data_4152 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Backbone Resonance Assignment of Escherichia coli Adenylate Kinase, a 23.6 kDa Protein ; _BMRB_accession_number 4152 _BMRB_flat_file_name bmr4152.str _Entry_type original _Submission_date 1998-06-22 _Accession_date 1998-06-22 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; We report the proton, nitrogen-15 and carbon-13 resonance assignments for the E.coli adenylate kinase, a 214 residue protein. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burlacu-Miron Simona . . 2 Perrier Veronique . . 3 Gilles Anne-Marie . . 4 Mispelter Joel . . 5 Barzu Octavian . . 6 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" 763 "13C chemical shifts" 381 "15N chemical shifts" 200 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-02 original author . stop_ _Original_release_date 2000-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C and 15N Backbone Resonance Assignment of Escherichia coli Adenylate Kinase, a 23.6 kDa Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99169957 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burlacu-Miron Simona . . 2 Perrier Veronique . . 3 Gilles Anne-Marie . . 4 Mispelter Joel . . 5 Barzu Octavian . . 6 Craescu Constantin T. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 13 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 93 _Page_last 94 _Year 1999 _Details . loop_ _Keyword 'Adenylate Kinase' AKe NMPkinase NMR 'nuclear magnetic resonance' protein 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_AKe _Saveframe_category molecular_system _Mol_system_name 'Adenylate kinase from E. coli' _Abbreviation_common AKe _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AKe $AKe stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AKe _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Adenylate kinase' _Abbreviation_common AKe _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 214 _Mol_residue_sequence ; MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDAGKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDRI VGRRVHAPSGRVYHVKFNPP KVEGKDDVTGEELTTRKDDQ EETVRKRLVEYHQMTAPLIG YYSKEAEAGNTKYAKVDGTK PVAEVRADLEKILG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ARG 3 3 ILE 4 4 ILE 5 5 LEU 6 6 LEU 7 7 GLY 8 8 ALA 9 9 PRO 10 10 GLY 11 11 ALA 12 12 GLY 13 13 LYS 14 14 GLY 15 15 THR 16 16 GLN 17 17 ALA 18 18 GLN 19 19 PHE 20 20 ILE 21 21 MET 22 22 GLU 23 23 LYS 24 24 TYR 25 25 GLY 26 26 ILE 27 27 PRO 28 28 GLN 29 29 ILE 30 30 SER 31 31 THR 32 32 GLY 33 33 ASP 34 34 MET 35 35 LEU 36 36 ARG 37 37 ALA 38 38 ALA 39 39 VAL 40 40 LYS 41 41 SER 42 42 GLY 43 43 SER 44 44 GLU 45 45 LEU 46 46 GLY 47 47 LYS 48 48 GLN 49 49 ALA 50 50 LYS 51 51 ASP 52 52 ILE 53 53 MET 54 54 ASP 55 55 ALA 56 56 GLY 57 57 LYS 58 58 LEU 59 59 VAL 60 60 THR 61 61 ASP 62 62 GLU 63 63 LEU 64 64 VAL 65 65 ILE 66 66 ALA 67 67 LEU 68 68 VAL 69 69 LYS 70 70 GLU 71 71 ARG 72 72 ILE 73 73 ALA 74 74 GLN 75 75 GLU 76 76 ASP 77 77 CYS 78 78 ARG 79 79 ASN 80 80 GLY 81 81 PHE 82 82 LEU 83 83 LEU 84 84 ASP 85 85 GLY 86 86 PHE 87 87 PRO 88 88 ARG 89 89 THR 90 90 ILE 91 91 PRO 92 92 GLN 93 93 ALA 94 94 ASP 95 95 ALA 96 96 MET 97 97 LYS 98 98 GLU 99 99 ALA 100 100 GLY 101 101 ILE 102 102 ASN 103 103 VAL 104 104 ASP 105 105 TYR 106 106 VAL 107 107 LEU 108 108 GLU 109 109 PHE 110 110 ASP 111 111 VAL 112 112 PRO 113 113 ASP 114 114 GLU 115 115 LEU 116 116 ILE 117 117 VAL 118 118 ASP 119 119 ARG 120 120 ILE 121 121 VAL 122 122 GLY 123 123 ARG 124 124 ARG 125 125 VAL 126 126 HIS 127 127 ALA 128 128 PRO 129 129 SER 130 130 GLY 131 131 ARG 132 132 VAL 133 133 TYR 134 134 HIS 135 135 VAL 136 136 LYS 137 137 PHE 138 138 ASN 139 139 PRO 140 140 PRO 141 141 LYS 142 142 VAL 143 143 GLU 144 144 GLY 145 145 LYS 146 146 ASP 147 147 ASP 148 148 VAL 149 149 THR 150 150 GLY 151 151 GLU 152 152 GLU 153 153 LEU 154 154 THR 155 155 THR 156 156 ARG 157 157 LYS 158 158 ASP 159 159 ASP 160 160 GLN 161 161 GLU 162 162 GLU 163 163 THR 164 164 VAL 165 165 ARG 166 166 LYS 167 167 ARG 168 168 LEU 169 169 VAL 170 170 GLU 171 171 TYR 172 172 HIS 173 173 GLN 174 174 MET 175 175 THR 176 176 ALA 177 177 PRO 178 178 LEU 179 179 ILE 180 180 GLY 181 181 TYR 182 182 TYR 183 183 SER 184 184 LYS 185 185 GLU 186 186 ALA 187 187 GLU 188 188 ALA 189 189 GLY 190 190 ASN 191 191 THR 192 192 LYS 193 193 TYR 194 194 ALA 195 195 LYS 196 196 VAL 197 197 ASP 198 198 GLY 199 199 THR 200 200 LYS 201 201 PRO 202 202 VAL 203 203 ALA 204 204 GLU 205 205 VAL 206 206 ARG 207 207 ALA 208 208 ASP 209 209 LEU 210 210 GLU 211 211 LYS 212 212 ILE 213 213 LEU 214 214 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 18683 adenylate_kinase 100.00 214 100.00 100.00 1.81e-151 BMRB 18685 adenylate_kinase 100.00 214 100.00 100.00 1.81e-151 BMRB 18686 adenylate_kinase 100.00 214 99.53 99.53 1.24e-150 BMRB 18687 adenylate_kinase 100.00 214 100.00 100.00 1.81e-151 BMRB 19089 adenylate_kinase_wild_type 100.00 214 100.00 100.00 1.81e-151 BMRB 19090 adenylate_kinase_wild_type 100.00 214 100.00 100.00 1.81e-151 BMRB 19091 adenylate_kinase_wild_type 100.00 214 100.00 100.00 1.81e-151 BMRB 19092 adenylate_kinase_R156K_mutant 100.00 214 99.53 100.00 4.73e-151 BMRB 19093 adenylate_kinase_R156K_mutant 100.00 214 99.53 100.00 4.73e-151 BMRB 25353 Kinase 100.00 214 99.53 99.53 1.78e-150 BMRB 25357 Adenylate_Kinase_Y171W 100.00 214 99.53 100.00 3.22e-151 BMRB 25360 Adenylate_Kinase_P177A 100.00 214 99.53 99.53 1.78e-150 BMRB 25361 Adenylate_Kinase_Y171W 100.00 214 99.53 100.00 3.22e-151 BMRB 25362 Adenylate_Kinase_Y171W 100.00 214 99.53 100.00 3.22e-151 BMRB 4193 "Adenylate kinase" 100.00 214 100.00 100.00 1.81e-151 BMRB 4350 "Adenylate kinase from E. coli" 100.00 214 100.00 100.00 1.81e-151 PDB 1AKE "Structure Of The Complex Between Adenylate Kinase From Escherichia Coli And The Inhibitor Ap5a Refined At 1.9 Angstroms Resolut" 100.00 214 100.00 100.00 1.81e-151 PDB 1ANK "The Closed Conformation Of A Highly Flexible Protein: The Structure Of E. Cloi Adenylate Kinase With Bound Amp And Amppnp" 100.00 214 100.00 100.00 1.81e-151 PDB 1E4V "Mutant G10v Of Adenylate Kinase From E. Coli, Modified In The Gly-Loop" 100.00 214 99.53 99.53 2.66e-150 PDB 1E4Y "Mutant P9l Of Adenylate Kinase