1 1 65 65 ARG HG2 H 1 1.21 0.03 . 2 . . . . . . . . 5065 1 312 . 1 1 65 65 ARG HG3 H 1 1.13 0.03 . 2 . . . . . . . . 5065 1 313 . 1 1 65 65 ARG HD2 H 1 3.20 0.03 . 2 . . . . . . . . 5065 1 314 . 1 1 65 65 ARG HD3 H 1 3.09 0.03 . 2 . . . . . . . . 5065 1 315 . 1 1 65 65 ARG CA C 13 52.70 0.50 . 1 . . . . . . . . 5065 1 316 . 1 1 65 65 ARG C C 13 173.95 0.50 . 1 . . . . . . . . 5065 1 317 . 1 1 65 65 ARG CB C 13 34.78 0.50 . 1 . . . . . . . . 5065 1 318 . 1 1 65 65 ARG CG C 13 27.59 0.50 . 1 . . . . . . . . 5065 1 319 . 1 1 65 65 ARG CD C 13 43.30 0.50 . 1 . . . . . . . . 5065 1 320 . 1 1 65 65 ARG N N 15 122.29 0.25 . 1 . . . . . . . . 5065 1 321 . 1 1 66 66 CYS H H 1 8.73 0.03 . 1 . . . . . . . . 5065 1 322 . 1 1 66 66 CYS HA H 1 3.82 0.03 . 1 . . . . . . . . 5065 1 323 . 1 1 66 66 CYS HB2 H 1 3.32 0.03 . 2 . . . . . . . . 5065 1 324 . 1 1 66 66 CYS HB3 H 1 2.76 0.03 . 2 . . . . . . . . 5065 1 325 . 1 1 66 66 CYS CA C 13 59.83 0.50 . 1 . . . . . . . . 5065 1 326 . 1 1 66 66 CYS C C 13 177.19 0.50 . 1 . . . . . . . . 5065 1 327 . 1 1 66 66 CYS CB C 13 30.89 0.50 . 1 . . . . . . . . 5065 1 328 . 1 1 66 66 CYS N N 15 123.85 0.25 . 1 . . . . . . . . 5065 1 329 . 1 1 67 67 ALA H H 1 8.86 0.03 . 1 . . . . . . . . 5065 1 330 . 1 1 67 67 ALA HA H 1 3.87 0.03 . 1 . . . . . . . . 5065 1 331 . 1 1 67 67 ALA HB1 H 1 1.21 0.03 . 1 . . . . . . . . 5065 1 332 . 1 1 67 67 ALA HB2 H 1 1.21 0.03 . 1 . . . . . . . . 5065 1 333 . 1 1 67 67 ALA HB3 H 1 1.21 0.03 . 1 . . . . . . . . 5065 1 334 . 1 1 67 67 ALA CA C 13 54.80 0.50 . 1 . . . . . . . . 5065 1 335 . 1 1 67 67 ALA C C 13 177.49 0.50 . 1 . . . . . . . . 5065 1 336 . 1 1 67 67 ALA CB C 13 18.23 0.50 . 1 . . . . . . . . 5065 1 337 . 1 1 67 67 ALA N N 15 133.93 0.25 . 1 . . . . . . . . 5065 1 338 . 1 1 68 68 LYS H H 1 8.98 0.03 . 1 . . . . . . . . 5065 1 339 . 1 1 68 68 LYS HA H 1 4.64 0.03 . 1 . . . . . . . . 5065 1 340 . 1 1 68 68 LYS HB2 H 1 2.40 0.03 . 2 . . . . . . . . 5065 1 341 . 1 1 68 68 LYS HB3 H 1 2.17 0.03 . 2 . . . . . . . . 5065 1 342 . 1 1 68 68 LYS HG2 H 1 1.52 0.03 . 1 . . . . . . . . 5065 1 343 . 1 1 68 68 LYS HG3 H 1 1.52 0.03 . 1 . . . . . . . . 5065 1 344 . 1 1 68 68 LYS CA C 13 56.69 0.50 . 1 . . . . . . . . 5065 1 345 . 1 1 68 68 LYS C C 13 176.98 0.50 . 1 . . . . . . . . 5065 1 346 . 1 1 68 68 LYS CB C 13 33.65 0.50 . 1 . . . . . . . . 5065 1 347 . 1 1 68 68 LYS CG C 13 25.21 0.50 . 1 . . . . . . . . 5065 1 348 . 1 1 68 68 LYS CD C 13 28.25 0.50 . 1 . . . . . . . . 5065 1 349 . 1 1 68 68 LYS CE C 13 42.04 0.50 . 1 . . . . . . . . 5065 1 350 . 