data_4840 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignment and secondary structure of Mycobacterium tuberculosis adenylate kinase ; _BMRB_accession_number 4840 _BMRB_flat_file_name bmr4840.str _Entry_type original _Submission_date 2000-09-26 _Accession_date 2000-09-26 _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 Miron Simona . . 2 Munier-Lehmann Helene . . 3 Craescu Constantin T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 702 "13C chemical shifts" 333 "15N chemical shifts" 178 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-14 original author . stop_ _Original_release_date 2001-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignment and secondary structure of Mycobacterium tuberculosis adenylate kinase ; _Citation_status published _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 Miron Simona . . 2 Munier-Lehmann Helene . . 3 Craescu Constantin T. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 89 _Page_last 90 _Year 2001 _Details . loop_ _Keyword 'nuclear magnetic resonance' protein 'resonance assignment' 'Adenylate kinase' 'NMP kinase' 'Mycobacterium tuberculosis' stop_ save_ ################################## # Molecular system description # ################################## save_system_AK _Saveframe_category molecular_system _Mol_system_name 'Adenylate kinase' _Abbreviation_common AK _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AK $AK stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Adenylate kinase from M. tuberculosis' _Abbreviation_common AKmt _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 181 _Mol_residue_sequence ; MRVLLLGPPGAGKGTQAVKL AEKLGIPQISTGELFRRNIE EGTKLGVEAKRYLDAGDLVP SDLTNELVDDRLNNPDAANG FILDGYPRSVEQAKALHEML ERRGTDIDAVLEFRVSEEVL LERLKGRGRADDTDDVILNR MKVYRDETAPLLEYYRDQLK TVDAVGTMDEVFARALRALG K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 VAL 4 LEU 5 LEU 6 LEU 7 GLY 8 PRO 9 PRO 10 GLY 11 ALA 12 GLY 13 LYS 14 GLY 15 THR 16 GLN 17 ALA 18 VAL 19 LYS 20 LEU 21 ALA 22 GLU 23 LYS 24 LEU 25 GLY 26 ILE 27 PRO 28 GLN 29 ILE 30 SER 31 THR 32 GLY 33 GLU 34 LEU 35 PHE 36 ARG 37 ARG 38 ASN 39 ILE 40 GLU 41 GLU 42 GLY 43 THR 44 LYS 45 LEU 46 GLY 47 VAL 48 GLU 49 ALA 50 LYS 51 ARG 52 TYR 53 LEU 54 ASP 55 ALA 56 GLY 57 ASP 58 LEU 59 VAL 60 PRO 61 SER 62 ASP 63 LEU 64 THR 65 ASN 66 GLU 67 LEU 68 VAL 69 ASP 70 ASP 71 ARG 72 LEU 73 ASN 74 ASN 75 PRO 76 ASP 77 ALA 78 ALA 79 ASN 80 GLY 81 PHE 82 ILE 83 LEU 84 ASP 85 GLY 86 TYR 87 PRO 88 ARG 89 SER 90 VAL 91 GLU 92 GLN 93 ALA 94 LYS 95 ALA 96 LEU 97 HIS 98 GLU 99 MET 100 LEU 101 GLU 102 ARG 103 ARG 104 GLY 105 THR 106 ASP 107 ILE 108 ASP 109 ALA 110 VAL 111 LEU 112 GLU 113 PHE 114 ARG 115 VAL 116 SER 117 GLU 118 GLU 119 VAL 120 LEU 121 LEU 122 GLU 123 ARG 124 LEU 125 LYS 126 GLY 127 ARG 128 GLY 129 ARG 130 ALA 131 ASP 132 ASP 133 THR 134 ASP 135 ASP 136 VAL 137 ILE 138 LEU 139 ASN 140 ARG 141 MET 142 LYS 143 VAL 144 TYR 145 ARG 146 ASP 147 GLU 148 THR 149 ALA 150 PRO 151 LEU 152 LEU 153 GLU 154 TYR 155 TYR 156 ARG 157 ASP 158 GLN 159 LEU 160 LYS 161 THR 162 VAL 163 ASP 164 ALA 165 VAL 166 GLY 167 THR 168 MET 169 ASP 170 GLU 171 VAL 172 PHE 173 ALA 174 ARG 175 ALA 176 LEU 177 ARG 178 ALA 179 LEU 180 GLY 181 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 PDB 1P4S "Solution Structure Of Mycobacterium Tuberculosis Adenylate Kinase" 100.00 181 100.00 100.00 2.27e-123 PDB 2CDN "Crystal Structure Of Mycobacterium Tuberculosis Adenylate Kinase Complexed With Two Molecules Of Adp And Mg" 100.00 201 100.00 100.00 6.21e-124 DBJ BAH25046 "adenylate kinase [Mycobacterium bovis BCG str. Tokyo 172]" 100.00 181 100.00 100.00 2.27e-123 DBJ BAL64618 "adenylate kinase [Mycobacterium tuberculosis str. Erdman = ATCC 35801]" 100.00 181 100.00 100.00 2.27e-123 DBJ BAQ04633 "adenylate kinase [Mycobacterium tuberculosis str. Kurono]" 90.61 164 99.39 100.00 6.78e-110 DBJ GAA44509 "adenylate kinase [Mycobacterium tuberculosis NCGM2209]" 100.00 181 100.00 100.00 2.27e-123 EMBL CAD93616 "PROBABLE ADENYLATE KINASE ADK (ATP-AMP TRANSPHOSPHORYLASE) [Mycobacterium bovis AF2122/97]" 100.00 181 100.00 100.00 2.27e-123 EMBL CAL70769 "Probable adenylate kinase adk [Mycobacterium bovis BCG str. Pasteur 1173P2]" 100.00 181 100.00 100.00 2.27e-123 EMBL CCC25815 "putative adenylate kinase ADK (ATP-AMP transphosphorylase) [Mycobacterium africanum GM041182]" 100.00 181 100.00 100.00 2.27e-123 EMBL CCC43078 "putative adenylate kinase ADK (ATP-AMP transphosphorylase) [Mycobacterium canettii CIPT 140010059]" 100.00 181 100.00 100.00 2.27e-123 EMBL CCC63341 "probable adenylate kinase adk [Mycobacterium bovis BCG str. Moreau RDJ]" 100.00 181 100.00 100.00 2.27e-123 GB AAD09879 "adenylate kinase [Mycobacterium bovis]" 100.00 181 100.00 100.00 2.27e-123 GB AAK44991 "adenylate kinase [Mycobacterium tuberculosis CDC1551]" 100.00 181 100.00 100.00 2.27e-123 GB ABQ72469 "adenylate kinase [Mycobacterium tuberculosis H37Ra]" 100.00 181 100.00 100.00 2.27e-123 GB ABR05090 "adenylate kinase adk (ATP-AMP transphosphorylase) [Mycobacterium tuberculosis F11]" 100.00 181 100.00 100.00 2.27e-123 GB ACT23783 "adenylate kinase adk [Mycobacterium tuberculosis KZN 1435]" 100.00 181 100.00 100.00 2.27e-123 REF NP_215247 "adenylate kinase [Mycobacterium tuberculosis H37Rv]" 100.00 181 100.00 100.00 2.27e-123 REF NP_335177 "adenylate kinase [Mycobacterium tuberculosis CDC1551]" 100.00 181 100.00 100.00 2.27e-123 REF NP_854412 "adenylate kinase [Mycobacterium bovis AF2122/97]" 100.00 181 100.00 100.00 2.27e-123 REF WP_003403726 "MULTISPECIES: adenylate kinase [Mycobacterium tuberculosis complex]" 100.00 181 100.00 100.00 2.27e-123 REF WP_003911271 "adenylate kinase [Mycobacterium tuberculosis]" 98.34 178 99.44 100.00 5.57e-121 SP A1KGL4 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 181 100.00 100.00 2.27e-123 SP A5U0B9 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 181 100.00 100.00 2.27e-123 SP C1AL67 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 181 100.00 100.00 2.27e-123 SP P69439 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 181 100.00 100.00 2.27e-123 SP P9WKF4 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 181 100.00 100.00 2.27e-123 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AK . 