data_7366 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Putative periplasmic protein: Northest Structural Genomics Target StR106 ; _BMRB_accession_number 7366 _BMRB_flat_file_name bmr7366.str _Entry_type original _Submission_date 2007-01-19 _Accession_date 2007-01-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Q. . . 2 Liu G. . . 3 Wang H. . . 4 Nwosu C. . . 5 Cunningham K. . . 6 Ma L. C. . 7 Xiao R. . . 8 Liu J. . . 9 Baran M. C. . 10 Swapna G. V.T. . 11 Thomas B. A. . 12 Rost B. . . 13 Montelione G. T. . 14 Szypersk T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 452 "13C chemical shifts" 261 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-10-09 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of Putative periplasmic protein: Northest Structural Genomics Target StR106' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Q. . . 2 Liu G. . . 3 Wang H. . . 4 Nwosu C. . . 5 Cunningham K. . . 6 Ma L. C. . 7 Xiao R. . . 8 Liu J. . . 9 Baran M. C. . 10 Swapna G. V.T. . 11 Thomas B. A. . 12 Montelione G. T. . 13 Szypersk T. . . stop_ _Journal_abbreviation 'To be Published' _Journal_volume . _Journal_issue . _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Periplasmic protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Periplasmic protein' $Putative_periplasmic_protein stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Putative_periplasmic_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Putative_periplasmic_protein _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; MKTGYKVMLGALAFVVTNVY AAEIMKKTDFDKVASEYTKI GTISTTGEMSPLDAREDLIK KADEKGADVVVLTSGQTENK IHGTADIYKKKLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 THR 4 GLY 5 TYR 6 LYS 7 VAL 8 MET 9 LEU 10 GLY 11 ALA 12 LEU 13 ALA 14 PHE 15 VAL 16 VAL 17 THR 18 ASN 19 VAL 20 TYR 21 ALA 22 ALA 23 GLU 24 ILE 25 MET 26 LYS 27 LYS 28 THR 29 ASP 30 PHE 31 ASP 32 LYS 33 VAL 34 ALA 35 SER 36 GLU 37 TYR 38 THR 39 LYS 40 ILE 41 GLY 42 THR 43 ILE 44 SER 45 THR 46 THR 47 GLY 48 GLU 49 MET 50 SER 51 PRO 52 LEU 53 ASP 54 ALA 55 ARG 56 GLU 57 ASP 58 LEU 59 ILE 60 LYS 61 LYS 62 ALA 63 ASP 64 GLU 65 LYS 66 GLY 67 ALA 68 ASP 69 VAL 70 VAL 71 VAL 72 LEU 73 THR 74 SER 75 GLY 76 GLN 77 THR 78 GLU 79 ASN 80 LYS 81 ILE 82 HIS 83 GLY 84 THR 85 ALA 86 ASP 87 ILE 88 TYR 89 LYS 90 LYS 91 LYS 92 LEU 93 GLU 94 HIS 95 HIS 96 HIS 97 HIS 98 HIS 99 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19327 StR106 78.79 78 100.00 100.00 4.39e-47 PDB 2MA4 "Solution Nmr Structure Of Yaho Protein From Salmonella Typhimurium, Northeast Structural Genomics Consortium (nesg) Target Str1" 78.79 78 100.00 100.00 4.39e-47 PDB 2NOC "Solution Structure Of Putative Periplasmic Protein: Northest Structural Genomics Target Str106" 100.00 99 100.00 100.00 2.47e-63 DBJ BAJ35371 "hypothetical protein STMDT12_C04280 [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 91.92 91 100.00 100.00 1.31e-56 DBJ BAP06126 "probable secreted protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 91.92 91 100.00 100.00 1.31e-56 EMBL CAC12674 "yahO [Salmonella typhimurium]" 67.68 67 100.00 100.00 1.04e-38 EMBL CAD08821 "probable secreted protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 91.92 91 100.00 100.00 1.31e-56 EMBL CAR31935 "probable secreted protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 91.92 91 100.00 100.00 1.31e-56 EMBL CAR36277 "probable secreted protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 91.92 91 100.00 100.00 1.31e-56 EMBL CAR60410 "probable secreted protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" 91.92 91 100.00 100.00 1.31e-56 GB AAL19320 "putative periplasmic protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 