1 1 68 68 LYS N N 15 118.75 0.25 . 1 . . . . . . . . 5065 1 351 . 1 1 69 69 CYS H H 1 8.41 0.03 . 1 . . . . . . . . 5065 1 352 . 1 1 69 69 CYS HA H 1 4.94 0.03 . 1 . . . . . . . . 5065 1 353 . 1 1 69 69 CYS HB2 H 1 3.28 0.03 . 2 . . . . . . . . 5065 1 354 . 1 1 69 69 CYS HB3 H 1 2.67 0.03 . 2 . . . . . . . . 5065 1 355 . 1 1 69 69 CYS CA C 13 59.19 0.50 . 1 . . . . . . . . 5065 1 356 . 1 1 69 69 CYS C C 13 177.14 0.50 . 1 . . . . . . . . 5065 1 357 . 1 1 69 69 CYS CB C 13 32.83 0.50 . 1 . . . . . . . . 5065 1 358 . 1 1 69 69 CYS N N 15 118.57 0.25 . 1 . . . . . . . . 5065 1 359 . 1 1 70 70 GLY H H 1 7.84 0.03 . 1 . . . . . . . . 5065 1 360 . 1 1 70 70 GLY HA2 H 1 4.19 0.03 . 2 . . . . . . . . 5065 1 361 . 1 1 70 70 GLY HA3 H 1 3.72 0.03 . 2 . . . . . . . . 5065 1 362 . 1 1 70 70 GLY CA C 13 46.19 0.50 . 1 . . . . . . . . 5065 1 363 . 1 1 70 70 GLY C C 13 173.21 0.50 . 1 . . . . . . . . 5065 1 364 . 1 1 70 70 GLY N N 15 112.67 0.25 . 1 . . . . . . . . 5065 1 365 . 1 1 71 71 LYS H H 1 8.60 0.03 . 1 . . . . . . . . 5065 1 366 . 1 1 71 71 LYS HA H 1 4.17 0.03 . 1 . . . . . . . . 5065 1 367 . 1 1 71 71 LYS HB2 H 1 1.82 0.03 . 2 . . . . . . . . 5065 1 368 . 1 1 71 71 LYS HB3 H 1 1.69 0.03 . 2 . . . . . . . . 5065 1 369 . 1 1 71 71 LYS HG2 H 1 1.41 0.03 . 1 . . . . . . . . 5065 1 370 . 1 1 71 71 LYS HG3 H 1 1.41 0.03 . 1 . . . . . . . . 5065 1 371 . 1 1 71 71 LYS HE2 H 1 2.97 0.03 . 1 . . . . . . . . 5065 1 372 . 1 1 71 71 LYS HE3 H 1 2.97 0.03 . 1 . . . . . . . . 5065 1 373 . 1 1 71 71 LYS CA C 13 57.23 0.50 . 1 . . . . . . . . 5065 1 374 . 1 1 71 71 LYS C C 13 176.54 0.50 . 1 . . . . . . . . 5065 1 375 . 1 1 71 71 LYS CB C 13 33.43 0.50 . 1 . . . . . . . . 5065 1 376 . 1 1 71 71 LYS CG C 13 24.78 0.50 . 1 . . . . . . . . 5065 1 377 . 1 1 71 71 LYS CD C 13 29.44 0.50 . 1 . . . . . . . . 5065 1 378 . 1 1 71 71 LYS CE C 13 41.91 0.50 . 1 . . . . . . . . 5065 1 379 . 1 1 71 71 LYS N N 15 125.02 0.25 . 1 . . . . . . . . 5065 1 380 . 1 1 72 72 SER H H 1 8.75 0.03 . 1 . . . . . . . . 5065 1 381 . 1 1 72 72 SER HA H 1 4.17 0.03 . 1 . . . . . . . . 5065 1 382 . 1 1 72 72 SER HB2 H 1 3.95 0.03 . 2 . . . . . . . . 5065 1 383 . 1 1 72 72 SER HB3 H 1 3.88 0.03 . 2 . . . . . . . . 5065 1 384 . 1 1 72 72 SER CA C 13 60.24 0.50 . 1 . . . . . . . . 5065 1 385 . 1 1 72 72 SER C C 13 174.20 0.50 . 1 . . . . . . . . 5065 1 386 . 1 1 72 72 SER CB C 13 63.06 0.50 . 1 . . . . . . . . 5065 1 387 . 1 1 72 72 SER N N 15 120.12 0.25 . 1 . . . . . . . . 5065 1 388 . 1 1 73 73 LEU H H 1 7.69 0.03 . 1 . . . . . . . . 5065 1 389 . 1 1 73 73 LEU HA H 1 4.34 0.03 . 