1773 Bacteria . Mycobacterium tuberculosis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $AK 'recombinant technology' 'E. coli' Escherichia coli BLI5 pET22b pHL20 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AK 1.0 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AK 1.0 mM [U-15N] H2O 95 % . D2O 5 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AK 1.2 mM '[U-15N; U-13C]' H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.1 . n/a temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS C 13 'methyl protons' ppm 0.0 internal indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_AKmt _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name AK _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 . 2 ARG H H 9.73 0.01 1 2 . 2 ARG HA H 4.30 0.01 1 3 . 2 ARG HB2 H 1.85 0.01 1 4 . 2 ARG HB3 H 1.85 0.01 1 5 . 2 ARG N N 124.3 0.1 1 6 . 2 ARG CA C 53.7 0.1 1 7 . 2 ARG CB C 27.7 0.1 1 8 . 3 VAL H H 8.48 0.01 1 9 . 3 VAL HA H 5.26 0.01 1 10 . 3 VAL HB H 2.08 0.01 1 11 . 3 VAL HG1 H 0.85 0.01 2 12 . 3 VAL HG2 H 0.92 0.01 2 13 . 3 VAL N N 125.2 0.1 1 14 . 3 VAL CA C 58.3 0.1 1 15 . 3 VAL CB C 34.0 0.1 1 16 . 4 LEU H H 8.21 0.01 1 17 . 4 LEU HA H 5.39 0.01 1 18 . 4 LEU HB2 H 1.68 0.01 1 19 . 4 LEU HB3 H 1.68 0.01 1 20 . 4 LEU HG H 1.65 0.01 1 21 . 4 LEU HD1 H 0.85 0.01 2 22 . 4 LEU HD2 H 1.05 0.01 2 23 . 4 LEU N N 125.4 0.1 1 24 . 4 LEU CA C 50.9 0.1 1 25 . 4 LEU CB C 42.8 0.1 1 26 . 5 LEU H H 8.35 0.01 1 27 . 5 LEU HA H 5.33 0.01 1 28 . 5 LEU HB2 H 2.00 0.01 1 29 . 5 LEU HB3 H 2.00 0.01 1 30 . 5 LEU HG H 1.31 0.01 1 31 . 5 LEU HD1 H 0.93 0.01 2 32 . 5 LEU HD2 H 0.87 0.01 2 33 . 5 LEU N N 121.2 0.1 1 34 . 5 LEU CA C 51.2 0.1 1 35 . 5 LEU CB C 41.2 0.1 1 36 . 6 LEU H H 9.33 0.01 1 37 . 6 LEU HA H 5.07 0.01 1 38 . 6 LEU HB2 H 1.68 0.01 2 39 . 6 LEU HB3 H 1.59 0.01 2 40 . 6 LEU HG H 1.49 0.01 1 41 . 6 LEU HD1 H 1.02 0.01 2 42 . 6 LEU HD2 H 0.75 0.01 2 43 . 6 LEU N N 123.5 0.1 1 44 . 6 LEU CA C 51.2 0.1 1 45 . 6 LEU CB C 43.9 0.1 1 46 . 7 GLY H H 8.55 0.01 1 47 . 7 GLY N N 109.9 0.1 1 48 . 7 GLY CA C 43.5 0.1 1 49 . 10 GLY CA C 43.3 0.1 1 50 . 11 ALA H H 8.03 0.01 1 51 . 11 ALA N N 122.5 0.1 1 52 . 11 ALA CA C 51.0 0.1 1 53 . 11 ALA CB C 17.0 0.1 1 54 . 12 GLY H H 8.42 0.01 1 55 . 12 GLY N N 108.2 0.1 1 56 . 12 GLY CA C 43.3 0.1 1 57 . 15 THR CA C 64 0.1 1 58 . 15 THR CB C 66.8 0.1 1 59 . 16 GLN H H 7.79 0.01 1 60 . 16 GLN HE21 H 6.55 0.01 2 61 . 16 GLN HE22 H 7.22 0.01 2 62 . 16 GLN N N 119.4 0.1 1 63 . 16 GLN NE2 N 108.3 0.1 2 64 . 16 GLN CA C 55.4 0.1 1 65 . 16 GLN CB C 24.8 0.1 1 66 . 17 ALA H H 8.93 0.01 1 67 . 17 ALA HA H 3.90 0.01 1 68 . 17 ALA HB H 1.51 0.01 1 69 . 17 ALA N N 122.1 0.1 1 70 . 17 ALA CA C 54.0 0.1 1 71 . 17 ALA CB C 16.0 0.1 1 72 . 18 VAL H H 7.04 0.01 1 73 . 18 VAL HA H 3.65 0.01 1 74 . 18 VAL HB H 2.18 0.01 1 75 . 18 VAL HG1 H 1.15 0.01 2 76 . 18 VAL HG2 H 1.01 0.01 2 77 . 18 VAL N N 114.8 0.1 1 78 . 18 VAL CA C 63.9 0.1 1 79 . 18 VAL CB C 30.0 0.1 1 80 . 19 LYS H H 7.38 0.01 1 81 . 19 LYS HA H 4.00 0.01 1 82 . 19 LYS HB2 H 1.56 0.01 2 83 . 19 LYS HB3 H 1.48 0.01 2 84 . 19 LYS HG2 H 1.19 0.01 2 85 . 19 LYS N N 120.2 0.1 1 86 . 19 LYS CA C 57.2 0.1 1 87 . 19 LYS CB C 29.8 0.1 1 88 . 20 LEU H H 9.33 0.01 1 89 . 20 LEU HA H 4.20 0.01 1 90 . 20 LEU HB2 H 2.15 0.01 1 91 . 20 LEU HB3 H 2.15 0.01 1 92 . 20 LEU N N 121.5 0.1 1 93 . 20 LEU CA C 56.2 0.1 1 94 . 20 LEU CB C 40.7 0.1 1 95 . 21 ALA H H 8.29 0.01 1 96 . 21 ALA HA H 4.06 0.01 1 97 . 21 ALA HB H 1.74 0.01 1 98 . 21 ALA N N 123.7 0.1 1 99 . 21 ALA CA C 53.7 0.1 1 100 . 21 ALA CB C 16.3 0.1 1 101 . 22 GLU H H 7.78 0.01 1 102 . 22 GLU HA H 4.11 0.01 1 103 . 22 GLU HB2 H 2.25 0.01 2 104 . 22 GLU HB3 H 2.15 0.01 2 105 . 22 GLU N N 116.9 0.1 1 106 . 22 GLU CA C 56.8 0.1 1 107 . 22 GLU CB C 27.4 0.1 1 108 . 23 LYS H H 7.85 0.01 1 109 . 23 LYS HA H 4.33 0.01 1 110 . 23 LYS N N 119.2 0.1 1 111 . 23 LYS CA C 55.4 0.1 1 112 . 23 LYS CB C 30.5 0.1 1 113 . 24 LEU H H 8.65 0.01 1 114 . 24 LEU HA H 4.38 0.01 1 115 . 24 LEU HB2 H 1.89 0.01 1 116 . 24 LEU HB3 H 1.89 0.01 1 117 . 24 LEU HG H 1.63 0.01 1 118 . 24 LEU HD1 H 0.87 0.01 1 119 . 24 LEU HD2 H 0.87 0.01 1 120 . 24 LEU N N 116.7 0.1 1 121 . 24 LEU CA C 53.3 0.1 1 122 . 24 LEU CB C 40.1 0.1 1 123 . 25 GLY H H 8.6 0.01 1 124 . 25 GLY HA2 H 4.00 0.01 2 125 . 25 GLY HA3 H 4.02 0.01 2 126 . 25 GLY N N 110.4 0.1 1 127 . 25 GLY CA C 44.9 0.1 1 128 . 26 ILE H H 7.66 0.01 1 129 . 26 ILE HA H 4.86 0.01 1 130 . 26 ILE N N 113.7 0.1 1 131 . 26 ILE CA C 55.6 0.1 1 132 . 26 ILE CB C 37.2 0.1 1 133 . 27 PRO CA C 60.6 0.1 1 134 . 27 PRO CB C 30.2 0.1 1 135 . 28 GLN H H 8.38 0.01 1 136 . 28 GLN HA H 5.11 0.01 1 137 . 28 GLN HB2 H 2.10 0.01 2 138 . 28 GLN HB3 H 2.06 0.01 2 139 . 28 GLN HG2 H 2.39 0.01 2 140 . 