data_17831 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17831 _Entry.Title ; 1H, 13C and 15N resonance assignments for oxidised and reduced nDsbD from Escherichia coli ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-08-04 _Entry.Accession_date 2011-08-04 _Entry.Last_release_date 2011-10-25 _Entry.Original_release_date 2011-10-25 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Despoina Mavridou . A.I. . 17831 2 Lukas Stelzl . S. . 17831 3 Stuart Ferguson . J. . 17831 4 Christina Redfield . . . 17831 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID . 1 'Department of Biochemistry, University of Oxford' . 17831 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17831 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 475 17831 '15N chemical shifts' 119 17831 '1H chemical shifts' 746 17831 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 . . 2011-10-25 2011-08-04 original author . 17831 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 17830 'reduced nDsbD' 17831 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17831 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 21543317 _Citation.Full_citation . _Citation.Title 'Oxidation state-dependent protein-protein interactions in disulfide cascades.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 286 _Citation.Journal_issue 28 _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 24943 _Citation.Page_last 24956 _Citation.Year 2011 _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 Despoina Mavridou . A.I. . 17831 1 2 Emmanuel Saridakis . . . 17831 1 3 Paraskevi Kritsiligkou . . . 17831 1 4 Alan Goddard . D. . 17831 1 5 Julie Stevens . M. . 17831 1 6 Stuart Ferguson . J. . 17831 1 7 Christina Redfield . . . 17831 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'E. coli DsbD' 17831 1 'NMR resonance assignments' 17831 1 oxidation/reduction 17831 1 'thiol:disulfide exchange reaction' 17831 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17831 _Assembly.ID 1 _Assembly.Name nDsbD-ox _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'N-terminal domain of DsbD' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 nDsbD-ox 1 $nDsbD-ox A . yes native no no . 'single polypeptide chain' 'this is the only component in the assembly' 17831 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 disulfide single . 1 nDsbD-ox 1 CYS 105 105 SG . 1 nDsbD-ox 1 CYS 111 111 SG . nDsbD-ox 103 CYS SG . nDsbD-ox 109 CYS SG 17831 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 1JPE . . X-ray 1.90 . . 17831 1 yes PDB 1L6P . . X-ray 1.65 . . 17831 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID oxidoreductase 17831 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_nDsbD-ox _Entity.Sf_category entity _Entity.Sf_framecode nDsbD-ox _Entity.Entry_ID 17831 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name nDsbD-ox _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 ; MDTLFDAPGRSQFVPADQAF AFDFQQNQHDLNLTWQIKDG YYLYRKQIRITPEHAKIADV QLPQGVWHEDEFYGKSEIYR DRLTLPVTINQASAGATLTV TYQGCADAGFCYPPETKTVP LSEVVANNAAPQPVGLVPR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq ; We use the following numbering at the N-terminus: M -1 D 0 T 1 L 2 etc Only assignments for residues from L2 to V132 are included in the deposition. ; _Entity.Polymer_author_seq_details 'Residues L2-V132 of the native sequence have been deposited. This is the N-terminal periplasmic domain of a membrane protein. The N-terminal residues MDT are a result of the cloning process. Residues G133-R137 remain after thrombin cleavage of the affinity tag.' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 139 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'N-terminal domain of DsbD' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 15604.5 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'contains C103-C109 disulfide bond' _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 17830 . nDsbD-red . . . . . 100.00 139 100.00 100.00 4.29e-98 . . . . 17831 1 2 no PDB 1JPE . "Crystal Structure Of Dsbd-Alpha; The N-Terminal Domain Of Dsbd" . . . . . 94.24 151 100.00 100.00 1.02e-91 . . . . 17831 1 3 no PDB 1JZD . "Dsbc-Dsbdalpha Complex" . . . . . 94.24 132 99.24 99.24 2.67e-90 . . . . 17831 1 4 no PDB 1L6P . "N-Terminal Of Dsbd (Residues 20-144) From E. Coli" . . . . . 89.21 125 100.00 100.00 2.51e-86 . . . . 17831 1 5 no PDB 1VRS . "Crystal Structure Of The Disulfide-Linked Complex Between The N- Terminal And C-Terminal Domain Of The Electron Transfer Cataly" . . . . . 95.68 143 97.74 98.50 1.47e-90 . . . . 17831 1 6 no PDB 1Z5Y . "Crystal Structure Of The Disulfide-linked Complex Between The N-terminal Domain Of The Electron Transfer Catalyst Dsbd And The " . . . . . 95.68 143 97.74 98.50 1.47e-90 . . . . 17831 1 7 no PDB 3PFU . "N-terminal Domain Of Thiol:disulfide Interchange Protein Dsbd In Its Reduced Form" . . . . . 100.00 139 100.00 100.00 4.29e-98 . . . . 17831 1 8 no DBJ BAB38540 . "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 95.68 565 96.99 97.74 1.10e-86 . . . . 17831 1 9 no DBJ BAE78138 . "fused thiol:disulfide interchange protein [Escherichia coli str. K12 substr. W3110]" . . . . . 95.68 565 98.50 99.25 3.73e-88 . . . . 17831 1 10 no DBJ BAG66862 . "fused thiol:disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O111:H-]" . . . . . 95.68 565 96.99 97.74 8.49e-87 . . . . 17831 1 11 no DBJ BAG79959 . "thiol:disulfide interchange protein [Escherichia coli SE11]" . . . . . 95.68 565 96.99 97.74 1.17e-86 . . . . 17831 1 12 no DBJ BAI28440 . "fused thiol: disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O26:H11 str. 11368]" . . . . . 95.68 565 96.99 97.74 1.55e-86 . . . . 17831 1 13 no EMBL CAA54781 . "disulphide isomerase like protein [Escherichia coli K-12]" . . . . . 53.96 489 98.67 100.00 4.80e-43 . . . . 17831 1 14 no EMBL CAA85375 . "inner membrane copper tolerance protein [Escherichia coli str. K-12 substr. W3110]" . . . . . 53.96 489 98.67 100.00 4.80e-43 . . . . 17831 1 15 no EMBL CAQ34485 . "DsbD[reduced] [Escherichia coli BL21(DE3)]" . . . . . 95.68 565 97.74 98.50 3.04e-87 . . . . 17831 1 16 no EMBL CAR01112 . "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli IAI1]" . . . . . 95.68 565 97.74 98.50 2.28e-87 . . . . 17831 1 17 no EMBL CAR05872 . "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli S88]" . . . . . 95.68 565 96.99 97.74 2.61e-86 . . . . 17831 1 18 no GB AAA97035 . "cycZ [Escherichia coli str. K-12 substr. MG1655]" . . . . . 95.68 565 98.50 99.25 3.73e-88 . . . . 17831 1 19 no GB AAC77096 . "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" . . . . . 95.68 565 98.50 99.25 3.73e-88 . . . . 17831 1 20 no GB AAG59335 . "thiol:disulfide interchange protein; copper tolerance [Escherichia coli O157:H7 str. EDL933]" . . . . . 95.68 565 96.99 97.74 1.10e-86 . . . . 17831 1 21 no GB AAN45708 . "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" . . . . . 95.68 565 96.99 97.74 2.75e-86 . . . . 17831 1 22 no GB AAN83640 . "Thiol:disulfide interchange protein dsbD precursor [Escherichia coli CFT073]" . . . . . 95.68 565 96.99 97.74 2.25e-86 . . . . 17831 1 23 no REF NP_313144 . "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 95.68 565 96.99 97.74 1.10e-86 . . . . 17831 1 24 no REF NP_418559 . "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" . . . . . 95.68 565 98.50 99.25 3.73e-88 . . . . 17831 1 25 no REF NP_710001 . "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" . . . . . 95.68 565 96.99 97.74 2.75e-86 . . . . 17831 1 26 no REF WP_000068901 . "thiol:disulfide interchange protein DsbD [Shigella sonnei]" . . . . . 95.68 565 96.99 97.74 1.63e-86 . . . . 17831 1 27 no REF WP_000068902 . "MULTISPECIES: thiol:disulfide interchange protein [Enterobacteriaceae]" . . . . . 95.68 565 96.99 97.74 1.80e-86 . . . . 17831 1 28 no SP P36655 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=C-type cytochrome biogenesis protein CycZ; AltName: Full=" . . . . . 95.68 565 98.50 99.25 3.73e-88 . . . . 17831 1 29 no SP P58162 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 95.68 565 96.99 97.74 1.10e-86 . . . . 17831 1 30 no SP Q0SXE3 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 95.68 565 97.74 98.50 2.28e-87 . . . . 17831 1 31 no SP Q0T9Q5 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 95.68 565 96.99 97.74 2.61e-86 . . . . 17831 1 32 no SP Q1R3C4 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 95.68 565 96.99 97.74 2.61e-86 . . . . 17831 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'thiol-disulfide oxidoreductase' 17831 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 -1 MET . 17831 1 2 0 ASP . 17831 1 3 1 THR . 17831 1 4 2 LEU . 17831 1 5 3 PHE . 17831 1 6 4 ASP . 17831 1 7 5 ALA . 17831 1 8 6 PRO . 17831 1 9 7 GLY . 17831 1 10 8 ARG . 17831 1 11 9 SER . 17831 1 12 10 GLN . 17831 1 13 11 PHE . 17831 1 14 12 VAL . 17831 1 15 13 PRO . 17831 1 16 14 ALA . 17831 1 17 15 ASP . 17831 1 18 16 GLN . 17831 1 19 17 ALA . 17831 1 20 18 PHE . 17831 1 21 19 ALA . 17831 1 22 20 PHE . 17831 1 23 21 ASP . 17831 1 24 22 PHE . 17831 1 25 23 GLN . 17831 1 26 24 GLN . 17831 1 27 25 ASN . 17831 1 28 26 GLN . 17831 1 29 27 HIS . 17831 1 30 28 ASP . 17831 1 31 29 LEU . 17831 1 32 30 ASN . 17831 1 33 31 LEU . 17831 1 34 32 THR . 17831 1 35 33 TRP . 17831 1 36 34 GLN . 17831 1 37 35 ILE . 17831 1 38 36 LYS . 17831 1 39 37 ASP . 17831 1 40 38 GLY . 17831 1 41 39 TYR . 17831 1 42 40 TYR . 17831 1 43 41 LEU . 17831 1 44 42 TYR . 17831 1 45 43 ARG . 17831 1 46 44 LYS . 17831 1 47 45 GLN . 17831 1 48 46 ILE . 17831 1 49 47 ARG . 17831 1 50 48 ILE . 17831 1 51 49 THR . 17831 1 52 50 PRO . 17831 1 53 51 GLU . 17831 1 54 52 HIS . 17831 1 55 53 ALA . 17831 1 56 54 LYS . 17831 1 57 55 ILE . 17831 1 58 56 ALA . 17831 1 59 57 ASP . 17831 1 60 58 VAL . 17831 1 61 59 GLN . 17831 1 62 60 LEU . 17831 1 63 61 PRO . 17831 1 64 62 GLN . 17831 1 65 63 GLY . 17831 1 66 64 VAL . 17831 1 67 65 TRP . 17831 1 68 66 HIS . 17831 1 69 67 GLU . 17831 1 70 68 ASP . 17831 1 71 69 GLU . 17831 1 72 70 PHE . 17831 1 73 71 TYR . 17831 1 74 72 GLY . 17831 1 75 73 LYS . 17831 1 76 74 SER . 17831 1 77 75 GLU . 17831 1 78 76 ILE . 17831 1 79 77 TYR . 17831 1 80 78 ARG . 17831 1 81 79 ASP . 17831 1 82 80 ARG . 17831 1 83 81 LEU . 17831 1 84 82 THR . 17831 1 85 83 LEU . 17831 1 86 84 PRO . 17831 1 87 85 VAL . 17831 1 88 86 THR . 17831 1 89 87 ILE . 17831 1 90 88 ASN . 17831 1 91 89 GLN . 17831 1 92 90 ALA . 17831 1 93 91 SER . 17831 1 94 92 ALA . 17831 1 95 93 GLY . 17831 1 96 94 ALA . 17831 1 97 95 THR . 17831 1 98 96 LEU . 17831 1 99 97 THR . 17831 1 100 98 VAL . 17831 1 101 99 THR . 17831 1 102 100 TYR . 17831 1 103 101 GLN . 17831 1 104 102 GLY . 17831 1 105 103 CYS . 17831 1 106 104 ALA . 17831 1 107 105 ASP . 17831 1 108 106 ALA . 17831 1 109 107 GLY . 17831 1 110 108 PHE . 17831 1 111 109 CYS . 17831 1 112 110 TYR . 17831 1 113 111 PRO . 17831 1 114 112 PRO . 17831 1 115 113 GLU . 17831 1 116 114 THR . 17831 1 117 115 LYS . 17831 1 118 116 THR . 17831 1 119 117 VAL . 17831 1 120 118 PRO . 17831 1 121 119 LEU . 17831 1 122 120 SER . 17831 1 123 121 GLU . 17831 1 124 122 VAL . 17831 1 125 123 VAL . 17831 1 126 124 ALA . 17831 1 127 125 ASN . 17831 1 128 126 ASN . 17831 1 129 127 ALA . 17831 1 130 128 ALA . 17831 1 131 129 PRO . 17831 1 132 130 GLN . 17831 1 133 131 PRO . 17831 1 134 132 VAL . 17831 1 135 133 GLY . 17831 1 136 134 LEU . 17831 1 137 135 VAL . 17831 1 138 136 PRO . 17831 1 139 137 ARG . 17831 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 17831 1 . ASP 2 2 17831 1 . THR 3 3 17831 1 . LEU 4 4 17831 1 . PHE 5 5 17831 1 . ASP 6 6 17831 1 . ALA 7 7 17831 1 . PRO 8 8 17831 1 . GLY 9 9 17831 1 . ARG 10 10 17831 1 . SER 11 11 17831 1 . GLN 12 12 17831 1 . PHE 13 13 17831 1 . VAL 14 14 17831 1 . PRO 15 15 17831 1 . ALA 16 16 17831 1 . ASP 17 17 17831 1 . GLN 18 18 17831 1 . ALA 19 19 17831 1 . PHE 20 20 17831 1 . ALA 21 21 17831 1 . PHE 22 22 17831 1 . ASP 23 23 17831 1 . PHE 24 24 17831 1 . GLN 25 25 17831 1 . GLN 26 26 17831 1 . ASN 27 27 17831 1 . GLN 28 28 17831 1 . HIS 29 29 17831 1 . ASP 30 30 17831 1 . LEU 31 31 17831 1 . ASN 32 32 17831 1 . LEU 33 33 17831 1 . THR 34 34 17831 1 . TRP 35 35 17831 1 . GLN 36 36 17831 1 . ILE 37 37 17831 1 . LYS 38 38 17831 1 . ASP 39 39 17831 1 . GLY 40 40 17831 1 . TYR 41 41 17831 1 . TYR 42 42 17831 1 . LEU 43 43 17831 1 . TYR 44 44 17831 1 . ARG 45 45 17831 1 . LYS 46 46 17831 1 . GLN 47 47 17831 1 . ILE 48 48 17831 1 . ARG 49 49 17831 1 . ILE 50 50 17831 1 . THR 51 51 17831 1 . PRO 52 52 17831 1 . GLU 53 53 17831 1 . HIS 54 54 17831 1 . ALA 55 55 17831 1 . LYS 56 56 17831 1 . ILE 57 57 17831 1 . ALA 58 58 17831 1 . ASP 59 59 17831 1 . VAL 60 60 17831 1 . GLN 61 61 17831 1 . LEU 62 62 17831 1 . PRO 63 63 17831 1 . GLN 64 64 17831 1 . GLY 65 65 17831 1 . VAL 66 66 17831 1 . TRP 67 67 17831 1 . HIS 68 68 17831 1 . GLU 69 69 17831 1 . ASP 70 70 17831 1 . GLU 71 71 17831 1 . PHE 72 72 17831 1 . TYR 73 73 17831 1 . GLY 74 74 17831 1 . LYS 75 75 17831 1 . SER 76 76 17831 1 . GLU 77 77 17831 1 . ILE 78 78 17831 1 . TYR 79 79 17831 1 . ARG 80 80 17831 1 . ASP 81 81 17831 1 . ARG 82 82 17831 1 . LEU 83 83 17831 1 . THR 84 84 17831 1 . LEU 85 85 17831 1 . PRO 86 86 17831 1 . VAL 87 87 17831 1 . THR 88 88 17831 1 . ILE 89 89 17831 1 . ASN 90 90 17831 1 . GLN 91 91 17831 1 . ALA 92 92 17831 1 . SER 93 93 17831 1 . ALA 94 94 17831 1 . GLY 95 95 17831 1 . ALA 96 96 17831 1 . THR 97 97 17831 1 . LEU 98 98 17831 1 . THR 99 99 17831 1 . VAL 100 100 17831 1 . THR 101 101 17831 1 . TYR 102 102 17831 1 . GLN 103 103 17831 1 . GLY 104 104 17831 1 . CYS 105 105 17831 1 . ALA 106 106 17831 1 . ASP 107 107 17831 1 . ALA 108 108 17831 1 . GLY 109 109 17831 1 . PHE 110 110 17831 1 . CYS 111 111 17831 1 . TYR 112 112 17831 1 . PRO 113 113 17831 1 . PRO 114 114 17831 1 . GLU 115 115 17831 1 . THR 116 116 17831 1 . LYS 117 117 17831 1 . THR 118 118 17831 1 . VAL 119 119 17831 1 . PRO 120 120 17831 1 . LEU 121 121 17831 1 . SER 122 122 17831 1 . GLU 123 123 17831 1 . VAL 124 124 17831 1 . VAL 125 125 17831 1 . ALA 126 126 17831 1 . ASN 127 127 17831 1 . ASN 128 128 17831 1 . ALA 129 129 17831 1 . ALA 130 130 17831 1 . PRO 131 131 17831 1 . GLN 132 132 17831 1 . PRO 133 133 17831 1 . VAL 134 134 17831 1 . GLY 135 135 17831 1 . LEU 136 136 17831 1 . VAL 137 137 17831 1 . PRO 138 138 17831 1 . ARG 139 139 17831 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 17831 _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 $nDsbD-ox . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli K12 . . . . . . . . . . . . . . . dsbd . 'Located in the periplasm' . . 17831 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 17831 _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 $nDsbD-ox . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . pET22b(+) . . . . . . 17831 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17831 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 nDsbD-ox '[U-98% 15N]' . . 1 $nDsbD-ox . . . 0.5 1.0 mM . . . . 17831 1 2 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17831 1 3 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17831 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 17831 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 nDsbD-ox '[U-98% 13C; U-98% 15N]' . . 1 $nDsbD-ox . . . 0.5 1.0 mM . . . . 17831 2 2 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17831 2 3 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17831 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 17831 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0 . M 17831 1 pH 6.5 . pH 17831 1 pressure 1 . atm 17831 1 temperature 298 . K 17831 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 17831 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 17831 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17831 1 stop_ save_ save_CcpNMR _Software.Sf_category software _Software.Sf_framecode CcpNMR _Software.Entry_ID 17831 _Software.ID 2 _Software.Name CcpNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 17831 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17831 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 17831 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'home-built spectrometer with triple-axis gradient probe' _NMR_spectrometer.Manufacturer home-built _NMR_spectrometer.Model 'home-built using GE Omega software' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 17831 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details 'with TCI CryoProbe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 17831 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 home-built 'home-built using GE Omega software' . 750 'home-built spectrometer with triple-axis gradient probe' . . 17831 1 2 spectrometer_2 Bruker Avance . 500 'with TCI CryoProbe' . . 17831 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 17831 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 2 '2D 1H-15N HSQC NH2 only' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 3 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 4 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 5 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 6 '3D HNCO' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 7 '3D HNCA' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 8 '3D HCCH-TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 9 '3D CBCA(CO)NH' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17831 1 10 '3D HBHA(CO)NH' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17831 1 11 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17831 1 12 '3D HN(CA)CO' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17831 1 13 '3D 1H-15N HSQC-NOESY-HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17831 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 17831 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details 'Water was used as the reference for 1H (4.75 ppm at 298K). The gamma ratios were used for 13C and 15N.' loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 water protons . . . . ppm 4.75 internal indirect 0.251449530 . . . . . . . . . 17831 1 H 1 water protons . . . . ppm 4.75 internal direct 1.0 . . . . . . . . . 17831 1 N 15 water protons . . . . ppm 4.75 internal indirect 0.101329118 . . . . . . . . . 17831 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17831 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.2 _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 'estimate from digital resolution' _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 6 '3D HNCO' . . . 17831 1 7 '3D HNCA' . . . 17831 1 8 '3D HCCH-TOCSY' . . . 17831 1 9 '3D CBCA(CO)NH' . . . 17831 1 10 '3D HBHA(CO)NH' . . . 17831 1 11 '2D 1H-15N HSQC' . . . 17831 1 12 '3D HN(CA)CO' . . . 17831 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 4 4 LEU H H 1 8.236 0.02 . 1 . . . . 2 Leu H . 17831 1 2 . 1 1 4 4 LEU HA H 1 4.274 0.02 . 1 . . . . 2 Leu HA . 17831 1 3 . 1 1 4 4 LEU HB2 H 1 1.488 0.02 . 2 . . . . 2 Leu HB2 . 17831 1 4 . 1 1 4 4 LEU HB3 H 1 1.413 0.02 . 2 . . . . 2 Leu HB3 . 17831 1 5 . 1 1 4 4 LEU HG H 1 1.452 0.02 . 1 . . . . 2 Leu HG . 17831 1 6 . 1 1 4 4 LEU HD11 H 1 0.810 0.02 . 2 . . . . 2 Leu HD1 . 17831 1 7 . 1 1 4 4 LEU HD12 H 1 0.810 0.02 . 2 . . . . 2 Leu HD1 . 17831 1 8 . 1 1 4 4 LEU HD13 H 1 0.810 0.02 . 2 . . . . 2 Leu HD1 . 17831 1 9 . 1 1 4 4 LEU HD21 H 1 0.828 0.02 . 2 . . . . 2 Leu HD2 . 17831 1 10 . 1 1 4 4 LEU HD22 H 1 0.828 0.02 . 2 . . . . 2 Leu HD2 . 17831 1 11 . 1 1 4 4 LEU HD23 H 1 0.828 0.02 . 2 . . . . 2 Leu HD2 . 17831 1 12 . 1 1 4 4 LEU C C 13 177.014 0.2 . 1 . . . . 2 Leu C . 17831 1 13 . 1 1 4 4 LEU CA C 13 55.390 0.2 . 1 . . . . 2 Leu CA . 17831 1 14 . 1 1 4 4 LEU CB C 13 42.266 0.2 . 1 . . . . 2 Leu CB . 17831 1 15 . 1 1 4 4 LEU CG C 13 27.153 0.2 . 1 . . . . 2 Leu CG . 17831 1 16 . 1 1 4 4 LEU CD1 C 13 23.674 0.2 . 2 . . . . 2 Leu CD1 . 17831 1 17 . 1 1 4 4 LEU CD2 C 13 24.684 0.2 . 2 . . . . 2 Leu CD2 . 17831 1 18 . 1 1 4 4 LEU N N 15 124.176 0.2 . 1 . . . . 2 Leu N . 17831 1 19 . 1 1 5 5 PHE H H 1 8.089 0.02 . 1 . . . . 3 Phe H . 17831 1 20 . 1 1 5 5 PHE HA H 1 4.560 0.02 . 1 . . . . 3 Phe HA . 17831 1 21 . 1 1 5 5 PHE HB2 H 1 3.142 0.02 . 2 . . . . 3 Phe HB2 . 17831 1 22 . 1 1 5 5 PHE HB3 H 1 2.956 0.02 . 2 . . . . 3 Phe HB3 . 17831 1 23 . 1 1 5 5 PHE C C 13 175.235 0.2 . 1 . . . . 3 Phe C . 17831 1 24 . 1 1 5 5 PHE CA C 13 57.813 0.2 . 1 . . . . 3 Phe CA . 17831 1 25 . 1 1 5 5 PHE CB C 13 39.584 0.2 . 1 . . . . 3 Phe CB . 17831 1 26 . 1 1 5 5 PHE N N 15 120.128 0.2 . 1 . . . . 3 Phe N . 17831 1 27 . 1 1 6 6 ASP H H 1 8.140 0.02 . 1 . . . . 4 Asp H . 17831 1 28 . 1 1 6 6 ASP HA H 1 4.543 0.02 . 1 . . . . 4 Asp HA . 17831 1 29 . 1 1 6 6 ASP HB2 H 1 2.545 0.02 . 2 . . . . 4 Asp HB2 . 17831 1 30 . 1 1 6 6 ASP HB3 H 1 2.572 0.02 . 2 . . . . 4 Asp HB3 . 17831 1 31 . 1 1 6 6 ASP C C 13 175.172 0.2 . 1 . . . . 4 Asp C . 17831 1 32 . 1 1 6 6 ASP CA C 13 53.869 0.2 . 1 . . . . 4 Asp CA . 17831 1 33 . 1 1 6 6 ASP CB C 13 41.587 0.2 . 1 . . . . 4 Asp CB . 17831 1 34 . 1 1 6 6 ASP N N 15 121.390 0.2 . 1 . . . . 4 Asp N . 17831 1 35 . 1 1 7 7 ALA H H 1 7.957 0.02 . 1 . . . . 5 Ala H . 17831 1 36 . 1 1 7 7 ALA HA H 1 4.513 0.02 . 1 . . . . 5 Ala HA . 17831 1 37 . 1 1 7 7 ALA HB1 H 1 1.327 0.02 . 1 . . . . 5 Ala HB . 17831 1 38 . 1 1 7 7 ALA HB2 H 1 1.327 0.02 . 1 . . . . 5 Ala HB . 17831 1 39 . 1 1 7 7 ALA HB3 H 1 1.327 0.02 . 1 . . . . 5 Ala HB . 17831 1 40 . 1 1 7 7 ALA CA C 13 50.819 0.2 . 1 . . . . 5 Ala CA . 17831 1 41 . 1 1 7 7 ALA CB C 13 18.080 0.2 . 1 . . . . 5 Ala CB . 17831 1 42 . 1 1 7 7 ALA N N 15 124.903 0.2 . 1 . . . . 5 Ala N . 17831 1 43 . 1 1 8 8 PRO HA H 1 4.391 0.02 . 1 . . . . 6 Pro HA . 17831 1 44 . 1 1 8 8 PRO HB2 H 1 2.259 0.02 . 2 . . . . 6 Pro HB2 . 17831 1 45 . 1 1 8 8 PRO HB3 H 1 1.906 0.02 . 2 . . . . 6 Pro HB3 . 17831 1 46 . 1 1 8 8 PRO C C 13 177.842 0.2 . 1 . . . . 6 Pro C . 17831 1 47 . 1 1 8 8 PRO CA C 13 63.825 0.2 . 1 . . . . 6 Pro CA . 17831 1 48 . 1 1 8 8 PRO CB C 13 31.932 0.2 . 1 . . . . 6 Pro CB . 17831 1 49 . 1 1 9 9 GLY H H 1 8.469 0.02 . 1 . . . . 7 Gly H . 17831 1 50 . 1 1 9 9 GLY HA2 H 1 3.931 0.02 . 1 . . . . 7 Gly HA2 . 17831 1 51 . 1 1 9 9 GLY HA3 H 1 3.931 0.02 . 1 . . . . 7 Gly HA3 . 17831 1 52 . 1 1 9 9 GLY C C 13 174.460 0.2 . 1 . . . . 7 Gly C . 17831 1 53 . 1 1 9 9 GLY CA C 13 45.345 0.2 . 1 . . . . 7 Gly CA . 17831 1 54 . 1 1 9 9 GLY N N 15 109.130 0.2 . 1 . . . . 7 Gly N . 17831 1 55 . 1 1 10 10 ARG H H 1 8.035 0.02 . 1 . . . . 8 Arg H . 17831 1 56 . 1 1 10 10 ARG HA H 1 4.292 0.02 . 1 . . . . 8 Arg HA . 17831 1 57 . 1 1 10 10 ARG HB2 H 1 1.857 0.02 . 2 . . . . 8 Arg HB2 . 17831 1 58 . 1 1 10 10 ARG HB3 H 1 1.756 0.02 . 2 . . . . 8 Arg HB3 . 17831 1 59 . 1 1 10 10 ARG HG2 H 1 1.567 0.02 . 1 . . . . 8 Arg HG2 . 17831 1 60 . 1 1 10 10 ARG HG3 H 1 1.567 0.02 . 1 . . . . 8 Arg HG3 . 17831 1 61 . 1 1 10 10 ARG HD2 H 1 3.127 0.02 . 1 . . . . 8 Arg HD2 . 17831 1 62 . 1 1 10 10 ARG HD3 H 1 3.127 0.02 . 1 . . . . 8 Arg HD3 . 17831 1 63 . 1 1 10 10 ARG C C 13 176.513 0.2 . 1 . . . . 8 Arg C . 17831 1 64 . 1 1 10 10 ARG CA C 13 56.317 0.2 . 1 . . . . 8 Arg CA . 17831 1 65 . 1 1 10 10 ARG CB C 13 30.737 0.2 . 1 . . . . 8 Arg CB . 17831 1 66 . 1 1 10 10 ARG CG C 13 26.990 0.2 . 1 . . . . 8 Arg CG . 17831 1 67 . 1 1 10 10 ARG CD C 13 43.336 0.2 . 1 . . . . 8 Arg CD . 17831 1 68 . 1 1 10 10 ARG N N 15 120.311 0.2 . 1 . . . . 8 Arg N . 17831 1 69 . 1 1 11 11 SER H H 1 8.262 0.02 . 1 . . . . 9 Ser H . 17831 1 70 . 1 1 11 11 SER HA H 1 4.346 0.02 . 1 . . . . 9 Ser HA . 17831 1 71 . 1 1 11 11 SER HB2 H 1 3.794 0.02 . 1 . . . . 9 Ser HB2 . 17831 1 72 . 1 1 11 11 SER HB3 H 1 3.794 0.02 . 1 . . . . 9 Ser HB3 . 17831 1 73 . 1 1 11 11 SER C C 13 174.279 0.2 . 1 . . . . 9 Ser C . 17831 1 74 . 1 1 11 11 SER CA C 13 58.699 0.2 . 1 . . . . 9 Ser CA . 17831 1 75 . 1 1 11 11 SER CB C 13 63.690 0.2 . 1 . . . . 9 Ser CB . 17831 1 76 . 1 1 11 11 SER N N 15 116.336 0.2 . 1 . . . . 9 Ser N . 17831 1 77 . 1 1 12 12 GLN H H 1 8.218 0.02 . 1 . . . . 10 Gln H . 17831 1 78 . 1 1 12 12 GLN HA H 1 4.187 0.02 . 1 . . . . 10 Gln HA . 17831 1 79 . 1 1 12 12 GLN HB2 H 1 1.758 0.02 . 2 . . . . 10 Gln HB2 . 17831 1 80 . 1 1 12 12 GLN HB3 H 1 1.841 0.02 . 2 . . . . 10 Gln HB3 . 17831 1 81 . 1 1 12 12 GLN HG2 H 1 2.040 0.02 . 2 . . . . 10 Gln HG2 . 17831 1 82 . 1 1 12 12 GLN HG3 H 1 2.124 0.02 . 2 . . . . 10 Gln HG3 . 17831 1 83 . 1 1 12 12 GLN C C 13 175.168 0.2 . 1 . . . . 10 Gln C . 17831 1 84 . 1 1 12 12 GLN CA C 13 55.908 0.2 . 1 . . . . 10 Gln CA . 17831 1 85 . 1 1 12 12 GLN CB C 13 29.354 0.2 . 1 . . . . 10 Gln CB . 17831 1 86 . 1 1 12 12 GLN CG C 13 33.649 0.2 . 1 . . . . 10 Gln CG . 17831 1 87 . 1 1 12 12 GLN N N 15 121.278 0.2 . 1 . . . . 10 Gln N . 17831 1 88 . 1 1 13 13 PHE H H 1 7.953 0.02 . 1 . . . . 11 Phe H . 17831 1 89 . 1 1 13 13 PHE HA H 1 4.638 0.02 . 1 . . . . 11 Phe HA . 17831 1 90 . 1 1 13 13 PHE HB2 H 1 3.175 0.02 . 2 . . . . 11 Phe HB2 . 17831 1 91 . 1 1 13 13 PHE HB3 H 1 2.763 0.02 . 2 . . . . 11 Phe HB3 . 17831 1 92 . 1 1 13 13 PHE C C 13 175.349 0.2 . 1 . . . . 11 Phe C . 17831 1 93 . 1 1 13 13 PHE CA C 13 57.624 0.2 . 1 . . . . 11 Phe CA . 17831 1 94 . 1 1 13 13 PHE CB C 13 39.555 0.2 . 1 . . . . 11 Phe CB . 17831 1 95 . 1 1 13 13 PHE N N 15 121.433 0.2 . 1 . . . . 11 Phe N . 17831 1 96 . 1 1 14 14 VAL H H 1 7.691 0.02 . 1 . . . . 12 Val H . 17831 1 97 . 1 1 14 14 VAL HA H 1 4.409 0.02 . 1 . . . . 12 Val HA . 17831 1 98 . 1 1 14 14 VAL HB H 1 2.055 0.02 . 1 . . . . 12 Val HB . 17831 1 99 . 1 1 14 14 VAL HG11 H 1 0.921 0.02 . 2 . . . . 12 Val HG1 . 17831 1 100 . 1 1 14 14 VAL HG12 H 1 0.921 0.02 . 2 . . . . 12 Val HG1 . 17831 1 101 . 1 1 14 14 VAL HG13 H 1 0.921 0.02 . 2 . . . . 12 Val HG1 . 17831 1 102 . 1 1 14 14 VAL HG21 H 1 0.948 0.02 . 2 . . . . 12 Val HG2 . 17831 1 103 . 1 1 14 14 VAL HG22 H 1 0.948 0.02 . 2 . . . . 12 Val HG2 . 17831 1 104 . 1 1 14 14 VAL HG23 H 1 0.948 0.02 . 2 . . . . 12 Val HG2 . 17831 1 105 . 1 1 14 14 VAL C C 13 173.459 0.2 . 1 . . . . 12 Val C . 17831 1 106 . 1 1 14 14 VAL CA C 13 59.502 0.2 . 1 . . . . 12 Val CA . 17831 1 107 . 1 1 14 14 VAL CB C 13 32.858 0.2 . 1 . . . . 12 Val CB . 17831 1 108 . 1 1 14 14 VAL CG1 C 13 20.337 0.2 . 2 . . . . 12 Val CG1 . 17831 1 109 . 1 1 14 14 VAL CG2 C 13 21.010 0.2 . 2 . . . . 12 Val CG2 . 17831 1 110 . 1 1 14 14 VAL N N 15 120.895 0.2 . 1 . . . . 12 Val N . 17831 1 111 . 1 1 15 15 PRO HA H 1 4.547 0.02 . 1 . . . . 13 Pro HA . 17831 1 112 . 1 1 15 15 PRO HB2 H 1 1.898 0.02 . 2 . . . . 13 Pro HB2 . 17831 1 113 . 1 1 15 15 PRO HB3 H 1 2.507 0.02 . 2 . . . . 13 Pro HB3 . 17831 1 114 . 1 1 15 15 PRO C C 13 177.382 0.2 . 1 . . . . 13 Pro C . 17831 1 115 . 1 1 15 15 PRO CA C 13 63.129 0.2 . 1 . . . . 13 Pro CA . 17831 1 116 . 1 1 15 15 PRO CB C 13 32.550 0.2 . 1 . . . . 13 Pro CB . 17831 1 117 . 1 1 16 16 ALA H H 1 9.227 0.02 . 1 . . . . 14 Ala H . 17831 1 118 . 1 1 16 16 ALA HA H 1 3.331 0.02 . 1 . . . . 14 Ala HA . 17831 1 119 . 1 1 16 16 ALA HB1 H 1 1.409 0.02 . 1 . . . . 14 Ala HB . 17831 1 120 . 1 1 16 16 ALA HB2 H 1 1.409 0.02 . 1 . . . . 14 Ala HB . 17831 1 121 . 1 1 16 16 ALA HB3 H 1 1.409 0.02 . 1 . . . . 14 Ala HB . 17831 1 122 . 1 1 16 16 ALA C C 13 178.440 0.2 . 1 . . . . 14 Ala C . 17831 1 123 . 1 1 16 16 ALA CA C 13 55.928 0.2 . 1 . . . . 14 Ala CA . 17831 1 124 . 1 1 16 16 ALA CB C 13 18.185 0.2 . 1 . . . . 14 Ala CB . 17831 1 125 . 1 1 16 16 ALA N N 15 126.708 0.2 . 1 . . . . 14 Ala N . 17831 1 126 . 1 1 17 17 ASP H H 1 8.450 0.02 . 1 . . . . 15 Asp H . 17831 1 127 . 1 1 17 17 ASP HA H 1 4.447 0.02 . 1 . . . . 15 Asp HA . 17831 1 128 . 1 1 17 17 ASP HB2 H 1 2.604 0.02 . 2 . . . . 15 Asp HB2 . 17831 1 129 . 1 1 17 17 ASP HB3 H 1 2.766 0.02 . 2 . . . . 15 Asp HB3 . 17831 1 130 . 1 1 17 17 ASP C C 13 176.599 0.2 . 1 . . . . 15 Asp C . 17831 1 131 . 1 1 17 17 ASP CA C 13 56.386 0.2 . 1 . . . . 15 Asp CA . 17831 1 132 . 1 1 17 17 ASP CB C 13 40.264 0.2 . 1 . . . . 15 Asp CB . 17831 1 133 . 1 1 17 17 ASP N N 15 112.545 0.2 . 1 . . . . 15 Asp N . 17831 1 134 . 1 1 18 18 GLN H H 1 7.447 0.02 . 1 . . . . 16 Gln H . 17831 1 135 . 1 1 18 18 GLN HA H 1 4.154 0.02 . 1 . . . . 16 Gln HA . 17831 1 136 . 1 1 18 18 GLN HB2 H 1 1.754 0.02 . 2 . . . . 16 Gln HB2 . 17831 1 137 . 1 1 18 18 GLN HB3 H 1 1.901 0.02 . 2 . . . . 16 Gln HB3 . 17831 1 138 . 1 1 18 18 GLN HG2 H 1 2.234 0.02 . 2 . . . . 16 Gln HG2 . 17831 1 139 . 1 1 18 18 GLN HG3 H 1 2.309 0.02 . 2 . . . . 16 Gln HG3 . 17831 1 140 . 1 1 18 18 GLN C C 13 176.326 0.2 . 1 . . . . 16 Gln C . 17831 1 141 . 1 1 18 18 GLN CA C 13 56.392 0.2 . 1 . . . . 16 Gln CA . 17831 1 142 . 1 1 18 18 GLN CB C 13 29.400 0.2 . 1 . . . . 16 Gln CB . 17831 1 143 . 1 1 18 18 GLN CG C 13 33.990 0.2 . 1 . . . . 16 Gln CG . 17831 1 144 . 1 1 18 18 GLN N N 15 115.386 0.2 . 1 . . . . 16 Gln N . 17831 1 145 . 1 1 19 19 ALA H H 1 7.199 0.02 . 