From E. Coli, Modified In The Gly-Loop" 100.00 214 99.07 99.07 4.57e-149 PDB 2ECK "Structure Of Phosphotransferase" 100.00 214 100.00 100.00 1.81e-151 PDB 3HPQ "Crystal Structure Of Wild-Type Adenylate Kinase From E. Coli, In Complex With Ap5a" 100.00 214 100.00 100.00 1.81e-151 PDB 3HPR "Crystal Structure Of V148g Adenylate Kinase From E. Coli, In Complex With Ap5a" 100.00 214 99.53 99.53 2.52e-150 PDB 3X2S "Crystal Structure Of Pyrene-conjugated Adenylate Kinase" 100.00 214 98.60 98.60 7.65e-149 PDB 4AKE "Adenylate Kinase" 100.00 214 100.00 100.00 1.81e-151 PDB 4JZK "Crystal Structure Of Adenylate Kinase Of E. Coli With Adp/amp Bound" 100.00 214 100.00 100.00 1.81e-151 PDB 4X8H "Crystal Structure Of E. Coli Adenylate Kinase P177a Mutant" 100.00 214 99.53 99.53 1.78e-150 PDB 4X8L "Crystal Structure Of E. Coli Adenylate Kinase P177a Mutant In Complex With Inhibitor Ap5a" 100.00 214 99.53 99.53 1.78e-150 PDB 4X8M "Crystal Structure Of E. Coli Adenylate Kinase Y171w Mutant" 100.00 214 99.53 100.00 3.22e-151 PDB 4X8O "Crystal Structure Of E. Coli Adenylate Kinase Y171w Mutant In Complex With Inhibitor Ap5a" 100.00 214 99.53 100.00 3.22e-151 DBJ BAA14303 "adenylate kinase [Escherichia coli K-12]" 50.00 107 100.00 100.00 1.11e-68 DBJ BAB33950 "adenylate kinase [Escherichia coli O157:H7 str. Sakai]" 100.00 214 100.00 100.00 1.81e-151 DBJ BAE76253 "adenylate kinase [Escherichia coli str. K12 substr. W3110]" 100.00 214 100.00 100.00 1.81e-151 DBJ BAG76023 "adenylate kinase [Escherichia coli SE11]" 100.00 214 100.00 100.00 1.81e-151 DBJ BAI23848 "adenylate kinase Adk [Escherichia coli O26:H11 str. 11368]" 100.00 214 100.00 100.00 1.81e-151 EMBL CAA26840 "unnamed protein product [Escherichia coli]" 100.00 214 100.00 100.00 1.81e-151 EMBL CAF33430 "adenylate kinase [Escherichia coli]" 71.96 154 100.00 100.00 3.83e-106 EMBL CAF33431 "adenylate kinase, partial [Escherichia coli]" 71.96 154 100.00 100.00 3.83e-106 EMBL CAF33432 "adenylate kinase, partial [Escherichia coli]" 71.96 154 100.00 100.00 3.83e-106 EMBL CAF33433 "adenylate kinase, partial [Escherichia coli]" 71.96 154 100.00 100.00 3.83e-106 GB AAA23461 "adk ORF [Escherichia coli]" 100.00 214 100.00 100.00 1.81e-151 GB AAB40228 "adenylate kinase [Escherichia coli]" 100.00 233 100.00 100.00 6.11e-152 GB AAC73576 "adenylate kinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 214 100.00 100.00 1.81e-151 GB AAG54823 "adenylate kinase activity; pleiotropic effects on glycerol-3-phosphate acyltransferase activity [Escherichia coli O157:H7 str. " 100.00 214 100.00 100.00 1.81e-151 GB AAM94352 "adenylate kinase [Escherichia coli]" 79.91 171 100.00 100.00 1.29e-119 REF NP_308554 "adenylate kinase [Escherichia coli O157:H7 str. Sakai]" 100.00 214 100.00 100.00 1.81e-151 REF NP_415007 "adenylate kinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 214 100.00 100.00 1.81e-151 REF NP_706367 "adenylate kinase [Shigella flexneri 2a str. 301]" 100.00 214 99.53 99.53 1.68e-150 REF WP_001220233 "MULTISPECIES: adenylate kinase [Proteobacteria]" 100.00 214 100.00 100.00 1.81e-151 REF WP_001220235 "adenylate kinase [Shigella flexneri]" 100.00 214 99.53 99.53 1.68e-150 SP A7ZIN4 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 214 100.00 100.00 1.81e-151 SP A7ZXD2 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 214 100.00 100.00 1.81e-151 SP B1IZC0 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 214 100.00 100.00 1.81e-151 SP B1LJN2 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 214 100.00 100.00 1.81e-151 SP B1XFR1 "RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A" 100.00 214 100.00 100.00 1.81e-151 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AKe 'E. coli' 562 Eubacteria . Escherichia coli 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 $AKe 'recombinant technology' 'E. coli' Escherichia coli HfrP4x8 Plasmid 'pIPD37(derived from pBR322)' 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 $AKe 1.2 mM . H2O 93 % . D2O 7 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AKe 1.0 mM [U-15N] H2O 93 % . D2O 7 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AKe 1.0 mM '[U-13C; U15-N]' H2O 93 % . D2O 7 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _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 6.7 . 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 TMS C 13 'methyl carbon' ppm 67.8 external indirect . . . H2O H 1 proton ppm 4.68 internal direct . . . 'liquid ammonia' N 15 nitrogen ppm 0.0 external . . . . 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_chemical_shifts_one _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 AKe _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 9.69 0.01 1 2 . 2 ARG HA H 4.76 0.01 1 3 . 2 ARG N N 127.0 0.1 1 4 . 2 ARG CA C 52.2 0.1 1 5 . 2 ARG CB C 29.9 0.1 1 6 . 3 ILE H H 8.61 0.01 1 7 . 3 ILE HA H 5.36 0.01 1 8 . 3 ILE HB H 1.56 0.01 1 9 . 3 ILE N N 124.8 0.1 1 10 . 3 ILE CA C 57.0 0.1 1 11 . 3 ILE CB C 42.1 0.1 1 12 . 4 ILE H H 8.67 0.01 1 13 . 4 ILE HA H 4.68 0.01 1 14 . 4 ILE HB H 1.72 0.01 1 15 . 4 ILE HG2 H 1.57 0.01 1 16 . 4 ILE HD1 H 0.88 0.01 1 17 . 4 ILE HG13 H 0.97 0.01 2 18 . 4 ILE N N 126.1 0.1 1 19 . 4 ILE CA C 59.0 0.1 1 20 . 4 ILE CB C 39.0 0.1 1 21 . 5 LEU H H 8.46 0.01 1 22 . 5 LEU HA H 5.29 0.01 1 23 . 5 LEU HB2 H 1.55 0.01 1 24 . 5 LEU HB3 H 1.55 0.01 1 25 . 5 LEU HG H 1.43 0.01 1 26 . 5 LEU HD1 H 0.87 0.01 2 27 . 5 LEU HD2 H 0.81 0.01 2 28 . 5 LEU N N 128.4 0.1 1 29 . 5 LEU CA C 51.0 0.1 1 30 . 5 LEU CB C 42.6 0.1 1 31 . 6 LEU H H 9.31 0.01 1 32 . 6 LEU HA H 5.11 0.01 1 33 . 6 LEU HB2 H 1.69 0.01 2 34 . 6 LEU HB3 H 1.65 0.01 2 35 . 6 LEU HG H 1.79 0.01 1 36 . 6 LEU HD1 H 0.86 0.01 2 37 . 6 LEU HD2 H 0.96 0.01 2 38 . 6 LEU N N 126.9 0.1 1 39 . 6 LEU CA C 50.8 0.1 1 40 . 6 LEU CB C 42.6 0.1 1 41 . 7 GLY H H 8.12 0.01 1 42 . 7 GLY HA2 H 3.99 0.01 2 43 . 7 GLY HA3 H 4.40 0.01 2 44 . 7 GLY N N 108.6 0.1 1 45 . 7 GLY CA C 43.7 0.1 1 46 . 8 ALA H H 9.18 0.01 1 47 . 8 ALA N N 126.8 0.1 1 48 . 8 ALA CA C 47.6 0.1 1 49 . 8 ALA CB C 16.0 0.1 1 50 . 9 PRO HA H 4.37 0.01 1 51 . 9 PRO CA C 60.0 0.1 1 52 . 10 GLY H H 8.40 0.01 1 53 . 10 GLY HA2 H 4.23 0.01 2 54 . 10 GLY N N 111.6 0.1 1 55 . 10 GLY CA C 43.0 0.1 1 56 . 