1 . . . . . . . . 5065 1 390 . 1 1 73 73 LEU HB2 H 1 0.72 0.03 . 2 . . . . . . . . 5065 1 391 . 1 1 73 73 LEU HB3 H 1 0.38 0.03 . 2 . . . . . . . . 5065 1 392 . 1 1 73 73 LEU HG H 1 1.24 0.03 . 1 . . . . . . . . 5065 1 393 . 1 1 73 73 LEU HD11 H 1 -0.07 0.03 . 2 . . . . . . . . 5065 1 394 . 1 1 73 73 LEU HD12 H 1 -0.07 0.03 . 2 . . . . . . . . 5065 1 395 . 1 1 73 73 LEU HD13 H 1 -0.07 0.03 . 2 . . . . . . . . 5065 1 396 . 1 1 73 73 LEU HD21 H 1 0.50 0.03 . 2 . . . . . . . . 5065 1 397 . 1 1 73 73 LEU HD22 H 1 0.50 0.03 . 2 . . . . . . . . 5065 1 398 . 1 1 73 73 LEU HD23 H 1 0.50 0.03 . 2 . . . . . . . . 5065 1 399 . 1 1 73 73 LEU CA C 13 53.30 0.50 . 1 . . . . . . . . 5065 1 400 . 1 1 73 73 LEU CB C 13 43.21 0.50 . 1 . . . . . . . . 5065 1 401 . 1 1 73 73 LEU CG C 13 26.14 0.50 . 1 . . . . . . . . 5065 1 402 . 1 1 73 73 LEU CD1 C 13 25.57 0.50 . 2 . . . . . . . . 5065 1 403 . 1 1 73 73 LEU CD2 C 13 22.20 0.50 . 2 . . . . . . . . 5065 1 404 . 1 1 73 73 LEU N N 15 124.90 0.25 . 1 . . . . . . . . 5065 1 405 . 1 1 74 74 GLU H H 1 7.51 0.03 . 1 . . . . . . . . 5065 1 406 . 1 1 74 74 GLU CA C 13 55.21 0.50 . 1 . . . . . . . . 5065 1 407 . 1 1 74 74 GLU N N 15 116.82 0.25 . 1 . . . . . . . . 5065 1 408 . 1 1 76 76 THR HA H 1 4.46 0.03 . 1 . . . . . . . . 5065 1 409 . 1 1 76 76 THR HB H 1 4.23 0.03 . 1 . . . . . . . . 5065 1 410 . 1 1 76 76 THR HG21 H 1 1.28 0.03 . 1 . . . . . . . . 5065 1 411 . 1 1 76 76 THR HG22 H 1 1.28 0.03 . 1 . . . . . . . . 5065 1 412 . 1 1 76 76 THR HG23 H 1 1.28 0.03 . 1 . . . . . . . . 5065 1 413 . 1 1 76 76 THR CA C 13 62.06 0.50 . 1 . . . . . . . . 5065 1 414 . 1 1 76 76 THR C C 13 175.37 0.50 . 1 . . . . . . . . 5065 1 415 . 1 1 76 76 THR CB C 13 69.29 0.50 . 1 . . . . . . . . 5065 1 416 . 1 1 76 76 THR CG2 C 13 21.70 0.50 . 1 . . . . . . . . 5065 1 417 . 1 1 77 77 THR H H 1 7.62 0.03 . 1 . . . . . . . . 5065 1 418 . 1 1 77 77 THR HA H 1 4.54 0.03 . 1 . . . . . . . . 5065 1 419 . 1 1 77 77 THR HB H 1 4.48 0.03 . 1 . . . . . . . . 5065 1 420 . 1 1 77 77 THR HG21 H 1 1.17 0.03 . 1 . . . . . . . . 5065 1 421 . 1 1 77 77 THR HG22 H 1 1.17 0.03 . 1 . . . . . . . . 5065 1 422 . 1 1 77 77 THR HG23 H 1 1.17 0.03 . 1 . . . . . . . . 5065 1 423 . 1 1 77 77 THR CA C 13 61.03 0.50 . 1 . . . . . . . . 5065 1 424 . 1 1 77 77 THR C C 13 173.61 0.50 . 1 . . . . . . . . 5065 1 425 . 1 1 77 77 THR CB C 13 69.75 0.50 . 1 . . . . . . . . 5065 1 426 . 1 1 77 77 THR CG2 C 13 22.29 0.50 . 1 . . . . . . . . 5065 1 427 . 1 1 77 77 THR N N 15 111.72 0.25 . 1 . . . . . . . . 5065 1 428 . 1 1 78 78 LEU H H 1 7.38 0.03 . 