28 GLN HE21 H 6.76 0.01 2 141 . 28 GLN HE22 H 7.33 0.01 2 142 . 28 GLN N N 119.3 0.1 1 143 . 28 GLN NE2 N 111.2 0.1 1 144 . 28 GLN CA C 52.0 0.1 1 145 . 28 GLN CB C 26.5 0.1 1 146 . 29 ILE H H 9.45 0.01 1 147 . 29 ILE HA H 4.25 0.01 1 148 . 29 ILE HB H 1.83 0.01 1 149 . 29 ILE N N 128.2 0.1 1 150 . 29 ILE CA C 58.9 0.1 1 151 . 29 ILE CB C 37.8 0.1 1 152 . 30 SER H H 8.27 0.01 1 153 . 30 SER HA H 5.67 0.01 1 154 . 30 SER HB2 H 4.01 0.01 2 155 . 30 SER HB3 H 4.08 0.01 2 156 . 30 SER N N 122.4 0.1 1 157 . 30 SER CA C 53.0 0.1 1 158 . 30 SER CB C 62.7 0.1 1 159 . 31 THR H H 8.47 0.01 1 160 . 31 THR N N 118.8 0.1 1 161 . 31 THR CA C 64.5 0.1 1 162 . 32 GLY H H 8.74 0.01 1 163 . 32 GLY HA2 H 3.95 0.01 2 164 . 32 GLY HA3 H 4.08 0.01 2 165 . 32 GLY N N 109.6 0.1 1 166 . 32 GLY CA C 45.4 0.1 1 167 . 33 GLU H H 7.41 0.01 1 168 . 33 GLU HA H 4.36 0.01 1 169 . 33 GLU HB2 H 2.14 0.01 2 170 . 33 GLU HB3 H 2.18 0.01 2 171 . 33 GLU HG2 H 2.42 0.01 1 172 . 33 GLU HG3 H 2.42 0.01 1 173 . 33 GLU N N 122.7 0.1 1 174 . 33 GLU CA C 56.2 0.1 1 175 . 33 GLU CB C 27.4 0.1 1 176 . 34 LEU H H 8.07 0.01 1 177 . 34 LEU HA H 4.17 0.01 1 178 . 34 LEU HB2 H 1.75 0.01 1 179 . 34 LEU HB3 H 1.75 0.01 1 180 . 34 LEU HG H 1.47 0.01 1 181 . 34 LEU HD1 H 0.71 0.01 1 182 . 34 LEU HD2 H 0.71 0.01 1 183 . 34 LEU N N 120.6 0.1 1 184 . 34 LEU CA C 55.7 0.1 1 185 . 34 LEU CB C 39.7 0.1 1 186 . 35 PHE H H 8.55 0.01 1 187 . 35 PHE HA H 4.23 0.01 1 188 . 35 PHE HB2 H 3.33 0.01 2 189 . 35 PHE HB3 H 3.12 0.01 2 190 . 35 PHE HD1 H 7.24 0.01 1 191 . 35 PHE HD2 H 7.24 0.01 1 192 . 35 PHE N N 120.0 0.1 1 193 . 35 PHE CA C 59.5 0.1 1 194 . 35 PHE CB C 36.0 0.1 1 195 . 36 ARG H H 7.94 0.01 1 196 . 36 ARG HA H 4.03 0.01 1 197 . 36 ARG HB2 H 2.00 0.01 2 198 . 36 ARG HB3 H 2.11 0.01 2 199 . 36 ARG N N 119.2 0.1 1 200 . 36 ARG CA C 58.1 0.1 1 201 . 36 ARG CB C 27.8 0.1 1 202 . 37 ARG H H 8.80 0.01 1 203 . 37 ARG HA H 4.18 0.01 1 204 . 37 ARG HB2 H 1.94 0.01 2 205 . 37 ARG HB3 H 2.05 0.01 2 206 . 37 ARG HG2 H 1.76 0.01 1 207 . 37 ARG HG3 H 1.76 0.01 1 208 . 37 ARG N N 118.4 0.1 1 209 . 37 ARG CA C 57.2 0.1 1 210 . 37 ARG CB C 27.6 0.1 1 211 . 38 ASN H H 7.60 0.01 1 212 . 38 ASN HA H 4.42 0.01 1 213 . 38 ASN HB2 H 2.86 0.01 1 214 . 38 ASN HB3 H 2.86 0.01 1 215 . 38 ASN HD21 H 7.69 0.01 2 216 . 38 ASN HD22 H 8.00 0.01 2 217 . 38 ASN N N 116.5 0.1 1 218 . 38 ASN ND2 N 116.1 0.1 1 219 . 38 ASN CA C 55.6 0.1 1 220 . 38 ASN CB C 36.5 0.1 1 221 . 39 ILE H H 8.43 0.01 1 222 . 39 ILE HA H 3.58 0.01 1 223 . 39 ILE HB H 2.04 0.01 1 224 . 39 ILE HG12 H 0.97 0.01 2 225 . 39 ILE HG13 H 0.88 0.01 2 226 . 39 ILE HD1 H 1.28 0.01 1 227 . 39 ILE N N 120.5 0.1 1 228 . 39 ILE CA C 64.1 0.1 1 229 . 39 ILE CB C 35.9 0.1 1 230 . 40 GLU H H 8.70 0.01 1 231 . 40 GLU HA H 4.10 0.01 1 232 . 40 GLU HB2 H 2.01 0.01 2 233 . 40 GLU N N 121.8 0.1 1 234 . 40 GLU CA C 57.5 0.1 1 235 . 40 GLU CB C 27.5 0.1 1 236 . 41 GLU H H 8.15 0.01 1 237 . 41 GLU HA H 4.31 0.01 1 238 . 41 GLU HB2 H 2.10 0.01 2 239 . 41 GLU HB3 H 2.12 0.01 2 240 . 41 GLU N N 116.2 0.1 1 241 . 41 GLU CA C 54.9 0.1 1 242 . 41 GLU CB C 28.0 0.1 1 243 . 42 GLY H H 7.88 0.01 1 244 . 42 GLY HA2 H 3.98 0.01 2 245 . 42 GLY HA3 H 3.89 0.01 2 246 . 42 GLY N N 109.9 0.1 1 247 . 42 GLY CA C 44.5 0.1 1 248 . 43 THR H H 7.86 0.01 1 249 . 43 THR HA H 4.40 0.01 1 250 . 43 THR HB H 4.91 0.01 1 251 . 43 THR HG2 H 1.47 0.01 1 252 . 43 THR N N 110.2 0.1 1 253 . 43 THR CA C 58.8 0.1 1 254 . 43 THR CB C 68.4 0.1 1 255 . 44 LYS H H 8.81 0.01 1 256 . 44 LYS HA H 4.09 0.01 1 257 . 44 LYS N N 122.4 0.1 1 258 . 44 LYS CA C 58.2 0.1 1 259 . 44 LYS CB C 30.0 0.1 1 260 . 45 LEU H H 8.30 0.01 1 261 . 45 LEU HA H 4.20 0.01 1 262 . 45 LEU HB2 H 1.67 0.01 1 263 . 45 LEU HB3 H 1.67 0.01 1 264 . 45 LEU HG H 1.28 0.01 1 265 . 45 LEU HD1 H 0.90 0.01 2 266 . 45 LEU N N 117.3 0.1 1 267 . 45 LEU CA C 55.2 0.1 1 268 . 45 LEU CB C 39.9 0.1 1 269 . 46 GLY H H 8.24 0.01 1 270 . 46 GLY HA2 H 3.65 0.01 2 271 . 46 GLY HA3 H 3.52 0.01 2 272 . 46 GLY N N 109.0 0.1 1 273 . 46 GLY CA C 44.5 0.1 1 274 . 47 VAL H H 8.74 0.01 1 275 . 47 VAL HA H 3.69 0.01 1 276 . 47 VAL HB H 2.23 0.01 1 277 . 47 VAL HG1 H 1.02 0.01 2 278 . 47 VAL HG2 H 1.09 0.01 2 279 . 47 VAL N N 122.0 0.1 1 280 . 47 VAL CA C 64.4 0.1 1 281 . 47 VAL CB C 29.6 0.1 1 282 . 48 GLU H H 7.49 0.01 1 283 . 48 GLU HA H 4.22 0.01 1 284 . 48 GLU HB2 H 2.52 0.01 2 285 . 48 GLU HB3 H 2.27 0.01 2 286 . 48 GLU N N 120.2 0.1 1 287 . 48 GLU CA C 56.9 0.1 1 288 . 48 GLU CB C 27.4 0.1 1 289 . 49 ALA H H 8.54 0.01 1 290 . 49 ALA HA H 4.19 0.01 1 291 . 49 ALA HB H 1.54 0.01 1 292 . 49 ALA N N 120.5 0.1 1 293 . 49 ALA CA C 53.4 0.1 1 294 . 49 ALA CB C 16.5 0.1 1 295 . 50 LYS H H 8.48 0.01 1 296 . 50 LYS HA H 3.89 0.01 1 297 . 50 LYS HB2 H 2.03 0.01 2 298 . 50 LYS HB3 H 2.00 0.01 2 299 . 50 LYS N N 118.2 0.1 1 300 . 50 LYS CA C 57.2 0.1 1 301 . 50 LYS CB C 30.6 0.1 1 302 . 51 ARG H H 7.42 0.01 1 303 . 51 ARG HA H 4.10 0.01 1 304 . 51 ARG HB2 H 1.83 0.01 1 305 . 51 ARG HB3 H 1.83 0.01 1 306 . 51 ARG HG2 H 1.70 0.01 2 307 . 51 ARG N N 117.8 0.1 1 308 . 51 ARG CA C 57.4 0.1 1 309 . 51 ARG CB C 27.8 0.1 1 310 . 52 TYR H H 7.30 0.01 1 311 . 52 TYR HA H 4.25 0.01 1 312 . 52 TYR HB2 H 2.97 0.01 1 313 . 52 TYR HB3 H 2.97 0.01 1 314 . 52 TYR HD1 H 7.36 0.01 1 315 . 52 TYR HD2 H 7.36 0.01 1 316 . 52 TYR HE1 H 6.89 0.01 1 317 . 52 TYR HE2 H 6.89 0.01 1 318 . 52 TYR N N 117.8 0.1 1 319 . 52 TYR CA C 59.7 0.1 1 320 . 52 TYR CB C 36.0 0.1 1 321 . 53 LEU H H 8.06 0.01 1 322 . 53 LEU HA H 4.24 0.01 1 323 . 