11 ALA H H 8.22 0.01 1 57 . 11 ALA HA H 4.37 0.01 1 58 . 11 ALA HB H 1.42 0.01 1 59 . 11 ALA N N 124.2 0.1 1 60 . 11 ALA CA C 50.4 0.1 1 61 . 11 ALA CB C 17.5 0.1 1 62 . 12 GLY H H 8.30 0.01 1 63 . 12 GLY N N 107.5 0.1 1 64 . 12 GLY CA C 43.0 0.1 1 65 . 13 LYS H H 8.23 0.01 1 66 . 13 LYS HA H 4.33 0.01 1 67 . 13 LYS HB2 H 1.94 0.01 2 68 . 13 LYS HB3 H 1.98 0.01 2 69 . 13 LYS N N 120.5 0.1 1 70 . 13 LYS CA C 54.3 0.1 1 71 . 13 LYS CB C 28.0 0.1 1 72 . 14 GLY H H 8.52 0.01 1 73 . 14 GLY HA2 H 4.29 0.01 2 74 . 14 GLY HA3 H 3.76 0.01 2 75 . 14 GLY N N 110.7 0.1 1 76 . 14 GLY CA C 43.3 0.1 1 77 . 15 THR H H 7.61 0.01 1 78 . 15 THR HA H 4.00 0.01 1 79 . 15 THR N N 116.4 0.1 1 80 . 15 THR CA C 63.6 0.1 1 81 . 15 THR CB C 67.0 0.1 1 82 . 16 GLN H H 7.18 0.01 1 83 . 16 GLN HA H 4.00 0.01 1 84 . 16 GLN HB2 H 2.03 0.01 1 85 . 16 GLN HB3 H 2.03 0.01 1 86 . 16 GLN N N 118.2 0.1 1 87 . 16 GLN CA C 53.2 0.1 1 88 . 16 GLN CB C 23.8 0.1 1 89 . 17 ALA H H 8.28 0.01 1 90 . 17 ALA HA H 3.79 0.01 1 91 . 17 ALA HB H 1.40 0.01 1 92 . 17 ALA N N 122.8 0.1 1 93 . 17 ALA CA C 53.3 0.1 1 94 . 17 ALA CB C 16.6 0.1 1 95 . 18 GLN H H 7.70 0.01 1 96 . 18 GLN HA H 4.07 0.01 1 97 . 18 GLN HB2 H 2.05 0.01 2 98 . 18 GLN HB3 H 2.08 0.01 2 99 . 18 GLN N N 114.9 0.1 1 100 . 18 GLN CA C 56.6 0.1 1 101 . 18 GLN CB C 25.5 0.1 1 102 . 19 PHE H H 7.02 0.01 1 103 . 19 PHE HA H 4.46 0.01 1 104 . 19 PHE HB2 H 3.25 0.01 2 105 . 19 PHE HB3 H 3.39 0.01 2 106 . 19 PHE HD1 H 7.27 0.01 1 107 . 19 PHE HD2 H 7.27 0.01 1 108 . 19 PHE N N 119.0 0.1 1 109 . 19 PHE CA C 57.9 0.1 1 110 . 19 PHE CB C 36.7 0.1 1 111 . 20 ILE H H 8.02 0.01 1 112 . 20 ILE N N 120.3 0.1 1 113 . 20 ILE CA C 63.3 0.1 1 114 . 22 GLU H H 7.85 0.01 1 115 . 22 GLU HA H 3.95 0.01 1 116 . 22 GLU HB2 H 1.98 0.01 2 117 . 22 GLU HB3 H 2.03 0.01 2 118 . 22 GLU N N 117.9 0.1 1 119 . 22 GLU CA C 56.3 0.1 1 120 . 22 GLU CB C 27.4 0.1 1 121 . 23 LYS H H 8.26 0.01 1 122 . 23 LYS HA H 3.76 0.01 1 123 . 23 LYS N N 120.1 0.1 1 124 . 23 LYS CA C 56.2 0.1 1 125 . 23 LYS CB C 29.4 0.1 1 126 . 24 TYR H H 7.89 0.01 1 127 . 24 TYR HA H 4.46 0.01 1 128 . 24 TYR HB2 H 3.19 0.01 2 129 . 24 TYR HD1 H 7.22 0.01 1 130 . 24 TYR HD2 H 7.22 0.01 1 131 . 24 TYR HE1 H 6.48 0.01 1 132 . 24 TYR HE2 H 6.48 0.01 1 133 . 24 TYR N N 112.7 0.1 1 134 . 24 TYR CA C 56.3 0.1 1 135 . 24 TYR CB C 36.2 0.1 1 136 . 25 GLY H H 7.74 0.01 1 137 . 25 GLY HA2 H 3.99 0.01 2 138 . 25 GLY HA3 H 3.85 0.01 2 139 . 25 GLY N N 111.0 0.1 1 140 . 25 GLY CA C 45.6 0.1 1 141 . 26 ILE H H 7.22 0.01 1 142 . 26 ILE HA H 4.92 0.01 1 143 . 26 ILE HB H 1.42 0.01 1 144 . 26 ILE N N 111.6 0.1 1 145 . 26 ILE CA C 54.3 0.1 1 146 . 26 ILE CB C 37.8 0.1 1 147 . 27 PRO HA H 4.66 0.01 1 148 . 27 PRO HB2 H 2.13 0.01 2 149 . 27 PRO CA C 59.8 0.1 1 150 . 27 PRO CB C 30.3 0.1 1 151 . 28 GLN H H 8.19 0.01 1 152 . 28 GLN HA H 5.13 0.01 1 153 . 28 GLN HB2 H 2.14 0.01 1 154 . 28 GLN HB3 H 2.14 0.01 1 155 . 28 GLN HG2 H 2.20 0.01 1 156 . 28 GLN HG3 H 2.20 0.01 1 157 . 28 GLN N N 119.4 0.1 1 158 . 28 GLN CA C 52.3 0.1 1 159 . 28 GLN CB C 28.3 0.1 1 160 . 29 ILE H H 9.42 0.01 1 161 . 29 ILE HA H 4.40 0.01 1 162 . 29 ILE HB H 1.90 0.01 1 163 . 29 ILE N N 127.6 0.1 1 164 . 29 ILE CA C 57.8 0.1 1 165 . 29 ILE CB C 36.9 0.1 1 166 . 30 SER H H 8.33 0.01 1 167 . 30 SER HA H 5.35 0.01 1 168 . 30 SER HB2 H 4.04 0.01 2 169 . 30 SER HB3 H 4.01 0.01 2 170 . 30 SER N N 120.7 0.1 1 171 . 30 SER CA C 53.2 0.1 1 172 . 30 SER CB C 63.3 0.1 1 173 . 31 THR H H 9.14 0.01 1 174 . 31 THR HA H 4.28 0.01 1 175 . 31 THR HB H 3.72 0.01 1 176 . 31 THR N N 118.4 0.1 1 177 . 31 THR CA C 64.8 0.1 1 178 . 32 GLY H H 8.73 0.01 1 179 . 32 GLY HA2 H 3.95 0.01 2 180 . 32 GLY HA3 H 3.77 0.01 2 181 . 32 GLY N N 110.0 0.1 1 182 . 32 GLY CA C 45.3 0.1 1 183 . 33 ASP H H 7.54 0.01 1 184 . 33 ASP HA H 4.46 0.01 1 185 . 33 ASP HB2 H 2.76 0.01 2 186 . 33 ASP N N 121.5 0.1 1 187 . 33 ASP CA C 54.7 0.1 1 188 . 33 ASP CB C 38.6 0.1 1 189 . 34 MET H H 8.17 0.01 1 190 . 34 MET HA H 4.40 0.01 1 191 . 34 MET HB2 H 1.89 0.01 2 192 . 34 MET HB3 H 1.75 0.01 2 193 . 34 MET N N 120.0 0.1 1 194 . 34 MET CA C 54.8 0.1 1 195 . 35 LEU H H 8.39 0.01 1 196 . 35 LEU HA H 3.96 0.01 1 197 . 35 LEU HB2 H 1.84 0.01 2 198 . 35 LEU HB3 H 1.55 0.01 2 199 . 35 LEU N N 121.2 0.1 1 200 . 35 LEU CA C 55.8 0.1 1 201 . 35 LEU CB C 39.2 0.1 1 202 . 36 ARG H H 7.76 0.01 1 203 . 36 ARG HA H 3.94 0.01 1 204 . 36 ARG HB2 H 1.96 0.01 2 205 . 36 ARG HB3 H 1.85 0.01 2 206 . 36 ARG N N 117.7 0.1 1 207 . 36 ARG CA C 57.3 0.1 1 208 . 36 ARG CB C 27.7 0.1 1 209 . 37 ALA H H 8.05 0.01 1 210 . 37 ALA HA H 4.14 0.01 1 211 . 37 ALA HB H 1.50 0.01 1 212 . 37 ALA N N 120.5 0.1 1 213 . 37 ALA CA C 52.2 0.1 1 214 . 37 ALA CB C 16.5 0.1 1 215 . 38 ALA H H 8.10 0.01 1 216 . 38 ALA HA H 4.19 0.01 1 217 . 38 ALA HB H 1.42 0.01 1 218 . 38 ALA N N 121.9 0.1 1 219 . 38 ALA CA C 52.6 0.1 1 220 . 38 ALA CB C 16.9 0.1 1 221 . 39 VAL H H 8.06 0.01 1 222 . 39 VAL HA H 3.63 0.01 1 223 . 39 VAL HB H 2.18 0.01 1 224 . 39 VAL HG1 H 1.09 0.01 2 225 . 39 VAL HG2 H 0.98 0.01 2 226 . 39 VAL N N 116.9 0.1 1 227 . 39 VAL CA C 63.6 0.1 1 228 . 39 VAL CB C 29.3 0.1 1 229 . 40 LYS H H 7.73 0.01 1 230 . 40 LYS HA H 4.20 0.01 1 231 . 40 LYS HB2 H 1.92 0.01 2 232 . 40 LYS HB3 H 1.96 0.01 2 233 . 40 LYS N N 119.3 0.1 1 234 . 40 LYS CA C 55.4 0.1 1 235 . 40 LYS CB C 30.2 0.1 1 236 . 41 SER H H 7.95 0.01 1 237 . 41 SER HA H 4.34 0.01 1 238 . 41 SER HB2 H 4.10 0.01 2 239 . 41 SER HB3 H 4.08 0.01 2 240 . 41 SER N N 113.8 0.1 1 241 . 41 SER CA C 57.5 0.1 1 242 . 41 SER CB C 62.3 0.1 1 243 . 42 GLY H H 7.96 0.01 1 244 . 42 GLY HA2 H 4.07 0.01 2 245 . 42 GLY HA3 H 3.91 0.01 2 246 . 42 GLY N N 109.9 0.1 1 247 . 42 GLY CA C 43.9 0.1 1 248 . 43 SER H H 7.87 0.01 1 249 . 43 SER HA H 4.45 0.01 1 250 . 43 SER HB2 H 3.25 0.01 2 251 . 43 SER HB3 H 3.20 0.01 2 252 . 43 SER N N 115.3 0.1 1 253 . 43 SER CA C 55.0 0.1 1 254 . 43 SER CB C 62.5 0.1 1 255 . 44 GLU H H 8.97 0.01 1 256 . 44 GLU HA H 4.08 0.01 1 257 . 44 GLU HB2 H 2.09 0.01 1 258 . 44 GLU HB3 H 2.09 0.01 1 259 . 44 GLU HG2 H 2.38 0.01 1 260 . 44 GLU HG3 H 2.38 0.01 1 261 . 44 GLU N N 122.8 0.1 1 262 . 44 GLU CA C 57.6 0.1 1 263 . 44 GLU CB C 26.7 0.1 1 264 . 45 LEU H H 8.38 0.01 1 265 . 45 LEU HA H 4.06 0.01 1 266 . 