1 . . . . . . . . 5065 1 429 . 1 1 78 78 LEU HA H 1 4.61 0.03 . 1 . . . . . . . . 5065 1 430 . 1 1 78 78 LEU HG H 1 1.64 0.03 . 1 . . . . . . . . 5065 1 431 . 1 1 78 78 LEU HD11 H 1 0.69 0.03 . 2 . . . . . . . . 5065 1 432 . 1 1 78 78 LEU HD12 H 1 0.69 0.03 . 2 . . . . . . . . 5065 1 433 . 1 1 78 78 LEU HD13 H 1 0.69 0.03 . 2 . . . . . . . . 5065 1 434 . 1 1 78 78 LEU HD21 H 1 0.78 0.03 . 2 . . . . . . . . 5065 1 435 . 1 1 78 78 LEU HD22 H 1 0.78 0.03 . 2 . . . . . . . . 5065 1 436 . 1 1 78 78 LEU HD23 H 1 0.78 0.03 . 2 . . . . . . . . 5065 1 437 . 1 1 78 78 LEU HB2 H 1 1.51 0.03 . 1 . . . . . . . . 5065 1 438 . 1 1 78 78 LEU HB3 H 1 1.51 0.03 . 1 . . . . . . . . 5065 1 439 . 1 1 78 78 LEU CA C 13 54.79 0.50 . 1 . . . . . . . . 5065 1 440 . 1 1 78 78 LEU C C 13 175.61 0.50 . 1 . . . . . . . . 5065 1 441 . 1 1 78 78 LEU CB C 13 44.54 0.50 . 1 . . . . . . . . 5065 1 442 . 1 1 78 78 LEU CG C 13 26.28 0.50 . 1 . . . . . . . . 5065 1 443 . 1 1 78 78 LEU CD1 C 13 25.38 0.50 . 2 . . . . . . . . 5065 1 444 . 1 1 78 78 LEU CD2 C 13 27.93 0.50 . 2 . . . . . . . . 5065 1 445 . 1 1 78 78 LEU N N 15 122.41 0.25 . 1 . . . . . . . . 5065 1 446 . 1 1 79 79 THR H H 1 8.72 0.03 . 1 . . . . . . . . 5065 1 447 . 1 1 79 79 THR HA H 1 4.37 0.03 . 1 . . . . . . . . 5065 1 448 . 1 1 79 79 THR HB H 1 3.45 0.03 . 1 . . . . . . . . 5065 1 449 . 1 1 79 79 THR HG21 H 1 0.58 0.03 . 1 . . . . . . . . 5065 1 450 . 1 1 79 79 THR HG22 H 1 0.58 0.03 . 1 . . . . . . . . 5065 1 451 . 1 1 79 79 THR HG23 H 1 0.58 0.03 . 1 . . . . . . . . 5065 1 452 . 1 1 79 79 THR CA C 13 61.72 0.50 . 1 . . . . . . . . 5065 1 453 . 1 1 79 79 THR C C 13 171.95 0.50 . 1 . . . . . . . . 5065 1 454 . 1 1 79 79 THR CB C 13 71.13 0.50 . 1 . . . . . . . . 5065 1 455 . 1 1 79 79 THR CG2 C 13 22.11 0.50 . 1 . . . . . . . . 5065 1 456 . 1 1 79 79 THR N N 15 118.09 0.25 . 1 . . . . . . . . 5065 1 457 . 1 1 80 80 GLU H H 1 8.50 0.03 . 1 . . . . . . . . 5065 1 458 . 1 1 80 80 GLU HA H 1 5.46 0.03 . 1 . . . . . . . . 5065 1 459 . 1 1 80 80 GLU HB2 H 1 2.02 0.03 . 2 . . . . . . . . 5065 1 460 . 1 1 80 80 GLU HB3 H 1 1.86 0.03 . 2 . . . . . . . . 5065 1 461 . 1 1 80 80 GLU HG2 H 1 2.18 0.03 . 1 . . . . . . . . 5065 1 462 . 1 1 80 80 GLU HG3 H 1 2.18 0.03 . 1 . . . . . . . . 5065 1 463 . 1 1 80 80 GLU CA C 13 54.42 0.50 . 1 . . . . . . . . 5065 1 464 . 1 1 80 80 GLU C C 13 175.27 0.50 . 1 . . . . . . . . 5065 1 465 . 1 1 80 80 GLU CB C 13 32.38 0.50 . 1 . . . . . . . . 5065 1 466 . 1 1 80 80 GLU CG C 13 35.99 0.50 . 1 . . . . . . . . 5065 1 467 . 1 1 80 80 GLU N N 15 124.90 0.25 . 