53 LEU HB2 H 1.82 0.01 1 324 . 53 LEU HB3 H 1.82 0.01 1 325 . 53 LEU HG H 1.66 0.01 1 326 . 53 LEU HD1 H 0.90 0.01 2 327 . 53 LEU N N 120.4 0.1 1 328 . 53 LEU CA C 56.3 0.1 1 329 . 53 LEU CB C 39.3 0.1 1 330 . 54 ASP H H 9.18 0.01 1 331 . 54 ASP HA H 4.47 0.01 1 332 . 54 ASP HB2 H 2.81 0.01 2 333 . 54 ASP HB3 H 2.70 0.01 2 334 . 54 ASP N N 121.2 0.1 1 335 . 54 ASP CA C 54.8 0.1 1 336 . 54 ASP CB C 37.8 0.1 1 337 . 55 ALA H H 7.21 0.01 1 338 . 55 ALA HA H 4.49 0.01 1 339 . 55 ALA HB H 1.59 0.01 1 340 . 55 ALA N N 120.3 0.1 1 341 . 55 ALA CA C 49.9 0.1 1 342 . 55 ALA CB C 17.4 0.1 1 343 . 56 GLY H H 7.96 0.01 1 344 . 56 GLY HA2 H 4.23 0.01 2 345 . 56 GLY HA3 H 3.89 0.01 2 346 . 56 GLY N N 107.7 0.1 1 347 . 56 GLY CA C 43.4 0.1 1 348 . 57 ASP H H 8.07 0.01 1 349 . 57 ASP HA H 5.00 0.01 1 350 . 57 ASP HB2 H 2.99 0.01 2 351 . 57 ASP HB3 H 2.72 0.01 2 352 . 57 ASP N N 121.2 0.1 1 353 . 57 ASP CA C 50.7 0.1 1 354 . 57 ASP CB C 41.7 0.1 1 355 . 58 LEU H H 8.20 0.01 1 356 . 58 LEU HA H 4.32 0.01 1 357 . 58 LEU HB2 H 1.57 0.01 2 358 . 58 LEU HB3 H 1.47 0.01 2 359 . 58 LEU HG H 1.76 0.01 1 360 . 58 LEU HD2 H 0.98 0.01 2 361 . 58 LEU N N 120.4 0.1 1 362 . 58 LEU CA C 52.0 0.1 1 363 . 58 LEU CB C 40.2 0.1 1 364 . 59 VAL H H 8.15 0.01 1 365 . 59 VAL HA H 3.61 0.01 1 366 . 59 VAL HB H 1.83 0.01 1 367 . 59 VAL HG1 H 0.95 0.01 2 368 . 59 VAL HG2 H 0.79 0.01 2 369 . 59 VAL N N 123.7 0.1 1 370 . 59 VAL CA C 58.3 0.1 1 371 . 59 VAL CB C 29.8 0.1 1 372 . 61 SER CA C 59.8 0.1 1 373 . 61 SER CB C 60.8 0.1 1 374 . 62 ASP H H 8.74 0.01 1 375 . 62 ASP HA H 4.50 0.01 1 376 . 62 ASP HB2 H 2.81 0.01 2 377 . 62 ASP HB3 H 2.66 0.01 2 378 . 62 ASP N N 118.4 0.1 1 379 . 62 ASP CA C 54.8 0.1 1 380 . 62 ASP CB C 37.4 0.1 1 381 . 63 LEU H H 7.24 0.01 1 382 . 63 LEU HA H 4.28 0.01 1 383 . 63 LEU HB2 H 1.70 0.01 2 384 . 63 LEU N N 122.0 0.1 1 385 . 63 LEU CA C 55.6 0.1 1 386 . 63 LEU CB C 39.6 0.1 1 387 . 64 THR H H 7.81 0.01 1 388 . 64 THR HA H 3.75 0.01 1 389 . 64 THR HB H 4.40 0.01 1 390 . 64 THR HG2 H 1.37 0.01 1 391 . 64 THR N N 116.3 0.1 1 392 . 64 THR CA C 56.8 0.1 1 393 . 64 THR CB C 65.5 0.1 1 394 . 65 ASN H H 8.33 0.01 1 395 . 65 ASN HA H 4.23 0.01 1 396 . 65 ASN HB2 H 2.83 0.01 2 397 . 65 ASN HB3 H 3.20 0.01 2 398 . 65 ASN HD21 H 6.74 0.01 2 399 . 65 ASN HD22 H 7.83 0.01 2 400 . 65 ASN N N 119.0 0.1 1 401 . 65 ASN ND2 N 113.7 0.1 1 402 . 65 ASN CA C 54.2 0.1 1 403 . 65 ASN CB C 35.2 0.1 1 404 . 66 GLU H H 7.64 0.01 1 405 . 66 GLU HA H 4.08 0.01 1 406 . 66 GLU N N 119.6 0.1 1 407 . 66 GLU CA C 57.4 0.1 1 408 . 66 GLU CB C 27.4 0.1 1 409 . 67 LEU H H 8.13 0.01 1 410 . 67 LEU HA H 3.91 0.01 1 411 . 67 LEU HB2 H 1.89 0.01 2 412 . 67 LEU N N 121.4 0.1 1 413 . 67 LEU CA C 56.5 0.1 1 414 . 67 LEU CB C 40.3 0.1 1 415 . 68 VAL H H 7.85 0.01 1 416 . 68 VAL HA H 3.07 0.01 1 417 . 68 VAL HB H 1.62 0.01 1 418 . 68 VAL HG1 H 0.49 0.01 2 419 . 68 VAL HG2 H -0.05 0.01 2 420 . 68 VAL N N 122.1 0.1 1 421 . 68 VAL CA C 65.3 0.1 1 422 . 68 VAL CB C 29.1 0.1 1 423 . 69 ASP H H 8.22 0.01 1 424 . 69 ASP HA H 4.29 0.01 1 425 . 69 ASP HB2 H 2.95 0.01 2 426 . 69 ASP HB3 H 2.72 0.01 2 427 . 69 ASP N N 120.7 0.1 1 428 . 69 ASP CA C 55.5 0.1 1 429 . 69 ASP CB C 39.4 0.1 1 430 . 70 ASP H H 7.80 0.01 1 431 . 70 ASP HA H 4.33 0.01 1 432 . 70 ASP HB2 H 2.59 0.01 2 433 . 70 ASP HB3 H 2.79 0.01 2 434 . 70 ASP N N 114.9 0.1 1 435 . 70 ASP CA C 54.9 0.1 1 436 . 70 ASP CB C 40.3 0.1 1 437 . 71 ARG H H 7.64 0.01 1 438 . 71 ARG HA H 4.27 0.01 1 439 . 71 ARG HB2 H 2.14 0.01 2 440 . 71 ARG HB3 H 1.89 0.01 2 441 . 71 ARG N N 121.5 0.1 1 442 . 71 ARG CA C 54.9 0.1 1 443 . 71 ARG CB C 26.5 0.1 1 444 . 72 LEU H H 8.09 0.01 1 445 . 72 LEU HA H 3.94 0.01 1 446 . 72 LEU HB2 H 1.67 0.01 1 447 . 72 LEU HB3 H 1.67 0.01 1 448 . 72 LEU HG H 1.65 0.01 1 449 . 72 LEU HD1 H 0.50 0.01 2 450 . 72 LEU HD2 H 0.17 0.01 2 451 . 72 LEU N N 118.9 0.1 1 452 . 72 LEU CA C 53.6 0.1 1 453 . 72 LEU CB C 38.1 0.1 1 454 . 73 ASN H H 7.48 0.01 1 455 . 73 ASN HA H 4.87 0.01 1 456 . 73 ASN HB2 H 3.04 0.01 1 457 . 73 ASN HB3 H 3.04 0.01 1 458 . 73 ASN HD21 H 7.02 0.01 2 459 . 73 ASN HD22 H 7.68 0.01 2 460 . 73 ASN N N 116.6 0.1 1 461 . 73 ASN ND2 N 113.6 0.1 1 462 . 73 ASN CA C 50.6 0.1 1 463 . 73 ASN CB C 36.5 0.1 1 464 . 74 ASN H H 7.50 0.01 1 465 . 74 ASN HA H 4.88 0.01 1 466 . 74 ASN HB2 H 3.07 0.01 2 467 . 74 ASN HB3 H 2.92 0.01 2 468 . 74 ASN HD21 H 7.05 0.01 2 469 . 74 ASN HD22 H 7.63 0.01 2 470 . 74 ASN N N 123.0 0.1 1 471 . 74 ASN ND2 N 114.2 0.1 1 472 . 74 ASN CA C 49.9 0.1 1 473 . 74 ASN CB C 37.2 0.1 1 474 . 75 PRO CA C 62.8 0.1 1 475 . 75 PRO CB C 29.9 0.1 1 476 . 76 ASP H H 8.99 0.01 1 477 . 76 ASP HA H 4.37 0.01 1 478 . 76 ASP HB2 H 2.93 0.01 2 479 . 76 ASP HB3 H 2.81 0.01 2 480 . 76 ASP N N 119.5 0.1 1 481 . 76 ASP CA C 53.7 0.1 1 482 . 76 ASP CB C 36.3 0.1 1 483 . 77 ALA H H 7.94 0.01 1 484 . 77 ALA HA H 5.02 0.01 1 485 . 77 ALA HB H 1.54 0.01 1 486 . 77 ALA N N 124.7 0.1 1 487 . 77 ALA CA C 49.4 0.1 1 488 . 77 ALA CB C 16.0 0.1 1 489 . 78 ALA H H 7.70 0.01 1 490 . 78 ALA HA H 4.19 0.01 1 491 . 78 ALA HB H 1.61 0.01 1 492 . 78 ALA N N 123.5 0.1 1 493 . 78 ALA CA C 53.3 0.1 1 494 . 78 ALA CB C 16.6 0.1 1 495 . 79 ASN H H 8.43 0.01 1 496 . 79 ASN HA H 5.09 0.01 1 497 . 79 ASN HB2 H 3.08 0.01 2 498 . 79 ASN HB3 H 2.78 0.01 2 499 . 79 ASN HD21 H 6.97 0.01 2 500 . 79 ASN HD22 H 7.71 0.01 2 501 . 79 ASN N N 113.4 0.1 1 502 . 79 ASN ND2 N 114.5 0.1 1 503 . 79 ASN CA C 50.3 0.1 1 504 . 79 ASN CB C 37.1 0.1 1 505 . 80 GLY H H 7.42 0.01 1 506 . 