45 LEU HB2 H 1.66 0.01 2 267 . 45 LEU HB3 H 1.23 0.01 2 268 . 45 LEU N N 119.3 0.1 1 269 . 45 LEU CA C 55.3 0.1 1 270 . 45 LEU CB C 40.0 0.1 1 271 . 46 GLY H H 8.11 0.01 1 272 . 46 GLY HA2 H 3.41 0.01 2 273 . 46 GLY HA3 H 3.70 0.01 2 274 . 46 GLY N N 108.0 0.1 1 275 . 46 GLY CA C 44.8 0.1 1 276 . 47 LYS H H 8.36 0.01 1 277 . 47 LYS HA H 4.02 0.01 1 278 . 47 LYS HB2 H 1.94 0.01 2 279 . 47 LYS HB3 H 1.96 0.01 2 280 . 47 LYS N N 122.2 0.1 1 281 . 47 LYS CA C 57.0 0.1 1 282 . 47 LYS CB C 29.8 0.1 1 283 . 48 GLN H H 7.65 0.01 1 284 . 48 GLN HA H 4.13 0.01 1 285 . 48 GLN HB2 H 2.13 0.01 1 286 . 48 GLN HB3 H 2.13 0.01 1 287 . 48 GLN N N 118.9 0.1 1 288 . 48 GLN CA C 56.6 0.1 1 289 . 48 GLN CB C 26.3 0.1 1 290 . 49 ALA H H 8.34 0.01 1 291 . 49 ALA HA H 3.93 0.01 1 292 . 49 ALA HB H 1.38 0.01 1 293 . 49 ALA N N 120.7 0.1 1 294 . 49 ALA CA C 52.8 0.1 1 295 . 49 ALA CB C 16.2 0.1 1 296 . 50 LYS H H 8.39 0.01 1 297 . 50 LYS HA H 3.92 0.01 1 298 . 50 LYS HB2 H 2.05 0.01 2 299 . 50 LYS HB3 H 1.94 0.01 2 300 . 50 LYS N N 119.4 0.1 1 301 . 50 LYS CA C 57.5 0.1 1 302 . 50 LYS CB C 30.4 0.1 1 303 . 51 ASP H H 8.02 0.01 1 304 . 51 ASP HA H 4.40 0.01 1 305 . 51 ASP HB2 H 2.78 0.01 2 306 . 51 ASP HB3 H 2.64 0.01 2 307 . 51 ASP N N 118.6 0.1 1 308 . 51 ASP CA C 55.0 0.1 1 309 . 51 ASP CB C 38.2 0.1 1 310 . 52 ILE H H 7.61 0.01 1 311 . 52 ILE HA H 3.71 0.01 1 312 . 52 ILE HB H 1.94 0.01 1 313 . 52 ILE HG2 H 1.15 0.01 1 314 . 52 ILE HD1 H 0.90 0.01 1 315 . 52 ILE HG12 H 0.70 0.01 2 316 . 52 ILE N N 120.8 0.1 1 317 . 52 ILE CA C 62.7 0.1 1 318 . 52 ILE CB C 36.2 0.1 1 319 . 54 ASP H H 9.18 0.01 1 320 . 54 ASP HA H 4.46 0.01 1 321 . 54 ASP HB2 H 2.88 0.01 2 322 . 54 ASP HB3 H 2.68 0.01 2 323 . 54 ASP N N 122.0 0.1 1 324 . 54 ASP CA C 54.0 0.1 1 325 . 54 ASP CB C 37.8 0.1 1 326 . 55 ALA H H 7.38 0.01 1 327 . 55 ALA HA H 4.47 0.01 1 328 . 55 ALA HB H 1.52 0.01 1 329 . 55 ALA N N 120.0 0.1 1 330 . 55 ALA CA C 49.6 0.1 1 331 . 55 ALA CB C 17.3 0.1 1 332 . 56 GLY H H 8.06 0.01 1 333 . 56 GLY HA2 H 4.08 0.01 2 334 . 56 GLY HA3 H 3.88 0.01 2 335 . 56 GLY N N 107.8 0.1 1 336 . 56 GLY CA C 43.9 0.1 1 337 . 57 LYS H H 7.56 0.01 1 338 . 57 LYS HA H 4.48 0.01 1 339 . 57 LYS HB2 H 1.72 0.01 2 340 . 57 LYS HB3 H 1.95 0.01 2 341 . 57 LYS N N 119.4 0.1 1 342 . 57 LYS CA C 52.5 0.1 1 343 . 57 LYS CB C 32.4 0.1 1 344 . 58 LEU H H 7.88 0.01 1 345 . 58 LEU HA H 4.40 0.01 1 346 . 58 LEU N N 119.5 0.1 1 347 . 58 LEU CA C 51.4 0.1 1 348 . 58 LEU CB C 40.4 0.1 1 349 . 59 VAL H H 8.26 0.01 1 350 . 59 VAL HA H 3.84 0.01 1 351 . 59 VAL HB H 2.05 0.01 1 352 . 59 VAL HG1 H 1.01 0.01 1 353 . 59 VAL HG2 H 1.01 0.01 1 354 . 59 VAL N N 121.4 0.1 1 355 . 59 VAL CA C 61.4 0.1 1 356 . 59 VAL CB C 29.0 0.1 1 357 . 60 THR H H 7.06 0.01 1 358 . 60 THR HA H 4.32 0.01 1 359 . 60 THR HB H 4.75 0.01 1 360 . 60 THR N N 116.4 0.1 1 361 . 60 THR CA C 58.4 0.1 1 362 . 60 THR CB C 68.3 0.1 1 363 . 61 ASP H H 8.88 0.01 1 364 . 61 ASP HA H 4.37 0.01 1 365 . 61 ASP HB2 H 2.67 0.01 2 366 . 61 ASP HB3 H 2.48 0.01 2 367 . 61 ASP N N 122.0 0.1 1 368 . 61 ASP CA C 55.3 0.1 1 369 . 61 ASP CB C 37.8 0.1 1 370 . 62 GLU H H 8.80 0.01 1 371 . 62 GLU HA H 3.93 0.01 1 372 . 62 GLU HB2 H 1.96 0.01 2 373 . 62 GLU N N 117.3 0.1 1 374 . 62 GLU CA C 57.7 0.1 1 375 . 62 GLU CB C 26.4 0.1 1 376 . 63 LEU H H 7.49 0.01 1 377 . 63 LEU HA H 4.18 0.01 1 378 . 63 LEU HB2 H 1.66 0.01 2 379 . 63 LEU HB3 H 1.56 0.01 2 380 . 63 LEU N N 122.2 0.1 1 381 . 63 LEU CA C 55.7 0.1 1 382 . 63 LEU CB C 39.5 0.1 1 383 . 64 VAL H H 7.92 0.01 1 384 . 64 VAL N N 118.5 0.1 1 385 . 64 VAL CA C 65.2 0.1 1 386 . 64 VAL CB C 29.0 0.1 1 387 . 65 ILE H H 8.36 0.01 1 388 . 65 ILE HA H 3.53 0.01 1 389 . 65 ILE HB H 2.02 0.01 1 390 . 65 ILE N N 118.9 0.1 1 391 . 65 ILE CA C 61.2 0.1 1 392 . 65 ILE CB C 33.8 0.1 1 393 . 66 ALA H H 7.63 0.01 1 394 . 66 ALA HA H 4.05 0.01 1 395 . 66 ALA HB H 1.56 0.01 1 396 . 66 ALA N N 122.6 0.1 1 397 . 66 ALA CA C 53.0 0.1 1 398 . 66 ALA CB C 16.4 0.1 1 399 . 67 LEU H H 8.26 0.01 1 400 . 67 LEU HA H 3.95 0.01 1 401 . 67 LEU N N 119.6 0.1 1 402 . 67 LEU CA C 55.6 0.1 1 403 . 67 LEU CB C 39.5 0.1 1 404 . 68 VAL H H 8.53 0.01 1 405 . 68 VAL HA H 3.40 0.01 1 406 . 68 VAL HB H 2.02 0.01 1 407 . 68 VAL HG1 H 0.64 0.01 2 408 . 68 VAL HG2 H 0.49 0.01 2 409 . 68 VAL N N 122.9 0.1 1 410 . 68 VAL CA C 64.7 0.1 1 411 . 68 VAL CB C 28.6 0.1 1 412 . 69 LYS H H 8.39 0.01 1 413 . 69 LYS HA H 3.65 0.01 1 414 . 69 LYS HB2 H 1.84 0.01 1 415 . 69 LYS HB3 H 1.84 0.01 1 416 . 69 LYS N N 119.0 0.1 1 417 . 69 LYS CA C 57.9 0.1 1 418 . 69 LYS CB C 29.8 0.1 1 419 . 70 GLU H H 7.52 0.01 1 420 . 70 GLU HA H 4.04 0.01 1 421 . 70 GLU HB2 H 1.98 0.01 2 422 . 70 GLU HB3 H 2.13 0.01 2 423 . 70 GLU N N 117.2 0.1 1 424 . 70 GLU CA C 56.5 0.1 1 425 . 70 GLU CB C 27.7 0.1 1 426 . 71 ARG H H 8.18 0.01 1 427 . 71 ARG HA H 4.28 0.01 1 428 . 71 ARG HB2 H 1.98 0.01 2 429 . 71 ARG N N 121.0 0.1 1 430 . 71 ARG CA C 55.0 0.1 1 431 . 72 ILE H H 8.27 0.01 1 432 . 72 ILE HA H 4.75 0.01 1 433 . 72 ILE HB H 1.99 0.01 1 434 . 72 ILE HG12 H 1.23 0.01 2 435 . 72 ILE HG13 H 1.39 0.01 2 436 . 72 ILE HG2 H 0.19 0.01 1 437 . 72 ILE HD1 H 0.70 0.01 1 438 . 72 ILE N N 111.1 0.1 1 439 . 72 ILE CA C 60.9 0.1 1 440 . 72 ILE CB C 34.7 0.1 1 441 . 73 ALA H H 7.10 0.01 1 442 . 73 ALA HA H 4.43 0.01 1 443 . 73 ALA HB H 1.53 0.01 1 444 . 73 ALA N N 122.3 0.1 1 445 . 73 ALA CA C 49.2 0.1 1 446 . 73 ALA CB C 17.2 0.1 1 447 . 74 GLN H H 7.31 0.01 1 448 . 74 GLN HA H 4.32 0.01 1 449 . 74 GLN N N 116.7 0.1 1 450 . 74 GLN CA C 53.7 0.1 1 451 . 74 GLN CB C 26.8 0.1 1 452 . 75 GLU H H 9.00 0.01 1 453 . 75 GLU HA H 4.07 0.01 1 454 . 75 GLU HB2 H 2.13 0.01 2 455 . 75 GLU HB3 H 2.08 0.01 2 456 . 75 GLU N N 122.0 0.1 1 457 . 75 GLU CA C 57.4 0.1 1 458 . 75 GLU CB C 27.3 0.1 1 459 . 76 ASP H H 8.53 0.01 1 460 . 76 ASP HA H 4.50 0.01 1 461 . 76 ASP HB2 H 2.97 0.01 2 462 . 76 ASP HB3 H 2.80 0.01 2 463 . 76 ASP N N 117.1 0.1 1 464 . 76 ASP CA C 52.8 0.1 1 465 . 76 ASP CB C 36.2 0.1 1 466 . 77 CYS H H 7.77 0.01 1 467 . 77 CYS HA H 5.34 0.01 1 468 . 77 CYS HB2 H 3.14 0.01 2 469 . 77 CYS HB3 H 3.33 0.01 2 470 . 77 CYS N N 118.0 0.1 1 471 . 77 CYS CA C 57.4 0.1 1 472 . 77 CYS CB C 25.5 0.1 1 473 . 78 ARG H H 7.73 0.01 1 474 . 78 ARG HA H 4.16 0.01 1 475 . 