91.92 91 100.00 100.00 1.31e-56 GB AAO70086 "probable secreted protein [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 91.92 91 100.00 100.00 1.31e-56 GB AAV78241 "probable secreted protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]" 91.92 91 100.00 100.00 1.31e-56 GB AAX64313 "putative periplasmic protein [Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67]" 91.92 91 100.00 100.00 1.31e-56 GB ABX68592 "hypothetical protein SPAB_03231 [Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]" 91.92 91 100.00 100.00 1.31e-56 PIR AE0547 "probable secreted protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 91.92 91 100.00 100.00 1.31e-56 REF NP_454961 "hypothetical protein STY0398 [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 91.92 91 100.00 100.00 1.31e-56 REF NP_459361 "periplasmic protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 91.92 91 100.00 100.00 1.31e-56 REF NP_806226 "hypothetical protein t2498 [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 91.92 91 100.00 100.00 1.31e-56 REF WP_000848022 "hypothetical protein [Salmonella enterica]" 91.92 91 97.80 100.00 5.68e-56 REF WP_000848024 "hypothetical protein [Salmonella enterica]" 91.92 91 97.80 98.90 1.60e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $Putative_periplasmic_protein 'Salmonella choleraesuis' 591 . Bacteria Salmonella Salmonella choleraesuis yahO stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Putative_periplasmic_protein 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details '1.1 mM protein, 10mM Tris, 100mM NaCl, 0.02% NaN3, 90% H2O, 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Putative_periplasmic_protein 1.1 mM . Tris 10 mM . NaCl 100 mM . NaN3 0.02 % . D2O 10 % . H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Guntert, P. et al.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Delaglio, F. et al.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, P. et al.' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunger, A.T. et al.' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_Xeasy _Saveframe_category software _Name Xeasy _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bartels, C., Xia, T.H.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Autostructure _Saveframe_category software _Name Autostructure _Version 2.0.0 loop_ _Vendor _Address _Electronic_address 'Huang, Y.J.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_UBNMR _Saveframe_category software _Name UBNMR _Version 1.0 loop_ _Vendor _Address _Electronic_address 'Shen, Y.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_GFT_(4,3)D_HNNCABCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HNNCABCA' _Sample_label $sample save_ save_GFT_(4,3)D_CABCA(CO)NHN_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D CABCA(CO)NHN' _Sample_label $sample save_ save_GFT_(4,3)D_HABCAB(CO)NHN_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HABCAB(CO)NHN' _Sample_label $sample save_ save_GFT_(4,3)D_HCCH_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HCCH' _Sample_label $sample save_ save_SIMULTANEOUS_HETERONUCLEAR_RESOLVED_[1H,1H]-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 'GFT (4,3)D HNNCABCA' 'GFT (4,3)D CABCA(CO)NHN' 'GFT (4,3)D HABCAB(CO)NHN' 'GFT (4,3)D HCCH' 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Periplasmic protein' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 22 22 ALA HA H 4.13 . 1 2 22 22 ALA HB H 1.18 . 1 3 22 22 ALA CA C 50.9 . 1 4 22 22 ALA CB C 20.2 . 1 5 23 23 GLU H H 7.92 . 1 6 23 23 GLU HA H 4.71 . 1 7 23 23 GLU HB2 H 1.98 . 2 8 23 23 GLU HB3 H 2.05 . 2 9 23 23 GLU HG2 H 2.26 . 2 10 23 23 GLU HG3 H 2.26 . 