80 GLY HA2 H 4.83 0.01 2 507 . 80 GLY HA3 H 3.14 0.01 2 508 . 80 GLY N N 107.7 0.1 1 509 . 80 GLY CA C 42.4 0.1 1 510 . 81 PHE H H 8.23 0.01 1 511 . 81 PHE HA H 5.08 0.01 1 512 . 81 PHE HB2 H 2.90 0.01 2 513 . 81 PHE HB3 H 3.70 0.01 2 514 . 81 PHE HD1 H 7.14 0.01 1 515 . 81 PHE HD2 H 7.14 0.01 1 516 . 81 PHE HE1 H 7.25 0.01 1 517 . 81 PHE HE2 H 7.25 0.01 1 518 . 81 PHE HZ H 6.91 0.01 1 519 . 81 PHE N N 111.2 0.1 1 520 . 81 PHE CA C 55.0 0.1 1 521 . 81 PHE CB C 37.8 0.1 1 522 . 82 ILE H H 8.70 0.01 1 523 . 82 ILE HA H 5.15 0.01 1 524 . 82 ILE HB H 1.85 0.01 2 525 . 82 ILE N N 119.5 0.1 1 526 . 82 ILE CA C 57.5 0.1 1 527 . 82 ILE CB C 38.2 0.1 1 528 . 83 LEU H H 9.28 0.01 1 529 . 83 LEU HA H 5.50 0.01 1 530 . 83 LEU HB2 H 1.91 0.01 1 531 . 83 LEU HB3 H 1.91 0.01 1 532 . 83 LEU HG H 1.87 0.01 1 533 . 83 LEU HD1 H 0.91 0.01 2 534 . 83 LEU HD2 H 0.89 0.01 2 535 . 83 LEU N N 130.6 0.1 1 536 . 83 LEU CA C 52.3 0.1 1 537 . 83 LEU CB C 43.6 0.1 1 538 . 84 ASP H H 8.64 0.01 1 539 . 84 ASP HA H 5.26 0.01 1 540 . 84 ASP HB2 H 2.71 0.01 2 541 . 84 ASP HB3 H 2.50 0.01 2 542 . 84 ASP N N 122.7 0.1 1 543 . 84 ASP CA C 51.0 0.1 1 544 . 84 ASP CB C 42.4 0.1 1 545 . 85 GLY H H 8.93 0.01 1 546 . 85 GLY HA2 H 3.80 0.01 2 547 . 85 GLY HA3 H 4.71 0.01 2 548 . 85 GLY N N 113.8 0.1 1 549 . 85 GLY CA C 43.2 0.1 1 550 . 86 TYR H H 7.50 0.01 1 551 . 86 TYR HA H 4.36 0.01 1 552 . 86 TYR HB2 H 3.14 0.01 2 553 . 86 TYR HB3 H 2.47 0.01 2 554 . 86 TYR HD1 H 7.02 0.01 1 555 . 86 TYR HD2 H 7.02 0.01 1 556 . 86 TYR HE1 H 6.81 0.01 1 557 . 86 TYR HE2 H 6.81 0.01 1 558 . 86 TYR N N 121.7 0.1 1 559 . 86 TYR CA C 53.0 0.1 1 560 . 86 TYR CB C 40.2 0.1 1 561 . 87 PRO CA C 60.1 0.1 1 562 . 87 PRO CB C 33.5 0.1 1 563 . 88 ARG H H 8.83 0.01 1 564 . 88 ARG HA H 4.60 0.01 1 565 . 88 ARG HB2 H 1.82 0.01 2 566 . 88 ARG N N 116.3 0.1 1 567 . 88 ARG CA C 52.9 0.1 1 568 . 88 ARG CB C 28.7 0.1 1 569 . 89 SER H H 7.45 0.01 1 570 . 89 SER HA H 4.90 0.01 1 571 . 89 SER HB2 H 4.39 0.01 2 572 . 89 SER HB3 H 3.95 0.01 2 573 . 89 SER N N 112.2 0.1 1 574 . 89 SER CA C 53.2 0.1 1 575 . 89 SER CB C 64.7 0.1 1 576 . 90 VAL H H 9.53 0.01 1 577 . 90 VAL HA H 4.39 0.01 1 578 . 90 VAL HB H 1.99 0.01 1 579 . 90 VAL HG1 H 0.97 0.01 2 580 . 90 VAL HG2 H 0.88 0.01 2 581 . 90 VAL N N 124.4 0.1 1 582 . 90 VAL CA C 64.1 0.1 1 583 . 90 VAL CB C 28.8 0.1 1 584 . 91 GLU H H 8.61 0.01 1 585 . 91 GLU HA H 3.99 0.01 1 586 . 91 GLU HB2 H 2.12 0.01 2 587 . 91 GLU HB3 H 2.00 0.01 2 588 . 91 GLU N N 121.2 0.1 1 589 . 91 GLU CA C 58.6 0.1 1 590 . 91 GLU CB C 26.4 0.1 1 591 . 92 GLN H H 7.67 0.01 1 592 . 92 GLN HA H 4.20 0.01 1 593 . 92 GLN HB2 H 2.90 0.01 2 594 . 92 GLN HB3 H 2.54 0.01 2 595 . 92 GLN HE21 H 7.02 0.01 2 596 . 92 GLN HE22 H 7.35 0.01 2 597 . 92 GLN N N 120.2 0.1 1 598 . 92 GLN NE2 N 109.6 0.1 1 599 . 92 GLN CA C 56.5 0.1 1 600 . 92 GLN CB C 26.1 0.1 1 601 . 93 ALA H H 8.06 0.01 1 602 . 93 ALA HA H 3.88 0.01 1 603 . 93 ALA HB H 0.91 0.01 1 604 . 93 ALA N N 125.9 0.1 1 605 . 93 ALA CA C 53.2 0.1 1 606 . 93 ALA CB C 15.7 0.1 1 607 . 94 LYS H H 8.33 0.01 1 608 . 94 LYS HA H 4.17 0.01 1 609 . 94 LYS HB2 H 1.86 0.01 2 610 . 94 LYS HB3 H 1.98 0.01 2 611 . 94 LYS N N 120.6 0.1 1 612 . 94 LYS CA C 57.9 0.1 1 613 . 94 LYS CB C 30.2 0.1 1 614 . 95 ALA H H 7.71 0.01 1 615 . 95 ALA HA H 4.30 0.01 1 616 . 95 ALA HB H 1.59 0.01 1 617 . 95 ALA N N 124.6 0.1 1 618 . 95 ALA CA C 53.3 0.1 1 619 . 95 ALA CB C 16.8 0.1 1 620 . 96 LEU H H 9.01 0.01 1 621 . 96 LEU HA H 4.56 0.01 1 622 . 96 LEU N N 122.8 0.1 1 623 . 96 LEU CA C 55.4 0.1 1 624 . 96 LEU CB C 38.3 0.1 1 625 . 97 HIS H H 8.48 0.01 1 626 . 97 HIS N N 118.9 0.1 1 627 . 97 HIS CA C 57.8 0.1 1 628 . 97 HIS CB C 26.4 0.1 1 629 . 98 GLU H H 8.12 0.01 1 630 . 98 GLU HA H 4.30 0.01 1 631 . 98 GLU HB2 H 2.28 0.01 2 632 . 98 GLU N N 119.6 0.1 1 633 . 98 GLU CA C 57.6 0.1 1 634 . 98 GLU CB C 27.2 0.1 1 635 . 99 MET H H 8.36 0.01 1 636 . 99 MET HA H 4.10 0.01 1 637 . 99 MET HB2 H 2.09 0.01 2 638 . 99 MET HB3 H 1.92 0.01 2 639 . 99 MET N N 119.6 0.1 1 640 . 99 MET CA C 57.0 0.1 1 641 . 99 MET CB C 30.6 0.1 1 642 . 100 LEU H H 8.18 0.01 1 643 . 100 LEU HA H 4.17 0.01 2 644 . 100 LEU N N 120.3 0.1 1 645 . 100 LEU CA C 54.9 0.1 1 646 . 100 LEU CB C 37.7 0.1 1 647 . 101 GLU H H 8.94 0.01 1 648 . 101 GLU HA H 4.19 0.01 1 649 . 101 GLU HB2 H 2.11 0.01 1 650 . 101 GLU HB3 H 2.11 0.01 1 651 . 101 GLU HG2 H 2.27 0.01 2 652 . 101 GLU N N 126.0 0.1 1 653 . 101 GLU CA C 58.0 0.1 1 654 . 101 GLU CB C 27.0 0.1 1 655 . 102 ARG H H 7.90 0.01 1 656 . 102 ARG HA H 4.20 0.01 1 657 . 102 ARG HB2 H 1.96 0.01 1 658 . 102 ARG HB3 H 1.96 0.01 1 659 . 102 ARG N N 119.8 0.1 1 660 . 102 ARG CA C 57.0 0.1 1 661 . 102 ARG CB C 28.3 0.1 1 662 . 103 ARG H H 7.25 0.01 1 663 . 103 ARG HA H 4.50 0.01 1 664 . 103 ARG HB2 H 1.76 0.01 1 665 . 103 ARG HB3 H 1.76 0.01 1 666 . 103 ARG N N 117.5 0.1 1 667 . 103 ARG CA C 53.3 0.1 1 668 . 103 ARG CB C 28.9 0.1 1 669 . 104 GLY H H 8.11 0.01 1 670 . 104 GLY HA2 H 4.14 0.01 2 671 . 104 GLY HA3 H 4.04 0.01 2 672 . 104 GLY N N 109.8 0.1 1 673 . 104 GLY CA C 44.0 0.1 1 674 . 105 THR H H 8.06 0.01 1 675 . 105 THR HA H 4.85 0.01 1 676 . 105 THR HB H 4.00 0.01 1 677 . 105 THR HG2 H 1.08 0.01 1 678 . 105 THR N N 114.9 0.1 1 679 . 105 THR CA C 57.5 0.1 1 680 . 105 THR CB C 68.4 0.1 1 681 . 106 ASP H H 8.62 0.01 1 682 . 106 ASP HA H 4.82 0.01 1 683 . 106 ASP HB2 H 2.81 0.01 2 684 . 106 ASP HB3 H 2.67 0.01 2 685 . 106 ASP N N 117.7 0.1 1 686 . 106 ASP CA C 50.7 0.1 1 687 . 106 ASP CB C 40.7 0.1 1 688 . 