1 . . . . . . . . 5065 1 468 . 1 1 81 81 LYS H H 1 9.02 0.03 . 1 . . . . . . . . 5065 1 469 . 1 1 81 81 LYS HA H 1 4.40 0.03 . 1 . . . . . . . . 5065 1 470 . 1 1 81 81 LYS CA C 13 56.39 0.50 . 1 . . . . . . . . 5065 1 471 . 1 1 81 81 LYS C C 13 175.68 0.50 . 1 . . . . . . . . 5065 1 472 . 1 1 81 81 LYS N N 15 123.83 0.25 . 1 . . . . . . . . 5065 1 473 . 1 1 82 82 GLU HA H 1 4.76 0.03 . 1 . . . . . . . . 5065 1 474 . 1 1 82 82 GLU HB2 H 1 2.23 0.03 . 2 . . . . . . . . 5065 1 475 . 1 1 82 82 GLU CA C 13 56.91 0.50 . 1 . . . . . . . . 5065 1 476 . 1 1 82 82 GLU C C 13 175.81 0.50 . 1 . . . . . . . . 5065 1 477 . 1 1 82 82 GLU CB C 13 27.78 0.50 . 1 . . . . . . . . 5065 1 478 . 1 1 82 82 GLU CG C 13 36.87 0.50 . 1 . . . . . . . . 5065 1 479 . 1 1 83 83 GLY H H 1 9.09 0.03 . 1 . . . . . . . . 5065 1 480 . 1 1 83 83 GLY HA2 H 1 4.25 0.03 . 2 . . . . . . . . 5065 1 481 . 1 1 83 83 GLY HA3 H 1 3.77 0.03 . 2 . . . . . . . . 5065 1 482 . 1 1 83 83 GLY CA C 13 45.61 0.50 . 1 . . . . . . . . 5065 1 483 . 1 1 83 83 GLY C C 13 172.96 0.50 . 1 . . . . . . . . 5065 1 484 . 1 1 83 83 GLY N N 15 106.46 0.25 . 1 . . . . . . . . 5065 1 485 . 1 1 84 84 GLU H H 1 7.95 0.03 . 1 . . . . . . . . 5065 1 486 . 1 1 84 84 GLU HA H 1 5.07 0.03 . 1 . . . . . . . . 5065 1 487 . 1 1 84 84 GLU HB2 H 1 1.96 0.03 . 2 . . . . . . . . 5065 1 488 . 1 1 84 84 GLU HB3 H 1 1.90 0.03 . 2 . . . . . . . . 5065 1 489 . 1 1 84 84 GLU HG2 H 1 2.34 0.03 . 2 . . . . . . . . 5065 1 490 . 1 1 84 84 GLU HG3 H 1 2.20 0.03 . 2 . . . . . . . . 5065 1 491 . 1 1 84 84 GLU CA C 13 53.41 0.50 . 1 . . . . . . . . 5065 1 492 . 1 1 84 84 GLU C C 13 174.64 0.50 . 1 . . . . . . . . 5065 1 493 . 1 1 84 84 GLU CB C 13 33.17 0.50 . 1 . . . . . . . . 5065 1 494 . 1 1 84 84 GLU CG C 13 36.68 0.50 . 1 . . . . . . . . 5065 1 495 . 1 1 84 84 GLU N N 15 122.78 0.25 . 1 . . . . . . . . 5065 1 496 . 1 1 85 85 ILE H H 1 8.84 0.03 . 1 . . . . . . . . 5065 1 497 . 1 1 85 85 ILE HA H 1 4.95 0.03 . 1 . . . . . . . . 5065 1 498 . 1 1 85 85 ILE HB H 1 1.14 0.03 . 1 . . . . . . . . 5065 1 499 . 1 1 85 85 ILE HG12 H 1 0.99 0.03 . 1 . . . . . . . . 5065 1 500 . 1 1 85 85 ILE HG13 H 1 0.51 0.03 . 1 . . . . . . . . 5065 1 501 . 1 1 85 85 ILE HG21 H 1 0.53 0.03 . 1 . . . . . . . . 5065 1 502 . 1 1 85 85 ILE HG22 H 1 0.53 0.03 . 1 . . . . . . . . 5065 1 503 . 1 1 85 85 ILE HG23 H 1 0.53 0.03 . 1 . . . . . . . . 5065 1 504 . 1 1 85 85 ILE HD11 H 1 -0.77 0.03 . 1 . . . . . . . . 5065 1 505 . 1 1 85 85 ILE HD12 H 1 -0.77 0.03 . 1 . . . . . . . . 5065 1 506 . 1 1 85 85 ILE HD13 H 1 -0.77 0.03 . 