2 11 23 23 GLU CA C 54.3 . 1 12 23 23 GLU CB C 32.5 . 1 13 23 23 GLU CG C 35.0 . 1 14 23 23 GLU N N 117.6 . 1 15 24 24 ILE H H 8.87 . 1 16 24 24 ILE HA H 4.87 . 1 17 24 24 ILE HB H 1.68 . 1 18 24 24 ILE HD1 H 0.78 . 1 19 24 24 ILE HG12 H 1.52 . 2 20 24 24 ILE HG13 H 0.77 . 2 21 24 24 ILE HG2 H 0.85 . 1 22 24 24 ILE CA C 60.2 . 1 23 24 24 ILE CB C 38.1 . 1 24 24 24 ILE CD1 C 17.3 . 1 25 24 24 ILE CG1 C 28.0 . 1 26 24 24 ILE CG2 C 13.2 . 1 27 24 24 ILE N N 123.8 . 1 28 25 25 MET H H 8.72 . 1 29 25 25 MET HA H 4.76 . 1 30 25 25 MET HB2 H 1.91 . 2 31 25 25 MET HB3 H 1.56 . 2 32 25 25 MET HG2 H 2.62 . 2 33 25 25 MET HG3 H 2.43 . 2 34 25 25 MET CA C 54.3 . 1 35 25 25 MET CB C 37.1 . 1 36 25 25 MET CG C 32.5 . 1 37 25 25 MET N N 127.1 . 1 38 26 26 LYS H H 9.19 . 1 39 26 26 LYS HA H 4.32 . 1 40 26 26 LYS HB2 H 2.02 . 2 41 26 26 LYS HB3 H 1.82 . 2 42 26 26 LYS HD2 H 1.75 . 2 43 26 26 LYS HD3 H 1.75 . 2 44 26 26 LYS HE2 H 3.01 . 2 45 26 26 LYS HE3 H 3.01 . 2 46 26 26 LYS HG2 H 1.59 . 2 47 26 26 LYS HG3 H 1.64 . 2 48 26 26 LYS CA C 56.6 . 1 49 26 26 LYS CB C 32.9 . 1 50 26 26 LYS CD C 29.3 . 1 51 26 26 LYS CE C 41.9 . 1 52 26 26 LYS CG C 25.3 . 1 53 26 26 LYS N N 123.5 . 1 54 27 27 LYS H H 8.87 . 1 55 27 27 LYS HA H 3.86 . 1 56 27 27 LYS HB2 H 1.97 . 2 57 27 27 LYS HB3 H 1.97 . 2 58 27 27 LYS HD2 H 1.63 . 2 59 27 27 LYS HD3 H 1.63 . 2 60 27 27 LYS HE2 H 3.08 . 2 61 27 27 LYS HE3 H 3.08 . 2 62 27 27 LYS HG2 H 1.52 . 2 63 27 27 LYS HG3 H 1.48 . 2 64 27 27 LYS CA C 60.5 . 1 65 27 27 LYS CB C 32.4 . 1 66 27 27 LYS CD C 28.8 . 1 67 27 27 LYS CE C 42.0 . 1 68 27 27 LYS CG C 24.8 . 1 69 27 27 LYS N N 126.2 . 1 70 28 28 THR H H 8.11 . 1 71 28 28 THR HA H 4.13 . 1 72 28 28 THR HB H 4.17 . 1 73 28 28 THR HG2 H 1.30 . 1 74 28 28 THR CA C 64.6 . 1 75 28 28 THR CB C 68.0 . 1 76 28 28 THR CG2 C 22.1 . 1 77 28 28 THR N N 107.1 . 1 78 29 29 ASP H H 6.77 . 1 79 29 29 ASP HA H 4.58 . 1 80 29 29 ASP HB2 H 2.72 . 2 81 29 29 ASP HB3 H 2.72 . 2 82 29 29 ASP CA C 56.6 . 1 83 29 29 ASP CB C 40.6 . 1 84 29 29 ASP N N 119.5 . 1 85 30 30 PHE H H 8.63 . 1 86 30 30 PHE HA H 3.93 . 1 87 30 30 PHE HB2 H 2.66 . 2 88 30 30 PHE HB3 H 2.77 . 2 89 30 30 PHE HD1 H 6.73 . 3 90 30 30 PHE HD2 H 6.73 . 3 91 30 30 PHE HE1 H 6.73 . 3 92 30 30 PHE HE2 H 6.73 . 3 93 30 30 PHE HZ H 6.81 . 1 94 30 30 PHE CA C 60.8 . 1 95 30 30 PHE CB C 38.9 . 1 96 30 30 PHE CD1 C 130.1 . 1 97 30 30 PHE CE1 C 130.1 . 1 98 30 30 PHE CZ C 128.2 . 1 99 30 30 PHE N N 123.3 . 1 100 31 31 ASP H H 8.65 . 1 101 31 31 ASP HA H 4.15 . 1 102 31 31 ASP HB2 H 2.59 . 2 103 31 31 ASP HB3 H 2.59 . 2 104 31 31 ASP CA C 57.0 . 1 105 31 31 ASP CB C 39.8 . 1 106 31 31 ASP N N 117.0 . 1 107 32 32 LYS H H 6.93 . 1 108 32 32 LYS HA H 4.11 . 1 109 32 32 LYS HB2 H 1.91 . 2 110 32 32 LYS HB3 H 1.98 . 2 111 32 32 LYS HD2 H 1.75 . 2 112 32 32 LYS HD3 H 1.73 . 2 113 32 32 LYS HE2 H 3.03 . 2 114 32 32 LYS HE3 H 3.03 . 2 115 32 32 LYS HG2 H 1.51 . 2 116 32 32 LYS HG3 H 1.51 . 2 117 32 32 LYS CA C 58.3 . 1 118 32 32 LYS CB C 33.1 . 1 119 32 32 LYS CD C 29.3 . 1 120 32 32 LYS CE C 41.8 . 1 121 32 32 LYS CG C 25.2 . 1 122 32 32 LYS N N 114.8 . 1 123 33 33 VAL H H 7.40 . 1 124 33 33 VAL HA H 4.62 . 1 125 33 33 VAL HB H 2.64 . 1 126 33 33 VAL HG1 H 0.82 . 2 127 33 33 VAL HG2 H 0.68 . 2 128 33 33 VAL CA C 60.1 . 1 129 33 33 VAL CB C 32.3 . 1 130 33 33 VAL CG1 C 21.0 . 1 131 33 33 VAL CG2 C 19.0 . 1 132 33 33 VAL N N 109.1 . 1 133 34 34 ALA H H 6.71 . 1 134 34 34 ALA HA H 3.01 . 1 135 34 34 ALA HB H 1.04 . 1 136 34 34 ALA CA C 55.1 . 1 137 34 34 ALA CB C 19.2 . 1 138 34 34 ALA N N 124.3 . 1 139 35 35 SER H H 8.12 . 1 140 35 35 SER HA H 4.32 . 1 141 35 35 SER HB2 H 4.00 . 2 142 35 35 SER HB3 H 3.88 . 2 143 35 35 SER CA C 60.4 . 