107 ILE H H 9.27 0.01 1 689 . 107 ILE HA H 3.87 0.01 1 690 . 107 ILE N N 120.5 0.1 1 691 . 107 ILE CA C 57.3 0.1 1 692 . 107 ILE CB C 35.7 0.1 1 693 . 108 ASP H H 9.18 0.01 1 694 . 108 ASP HA H 4.86 0.01 1 695 . 108 ASP HB2 H 2.61 0.01 2 696 . 108 ASP HB3 H 2.75 0.01 2 697 . 108 ASP N N 125.0 0.1 1 698 . 108 ASP CA C 54.2 0.1 1 699 . 108 ASP CB C 41.8 0.1 1 700 . 109 ALA H H 7.58 0.01 1 701 . 109 ALA HA H 4.84 0.01 1 702 . 109 ALA HB H 1.29 0.01 1 703 . 109 ALA N N 118.7 0.1 1 704 . 109 ALA CA C 49.5 0.1 1 705 . 109 ALA CB C 20.5 0.1 1 706 . 110 VAL H H 7.98 0.01 1 707 . 110 VAL HA H 4.65 0.01 1 708 . 110 VAL HB H 1.68 0.01 1 709 . 110 VAL HG1 H 0.45 0.01 2 710 . 110 VAL HG2 H 0.60 0.01 2 711 . 110 VAL N N 122.8 0.1 1 712 . 110 VAL CA C 58.7 0.1 1 713 . 110 VAL CB C 31.5 0.1 1 714 . 111 LEU H H 8.97 0.01 1 715 . 111 LEU HA H 5.14 0.01 1 716 . 111 LEU HB2 H 1.86 0.01 1 717 . 111 LEU HB3 H 1.86 0.01 1 718 . 111 LEU HG H 1.04 0.01 1 719 . 111 LEU HD2 H 0.93 0.01 2 720 . 111 LEU N N 127.2 0.1 1 721 . 111 LEU CA C 50.8 0.1 1 722 . 111 LEU CB C 40.7 0.1 1 723 . 112 GLU H H 8.61 0.01 1 724 . 112 GLU HA H 4.94 0.01 1 725 . 112 GLU HB2 H 2.27 0.01 2 726 . 112 GLU N N 125.2 0.1 1 727 . 112 GLU CA C 52.0 0.1 1 728 . 112 GLU CB C 28.8 0.1 1 729 . 113 PHE H H 9.23 0.01 1 730 . 113 PHE HA H 4.85 0.01 1 731 . 113 PHE HB2 H 3.15 0.01 2 732 . 113 PHE HB3 H 2.75 0.01 2 733 . 113 PHE HD1 H 7.28 0.01 1 734 . 113 PHE HD2 H 7.28 0.01 1 735 . 113 PHE HE1 H 7.16 0.01 1 736 . 113 PHE HE2 H 7.16 0.01 1 737 . 113 PHE N N 130.0 0.1 1 738 . 113 PHE CA C 55.4 0.1 1 739 . 113 PHE CB C 36.1 0.1 1 740 . 114 ARG H H 8.87 0.01 1 741 . 114 ARG HA H 4.70 0.01 1 742 . 114 ARG N N 126.0 0.1 1 743 . 114 ARG CA C 53.3 0.1 1 744 . 114 ARG CB C 29.8 0.1 1 745 . 115 VAL H H 8.54 0.01 1 746 . 115 VAL HA H 4.37 0.01 1 747 . 115 VAL HB H 1.98 0.01 1 748 . 115 VAL HG1 H 0.99 0.01 1 749 . 115 VAL HG2 H 0.99 0.01 1 750 . 115 VAL N N 124.9 0.1 1 751 . 115 VAL CA C 58.3 0.1 1 752 . 115 VAL CB C 32.5 0.1 1 753 . 116 SER H H 7.46 0.01 1 754 . 116 SER HA H 4.47 0.01 1 755 . 116 SER HB2 H 4.08 0.01 2 756 . 116 SER HB3 H 3.96 0.01 2 757 . 116 SER N N 120.7 0.1 1 758 . 116 SER CA C 55.8 0.1 1 759 . 116 SER CB C 62.4 0.1 1 760 . 117 GLU H H 9.24 0.01 1 761 . 117 GLU HA H 4.34 0.01 1 762 . 117 GLU HB2 H 2.18 0.01 2 763 . 117 GLU HB3 H 2.08 0.01 2 764 . 117 GLU HG2 H 2.44 0.01 1 765 . 117 GLU HG3 H 2.44 0.01 1 766 . 117 GLU N N 124.2 0.1 1 767 . 117 GLU CA C 58.7 0.1 1 768 . 117 GLU CB C 27.5 0.1 1 769 . 118 GLU H H 8.99 0.01 1 770 . 118 GLU HA H 4.10 0.01 1 771 . 118 GLU HB2 H 2.10 0.01 2 772 . 118 GLU HB3 H 2.15 0.01 2 773 . 118 GLU HG2 H 2.44 0.01 1 774 . 118 GLU HG3 H 2.44 0.01 1 775 . 118 GLU N N 117.4 0.1 1 776 . 118 GLU CA C 58.0 0.1 1 777 . 118 GLU CB C 26.7 0.1 1 778 . 119 VAL H H 7.31 0.01 1 779 . 119 VAL HA H 3.88 0.01 1 780 . 119 VAL HB H 2.15 0.01 1 781 . 119 VAL HG1 H 1.10 0.01 2 782 . 119 VAL HG2 H 0.99 0.01 2 783 . 119 VAL N N 121.4 0.1 1 784 . 119 VAL CA C 63.4 0.1 1 785 . 119 VAL CB C 29.5 0.1 1 786 . 120 LEU H H 8.19 0.01 1 787 . 120 LEU HA H 3.95 0.01 1 788 . 120 LEU HB2 H 1.75 0.01 2 789 . 120 LEU N N 122.1 0.1 1 790 . 120 LEU CA C 56.1 0.1 1 791 . 120 LEU CB C 39.5 0.1 1 792 . 121 LEU H H 8.38 0.01 1 793 . 121 LEU HA H 4.03 0.01 1 794 . 121 LEU HB2 H 1.76 0.01 1 795 . 121 LEU HB3 H 1.76 0.01 1 796 . 121 LEU HG H 1.73 0.01 1 797 . 121 LEU HD1 H 1.00 0.01 2 798 . 121 LEU HD2 H 0.91 0.01 2 799 . 121 LEU N N 118.5 0.1 1 800 . 121 LEU CA C 56.5 0.1 1 801 . 121 LEU CB C 39.8 0.1 1 802 . 122 GLU H H 7.38 0.01 1 803 . 122 GLU HA H 4.08 0.01 1 804 . 122 GLU HB2 H 2.27 0.01 2 805 . 122 GLU HG2 H 2.37 0.01 2 806 . 122 GLU HG3 H 2.47 0.01 2 807 . 122 GLU N N 118.1 0.1 1 808 . 122 GLU CA C 57.2 0.1 1 809 . 122 GLU CB C 27.5 0.1 1 810 . 123 ARG H H 8.30 0.01 1 811 . 123 ARG HA H 4.19 0.01 1 812 . 123 ARG N N 119.4 0.1 1 813 . 123 ARG CA C 56.7 0.1 1 814 . 123 ARG CB C 28.6 0.1 1 815 . 124 LEU H H 8.42 0.01 1 816 . 124 LEU HA H 4.23 0.01 1 817 . 124 LEU N N 119.5 0.1 1 818 . 124 LEU CA C 54.8 0.1 1 819 . 124 LEU CB C 40.0 0.1 1 820 . 125 LYS H H 8.20 0.01 1 821 . 125 LYS HA H 4.21 0.01 1 822 . 125 LYS HB2 H 1.96 0.01 2 823 . 125 LYS N N 120.7 0.01 1 824 . 125 LYS CA C 56.6 0.1 1 825 . 125 LYS CB C 29.9 0.1 1 826 . 126 GLY H H 8.14 0.01 1 827 . 126 GLY HA2 H 4.04 0.01 2 828 . 126 GLY HA3 H 4.10 0.01 2 829 . 126 GLY N N 108.0 0.1 1 830 . 126 GLY CA C 43.6 0.1 1 831 . 127 ARG H H 7.74 0.01 1 832 . 127 ARG N N 120.0 0.1 1 833 . 127 ARG CA C 54.2 0.1 1 834 . 127 ARG CB C 28.6 0.1 1 835 . 128 GLY H H 8.03 0.01 1 836 . 128 GLY N N 109.0 0.1 1 837 . 128 GLY CA C 43.4 0.1 1 838 . 129 ARG H H 8.46 0.01 1 839 . 129 ARG N N 121.6 0.1 1 840 . 129 ARG CA C 53.8 0.1 1 841 . 129 ARG CB C 28.6 0.1 1 842 . 130 ALA H H 8.59 0.01 1 843 . 130 ALA HA H 4.33 0.01 1 844 . 130 ALA HB H 1.50 0.01 1 845 . 130 ALA N N 125.8 0.1 1 846 . 130 ALA CA C 51.6 0.1 1 847 . 130 ALA CB C 16.6 0.1 1 848 . 131 ASP H H 8.31 0.01 1 849 . 131 ASP HA H 4.70 0.01 1 850 . 131 ASP HB2 H 2.79 0.01 2 851 . 131 ASP N N 116.4 0.1 1 852 . 131 ASP CA C 51.7 0.1 1 853 . 131 ASP CB C 38.3 0.1 1 854 . 132 ASP H H 7.79 0.01 1 855 . 132 ASP HA H 4.85 0.01 1 856 . 132 ASP HB2 H 2.75 0.01 1 857 . 132 ASP HB3 H 2.75 0.01 1 858 . 132 ASP N N 121.5 0.1 1 859 . 132 ASP CA C 52.3 0.1 1 860 . 132 ASP CB C 39.0 0.1 1 861 . 133 THR H H 7.74 0.01 1 862 . 133 THR HA H 4.52 0.01 1 863 . 133 THR N N 112.0 0.1 1 864 . 133 THR CA C 58.9 0.1 1 865 . 133 THR CB C 68.4 0.1 1 866 . 