1 . . . . 17 Ala H . 17831 1 146 . 1 1 19 19 ALA HA H 1 3.079 0.02 . 1 . . . . 17 Ala HA . 17831 1 147 . 1 1 19 19 ALA HB1 H 1 -0.326 0.02 . 1 . . . . 17 Ala HB . 17831 1 148 . 1 1 19 19 ALA HB2 H 1 -0.326 0.02 . 1 . . . . 17 Ala HB . 17831 1 149 . 1 1 19 19 ALA HB3 H 1 -0.326 0.02 . 1 . . . . 17 Ala HB . 17831 1 150 . 1 1 19 19 ALA C C 13 175.480 0.2 . 1 . . . . 17 Ala C . 17831 1 151 . 1 1 19 19 ALA CA C 13 54.002 0.2 . 1 . . . . 17 Ala CA . 17831 1 152 . 1 1 19 19 ALA CB C 13 17.158 0.2 . 1 . . . . 17 Ala CB . 17831 1 153 . 1 1 19 19 ALA N N 15 123.409 0.2 . 1 . . . . 17 Ala N . 17831 1 154 . 1 1 20 20 PHE H H 1 7.857 0.02 . 1 . . . . 18 Phe H . 17831 1 155 . 1 1 20 20 PHE HA H 1 4.929 0.02 . 1 . . . . 18 Phe HA . 17831 1 156 . 1 1 20 20 PHE HB2 H 1 2.713 0.02 . 2 . . . . 18 Phe HB2 . 17831 1 157 . 1 1 20 20 PHE HB3 H 1 3.396 0.02 . 2 . . . . 18 Phe HB3 . 17831 1 158 . 1 1 20 20 PHE C C 13 173.305 0.2 . 1 . . . . 18 Phe C . 17831 1 159 . 1 1 20 20 PHE CA C 13 53.285 0.2 . 1 . . . . 18 Phe CA . 17831 1 160 . 1 1 20 20 PHE CB C 13 39.220 0.2 . 1 . . . . 18 Phe CB . 17831 1 161 . 1 1 20 20 PHE N N 15 114.612 0.2 . 1 . . . . 18 Phe N . 17831 1 162 . 1 1 21 21 ALA H H 1 8.147 0.02 . 1 . . . . 19 Ala H . 17831 1 163 . 1 1 21 21 ALA HA H 1 4.643 0.02 . 1 . . . . 19 Ala HA . 17831 1 164 . 1 1 21 21 ALA HB1 H 1 1.362 0.02 . 1 . . . . 19 Ala HB . 17831 1 165 . 1 1 21 21 ALA HB2 H 1 1.362 0.02 . 1 . . . . 19 Ala HB . 17831 1 166 . 1 1 21 21 ALA HB3 H 1 1.362 0.02 . 1 . . . . 19 Ala HB . 17831 1 167 . 1 1 21 21 ALA C C 13 176.407 0.2 . 1 . . . . 19 Ala C . 17831 1 168 . 1 1 21 21 ALA CA C 13 52.243 0.2 . 1 . . . . 19 Ala CA . 17831 1 169 . 1 1 21 21 ALA CB C 13 18.968 0.2 . 1 . . . . 19 Ala CB . 17831 1 170 . 1 1 21 21 ALA N N 15 126.059 0.2 . 1 . . . . 19 Ala N . 17831 1 171 . 1 1 22 22 PHE H H 1 8.705 0.02 . 1 . . . . 20 Phe H . 17831 1 172 . 1 1 22 22 PHE HA H 1 4.964 0.02 . 1 . . . . 20 Phe HA . 17831 1 173 . 1 1 22 22 PHE HB2 H 1 2.640 0.02 . 2 . . . . 20 Phe HB2 . 17831 1 174 . 1 1 22 22 PHE HB3 H 1 2.755 0.02 . 2 . . . . 20 Phe HB3 . 17831 1 175 . 1 1 22 22 PHE C C 13 174.090 0.2 . 1 . . . . 20 Phe C . 17831 1 176 . 1 1 22 22 PHE CA C 13 56.604 0.2 . 1 . . . . 20 Phe CA . 17831 1 177 . 1 1 22 22 PHE CB C 13 42.173 0.2 . 1 . . . . 20 Phe CB . 17831 1 178 . 1 1 22 22 PHE N N 15 128.991 0.2 . 1 . . . . 20 Phe N . 17831 1 179 . 1 1 23 23 ASP H H 1 8.340 0.02 . 1 . . . . 21 Asp H . 17831 1 180 . 1 1 23 23 ASP HA H 1 4.235 0.02 . 1 . . . . 21 Asp HA . 17831 1 181 . 1 1 23 23 ASP HB2 H 1 2.116 0.02 . 2 . . . . 21 Asp HB2 . 17831 1 182 . 1 1 23 23 ASP HB3 H 1 2.268 0.02 . 2 . . . . 21 Asp HB3 . 17831 1 183 . 1 1 23 23 ASP C C 13 171.316 0.2 . 1 . . . . 21 Asp C . 17831 1 184 . 1 1 23 23 ASP CA C 13 52.537 0.2 . 1 . . . . 21 Asp CA . 17831 1 185 . 1 1 23 23 ASP CB C 13 44.688 0.2 . 1 . . . . 21 Asp CB . 17831 1 186 . 1 1 23 23 ASP N N 15 128.388 0.2 . 1 . . . . 21 Asp N . 17831 1 187 . 1 1 24 24 PHE H H 1 7.593 0.02 . 1 . . . . 22 Phe H . 17831 1 188 . 1 1 24 24 PHE HA H 1 5.293 0.02 . 1 . . . . 22 Phe HA . 17831 1 189 . 1 1 24 24 PHE HB2 H 1 2.562 0.02 . 1 . . . . 22 Phe HB2 . 17831 1 190 . 1 1 24 24 PHE HB3 H 1 2.562 0.02 . 1 . . . . 22 Phe HB3 . 17831 1 191 . 1 1 24 24 PHE C C 13 173.586 0.2 . 1 . . . . 22 Phe C . 17831 1 192 . 1 1 24 24 PHE CA C 13 55.105 0.2 . 1 . . . . 22 Phe CA . 17831 1 193 . 1 1 24 24 PHE CB C 13 42.804 0.2 . 1 . . . . 22 Phe CB . 17831 1 194 . 1 1 24 24 PHE N N 15 112.739 0.2 . 1 . . . . 22 Phe N . 17831 1 195 . 1 1 25 25 GLN H H 1 8.059 0.02 . 1 . . . . 23 Gln H . 17831 1 196 . 1 1 25 25 GLN HA H 1 4.334 0.02 . 1 . . . . 23 Gln HA . 17831 1 197 . 1 1 25 25 GLN HB2 H 1 1.889 0.02 . 1 . . . . 23 Gln HB2 . 17831 1 198 . 1 1 25 25 GLN HB3 H 1 1.889 0.02 . 1 . . . . 23 Gln HB3 . 17831 1 199 . 1 1 25 25 GLN HG2 H 1 2.172 0.02 . 2 . . . . 23 Gln HG2 . 17831 1 200 . 1 1 25 25 GLN HG3 H 1 2.086 0.02 . 2 . . . . 23 Gln HG3 . 17831 1 201 . 1 1 25 25 GLN C C 13 173.922 0.2 . 1 . . . . 23 Gln C . 17831 1 202 . 1 1 25 25 GLN CA C 13 55.689 0.2 . 1 . . . . 23 Gln CA . 17831 1 203 . 1 1 25 25 GLN CB C 13 32.305 0.2 . 1 . . . . 23 Gln CB . 17831 1 204 . 1 1 25 25 GLN CG C 13 33.315 0.2 . 1 . . . . 23 Gln CG . 17831 1 205 . 1 1 25 25 GLN N N 15 116.827 0.2 . 1 . . . . 23 Gln N . 17831 1 206 . 1 1 26 26 GLN H H 1 9.378 0.02 . 1 . . . . 24 Gln H . 17831 1 207 . 1 1 26 26 GLN HA H 1 5.006 0.02 . 1 . . . . 24 Gln HA . 17831 1 208 . 1 1 26 26 GLN HB2 H 1 1.837 0.02 . 2 . . . . 24 Gln HB2 . 17831 1 209 . 1 1 26 26 GLN HB3 H 1 2.078 0.02 . 2 . . . . 24 Gln HB3 . 17831 1 210 . 1 1 26 26 GLN HG2 H 1 2.375 0.02 . 2 . . . . 24 Gln HG2 . 17831 1 211 . 1 1 26 26 GLN HG3 H 1 2.115 0.02 . 2 . . . . 24 Gln HG3 . 17831 1 212 . 1 1 26 26 GLN C C 13 174.265 0.2 . 1 . . . . 24 Gln C . 17831 1 213 . 1 1 26 26 GLN CA C 13 54.342 0.2 . 1 . . . . 24 Gln CA . 17831 1 214 . 1 1 26 26 GLN CB C 13 30.712 0.2 . 1 . . . . 24 Gln CB . 17831 1 215 . 1 1 26 26 GLN CG C 13 32.784 0.2 . 1 . . . . 24 Gln CG . 17831 1 216 . 1 1 26 26 GLN N N 15 128.881 0.2 . 1 . . . . 24 Gln N . 17831 1 217 . 1 1 27 27 ASN H H 1 9.170 0.02 . 1 . . . . 25 Asn H . 17831 1 218 . 1 1 27 27 ASN HA H 1 4.801 0.02 . 1 . . . . 25 Asn HA . 17831 1 219 . 1 1 27 27 ASN HB2 H 1 2.869 0.02 . 2 . . . . 25 Asn HB2 . 17831 1 220 . 1 1 27 27 ASN HB3 H 1 2.631 0.02 . 2 . . . . 25 Asn HB3 . 17831 1 221 . 1 1 27 27 ASN C C 13 174.356 0.2 . 1 . . . . 25 Asn C . 17831 1 222 . 1 1 27 27 ASN CA C 13 52.522 0.2 . 1 . . . . 25 Asn CA . 17831 1 223 . 1 1 27 27 ASN CB C 13 39.326 0.2 . 1 . . . . 25 Asn CB . 17831 1 224 . 1 1 27 27 ASN N N 15 126.141 0.2 . 1 . . . . 25 Asn N . 17831 1 225 . 1 1 28 28 GLN H H 1 9.410 0.02 . 1 . . . . 26 Gln H . 17831 1 226 . 1 1 28 28 GLN HA H 1 3.603 0.02 . 1 . . . . 26 Gln HA . 17831 1 227 . 1 1 28 28 GLN HB2 H 1 2.466 0.02 . 2 . . . . 26 Gln HB2 . 17831 1 228 . 1 1 28 28 GLN HB3 H 1 2.086 0.02 . 2 . . . . 26 Gln HB3 . 17831 1 229 . 1 1 28 28 GLN HG2 H 1 2.313 0.02 . 2 . . . . 26 Gln HG2 . 17831 1 230 . 1 1 28 28 GLN HG3 H 1 2.436 0.02 . 2 . . . . 26 Gln HG3 . 17831 1 231 . 1 1 28 28 GLN C C 13 174.479 0.2 . 1 . . . . 26 Gln C . 17831 1 232 . 1 1 28 28 GLN CA C 13 58.453 0.2 . 1 . . . . 26 Gln CA . 17831 1 233 . 1 1 28 28 GLN CB C 13 26.593 0.2 . 1 . . . . 26 Gln CB . 17831 1 234 . 1 1 28 28 GLN CG C 13 34.081 0.2 . 1 . . . . 26 Gln CG . 17831 1 235 . 1 1 28 28 GLN N N 15 122.178 0.2 . 1 . . . . 26 Gln N . 17831 1 236 . 1 1 29 29 HIS H H 1 8.209 0.02 . 1 . . . . 27 His H . 17831 1 237 . 1 1 29 29 HIS HA H 1 4.493 0.02 . 1 . . . . 27 His HA . 17831 1 238 . 1 1 29 29 HIS HB2 H 1 3.385 0.02 . 1 . . . . 27 His HB2 . 17831 1 239 . 1 1 29 29 HIS HB3 H 1 3.385 0.02 . 1 . . . . 27 His HB3 . 17831 1 240 . 1 1 29 29 HIS C C 13 173.691 0.2 . 1 . . . . 27 His C . 17831 1 241 . 1 1 29 29 HIS CA C 13 57.798 0.2 . 1 . . . . 27 His CA . 17831 1 242 . 1 1 29 29 HIS CB C 13 29.145 0.2 . 1 . . . . 27 His CB . 17831 1 243 . 1 1 29 29 HIS N N 15 117.893 0.2 . 1 . . . . 27 His N . 17831 1 244 . 1 1 30 30 ASP H H 1 7.997 0.02 . 1 . . . . 28 Asp H . 17831 1 245 . 1 1 30 30 ASP HA H 1 4.999 0.02 . 1 . . . . 28 Asp HA . 17831 1 246 . 1 1 30 30 ASP HB2 H 1 2.662 0.02 . 1 . . . . 28 Asp HB2 . 17831 1 247 . 1 1 30 30 ASP HB3 H 1 2.662 0.02 . 1 . . . . 28 Asp HB3 . 17831 1 248 . 1 1 30 30 ASP C C 13 173.831 0.2 . 1 . . . . 28 Asp C . 17831 1 249 . 1 1 30 30 ASP CA C 13 54.394 0.2 . 1 . . . . 28 Asp CA . 17831 1 250 . 1 1 30 30 ASP CB C 13 42.294 0.2 . 1 . . . . 28 Asp CB . 17831 1 251 . 1 1 30 30 ASP N N 15 118.632 0.2 . 1 . . . . 28 Asp N . 17831 1 252 . 1 1 31 31 LEU H H 1 8.726 0.02 . 1 . . . . 29 Leu H . 17831 1 253 . 1 1 31 31 LEU HA H 1 5.080 0.02 . 1 . . . . 29 Leu HA . 17831 1 254 . 1 1 31 31 LEU HB2 H 1 1.932 0.02 . 2 . . . . 29 Leu HB2 . 17831 1 255 . 1 1 31 31 LEU HB3 H 1 1.129 0.02 . 2 . . . . 29 Leu HB3 . 17831 1 256 . 1 1 31 31 LEU HG H 1 1.292 0.02 . 1 . . . . 29 Leu HG . 17831 1 257 . 1 1 31 31 LEU HD11 H 1 0.660 0.02 . 2 . . . . 29 Leu HD1 . 17831 1 258 . 1 1 31 31 LEU HD12 H 1 0.660 0.02 . 2 . . . . 29 Leu HD1 . 17831 1 259 . 1 1 31 31 LEU HD13 H 1 0.660 0.02 . 2 . . . . 29 Leu HD1 . 17831 1 260 . 1 1 31 31 LEU HD21 H 1 0.742 0.02 . 2 . . . . 29 Leu HD2 . 17831 1 261 . 1 1 31 31 LEU HD22 H 1 0.742 0.02 . 2 . . . . 29 Leu HD2 . 17831 1 262 . 1 1 31 31 LEU HD23 H 1 0.742 0.02 . 2 . . . . 29 Leu HD2 . 17831 1 263 . 1 1 31 31 LEU C C 13 173.752 0.2 . 1 . . . . 29 Leu C . 17831 1 264 . 1 1 31 31 LEU CA C 13 53.165 0.2 . 1 . . . . 29 Leu CA . 17831 1 265 . 1 1 31 31 LEU CB C 13 44.832 0.2 . 1 . . . . 29 Leu CB . 17831 1 266 . 1 1 31 31 LEU CG C 13 27.378 0.2 . 1 . . . . 29 Leu CG . 17831 1 267 . 1 1 31 31 LEU CD1 C 13 27.715 0.2 . 2 . . . . 29 Leu CD1 . 17831 1 268 . 1 1 31 31 LEU CD2 C 13 24.347 0.2 . 2 . . . . 29 Leu CD2 . 17831 1 269 . 1 1 31 31 LEU N N 15 126.747 0.2 . 1 . . . . 29 Leu N . 17831 1 270 . 1 1 32 32 ASN H H 1 8.781 0.02 . 1 . . . . 30 Asn H . 17831 1 271 . 1 1 32 32 ASN HA H 1 5.314 0.02 . 1 . . . . 30 Asn HA . 17831 1 272 . 1 1 32 32 ASN HB2 H 1 2.534 0.02 . 2 . . . . 30 Asn HB2 . 17831 1 273 . 1 1 32 32 ASN HB3 H 1 2.303 0.02 . 2 . . . . 30 Asn HB3 . 17831 1 274 . 1 1 32 32 ASN C C 13 174.294 0.2 . 1 . . . . 30 Asn C . 17831 1 275 . 1 1 32 32 ASN CA C 13 52.467 0.2 . 1 . . . . 30 Asn CA . 17831 1 276 . 1 1 32 32 ASN CB C 13 41.323 0.2 . 1 . . . . 30 Asn CB . 17831 1 277 . 1 1 32 32 ASN N N 15 124.808 0.2 . 1 . . . . 30 Asn N . 17831 1 278 . 1 1 33 33 LEU H H 1 8.346 0.02 . 1 . . . . 31 Leu H . 17831 1 279 . 1 1 33 33 LEU HA H 1 4.561 0.02 . 1 . . . . 31 Leu HA . 17831 1 280 . 1 1 33 33 LEU HB2 H 1 1.068 0.02 . 2 . . . . 31 Leu HB2 . 17831 1 281 . 1 1 33 33 LEU HB3 H 1 2.170 0.02 . 2 . . . . 31 Leu HB3 . 17831 1 282 . 1 1 33 33 LEU HG H 1 1.699 0.02 . 1 . . . . 31 Leu HG . 17831 1 283 . 1 1 33 33 LEU HD11 H 1 0.839 0.02 . 2 . . . . 31 Leu HD1 . 17831 1 284 . 1 1 33 33 LEU HD12 H 1 0.839 0.02 . 2 . . . . 31 Leu HD1 . 17831 1 285 . 1 1 33 33 LEU HD13 H 1 0.839 0.02 . 2 . . . . 31 Leu HD1 . 17831 1 286 . 1 1 33 33 LEU HD21 H 1 0.939 0.02 . 2 . . . . 31 Leu HD2 . 17831 1 287 . 1 1 33 33 LEU HD22 H 1 0.939 0.02 . 2 . . . . 31 Leu HD2 . 17831 1 288 . 1 1 33 33 LEU HD23 H 1 0.939 0.02 . 2 . . . . 31 Leu HD2 . 17831 1 289 . 1 1 33 33 LEU C C 13 175.007 0.2 . 1 . . . . 31 Leu C . 17831 1 290 . 1 1 33 33 LEU CA C 13 53.190 0.2 . 1 . . . . 31 Leu CA . 17831 1 291 . 1 1 33 33 LEU CB C 13 43.140 0.2 . 1 . . . . 31 Leu CB . 17831 1 292 . 1 1 33 33 LEU CG C 13 26.705 0.2 . 1 . . . . 31 Leu CG . 17831 1 293 . 1 1 33 33 LEU CD1 C 13 24.010 0.2 . 2 . . . . 31 Leu CD1 . 17831 1 294 . 1 1 33 33 LEU CD2 C 13 27.042 0.2 . 2 . . . . 31 Leu CD2 . 17831 1 295 . 1 1 33 33 LEU N N 15 125.200 0.2 . 1 . . . . 31 Leu N . 17831 1 296 . 1 1 34 34 THR H H 1 8.325 0.02 . 1 . . . . 32 Thr H . 17831 1 297 . 1 1 34 34 THR HA H 1 5.469 0.02 . 1 . . . . 32 Thr HA . 17831 1 298 . 1 1 34 34 THR HB H 1 3.700 0.02 . 1 . . . . 32 Thr HB . 17831 1 299 . 1 1 34 34 THR HG21 H 1 0.933 0.02 . 1 . . . . 32 Thr HG2 . 17831 1 300 . 1 1 34 34 THR HG22 H 1 0.933 0.02 . 1 . . . . 32 Thr HG2 . 17831 1 301 . 1 1 34 34 THR HG23 H 1 0.933 0.02 . 1 . . . . 32 Thr HG2 . 17831 1 302 . 1 1 34 34 THR C C 13 172.040 0.2 . 1 . . . . 32 Thr C . 17831 1 303 . 1 1 34 34 THR CA C 13 60.367 0.2 . 1 . . . . 32 Thr CA . 17831 1 304 . 1 1 34 34 THR CB C 13 71.968 0.2 . 1 . . . . 32 Thr CB . 17831 1 305 . 1 1 34 34 THR CG2 C 13 24.674 0.2 . 1 . . . . 32 Thr CG2 . 17831 1 306 . 1 1 34 34 THR N N 15 115.837 0.2 . 1 . . . . 32 Thr N . 17831 1 307 . 1 1 35 35 TRP H H 1 9.368 0.02 . 1 . . . . 33 Trp H . 17831 1 308 . 1 1 35 35 TRP HA H 1 5.395 0.02 . 1 . . . . 33 Trp HA . 17831 1 309 . 1 1 35 35 TRP HB2 H 1 2.456 0.02 . 2 . . . . 33 Trp HB2 . 17831 1 310 . 1 1 35 35 TRP HB3 H 1 2.951 0.02 . 2 . . . . 33 Trp HB3 . 17831 1 311 . 1 1 35 35 TRP HE1 H 1 5.661 0.02 . 1 . . . . 33 Trp HE1 . 17831 1 312 . 1 1 35 35 TRP C C 13 175.739 0.2 . 1 . . . . 33 Trp C . 17831 1 313 . 1 1 35 35 TRP CA C 13 57.512 0.2 . 1 . . . . 33 Trp CA . 17831 1 314 . 1 1 35 35 TRP CB C 13 34.024 0.2 . 1 . . . . 33 Trp CB . 17831 1 315 . 1 1 35 35 TRP N N 15 122.333 0.2 . 1 . . . . 33 Trp N . 17831 1 316 . 1 1 35 35 TRP NE1 N 15 121.647 0.2 . 1 . . . . 33 Trp NE1 . 17831 1 317 . 1 1 36 36 GLN H H 1 8.830 0.02 . 1 . . . . 34 Gln H . 17831 1 318 . 1 1 36 36 GLN HA H 1 4.640 0.02 . 1 . . . . 34 Gln HA . 17831 1 319 . 1 1 36 36 GLN HB2 H 1 1.946 0.02 . 2 . . . . 34 Gln HB2 . 17831 1 320 . 1 1 36 36 GLN HB3 H 1 2.112 0.02 . 2 . . . . 34 Gln HB3 . 17831 1 321 . 1 1 36 36 GLN HG2 H 1 2.272 0.02 . 1 . . . . 34 Gln HG2 . 17831 1 322 . 1 1 36 36 GLN HG3 H 1 2.272 0.02 . 1 . . . . 34 Gln HG3 . 17831 1 323 . 1 1 36 36 GLN C C 13 175.440 0.2 . 1 . . . . 34 Gln C . 17831 1 324 . 1 1 36 36 GLN CA C 13 55.157 0.2 . 1 . . . . 34 Gln CA . 17831 1 325 . 1 1 36 36 GLN CB C 13 29.209 0.2 . 1 . . . . 34 Gln CB . 17831 1 326 . 1 1 36 36 GLN CG C 13 33.251 0.2 . 1 . . . . 34 Gln CG . 17831 1 327 . 1 1 36 36 GLN N N 15 122.652 0.2 . 1 . . . . 34 Gln N . 17831 1 328 . 1 1 37 37 ILE H H 1 8.485 0.02 . 1 . . . . 35 Ile H . 17831 1 329 . 1 1 37 37 ILE HA H 1 4.661 0.02 . 1 . . . . 35 Ile HA . 17831 1 330 . 1 1 37 37 ILE HB H 1 1.807 0.02 . 1 . . . . 35 Ile HB . 17831 1 331 . 1 1 37 37 ILE HG12 H 1 0.684 0.02 . 2 . . . . 35 Ile HG12 . 17831 1 332 . 1 1 37 37 ILE HG13 H 1 1.520 0.02 . 2 . . . . 35 Ile HG13 . 17831 1 333 . 1 1 37 37 ILE HG21 H 1 1.103 0.02 . 1 . . . . 35 Ile HG2 . 17831 1 334 . 1 1 37 37 ILE HG22 H 1 1.103 0.02 . 1 . . . . 35 Ile HG2 . 17831 1 335 . 1 1 37 37 ILE HG23 H 1 1.103 0.02 . 1 . . . . 35 Ile HG2 . 17831 1 336 . 1 1 37 37 ILE HD11 H 1 0.544 0.02 . 1 . . . . 35 Ile HD1 . 17831 1 337 . 1 1 37 37 ILE HD12 H 1 0.544 0.02 . 1 . . . . 35 Ile HD1 . 17831 1 338 . 1 1 37 37 ILE HD13 H 1 0.544 0.02 . 1 . . . . 35 Ile HD1 . 17831 1 339 . 1 1 37 37 ILE C C 13 175.064 0.2 . 1 . . . . 35 Ile C . 17831 1 340 . 1 1 37 37 ILE CA C 13 61.046 0.2 . 1 . . . . 35 Ile CA . 17831 1 341 . 1 1 37 37 ILE CB C 13 38.598 0.2 . 1 . . . . 35 Ile CB . 17831 1 342 . 1 1 37 37 ILE CG1 C 13 27.979 0.2 . 1 . . . . 35 Ile CG1 . 17831 1 343 . 1 1 37 37 ILE CG2 C 13 18.839 0.2 . 1 . . . . 35 Ile CG2 . 17831 1 344 . 1 1 37 37 ILE CD1 C 13 14.028 0.2 . 1 . . . . 35 Ile CD1 . 17831 1 345 . 1 1 37 37 ILE N N 15 130.017 0.2 . 1 . . . . 35 Ile N . 17831 1 346 . 1 1 38 38 LYS H H 1 8.662 0.02 . 1 . . . . 36 Lys H . 17831 1 347 . 1 1 38 38 LYS HA H 1 4.059 0.02 . 1 . . . . 36 Lys HA . 