1 144 35 35 SER CB C 62.4 . 1 145 35 35 SER N N 110.4 . 1 146 36 36 GLU H H 8.30 . 1 147 36 36 GLU HA H 4.27 . 1 148 36 36 GLU HB2 H 1.97 . 2 149 36 36 GLU HB3 H 2.02 . 2 150 36 36 GLU HG2 H 2.27 . 2 151 36 36 GLU HG3 H 2.17 . 2 152 36 36 GLU CA C 55.7 . 1 153 36 36 GLU CB C 28.9 . 1 154 36 36 GLU CG C 35.1 . 1 155 36 36 GLU N N 119.2 . 1 156 37 37 TYR H H 7.92 . 1 157 37 37 TYR HA H 5.15 . 1 158 37 37 TYR HB2 H 2.88 . 2 159 37 37 TYR HB3 H 3.14 . 2 160 37 37 TYR HD1 H 6.90 . 3 161 37 37 TYR HD2 H 6.90 . 3 162 37 37 TYR HE1 H 6.62 . 3 163 37 37 TYR HE2 H 6.62 . 3 164 37 37 TYR CA C 57.9 . 1 165 37 37 TYR CB C 44.1 . 1 166 37 37 TYR CD1 C 132.3 . 1 167 37 37 TYR CE1 C 117.7 . 1 168 37 37 TYR N N 117.2 . 1 169 38 38 THR H H 9.48 . 1 170 38 38 THR HA H 4.84 . 1 171 38 38 THR HB H 3.96 . 1 172 38 38 THR HG2 H 1.26 . 1 173 38 38 THR CA C 60.4 . 1 174 38 38 THR CB C 71.2 . 1 175 38 38 THR CG2 C 21.0 . 1 176 38 38 THR N N 115.4 . 1 177 39 39 LYS H H 9.29 . 1 178 39 39 LYS HA H 3.88 . 1 179 39 39 LYS HB2 H 1.69 . 2 180 39 39 LYS HB3 H 1.84 . 2 181 39 39 LYS HD2 H 1.50 . 2 182 39 39 LYS HD3 H 1.50 . 2 183 39 39 LYS HE2 H 2.69 . 2 184 39 39 LYS HE3 H 2.69 . 2 185 39 39 LYS HG2 H 1.06 . 2 186 39 39 LYS HG3 H 0.79 . 2 187 39 39 LYS CA C 57.5 . 1 188 39 39 LYS CB C 32.3 . 1 189 39 39 LYS CD C 29.5 . 1 190 39 39 LYS CE C 41.8 . 1 191 39 39 LYS CG C 25.4 . 1 192 39 39 LYS N N 130.4 . 1 193 40 40 ILE H H 8.82 . 1 194 40 40 ILE HA H 4.55 . 1 195 40 40 ILE HB H 1.95 . 1 196 40 40 ILE HD1 H 0.75 . 1 197 40 40 ILE HG12 H 0.77 . 2 198 40 40 ILE HG13 H 1.14 . 2 199 40 40 ILE HG2 H 0.92 . 1 200 40 40 ILE CA C 60.9 . 1 201 40 40 ILE CB C 39.2 . 1 202 40 40 ILE CD1 C 14.5 . 1 203 40 40 ILE CG1 C 26.6 . 1 204 40 40 ILE CG2 C 17.8 . 1 205 40 40 ILE N N 121.9 . 1 206 41 41 GLY H H 7.13 . 1 207 41 41 GLY HA2 H 3.95 . 2 208 41 41 GLY HA3 H 4.26 . 2 209 41 41 GLY CA C 45.1 . 1 210 41 41 GLY N N 107.4 . 1 211 42 42 THR H H 8.21 . 1 212 42 42 THR HA H 5.23 . 1 213 42 42 THR HB H 3.90 . 1 214 42 42 THR HG2 H 1.21 . 1 215 42 42 THR CA C 60.9 . 1 216 42 42 THR CB C 72.3 . 1 217 42 42 THR CG2 C 21.0 . 1 218 42 42 THR N N 115.1 . 1 219 43 43 ILE H H 9.13 . 1 220 43 43 ILE HA H 4.79 . 1 221 43 43 ILE HB H 1.77 . 1 222 43 43 ILE HD1 H 0.70 . 1 223 43 43 ILE HG12 H 1.25 . 2 224 43 43 ILE HG13 H 0.85 . 2 225 43 43 ILE HG2 H 0.76 . 1 226 43 43 ILE CA C 59.4 . 1 227 43 43 ILE CB C 42.6 . 1 228 43 43 ILE CD1 C 16.4 . 1 229 43 43 ILE CG1 C 25.2 . 1 230 43 43 ILE CG2 C 18.0 . 1 231 43 43 ILE N N 118.0 . 1 232 44 44 SER H H 8.33 . 1 233 44 44 SER HA H 5.25 . 1 234 44 44 SER HB2 H 3.75 . 2 235 44 44 SER HB3 H 3.68 . 2 236 44 44 SER CA C 56.7 . 1 237 44 44 SER CB C 66.0 . 1 238 44 44 SER N N 113.3 . 1 239 45 45 THR H H 8.38 . 1 240 45 45 THR HA H 4.55 . 1 241 45 45 THR HB H 4.30 . 1 242 45 45 THR HG2 H 1.23 . 1 243 45 45 THR CA C 60.9 . 1 244 45 45 THR CB C 70.0 . 1 245 45 45 THR CG2 C 21.6 . 1 246 45 45 THR N N 113.3 . 1 247 46 46 THR H H 8.54 . 1 248 46 46 THR HA H 4.40 . 1 249 46 46 THR HB H 4.16 . 1 250 46 46 THR HG2 H 1.19 . 1 251 46 46 THR CA C 62.0 . 1 252 46 46 THR CB C 69.3 . 1 253 46 46 THR CG2 C 21.1 . 1 254 46 46 THR N N 117.7 . 1 255 47 47 GLY H H 8.32 . 1 256 47 47 GLY HA2 H 3.89 . 2 257 47 47 GLY HA3 H 3.98 . 2 258 47 47 GLY CA C 44.8 . 1 259 47 47 GLY N N 111.7 . 1 260 48 48 GLU H H 8.43 . 1 261 48 48 GLU HA H 4.39 . 1 262 48 48 GLU HB2 H 1.86 . 2 263 48 48 GLU HB3 H 1.86 . 2 264 48 48 GLU HG2 H 2.12 . 2 265 48 48 GLU HG3 H 2.18 . 2 266 48 48 GLU CA C 55.6 . 1 267 48 48 GLU CB C 29.4 . 1 268 48 48 GLU CG C 35.3 . 1 269 48 48 GLU N N 120.1 . 1 270 49 49 MET H H 8.39 . 1 271 49 49 MET HA H 4.70 . 1 272 49 49 MET HB2 H 2.26 . 2 273 49 49 MET HB3 H 1.91 . 