134 ASP H H 8.78 0.01 1 867 . 134 ASP HA H 4.32 0.01 1 868 . 134 ASP HB2 H 2.75 0.01 1 869 . 134 ASP HB3 H 2.75 0.01 1 870 . 134 ASP N N 121.8 0.1 1 871 . 134 ASP CA C 55.5 0.1 1 872 . 134 ASP CB C 37.9 0.1 1 873 . 135 ASP H H 8.46 0.01 1 874 . 135 ASP HA H 4.41 0.01 1 875 . 135 ASP HB2 H 2.67 0.01 2 876 . 135 ASP HB3 H 2.77 0.01 2 877 . 135 ASP N N 116.9 0.1 1 878 . 135 ASP CA C 55.0 0.1 1 879 . 135 ASP CB C 38.2 0.1 1 880 . 136 VAL H H 7.55 0.01 1 881 . 136 VAL HA H 3.84 0.01 1 882 . 136 VAL HB H 2.33 0.01 1 883 . 136 VAL HG1 H 1.19 0.01 2 884 . 136 VAL HG2 H 1.08 0.01 2 885 . 136 VAL N N 121.7 0.1 1 886 . 136 VAL CA C 64.0 0.1 1 887 . 136 VAL CB C 29.9 0.1 1 888 . 137 ILE H H 8.00 0.01 1 889 . 137 ILE HA H 3.71 0.01 1 890 . 137 ILE N N 122.2 0.1 1 891 . 137 ILE CA C 62.9 0.1 1 892 . 137 ILE CB C 35.3 0.1 1 893 . 138 LEU H H 8.65 0.01 1 894 . 138 LEU HA H 4.20 0.01 1 895 . 138 LEU HB2 H 2.00 0.01 2 896 . 138 LEU HG H 1.63 0.01 1 897 . 138 LEU HD2 H 1.00 0.01 2 898 . 138 LEU N N 120.5 0.1 1 899 . 138 LEU CA C 56.2 0.1 1 900 . 138 LEU CB C 39.1 0.1 1 901 . 139 ASN H H 8.17 0.01 1 902 . 139 ASN HA H 4.65 0.01 1 903 . 139 ASN HB2 H 3.04 0.01 2 904 . 139 ASN HB3 H 2.96 0.01 2 905 . 139 ASN HD21 H 7.00 0.01 2 906 . 139 ASN HD22 H 7.78 0.01 2 907 . 139 ASN N N 119.5 0.1 1 908 . 139 ASN ND2 N 115.3 0.1 1 909 . 139 ASN CA C 54.7 0.1 1 910 . 139 ASN CB C 36.3 0.1 1 911 . 140 ARG H H 8.17 0.01 1 912 . 140 ARG HA H 4.19 0.01 1 913 . 140 ARG N N 120.7 0.1 1 914 . 140 ARG CA C 57.4 0.1 1 915 . 140 ARG CB C 27.7 0.1 1 916 . 141 MET H H 8.24 0.01 1 917 . 141 MET HA H 4.38 0.01 1 918 . 141 MET HB2 H 2.39 0.01 2 919 . 141 MET N N 120.4 0.1 1 920 . 141 MET CA C 56.9 0.1 1 921 . 141 MET CB C 30.5 0.1 1 922 . 142 LYS H H 7.95 0.01 1 923 . 142 LYS HA H 4.13 0.01 1 924 . 142 LYS HB2 H 2.20 0.01 1 925 . 142 LYS HB3 H 2.20 0.01 1 926 . 142 LYS N N 122.7 0.1 1 927 . 142 LYS CA C 58.0 0.1 1 928 . 142 LYS CB C 29.8 0.1 1 929 . 143 VAL H H 8.07 0.01 1 930 . 143 VAL HA H 3.90 0.01 1 931 . 143 VAL HB H 2.24 0.01 1 932 . 143 VAL HG1 H 1.21 0.01 2 933 . 143 VAL HG2 H 1.10 0.01 2 934 . 143 VAL N N 119.7 0.1 1 935 . 143 VAL CA C 64.4 0.1 1 936 . 143 VAL CB C 29.5 0.1 1 937 . 144 TYR H H 7.87 0.01 1 938 . 144 TYR HA H 4.42 0.01 1 939 . 144 TYR HB2 H 3.34 0.01 1 940 . 144 TYR HB3 H 3.34 0.01 1 941 . 144 TYR HD1 H 7.23 0.01 1 942 . 144 TYR HD2 H 7.23 0.01 1 943 . 144 TYR HE1 H 6.86 0.01 1 944 . 144 TYR HE2 H 6.86 0.01 1 945 . 144 TYR N N 119.7 0.1 1 946 . 144 TYR CA C 59.4 0.1 1 947 . 144 TYR CB C 35.7 0.1 1 948 . 145 ARG H H 8.40 0.01 1 949 . 145 ARG HA H 3.78 0.01 1 950 . 145 ARG HB2 H 2.25 0.01 2 951 . 145 ARG HB3 H 2.11 0.01 2 952 . 145 ARG HG2 H 1.81 0.01 2 953 . 145 ARG N N 122.7 0.1 1 954 . 145 ARG CA C 57.9 0.1 1 955 . 145 ARG CB C 27.8 0.1 1 956 . 146 ASP H H 8.49 0.01 1 957 . 146 ASP HA H 4.53 0.01 1 958 . 146 ASP HB2 H 2.94 0.01 2 959 . 146 ASP HB3 H 2.77 0.01 2 960 . 146 ASP N N 120.7 0.1 1 961 . 146 ASP CA C 55.0 0.1 1 962 . 146 ASP CB C 38.2 0.1 1 963 . 147 GLU H H 8.50 0.01 1 964 . 147 GLU HA H 4.23 0.01 1 965 . 147 GLU HB2 H 2.14 0.01 2 966 . 147 GLU HB3 H 2.24 0.01 2 967 . 147 GLU HG2 H 2.59 0.01 2 968 . 147 GLU N N 118.6 0.1 1 969 . 147 GLU CA C 56.4 0.1 1 970 . 147 GLU CB C 28.2 0.1 1 971 . 148 THR H H 7.87 0.01 1 972 . 148 THR HA H 3.77 0.01 1 973 . 148 THR HB H 4.08 0.01 1 974 . 148 THR N N 113.1 0.1 1 975 . 148 THR CA C 62.5 0.1 1 976 . 148 THR CB C 67.1 0.1 1 977 . 149 ALA H H 7.86 0.01 1 978 . 149 ALA HA H 4.25 0.01 1 979 . 149 ALA HB H 1.65 0.01 1 980 . 149 ALA N N 127.0 0.1 1 981 . 149 ALA CA C 55.2 0.1 1 982 . 150 PRO CA C 63.4 0.1 1 983 . 150 PRO CB C 29.4 0.1 1 984 . 151 LEU H H 7.45 0.01 1 985 . 151 LEU HA H 4.10 0.01 1 986 . 151 LEU N N 118.9 0.1 1 987 . 151 LEU CA C 55.3 0.1 1 988 . 151 LEU CB C 39.9 0.1 1 989 . 152 LEU H H 7.94 0.01 1 990 . 152 LEU HA H 3.99 0.01 1 991 . 152 LEU N N 119.0 0.1 1 992 . 152 LEU CA C 55.8 0.1 1 993 . 152 LEU CB C 37.6 0.1 1 994 . 153 GLU H H 7.13 0.01 1 995 . 153 GLU HA H 4.18 0.01 1 996 . 153 GLU HB2 H 2.11 0.01 2 997 . 153 GLU N N 115.7 0.1 1 998 . 153 GLU CA C 56.6 0.1 1 999 . 153 GLU CB C 27.7 0.1 1 1000 . 154 TYR H H 7.89 0.01 1 1001 . 154 TYR HA H 3.92 0.01 1 1002 . 154 TYR HB2 H 3.02 0.01 2 1003 . 154 TYR HB3 H 2.74 0.01 2 1004 . 154 TYR HD1 H 6.02 0.01 1 1005 . 154 TYR HD2 H 6.02 0.01 1 1006 . 154 TYR HE1 H 6.45 0.01 1 1007 . 154 TYR HE2 H 6.45 0.01 1 1008 . 154 TYR N N 122.8 0.1 1 1009 . 154 TYR CA C 60.2 0.1 1 1010 . 154 TYR CB C 36.5 0.1 1 1011 . 155 TYR H H 8.05 0.01 1 1012 . 155 TYR HA H 4.91 0.01 1 1013 . 155 TYR HB2 H 2.63 0.01 2 1014 . 155 TYR HB3 H 2.61 0.01 2 1015 . 155 TYR HD1 H 7.25 0.01 1 1016 . 155 TYR HD2 H 7.25 0.01 1 1017 . 155 TYR HE1 H 6.73 0.01 1 1018 . 155 TYR HE2 H 6.73 0.01 1 1019 . 155 TYR N N 115.4 0.1 1 1020 . 155 TYR CA C 56.0 0.1 1 1021 . 155 TYR CB C 35.5 0.1 1 1022 . 156 ARG H H 7.02 0.01 1 1023 . 156 ARG HA H 4.02 0.01 1 1024 . 156 ARG HB2 H 2.20 0.01 2 1025 . 156 ARG HB3 H 1.94 0.01 2 1026 . 156 ARG HG2 H 1.74 0.01 1 1027 . 156 ARG HG3 H 1.74 0.01 1 1028 . 156 ARG HD2 H 3.32 0.01 1 1029 . 156 ARG HD3 H 3.32 0.01 1 1030 . 156 ARG N N 120.5 0.1 1 1031 . 156 ARG CA C 58.4 0.1 1 1032 . 156 ARG CB C 30.0 0.1 1 1033 . 157 ASP H H 8.73 0.01 1 1034 . 157 ASP HA H 4.63 0.01 1 1035 . 157 ASP HB2 H 2.59 0.01 2 1036 . 157 ASP HB3 H 2.79 0.01 2 1037 . 157 ASP N N 117.5 0.1 1 1038 . 157 ASP CA C 54.6 0.1 1 1039 . 157 ASP CB C 37.8 0.1 1 1040 . 158 GLN H H 8.06 0.01 1 1041 . 158 GLN HA H 4.60 0.01 1 1042 . 