17831 1 348 . 1 1 38 38 LYS HB2 H 1 1.472 0.02 . 2 . . . . 36 Lys HB2 . 17831 1 349 . 1 1 38 38 LYS HB3 H 1 1.639 0.02 . 2 . . . . 36 Lys HB3 . 17831 1 350 . 1 1 38 38 LYS HG2 H 1 1.622 0.02 . 2 . . . . 36 Lys HG2 . 17831 1 351 . 1 1 38 38 LYS HG3 H 1 1.764 0.02 . 2 . . . . 36 Lys HG3 . 17831 1 352 . 1 1 38 38 LYS HD2 H 1 1.368 0.02 . 2 . . . . 36 Lys HD2 . 17831 1 353 . 1 1 38 38 LYS HD3 H 1 1.368 0.02 . 2 . . . . 36 Lys HD3 . 17831 1 354 . 1 1 38 38 LYS HE2 H 1 3.027 0.02 . 2 . . . . 36 Lys HE2 . 17831 1 355 . 1 1 38 38 LYS HE3 H 1 3.046 0.02 . 2 . . . . 36 Lys HE3 . 17831 1 356 . 1 1 38 38 LYS C C 13 175.420 0.2 . 1 . . . . 36 Lys C . 17831 1 357 . 1 1 38 38 LYS CA C 13 57.452 0.2 . 1 . . . . 36 Lys CA . 17831 1 358 . 1 1 38 38 LYS CB C 13 33.566 0.2 . 1 . . . . 36 Lys CB . 17831 1 359 . 1 1 38 38 LYS CG C 13 24.674 0.2 . 1 . . . . 36 Lys CG . 17831 1 360 . 1 1 38 38 LYS CD C 13 29.389 0.2 . 1 . . . . 36 Lys CD . 17831 1 361 . 1 1 38 38 LYS CE C 13 41.830 0.2 . 1 . . . . 36 Lys CE . 17831 1 362 . 1 1 38 38 LYS N N 15 131.135 0.2 . 1 . . . . 36 Lys N . 17831 1 363 . 1 1 39 39 ASP H H 1 8.450 0.02 . 1 . . . . 37 Asp H . 17831 1 364 . 1 1 39 39 ASP HA H 1 4.635 0.02 . 1 . . . . 37 Asp HA . 17831 1 365 . 1 1 39 39 ASP HB2 H 1 2.783 0.02 . 2 . . . . 37 Asp HB2 . 17831 1 366 . 1 1 39 39 ASP HB3 H 1 2.728 0.02 . 2 . . . . 37 Asp HB3 . 17831 1 367 . 1 1 39 39 ASP C C 13 177.466 0.2 . 1 . . . . 37 Asp C . 17831 1 368 . 1 1 39 39 ASP CA C 13 56.646 0.2 . 1 . . . . 37 Asp CA . 17831 1 369 . 1 1 39 39 ASP CB C 13 41.298 0.2 . 1 . . . . 37 Asp CB . 17831 1 370 . 1 1 39 39 ASP N N 15 124.591 0.2 . 1 . . . . 37 Asp N . 17831 1 371 . 1 1 40 40 GLY H H 1 9.183 0.02 . 1 . . . . 38 Gly H . 17831 1 372 . 1 1 40 40 GLY HA2 H 1 4.225 0.02 . 2 . . . . 38 Gly HA2 . 17831 1 373 . 1 1 40 40 GLY HA3 H 1 3.875 0.02 . 2 . . . . 38 Gly HA3 . 17831 1 374 . 1 1 40 40 GLY C C 13 173.908 0.2 . 1 . . . . 38 Gly C . 17831 1 375 . 1 1 40 40 GLY CA C 13 44.952 0.2 . 1 . . . . 38 Gly CA . 17831 1 376 . 1 1 40 40 GLY N N 15 112.948 0.2 . 1 . . . . 38 Gly N . 17831 1 377 . 1 1 41 41 TYR H H 1 8.234 0.02 . 1 . . . . 39 Tyr H . 17831 1 378 . 1 1 41 41 TYR HA H 1 5.214 0.02 . 1 . . . . 39 Tyr HA . 17831 1 379 . 1 1 41 41 TYR HB2 H 1 3.002 0.02 . 2 . . . . 39 Tyr HB2 . 17831 1 380 . 1 1 41 41 TYR HB3 H 1 2.848 0.02 . 2 . . . . 39 Tyr HB3 . 17831 1 381 . 1 1 41 41 TYR C C 13 173.851 0.2 . 1 . . . . 39 Tyr C . 17831 1 382 . 1 1 41 41 TYR CA C 13 56.804 0.2 . 1 . . . . 39 Tyr CA . 17831 1 383 . 1 1 41 41 TYR CB C 13 40.409 0.2 . 1 . . . . 39 Tyr CB . 17831 1 384 . 1 1 41 41 TYR N N 15 120.577 0.2 . 1 . . . . 39 Tyr N . 17831 1 385 . 1 1 42 42 TYR H H 1 8.657 0.02 . 1 . . . . 40 Tyr H . 17831 1 386 . 1 1 42 42 TYR HA H 1 5.382 0.02 . 1 . . . . 40 Tyr HA . 17831 1 387 . 1 1 42 42 TYR HB2 H 1 2.619 0.02 . 2 . . . . 40 Tyr HB2 . 17831 1 388 . 1 1 42 42 TYR HB3 H 1 2.741 0.02 . 2 . . . . 40 Tyr HB3 . 17831 1 389 . 1 1 42 42 TYR C C 13 173.424 0.2 . 1 . . . . 40 Tyr C . 17831 1 390 . 1 1 42 42 TYR CA C 13 56.243 0.2 . 1 . . . . 40 Tyr CA . 17831 1 391 . 1 1 42 42 TYR CB C 13 41.661 0.2 . 1 . . . . 40 Tyr CB . 17831 1 392 . 1 1 42 42 TYR N N 15 113.026 0.2 . 1 . . . . 40 Tyr N . 17831 1 393 . 1 1 43 43 LEU H H 1 8.483 0.02 . 1 . . . . 41 Leu H . 17831 1 394 . 1 1 43 43 LEU HA H 1 4.623 0.02 . 1 . . . . 41 Leu HA . 17831 1 395 . 1 1 43 43 LEU HB2 H 1 1.196 0.02 . 2 . . . . 41 Leu HB2 . 17831 1 396 . 1 1 43 43 LEU HB3 H 1 1.391 0.02 . 2 . . . . 41 Leu HB3 . 17831 1 397 . 1 1 43 43 LEU HG H 1 1.212 0.02 . 1 . . . . 41 Leu HG . 17831 1 398 . 1 1 43 43 LEU HD11 H 1 -0.209 0.02 . 2 . . . . 41 Leu HD1 . 17831 1 399 . 1 1 43 43 LEU HD12 H 1 -0.209 0.02 . 2 . . . . 41 Leu HD1 . 17831 1 400 . 1 1 43 43 LEU HD13 H 1 -0.209 0.02 . 2 . . . . 41 Leu HD1 . 17831 1 401 . 1 1 43 43 LEU HD21 H 1 -0.157 0.02 . 2 . . . . 41 Leu HD2 . 17831 1 402 . 1 1 43 43 LEU HD22 H 1 -0.157 0.02 . 2 . . . . 41 Leu HD2 . 17831 1 403 . 1 1 43 43 LEU HD23 H 1 -0.157 0.02 . 2 . . . . 41 Leu HD2 . 17831 1 404 . 1 1 43 43 LEU C C 13 177.781 0.2 . 1 . . . . 41 Leu C . 17831 1 405 . 1 1 43 43 LEU CA C 13 52.636 0.2 . 1 . . . . 41 Leu CA . 17831 1 406 . 1 1 43 43 LEU CB C 13 46.745 0.2 . 1 . . . . 41 Leu CB . 17831 1 407 . 1 1 43 43 LEU CG C 13 26.347 0.2 . 1 . . . . 41 Leu CG . 17831 1 408 . 1 1 43 43 LEU CD1 C 13 24.497 0.2 . 2 . . . . 41 Leu CD1 . 17831 1 409 . 1 1 43 43 LEU CD2 C 13 23.421 0.2 . 2 . . . . 41 Leu CD2 . 17831 1 410 . 1 1 43 43 LEU N N 15 116.234 0.2 . 1 . . . . 41 Leu N . 17831 1 411 . 1 1 44 44 TYR H H 1 7.666 0.02 . 1 . . . . 42 Tyr H . 17831 1 412 . 1 1 44 44 TYR HA H 1 4.675 0.02 . 1 . . . . 42 Tyr HA . 17831 1 413 . 1 1 44 44 TYR HB2 H 1 2.540 0.02 . 2 . . . . 42 Tyr HB2 . 17831 1 414 . 1 1 44 44 TYR HB3 H 1 3.082 0.02 . 2 . . . . 42 Tyr HB3 . 17831 1 415 . 1 1 44 44 TYR C C 13 176.864 0.2 . 1 . . . . 42 Tyr C . 17831 1 416 . 1 1 44 44 TYR CA C 13 58.081 0.2 . 1 . . . . 42 Tyr CA . 17831 1 417 . 1 1 44 44 TYR CB C 13 39.895 0.2 . 1 . . . . 42 Tyr CB . 17831 1 418 . 1 1 44 44 TYR N N 15 116.762 0.2 . 1 . . . . 42 Tyr N . 17831 1 419 . 1 1 45 45 ARG H H 1 8.243 0.02 . 1 . . . . 43 Arg H . 17831 1 420 . 1 1 45 45 ARG HA H 1 3.917 0.02 . 1 . . . . 43 Arg HA . 17831 1 421 . 1 1 45 45 ARG HB2 H 1 1.342 0.02 . 2 . . . . 43 Arg HB2 . 17831 1 422 . 1 1 45 45 ARG HB3 H 1 0.657 0.02 . 2 . . . . 43 Arg HB3 . 17831 1 423 . 1 1 45 45 ARG HD2 H 1 2.804 0.02 . 2 . . . . 43 Arg HD2 . 17831 1 424 . 1 1 45 45 ARG HD3 H 1 2.658 0.02 . 2 . . . . 43 Arg HD3 . 17831 1 425 . 1 1 45 45 ARG C C 13 177.621 0.2 . 1 . . . . 43 Arg C . 17831 1 426 . 1 1 45 45 ARG CA C 13 60.182 0.2 . 1 . . . . 43 Arg CA . 17831 1 427 . 1 1 45 45 ARG CB C 13 30.625 0.2 . 1 . . . . 43 Arg CB . 17831 1 428 . 1 1 45 45 ARG CD C 13 43.763 0.2 . 1 . . . . 43 Arg CD . 17831 1 429 . 1 1 45 45 ARG N N 15 127.112 0.2 . 1 . . . . 43 Arg N . 17831 1 430 . 1 1 46 46 LYS H H 1 9.110 0.02 . 1 . . . . 44 Lys H . 17831 1 431 . 1 1 46 46 LYS HA H 1 4.116 0.02 . 1 . . . . 44 Lys HA . 17831 1 432 . 1 1 46 46 LYS HB2 H 1 1.776 0.02 . 2 . . . . 44 Lys HB2 . 17831 1 433 . 1 1 46 46 LYS HB3 H 1 1.773 0.02 . 2 . . . . 44 Lys HB3 . 17831 1 434 . 1 1 46 46 LYS HG2 H 1 1.359 0.02 . 2 . . . . 44 Lys HG2 . 17831 1 435 . 1 1 46 46 LYS HG3 H 1 1.369 0.02 . 2 . . . . 44 Lys HG3 . 17831 1 436 . 1 1 46 46 LYS HD2 H 1 1.579 0.02 . 1 . . . . 44 Lys HD2 . 17831 1 437 . 1 1 46 46 LYS HD3 H 1 1.579 0.02 . 1 . . . . 44 Lys HD3 . 17831 1 438 . 1 1 46 46 LYS HE2 H 1 2.790 0.02 . 2 . . . . 44 Lys HE2 . 17831 1 439 . 1 1 46 46 LYS HE3 H 1 2.796 0.02 . 2 . . . . 44 Lys HE3 . 17831 1 440 . 1 1 46 46 LYS C C 13 176.300 0.2 . 1 . . . . 44 Lys C . 17831 1 441 . 1 1 46 46 LYS CA C 13 57.824 0.2 . 1 . . . . 44 Lys CA . 17831 1 442 . 1 1 46 46 LYS CB C 13 31.983 0.2 . 1 . . . . 44 Lys CB . 17831 1 443 . 1 1 46 46 LYS CG C 13 25.174 0.2 . 1 . . . . 44 Lys CG . 17831 1 444 . 1 1 46 46 LYS CD C 13 28.878 0.2 . 1 . . . . 44 Lys CD . 17831 1 445 . 1 1 46 46 LYS CE C 13 41.857 0.2 . 1 . . . . 44 Lys CE . 17831 1 446 . 1 1 46 46 LYS N N 15 113.180 0.2 . 1 . . . . 44 Lys N . 17831 1 447 . 1 1 47 47 GLN H H 1 6.605 0.02 . 1 . . . . 45 Gln H . 17831 1 448 . 1 1 47 47 GLN HA H 1 4.525 0.02 . 1 . . . . 45 Gln HA . 17831 1 449 . 1 1 47 47 GLN HB2 H 1 1.956 0.02 . 2 . . . . 45 Gln HB2 . 17831 1 450 . 1 1 47 47 GLN HB3 H 1 2.507 0.02 . 2 . . . . 45 Gln HB3 . 17831 1 451 . 1 1 47 47 GLN C C 13 174.943 0.2 . 1 . . . . 45 Gln C . 17831 1 452 . 1 1 47 47 GLN CA C 13 54.087 0.2 . 1 . . . . 45 Gln CA . 17831 1 453 . 1 1 47 47 GLN CB C 13 29.549 0.2 . 1 . . . . 45 Gln CB . 17831 1 454 . 1 1 47 47 GLN N N 15 112.785 0.2 . 1 . . . . 45 Gln N . 17831 1 455 . 1 1 48 48 ILE H H 1 6.865 0.02 . 1 . . . . 46 Ile H . 17831 1 456 . 1 1 48 48 ILE HA H 1 4.852 0.02 . 1 . . . . 46 Ile HA . 17831 1 457 . 1 1 48 48 ILE HB H 1 1.815 0.02 . 1 . . . . 46 Ile HB . 17831 1 458 . 1 1 48 48 ILE HG12 H 1 0.794 0.02 . 2 . . . . 46 Ile HG12 . 17831 1 459 . 1 1 48 48 ILE HG13 H 1 1.798 0.02 . 2 . . . . 46 Ile HG13 . 17831 1 460 . 1 1 48 48 ILE HG21 H 1 0.781 0.02 . 1 . . . . 46 Ile HG2 . 17831 1 461 . 1 1 48 48 ILE HG22 H 1 0.781 0.02 . 1 . . . . 46 Ile HG2 . 17831 1 462 . 1 1 48 48 ILE HG23 H 1 0.781 0.02 . 1 . . . . 46 Ile HG2 . 17831 1 463 . 1 1 48 48 ILE HD11 H 1 0.461 0.02 . 1 . . . . 46 Ile HD1 . 17831 1 464 . 1 1 48 48 ILE HD12 H 1 0.461 0.02 . 1 . . . . 46 Ile HD1 . 17831 1 465 . 1 1 48 48 ILE HD13 H 1 0.461 0.02 . 1 . . . . 46 Ile HD1 . 17831 1 466 . 1 1 48 48 ILE C C 13 176.040 0.2 . 1 . . . . 46 Ile C . 17831 1 467 . 1 1 48 48 ILE CA C 13 61.841 0.2 . 1 . . . . 46 Ile CA . 17831 1 468 . 1 1 48 48 ILE CB C 13 37.687 0.2 . 1 . . . . 46 Ile CB . 17831 1 469 . 1 1 48 48 ILE CG1 C 13 28.010 0.2 . 1 . . . . 46 Ile CG1 . 17831 1 470 . 1 1 48 48 ILE CG2 C 13 16.705 0.2 . 1 . . . . 46 Ile CG2 . 17831 1 471 . 1 1 48 48 ILE CD1 C 13 13.680 0.2 . 1 . . . . 46 Ile CD1 . 17831 1 472 . 1 1 48 48 ILE N N 15 119.118 0.2 . 1 . . . . 46 Ile N . 17831 1 473 . 1 1 49 49 ARG H H 1 8.868 0.02 . 1 . . . . 47 Arg H . 17831 1 474 . 1 1 49 49 ARG HA H 1 4.677 0.02 . 1 . . . . 47 Arg HA . 17831 1 475 . 1 1 49 49 ARG HB2 H 1 1.634 0.02 . 2 . . . . 47 Arg HB2 . 17831 1 476 . 1 1 49 49 ARG HB3 H 1 1.734 0.02 . 2 . . . . 47 Arg HB3 . 17831 1 477 . 1 1 49 49 ARG HG2 H 1 1.499 0.02 . 2 . . . . 47 Arg HG2 . 17831 1 478 . 1 1 49 49 ARG HG3 H 1 1.525 0.02 . 2 . . . . 47 Arg HG3 . 17831 1 479 . 1 1 49 49 ARG HD2 H 1 3.120 0.02 . 2 . . . . 47 Arg HD2 . 17831 1 480 . 1 1 49 49 ARG HD3 H 1 3.187 0.02 . 2 . . . . 47 Arg HD3 . 17831 1 481 . 1 1 49 49 ARG C C 13 174.557 0.2 . 1 . . . . 47 Arg C . 17831 1 482 . 1 1 49 49 ARG CA C 13 55.201 0.2 . 1 . . . . 47 Arg CA . 17831 1 483 . 1 1 49 49 ARG CB C 13 33.610 0.2 . 1 . . . . 47 Arg CB . 17831 1 484 . 1 1 49 49 ARG CG C 13 26.847 0.2 . 1 . . . . 47 Arg CG . 17831 1 485 . 1 1 49 49 ARG CD C 13 43.347 0.2 . 1 . . . . 47 Arg CD . 17831 1 486 . 1 1 49 49 ARG N N 15 129.557 0.2 . 1 . . . . 47 Arg N . 17831 1 487 . 1 1 50 50 ILE H H 1 8.772 0.02 . 1 . . . . 48 Ile H . 17831 1 488 . 1 1 50 50 ILE HA H 1 4.923 0.02 . 1 . . . . 48 Ile HA . 17831 1 489 . 1 1 50 50 ILE HB H 1 1.786 0.02 . 1 . . . . 48 Ile HB . 17831 1 490 . 1 1 50 50 ILE HG12 H 1 1.059 0.02 . 2 . . . . 48 Ile HG12 . 17831 1 491 . 1 1 50 50 ILE HG13 H 1 1.565 0.02 . 2 . . . . 48 Ile HG13 . 17831 1 492 . 1 1 50 50 ILE HG21 H 1 0.760 0.02 . 1 . . . . 48 Ile HG2 . 17831 1 493 . 1 1 50 50 ILE HG22 H 1 0.760 0.02 . 1 . . . . 48 Ile HG2 . 17831 1 494 . 1 1 50 50 ILE HG23 H 1 0.760 0.02 . 1 . . . . 48 Ile HG2 . 17831 1 495 . 1 1 50 50 ILE HD11 H 1 0.862 0.02 . 1 . . . . 48 Ile HD1 . 17831 1 496 . 1 1 50 50 ILE HD12 H 1 0.862 0.02 . 1 . . . . 48 Ile HD1 . 17831 1 497 . 1 1 50 50 ILE HD13 H 1 0.862 0.02 . 1 . . . . 48 Ile HD1 . 17831 1 498 . 1 1 50 50 ILE C C 13 175.317 0.2 . 1 . . . . 48 Ile C . 17831 1 499 . 1 1 50 50 ILE CA C 13 60.493 0.2 . 1 . . . . 48 Ile CA . 17831 1 500 . 1 1 50 50 ILE CB C 13 40.676 0.2 . 1 . . . . 48 Ile CB . 17831 1 501 . 1 1 50 50 ILE CG1 C 13 28.010 0.2 . 1 . . . . 48 Ile CG1 . 17831 1 502 . 1 1 50 50 ILE CG2 C 13 19.010 0.2 . 1 . . . . 48 Ile CG2 . 17831 1 503 . 1 1 50 50 ILE CD1 C 13 14.681 0.2 . 1 . . . . 48 Ile CD1 . 17831 1 504 . 1 1 50 50 ILE N N 15 124.911 0.2 . 1 . . . . 48 Ile N . 17831 1 505 . 1 1 51 51 THR H H 1 9.030 0.02 . 1 . . . . 49 Thr H . 17831 1 506 . 1 1 51 51 THR HA H 1 5.009 0.02 . 1 . . . . 49 Thr HA . 17831 1 507 . 1 1 51 51 THR HB H 1 3.997 0.02 . 1 . . . . 49 Thr HB . 17831 1 508 . 1 1 51 51 THR HG21 H 1 1.215 0.02 . 1 . . . . 49 Thr HG2 . 17831 1 509 . 1 1 51 51 THR HG22 H 1 1.215 0.02 . 1 . . . . 49 Thr HG2 . 17831 1 510 . 1 1 51 51 THR HG23 H 1 1.215 0.02 . 1 . . . . 49 Thr HG2 . 17831 1 511 . 1 1 51 51 THR C C 13 173.229 0.2 . 1 . . . . 49 Thr C . 17831 1 512 . 1 1 51 51 THR CA C 13 59.139 0.2 . 1 . . . . 49 Thr CA . 17831 1 513 . 1 1 51 51 THR CB C 13 71.594 0.2 . 1 . . . . 49 Thr CB . 17831 1 514 . 1 1 51 51 THR CG2 C 13 21.511 0.2 . 1 . . . . 49 Thr CG2 . 17831 1 515 . 1 1 51 51 THR N N 15 122.373 0.2 . 1 . . . . 49 Thr N . 17831 1 516 . 1 1 52 52 PRO HA H 1 5.122 0.02 . 1 . . . . 50 Pro HA . 17831 1 517 . 1 1 52 52 PRO HB2 H 1 1.736 0.02 . 2 . . . . 50 Pro HB2 . 17831 1 518 . 1 1 52 52 PRO HB3 H 1 2.088 0.02 . 2 . . . . 50 Pro HB3 . 17831 1 519 . 1 1 52 52 PRO C C 13 175.275 0.2 . 1 . . . . 50 Pro C . 17831 1 520 . 1 1 52 52 PRO CA C 13 62.056 0.2 . 1 . . . . 50 Pro CA . 17831 1 521 . 1 1 52 52 PRO CB C 13 33.477 0.2 . 1 . . . . 50 Pro CB . 17831 1 522 . 1 1 53 53 GLU H H 1 8.797 0.02 . 1 . . . . 51 Glu H . 17831 1 523 . 1 1 53 53 GLU HA H 1 4.427 0.02 . 1 . . . . 51 Glu HA . 17831 1 524 . 1 1 53 53 GLU HB2 H 1 1.812 0.02 . 1 . . . . 51 Glu HB2 . 17831 1 525 . 1 1 53 53 GLU HB3 H 1 1.812 0.02 . 1 . . . . 51 Glu HB3 . 17831 1 526 . 1 1 53 53 GLU HG2 H 1 1.866 0.02 . 2 . . . . 51 Glu HG2 . 17831 1 527 . 1 1 53 53 GLU HG3 H 1 1.789 0.02 . 2 . . . . 51 Glu HG3 . 17831 1 528 . 1 1 53 53 GLU C C 13 174.817 0.2 . 1 . . . . 51 Glu C . 17831 1 529 . 1 1 53 53 GLU CA C 13 56.525 0.2 . 1 . . . . 51 Glu CA . 17831 1 530 . 1 1 53 53 GLU CB C 13 31.620 0.2 . 1 . . . . 51 Glu CB . 17831 1 531 . 1 1 53 53 GLU CG C 13 36.184 0.2 . 1 . . . . 51 Glu CG . 17831 1 532 . 1 1 53 53 GLU N N 15 120.918 0.2 . 1 . . . . 51 Glu N . 17831 1 533 . 1 1 54 54 HIS H H 1 8.879 0.02 . 1 . . . . 52 His H . 17831 1 534 . 1 1 54 54 HIS HA H 1 4.170 0.02 . 1 . . . . 52 His HA . 17831 1 535 . 1 1 54 54 HIS HB2 H 1 3.333 0.02 . 2 . . . . 52 His HB2 . 17831 1 536 . 1 1 54 54 HIS HB3 H 1 3.324 0.02 . 2 . . . . 52 His HB3 . 17831 1 537 . 1 1 54 54 HIS C C 13 171.982 0.2 . 1 . . . . 52 His C . 17831 1 538 . 1 1 54 54 HIS CA C 13 56.776 0.2 . 1 . . . . 52 His CA . 17831 1 539 . 1 1 54 54 HIS CB C 13 26.469 0.2 . 1 . . . . 52 His CB . 17831 1 540 . 1 1 54 54 HIS N N 15 118.018 0.2 . 1 . . . . 52 His N . 17831 1 541 . 1 1 55 55 ALA H H 1 7.268 0.02 . 1 . . . . 53 Ala H . 17831 1 542 . 1 1 55 55 ALA HA H 1 4.910 0.02 . 1 . . . . 53 Ala HA . 17831 1 543 . 1 1 55 55 ALA HB1 H 1 1.202 0.02 . 1 . . . . 53 Ala HB . 17831 1 544 . 1 1 55 55 ALA HB2 H 1 1.202 0.02 . 1 . . . . 53 Ala HB . 17831 1 545 . 1 1 55 55 ALA HB3 H 1 1.202 0.02 . 1 . . . . 53 Ala HB . 17831 1 546 . 1 1 55 55 ALA C C 13 174.966 0.2 . 1 . . . . 53 Ala C . 17831 1 547 . 1 1 55 55 ALA CA C 13 50.678 0.2 . 1 . . . . 53 Ala CA . 17831 1 548 . 1 1 55 55 ALA CB C 13 22.970 0.2 . 1 . . . . 53 Ala CB . 17831 1 549 . 1 1 55 55 ALA N N 15 114.482 0.2 . 1 . . . . 53 Ala N . 