2 274 49 49 MET HG2 H 2.52 . 2 275 49 49 MET HG3 H 2.52 . 2 276 49 49 MET CA C 55.0 . 1 277 49 49 MET CB C 35.9 . 1 278 49 49 MET CG C 32.0 . 1 279 49 49 MET N N 120.0 . 1 280 50 50 SER H H 9.02 . 1 281 50 50 SER HA H 4.78 . 1 282 50 50 SER HB2 H 4.26 . 2 283 50 50 SER HB3 H 4.05 . 2 284 50 50 SER CA C 57.7 . 1 285 50 50 SER CB C 62.6 . 1 286 50 50 SER N N 117.9 . 1 287 51 51 PRO HA H 4.24 . 1 288 51 51 PRO HB2 H 1.98 . 2 289 51 51 PRO HB3 H 2.40 . 2 290 51 51 PRO HD2 H 3.91 . 2 291 51 51 PRO HD3 H 3.87 . 2 292 51 51 PRO HG2 H 2.20 . 2 293 51 51 PRO HG3 H 2.01 . 2 294 51 51 PRO CA C 66.0 . 1 295 51 51 PRO CB C 31.8 . 1 296 51 51 PRO CD C 49.7 . 1 297 51 51 PRO CG C 28.0 . 1 298 52 52 LEU H H 8.16 . 1 299 52 52 LEU HA H 4.11 . 1 300 52 52 LEU HB2 H 1.67 . 2 301 52 52 LEU HB3 H 1.57 . 2 302 52 52 LEU HD1 H 0.94 . 2 303 52 52 LEU HD2 H 0.88 . 2 304 52 52 LEU HG H 1.66 . 1 305 52 52 LEU CA C 57.9 . 1 306 52 52 LEU CB C 41.4 . 1 307 52 52 LEU CD1 C 24.4 . 1 308 52 52 LEU CD2 C 24.0 . 1 309 52 52 LEU CG C 27.1 . 1 310 52 52 LEU N N 117.6 . 1 311 53 53 ASP H H 7.51 . 1 312 53 53 ASP HA H 4.42 . 1 313 53 53 ASP HB2 H 2.77 . 2 314 53 53 ASP HB3 H 2.77 . 2 315 53 53 ASP CA C 56.6 . 1 316 53 53 ASP CB C 39.8 . 1 317 53 53 ASP N N 119.9 . 1 318 54 54 ALA H H 8.80 . 1 319 54 54 ALA HA H 4.21 . 1 320 54 54 ALA HB H 1.38 . 1 321 54 54 ALA CA C 54.7 . 1 322 54 54 ALA CB C 18.2 . 1 323 54 54 ALA N N 123.4 . 1 324 55 55 ARG H H 7.86 . 1 325 55 55 ARG HA H 3.73 . 1 326 55 55 ARG HB2 H 1.92 . 2 327 55 55 ARG HB3 H 1.97 . 2 328 55 55 ARG HD2 H 3.25 . 2 329 55 55 ARG HD3 H 3.20 . 2 330 55 55 ARG HG2 H 1.80 . 2 331 55 55 ARG HG3 H 1.46 . 2 332 55 55 ARG CA C 60.2 . 1 333 55 55 ARG CB C 30.1 . 1 334 55 55 ARG CD C 43.6 . 1 335 55 55 ARG CG C 28.3 . 1 336 55 55 ARG N N 117.1 . 1 337 56 56 GLU H H 7.63 . 1 338 56 56 GLU HA H 4.00 . 1 339 56 56 GLU HB2 H 2.14 . 2 340 56 56 GLU HB3 H 2.14 . 2 341 56 56 GLU HG2 H 2.53 . 2 342 56 56 GLU HG3 H 2.42 . 2 343 56 56 GLU CA C 58.8 . 1 344 56 56 GLU CB C 28.3 . 1 345 56 56 GLU CG C 34.9 . 1 346 56 56 GLU N N 115.9 . 1 347 57 57 ASP H H 8.12 . 1 348 57 57 ASP HA H 4.38 . 1 349 57 57 ASP HB2 H 2.78 . 2 350 57 57 ASP HB3 H 2.69 . 2 351 57 57 ASP CA C 57.4 . 1 352 57 57 ASP CB C 42.5 . 1 353 57 57 ASP N N 120.2 . 1 354 58 58 LEU H H 8.16 . 1 355 58 58 LEU HA H 3.86 . 1 356 58 58 LEU HB2 H 1.91 . 2 357 58 58 LEU HB3 H 1.08 . 2 358 58 58 LEU HD1 H 0.58 . 2 359 58 58 LEU HD2 H 0.53 . 2 360 58 58 LEU HG H 1.80 . 1 361 58 58 LEU CA C 57.5 . 1 362 58 58 LEU CB C 41.4 . 1 363 58 58 LEU CD1 C 25.9 . 1 364 58 58 LEU CD2 C 22.4 . 1 365 58 58 LEU CG C 26.2 . 1 366 58 58 LEU N N 117.3 . 1 367 59 59 ILE H H 8.02 . 1 368 59 59 ILE HA H 3.30 . 1 369 59 59 ILE HB H 1.87 . 1 370 59 59 ILE HD1 H 0.81 . 1 371 59 59 ILE HG12 H 0.85 . 2 372 59 59 ILE HG13 H 1.70 . 2 373 59 59 ILE HG2 H 0.88 . 1 374 59 59 ILE CA C 65.7 . 1 375 59 59 ILE CB C 37.5 . 1 376 59 59 ILE CD1 C 12.8 . 1 377 59 59 ILE CG1 C 29.6 . 1 378 59 59 ILE CG2 C 17.6 . 1 379 59 59 ILE N N 118.6 . 1 380 60 60 LYS H H 7.89 . 1 381 60 60 LYS HA H 4.09 . 1 382 60 60 LYS HB2 H 1.98 . 2 383 60 60 LYS HB3 H 1.98 . 2 384 60 60 LYS HD2 H 1.73 . 2 385 60 60 LYS HD3 H 1.73 . 2 386 60 60 LYS HE2 H 3.00 . 2 387 60 60 LYS HE3 H 3.00 . 2 388 60 60 LYS HG2 H 1.62 . 2 389 60 60 LYS HG3 H 1.42 . 2 390 60 60 LYS CA C 59.8 . 1 391 60 60 LYS CB C 31.9 . 1 392 60 60 LYS CD C 29.3 . 1 393 60 60 LYS CE C 41.9 . 1 394 60 60 LYS CG C 25.0 . 1 395 60 60 LYS N N 119.4 . 1 396 61 61 LYS H H 8.08 . 1 397 61 61 LYS HA H 3.98 . 1 398 61 61 LYS HB2 H 1.82 . 2 399 61 61 LYS HB3 H 1.69 . 2 400 61 61 LYS HD2 H 1.62 . 2 401 61 61 LYS HD3 H 1.47 . 2 402 61 61 LYS HE2 H 3.08 . 