158 GLN HB2 H 2.10 0.01 2 1043 . 158 GLN HB3 H 2.25 0.01 2 1044 . 158 GLN HG2 H 2.43 0.01 2 1045 . 158 GLN HE21 H 6.64 0.01 2 1046 . 158 GLN HE22 H 7.45 0.01 2 1047 . 158 GLN N N 117.9 0.1 1 1048 . 158 GLN NE2 N 110.3 0.1 1 1049 . 158 GLN CA C 54.5 0.1 1 1050 . 158 GLN CB C 27.8 0.1 1 1051 . 159 LEU H H 7.35 0.01 1 1052 . 159 LEU HA H 4.80 0.01 1 1053 . 159 LEU HB2 H 1.89 0.01 1 1054 . 159 LEU HB3 H 1.89 0.01 1 1055 . 159 LEU HG H 1.63 0.01 1 1056 . 159 LEU HD1 H 0.96 0.01 1 1057 . 159 LEU HD2 H 0.96 0.01 1 1058 . 159 LEU N N 124.3 0.1 1 1059 . 159 LEU CA C 54.1 0.1 1 1060 . 159 LEU CB C 41.6 0.1 1 1061 . 160 LYS H H 9.39 0.01 1 1062 . 160 LYS HA H 4.80 0.01 1 1063 . 160 LYS N N 127.3 0.1 1 1064 . 160 LYS CA C 51.9 0.1 1 1065 . 160 LYS CB C 32.7 0.1 1 1066 . 161 THR H H 8.55 0.01 1 1067 . 161 THR HA H 4.82 0.01 1 1068 . 161 THR HB H 3.95 0.01 1 1069 . 161 THR HG2 H 1.21 0.01 1 1070 . 161 THR N N 118.9 0.1 1 1071 . 161 THR CA C 60.5 0.1 1 1072 . 161 THR CB C 67.7 0.1 1 1073 . 162 VAL H H 9.12 0.01 1 1074 . 162 VAL HA H 4.06 0.01 1 1075 . 162 VAL HB H 1.50 0.01 1 1076 . 162 VAL HG1 H 0.56 0.01 2 1077 . 162 VAL N N 127.2 0.1 1 1078 . 162 VAL CA C 58.4 0.1 1 1079 . 162 VAL CB C 32.4 0.1 1 1080 . 163 ASP H H 8.56 0.01 1 1081 . 163 ASP HA H 4.64 0.01 1 1082 . 163 ASP HB2 H 2.70 0.01 2 1083 . 163 ASP HB3 H 2.79 0.01 2 1084 . 163 ASP N N 127.5 0.1 1 1085 . 163 ASP CA C 52.1 0.1 1 1086 . 163 ASP CB C 37.8 0.1 1 1087 . 164 ALA H H 8.73 0.01 1 1088 . 164 ALA HA H 4.71 0.01 1 1089 . 164 ALA HB H 1.50 0.01 1 1090 . 164 ALA N N 131.6 0.1 1 1091 . 164 ALA CA C 48.5 0.1 1 1092 . 164 ALA CB C 16.4 0.1 1 1093 . 165 VAL H H 8.11 0.01 1 1094 . 165 VAL HA H 4.06 0.01 1 1095 . 165 VAL HB H 2.46 0.01 1 1096 . 165 VAL HG1 H 1.19 0.01 2 1097 . 165 VAL N N 121.8 0.1 1 1098 . 165 VAL CA C 61.2 0.1 1 1099 . 165 VAL CB C 29.0 0.1 1 1100 . 166 GLY H H 7.86 0.01 1 1101 . 166 GLY HA2 H 4.09 0.01 2 1102 . 166 GLY HA3 H 4.40 0.01 2 1103 . 166 GLY N N 115.7 0.1 1 1104 . 166 GLY CA C 42.0 0.1 1 1105 . 167 THR H H 9.03 0.01 1 1106 . 167 THR HA H 4.53 0.01 1 1107 . 167 THR N N 112.4 0.1 1 1108 . 167 THR CA C 59.3 0.1 1 1109 . 167 THR CB C 68.5 0.1 1 1110 . 168 MET H H 9.05 0.01 1 1111 . 168 MET N N 120.2 0.1 1 1112 . 168 MET CA C 57.0 0.1 1 1113 . 168 MET CB C 30.7 0.1 1 1114 . 169 ASP H H 8.26 0.01 1 1115 . 169 ASP HA H 4.71 0.01 1 1116 . 169 ASP HB2 H 2.61 0.01 2 1117 . 169 ASP HB3 H 2.79 0.01 2 1118 . 169 ASP N N 118.2 0.1 1 1119 . 169 ASP CA C 55.4 0.1 1 1120 . 169 ASP CB C 38.6 0.1 1 1121 . 170 GLU H H 7.89 0.01 1 1122 . 170 GLU HA H 4.17 0.01 1 1123 . 170 GLU N N 124.0 0.1 1 1124 . 170 GLU CA C 57.2 0.1 1 1125 . 170 GLU CB C 27.7 0.1 1 1126 . 171 VAL H H 8.47 0.01 1 1127 . 171 VAL HA H 3.45 0.01 1 1128 . 171 VAL HB H 2.07 0.01 1 1129 . 171 VAL HG1 H 0.95 0.01 1 1130 . 171 VAL HG2 H 0.95 0.01 1 1131 . 171 VAL N N 120.7 0.1 1 1132 . 171 VAL CA C 65.2 0.1 1 1133 . 171 VAL CB C 29.6 0.1 1 1134 . 172 PHE H H 8.15 0.01 1 1135 . 172 PHE HA H 4.65 0.01 1 1136 . 172 PHE HB2 H 3.18 0.01 1 1137 . 172 PHE HB3 H 3.18 0.01 1 1138 . 172 PHE HD1 H 7.51 0.01 1 1139 . 172 PHE HD2 H 7.51 0.01 1 1140 . 172 PHE HE1 H 7.21 0.01 1 1141 . 172 PHE HE2 H 7.21 0.01 1 1142 . 172 PHE HZ H 7.08 0.01 1 1143 . 172 PHE N N 121.9 0.1 1 1144 . 172 PHE CA C 58.5 0.1 1 1145 . 172 PHE CB C 37.3 0.1 1 1146 . 173 ALA H H 7.71 0.01 1 1147 . 173 ALA HA H 3.90 0.01 1 1148 . 173 ALA HB H 1.60 0.01 1 1149 . 173 ALA N N 119.9 0.1 1 1150 . 173 ALA CA C 53.0 0.1 1 1151 . 173 ALA CB C 15.5 0.1 1 1152 . 174 ARG H H 7.84 0.01 1 1153 . 174 ARG HA H 4.01 0.01 1 1154 . 174 ARG HB2 H 2.10 0.01 2 1155 . 174 ARG HB3 H 2.00 0.01 2 1156 . 174 ARG HG2 H 1.82 0.01 1 1157 . 174 ARG HG3 H 1.82 0.01 1 1158 . 174 ARG HD2 H 3.21 0.01 1 1159 . 174 ARG HD3 H 3.21 0.01 1 1160 . 174 ARG N N 118.1 0.1 1 1161 . 174 ARG CA C 57.4 0.1 1 1162 . 174 ARG CB C 28.8 0.1 1 1163 . 175 ALA H H 8.77 0.01 1 1164 . 175 ALA HA H 3.91 0.01 1 1165 . 175 ALA HB H 1.55 0.01 1 1166 . 175 ALA N N 126.0 0.1 1 1167 . 175 ALA CA C 52.9 0.1 1 1168 . 175 ALA CB C 15.5 0.1 1 1169 . 176 LEU H H 8.24 0.01 1 1170 . 176 LEU HA H 3.73 0.01 1 1171 . 176 LEU HB2 H 1.53 0.01 1 1172 . 176 LEU HB3 H 1.53 0.01 1 1173 . 176 LEU HG H 1.28 0.01 1 1174 . 176 LEU HD1 H 0.59 0.01 2 1175 . 176 LEU HD2 H 0.49 0.01 2 1176 . 176 LEU N N 117.2 0.1 1 1177 . 176 LEU CA C 55.9 0.1 1 1178 . 176 LEU CB C 38.8 0.1 1 1179 . 177 ARG H H 7.84 0.01 1 1180 . 177 ARG HA H 4.24 0.01 1 1181 . 177 ARG HB2 H 1.97 0.01 2 1182 . 177 ARG HG2 H 1.82 0.01 2 1183 . 177 ARG N N 118.6 0.1 1 1184 . 177 ARG CA C 57.0 0.1 1 1185 . 177 ARG CB C 27.7 0.1 1 1186 . 178 ALA H H 7.95 0.01 1 1187 . 178 ALA HA H 4.17 0.01 1 1188 . 178 ALA HB H 1.43 0.01 1 1189 . 178 ALA N N 123.8 0.1 1 1190 . 178 ALA CA C 52.5 0.1 1 1191 . 178 ALA CB C 16.0 0.1 1 1192 . 179 LEU H H 7.40 0.01 1 1193 . 179 LEU HA H 4.23 0.01 1 1194 . 179 LEU HB2 H 2.02 0.01 2 1195 . 179 LEU HB3 H 1.90 0.01 2 1196 . 179 LEU HG H 1.62 0.01 1 1197 . 179 LEU HD1 H 0.87 0.01 2 1198 . 179 LEU HD2 H 0.76 0.01 2 1199 . 179 LEU N N 115.4 0.1 1 1200 . 179 LEU CA C 52.4 0.1 1 1201 . 179 LEU CB C 40.3 0.1 1 1202 . 180 GLY H H 7.95 0.01 1 1203 . 180 GLY HA2 H 3.92 0.01 2 1204 . 180 GLY HA3 H 4.11 0.01 2 1205 . 180 GLY N N 108.4 0.1 1 1206 . 180 GLY CA C 43.6 0.1 1 1207 . 181 LYS H H 7.81 0.01 1 1208 . 181 LYS HA H 4.36 0.01 1 1209 . 181 LYS HB2 H 1.96 0.01 2 1210 . 181 LYS HB3 H 1.57 0.01 2 1211 . 181 LYS N N 126.4 0.1 1 1212 . 181 LYS CA C 52.7 0.1 1 1213 . 181 LYS CB C 31.6 0.1 1 stop_ save_