78 ARG HB2 H 1.90 0.01 2 476 . 78 ARG HB3 H 2.05 0.01 2 477 . 78 ARG N N 122.5 0.1 1 478 . 78 ARG CA C 57.2 0.1 1 479 . 78 ARG CB C 27.4 0.1 1 480 . 79 ASN H H 8.89 0.01 1 481 . 79 ASN HA H 4.98 0.01 1 482 . 79 ASN HB2 H 3.03 0.01 2 483 . 79 ASN HB3 H 2.75 0.01 2 484 . 79 ASN HD21 H 6.89 0.01 2 485 . 79 ASN HD22 H 7.72 0.01 2 486 . 79 ASN N N 115.0 0.1 1 487 . 79 ASN ND2 N 113.7 0.1 1 488 . 79 ASN CA C 50.4 0.1 1 489 . 79 ASN CB C 36.9 0.1 1 490 . 80 GLY H H 7.71 0.01 1 491 . 80 GLY HA2 H 4.96 0.01 2 492 . 80 GLY HA3 H 3.24 0.01 2 493 . 80 GLY N N 108.8 0.1 1 494 . 80 GLY CA C 41.7 0.1 1 495 . 81 PHE H H 7.49 0.01 1 496 . 81 PHE HA H 4.89 0.01 1 497 . 81 PHE HD1 H 7.03 0.01 1 498 . 81 PHE HD2 H 7.03 0.01 1 499 . 81 PHE N N 108.8 0.1 1 500 . 81 PHE CA C 54.8 0.1 1 501 . 81 PHE CB C 37.9 0.1 1 502 . 82 LEU H H 8.89 0.01 1 503 . 82 LEU HA H 5.36 0.01 1 504 . 82 LEU HB2 H 1.81 0.01 1 505 . 82 LEU HB3 H 1.81 0.01 1 506 . 82 LEU HG H 1.30 0.01 1 507 . 82 LEU HD1 H 0.85 0.01 2 508 . 82 LEU HD2 H 0.90 0.01 2 509 . 82 LEU N N 122.3 0.1 1 510 . 82 LEU CA C 51.2 0.1 1 511 . 82 LEU CB C 42.3 0.1 1 512 . 83 LEU H H 9.52 0.01 1 513 . 83 LEU HA H 5.00 0.01 1 514 . 83 LEU HB2 H 2.04 0.01 1 515 . 83 LEU HB3 H 2.04 0.01 1 516 . 83 LEU HG H 1.90 0.01 1 517 . 83 LEU HD1 H 0.98 0.01 2 518 . 83 LEU HD2 H 0.88 0.01 2 519 . 83 LEU N N 128.0 0.1 1 520 . 83 LEU CA C 52.2 0.1 1 521 . 83 LEU CB C 41.3 0.1 1 522 . 84 ASP H H 8.73 0.01 1 523 . 84 ASP HA H 5.10 0.01 1 524 . 84 ASP HB2 H 2.75 0.01 2 525 . 84 ASP HB3 H 2.40 0.01 2 526 . 84 ASP N N 124.5 0.1 1 527 . 84 ASP CA C 50.5 0.1 1 528 . 84 ASP CB C 41.3 0.1 1 529 . 85 GLY H H 8.95 0.01 1 530 . 85 GLY HA2 H 4.33 0.01 2 531 . 85 GLY HA3 H 3.95 0.01 2 532 . 85 GLY N N 113.2 0.1 1 533 . 85 GLY CA C 44.1 0.1 1 534 . 86 PHE H H 7.45 0.01 1 535 . 86 PHE HA H 4.40 0.01 1 536 . 86 PHE HB2 H 3.20 0.01 2 537 . 86 PHE HB3 H 2.64 0.01 2 538 . 86 PHE HD1 H 7.22 0.01 1 539 . 86 PHE HD2 H 7.22 0.01 1 540 . 86 PHE N N 120.2 0.1 1 541 . 86 PHE CA C 53.4 0.1 1 542 . 86 PHE CB C 40.9 0.1 1 543 . 87 PRO CA C 59.9 0.1 1 544 . 87 PRO CB C 33.4 0.1 1 545 . 88 ARG H H 8.66 0.01 1 546 . 88 ARG HA H 4.46 0.01 1 547 . 88 ARG HB2 H 1.95 0.01 2 548 . 88 ARG N N 114.5 0.1 1 549 . 88 ARG CA C 53.6 0.1 1 550 . 88 ARG CB C 29.9 0.1 1 551 . 89 THR H H 7.16 0.01 1 552 . 89 THR HA H 4.75 0.01 1 553 . 89 THR N N 106.9 0.1 1 554 . 89 THR CA C 55.6 0.1 1 555 . 89 THR CB C 70.1 0.1 1 556 . 90 ILE H H 9.08 0.01 1 557 . 90 ILE N N 121.6 0.1 1 558 . 90 ILE CA C 64.0 0.1 1 559 . 90 ILE CB C 32.6 0.1 1 560 . 91 PRO HA H 4.33 0.01 1 561 . 91 PRO CA C 63.8 0.1 1 562 . 91 PRO CB C 29.0 0.1 1 563 . 92 GLN H H 7.29 0.01 1 564 . 92 GLN HA H 3.83 0.01 1 565 . 92 GLN HB2 H 2.17 0.01 2 566 . 92 GLN HB3 H 2.10 0.01 2 567 . 92 GLN HG2 H 2.61 0.01 1 568 . 92 GLN HG3 H 2.61 0.01 1 569 . 92 GLN N N 116.5 0.1 1 570 . 92 GLN CA C 56.8 0.1 1 571 . 92 GLN CB C 25.8 0.1 1 572 . 93 ALA H H 7.79 0.01 1 573 . 93 ALA HA H 3.95 0.01 1 574 . 93 ALA HB H 0.92 0.01 1 575 . 93 ALA N N 124.6 0.1 1 576 . 93 ALA CA C 53.1 0.1 1 577 . 93 ALA CB C 16.8 0.1 1 578 . 94 ASP H H 8.85 0.01 1 579 . 94 ASP HA H 4.57 0.01 1 580 . 94 ASP HB2 H 2.60 0.01 2 581 . 94 ASP HB3 H 2.55 0.01 2 582 . 94 ASP N N 119.7 0.1 1 583 . 94 ASP CA C 54.6 0.1 1 584 . 94 ASP CB C 38.4 0.1 1 585 . 95 ALA H H 8.11 0.01 1 586 . 95 ALA HA H 4.24 0.01 1 587 . 95 ALA HB H 1.55 0.01 1 588 . 95 ALA N N 122.9 0.1 1 589 . 95 ALA CA C 52.6 0.1 1 590 . 95 ALA CB C 16.0 0.1 1 591 . 96 MET H H 8.20 0.01 1 592 . 96 MET HA H 4.37 0.01 1 593 . 96 MET N N 119.4 0.1 1 594 . 97 LYS H H 7.68 0.01 1 595 . 97 LYS HA H 4.07 0.01 1 596 . 97 LYS HB2 H 2.08 0.01 1 597 . 97 LYS HB3 H 2.08 0.01 1 598 . 97 LYS N N 120.8 0.1 1 599 . 97 LYS CA C 57.5 0.1 1 600 . 97 LYS CB C 30.0 0.1 1 601 . 98 GLU H H 8.48 0.01 1 602 . 98 GLU HA H 4.04 0.01 1 603 . 98 GLU HB2 H 2.14 0.01 1 604 . 98 GLU HB3 H 2.14 0.01 1 605 . 98 GLU N N 121.4 0.1 1 606 . 98 GLU CA C 56.5 0.1 1 607 . 98 GLU CB C 27.0 0.1 1 608 . 99 ALA H H 7.61 0.01 1 609 . 99 ALA HA H 4.43 0.01 1 610 . 99 ALA HB H 1.50 0.01 1 611 . 99 ALA N N 118.9 0.1 1 612 . 99 ALA CA C 49.4 0.1 1 613 . 99 ALA CB C 17.7 0.1 1 614 . 100 GLY H H 7.93 0.01 1 615 . 100 GLY HA2 H 4.13 0.01 2 616 . 100 GLY HA3 H 3.85 0.01 2 617 . 100 GLY N N 106.7 0.1 1 618 . 100 GLY CA C 43.5 0.1 1 619 . 101 ILE H H 8.11 0.01 1 620 . 101 ILE HA H 4.07 0.01 1 621 . 101 ILE HB H 1.89 0.01 1 622 . 101 ILE N N 122.0 0.1 1 623 . 101 ILE CA C 58.4 0.1 1 624 . 101 ILE CB C 34.7 0.1 1 625 . 102 ASN H H 7.94 0.01 1 626 . 102 ASN HA H 4.82 0.01 1 627 . 102 ASN HB2 H 2.66 0.01 2 628 . 102 ASN HB3 H 2.80 0.01 2 629 . 102 ASN HD21 H 7.49 0.01 2 630 . 102 ASN HD22 H 6.90 0.01 2 631 . 102 ASN N N 123.9 0.1 1 632 . 102 ASN ND2 N 114.0 0.1 1 633 . 102 ASN CA C 50.2 0.1 1 634 . 102 ASN CB C 37.8 0.1 1 635 . 103 VAL H H 8.38 0.01 1 636 . 103 VAL HA H 4.27 0.01 1 637 . 103 VAL HB H 1.91 0.01 1 638 . 103 VAL HG1 H 0.78 0.01 1 639 . 103 VAL HG2 H 0.82 0.01 1 640 . 103 VAL N N 113.2 0.1 1 641 . 103 VAL CA C 58.0 0.1 1 642 . 103 VAL CB C 32.1 0.1 1 643 . 104 ASP H H 8.57 0.01 1 644 . 104 ASP HA H 4.56 0.01 1 645 . 104 ASP HB2 H 2.85 0.01 2 646 . 104 ASP HB3 H 2.57 0.01 2 647 . 104 ASP N N 124.2 0.1 1 648 . 104 ASP CA C 54.4 0.1 1 649 . 104 ASP CB C 41.8 0.1 1 650 . 105 TYR H H 7.72 0.01 1 651 . 105 TYR HA H 5.20 0.01 1 652 . 105 TYR HB2 H 2.61 0.01 2 653 . 105 TYR HB3 H 2.47 0.01 2 654 . 105 TYR HD1 H 6.69 0.01 1 655 . 105 TYR HD2 H 6.69 0.01 1 656 . 105 TYR HE1 H 6.69 0.01 1 657 . 105 TYR HE2 H 6.69 0.01 1 658 . 105 TYR N N 114.8 0.1 1 659 . 105 TYR CA C 54.5 0.1 1 660 . 105 TYR CB C 42.0 0.1 1 661 . 106 VAL H H 8.97 0.01 1 662 . 106 VAL HA H 4.47 0.01 1 663 . 106 VAL HB H 1.89 0.01 1 664 . 106 VAL HG1 H 0.60 0.01 1 665 . 106 VAL HG2 H 0.38 0.01 1 666 . 106 VAL N N 123.3 0.1 1 667 . 106 VAL CA C 60.0 0.1 1 668 . 106 VAL CB C 30.4 0.1 1 669 . 107 LEU H H 8.95 0.01 1 670 . 107 LEU HA H 5.24 0.01 1 671 . 107 LEU HB2 H 1.84 0.01 2 672 . 107 LEU HB3 H 1.02 0.01 2 673 . 107 LEU HG H 1.02 0.01 1 674 . 107 LEU HD1 H 0.73 0.01 1 675 . 107 LEU HD2 H 0.73 0.01 1 676 . 107 LEU N N 124.8 0.1 1 677 . 107 LEU CA C 49.6 0.1 1 678 . 107 LEU CB C 42.6 0.1 1 679 . 108 GLU H H 8.77 0.01 1 680 . 108 GLU HA H 4.96 0.01 1 681 . 