17831 1 550 . 1 1 56 56 LYS H H 1 8.863 0.02 . 1 . . . . 54 Lys H . 17831 1 551 . 1 1 56 56 LYS HA H 1 4.755 0.02 . 1 . . . . 54 Lys HA . 17831 1 552 . 1 1 56 56 LYS HB2 H 1 1.639 0.02 . 2 . . . . 54 Lys HB2 . 17831 1 553 . 1 1 56 56 LYS HB3 H 1 1.903 0.02 . 2 . . . . 54 Lys HB3 . 17831 1 554 . 1 1 56 56 LYS HG2 H 1 1.372 0.02 . 2 . . . . 54 Lys HG2 . 17831 1 555 . 1 1 56 56 LYS HG3 H 1 1.451 0.02 . 2 . . . . 54 Lys HG3 . 17831 1 556 . 1 1 56 56 LYS HD2 H 1 1.610 0.02 . 2 . . . . 54 Lys HD2 . 17831 1 557 . 1 1 56 56 LYS HD3 H 1 1.682 0.02 . 2 . . . . 54 Lys HD3 . 17831 1 558 . 1 1 56 56 LYS HE2 H 1 2.932 0.02 . 2 . . . . 54 Lys HE2 . 17831 1 559 . 1 1 56 56 LYS HE3 H 1 2.932 0.02 . 2 . . . . 54 Lys HE3 . 17831 1 560 . 1 1 56 56 LYS C C 13 175.801 0.2 . 1 . . . . 54 Lys C . 17831 1 561 . 1 1 56 56 LYS CA C 13 54.939 0.2 . 1 . . . . 54 Lys CA . 17831 1 562 . 1 1 56 56 LYS CB C 13 35.265 0.2 . 1 . . . . 54 Lys CB . 17831 1 563 . 1 1 56 56 LYS CG C 13 24.291 0.2 . 1 . . . . 54 Lys CG . 17831 1 564 . 1 1 56 56 LYS CD C 13 29.010 0.2 . 1 . . . . 54 Lys CD . 17831 1 565 . 1 1 56 56 LYS CE C 13 42.256 0.2 . 1 . . . . 54 Lys CE . 17831 1 566 . 1 1 56 56 LYS N N 15 119.737 0.2 . 1 . . . . 54 Lys N . 17831 1 567 . 1 1 57 57 ILE H H 1 8.785 0.02 . 1 . . . . 55 Ile H . 17831 1 568 . 1 1 57 57 ILE HA H 1 5.208 0.02 . 1 . . . . 55 Ile HA . 17831 1 569 . 1 1 57 57 ILE HB H 1 2.017 0.02 . 1 . . . . 55 Ile HB . 17831 1 570 . 1 1 57 57 ILE HG12 H 1 1.534 0.02 . 2 . . . . 55 Ile HG12 . 17831 1 571 . 1 1 57 57 ILE HG13 H 1 0.890 0.02 . 2 . . . . 55 Ile HG13 . 17831 1 572 . 1 1 57 57 ILE HG21 H 1 0.688 0.02 . 1 . . . . 55 Ile HG2 . 17831 1 573 . 1 1 57 57 ILE HG22 H 1 0.688 0.02 . 1 . . . . 55 Ile HG2 . 17831 1 574 . 1 1 57 57 ILE HG23 H 1 0.688 0.02 . 1 . . . . 55 Ile HG2 . 17831 1 575 . 1 1 57 57 ILE HD11 H 1 0.733 0.02 . 1 . . . . 55 Ile HD1 . 17831 1 576 . 1 1 57 57 ILE HD12 H 1 0.733 0.02 . 1 . . . . 55 Ile HD1 . 17831 1 577 . 1 1 57 57 ILE HD13 H 1 0.733 0.02 . 1 . . . . 55 Ile HD1 . 17831 1 578 . 1 1 57 57 ILE C C 13 175.307 0.2 . 1 . . . . 55 Ile C . 17831 1 579 . 1 1 57 57 ILE CA C 13 58.571 0.2 . 1 . . . . 55 Ile CA . 17831 1 580 . 1 1 57 57 ILE CB C 13 40.948 0.2 . 1 . . . . 55 Ile CB . 17831 1 581 . 1 1 57 57 ILE CG1 C 13 25.420 0.2 . 1 . . . . 55 Ile CG1 . 17831 1 582 . 1 1 57 57 ILE CG2 C 13 18.010 0.2 . 1 . . . . 55 Ile CG2 . 17831 1 583 . 1 1 57 57 ILE CD1 C 13 13.997 0.2 . 1 . . . . 55 Ile CD1 . 17831 1 584 . 1 1 57 57 ILE N N 15 117.825 0.2 . 1 . . . . 55 Ile N . 17831 1 585 . 1 1 58 58 ALA H H 1 8.235 0.02 . 1 . . . . 56 Ala H . 17831 1 586 . 1 1 58 58 ALA HA H 1 4.436 0.02 . 1 . . . . 56 Ala HA . 17831 1 587 . 1 1 58 58 ALA HB1 H 1 1.532 0.02 . 1 . . . . 56 Ala HB . 17831 1 588 . 1 1 58 58 ALA HB2 H 1 1.532 0.02 . 1 . . . . 56 Ala HB . 17831 1 589 . 1 1 58 58 ALA HB3 H 1 1.532 0.02 . 1 . . . . 56 Ala HB . 17831 1 590 . 1 1 58 58 ALA C C 13 177.580 0.2 . 1 . . . . 56 Ala C . 17831 1 591 . 1 1 58 58 ALA CA C 13 51.185 0.2 . 1 . . . . 56 Ala CA . 17831 1 592 . 1 1 58 58 ALA CB C 13 19.526 0.2 . 1 . . . . 56 Ala CB . 17831 1 593 . 1 1 58 58 ALA N N 15 125.369 0.2 . 1 . . . . 56 Ala N . 17831 1 594 . 1 1 59 59 ASP H H 1 8.357 0.02 . 1 . . . . 57 Asp H . 17831 1 595 . 1 1 59 59 ASP HA H 1 4.404 0.02 . 1 . . . . 57 Asp HA . 17831 1 596 . 1 1 59 59 ASP HB2 H 1 2.604 0.02 . 2 . . . . 57 Asp HB2 . 17831 1 597 . 1 1 59 59 ASP HB3 H 1 2.545 0.02 . 2 . . . . 57 Asp HB3 . 17831 1 598 . 1 1 59 59 ASP C C 13 176.630 0.2 . 1 . . . . 57 Asp C . 17831 1 599 . 1 1 59 59 ASP CA C 13 55.665 0.2 . 1 . . . . 57 Asp CA . 17831 1 600 . 1 1 59 59 ASP CB C 13 40.591 0.2 . 1 . . . . 57 Asp CB . 17831 1 601 . 1 1 59 59 ASP N N 15 120.237 0.2 . 1 . . . . 57 Asp N . 17831 1 602 . 1 1 60 60 VAL H H 1 8.361 0.02 . 1 . . . . 58 Val H . 17831 1 603 . 1 1 60 60 VAL HA H 1 4.065 0.02 . 1 . . . . 58 Val HA . 17831 1 604 . 1 1 60 60 VAL HB H 1 2.052 0.02 . 1 . . . . 58 Val HB . 17831 1 605 . 1 1 60 60 VAL HG11 H 1 0.956 0.02 . 2 . . . . 58 Val HG1 . 17831 1 606 . 1 1 60 60 VAL HG12 H 1 0.956 0.02 . 2 . . . . 58 Val HG1 . 17831 1 607 . 1 1 60 60 VAL HG13 H 1 0.956 0.02 . 2 . . . . 58 Val HG1 . 17831 1 608 . 1 1 60 60 VAL HG21 H 1 1.115 0.02 . 2 . . . . 58 Val HG2 . 17831 1 609 . 1 1 60 60 VAL HG22 H 1 1.115 0.02 . 2 . . . . 58 Val HG2 . 17831 1 610 . 1 1 60 60 VAL HG23 H 1 1.115 0.02 . 2 . . . . 58 Val HG2 . 17831 1 611 . 1 1 60 60 VAL C C 13 176.012 0.2 . 1 . . . . 58 Val C . 17831 1 612 . 1 1 60 60 VAL CA C 13 62.856 0.2 . 1 . . . . 58 Val CA . 17831 1 613 . 1 1 60 60 VAL CB C 13 32.810 0.2 . 1 . . . . 58 Val CB . 17831 1 614 . 1 1 60 60 VAL CG1 C 13 21.010 0.2 . 2 . . . . 58 Val CG1 . 17831 1 615 . 1 1 60 60 VAL CG2 C 13 22.021 0.2 . 2 . . . . 58 Val CG2 . 17831 1 616 . 1 1 60 60 VAL N N 15 124.820 0.2 . 1 . . . . 58 Val N . 17831 1 617 . 1 1 61 61 GLN H H 1 8.703 0.02 . 1 . . . . 59 Gln H . 17831 1 618 . 1 1 61 61 GLN HA H 1 4.524 0.02 . 1 . . . . 59 Gln HA . 17831 1 619 . 1 1 61 61 GLN HB2 H 1 1.956 0.02 . 2 . . . . 59 Gln HB2 . 17831 1 620 . 1 1 61 61 GLN HB3 H 1 1.978 0.02 . 2 . . . . 59 Gln HB3 . 17831 1 621 . 1 1 61 61 GLN HG2 H 1 2.290 0.02 . 1 . . . . 59 Gln HG2 . 17831 1 622 . 1 1 61 61 GLN HG3 H 1 2.290 0.02 . 1 . . . . 59 Gln HG3 . 17831 1 623 . 1 1 61 61 GLN C C 13 174.849 0.2 . 1 . . . . 59 Gln C . 17831 1 624 . 1 1 61 61 GLN CA C 13 53.870 0.2 . 1 . . . . 59 Gln CA . 17831 1 625 . 1 1 61 61 GLN CB C 13 28.882 0.2 . 1 . . . . 59 Gln CB . 17831 1 626 . 1 1 61 61 GLN CG C 13 33.442 0.2 . 1 . . . . 59 Gln CG . 17831 1 627 . 1 1 61 61 GLN N N 15 128.224 0.2 . 1 . . . . 59 Gln N . 17831 1 628 . 1 1 62 62 LEU H H 1 8.610 0.02 . 1 . . . . 60 Leu H . 17831 1 629 . 1 1 62 62 LEU HA H 1 4.512 0.02 . 1 . . . . 60 Leu HA . 17831 1 630 . 1 1 62 62 LEU HB2 H 1 1.757 0.02 . 2 . . . . 60 Leu HB2 . 17831 1 631 . 1 1 62 62 LEU HB3 H 1 1.587 0.02 . 2 . . . . 60 Leu HB3 . 17831 1 632 . 1 1 62 62 LEU HG H 1 1.681 0.02 . 1 . . . . 60 Leu HG . 17831 1 633 . 1 1 62 62 LEU HD11 H 1 1.000 0.02 . 2 . . . . 60 Leu HD1 . 17831 1 634 . 1 1 62 62 LEU HD12 H 1 1.000 0.02 . 2 . . . . 60 Leu HD1 . 17831 1 635 . 1 1 62 62 LEU HD13 H 1 1.000 0.02 . 2 . . . . 60 Leu HD1 . 17831 1 636 . 1 1 62 62 LEU HD21 H 1 0.907 0.02 . 2 . . . . 60 Leu HD2 . 17831 1 637 . 1 1 62 62 LEU HD22 H 1 0.907 0.02 . 2 . . . . 60 Leu HD2 . 17831 1 638 . 1 1 62 62 LEU HD23 H 1 0.907 0.02 . 2 . . . . 60 Leu HD2 . 17831 1 639 . 1 1 62 62 LEU C C 13 175.848 0.2 . 1 . . . . 60 Leu C . 17831 1 640 . 1 1 62 62 LEU CA C 13 52.859 0.2 . 1 . . . . 60 Leu CA . 17831 1 641 . 1 1 62 62 LEU CB C 13 40.009 0.2 . 1 . . . . 60 Leu CB . 17831 1 642 . 1 1 62 62 LEU CG C 13 28.042 0.2 . 1 . . . . 60 Leu CG . 17831 1 643 . 1 1 62 62 LEU CD1 C 13 26.358 0.2 . 2 . . . . 60 Leu CD1 . 17831 1 644 . 1 1 62 62 LEU CD2 C 13 25.010 0.2 . 2 . . . . 60 Leu CD2 . 17831 1 645 . 1 1 62 62 LEU N N 15 127.363 0.2 . 1 . . . . 60 Leu N . 17831 1 646 . 1 1 63 63 PRO HA H 1 4.641 0.02 . 1 . . . . 61 Pro HA . 17831 1 647 . 1 1 63 63 PRO HB2 H 1 2.112 0.02 . 2 . . . . 61 Pro HB2 . 17831 1 648 . 1 1 63 63 PRO HB3 H 1 2.422 0.02 . 2 . . . . 61 Pro HB3 . 17831 1 649 . 1 1 63 63 PRO C C 13 177.272 0.2 . 1 . . . . 61 Pro C . 17831 1 650 . 1 1 63 63 PRO CA C 13 62.127 0.2 . 1 . . . . 61 Pro CA . 17831 1 651 . 1 1 63 63 PRO CB C 13 32.628 0.2 . 1 . . . . 61 Pro CB . 17831 1 652 . 1 1 64 64 GLN H H 1 8.980 0.02 . 1 . . . . 62 Gln H . 17831 1 653 . 1 1 64 64 GLN HA H 1 4.116 0.02 . 1 . . . . 62 Gln HA . 17831 1 654 . 1 1 64 64 GLN HB2 H 1 2.149 0.02 . 1 . . . . 62 Gln HB2 . 17831 1 655 . 1 1 64 64 GLN HB3 H 1 2.149 0.02 . 1 . . . . 62 Gln HB3 . 17831 1 656 . 1 1 64 64 GLN HG2 H 1 2.564 0.02 . 2 . . . . 62 Gln HG2 . 17831 1 657 . 1 1 64 64 GLN HG3 H 1 2.588 0.02 . 2 . . . . 62 Gln HG3 . 17831 1 658 . 1 1 64 64 GLN C C 13 176.989 0.2 . 1 . . . . 62 Gln C . 17831 1 659 . 1 1 64 64 GLN CA C 13 57.546 0.2 . 1 . . . . 62 Gln CA . 17831 1 660 . 1 1 64 64 GLN CB C 13 29.354 0.2 . 1 . . . . 62 Gln CB . 17831 1 661 . 1 1 64 64 GLN CG C 13 34.003 0.2 . 1 . . . . 62 Gln CG . 17831 1 662 . 1 1 64 64 GLN N N 15 123.192 0.2 . 1 . . . . 62 Gln N . 17831 1 663 . 1 1 65 65 GLY H H 1 9.595 0.02 . 1 . . . . 63 Gly H . 17831 1 664 . 1 1 65 65 GLY HA2 H 1 3.143 0.02 . 2 . . . . 63 Gly HA2 . 17831 1 665 . 1 1 65 65 GLY HA3 H 1 4.667 0.02 . 2 . . . . 63 Gly HA3 . 17831 1 666 . 1 1 65 65 GLY C C 13 173.256 0.2 . 1 . . . . 63 Gly C . 17831 1 667 . 1 1 65 65 GLY CA C 13 44.008 0.2 . 1 . . . . 63 Gly CA . 17831 1 668 . 1 1 65 65 GLY N N 15 115.580 0.2 . 1 . . . . 63 Gly N . 17831 1 669 . 1 1 66 66 VAL H H 1 8.706 0.02 . 1 . . . . 64 Val H . 17831 1 670 . 1 1 66 66 VAL HA H 1 4.502 0.02 . 1 . . . . 64 Val HA . 17831 1 671 . 1 1 66 66 VAL HB H 1 2.106 0.02 . 1 . . . . 64 Val HB . 17831 1 672 . 1 1 66 66 VAL HG11 H 1 0.991 0.02 . 2 . . . . 64 Val HG1 . 17831 1 673 . 1 1 66 66 VAL HG12 H 1 0.991 0.02 . 2 . . . . 64 Val HG1 . 17831 1 674 . 1 1 66 66 VAL HG13 H 1 0.991 0.02 . 2 . . . . 64 Val HG1 . 17831 1 675 . 1 1 66 66 VAL HG21 H 1 0.825 0.02 . 2 . . . . 64 Val HG2 . 17831 1 676 . 1 1 66 66 VAL HG22 H 1 0.825 0.02 . 2 . . . . 64 Val HG2 . 17831 1 677 . 1 1 66 66 VAL HG23 H 1 0.825 0.02 . 2 . . . . 64 Val HG2 . 17831 1 678 . 1 1 66 66 VAL C C 13 175.124 0.2 . 1 . . . . 64 Val C . 17831 1 679 . 1 1 66 66 VAL CA C 13 59.994 0.2 . 1 . . . . 64 Val CA . 17831 1 680 . 1 1 66 66 VAL CB C 13 34.264 0.2 . 1 . . . . 64 Val CB . 17831 1 681 . 1 1 66 66 VAL CG1 C 13 21.531 0.2 . 2 . . . . 64 Val CG1 . 17831 1 682 . 1 1 66 66 VAL CG2 C 13 19.510 0.2 . 2 . . . . 64 Val CG2 . 17831 1 683 . 1 1 66 66 VAL N N 15 117.637 0.2 . 1 . . . . 64 Val N . 17831 1 684 . 1 1 67 67 TRP H H 1 8.622 0.02 . 1 . . . . 65 Trp H . 17831 1 685 . 1 1 67 67 TRP HA H 1 4.843 0.02 . 1 . . . . 65 Trp HA . 17831 1 686 . 1 1 67 67 TRP HB2 H 1 3.069 0.02 . 2 . . . . 65 Trp HB2 . 17831 1 687 . 1 1 67 67 TRP HB3 H 1 3.039 0.02 . 2 . . . . 65 Trp HB3 . 17831 1 688 . 1 1 67 67 TRP HE1 H 1 10.034 0.02 . 1 . . . . 65 Trp HE1 . 17831 1 689 . 1 1 67 67 TRP C C 13 176.449 0.2 . 1 . . . . 65 Trp C . 17831 1 690 . 1 1 67 67 TRP CA C 13 58.225 0.2 . 1 . . . . 65 Trp CA . 17831 1 691 . 1 1 67 67 TRP CB C 13 30.090 0.2 . 1 . . . . 65 Trp CB . 17831 1 692 . 1 1 67 67 TRP N N 15 122.710 0.2 . 1 . . . . 65 Trp N . 17831 1 693 . 1 1 67 67 TRP NE1 N 15 128.942 0.2 . 1 . . . . 65 Trp NE1 . 17831 1 694 . 1 1 68 68 HIS H H 1 9.212 0.02 . 1 . . . . 66 His H . 17831 1 695 . 1 1 68 68 HIS C C 13 172.920 0.2 . 1 . . . . 66 His C . 17831 1 696 . 1 1 68 68 HIS CA C 13 55.084 0.2 . 1 . . . . 66 His CA . 17831 1 697 . 1 1 68 68 HIS N N 15 124.593 0.2 . 1 . . . . 66 His N . 17831 1 698 . 1 1 69 69 GLU HA H 1 4.796 0.02 . 1 . . . . 67 Glu HA . 17831 1 699 . 1 1 69 69 GLU HB2 H 1 1.675 0.02 . 2 . . . . 67 Glu HB2 . 17831 1 700 . 1 1 69 69 GLU HB3 H 1 1.794 0.02 . 2 . . . . 67 Glu HB3 . 17831 1 701 . 1 1 69 69 GLU HG2 H 1 1.967 0.02 . 1 . . . . 67 Glu HG2 . 17831 1 702 . 1 1 69 69 GLU HG3 H 1 1.967 0.02 . 1 . . . . 67 Glu HG3 . 17831 1 703 . 1 1 69 69 GLU C C 13 174.065 0.2 . 1 . . . . 67 Glu C . 17831 1 704 . 1 1 69 69 GLU CA C 13 55.490 0.2 . 1 . . . . 67 Glu CA . 17831 1 705 . 1 1 69 69 GLU CB C 13 31.528 0.2 . 1 . . . . 67 Glu CB . 17831 1 706 . 1 1 69 69 GLU CG C 13 36.298 0.2 . 1 . . . . 67 Glu CG . 17831 1 707 . 1 1 70 70 ASP H H 1 8.019 0.02 . 1 . . . . 68 Asp H . 17831 1 708 . 1 1 70 70 ASP HA H 1 4.721 0.02 . 1 . . . . 68 Asp HA . 17831 1 709 . 1 1 70 70 ASP HB2 H 1 2.851 0.02 . 2 . . . . 68 Asp HB2 . 17831 1 710 . 1 1 70 70 ASP HB3 H 1 3.093 0.02 . 2 . . . . 68 Asp HB3 . 17831 1 711 . 1 1 70 70 ASP C C 13 176.425 0.2 . 1 . . . . 68 Asp C . 17831 1 712 . 1 1 70 70 ASP CA C 13 53.089 0.2 . 1 . . . . 68 Asp CA . 17831 1 713 . 1 1 70 70 ASP CB C 13 44.538 0.2 . 1 . . . . 68 Asp CB . 17831 1 714 . 1 1 70 70 ASP N N 15 121.454 0.2 . 1 . . . . 68 Asp N . 17831 1 715 . 1 1 71 71 GLU H H 1 8.811 0.02 . 1 . . . . 69 Glu H . 17831 1 716 . 1 1 71 71 GLU HA H 1 4.079 0.02 . 1 . . . . 69 Glu HA . 17831 1 717 . 1 1 71 71 GLU HB2 H 1 1.755 0.02 . 2 . . . . 69 Glu HB2 . 17831 1 718 . 1 1 71 71 GLU HB3 H 1 1.766 0.02 . 2 . . . . 69 Glu HB3 . 17831 1 719 . 1 1 71 71 GLU HG2 H 1 1.776 0.02 . 2 . . . . 69 Glu HG2 . 17831 1 720 . 1 1 71 71 GLU HG3 H 1 1.882 0.02 . 2 . . . . 69 Glu HG3 . 17831 1 721 . 1 1 71 71 GLU C C 13 175.857 0.2 . 1 . . . . 69 Glu C . 17831 1 722 . 1 1 71 71 GLU CA C 13 57.660 0.2 . 1 . . . . 69 Glu CA . 17831 1 723 . 1 1 71 71 GLU CB C 13 29.422 0.2 . 1 . . . . 69 Glu CB . 17831 1 724 . 1 1 71 71 GLU CG C 13 35.821 0.2 . 1 . . . . 69 Glu CG . 17831 1 725 . 1 1 71 71 GLU N N 15 119.166 0.2 . 1 . . . . 69 Glu N . 17831 1 726 . 1 1 72 72 PHE H H 1 8.434 0.02 . 1 . . . . 70 Phe H . 17831 1 727 . 1 1 72 72 PHE HA H 1 4.346 0.02 . 1 . . . . 70 Phe HA . 17831 1 728 . 1 1 72 72 PHE HB2 H 1 2.888 0.02 . 2 . . . . 70 Phe HB2 . 17831 1 729 . 1 1 72 72 PHE HB3 H 1 2.873 0.02 . 2 . . . . 70 Phe HB3 . 17831 1 730 . 1 1 72 72 PHE C C 13 176.979 0.2 . 1 . . . . 70 Phe C . 17831 1 731 . 1 1 72 72 PHE CA C 13 59.556 0.2 . 1 . . . . 70 Phe CA . 17831 1 732 . 1 1 72 72 PHE CB C 13 39.877 0.2 . 1 . . . . 70 Phe CB . 17831 1 733 . 1 1 72 72 PHE N N 15 121.090 0.2 . 1 . . . . 70 Phe N . 17831 1 734 . 1 1 73 73 TYR H H 1 8.835 0.02 . 1 . . . . 71 Tyr H . 17831 1 735 . 1 1 73 73 TYR HA H 1 4.576 0.02 . 1 . . . . 71 Tyr HA . 17831 1 736 . 1 1 73 73 TYR HB2 H 1 2.680 0.02 . 2 . . . . 71 Tyr HB2 . 17831 1 737 . 1 1 73 73 TYR HB3 H 1 3.144 0.02 . 2 . . . . 71 Tyr HB3 . 17831 1 738 . 1 1 73 73 TYR C C 13 176.394 0.2 . 1 . . . . 71 Tyr C . 17831 1 739 . 1 1 73 73 TYR CA C 13 57.784 0.2 . 1 . . . . 71 Tyr CA . 17831 1 740 . 1 1 73 73 TYR CB C 13 39.494 0.2 . 1 . . . . 71 Tyr CB . 17831 1 741 . 1 1 73 73 TYR N N 15 116.401 0.2 . 1 . . . . 71 Tyr N . 17831 1 742 . 1 1 74 74 GLY H H 1 7.707 0.02 . 1 . . . . 72 Gly H . 17831 1 743 . 1 1 74 74 GLY HA2 H 1 3.978 0.02 . 2 . . . . 72 Gly HA2 . 17831 1 744 . 1 1 74 74 GLY HA3 H 1 4.196 0.02 . 2 . . . . 72 Gly HA3 . 17831 1 745 . 1 1 74 74 GLY C C 13 174.756 0.2 . 1 . . . . 72 Gly C . 17831 1 746 . 1 1 74 74 GLY CA C 13 45.529 0.2 . 1 . . . . 72 Gly CA . 17831 1 747 . 1 1 74 74 GLY N N 15 109.794 0.2 . 1 . . . . 72 Gly N . 17831 1 748 . 1 1 75 75 LYS H H 1 8.738 0.02 . 1 . . . . 73 Lys H . 17831 1 749 . 1 1 75 75 LYS HA H 1 5.037 0.02 . 1 . . . . 73 Lys HA . 17831 1 750 . 1 1 75 75 LYS HB2 H 1 1.781 0.02 . 2 . . . . 73 Lys HB2 . 17831 1 751 . 1 1 75 75 LYS HB3 H 1 1.868 0.02 . 2 . . . . 73 Lys HB3 . 17831 1 752 . 