1 . . . . . . . . 5065 1 507 . 1 1 85 85 ILE CA C 13 59.63 0.50 . 1 . . . . . . . . 5065 1 508 . 1 1 85 85 ILE C C 13 173.12 0.50 . 1 . . . . . . . . 5065 1 509 . 1 1 85 85 ILE CB C 13 40.56 0.50 . 1 . . . . . . . . 5065 1 510 . 1 1 85 85 ILE CG1 C 13 23.80 0.50 . 1 . . . . . . . . 5065 1 511 . 1 1 85 85 ILE CG2 C 13 18.31 0.50 . 1 . . . . . . . . 5065 1 512 . 1 1 85 85 ILE CD1 C 13 12.93 0.50 . 1 . . . . . . . . 5065 1 513 . 1 1 85 85 ILE N N 15 114.84 0.25 . 1 . . . . . . . . 5065 1 514 . 1 1 86 86 TYR H H 1 8.23 0.03 . 1 . . . . . . . . 5065 1 515 . 1 1 86 86 TYR HA H 1 5.66 0.03 . 1 . . . . . . . . 5065 1 516 . 1 1 86 86 TYR HB2 H 1 3.36 0.03 . 2 . . . . . . . . 5065 1 517 . 1 1 86 86 TYR HB3 H 1 2.82 0.03 . 2 . . . . . . . . 5065 1 518 . 1 1 86 86 TYR HD1 H 1 7.08 0.03 . 1 . . . . . . . . 5065 1 519 . 1 1 86 86 TYR HD2 H 1 7.08 0.03 . 1 . . . . . . . . 5065 1 520 . 1 1 86 86 TYR HE1 H 1 6.84 0.03 . 1 . . . . . . . . 5065 1 521 . 1 1 86 86 TYR HE2 H 1 6.84 0.03 . 1 . . . . . . . . 5065 1 522 . 1 1 86 86 TYR CA C 13 56.23 0.50 . 1 . . . . . . . . 5065 1 523 . 1 1 86 86 TYR C C 13 176.20 0.50 . 1 . . . . . . . . 5065 1 524 . 1 1 86 86 TYR CB C 13 43.73 0.50 . 1 . . . . . . . . 5065 1 525 . 1 1 86 86 TYR CD1 C 13 133.17 0.50 . 1 . . . . . . . . 5065 1 526 . 1 1 86 86 TYR CD2 C 13 133.17 0.50 . 1 . . . . . . . . 5065 1 527 . 1 1 86 86 TYR N N 15 118.22 0.25 . 1 . . . . . . . . 5065 1 528 . 1 1 87 87 CYS H H 1 9.69 0.03 . 1 . . . . . . . . 5065 1 529 . 1 1 87 87 CYS HA H 1 5.03 0.03 . 1 . . . . . . . . 5065 1 530 . 1 1 87 87 CYS HB2 H 1 3.48 0.03 . 2 . . . . . . . . 5065 1 531 . 1 1 87 87 CYS HB3 H 1 2.79 0.03 . 2 . . . . . . . . 5065 1 532 . 1 1 87 87 CYS CA C 13 57.40 0.50 . 1 . . . . . . . . 5065 1 533 . 1 1 87 87 CYS C C 13 175.91 0.50 . 1 . . . . . . . . 5065 1 534 . 1 1 87 87 CYS CB C 13 30.99 0.50 . 1 . . . . . . . . 5065 1 535 . 1 1 87 87 CYS N N 15 120.71 0.25 . 1 . . . . . . . . 5065 1 536 . 1 1 88 88 LYS H H 1 8.58 0.03 . 1 . . . . . . . . 5065 1 537 . 1 1 88 88 LYS HA H 1 3.96 0.03 . 1 . . . . . . . . 5065 1 538 . 1 1 88 88 LYS HB2 H 1 1.85 0.03 . 1 . . . . . . . . 5065 1 539 . 1 1 88 88 LYS HB3 H 1 1.85 0.03 . 1 . . . . . . . . 5065 1 540 . 1 1 88 88 LYS HG2 H 1 1.44 0.03 . 1 . . . . . . . . 5065 1 541 . 1 1 88 88 LYS HG3 H 1 1.44 0.03 . 1 . . . . . . . . 5065 1 542 . 1 1 88 88 LYS HD2 H 1 1.68 0.03 . 1 . . . . . . . . 5065 1 543 . 1 1 88 88 LYS HD3 H 1 1.68 0.03 . 1 . . . . . . . . 5065 1 544 . 1 1 88 88 LYS HE2 H 1 3.01 0.03 . 1 . . . . . . . . 5065 1 545 . 1 1 88 88 LYS HE3 H 1 3.01 0.03 . 1 . . . . . . . . 