108 GLU N N 124.5 0.1 1 682 . 108 GLU CA C 51.6 0.1 1 683 . 109 PHE H H 9.34 0.01 1 684 . 109 PHE HA H 4.64 0.01 1 685 . 109 PHE HB2 H 3.29 0.01 2 686 . 109 PHE N N 130.4 0.1 1 687 . 109 PHE CA C 55.3 0.1 1 688 . 109 PHE CB C 37.3 0.1 1 689 . 110 ASP H H 8.82 0.01 1 690 . 110 ASP HA H 4.73 0.01 1 691 . 110 ASP HB2 H 2.90 0.01 2 692 . 110 ASP HB3 H 2.26 0.01 2 693 . 110 ASP N N 128.2 0.1 1 694 . 110 ASP CA C 52.3 0.1 1 695 . 110 ASP CB C 41.7 0.1 1 696 . 111 VAL H H 7.45 0.01 1 697 . 111 VAL HA H 4.37 0.01 1 698 . 111 VAL HB H 1.91 0.01 1 699 . 111 VAL HG1 H 0.87 0.01 1 700 . 111 VAL HG2 H 0.87 0.01 1 701 . 111 VAL N N 126.0 0.1 1 702 . 111 VAL CA C 56.9 0.1 1 703 . 111 VAL CB C 34.3 0.1 1 704 . 112 PRO HA H 4.59 0.01 1 705 . 112 PRO HB2 H 2.05 0.01 2 706 . 112 PRO CA C 60.9 0.1 1 707 . 112 PRO CB C 30.4 0.1 1 708 . 113 ASP H H 8.84 0.01 1 709 . 113 ASP HA H 4.30 0.01 1 710 . 113 ASP HB2 H 2.78 0.01 2 711 . 113 ASP N N 124.0 0.1 1 712 . 113 ASP CA C 55.7 0.1 1 713 . 113 ASP CB C 38.4 0.1 1 714 . 114 GLU H H 9.04 0.01 1 715 . 114 GLU HA H 3.92 0.01 1 716 . 114 GLU HB2 H 1.99 0.01 2 717 . 114 GLU HB3 H 2.03 0.01 2 718 . 114 GLU N N 114.7 0.1 1 719 . 114 GLU CA C 57.1 0.1 1 720 . 114 GLU CB C 26.8 0.1 1 721 . 115 LEU H H 7.18 0.01 1 722 . 115 LEU HA H 4.36 0.01 1 723 . 115 LEU HB2 H 1.66 0.01 1 724 . 115 LEU HB3 H 1.66 0.01 1 725 . 115 LEU HG H 1.62 0.01 1 726 . 115 LEU HD1 H 0.92 0.01 2 727 . 115 LEU HD2 H 0.98 0.01 2 728 . 115 LEU N N 119.2 0.1 1 729 . 115 LEU CA C 54.8 0.1 1 730 . 115 LEU CB C 39.5 0.1 1 731 . 116 ILE H H 7.46 0.01 1 732 . 116 ILE HA H 3.44 0.01 1 733 . 116 ILE HB H 2.10 0.01 1 734 . 116 ILE N N 121.0 0.1 1 735 . 116 ILE CA C 63.8 0.1 1 736 . 116 ILE CB C 35.3 0.1 1 737 . 117 VAL H H 8.28 0.01 1 738 . 117 VAL HA H 3.44 0.01 1 739 . 117 VAL HB H 2.10 0.01 1 740 . 117 VAL HG1 H 0.95 0.01 2 741 . 117 VAL HG2 H 0.98 0.01 2 742 . 117 VAL N N 117.3 0.1 1 743 . 117 VAL CA C 65.5 0.1 1 744 . 117 VAL CB C 29.3 0.1 1 745 . 118 ASP H H 7.71 0.01 1 746 . 118 ASP HA H 4.53 0.01 1 747 . 118 ASP HB2 H 2.97 0.01 2 748 . 118 ASP HB3 H 2.78 0.01 2 749 . 118 ASP N N 117.2 0.1 1 750 . 118 ASP CA C 55.0 0.1 1 751 . 118 ASP CB C 39.7 0.1 1 752 . 119 ARG H H 8.18 0.01 1 753 . 119 ARG HA H 4.13 0.01 1 754 . 119 ARG HB2 H 2.03 0.01 1 755 . 119 ARG HB3 H 2.03 0.01 1 756 . 119 ARG N N 117.4 0.1 1 757 . 119 ARG CA C 57.7 0.1 1 758 . 119 ARG CB C 28.5 0.1 1 759 . 120 ILE H H 8.10 0.01 1 760 . 120 ILE HA H 3.99 0.01 1 761 . 120 ILE HB H 1.88 0.01 1 762 . 120 ILE N N 118.9 0.1 1 763 . 120 ILE CA C 61.6 0.1 1 764 . 120 ILE CB C 36.5 0.1 1 765 . 121 VAL H H 8.93 0.01 1 766 . 121 VAL HA H 4.37 0.01 1 767 . 121 VAL HB H 2.42 0.01 1 768 . 121 VAL HG1 H 1.12 0.01 1 769 . 121 VAL HG2 H 1.12 0.01 1 770 . 121 VAL N N 115.4 0.1 1 771 . 121 VAL CA C 61.8 0.1 1 772 . 121 VAL CB C 29.0 0.1 1 773 . 122 GLY H H 7.44 0.01 1 774 . 122 GLY HA2 H 3.90 0.01 2 775 . 122 GLY HA3 H 3.10 0.01 2 776 . 122 GLY N N 106.1 0.1 1 777 . 122 GLY CA C 42.3 0.1 1 778 . 123 ARG H H 7.68 0.01 1 779 . 123 ARG HA H 4.90 0.01 1 780 . 123 ARG HB2 H 2.13 0.01 1 781 . 123 ARG HB3 H 2.13 0.01 1 782 . 123 ARG N N 120.9 0.1 1 783 . 123 ARG CA C 55.2 0.1 1 784 . 123 ARG CB C 29.5 0.1 1 785 . 124 ARG H H 8.89 0.01 1 786 . 124 ARG HA H 5.08 0.01 1 787 . 124 ARG N N 125.6 0.1 1 788 . 124 ARG CA C 50.9 0.1 1 789 . 124 ARG CB C 32.8 0.1 1 790 . 125 VAL H H 9.32 0.01 1 791 . 125 VAL HA H 5.53 0.01 1 792 . 125 VAL HB H 1.95 0.01 1 793 . 125 VAL HG1 H 0.89 0.01 2 794 . 125 VAL HG2 H 0.87 0.01 2 795 . 125 VAL N N 118.2 0.1 1 796 . 125 VAL CA C 57.0 0.1 1 797 . 125 VAL CB C 34.0 0.1 1 798 . 126 HIS H H 9.23 0.01 1 799 . 126 HIS HA H 5.05 0.01 1 800 . 126 HIS HB2 H 3.47 0.01 2 801 . 126 HIS HB3 H 2.84 0.01 2 802 . 126 HIS HD2 H 6.97 0.01 1 803 . 126 HIS HE1 H 7.89 0.01 1 804 . 126 HIS N N 126.8 0.1 1 805 . 126 HIS CA C 53.0 0.1 1 806 . 126 HIS CB C 29.0 0.1 1 807 . 127 ALA H H 9.05 0.01 1 808 . 127 ALA HA H 3.97 0.01 1 809 . 127 ALA HB H 1.36 0.01 1 810 . 127 ALA N N 129.8 0.1 1 811 . 127 ALA CA C 53.8 0.1 1 812 . 127 ALA CB C 14.3 0.1 1 813 . 128 PRO HA H 4.21 0.01 1 814 . 128 PRO CA C 63.6 0.1 1 815 . 128 PRO CB C 29.2 0.1 1 816 . 129 SER H H 6.84 0.01 1 817 . 129 SER HA H 4.60 0.01 1 818 . 129 SER N N 107.7 0.1 1 819 . 129 SER CA C 56.4 0.1 1 820 . 129 SER CB C 63.0 0.1 1 821 . 130 GLY H H 8.61 0.01 1 822 . 130 GLY HA2 H 4.28 0.01 2 823 . 130 GLY HA3 H 3.53 0.01 2 824 . 130 GLY N N 113.2 0.1 1 825 . 130 GLY CA C 43.0 0.1 1 826 . 131 ARG H H 8.47 0.01 1 827 . 131 ARG HA H 4.05 0.01 1 828 . 131 ARG N N 122.1 0.1 1 829 . 131 ARG CA C 57.0 0.1 1 830 . 131 ARG CB C 30.6 0.1 1 831 . 132 VAL H H 7.92 0.01 1 832 . 132 VAL HA H 4.84 0.01 1 833 . 132 VAL HB H 1.94 0.01 1 834 . 132 VAL HG1 H 1.06 0.01 2 835 . 132 VAL HG2 H 0.90 0.01 2 836 . 132 VAL N N 120.3 0.1 1 837 . 132 VAL CA C 58.8 0.1 1 838 . 132 VAL CB C 32.1 0.1 1 839 . 133 TYR H H 9.29 0.01 1 840 . 133 TYR HA H 4.94 0.01 1 841 . 133 TYR HB2 H 3.27 0.01 2 842 . 133 TYR HB3 H 2.41 0.01 2 843 . 133 TYR HD1 H 7.00 0.01 1 844 . 133 TYR HD2 H 7.00 0.01 1 845 . 133 TYR HE1 H 6.90 0.01 1 846 . 133 TYR HE2 H 6.90 0.01 1 847 . 133 TYR N N 124.5 0.1 1 848 . 133 TYR CA C 53.6 0.1 1 849 . 133 TYR CB C 40.0 0.1 1 850 . 134 HIS H H 8.42 0.01 1 851 . 134 HIS HA H 5.18 0.01 1 852 . 134 HIS HB2 H 2.93 0.01 1 853 . 134 HIS HB3 H 2.93 0.01 1 854 . 134 HIS HD2 H 7.52 0.01 1 855 . 134 HIS N N 120.9 0.1 1 856 . 134 HIS CA C 54.7 0.1 1 857 . 134 HIS CB C 32.0 0.1 1 858 . 135 VAL H H 8.19 0.01 1 859 . 135 VAL HA H 3.79 0.01 1 860 . 135 VAL N N 120.8 0.1 1 861 . 135 VAL CA C 63.6 0.1 1 862 . 136 LYS H H 9.55 0.01 1 863 . 136 LYS HA H 4.57 0.01 1 864 . 136 LYS N N 120.1 0.1 1 865 . 136 LYS CA C 54.8 0.1 1 866 . 136 LYS CB C 33.0 0.1 1 867 . 137 PHE HD1 H 7.29 0.01 1 868 . 137 PHE HD2 H 7.29 0.01 1 869 . 137 PHE HE1 H 7.12 0.01 1 870 . 137 PHE HE2 H 7.12 0.01 1 871 . 137 PHE HZ H 6.58 0.01 1 872 . 140 PRO CA C 59.8 0.1 1 873 . 141 LYS H H 10.12 0.01 1 874 . 141 LYS HA H 3.92 0.01 1 875 . 141 LYS HB2 H 1.73 0.01 2 876 . 141 LYS HB3 H 1.70 0.01 2 877 . 141 LYS N N 124.1 0.1 1 878 . 141 LYS CA C 56.8 0.1 1 879 . 141 LYS CB C 30.2 0.1 1 880 . 142 VAL H H 8.87 0.01 1 881 . 142 VAL HA H 3.92 0.01 1 882 . 142 VAL HB H 1.69 0.01 1 883 . 