2 403 61 61 LYS HE3 H 3.01 . 2 404 61 61 LYS HG2 H 1.41 . 2 405 61 61 LYS HG3 H 1.64 . 2 406 61 61 LYS CA C 59.2 . 1 407 61 61 LYS CB C 33.5 . 1 408 61 61 LYS CD C 29.3 . 1 409 61 61 LYS CE C 42.1 . 1 410 61 61 LYS CG C 26.6 . 1 411 61 61 LYS N N 119.2 . 1 412 62 62 ALA H H 8.49 . 1 413 62 62 ALA HA H 3.77 . 1 414 62 62 ALA HB H 1.19 . 1 415 62 62 ALA CA C 54.9 . 1 416 62 62 ALA CB C 19.1 . 1 417 62 62 ALA N N 122.2 . 1 418 63 63 ASP H H 8.85 . 1 419 63 63 ASP HA H 4.59 . 1 420 63 63 ASP HB2 H 2.88 . 2 421 63 63 ASP HB3 H 2.70 . 2 422 63 63 ASP CA C 56.9 . 1 423 63 63 ASP CB C 39.0 . 1 424 63 63 ASP N N 120.2 . 1 425 64 64 GLU H H 8.05 . 1 426 64 64 GLU HA H 4.07 . 1 427 64 64 GLU HB2 H 2.23 . 2 428 64 64 GLU HB3 H 2.13 . 2 429 64 64 GLU HG2 H 2.36 . 2 430 64 64 GLU HG3 H 2.56 . 2 431 64 64 GLU CA C 58.8 . 1 432 64 64 GLU CB C 29.0 . 1 433 64 64 GLU CG C 35.7 . 1 434 64 64 GLU N N 121.3 . 1 435 65 65 LYS H H 7.18 . 1 436 65 65 LYS HA H 4.31 . 1 437 65 65 LYS HB2 H 1.95 . 2 438 65 65 LYS HB3 H 1.66 . 2 439 65 65 LYS HD2 H 1.53 . 2 440 65 65 LYS HD3 H 1.53 . 2 441 65 65 LYS HE2 H 2.97 . 2 442 65 65 LYS HE3 H 2.97 . 2 443 65 65 LYS HG2 H 1.38 . 2 444 65 65 LYS HG3 H 1.38 . 2 445 65 65 LYS CA C 54.8 . 1 446 65 65 LYS CB C 33.0 . 1 447 65 65 LYS CD C 24.8 . 1 448 65 65 LYS CE C 42.0 . 1 449 65 65 LYS CG C 24.9 . 1 450 65 65 LYS N N 115.6 . 1 451 66 66 GLY H H 7.87 . 1 452 66 66 GLY HA2 H 3.86 . 2 453 66 66 GLY HA3 H 3.98 . 2 454 66 66 GLY CA C 45.7 . 1 455 66 66 GLY N N 107.5 . 1 456 67 67 ALA H H 7.92 . 1 457 67 67 ALA HA H 4.02 . 1 458 67 67 ALA HB H 1.26 . 1 459 67 67 ALA CA C 51.7 . 1 460 67 67 ALA CB C 21.1 . 1 461 67 67 ALA N N 118.9 . 1 462 68 68 ASP H H 8.79 . 1 463 68 68 ASP HA H 5.07 . 1 464 68 68 ASP HB2 H 3.24 . 2 465 68 68 ASP HB3 H 2.67 . 2 466 68 68 ASP CA C 56.5 . 1 467 68 68 ASP CB C 44.9 . 1 468 68 68 ASP N N 116.5 . 1 469 69 69 VAL H H 8.07 . 1 470 69 69 VAL HA H 5.13 . 1 471 69 69 VAL HB H 1.43 . 1 472 69 69 VAL HG1 H 0.71 . 2 473 69 69 VAL HG2 H 0.57 . 2 474 69 69 VAL CA C 60.3 . 1 475 69 69 VAL CB C 37.4 . 1 476 69 69 VAL CG1 C 23.4 . 1 477 69 69 VAL CG2 C 22.4 . 1 478 69 69 VAL N N 118.4 . 1 479 70 70 VAL H H 8.72 . 1 480 70 70 VAL HA H 4.55 . 1 481 70 70 VAL HB H 1.74 . 1 482 70 70 VAL HG1 H 0.75 . 2 483 70 70 VAL HG2 H 0.55 . 2 484 70 70 VAL CA C 59.8 . 1 485 70 70 VAL CB C 34.2 . 1 486 70 70 VAL CG1 C 20.0 . 1 487 70 70 VAL CG2 C 22.1 . 1 488 70 70 VAL N N 127.3 . 1 489 71 71 VAL H H 8.89 . 1 490 71 71 VAL HA H 4.55 . 1 491 71 71 VAL HB H 1.79 . 1 492 71 71 VAL HG1 H 0.02 . 2 493 71 71 VAL HG2 H 0.76 . 2 494 71 71 VAL CA C 60.8 . 1 495 71 71 VAL CB C 34.0 . 1 496 71 71 VAL CG1 C 20.6 . 1 497 71 71 VAL CG2 C 20.1 . 1 498 71 71 VAL N N 126.7 . 1 499 72 72 LEU H H 8.80 . 1 500 72 72 LEU HA H 4.44 . 1 501 72 72 LEU HB2 H 1.73 . 2 502 72 72 LEU HB3 H 1.63 . 2 503 72 72 LEU HD1 H 0.85 . 2 504 72 72 LEU HD2 H 0.77 . 2 505 72 72 LEU HG H 1.68 . 1 506 72 72 LEU CA C 55.7 . 1 507 72 72 LEU CB C 41.5 . 1 508 72 72 LEU CD1 C 25.3 . 1 509 72 72 LEU CD2 C 23.5 . 1 510 72 72 LEU CG C 27.6 . 1 511 72 72 LEU N N 127.4 . 1 512 73 73 THR H H 8.63 . 1 513 73 73 THR HA H 4.43 . 1 514 73 73 THR HB H 4.34 . 1 515 73 73 THR HG2 H 1.18 . 1 516 73 73 THR CA C 61.5 . 1 517 73 73 THR CB C 69.4 . 1 518 73 73 THR CG2 C 20.9 . 1 519 73 73 THR N N 114.0 . 1 520 74 74 SER H H 8.13 . 1 521 74 74 SER HA H 4.54 . 1 522 74 74 SER HB2 H 4.01 . 2 523 74 74 SER HB3 H 4.01 . 2 524 74 74 SER CA C 58.0 . 1 525 74 74 SER CB C 63.8 . 1 526 74 74 SER N N 116.0 . 1 527 75 75 GLY H H 8.57 . 1 528 75 75 GLY HA2 H 4.04 . 2 529 75 75 GLY HA3 H 4.04 . 2 530 75 75 GLY CA C 45.1 . 1 531 75 75 GLY N N 109.8 . 1 532 76 76 GLN H H 8.39 . 