1 1 75 75 LYS HG2 H 1 1.400 0.02 . 2 . . . . 73 Lys HG2 . 17831 1 753 . 1 1 75 75 LYS HG3 H 1 1.323 0.02 . 2 . . . . 73 Lys HG3 . 17831 1 754 . 1 1 75 75 LYS HD2 H 1 1.453 0.02 . 1 . . . . 73 Lys HD2 . 17831 1 755 . 1 1 75 75 LYS HD3 H 1 1.453 0.02 . 1 . . . . 73 Lys HD3 . 17831 1 756 . 1 1 75 75 LYS HE2 H 1 2.525 0.02 . 2 . . . . 73 Lys HE2 . 17831 1 757 . 1 1 75 75 LYS HE3 H 1 2.625 0.02 . 2 . . . . 73 Lys HE3 . 17831 1 758 . 1 1 75 75 LYS C C 13 176.720 0.2 . 1 . . . . 73 Lys C . 17831 1 759 . 1 1 75 75 LYS CA C 13 56.820 0.2 . 1 . . . . 73 Lys CA . 17831 1 760 . 1 1 75 75 LYS CB C 13 33.047 0.2 . 1 . . . . 73 Lys CB . 17831 1 761 . 1 1 75 75 LYS CG C 13 25.347 0.2 . 1 . . . . 73 Lys CG . 17831 1 762 . 1 1 75 75 LYS CD C 13 29.343 0.2 . 1 . . . . 73 Lys CD . 17831 1 763 . 1 1 75 75 LYS CE C 13 41.800 0.2 . 1 . . . . 73 Lys CE . 17831 1 764 . 1 1 75 75 LYS N N 15 126.972 0.2 . 1 . . . . 73 Lys N . 17831 1 765 . 1 1 76 76 SER H H 1 9.294 0.02 . 1 . . . . 74 Ser H . 17831 1 766 . 1 1 76 76 SER HA H 1 4.903 0.02 . 1 . . . . 74 Ser HA . 17831 1 767 . 1 1 76 76 SER HB2 H 1 3.796 0.02 . 2 . . . . 74 Ser HB2 . 17831 1 768 . 1 1 76 76 SER HB3 H 1 3.880 0.02 . 2 . . . . 74 Ser HB3 . 17831 1 769 . 1 1 76 76 SER C C 13 171.364 0.2 . 1 . . . . 74 Ser C . 17831 1 770 . 1 1 76 76 SER CA C 13 58.446 0.2 . 1 . . . . 74 Ser CA . 17831 1 771 . 1 1 76 76 SER CB C 13 66.978 0.2 . 1 . . . . 74 Ser CB . 17831 1 772 . 1 1 76 76 SER N N 15 121.508 0.2 . 1 . . . . 74 Ser N . 17831 1 773 . 1 1 77 77 GLU H H 1 8.277 0.02 . 1 . . . . 75 Glu H . 17831 1 774 . 1 1 77 77 GLU HA H 1 3.951 0.02 . 1 . . . . 75 Glu HA . 17831 1 775 . 1 1 77 77 GLU HB2 H 1 0.834 0.02 . 2 . . . . 75 Glu HB2 . 17831 1 776 . 1 1 77 77 GLU HB3 H 1 1.164 0.02 . 2 . . . . 75 Glu HB3 . 17831 1 777 . 1 1 77 77 GLU HG2 H 1 0.863 0.02 . 1 . . . . 75 Glu HG2 . 17831 1 778 . 1 1 77 77 GLU HG3 H 1 0.863 0.02 . 1 . . . . 75 Glu HG3 . 17831 1 779 . 1 1 77 77 GLU C C 13 176.918 0.2 . 1 . . . . 75 Glu C . 17831 1 780 . 1 1 77 77 GLU CA C 13 55.297 0.2 . 1 . . . . 75 Glu CA . 17831 1 781 . 1 1 77 77 GLU CB C 13 30.848 0.2 . 1 . . . . 75 Glu CB . 17831 1 782 . 1 1 77 77 GLU CG C 13 36.150 0.2 . 1 . . . . 75 Glu CG . 17831 1 783 . 1 1 77 77 GLU N N 15 124.161 0.2 . 1 . . . . 75 Glu N . 17831 1 784 . 1 1 78 78 ILE H H 1 9.331 0.02 . 1 . . . . 76 Ile H . 17831 1 785 . 1 1 78 78 ILE HA H 1 5.055 0.02 . 1 . . . . 76 Ile HA . 17831 1 786 . 1 1 78 78 ILE HB H 1 1.530 0.02 . 1 . . . . 76 Ile HB . 17831 1 787 . 1 1 78 78 ILE HG12 H 1 0.970 0.02 . 2 . . . . 76 Ile HG12 . 17831 1 788 . 1 1 78 78 ILE HG13 H 1 0.655 0.02 . 2 . . . . 76 Ile HG13 . 17831 1 789 . 1 1 78 78 ILE HG21 H 1 0.423 0.02 . 1 . . . . 76 Ile HG2 . 17831 1 790 . 1 1 78 78 ILE HG22 H 1 0.423 0.02 . 1 . . . . 76 Ile HG2 . 17831 1 791 . 1 1 78 78 ILE HG23 H 1 0.423 0.02 . 1 . . . . 76 Ile HG2 . 17831 1 792 . 1 1 78 78 ILE HD11 H 1 -0.173 0.02 . 1 . . . . 76 Ile HD1 . 17831 1 793 . 1 1 78 78 ILE HD12 H 1 -0.173 0.02 . 1 . . . . 76 Ile HD1 . 17831 1 794 . 1 1 78 78 ILE HD13 H 1 -0.173 0.02 . 1 . . . . 76 Ile HD1 . 17831 1 795 . 1 1 78 78 ILE C C 13 173.511 0.2 . 1 . . . . 76 Ile C . 17831 1 796 . 1 1 78 78 ILE CA C 13 59.347 0.2 . 1 . . . . 76 Ile CA . 17831 1 797 . 1 1 78 78 ILE CB C 13 42.859 0.2 . 1 . . . . 76 Ile CB . 17831 1 798 . 1 1 78 78 ILE CG1 C 13 25.784 0.2 . 1 . . . . 76 Ile CG1 . 17831 1 799 . 1 1 78 78 ILE CG2 C 13 18.780 0.2 . 1 . . . . 76 Ile CG2 . 17831 1 800 . 1 1 78 78 ILE CD1 C 13 13.476 0.2 . 1 . . . . 76 Ile CD1 . 17831 1 801 . 1 1 78 78 ILE N N 15 121.887 0.2 . 1 . . . . 76 Ile N . 17831 1 802 . 1 1 79 79 TYR H H 1 8.736 0.02 . 1 . . . . 77 Tyr H . 17831 1 803 . 1 1 79 79 TYR HA H 1 5.276 0.02 . 1 . . . . 77 Tyr HA . 17831 1 804 . 1 1 79 79 TYR HB2 H 1 2.216 0.02 . 2 . . . . 77 Tyr HB2 . 17831 1 805 . 1 1 79 79 TYR HB3 H 1 2.976 0.02 . 2 . . . . 77 Tyr HB3 . 17831 1 806 . 1 1 79 79 TYR C C 13 175.079 0.2 . 1 . . . . 77 Tyr C . 17831 1 807 . 1 1 79 79 TYR CA C 13 55.670 0.2 . 1 . . . . 77 Tyr CA . 17831 1 808 . 1 1 79 79 TYR CB C 13 41.606 0.2 . 1 . . . . 77 Tyr CB . 17831 1 809 . 1 1 79 79 TYR N N 15 116.283 0.2 . 1 . . . . 77 Tyr N . 17831 1 810 . 1 1 80 80 ARG H H 1 8.358 0.02 . 1 . . . . 78 Arg H . 17831 1 811 . 1 1 80 80 ARG HA H 1 4.630 0.02 . 1 . . . . 78 Arg HA . 17831 1 812 . 1 1 80 80 ARG HB2 H 1 1.609 0.02 . 2 . . . . 78 Arg HB2 . 17831 1 813 . 1 1 80 80 ARG HB3 H 1 1.966 0.02 . 2 . . . . 78 Arg HB3 . 17831 1 814 . 1 1 80 80 ARG HD2 H 1 3.090 0.02 . 1 . . . . 78 Arg HD2 . 17831 1 815 . 1 1 80 80 ARG HD3 H 1 3.090 0.02 . 1 . . . . 78 Arg HD3 . 17831 1 816 . 1 1 80 80 ARG C C 13 176.088 0.2 . 1 . . . . 78 Arg C . 17831 1 817 . 1 1 80 80 ARG CA C 13 54.618 0.2 . 1 . . . . 78 Arg CA . 17831 1 818 . 1 1 80 80 ARG CB C 13 34.343 0.2 . 1 . . . . 78 Arg CB . 17831 1 819 . 1 1 80 80 ARG N N 15 118.543 0.2 . 1 . . . . 78 Arg N . 17831 1 820 . 1 1 81 81 ASP H H 1 9.009 0.02 . 1 . . . . 79 Asp H . 17831 1 821 . 1 1 81 81 ASP HA H 1 4.391 0.02 . 1 . . . . 79 Asp HA . 17831 1 822 . 1 1 81 81 ASP HB2 H 1 2.928 0.02 . 2 . . . . 79 Asp HB2 . 17831 1 823 . 1 1 81 81 ASP HB3 H 1 3.089 0.02 . 2 . . . . 79 Asp HB3 . 17831 1 824 . 1 1 81 81 ASP C C 13 174.720 0.2 . 1 . . . . 79 Asp C . 17831 1 825 . 1 1 81 81 ASP CA C 13 59.065 0.2 . 1 . . . . 79 Asp CA . 17831 1 826 . 1 1 81 81 ASP CB C 13 40.403 0.2 . 1 . . . . 79 Asp CB . 17831 1 827 . 1 1 81 81 ASP N N 15 115.480 0.2 . 1 . . . . 79 Asp N . 17831 1 828 . 1 1 82 82 ARG H H 1 8.998 0.02 . 1 . . . . 80 Arg H . 17831 1 829 . 1 1 82 82 ARG HA H 1 5.040 0.02 . 1 . . . . 80 Arg HA . 17831 1 830 . 1 1 82 82 ARG HB2 H 1 1.838 0.02 . 1 . . . . 80 Arg HB2 . 17831 1 831 . 1 1 82 82 ARG HB3 H 1 1.838 0.02 . 1 . . . . 80 Arg HB3 . 17831 1 832 . 1 1 82 82 ARG HG2 H 1 1.473 0.02 . 2 . . . . 80 Arg HG2 . 17831 1 833 . 1 1 82 82 ARG HG3 H 1 1.508 0.02 . 2 . . . . 80 Arg HG3 . 17831 1 834 . 1 1 82 82 ARG HD2 H 1 3.147 0.02 . 2 . . . . 80 Arg HD2 . 17831 1 835 . 1 1 82 82 ARG HD3 H 1 3.137 0.02 . 2 . . . . 80 Arg HD3 . 17831 1 836 . 1 1 82 82 ARG C C 13 174.057 0.2 . 1 . . . . 80 Arg C . 17831 1 837 . 1 1 82 82 ARG CA C 13 55.523 0.2 . 1 . . . . 80 Arg CA . 17831 1 838 . 1 1 82 82 ARG CB C 13 32.628 0.2 . 1 . . . . 80 Arg CB . 17831 1 839 . 1 1 82 82 ARG CG C 13 27.052 0.2 . 1 . . . . 80 Arg CG . 17831 1 840 . 1 1 82 82 ARG CD C 13 43.379 0.2 . 1 . . . . 80 Arg CD . 17831 1 841 . 1 1 82 82 ARG N N 15 124.062 0.2 . 1 . . . . 80 Arg N . 17831 1 842 . 1 1 83 83 LEU H H 1 8.713 0.02 . 1 . . . . 81 Leu H . 17831 1 843 . 1 1 83 83 LEU HA H 1 4.582 0.02 . 1 . . . . 81 Leu HA . 17831 1 844 . 1 1 83 83 LEU HB2 H 1 0.756 0.02 . 2 . . . . 81 Leu HB2 . 17831 1 845 . 1 1 83 83 LEU HB3 H 1 1.567 0.02 . 2 . . . . 81 Leu HB3 . 17831 1 846 . 1 1 83 83 LEU HG H 1 1.051 0.02 . 1 . . . . 81 Leu HG . 17831 1 847 . 1 1 83 83 LEU HD11 H 1 -0.025 0.02 . 2 . . . . 81 Leu HD1 . 17831 1 848 . 1 1 83 83 LEU HD12 H 1 -0.025 0.02 . 2 . . . . 81 Leu HD1 . 17831 1 849 . 1 1 83 83 LEU HD13 H 1 -0.025 0.02 . 2 . . . . 81 Leu HD1 . 17831 1 850 . 1 1 83 83 LEU HD21 H 1 -0.259 0.02 . 2 . . . . 81 Leu HD2 . 17831 1 851 . 1 1 83 83 LEU HD22 H 1 -0.259 0.02 . 2 . . . . 81 Leu HD2 . 17831 1 852 . 1 1 83 83 LEU HD23 H 1 -0.259 0.02 . 2 . . . . 81 Leu HD2 . 17831 1 853 . 1 1 83 83 LEU C C 13 174.281 0.2 . 1 . . . . 81 Leu C . 17831 1 854 . 1 1 83 83 LEU CA C 13 54.026 0.2 . 1 . . . . 81 Leu CA . 17831 1 855 . 1 1 83 83 LEU CB C 13 45.405 0.2 . 1 . . . . 81 Leu CB . 17831 1 856 . 1 1 83 83 LEU CG C 13 27.021 0.2 . 1 . . . . 81 Leu CG . 17831 1 857 . 1 1 83 83 LEU CD1 C 13 21.278 0.2 . 2 . . . . 81 Leu CD1 . 17831 1 858 . 1 1 83 83 LEU CD2 C 13 26.396 0.2 . 2 . . . . 81 Leu CD2 . 17831 1 859 . 1 1 83 83 LEU N N 15 126.191 0.2 . 1 . . . . 81 Leu N . 17831 1 860 . 1 1 84 84 THR H H 1 8.532 0.02 . 1 . . . . 82 Thr H . 17831 1 861 . 1 1 84 84 THR HA H 1 5.235 0.02 . 1 . . . . 82 Thr HA . 17831 1 862 . 1 1 84 84 THR HB H 1 3.875 0.02 . 1 . . . . 82 Thr HB . 17831 1 863 . 1 1 84 84 THR HG21 H 1 1.046 0.02 . 1 . . . . 82 Thr HG2 . 17831 1 864 . 1 1 84 84 THR HG22 H 1 1.046 0.02 . 1 . . . . 82 Thr HG2 . 17831 1 865 . 1 1 84 84 THR HG23 H 1 1.046 0.02 . 1 . . . . 82 Thr HG2 . 17831 1 866 . 1 1 84 84 THR C C 13 172.529 0.2 . 1 . . . . 82 Thr C . 17831 1 867 . 1 1 84 84 THR CA C 13 61.232 0.2 . 1 . . . . 82 Thr CA . 17831 1 868 . 1 1 84 84 THR CB C 13 70.446 0.2 . 1 . . . . 82 Thr CB . 17831 1 869 . 1 1 84 84 THR CG2 C 13 21.319 0.2 . 1 . . . . 82 Thr CG2 . 17831 1 870 . 1 1 84 84 THR N N 15 123.547 0.2 . 1 . . . . 82 Thr N . 17831 1 871 . 1 1 85 85 LEU H H 1 9.701 0.02 . 1 . . . . 83 Leu H . 17831 1 872 . 1 1 85 85 LEU HA H 1 5.084 0.02 . 1 . . . . 83 Leu HA . 17831 1 873 . 1 1 85 85 LEU HB2 H 1 1.533 0.02 . 2 . . . . 83 Leu HB2 . 17831 1 874 . 1 1 85 85 LEU HB3 H 1 1.814 0.02 . 2 . . . . 83 Leu HB3 . 17831 1 875 . 1 1 85 85 LEU HG H 1 1.620 0.02 . 1 . . . . 83 Leu HG . 17831 1 876 . 1 1 85 85 LEU HD11 H 1 0.939 0.02 . 2 . . . . 83 Leu HD1 . 17831 1 877 . 1 1 85 85 LEU HD12 H 1 0.939 0.02 . 2 . . . . 83 Leu HD1 . 17831 1 878 . 1 1 85 85 LEU HD13 H 1 0.939 0.02 . 2 . . . . 83 Leu HD1 . 17831 1 879 . 1 1 85 85 LEU HD21 H 1 0.894 0.02 . 2 . . . . 83 Leu HD2 . 17831 1 880 . 1 1 85 85 LEU HD22 H 1 0.894 0.02 . 2 . . . . 83 Leu HD2 . 17831 1 881 . 1 1 85 85 LEU HD23 H 1 0.894 0.02 . 2 . . . . 83 Leu HD2 . 17831 1 882 . 1 1 85 85 LEU C C 13 173.095 0.2 . 1 . . . . 83 Leu C . 17831 1 883 . 1 1 85 85 LEU CA C 13 50.737 0.2 . 1 . . . . 83 Leu CA . 17831 1 884 . 1 1 85 85 LEU CB C 13 45.668 0.2 . 1 . . . . 83 Leu CB . 17831 1 885 . 1 1 85 85 LEU CG C 13 26.979 0.2 . 1 . . . . 83 Leu CG . 17831 1 886 . 1 1 85 85 LEU CD1 C 13 25.969 0.2 . 2 . . . . 83 Leu CD1 . 17831 1 887 . 1 1 85 85 LEU CD2 C 13 25.632 0.2 . 2 . . . . 83 Leu CD2 . 17831 1 888 . 1 1 85 85 LEU N N 15 128.161 0.2 . 1 . . . . 83 Leu N . 17831 1 889 . 1 1 86 86 PRO HA H 1 5.172 0.02 . 1 . . . . 84 Pro HA . 17831 1 890 . 1 1 86 86 PRO HB2 H 1 1.981 0.02 . 2 . . . . 84 Pro HB2 . 17831 1 891 . 1 1 86 86 PRO HB3 H 1 2.243 0.02 . 2 . . . . 84 Pro HB3 . 17831 1 892 . 1 1 86 86 PRO C C 13 176.393 0.2 . 1 . . . . 84 Pro C . 17831 1 893 . 1 1 86 86 PRO CA C 13 61.727 0.2 . 1 . . . . 84 Pro CA . 17831 1 894 . 1 1 86 86 PRO CB C 13 31.862 0.2 . 1 . . . . 84 Pro CB . 17831 1 895 . 1 1 87 87 VAL H H 1 9.315 0.02 . 1 . . . . 85 Val H . 17831 1 896 . 1 1 87 87 VAL HA H 1 4.443 0.02 . 1 . . . . 85 Val HA . 17831 1 897 . 1 1 87 87 VAL HB H 1 1.934 0.02 . 1 . . . . 85 Val HB . 17831 1 898 . 1 1 87 87 VAL HG11 H 1 0.845 0.02 . 1 . . . . 85 Val HG1 . 17831 1 899 . 1 1 87 87 VAL HG12 H 1 0.845 0.02 . 1 . . . . 85 Val HG1 . 17831 1 900 . 1 1 87 87 VAL HG13 H 1 0.845 0.02 . 1 . . . . 85 Val HG1 . 17831 1 901 . 1 1 87 87 VAL HG21 H 1 0.845 0.02 . 1 . . . . 85 Val HG2 . 17831 1 902 . 1 1 87 87 VAL HG22 H 1 0.845 0.02 . 1 . . . . 85 Val HG2 . 17831 1 903 . 1 1 87 87 VAL HG23 H 1 0.845 0.02 . 1 . . . . 85 Val HG2 . 17831 1 904 . 1 1 87 87 VAL C C 13 175.392 0.2 . 1 . . . . 85 Val C . 17831 1 905 . 1 1 87 87 VAL CA C 13 60.696 0.2 . 1 . . . . 85 Val CA . 17831 1 906 . 1 1 87 87 VAL CB C 13 35.443 0.2 . 1 . . . . 85 Val CB . 17831 1 907 . 1 1 87 87 VAL CG1 C 13 21.653 0.2 . 1 . . . . 85 Val CG1 . 17831 1 908 . 1 1 87 87 VAL CG2 C 13 21.653 0.2 . 1 . . . . 85 Val CG2 . 17831 1 909 . 1 1 87 87 VAL N N 15 125.245 0.2 . 1 . . . . 85 Val N . 17831 1 910 . 1 1 88 88 THR H H 1 9.334 0.02 . 1 . . . . 86 Thr H . 17831 1 911 . 1 1 88 88 THR HA H 1 4.909 0.02 . 1 . . . . 86 Thr HA . 17831 1 912 . 1 1 88 88 THR HB H 1 3.958 0.02 . 1 . . . . 86 Thr HB . 17831 1 913 . 1 1 88 88 THR C C 13 173.342 0.2 . 1 . . . . 86 Thr C . 17831 1 914 . 1 1 88 88 THR CA C 13 62.301 0.2 . 1 . . . . 86 Thr CA . 17831 1 915 . 1 1 88 88 THR CB C 13 70.017 0.2 . 1 . . . . 86 Thr CB . 17831 1 916 . 1 1 88 88 THR N N 15 125.286 0.2 . 1 . . . . 86 Thr N . 17831 1 917 . 1 1 89 89 ILE H H 1 9.882 0.02 . 1 . . . . 87 Ile H . 17831 1 918 . 1 1 89 89 ILE HA H 1 4.129 0.02 . 1 . . . . 87 Ile HA . 17831 1 919 . 1 1 89 89 ILE HB H 1 2.001 0.02 . 1 . . . . 87 Ile HB . 17831 1 920 . 1 1 89 89 ILE HG12 H 1 0.867 0.02 . 2 . . . . 87 Ile HG12 . 17831 1 921 . 1 1 89 89 ILE HG13 H 1 1.475 0.02 . 2 . . . . 87 Ile HG13 . 17831 1 922 . 1 1 89 89 ILE HG21 H 1 0.636 0.02 . 1 . . . . 87 Ile HG2 . 17831 1 923 . 1 1 89 89 ILE HG22 H 1 0.636 0.02 . 1 . . . . 87 Ile HG2 . 17831 1 924 . 1 1 89 89 ILE HG23 H 1 0.636 0.02 . 1 . . . . 87 Ile HG2 . 17831 1 925 . 1 1 89 89 ILE HD11 H 1 0.752 0.02 . 1 . . . . 87 Ile HD1 . 17831 1 926 . 1 1 89 89 ILE HD12 H 1 0.752 0.02 . 1 . . . . 87 Ile HD1 . 17831 1 927 . 1 1 89 89 ILE HD13 H 1 0.752 0.02 . 1 . . . . 87 Ile HD1 . 17831 1 928 . 1 1 89 89 ILE C C 13 175.261 0.2 . 1 . . . . 87 Ile C . 17831 1 929 . 1 1 89 89 ILE CA C 13 59.880 0.2 . 1 . . . . 87 Ile CA . 17831 1 930 . 1 1 89 89 ILE CB C 13 38.252 0.2 . 1 . . . . 87 Ile CB . 17831 1 931 . 1 1 89 89 ILE CG1 C 13 26.222 0.2 . 1 . . . . 87 Ile CG1 . 17831 1 932 . 1 1 89 89 ILE CG2 C 13 18.813 0.2 . 1 . . . . 87 Ile CG2 . 17831 1 933 . 1 1 89 89 ILE CD1 C 13 14.771 0.2 . 1 . . . . 87 Ile CD1 . 17831 1 934 . 1 1 89 89 ILE N N 15 128.207 0.2 . 1 . . . . 87 Ile N . 17831 1 935 . 1 1 90 90 ASN H H 1 9.026 0.02 . 1 . . . . 88 Asn H . 17831 1 936 . 1 1 90 90 ASN HA H 1 4.736 0.02 . 1 . . . . 88 Asn HA . 17831 1 937 . 1 1 90 90 ASN HB2 H 1 2.857 0.02 . 2 . . . . 88 Asn HB2 . 17831 1 938 . 1 1 90 90 ASN HB3 H 1 2.339 0.02 . 2 . . . . 88 Asn HB3 . 17831 1 939 . 1 1 90 90 ASN C C 13 175.124 0.2 . 1 . . . . 88 Asn C . 17831 1 940 . 1 1 90 90 ASN CA C 13 55.551 0.2 . 1 . . . . 88 Asn CA . 17831 1 941 . 1 1 90 90 ASN CB C 13 39.169 0.2 . 1 . . . . 88 Asn CB . 17831 1 942 . 1 1 90 90 ASN N N 15 127.444 0.2 . 1 . . . . 88 Asn N . 17831 1 943 . 1 1 91 91 GLN H H 1 7.726 0.02 . 1 . . . . 89 Gln H . 17831 1 944 . 1 1 91 91 GLN HA H 1 4.176 0.02 . 1 . . . . 89 Gln HA . 17831 1 945 . 1 1 91 91 GLN HB2 H 1 2.015 0.02 . 2 . . . . 89 Gln HB2 . 17831 1 946 . 1 1 91 91 GLN HB3 H 1 2.016 0.02 . 2 . . . . 89 Gln HB3 . 17831 1 947 . 1 1 91 91 GLN HG2 H 1 2.322 0.02 . 2 . . . . 89 Gln HG2 . 17831 1 948 . 1 1 91 91 GLN HG3 H 1 2.397 0.02 . 2 . . . . 89 Gln HG3 . 17831 1 949 . 1 1 91 91 GLN C C 13 173.145 0.2 . 1 . . . . 89 Gln C . 17831 1 950 . 1 1 91 91 GLN CA C 13 55.768 0.2 . 1 . . . . 89 Gln CA . 17831 1 951 . 1 1 91 91 GLN CB C 13 30.797 0.2 . 1 . . . . 89 Gln CB . 17831 1 952 . 1 1 91 91 GLN CG C 13 33.010 0.2 . 1 . . . . 89 Gln CG . 17831 1 953 . 1 1 91 91 GLN N N 15 115.441 0.2 . 