142 VAL HG1 H 0.89 0.01 2 884 . 142 VAL HG2 H 0.82 0.01 2 885 . 142 VAL N N 120.5 0.1 1 886 . 142 VAL CA C 59.0 0.1 1 887 . 142 VAL CB C 31.0 0.1 1 888 . 143 GLU H H 8.15 0.01 1 889 . 143 GLU HA H 3.77 0.01 1 890 . 143 GLU HB2 H 1.96 0.01 2 891 . 143 GLU N N 125.5 0.1 1 892 . 143 GLU CA C 55.2 0.1 1 893 . 143 GLU CB C 27.4 0.1 1 894 . 144 GLY H H 8.81 0.01 1 895 . 144 GLY HA2 H 4.16 0.01 2 896 . 144 GLY HA3 H 3.52 0.01 2 897 . 144 GLY N N 111.6 0.1 1 898 . 144 GLY CA C 43.6 0.1 1 899 . 145 LYS H H 8.01 0.01 1 900 . 145 LYS HA H 4.92 0.01 1 901 . 145 LYS N N 119.2 0.1 1 902 . 145 LYS CA C 51.3 0.1 1 903 . 145 LYS CB C 33.8 0.1 1 904 . 146 ASP H H 9.05 0.01 1 905 . 146 ASP HA H 4.11 0.01 1 906 . 146 ASP HB2 H 2.26 0.01 2 907 . 146 ASP N N 119.9 0.1 1 908 . 146 ASP CA C 51.4 0.1 1 909 . 146 ASP CB C 41.5 0.1 1 910 . 147 ASP H H 7.93 0.01 1 911 . 147 ASP HA H 4.32 0.01 1 912 . 147 ASP HB2 H 2.78 0.01 2 913 . 147 ASP HB3 H 2.87 0.01 2 914 . 147 ASP N N 127.0 0.1 1 915 . 147 ASP CA C 54.9 0.1 1 916 . 147 ASP CB C 38.4 0.1 1 917 . 148 VAL H H 6.42 0.01 1 918 . 148 VAL HA H 3.80 0.01 1 919 . 148 VAL HB H 2.08 0.01 1 920 . 148 VAL HG1 H 0.92 0.01 2 921 . 148 VAL HG2 H 0.94 0.01 2 922 . 148 VAL N N 115.0 0.1 1 923 . 148 VAL CA C 63.0 0.1 1 924 . 148 VAL CB C 30.2 0.1 1 925 . 149 THR H H 7.53 0.01 1 926 . 149 THR HA H 4.46 0.01 1 927 . 149 THR HB H 4.39 0.01 1 928 . 149 THR N N 105.7 0.1 1 929 . 149 THR CA C 59.8 0.1 1 930 . 149 THR CB C 70.8 0.1 1 931 . 150 GLY H H 7.90 0.01 1 932 . 150 GLY HA2 H 4.21 0.01 2 933 . 150 GLY HA3 H 3.74 0.01 2 934 . 150 GLY N N 111.2 0.1 1 935 . 150 GLY CA C 43.9 0.1 1 936 . 151 GLU H H 7.71 0.01 1 937 . 151 GLU HA H 4.28 0.01 1 938 . 151 GLU HB2 H 2.03 0.01 2 939 . 151 GLU HB3 H 1.89 0.01 2 940 . 151 GLU N N 118.6 0.1 1 941 . 151 GLU CA C 53.3 0.1 1 942 . 151 GLU CB C 28.7 0.1 1 943 . 152 GLU H H 8.69 0.01 1 944 . 152 GLU HA H 4.43 0.01 1 945 . 152 GLU HB2 H 2.07 0.01 2 946 . 152 GLU HB3 H 2.13 0.01 2 947 . 152 GLU N N 119.7 0.1 1 948 . 152 GLU CA C 55.3 0.1 1 949 . 152 GLU CB C 28.5 0.1 1 950 . 153 LEU H H 7.92 0.01 1 951 . 153 LEU HA H 4.80 0.01 1 952 . 153 LEU HB2 H 1.54 0.01 1 953 . 153 LEU HB3 H 1.54 0.01 1 954 . 153 LEU HG H 1.25 0.01 1 955 . 153 LEU HD1 H 0.27 0.01 2 956 . 153 LEU HD2 H 0.77 0.01 2 957 . 153 LEU N N 120.8 0.1 1 958 . 153 LEU CA C 50.8 0.1 1 959 . 153 LEU CB C 41.0 0.1 1 960 . 154 THR H H 9.34 0.01 1 961 . 154 THR HA H 4.84 0.01 1 962 . 154 THR HB H 4.28 0.01 1 963 . 154 THR HG2 H 1.23 0.01 1 964 . 154 THR N N 114.6 0.1 1 965 . 154 THR CA C 57.7 0.1 1 966 . 154 THR CB C 69.5 0.1 1 967 . 155 THR H H 8.37 0.01 1 968 . 155 THR N N 116.0 0.1 1 969 . 155 THR CA C 58.1 0.1 1 970 . 155 THR CB C 68.1 0.1 1 971 . 156 ARG H H 9.80 0.01 1 972 . 156 ARG N N 127.0 0.1 1 973 . 156 ARG CA C 53.6 0.1 1 974 . 157 LYS HA H 4.05 0.01 1 975 . 157 LYS HB2 H 1.85 0.01 2 976 . 157 LYS HB3 H 1.89 0.01 2 977 . 157 LYS CA C 57.2 0.1 1 978 . 157 LYS CB C 29.6 0.1 1 979 . 158 ASP H H 8.38 0.01 1 980 . 158 ASP HA H 4.47 0.01 1 981 . 158 ASP HB2 H 2.73 0.01 2 982 . 158 ASP HB3 H 2.38 0.01 2 983 . 158 ASP N N 114.5 0.1 1 984 . 158 ASP CA C 53.0 0.1 1 985 . 158 ASP CB C 38.4 0.1 1 986 . 159 ASP H H 7.45 0.01 1 987 . 159 ASP HA H 4.66 0.01 1 988 . 159 ASP HB2 H 2.78 0.01 2 989 . 159 ASP HB3 H 3.16 0.01 2 990 . 159 ASP N N 117.0 0.1 1 991 . 159 ASP CA C 50.9 0.1 1 992 . 159 ASP CB C 38.6 0.1 1 993 . 160 GLN H H 7.10 0.01 1 994 . 160 GLN HA H 4.35 0.01 1 995 . 160 GLN HB2 H 2.16 0.01 2 996 . 160 GLN HB3 H 2.37 0.01 2 997 . 160 GLN N N 117.4 0.1 1 998 . 160 GLN CA C 53.5 0.1 1 999 . 160 GLN CB C 27.0 0.1 1 1000 . 161 GLU H H 9.21 0.01 1 1001 . 161 GLU HA H 3.69 0.01 1 1002 . 161 GLU HB2 H 2.07 0.01 1 1003 . 161 GLU HB3 H 2.07 0.01 1 1004 . 161 GLU N N 124.4 0.1 1 1005 . 161 GLU CA C 59.1 0.1 1 1006 . 161 GLU CB C 27.5 0.1 1 1007 . 162 GLU H H 9.26 0.01 1 1008 . 162 GLU HA H 4.05 0.01 1 1009 . 162 GLU HB2 H 2.03 0.01 2 1010 . 162 GLU HB3 H 2.09 0.01 2 1011 . 162 GLU N N 116.6 0.1 1 1012 . 162 GLU CA C 57.7 0.1 1 1013 . 162 GLU CB C 26.7 0.1 1 1014 . 163 THR H H 7.25 0.01 1 1015 . 163 THR HA H 4.04 0.01 1 1016 . 163 THR HB H 4.39 0.01 1 1017 . 163 THR HG2 H 1.36 0.01 1 1018 . 163 THR N N 116.2 0.1 1 1019 . 163 THR CA C 63.8 0.1 1 1020 . 163 THR CB C 66.2 0.1 1 1021 . 164 VAL H H 8.28 0.01 1 1022 . 164 VAL HA H 3.56 0.01 1 1023 . 164 VAL HB H 2.13 0.01 1 1024 . 164 VAL HG1 H 1.08 0.01 2 1025 . 164 VAL HG2 H 0.98 0.01 2 1026 . 164 VAL N N 123.0 0.1 1 1027 . 164 VAL CA C 64.4 0.1 1 1028 . 164 VAL CB C 29.8 0.1 1 1029 . 165 ARG H H 8.74 0.01 1 1030 . 165 ARG HA H 4.00 0.01 1 1031 . 165 ARG N N 117.0 0.1 1 1032 . 165 ARG CA C 58.4 0.1 1 1033 . 165 ARG CB C 27.9 0.1 1 1034 . 166 LYS H H 7.74 0.01 1 1035 . 166 LYS HA H 4.18 0.01 1 1036 . 166 LYS HB2 H 2.03 0.01 1 1037 . 166 LYS HB3 H 2.03 0.01 1 1038 . 166 LYS N N 119.0 0.1 1 1039 . 166 LYS CA C 57.4 0.1 1 1040 . 166 LYS CB C 30.3 0.1 1 1041 . 167 ARG H H 8.08 0.01 1 1042 . 167 ARG N N 119.0 0.1 1 1043 . 167 ARG CA C 57.0 0.1 1 1044 . 167 ARG CB C 27.7 0.1 1 1045 . 168 LEU H H 8.25 0.01 1 1046 . 168 LEU N N 120.0 0.1 1 1047 . 168 LEU CA C 55.6 0.1 1 1048 . 168 LEU CB C 39.0 0.1 1 1049 . 169 VAL H H 8.25 0.01 1 1050 . 169 VAL HA H 3.91 0.01 1 1051 . 169 VAL HB H 2.31 0.01 1 1052 . 169 VAL N N 121.5 0.1 1 1053 . 169 VAL CA C 65.2 0.1 1 1054 . 169 VAL CB C 29.5 0.1 1 1055 . 170 GLU H H 7.98 0.01 1 1056 . 170 GLU HA H 4.12 0.01 1 1057 . 170 GLU HB2 H 2.21 0.01 2 1058 . 170 GLU HB3 H 2.17 0.01 2 1059 . 170 GLU N N 119.5 0.1 1 1060 . 170 GLU CA C 56.9 0.1 1 1061 . 170 GLU CB C 27.4 0.1 1 1062 . 171 TYR H H 8.28 0.01 1 1063 . 171 TYR HA H 4.32 0.01 1 1064 . 171 TYR HD1 H 6.65 0.01 1 1065 . 171 TYR HD2 H 6.65 0.01 1 1066 . 171 TYR HE1 H 6.76 0.01 1 1067 . 171 TYR HE2 H 6.76 0.01 1 1068 . 171 TYR N N 120.0 0.1 1 1069 . 171 TYR CA C 59.6 0.1 1 1070 . 171 TYR CB C 35.8 0.1 1 1071 . 172 HIS H H 8.82 0.01 1 1072 . 172 HIS HA H 4.27 0.01 1 1073 . 172 HIS HB2 H 3.40 0.01 2 1074 . 172 HIS HD2 H 7.54 0.01 1 1075 . 172 HIS HE1 H 8.68 0.01 1 1076 . 172 HIS N N 120.4 0.1 1 1077 . 172 HIS CA C 57.2 0.1 1 1078 . 172 HIS CB C 26.0 0.1 1 1079 . 173 GLN H H 8.48 0.01 1 1080 . 173 GLN N N 118.6 0.1 1 1081 . 173 GLN CA C 56.6 0.1 1 1082 . 