5065 1 546 . 1 1 88 88 LYS CA C 13 59.78 0.50 . 1 . . . . . . . . 5065 1 547 . 1 1 88 88 LYS C C 13 179.70 0.50 . 1 . . . . . . . . 5065 1 548 . 1 1 88 88 LYS CB C 13 32.12 0.50 . 1 . . . . . . . . 5065 1 549 . 1 1 88 88 LYS CG C 13 25.32 0.50 . 1 . . . . . . . . 5065 1 550 . 1 1 88 88 LYS CD C 13 29.24 0.50 . 1 . . . . . . . . 5065 1 551 . 1 1 88 88 LYS CE C 13 42.04 0.50 . 1 . . . . . . . . 5065 1 552 . 1 1 88 88 LYS N N 15 120.75 0.25 . 1 . . . . . . . . 5065 1 553 . 1 1 89 89 GLY H H 1 8.50 0.03 . 1 . . . . . . . . 5065 1 554 . 1 1 89 89 GLY HA2 H 1 4.05 0.03 . 2 . . . . . . . . 5065 1 555 . 1 1 89 89 GLY HA3 H 1 3.90 0.03 . 2 . . . . . . . . 5065 1 556 . 1 1 89 89 GLY CA C 13 46.76 0.50 . 1 . . . . . . . . 5065 1 557 . 1 1 89 89 GLY C C 13 176.85 0.50 . 1 . . . . . . . . 5065 1 558 . 1 1 89 89 GLY N N 15 109.66 0.25 . 1 . . . . . . . . 5065 1 559 . 1 1 90 90 CYS H H 1 9.18 0.03 . 1 . . . . . . . . 5065 1 560 . 1 1 90 90 CYS HA H 1 3.94 0.03 . 1 . . . . . . . . 5065 1 561 . 1 1 90 90 CYS HB2 H 1 3.20 0.03 . 2 . . . . . . . . 5065 1 562 . 1 1 90 90 CYS HB3 H 1 2.77 0.03 . 2 . . . . . . . . 5065 1 563 . 1 1 90 90 CYS CA C 13 64.69 0.50 . 1 . . . . . . . . 5065 1 564 . 1 1 90 90 CYS C C 13 178.59 0.50 . 1 . . . . . . . . 5065 1 565 . 1 1 90 90 CYS CB C 13 29.71 0.50 . 1 . . . . . . . . 5065 1 566 . 1 1 90 90 CYS N N 15 127.03 0.25 . 1 . . . . . . . . 5065 1 567 . 1 1 91 91 TYR H H 1 8.83 0.03 . 1 . . . . . . . . 5065 1 568 . 1 1 91 91 TYR HA H 1 3.74 0.03 . 1 . . . . . . . . 5065 1 569 . 1 1 91 91 TYR HB2 H 1 3.13 0.03 . 1 . . . . . . . . 5065 1 570 . 1 1 91 91 TYR HB3 H 1 3.13 0.03 . 1 . . . . . . . . 5065 1 571 . 1 1 91 91 TYR HD1 H 1 6.83 0.03 . 1 . . . . . . . . 5065 1 572 . 1 1 91 91 TYR HD2 H 1 6.83 0.03 . 1 . . . . . . . . 5065 1 573 . 1 1 91 91 TYR HE1 H 1 6.84 0.03 . 1 . . . . . . . . 5065 1 574 . 1 1 91 91 TYR HE2 H 1 6.84 0.03 . 1 . . . . . . . . 5065 1 575 . 1 1 91 91 TYR CA C 13 61.84 0.50 . 1 . . . . . . . . 5065 1 576 . 1 1 91 91 TYR C C 13 177.10 0.50 . 1 . . . . . . . . 5065 1 577 . 1 1 91 91 TYR CB C 13 38.33 0.50 . 1 . . . . . . . . 5065 1 578 . 1 1 91 91 TYR CD1 C 13 133.27 0.50 . 1 . . . . . . . . 5065 1 579 . 1 1 91 91 TYR CD2 C 13 133.27 0.50 . 1 . . . . . . . . 5065 1 580 . 1 1 91 91 TYR N N 15 122.67 0.25 . 1 . . . . . . . . 5065 1 581 . 1 1 92 92 ALA H H 1 8.02 0.03 . 1 . . . . . . . . 5065 1 582 . 1 1 92 92 ALA HA H 1 4.06 0.03 . 1 . . . . . . . . 5065 1 583 . 1 1 92 92 ALA HB1 H 1 1.56 0.03 . 1 . . . . . . . . 5065 1 584 . 1 1 92 92 ALA HB2 H 1 1.56 0.03 . 1 . . . . . . . . 5065 1 585 . 