1 . . . . 89 Gln N . 17831 1 954 . 1 1 92 92 ALA H H 1 9.342 0.02 . 1 . . . . 90 Ala H . 17831 1 955 . 1 1 92 92 ALA HA H 1 4.740 0.02 . 1 . . . . 90 Ala HA . 17831 1 956 . 1 1 92 92 ALA HB1 H 1 1.271 0.02 . 1 . . . . 90 Ala HB . 17831 1 957 . 1 1 92 92 ALA HB2 H 1 1.271 0.02 . 1 . . . . 90 Ala HB . 17831 1 958 . 1 1 92 92 ALA HB3 H 1 1.271 0.02 . 1 . . . . 90 Ala HB . 17831 1 959 . 1 1 92 92 ALA C C 13 176.138 0.2 . 1 . . . . 90 Ala C . 17831 1 960 . 1 1 92 92 ALA CA C 13 53.158 0.2 . 1 . . . . 90 Ala CA . 17831 1 961 . 1 1 92 92 ALA CB C 13 21.274 0.2 . 1 . . . . 90 Ala CB . 17831 1 962 . 1 1 92 92 ALA N N 15 125.683 0.2 . 1 . . . . 90 Ala N . 17831 1 963 . 1 1 93 93 SER H H 1 8.390 0.02 . 1 . . . . 91 Ser H . 17831 1 964 . 1 1 93 93 SER HA H 1 4.653 0.02 . 1 . . . . 91 Ser HA . 17831 1 965 . 1 1 93 93 SER HB2 H 1 3.816 0.02 . 2 . . . . 91 Ser HB2 . 17831 1 966 . 1 1 93 93 SER HB3 H 1 4.025 0.02 . 2 . . . . 91 Ser HB3 . 17831 1 967 . 1 1 93 93 SER C C 13 172.775 0.2 . 1 . . . . 91 Ser C . 17831 1 968 . 1 1 93 93 SER CA C 13 57.789 0.2 . 1 . . . . 91 Ser CA . 17831 1 969 . 1 1 93 93 SER CB C 13 64.496 0.2 . 1 . . . . 91 Ser CB . 17831 1 970 . 1 1 93 93 SER N N 15 120.048 0.2 . 1 . . . . 91 Ser N . 17831 1 971 . 1 1 94 94 ALA H H 1 8.498 0.02 . 1 . . . . 92 Ala H . 17831 1 972 . 1 1 94 94 ALA HA H 1 4.179 0.02 . 1 . . . . 92 Ala HA . 17831 1 973 . 1 1 94 94 ALA HB1 H 1 1.322 0.02 . 1 . . . . 92 Ala HB . 17831 1 974 . 1 1 94 94 ALA HB2 H 1 1.322 0.02 . 1 . . . . 92 Ala HB . 17831 1 975 . 1 1 94 94 ALA HB3 H 1 1.322 0.02 . 1 . . . . 92 Ala HB . 17831 1 976 . 1 1 94 94 ALA C C 13 179.320 0.2 . 1 . . . . 92 Ala C . 17831 1 977 . 1 1 94 94 ALA CA C 13 53.851 0.2 . 1 . . . . 92 Ala CA . 17831 1 978 . 1 1 94 94 ALA CB C 13 17.729 0.2 . 1 . . . . 92 Ala CB . 17831 1 979 . 1 1 94 94 ALA N N 15 123.702 0.2 . 1 . . . . 92 Ala N . 17831 1 980 . 1 1 95 95 GLY H H 1 9.109 0.02 . 1 . . . . 93 Gly H . 17831 1 981 . 1 1 95 95 GLY HA2 H 1 3.729 0.02 . 2 . . . . 93 Gly HA2 . 17831 1 982 . 1 1 95 95 GLY HA3 H 1 4.033 0.02 . 2 . . . . 93 Gly HA3 . 17831 1 983 . 1 1 95 95 GLY C C 13 174.449 0.2 . 1 . . . . 93 Gly C . 17831 1 984 . 1 1 95 95 GLY CA C 13 45.242 0.2 . 1 . . . . 93 Gly CA . 17831 1 985 . 1 1 95 95 GLY N N 15 112.425 0.2 . 1 . . . . 93 Gly N . 17831 1 986 . 1 1 96 96 ALA H H 1 7.869 0.02 . 1 . . . . 94 Ala H . 17831 1 987 . 1 1 96 96 ALA HA H 1 4.497 0.02 . 1 . . . . 94 Ala HA . 17831 1 988 . 1 1 96 96 ALA HB1 H 1 1.640 0.02 . 1 . . . . 94 Ala HB . 17831 1 989 . 1 1 96 96 ALA HB2 H 1 1.640 0.02 . 1 . . . . 94 Ala HB . 17831 1 990 . 1 1 96 96 ALA HB3 H 1 1.640 0.02 . 1 . . . . 94 Ala HB . 17831 1 991 . 1 1 96 96 ALA C C 13 177.119 0.2 . 1 . . . . 94 Ala C . 17831 1 992 . 1 1 96 96 ALA CA C 13 52.950 0.2 . 1 . . . . 94 Ala CA . 17831 1 993 . 1 1 96 96 ALA CB C 13 22.052 0.2 . 1 . . . . 94 Ala CB . 17831 1 994 . 1 1 96 96 ALA N N 15 122.521 0.2 . 1 . . . . 94 Ala N . 17831 1 995 . 1 1 97 97 THR H H 1 8.333 0.02 . 1 . . . . 95 Thr H . 17831 1 996 . 1 1 97 97 THR HA H 1 5.155 0.02 . 1 . . . . 95 Thr HA . 17831 1 997 . 1 1 97 97 THR HB H 1 3.848 0.02 . 1 . . . . 95 Thr HB . 17831 1 998 . 1 1 97 97 THR C C 13 173.551 0.2 . 1 . . . . 95 Thr C . 17831 1 999 . 1 1 97 97 THR CA C 13 59.557 0.2 . 1 . . . . 95 Thr CA . 17831 1 1000 . 1 1 97 97 THR CB C 13 74.133 0.2 . 1 . . . . 95 Thr CB . 17831 1 1001 . 1 1 97 97 THR N N 15 109.165 0.2 . 1 . . . . 95 Thr N . 17831 1 1002 . 1 1 98 98 LEU H H 1 8.830 0.02 . 1 . . . . 96 Leu H . 17831 1 1003 . 1 1 98 98 LEU HA H 1 4.874 0.02 . 1 . . . . 96 Leu HA . 17831 1 1004 . 1 1 98 98 LEU HB2 H 1 1.308 0.02 . 2 . . . . 96 Leu HB2 . 17831 1 1005 . 1 1 98 98 LEU HB3 H 1 1.306 0.02 . 2 . . . . 96 Leu HB3 . 17831 1 1006 . 1 1 98 98 LEU HG H 1 1.438 0.02 . 1 . . . . 96 Leu HG . 17831 1 1007 . 1 1 98 98 LEU HD11 H 1 0.641 0.02 . 2 . . . . 96 Leu HD1 . 17831 1 1008 . 1 1 98 98 LEU HD12 H 1 0.641 0.02 . 2 . . . . 96 Leu HD1 . 17831 1 1009 . 1 1 98 98 LEU HD13 H 1 0.641 0.02 . 2 . . . . 96 Leu HD1 . 17831 1 1010 . 1 1 98 98 LEU HD21 H 1 0.684 0.02 . 2 . . . . 96 Leu HD2 . 17831 1 1011 . 1 1 98 98 LEU HD22 H 1 0.684 0.02 . 2 . . . . 96 Leu HD2 . 17831 1 1012 . 1 1 98 98 LEU HD23 H 1 0.684 0.02 . 2 . . . . 96 Leu HD2 . 17831 1 1013 . 1 1 98 98 LEU C C 13 175.713 0.2 . 1 . . . . 96 Leu C . 17831 1 1014 . 1 1 98 98 LEU CA C 13 53.556 0.2 . 1 . . . . 96 Leu CA . 17831 1 1015 . 1 1 98 98 LEU CB C 13 45.352 0.2 . 1 . . . . 96 Leu CB . 17831 1 1016 . 1 1 98 98 LEU CG C 13 26.378 0.2 . 1 . . . . 96 Leu CG . 17831 1 1017 . 1 1 98 98 LEU CD1 C 13 25.705 0.2 . 2 . . . . 96 Leu CD1 . 17831 1 1018 . 1 1 98 98 LEU CD2 C 13 25.031 0.2 . 2 . . . . 96 Leu CD2 . 17831 1 1019 . 1 1 98 98 LEU N N 15 117.236 0.2 . 1 . . . . 96 Leu N . 17831 1 1020 . 1 1 99 99 THR H H 1 8.849 0.02 . 1 . . . . 97 Thr H . 17831 1 1021 . 1 1 99 99 THR HA H 1 4.872 0.02 . 1 . . . . 97 Thr HA . 17831 1 1022 . 1 1 99 99 THR HB H 1 3.973 0.02 . 1 . . . . 97 Thr HB . 17831 1 1023 . 1 1 99 99 THR HG21 H 1 1.049 0.02 . 1 . . . . 97 Thr HG2 . 17831 1 1024 . 1 1 99 99 THR HG22 H 1 1.049 0.02 . 1 . . . . 97 Thr HG2 . 17831 1 1025 . 1 1 99 99 THR HG23 H 1 1.049 0.02 . 1 . . . . 97 Thr HG2 . 17831 1 1026 . 1 1 99 99 THR C C 13 173.940 0.2 . 1 . . . . 97 Thr C . 17831 1 1027 . 1 1 99 99 THR CA C 13 62.870 0.2 . 1 . . . . 97 Thr CA . 17831 1 1028 . 1 1 99 99 THR CB C 13 69.259 0.2 . 1 . . . . 97 Thr CB . 17831 1 1029 . 1 1 99 99 THR CG2 C 13 21.845 0.2 . 1 . . . . 97 Thr CG2 . 17831 1 1030 . 1 1 99 99 THR N N 15 121.892 0.2 . 1 . . . . 97 Thr N . 17831 1 1031 . 1 1 100 100 VAL H H 1 9.371 0.02 . 1 . . . . 98 Val H . 17831 1 1032 . 1 1 100 100 VAL HA H 1 4.977 0.02 . 1 . . . . 98 Val HA . 17831 1 1033 . 1 1 100 100 VAL HB H 1 1.848 0.02 . 1 . . . . 98 Val HB . 17831 1 1034 . 1 1 100 100 VAL HG11 H 1 0.882 0.02 . 2 . . . . 98 Val HG1 . 17831 1 1035 . 1 1 100 100 VAL HG12 H 1 0.882 0.02 . 2 . . . . 98 Val HG1 . 17831 1 1036 . 1 1 100 100 VAL HG13 H 1 0.882 0.02 . 2 . . . . 98 Val HG1 . 17831 1 1037 . 1 1 100 100 VAL HG21 H 1 1.031 0.02 . 2 . . . . 98 Val HG2 . 17831 1 1038 . 1 1 100 100 VAL HG22 H 1 1.031 0.02 . 2 . . . . 98 Val HG2 . 17831 1 1039 . 1 1 100 100 VAL HG23 H 1 1.031 0.02 . 2 . . . . 98 Val HG2 . 17831 1 1040 . 1 1 100 100 VAL C C 13 173.756 0.2 . 1 . . . . 98 Val C . 17831 1 1041 . 1 1 100 100 VAL CA C 13 60.812 0.2 . 1 . . . . 98 Val CA . 17831 1 1042 . 1 1 100 100 VAL CB C 13 34.174 0.2 . 1 . . . . 98 Val CB . 17831 1 1043 . 1 1 100 100 VAL N N 15 129.946 0.2 . 1 . . . . 98 Val N . 17831 1 1044 . 1 1 101 101 THR H H 1 9.182 0.02 . 1 . . . . 99 Thr H . 17831 1 1045 . 1 1 101 101 THR HA H 1 5.779 0.02 . 1 . . . . 99 Thr HA . 17831 1 1046 . 1 1 101 101 THR HB H 1 3.815 0.02 . 1 . . . . 99 Thr HB . 17831 1 1047 . 1 1 101 101 THR HG21 H 1 1.133 0.02 . 1 . . . . 99 Thr HG2 . 17831 1 1048 . 1 1 101 101 THR HG22 H 1 1.133 0.02 . 1 . . . . 99 Thr HG2 . 17831 1 1049 . 1 1 101 101 THR HG23 H 1 1.133 0.02 . 1 . . . . 99 Thr HG2 . 17831 1 1050 . 1 1 101 101 THR C C 13 172.579 0.2 . 1 . . . . 99 Thr C . 17831 1 1051 . 1 1 101 101 THR CA C 13 60.262 0.2 . 1 . . . . 99 Thr CA . 17831 1 1052 . 1 1 101 101 THR CB C 13 71.326 0.2 . 1 . . . . 99 Thr CB . 17831 1 1053 . 1 1 101 101 THR CG2 C 13 21.526 0.2 . 1 . . . . 99 Thr CG2 . 17831 1 1054 . 1 1 101 101 THR N N 15 124.073 0.2 . 1 . . . . 99 Thr N . 17831 1 1055 . 1 1 102 102 TYR H H 1 8.212 0.02 . 1 . . . . 100 Tyr H . 17831 1 1056 . 1 1 102 102 TYR HA H 1 4.833 0.02 . 1 . . . . 100 Tyr HA . 17831 1 1057 . 1 1 102 102 TYR HB2 H 1 2.528 0.02 . 2 . . . . 100 Tyr HB2 . 17831 1 1058 . 1 1 102 102 TYR HB3 H 1 2.982 0.02 . 2 . . . . 100 Tyr HB3 . 17831 1 1059 . 1 1 102 102 TYR C C 13 172.397 0.2 . 1 . . . . 100 Tyr C . 17831 1 1060 . 1 1 102 102 TYR CA C 13 55.747 0.2 . 1 . . . . 100 Tyr CA . 17831 1 1061 . 1 1 102 102 TYR CB C 13 38.787 0.2 . 1 . . . . 100 Tyr CB . 17831 1 1062 . 1 1 102 102 TYR N N 15 117.427 0.2 . 1 . . . . 100 Tyr N . 17831 1 1063 . 1 1 103 103 GLN H H 1 8.337 0.02 . 1 . . . . 101 Gln H . 17831 1 1064 . 1 1 103 103 GLN HA H 1 5.049 0.02 . 1 . . . . 101 Gln HA . 17831 1 1065 . 1 1 103 103 GLN HB2 H 1 1.660 0.02 . 2 . . . . 101 Gln HB2 . 17831 1 1066 . 1 1 103 103 GLN HB3 H 1 1.987 0.02 . 2 . . . . 101 Gln HB3 . 17831 1 1067 . 1 1 103 103 GLN HG2 H 1 2.265 0.02 . 2 . . . . 101 Gln HG2 . 17831 1 1068 . 1 1 103 103 GLN HG3 H 1 2.499 0.02 . 2 . . . . 101 Gln HG3 . 17831 1 1069 . 1 1 103 103 GLN C C 13 173.938 0.2 . 1 . . . . 101 Gln C . 17831 1 1070 . 1 1 103 103 GLN CA C 13 54.820 0.2 . 1 . . . . 101 Gln CA . 17831 1 1071 . 1 1 103 103 GLN CB C 13 32.663 0.2 . 1 . . . . 101 Gln CB . 17831 1 1072 . 1 1 103 103 GLN CG C 13 33.635 0.2 . 1 . . . . 101 Gln CG . 17831 1 1073 . 1 1 103 103 GLN N N 15 117.968 0.2 . 1 . . . . 101 Gln N . 17831 1 1074 . 1 1 104 104 GLY H H 1 8.103 0.02 . 1 . . . . 102 Gly H . 17831 1 1075 . 1 1 104 104 GLY HA2 H 1 3.535 0.02 . 2 . . . . 102 Gly HA2 . 17831 1 1076 . 1 1 104 104 GLY HA3 H 1 4.411 0.02 . 2 . . . . 102 Gly HA3 . 17831 1 1077 . 1 1 104 104 GLY C C 13 171.340 0.2 . 1 . . . . 102 Gly C . 17831 1 1078 . 1 1 104 104 GLY CA C 13 45.265 0.2 . 1 . . . . 102 Gly CA . 17831 1 1079 . 1 1 104 104 GLY N N 15 114.319 0.2 . 1 . . . . 102 Gly N . 17831 1 1080 . 1 1 105 105 CYS HA H 1 5.257 0.02 . 1 . . . . 103 Cys HA . 17831 1 1081 . 1 1 105 105 CYS HB2 H 1 2.054 0.02 . 2 . . . . 103 Cys HB2 . 17831 1 1082 . 1 1 105 105 CYS HB3 H 1 2.727 0.02 . 2 . . . . 103 Cys HB3 . 17831 1 1083 . 1 1 105 105 CYS C C 13 175.704 0.2 . 1 . . . . 103 Cys C . 17831 1 1084 . 1 1 105 105 CYS CA C 13 56.364 0.2 . 1 . . . . 103 Cys CA . 17831 1 1085 . 1 1 105 105 CYS CB C 13 51.937 0.2 . 1 . . . . 103 Cys CB . 17831 1 1086 . 1 1 106 106 ALA H H 1 8.858 0.02 . 1 . . . . 104 Ala H . 17831 1 1087 . 1 1 106 106 ALA HA H 1 4.519 0.02 . 1 . . . . 104 Ala HA . 17831 1 1088 . 1 1 106 106 ALA HB1 H 1 0.975 0.02 . 1 . . . . 104 Ala HB . 17831 1 1089 . 1 1 106 106 ALA HB2 H 1 0.975 0.02 . 1 . . . . 104 Ala HB . 17831 1 1090 . 1 1 106 106 ALA HB3 H 1 0.975 0.02 . 1 . . . . 104 Ala HB . 17831 1 1091 . 1 1 106 106 ALA C C 13 179.132 0.2 . 1 . . . . 104 Ala C . 17831 1 1092 . 1 1 106 106 ALA CA C 13 49.969 0.2 . 1 . . . . 104 Ala CA . 17831 1 1093 . 1 1 106 106 ALA CB C 13 21.706 0.2 . 1 . . . . 104 Ala CB . 17831 1 1094 . 1 1 106 106 ALA N N 15 120.705 0.2 . 1 . . . . 104 Ala N . 17831 1 1095 . 1 1 107 107 ASP H H 1 8.916 0.02 . 1 . . . . 105 Asp H . 17831 1 1096 . 1 1 107 107 ASP HA H 1 4.518 0.02 . 1 . . . . 105 Asp HA . 17831 1 1097 . 1 1 107 107 ASP HB2 H 1 2.465 0.02 . 2 . . . . 105 Asp HB2 . 17831 1 1098 . 1 1 107 107 ASP HB3 H 1 2.666 0.02 . 2 . . . . 105 Asp HB3 . 17831 1 1099 . 1 1 107 107 ASP C C 13 177.434 0.2 . 1 . . . . 105 Asp C . 17831 1 1100 . 1 1 107 107 ASP CA C 13 57.771 0.2 . 1 . . . . 105 Asp CA . 17831 1 1101 . 1 1 107 107 ASP CB C 13 40.538 0.2 . 1 . . . . 105 Asp CB . 17831 1 1102 . 1 1 107 107 ASP N N 15 125.658 0.2 . 1 . . . . 105 Asp N . 17831 1 1103 . 1 1 108 108 ALA H H 1 7.845 0.02 . 1 . . . . 106 Ala H . 17831 1 1104 . 1 1 108 108 ALA HA H 1 4.293 0.02 . 1 . . . . 106 Ala HA . 17831 1 1105 . 1 1 108 108 ALA HB1 H 1 1.474 0.02 . 1 . . . . 106 Ala HB . 17831 1 1106 . 1 1 108 108 ALA HB2 H 1 1.474 0.02 . 1 . . . . 106 Ala HB . 17831 1 1107 . 1 1 108 108 ALA HB3 H 1 1.474 0.02 . 1 . . . . 106 Ala HB . 17831 1 1108 . 1 1 108 108 ALA C C 13 178.195 0.2 . 1 . . . . 106 Ala C . 17831 1 1109 . 1 1 108 108 ALA CA C 13 53.359 0.2 . 1 . . . . 106 Ala CA . 17831 1 1110 . 1 1 108 108 ALA CB C 13 18.726 0.2 . 1 . . . . 106 Ala CB . 17831 1 1111 . 1 1 108 108 ALA N N 15 117.797 0.2 . 1 . . . . 106 Ala N . 17831 1 1112 . 1 1 109 109 GLY H H 1 7.728 0.02 . 1 . . . . 107 Gly H . 17831 1 1113 . 1 1 109 109 GLY HA2 H 1 3.873 0.02 . 2 . . . . 107 Gly HA2 . 17831 1 1114 . 1 1 109 109 GLY HA3 H 1 4.487 0.02 . 2 . . . . 107 Gly HA3 . 17831 1 1115 . 1 1 109 109 GLY C C 13 173.038 0.2 . 1 . . . . 107 Gly C . 17831 1 1116 . 1 1 109 109 GLY CA C 13 46.178 0.2 . 1 . . . . 107 Gly CA . 17831 1 1117 . 1 1 109 109 GLY N N 15 103.819 0.2 . 1 . . . . 107 Gly N . 17831 1 1118 . 1 1 110 110 PHE H H 1 6.851 0.02 . 1 . . . . 108 Phe H . 17831 1 1119 . 1 1 110 110 PHE HA H 1 4.679 0.02 . 1 . . . . 108 Phe HA . 17831 1 1120 . 1 1 110 110 PHE HB2 H 1 2.827 0.02 . 2 . . . . 108 Phe HB2 . 17831 1 1121 . 1 1 110 110 PHE HB3 H 1 2.466 0.02 . 2 . . . . 108 Phe HB3 . 17831 1 1122 . 1 1 110 110 PHE CA C 13 56.800 0.2 . 1 . . . . 108 Phe CA . 17831 1 1123 . 1 1 110 110 PHE N N 15 117.941 0.2 . 1 . . . . 108 Phe N . 17831 1 1124 . 1 1 114 114 PRO HA H 1 4.327 0.02 . 1 . . . . 112 Pro HA . 17831 1 1125 . 1 1 114 114 PRO HB2 H 1 1.984 0.02 . 2 . . . . 112 Pro HB2 . 17831 1 1126 . 1 1 114 114 PRO HB3 H 1 1.658 0.02 . 2 . . . . 112 Pro HB3 . 17831 1 1127 . 1 1 114 114 PRO C C 13 175.870 0.2 . 1 . . . . 112 Pro C . 17831 1 1128 . 1 1 114 114 PRO CA C 13 63.505 0.2 . 1 . . . . 112 Pro CA . 17831 1 1129 . 1 1 114 114 PRO CB C 13 31.461 0.2 . 1 . . . . 112 Pro CB . 17831 1 1130 . 1 1 115 115 GLU H H 1 8.621 0.02 . 1 . . . . 113 Glu H . 17831 1 1131 . 1 1 115 115 GLU HA H 1 4.360 0.02 . 1 . . . . 113 Glu HA . 17831 1 1132 . 1 1 115 115 GLU HB2 H 1 0.935 0.02 . 2 . . . . 113 Glu HB2 . 17831 1 1133 . 1 1 115 115 GLU HB3 H 1 1.256 0.02 . 2 . . . . 113 Glu HB3 . 17831 1 1134 . 1 1 115 115 GLU HG2 H 1 1.969 0.02 . 2 . . . . 113 Glu HG2 . 17831 1 1135 . 1 1 115 115 GLU HG3 H 1 2.067 0.02 . 2 . . . . 113 Glu HG3 . 17831 1 1136 . 1 1 115 115 GLU C C 13 174.542 0.2 . 1 . . . . 113 Glu C . 17831 1 1137 . 1 1 115 115 GLU CA C 13 54.241 0.2 . 1 . . . . 113 Glu CA . 17831 1 1138 . 1 1 115 115 GLU CB C 13 32.917 0.2 . 1 . . . . 113 Glu CB . 17831 1 1139 . 1 1 115 115 GLU CG C 13 35.611 0.2 . 1 . . . . 113 Glu CG . 17831 1 1140 . 1 1 115 115 GLU N N 15 125.351 0.2 . 1 . . . . 113 Glu N . 17831 1 1141 . 1 1 116 116 THR H H 1 8.240 0.02 . 1 . . . . 114 Thr H . 17831 1 1142 . 1 1 116 116 THR HA H 1 5.090 0.02 . 1 . . . . 114 Thr HA . 17831 1 1143 . 1 1 116 116 THR HB H 1 3.701 0.02 . 1 . . . . 114 Thr HB . 17831 1 1144 . 1 1 116 116 THR HG21 H 1 0.946 0.02 . 1 . . . . 114 Thr HG2 . 17831 1 1145 . 1 1 116 116 THR HG22 H 1 0.946 0.02 . 1 . . . . 114 Thr HG2 . 17831 1 1146 . 1 1 116 116 THR HG23 H 1 0.946 0.02 . 1 . . . . 114 Thr HG2 . 17831 1 1147 . 1 1 116 116 THR C C 13 174.017 0.2 . 1 . . . . 114 Thr C . 17831 1 1148 . 1 1 116 116 THR CA C 13 61.672 0.2 . 1 . . . . 114 Thr CA . 17831 1 1149 . 1 1 116 116 THR CB C 13 71.116 0.2 . 1 . . . . 114 Thr CB . 