1 533 76 76 GLN HA H 4.49 . 1 534 76 76 GLN HB2 H 2.19 . 2 535 76 76 GLN HB3 H 2.02 . 2 536 76 76 GLN HE21 H 7.51 . 2 537 76 76 GLN HE22 H 6.84 . 2 538 76 76 GLN HG2 H 2.35 . 2 539 76 76 GLN HG3 H 2.35 . 2 540 76 76 GLN CA C 55.9 . 1 541 76 76 GLN CB C 29.6 . 1 542 76 76 GLN CG C 33.9 . 1 543 76 76 GLN N N 119.2 . 1 544 76 76 GLN NE2 N 111.9 . 1 545 77 77 THR H H 8.10 . 1 546 77 77 THR HA H 4.42 . 1 547 77 77 THR HB H 4.34 . 1 548 77 77 THR HG2 H 1.18 . 1 549 77 77 THR CA C 61.3 . 1 550 77 77 THR CB C 69.7 . 1 551 77 77 THR CG2 C 21.6 . 1 552 77 77 THR N N 113.0 . 1 553 78 78 GLU H H 8.45 . 1 554 78 78 GLU HA H 4.25 . 1 555 78 78 GLU HB2 H 2.12 . 2 556 78 78 GLU HB3 H 1.96 . 2 557 78 78 GLU HG2 H 2.31 . 2 558 78 78 GLU HG3 H 2.31 . 2 559 78 78 GLU CA C 56.9 . 1 560 78 78 GLU CB C 29.5 . 1 561 78 78 GLU CG C 35.8 . 1 562 78 78 GLU N N 120.7 . 1 563 79 79 ASN H H 8.32 . 1 564 79 79 ASN HA H 4.60 . 1 565 79 79 ASN HB2 H 2.85 . 2 566 79 79 ASN HB3 H 2.78 . 2 567 79 79 ASN HD21 H 7.61 . 2 568 79 79 ASN HD22 H 6.96 . 2 569 79 79 ASN CA C 53.7 . 1 570 79 79 ASN CB C 38.6 . 1 571 79 79 ASN N N 117.0 . 1 572 79 79 ASN ND2 N 112.8 . 1 573 80 80 LYS H H 7.91 . 1 574 80 80 LYS HA H 4.30 . 1 575 80 80 LYS HB2 H 1.68 . 2 576 80 80 LYS HB3 H 1.68 . 2 577 80 80 LYS HD2 H 1.61 . 2 578 80 80 LYS HD3 H 1.61 . 2 579 80 80 LYS HE2 H 2.96 . 2 580 80 80 LYS HE3 H 2.96 . 2 581 80 80 LYS HG2 H 1.38 . 2 582 80 80 LYS HG3 H 1.27 . 2 583 80 80 LYS CA C 56.0 . 1 584 80 80 LYS CB C 33.3 . 1 585 80 80 LYS CD C 28.2 . 1 586 80 80 LYS CE C 42.0 . 1 587 80 80 LYS CG C 24.9 . 1 588 80 80 LYS N N 118.8 . 1 589 81 81 ILE H H 8.34 . 1 590 81 81 ILE HA H 4.30 . 1 591 81 81 ILE HB H 1.75 . 1 592 81 81 ILE HD1 H 0.81 . 1 593 81 81 ILE HG12 H 1.37 . 2 594 81 81 ILE HG13 H 1.05 . 2 595 81 81 ILE HG2 H 0.77 . 1 596 81 81 ILE CA C 60.5 . 1 597 81 81 ILE CB C 39.8 . 1 598 81 81 ILE CD1 C 13.4 . 1 599 81 81 ILE CG1 C 27.1 . 1 600 81 81 ILE CG2 C 17.6 . 1 601 81 81 ILE N N 119.6 . 1 602 82 82 HIS H H 8.47 . 1 603 82 82 HIS HA H 4.78 . 1 604 82 82 HIS HB2 H 3.27 . 2 605 82 82 HIS HB3 H 3.12 . 2 606 82 82 HIS HD2 H 7.27 . 1 607 82 82 HIS HE1 H 8.09 . 1 608 82 82 HIS CA C 54.7 . 1 609 82 82 HIS CB C 28.9 . 1 610 82 82 HIS CD2 C 119.4 . 1 611 82 82 HIS CE1 C 135.2 . 1 612 82 82 HIS N N 121.6 . 1 613 83 83 GLY H H 8.34 . 1 614 83 83 GLY HA2 H 3.69 . 2 615 83 83 GLY HA3 H 4.19 . 2 616 83 83 GLY CA C 45.0 . 1 617 83 83 GLY N N 111.6 . 1 618 84 84 THR H H 8.12 . 1 619 84 84 THR HA H 5.03 . 1 620 84 84 THR HB H 4.07 . 1 621 84 84 THR HG2 H 1.07 . 1 622 84 84 THR CA C 60.1 . 1 623 84 84 THR CB C 72.0 . 1 624 84 84 THR CG2 C 21.0 . 1 625 84 84 THR N N 112.3 . 1 626 85 85 ALA H H 8.84 . 1 627 85 85 ALA HA H 4.95 . 1 628 85 85 ALA HB H 1.10 . 1 629 85 85 ALA CA C 51.2 . 1 630 85 85 ALA CB C 23.8 . 1 631 85 85 ALA N N 122.5 . 1 632 86 86 ASP H H 8.51 . 1 633 86 86 ASP HA H 5.20 . 1 634 86 86 ASP HB2 H 2.54 . 2 635 86 86 ASP HB3 H 2.14 . 2 636 86 86 ASP CA C 53.4 . 1 637 86 86 ASP CB C 43.1 . 1 638 86 86 ASP N N 121.4 . 1 639 87 87 ILE H H 7.97 . 1 640 87 87 ILE HA H 5.37 . 1 641 87 87 ILE HB H 1.53 . 1 642 87 87 ILE HD1 H 0.63 . 1 643 87 87 ILE HG12 H 0.55 . 2 644 87 87 ILE HG13 H 1.38 . 2 645 87 87 ILE HG2 H 0.76 . 1 646 87 87 ILE CA C 58.2 . 1 647 87 87 ILE CB C 41.2 . 1 648 87 87 ILE CD1 C 14.7 . 1 649 87 87 ILE CG1 C 25.9 . 1 650 87 87 ILE CG2 C 19.8 . 1 651 87 87 ILE N N 111.2 . 1 652 88 88 TYR H H 8.75 . 1 653 88 88 TYR HA H 5.44 . 1 654 88 88 TYR HB2 H 3.06 . 2 655 88 88 TYR HB3 H 2.46 . 2 656 88 88 TYR HD1 H 6.90 . 3 657 88 88 TYR HD2 H 6.90 . 3 658 88 88 TYR HE1 H 6.63 . 3 659 88 88 TYR HE2 H 6.63 . 3 660 88 88 TYR CA C 56.9 . 1 661 88 88 TYR CB C 44.0 . 1 662 88 88 TYR CD1 C 132.4 . 