1 1 92 92 ALA HB3 H 1 1.56 0.03 . 1 . . . . . . . . 5065 1 586 . 1 1 92 92 ALA CA C 13 54.66 0.50 . 1 . . . . . . . . 5065 1 587 . 1 1 92 92 ALA C C 13 174.64 0.50 . 1 . . . . . . . . 5065 1 588 . 1 1 92 92 ALA CB C 13 18.04 0.50 . 1 . . . . . . . . 5065 1 589 . 1 1 92 92 ALA N N 15 121.09 0.25 . 1 . . . . . . . . 5065 1 590 . 1 1 93 93 LYS H H 1 7.51 0.03 . 1 . . . . . . . . 5065 1 591 . 1 1 93 93 LYS HA H 1 3.95 0.03 . 1 . . . . . . . . 5065 1 592 . 1 1 93 93 LYS HB2 H 1 1.74 0.03 . 1 . . . . . . . . 5065 1 593 . 1 1 93 93 LYS HB3 H 1 1.74 0.03 . 1 . . . . . . . . 5065 1 594 . 1 1 93 93 LYS HD2 H 1 1.70 0.03 . 2 . . . . . . . . 5065 1 595 . 1 1 93 93 LYS HD3 H 1 1.62 0.03 . 2 . . . . . . . . 5065 1 596 . 1 1 93 93 LYS HG2 H 1 1.45 0.03 . 1 . . . . . . . . 5065 1 597 . 1 1 93 93 LYS HG3 H 1 1.45 0.03 . 1 . . . . . . . . 5065 1 598 . 1 1 93 93 LYS HE2 H 1 2.93 0.03 . 1 . . . . . . . . 5065 1 599 . 1 1 93 93 LYS HE3 H 1 2.93 0.03 . 1 . . . . . . . . 5065 1 600 . 1 1 93 93 LYS CA C 13 58.15 0.50 . 1 . . . . . . . . 5065 1 601 . 1 1 93 93 LYS C C 13 177.09 0.50 . 1 . . . . . . . . 5065 1 602 . 1 1 93 93 LYS CB C 13 32.99 0.50 . 1 . . . . . . . . 5065 1 603 . 1 1 93 93 LYS CG C 13 25.16 0.50 . 1 . . . . . . . . 5065 1 604 . 1 1 93 93 LYS CD C 13 29.15 0.50 . 1 . . . . . . . . 5065 1 605 . 1 1 93 93 LYS CE C 13 42.18 0.50 . 1 . . . . . . . . 5065 1 606 . 1 1 93 93 LYS N N 15 116.27 0.25 . 1 . . . . . . . . 5065 1 607 . 1 1 94 94 ASN H H 1 7.43 0.03 . 1 . . . . . . . . 5065 1 608 . 1 1 94 94 ASN HA H 1 3.89 0.03 . 1 . . . . . . . . 5065 1 609 . 1 1 94 94 ASN HB2 H 1 2.80 0.03 . 2 . . . . . . . . 5065 1 610 . 1 1 94 94 ASN HB3 H 1 2.68 0.03 . 2 . . . . . . . . 5065 1 611 . 1 1 94 94 ASN CA C 13 54.76 0.50 . 1 . . . . . . . . 5065 1 612 . 1 1 94 94 ASN C C 13 175.16 0.50 . 1 . . . . . . . . 5065 1 613 . 1 1 94 94 ASN CB C 13 39.08 0.50 . 1 . . . . . . . . 5065 1 614 . 1 1 94 94 ASN N N 15 114.76 0.25 . 1 . . . . . . . . 5065 1 615 . 1 1 95 95 PHE H H 1 8.05 0.03 . 1 . . . . . . . . 5065 1 616 . 1 1 95 95 PHE CA C 13 56.15 0.50 . 1 . . . . . . . . 5065 1 617 . 1 1 95 95 PHE C C 13 175.75 0.50 . 1 . . . . . . . . 5065 1 618 . 1 1 95 95 PHE CB C 13 39.09 0.50 . 1 . . . . . . . . 5065 1 619 . 1 1 95 95 PHE N N 15 117.33 0.25 . 1 . . . . . . . . 5065 1 620 . 1 1 96 96 GLY H H 1 7.56 0.03 . 1 . . . . . . . . 5065 1 621 . 1 1 96 96 GLY CA C 13 44.70 0.50 . 1 . . . . . . . . 5065 1 622 . 1 1 96 96 GLY C C 13 171.48 0.50 . 1 . . . . . . . . 5065 1 623 . 1 1 96 96 GLY N N 15 109.52 0.25 . 1 . . . . . . . . 5065 1 stop_ save_