17831 1 1150 . 1 1 116 116 THR CG2 C 13 21.493 0.2 . 1 . . . . 114 Thr CG2 . 17831 1 1151 . 1 1 116 116 THR N N 15 117.242 0.2 . 1 . . . . 114 Thr N . 17831 1 1152 . 1 1 117 117 LYS H H 1 9.359 0.02 . 1 . . . . 115 Lys H . 17831 1 1153 . 1 1 117 117 LYS HA H 1 4.689 0.02 . 1 . . . . 115 Lys HA . 17831 1 1154 . 1 1 117 117 LYS HB2 H 1 1.567 0.02 . 2 . . . . 115 Lys HB2 . 17831 1 1155 . 1 1 117 117 LYS HB3 H 1 1.282 0.02 . 2 . . . . 115 Lys HB3 . 17831 1 1156 . 1 1 117 117 LYS HG2 H 1 1.019 0.02 . 2 . . . . 115 Lys HG2 . 17831 1 1157 . 1 1 117 117 LYS HG3 H 1 1.160 0.02 . 2 . . . . 115 Lys HG3 . 17831 1 1158 . 1 1 117 117 LYS HD2 H 1 1.805 0.02 . 2 . . . . 115 Lys HD2 . 17831 1 1159 . 1 1 117 117 LYS HD3 H 1 1.635 0.02 . 2 . . . . 115 Lys HD3 . 17831 1 1160 . 1 1 117 117 LYS HE2 H 1 3.062 0.02 . 2 . . . . 115 Lys HE2 . 17831 1 1161 . 1 1 117 117 LYS HE3 H 1 3.137 0.02 . 2 . . . . 115 Lys HE3 . 17831 1 1162 . 1 1 117 117 LYS C C 13 175.169 0.2 . 1 . . . . 115 Lys C . 17831 1 1163 . 1 1 117 117 LYS CA C 13 52.730 0.2 . 1 . . . . 115 Lys CA . 17831 1 1164 . 1 1 117 117 LYS CB C 13 35.474 0.2 . 1 . . . . 115 Lys CB . 17831 1 1165 . 1 1 117 117 LYS CG C 13 24.510 0.2 . 1 . . . . 115 Lys CG . 17831 1 1166 . 1 1 117 117 LYS CD C 13 28.705 0.2 . 1 . . . . 115 Lys CD . 17831 1 1167 . 1 1 117 117 LYS CE C 13 42.750 0.2 . 1 . . . . 115 Lys CE . 17831 1 1168 . 1 1 117 117 LYS N N 15 126.772 0.2 . 1 . . . . 115 Lys N . 17831 1 1169 . 1 1 118 118 THR H H 1 8.688 0.02 . 1 . . . . 116 Thr H . 17831 1 1170 . 1 1 118 118 THR HA H 1 4.735 0.02 . 1 . . . . 116 Thr HA . 17831 1 1171 . 1 1 118 118 THR HB H 1 3.884 0.02 . 1 . . . . 116 Thr HB . 17831 1 1172 . 1 1 118 118 THR C C 13 173.733 0.2 . 1 . . . . 116 Thr C . 17831 1 1173 . 1 1 118 118 THR CA C 13 62.410 0.2 . 1 . . . . 116 Thr CA . 17831 1 1174 . 1 1 118 118 THR CB C 13 69.569 0.2 . 1 . . . . 116 Thr CB . 17831 1 1175 . 1 1 118 118 THR N N 15 118.791 0.2 . 1 . . . . 116 Thr N . 17831 1 1176 . 1 1 119 119 VAL H H 1 9.261 0.02 . 1 . . . . 117 Val H . 17831 1 1177 . 1 1 119 119 VAL HA H 1 3.967 0.02 . 1 . . . . 117 Val HA . 17831 1 1178 . 1 1 119 119 VAL HB H 1 1.755 0.02 . 1 . . . . 117 Val HB . 17831 1 1179 . 1 1 119 119 VAL HG11 H 1 0.551 0.02 . 2 . . . . 117 Val HG1 . 17831 1 1180 . 1 1 119 119 VAL HG12 H 1 0.551 0.02 . 2 . . . . 117 Val HG1 . 17831 1 1181 . 1 1 119 119 VAL HG13 H 1 0.551 0.02 . 2 . . . . 117 Val HG1 . 17831 1 1182 . 1 1 119 119 VAL HG21 H 1 -0.140 0.02 . 2 . . . . 117 Val HG2 . 17831 1 1183 . 1 1 119 119 VAL HG22 H 1 -0.140 0.02 . 2 . . . . 117 Val HG2 . 17831 1 1184 . 1 1 119 119 VAL HG23 H 1 -0.140 0.02 . 2 . . . . 117 Val HG2 . 17831 1 1185 . 1 1 119 119 VAL C C 13 172.958 0.2 . 1 . . . . 117 Val C . 17831 1 1186 . 1 1 119 119 VAL CA C 13 58.525 0.2 . 1 . . . . 117 Val CA . 17831 1 1187 . 1 1 119 119 VAL CB C 13 33.351 0.2 . 1 . . . . 117 Val CB . 17831 1 1188 . 1 1 119 119 VAL CG1 C 13 20.349 0.2 . 2 . . . . 117 Val CG1 . 17831 1 1189 . 1 1 119 119 VAL CG2 C 13 19.599 0.2 . 2 . . . . 117 Val CG2 . 17831 1 1190 . 1 1 119 119 VAL N N 15 129.408 0.2 . 1 . . . . 117 Val N . 17831 1 1191 . 1 1 120 120 PRO HA H 1 4.511 0.02 . 1 . . . . 118 Pro HA . 17831 1 1192 . 1 1 120 120 PRO HB2 H 1 2.178 0.02 . 2 . . . . 118 Pro HB2 . 17831 1 1193 . 1 1 120 120 PRO HB3 H 1 1.955 0.02 . 2 . . . . 118 Pro HB3 . 17831 1 1194 . 1 1 120 120 PRO C C 13 175.549 0.2 . 1 . . . . 118 Pro C . 17831 1 1195 . 1 1 120 120 PRO CA C 13 62.384 0.2 . 1 . . . . 118 Pro CA . 17831 1 1196 . 1 1 120 120 PRO CB C 13 31.635 0.2 . 1 . . . . 118 Pro CB . 17831 1 1197 . 1 1 121 121 LEU H H 1 7.774 0.02 . 1 . . . . 119 Leu H . 17831 1 1198 . 1 1 121 121 LEU HA H 1 4.577 0.02 . 1 . . . . 119 Leu HA . 17831 1 1199 . 1 1 121 121 LEU HB2 H 1 1.078 0.02 . 2 . . . . 119 Leu HB2 . 17831 1 1200 . 1 1 121 121 LEU HB3 H 1 1.390 0.02 . 2 . . . . 119 Leu HB3 . 17831 1 1201 . 1 1 121 121 LEU HG H 1 1.387 0.02 . 1 . . . . 119 Leu HG . 17831 1 1202 . 1 1 121 121 LEU HD11 H 1 0.498 0.02 . 2 . . . . 119 Leu HD1 . 17831 1 1203 . 1 1 121 121 LEU HD12 H 1 0.498 0.02 . 2 . . . . 119 Leu HD1 . 17831 1 1204 . 1 1 121 121 LEU HD13 H 1 0.498 0.02 . 2 . . . . 119 Leu HD1 . 17831 1 1205 . 1 1 121 121 LEU HD21 H 1 0.527 0.02 . 2 . . . . 119 Leu HD2 . 17831 1 1206 . 1 1 121 121 LEU HD22 H 1 0.527 0.02 . 2 . . . . 119 Leu HD2 . 17831 1 1207 . 1 1 121 121 LEU HD23 H 1 0.527 0.02 . 2 . . . . 119 Leu HD2 . 17831 1 1208 . 1 1 121 121 LEU C C 13 177.282 0.2 . 1 . . . . 119 Leu C . 17831 1 1209 . 1 1 121 121 LEU CA C 13 52.616 0.2 . 1 . . . . 119 Leu CA . 17831 1 1210 . 1 1 121 121 LEU CB C 13 43.395 0.2 . 1 . . . . 119 Leu CB . 17831 1 1211 . 1 1 121 121 LEU CG C 13 26.358 0.2 . 1 . . . . 119 Leu CG . 17831 1 1212 . 1 1 121 121 LEU CD1 C 13 25.471 0.2 . 2 . . . . 119 Leu CD1 . 17831 1 1213 . 1 1 121 121 LEU CD2 C 13 23.340 0.2 . 2 . . . . 119 Leu CD2 . 17831 1 1214 . 1 1 121 121 LEU N N 15 120.917 0.2 . 1 . . . . 119 Leu N . 17831 1 1215 . 1 1 122 122 SER H H 1 9.297 0.02 . 1 . . . . 120 Ser H . 17831 1 1216 . 1 1 122 122 SER HA H 1 4.371 0.02 . 1 . . . . 120 Ser HA . 17831 1 1217 . 1 1 122 122 SER HB2 H 1 3.811 0.02 . 2 . . . . 120 Ser HB2 . 17831 1 1218 . 1 1 122 122 SER HB3 H 1 3.657 0.02 . 2 . . . . 120 Ser HB3 . 17831 1 1219 . 1 1 122 122 SER C C 13 173.145 0.2 . 1 . . . . 120 Ser C . 17831 1 1220 . 1 1 122 122 SER CA C 13 58.127 0.2 . 1 . . . . 120 Ser CA . 17831 1 1221 . 1 1 122 122 SER CB C 13 63.893 0.2 . 1 . . . . 120 Ser CB . 17831 1 1222 . 1 1 122 122 SER N N 15 119.439 0.2 . 1 . . . . 120 Ser N . 17831 1 1223 . 1 1 123 123 GLU H H 1 8.205 0.02 . 1 . . . . 121 Glu H . 17831 1 1224 . 1 1 123 123 GLU HA H 1 3.641 0.02 . 1 . . . . 121 Glu HA . 17831 1 1225 . 1 1 123 123 GLU HB2 H 1 1.819 0.02 . 2 . . . . 121 Glu HB2 . 17831 1 1226 . 1 1 123 123 GLU HB3 H 1 1.888 0.02 . 2 . . . . 121 Glu HB3 . 17831 1 1227 . 1 1 123 123 GLU HG2 H 1 2.399 0.02 . 2 . . . . 121 Glu HG2 . 17831 1 1228 . 1 1 123 123 GLU HG3 H 1 2.017 0.02 . 2 . . . . 121 Glu HG3 . 17831 1 1229 . 1 1 123 123 GLU C C 13 176.309 0.2 . 1 . . . . 121 Glu C . 17831 1 1230 . 1 1 123 123 GLU CA C 13 57.660 0.2 . 1 . . . . 121 Glu CA . 17831 1 1231 . 1 1 123 123 GLU CB C 13 30.817 0.2 . 1 . . . . 121 Glu CB . 17831 1 1232 . 1 1 123 123 GLU CG C 13 36.299 0.2 . 1 . . . . 121 Glu CG . 17831 1 1233 . 1 1 123 123 GLU N N 15 121.007 0.2 . 1 . . . . 121 Glu N . 17831 1 1234 . 1 1 124 124 VAL H H 1 8.775 0.02 . 1 . . . . 122 Val H . 17831 1 1235 . 1 1 124 124 VAL HA H 1 4.155 0.02 . 1 . . . . 122 Val HA . 17831 1 1236 . 1 1 124 124 VAL HB H 1 1.542 0.02 . 1 . . . . 122 Val HB . 17831 1 1237 . 1 1 124 124 VAL HG11 H 1 0.343 0.02 . 2 . . . . 122 Val HG1 . 17831 1 1238 . 1 1 124 124 VAL HG12 H 1 0.343 0.02 . 2 . . . . 122 Val HG1 . 17831 1 1239 . 1 1 124 124 VAL HG13 H 1 0.343 0.02 . 2 . . . . 122 Val HG1 . 17831 1 1240 . 1 1 124 124 VAL HG21 H 1 0.545 0.02 . 2 . . . . 122 Val HG2 . 17831 1 1241 . 1 1 124 124 VAL HG22 H 1 0.545 0.02 . 2 . . . . 122 Val HG2 . 17831 1 1242 . 1 1 124 124 VAL HG23 H 1 0.545 0.02 . 2 . . . . 122 Val HG2 . 17831 1 1243 . 1 1 124 124 VAL C C 13 175.241 0.2 . 1 . . . . 122 Val C . 17831 1 1244 . 1 1 124 124 VAL CA C 13 61.361 0.2 . 1 . . . . 122 Val CA . 17831 1 1245 . 1 1 124 124 VAL CB C 13 35.351 0.2 . 1 . . . . 122 Val CB . 17831 1 1246 . 1 1 124 124 VAL CG1 C 13 21.004 0.2 . 2 . . . . 122 Val CG1 . 17831 1 1247 . 1 1 124 124 VAL CG2 C 13 21.001 0.2 . 2 . . . . 122 Val CG2 . 17831 1 1248 . 1 1 124 124 VAL N N 15 124.504 0.2 . 1 . . . . 122 Val N . 17831 1 1249 . 1 1 125 125 VAL H H 1 8.641 0.02 . 1 . . . . 123 Val H . 17831 1 1250 . 1 1 125 125 VAL HA H 1 4.187 0.02 . 1 . . . . 123 Val HA . 17831 1 1251 . 1 1 125 125 VAL HB H 1 2.035 0.02 . 1 . . . . 123 Val HB . 17831 1 1252 . 1 1 125 125 VAL HG11 H 1 0.966 0.02 . 2 . . . . 123 Val HG1 . 17831 1 1253 . 1 1 125 125 VAL HG12 H 1 0.966 0.02 . 2 . . . . 123 Val HG1 . 17831 1 1254 . 1 1 125 125 VAL HG13 H 1 0.966 0.02 . 2 . . . . 123 Val HG1 . 17831 1 1255 . 1 1 125 125 VAL HG21 H 1 0.920 0.02 . 2 . . . . 123 Val HG2 . 17831 1 1256 . 1 1 125 125 VAL HG22 H 1 0.920 0.02 . 2 . . . . 123 Val HG2 . 17831 1 1257 . 1 1 125 125 VAL HG23 H 1 0.920 0.02 . 2 . . . . 123 Val HG2 . 17831 1 1258 . 1 1 125 125 VAL C C 13 175.604 0.2 . 1 . . . . 123 Val C . 17831 1 1259 . 1 1 125 125 VAL CA C 13 62.045 0.2 . 1 . . . . 123 Val CA . 17831 1 1260 . 1 1 125 125 VAL CB C 13 32.654 0.2 . 1 . . . . 123 Val CB . 17831 1 1261 . 1 1 125 125 VAL CG1 C 13 21.358 0.2 . 2 . . . . 123 Val CG1 . 17831 1 1262 . 1 1 125 125 VAL CG2 C 13 20.684 0.2 . 2 . . . . 123 Val CG2 . 17831 1 1263 . 1 1 125 125 VAL N N 15 127.676 0.2 . 1 . . . . 123 Val N . 17831 1 1264 . 1 1 126 126 ALA H H 1 8.600 0.02 . 1 . . . . 124 Ala H . 17831 1 1265 . 1 1 126 126 ALA HA H 1 4.537 0.02 . 1 . . . . 124 Ala HA . 17831 1 1266 . 1 1 126 126 ALA HB1 H 1 1.377 0.02 . 1 . . . . 124 Ala HB . 17831 1 1267 . 1 1 126 126 ALA HB2 H 1 1.377 0.02 . 1 . . . . 124 Ala HB . 17831 1 1268 . 1 1 126 126 ALA HB3 H 1 1.377 0.02 . 1 . . . . 124 Ala HB . 17831 1 1269 . 1 1 126 126 ALA C C 13 177.806 0.2 . 1 . . . . 124 Ala C . 17831 1 1270 . 1 1 126 126 ALA CA C 13 52.379 0.2 . 1 . . . . 124 Ala CA . 17831 1 1271 . 1 1 126 126 ALA CB C 13 19.475 0.2 . 1 . . . . 124 Ala CB . 17831 1 1272 . 1 1 126 126 ALA N N 15 127.666 0.2 . 1 . . . . 124 Ala N . 17831 1 1273 . 1 1 127 127 ASN H H 1 8.622 0.02 . 1 . . . . 125 Asn H . 17831 1 1274 . 1 1 127 127 ASN HA H 1 4.684 0.02 . 1 . . . . 125 Asn HA . 17831 1 1275 . 1 1 127 127 ASN HB2 H 1 2.747 0.02 . 1 . . . . 125 Asn HB2 . 17831 1 1276 . 1 1 127 127 ASN HB3 H 1 2.747 0.02 . 1 . . . . 125 Asn HB3 . 17831 1 1277 . 1 1 127 127 ASN C C 13 175.078 0.2 . 1 . . . . 125 Asn C . 17831 1 1278 . 1 1 127 127 ASN CA C 13 53.018 0.2 . 1 . . . . 125 Asn CA . 17831 1 1279 . 1 1 127 127 ASN CB C 13 38.880 0.2 . 1 . . . . 125 Asn CB . 17831 1 1280 . 1 1 127 127 ASN N N 15 119.392 0.2 . 1 . . . . 125 Asn N . 17831 1 1281 . 1 1 128 128 ASN H H 1 8.413 0.02 . 1 . . . . 126 Asn H . 17831 1 1282 . 1 1 128 128 ASN HA H 1 4.666 0.02 . 1 . . . . 126 Asn HA . 17831 1 1283 . 1 1 128 128 ASN HB2 H 1 2.757 0.02 . 1 . . . . 126 Asn HB2 . 17831 1 1284 . 1 1 128 128 ASN HB3 H 1 2.757 0.02 . 1 . . . . 126 Asn HB3 . 17831 1 1285 . 1 1 128 128 ASN C C 13 174.688 0.2 . 1 . . . . 126 Asn C . 17831 1 1286 . 1 1 128 128 ASN CA C 13 53.122 0.2 . 1 . . . . 126 Asn CA . 17831 1 1287 . 1 1 128 128 ASN CB C 13 38.880 0.2 . 1 . . . . 126 Asn CB . 17831 1 1288 . 1 1 128 128 ASN N N 15 119.516 0.2 . 1 . . . . 126 Asn N . 17831 1 1289 . 1 1 129 129 ALA H H 1 8.121 0.02 . 1 . . . . 127 Ala H . 17831 1 1290 . 1 1 129 129 ALA HA H 1 4.271 0.02 . 1 . . . . 127 Ala HA . 17831 1 1291 . 1 1 129 129 ALA HB1 H 1 1.318 0.02 . 1 . . . . 127 Ala HB . 17831 1 1292 . 1 1 129 129 ALA HB2 H 1 1.318 0.02 . 1 . . . . 127 Ala HB . 17831 1 1293 . 1 1 129 129 ALA HB3 H 1 1.318 0.02 . 1 . . . . 127 Ala HB . 17831 1 1294 . 1 1 129 129 ALA C C 13 176.900 0.2 . 1 . . . . 127 Ala C . 17831 1 1295 . 1 1 129 129 ALA CA C 13 52.211 0.2 . 1 . . . . 127 Ala CA . 17831 1 1296 . 1 1 129 129 ALA CB C 13 19.378 0.2 . 1 . . . . 127 Ala CB . 17831 1 1297 . 1 1 129 129 ALA N N 15 124.059 0.2 . 1 . . . . 127 Ala N . 17831 1 1298 . 1 1 130 130 ALA H H 1 8.157 0.02 . 1 . . . . 128 Ala H . 17831 1 1299 . 1 1 130 130 ALA HA H 1 4.557 0.02 . 1 . . . . 128 Ala HA . 17831 1 1300 . 1 1 130 130 ALA HB1 H 1 1.330 0.02 . 1 . . . . 128 Ala HB . 17831 1 1301 . 1 1 130 130 ALA HB2 H 1 1.330 0.02 . 1 . . . . 128 Ala HB . 17831 1 1302 . 1 1 130 130 ALA HB3 H 1 1.330 0.02 . 1 . . . . 128 Ala HB . 17831 1 1303 . 1 1 130 130 ALA CA C 13 50.231 0.2 . 1 . . . . 128 Ala CA . 17831 1 1304 . 1 1 130 130 ALA CB C 13 18.358 0.2 . 1 . . . . 128 Ala CB . 17831 1 1305 . 1 1 130 130 ALA N N 15 124.742 0.2 . 1 . . . . 128 Ala N . 17831 1 1306 . 1 1 131 131 PRO HA H 1 4.407 0.02 . 1 . . . . 129 Pro HA . 17831 1 1307 . 1 1 131 131 PRO HB2 H 1 2.259 0.02 . 2 . . . . 129 Pro HB2 . 17831 1 1308 . 1 1 131 131 PRO HB3 H 1 1.854 0.02 . 2 . . . . 129 Pro HB3 . 17831 1 1309 . 1 1 131 131 PRO C C 13 176.739 0.2 . 1 . . . . 129 Pro C . 17831 1 1310 . 1 1 131 131 PRO CA C 13 63.045 0.2 . 1 . . . . 129 Pro CA . 17831 1 1311 . 1 1 132 132 GLN H H 1 8.418 0.02 . 1 . . . . 130 Gln H . 17831 1 1312 . 1 1 132 132 GLN HA H 1 4.580 0.02 . 1 . . . . 130 Gln HA . 17831 1 1313 . 1 1 132 132 GLN HB2 H 1 2.065 0.02 . 2 . . . . 130 Gln HB2 . 17831 1 1314 . 1 1 132 132 GLN HB3 H 1 1.896 0.02 . 2 . . . . 130 Gln HB3 . 17831 1 1315 . 1 1 132 132 GLN HG2 H 1 2.410 0.02 . 1 . . . . 130 Gln HG2 . 17831 1 1316 . 1 1 132 132 GLN HG3 H 1 2.410 0.02 . 1 . . . . 130 Gln HG3 . 17831 1 1317 . 1 1 132 132 GLN CA C 13 53.478 0.2 . 1 . . . . 130 Gln CA . 17831 1 1318 . 1 1 132 132 GLN CB C 13 29.120 0.2 . 1 . . . . 130 Gln CB . 17831 1 1319 . 1 1 132 132 GLN CG C 13 33.527 0.2 . 1 . . . . 130 Gln CG . 17831 1 1320 . 1 1 132 132 GLN N N 15 121.710 0.2 . 1 . . . . 130 Gln N . 17831 1 1321 . 1 1 133 133 PRO HA H 1 4.448 0.02 . 1 . . . . 131 Pro HA . 17831 1 1322 . 1 1 133 133 PRO HB2 H 1 1.908 0.02 . 2 . . . . 131 Pro HB2 . 17831 1 1323 . 1 1 133 133 PRO HB3 H 1 2.265 0.02 . 2 . . . . 131 Pro HB3 . 17831 1 1324 . 1 1 133 133 PRO C C 13 176.837 0.2 . 1 . . . . 131 Pro C . 17831 1 1325 . 1 1 133 133 PRO CA C 13 62.857 0.2 . 1 . . . . 131 Pro CA . 17831 1 1326 . 1 1 134 134 VAL H H 1 8.233 0.02 . 1 . . . . 132 Val H . 17831 1 1327 . 1 1 134 134 VAL HA H 1 4.127 0.02 . 1 . . . . 132 Val HA . 17831 1 1328 . 1 1 134 134 VAL HB H 1 2.062 0.02 . 1 . . . . 132 Val HB . 17831 1 1329 . 1 1 134 134 VAL HG11 H 1 0.946 0.02 . 1 . . . . 132 Val HG1 . 17831 1 1330 . 1 1 134 134 VAL HG12 H 1 0.946 0.02 . 1 . . . . 132 Val HG1 . 17831 1 1331 . 1 1 134 134 VAL HG13 H 1 0.946 0.02 . 1 . . . . 132 Val HG1 . 17831 1 1332 . 1 1 134 134 VAL HG21 H 1 0.946 0.02 . 1 . . . . 132 Val HG2 . 17831 1 1333 . 1 1 134 134 VAL HG22 H 1 0.946 0.02 . 1 . . . . 132 Val HG2 . 17831 1 1334 . 1 1 134 134 VAL HG23 H 1 0.946 0.02 . 1 . . . . 132 Val HG2 . 17831 1 1335 . 1 1 134 134 VAL C C 13 176.734 0.2 . 1 . . . . 132 Val C . 17831 1 1336 . 1 1 134 134 VAL CA C 13 62.699 0.2 . 1 . . . . 132 Val CA . 17831 1 1337 . 1 1 134 134 VAL CB C 13 32.808 0.2 . 1 . . . . 132 Val CB . 17831 1 1338 . 1 1 134 134 VAL CG1 C 13 20.500 0.2 . 1 . . . . 132 Val CG1 . 17831 1 1339 . 1 1 134 134 VAL CG2 C 13 20.500 0.2 . 1 . . . . 132 Val CG2 . 17831 1 1340 . 1 1 134 134 VAL N N 15 120.803 0.2 . 1 . . . . 132 Val N . 17831 1 stop_ save_