1 663 88 88 TYR CE1 C 117.6 . 1 664 88 88 TYR N N 118.0 . 1 665 89 89 LYS H H 9.59 . 1 666 89 89 LYS HA H 5.17 . 1 667 89 89 LYS HB2 H 2.01 . 2 668 89 89 LYS HB3 H 1.75 . 2 669 89 89 LYS HD2 H 1.84 . 2 670 89 89 LYS HD3 H 1.77 . 2 671 89 89 LYS HE2 H 3.08 . 2 672 89 89 LYS HE3 H 3.08 . 2 673 89 89 LYS HG2 H 1.62 . 2 674 89 89 LYS HG3 H 1.62 . 2 675 89 89 LYS CA C 54.4 . 1 676 89 89 LYS CB C 36.8 . 1 677 89 89 LYS CD C 29.3 . 1 678 89 89 LYS CE C 42.2 . 1 679 89 89 LYS CG C 24.8 . 1 680 89 89 LYS N N 123.5 . 1 681 90 90 LYS H H 10.19 . 1 682 90 90 LYS HA H 3.81 . 1 683 90 90 LYS HB2 H 1.74 . 2 684 90 90 LYS HB3 H 1.57 . 2 685 90 90 LYS HD2 H 1.50 . 2 686 90 90 LYS HD3 H 1.50 . 2 687 90 90 LYS HE2 H 2.89 . 2 688 90 90 LYS HE3 H 2.89 . 2 689 90 90 LYS HG2 H 1.01 . 2 690 90 90 LYS HG3 H 1.35 . 2 691 90 90 LYS CA C 57.5 . 1 692 90 90 LYS CB C 32.7 . 1 693 90 90 LYS CD C 28.9 . 1 694 90 90 LYS CE C 42.2 . 1 695 90 90 LYS CG C 25.5 . 1 696 90 90 LYS N N 129.2 . 1 697 91 91 LYS H H 8.45 . 1 698 91 91 LYS HA H 4.10 . 1 699 91 91 LYS HB2 H 1.69 . 2 700 91 91 LYS HB3 H 1.46 . 2 701 91 91 LYS HD2 H 1.61 . 2 702 91 91 LYS HD3 H 1.57 . 2 703 91 91 LYS HE2 H 2.86 . 2 704 91 91 LYS HE3 H 2.86 . 2 705 91 91 LYS HG2 H 1.34 . 2 706 91 91 LYS HG3 H 1.15 . 2 707 91 91 LYS CA C 57.3 . 1 708 91 91 LYS CB C 33.1 . 1 709 91 91 LYS CD C 29.2 . 1 710 91 91 LYS CE C 42.0 . 1 711 91 91 LYS CG C 25.9 . 1 712 91 91 LYS N N 125.9 . 1 713 92 92 LEU H H 8.27 . 1 714 92 92 LEU HA H 4.28 . 1 715 92 92 LEU HB2 H 1.55 . 2 716 92 92 LEU HB3 H 1.47 . 2 717 92 92 LEU HD1 H 0.83 . 2 718 92 92 LEU HD2 H 0.90 . 2 719 92 92 LEU HG H 1.55 . 1 720 92 92 LEU CA C 54.6 . 1 721 92 92 LEU CB C 42.1 . 1 722 92 92 LEU CD1 C 23.6 . 1 723 92 92 LEU CD2 C 24.7 . 1 724 92 92 LEU CG C 26.8 . 1 725 92 92 LEU N N 123.2 . 1 726 93 93 GLU H H 8.31 . 1 727 93 93 GLU HA H 4.22 . 1 728 93 93 GLU HB2 H 1.86 . 2 729 93 93 GLU HB3 H 1.83 . 2 730 93 93 GLU HG2 H 2.16 . 2 731 93 93 GLU HG3 H 2.16 . 2 732 93 93 GLU CA C 55.7 . 1 733 93 93 GLU CB C 30.2 . 1 734 93 93 GLU CG C 35.5 . 1 735 93 93 GLU N N 122.0 . 1 736 94 94 HIS H H 8.57 . 1 737 94 94 HIS HA H 4.63 . 1 738 94 94 HIS HB2 H 3.06 . 2 739 94 94 HIS HB3 H 3.15 . 2 740 94 94 HIS HD2 H 7.08 . 1 741 94 94 HIS HE1 H 8.08 . 1 742 94 94 HIS CA C 55.0 . 1 743 94 94 HIS CB C 28.9 . 1 744 94 94 HIS CD2 C 119.0 . 1 745 94 94 HIS CE1 C 135.2 . 1 746 94 94 HIS N N 119.7 . 1 747 95 95 HIS H H 8.61 . 1 748 95 95 HIS HA H 4.65 . 1 749 95 95 HIS HB2 H 3.14 . 2 750 95 95 HIS HB3 H 3.14 . 2 751 95 95 HIS HD2 H 7.08 . 1 752 95 95 HIS HE1 H 8.08 . 1 753 95 95 HIS CA C 55.2 . 1 754 95 95 HIS CB C 28.9 . 1 755 95 95 HIS CD2 C 119.0 . 1 756 95 95 HIS CE1 C 135.2 . 1 757 95 95 HIS N N 119.3 . 1 758 96 96 HIS H H 8.68 . 1 759 96 96 HIS HA H 4.66 . 1 760 96 96 HIS HB2 H 3.17 . 2 761 96 96 HIS HB3 H 3.17 . 2 762 96 96 HIS HD2 H 7.08 . 1 763 96 96 HIS HE1 H 8.08 . 1 764 96 96 HIS CA C 55.2 . 1 765 96 96 HIS CB C 29.1 . 1 766 96 96 HIS CD2 C 119.0 . 1 767 96 96 HIS CE1 C 135.2 . 1 768 96 96 HIS N N 120.1 . 1 769 97 97 HIS H H 8.58 . 1 770 97 97 HIS HA H 4.66 . 1 771 97 97 HIS HB2 H 3.27 . 2 772 97 97 HIS HB3 H 3.27 . 2 773 97 97 HIS HD2 H 7.08 . 1 774 97 97 HIS HE1 H 8.08 . 1 775 97 97 HIS CA C 55.4 . 1 776 97 97 HIS CB C 29.2 . 1 777 97 97 HIS CD2 C 119.0 . 1 778 97 97 HIS CE1 C 135.2 . 1 779 97 97 HIS N N 120.4 . 1 780 98 98 HIS H H 8.39 . 1 781 98 98 HIS HA H 4.62 . 1 782 98 98 HIS HB2 H 3.12 . 2 783 98 98 HIS HB3 H 3.12 . 2 784 98 98 HIS HD2 H 7.08 . 1 785 98 98 HIS HE1 H 8.08 . 1 786 98 98 HIS CA C 55.5 . 1 787 98 98 HIS CB C 29.1 . 1 788 98 98 HIS CD2 C 119.0 . 1 789 98 98 HIS CE1 C 135.2 . 1 790 98 98 HIS N N 125.3 . 1 stop_ save_