173 GLN CB C 26.2 0.1 1 1083 . 175 THR H H 8.18 0.01 1 1084 . 175 THR HA H 4.09 0.01 1 1085 . 175 THR HB H 3.67 0.01 1 1086 . 175 THR N N 113.2 0.1 1 1087 . 175 THR CA C 62.8 0.1 1 1088 . 175 THR CB C 67.0 0.1 1 1089 . 176 ALA H H 8.33 0.01 1 1090 . 176 ALA N N 126.0 0.1 1 1091 . 176 ALA CA C 54.9 0.1 1 1092 . 176 ALA CB C 13.8 0.1 1 1093 . 177 PRO HA H 4.44 0.01 1 1094 . 178 LEU H H 7.03 0.01 1 1095 . 178 LEU HA H 3.95 0.01 1 1096 . 178 LEU HB2 H 1.80 0.01 1 1097 . 178 LEU HB3 H 1.80 0.01 1 1098 . 178 LEU N N 119.0 0.1 1 1099 . 178 LEU CA C 54.7 0.1 1 1100 . 178 LEU CB C 40.2 0.1 1 1101 . 179 ILE H H 8.43 0.01 1 1102 . 179 ILE HA H 3.67 0.01 1 1103 . 179 ILE HB H 1.99 0.01 1 1104 . 179 ILE N N 121.0 0.1 1 1105 . 179 ILE CA C 62.4 0.1 1 1106 . 179 ILE CB C 35.2 0.1 1 1107 . 180 GLY H H 7.89 0.01 1 1108 . 180 GLY HA2 H 3.77 0.01 2 1109 . 180 GLY HA3 H 3.91 0.01 2 1110 . 180 GLY N N 107.8 0.1 1 1111 . 180 GLY CA C 45.2 0.1 1 1112 . 181 TYR H H 7.93 0.01 1 1113 . 181 TYR HA H 4.04 0.01 1 1114 . 181 TYR HB2 H 3.11 0.01 2 1115 . 181 TYR HB3 H 2.82 0.01 2 1116 . 181 TYR HD1 H 6.18 0.01 1 1117 . 181 TYR HD2 H 6.18 0.01 1 1118 . 181 TYR HE1 H 6.50 0.01 1 1119 . 181 TYR HE2 H 6.50 0.01 1 1120 . 181 TYR N N 123.9 0.1 1 1121 . 181 TYR CA C 58.9 0.1 1 1122 . 181 TYR CB C 36.4 0.1 1 1123 . 182 TYR H H 8.91 0.01 1 1124 . 182 TYR HA H 4.28 0.01 1 1125 . 182 TYR HD1 H 7.05 0.01 1 1126 . 182 TYR HD2 H 7.05 0.01 1 1127 . 182 TYR HE1 H 6.77 0.01 1 1128 . 182 TYR HE2 H 6.77 0.01 1 1129 . 182 TYR N N 118.7 0.1 1 1130 . 182 TYR CA C 60.7 0.1 1 1131 . 182 TYR CB C 35.5 0.1 1 1132 . 183 SER H H 8.48 0.01 1 1133 . 183 SER HA H 3.81 0.01 1 1134 . 183 SER HB2 H 3.61 0.01 2 1135 . 183 SER N N 117.1 0.1 1 1136 . 183 SER CA C 59.8 0.1 1 1137 . 183 SER CB C 63.6 0.1 1 1138 . 184 LYS H H 7.50 0.01 1 1139 . 184 LYS HA H 4.13 0.01 1 1140 . 184 LYS HB2 H 1.85 0.01 1 1141 . 184 LYS HB3 H 1.85 0.01 1 1142 . 184 LYS N N 123.3 0.1 1 1143 . 184 LYS CA C 56.7 0.1 1 1144 . 184 LYS CB C 28.9 0.1 1 1145 . 185 GLU H H 8.00 0.01 1 1146 . 185 GLU HA H 3.99 0.01 1 1147 . 185 GLU HB2 H 2.07 0.01 2 1148 . 185 GLU HB3 H 2.24 0.01 2 1149 . 185 GLU N N 120.7 0.1 1 1150 . 185 GLU CA C 56.4 0.1 1 1151 . 185 GLU CB C 27.8 0.1 1 1152 . 186 ALA H H 8.38 0.01 1 1153 . 186 ALA HA H 4.66 0.01 1 1154 . 186 ALA HB H 1.64 0.01 1 1155 . 186 ALA N N 122.8 0.1 1 1156 . 186 ALA CA C 52.0 0.1 1 1157 . 186 ALA CB C 17.2 0.1 1 1158 . 187 GLU H H 8.01 0.01 1 1159 . 187 GLU HA H 4.13 0.01 1 1160 . 187 GLU HB2 H 2.22 0.01 1 1161 . 187 GLU HB3 H 2.22 0.01 1 1162 . 187 GLU N N 122.0 0.1 1 1163 . 187 GLU CA C 56.8 0.1 1 1164 . 187 GLU CB C 27.0 0.1 1 1165 . 188 ALA H H 7.54 0.01 1 1166 . 188 ALA HA H 4.36 0.01 1 1167 . 188 ALA HB H 1.48 0.01 1 1168 . 188 ALA N N 118.8 0.1 1 1169 . 188 ALA CA C 50.0 0.1 1 1170 . 188 ALA CB C 17.3 0.1 1 1171 . 189 GLY H H 7.86 0.01 1 1172 . 189 GLY HA2 H 4.26 0.01 2 1173 . 189 GLY HA3 H 3.89 0.01 2 1174 . 189 GLY N N 105.6 0.1 1 1175 . 189 GLY CA C 43.2 0.1 1 1176 . 190 ASN H H 8.18 0.01 1 1177 . 190 ASN HA H 4.73 0.01 1 1178 . 190 ASN HB2 H 2.97 0.01 1 1179 . 190 ASN HB3 H 2.69 0.01 1 1180 . 190 ASN HD21 H 6.87 0.01 2 1181 . 190 ASN HD22 H 7.85 0.01 2 1182 . 190 ASN N N 117.3 0.1 1 1183 . 190 ASN ND2 N 113.5 0.1 1 1184 . 190 ASN CA C 51.8 0.1 1 1185 . 190 ASN CB C 37.4 0.1 1 1186 . 191 THR H H 7.57 0.01 1 1187 . 191 THR HA H 4.27 0.01 1 1188 . 191 THR HB H 4.10 0.01 1 1189 . 191 THR N N 113.2 0.1 1 1190 . 191 THR CA C 58.7 0.1 1 1191 . 191 THR CB C 66.6 0.1 1 1192 . 192 LYS H H 7.90 0.01 1 1193 . 192 LYS HA H 4.36 0.01 1 1194 . 192 LYS N N 122.8 0.1 1 1195 . 192 LYS CA C 53.5 0.1 1 1196 . 192 LYS CB C 32.1 0.1 1 1197 . 193 TYR H H 8.29 0.01 1 1198 . 193 TYR HA H 5.76 0.01 1 1199 . 193 TYR HB2 H 2.78 0.01 2 1200 . 193 TYR HB3 H 2.72 0.01 2 1201 . 193 TYR HD1 H 6.87 0.01 1 1202 . 193 TYR HD2 H 6.87 0.01 1 1203 . 193 TYR HE1 H 6.69 0.01 1 1204 . 193 TYR HE2 H 6.69 0.01 1 1205 . 193 TYR N N 124.0 0.1 1 1206 . 193 TYR CA C 53.5 0.1 1 1207 . 193 TYR CB C 39.8 0.1 1 1208 . 194 ALA H H 8.37 0.01 1 1209 . 194 ALA HA H 4.30 0.01 1 1210 . 194 ALA HB H 1.26 0.01 1 1211 . 194 ALA N N 130.2 0.1 1 1212 . 194 ALA CA C 49.3 0.1 1 1213 . 194 ALA CB C 20.3 0.1 1 1214 . 195 LYS H H 8.28 0.01 1 1215 . 195 LYS HA H 4.96 0.01 1 1216 . 195 LYS HB2 H 1.83 0.01 2 1217 . 195 LYS HB3 H 1.75 0.01 2 1218 . 195 LYS HG2 H 1.38 0.01 2 1219 . 195 LYS N N 122.4 0.1 1 1220 . 195 LYS CA C 52.6 0.1 1 1221 . 195 LYS CB C 31.7 0.1 1 1222 . 196 VAL H H 9.16 0.01 1 1223 . 196 VAL HA H 4.27 0.01 1 1224 . 196 VAL HB H 1.83 0.01 1 1225 . 196 VAL HG1 H 0.76 0.01 2 1226 . 196 VAL HG2 H 0.66 0.01 2 1227 . 196 VAL N N 126.0 0.1 1 1228 . 196 VAL CA C 57.8 0.1 1 1229 . 196 VAL CB C 32.1 0.1 1 1230 . 197 ASP H H 8.77 0.01 1 1231 . 197 ASP HA H 4.67 0.01 1 1232 . 197 ASP HB2 H 2.94 0.01 2 1233 . 197 ASP N N 125.0 0.1 1 1234 . 197 ASP CA C 50.7 0.1 1 1235 . 197 ASP CB C 37.8 0.1 1 1236 . 198 GLY H H 8.39 0.01 1 1237 . 198 GLY HA2 H 3.80 0.01 2 1238 . 198 GLY HA3 H 2.74 0.01 2 1239 . 198 GLY N N 112.1 0.1 1 1240 . 198 GLY CA C 44.0 0.1 1 1241 . 199 THR H H 8.72 0.01 1 1242 . 199 THR HA H 4.27 0.01 1 1243 . 199 THR N N 111.7 0.1 1 1244 . 199 THR CA C 60.5 0.1 1 1245 . 199 THR CB C 67.0 0.1 1 1246 . 200 LYS H H 6.61 0.01 1 1247 . 200 LYS HA H 4.40 0.01 1 1248 . 200 LYS HB2 H 1.66 0.01 2 1249 . 200 LYS N N 121.8 0.1 1 1250 . 200 LYS CA C 53.0 0.1 1 1251 . 200 LYS CB C 29.5 0.1 1 1252 . 201 PRO HA H 4.51 0.01 1 1253 . 201 PRO HB2 H 1.76 0.01 2 1254 . 201 PRO CA C 60.7 0.1 1 1255 . 201 PRO CB C 30.0 0.1 1 1256 . 202 VAL H H 8.44 0.01 1 1257 . 202 VAL HA H 3.53 0.01 1 1258 . 202 VAL HB H 2.03 0.01 1 1259 . 202 VAL HG1 H 0.85 0.01 1 1260 . 202 VAL HG2 H 0.85 0.01 1 1261 . 202 VAL N N 123.3 0.1 1 1262 . 202 VAL CA C 64.8 0.1 1 1263 . 202 VAL CB C 29.5 0.1 1 1264 . 203 ALA H H 8.82 0.01 1 1265 . 203 ALA HA H 3.95 0.01 1 1266 . 203 ALA HB H 1.40 0.01 1 1267 . 203 ALA N N 119.6 0.1 1 1268 . 203 ALA CA C 52.8 0.1 1 1269 . 203 ALA CB C 16.8 0.1 1 1270 . 204 GLU H H 7.47 0.01 1 1271 . 204 GLU HA H 4.15 0.01 1 1272 . 204 GLU N N 117.7 0.1 1 1273 . 204 GLU CA C 56.2 0.1 1 1274 . 204 GLU CB C 27.8 0.1 1 1275 . 205 VAL H H 7.93 0.01 1 1276 . 205 VAL HA H 3.69 0.01 1 1277 . 205 VAL HB H 2.03 0.01 1 1278 . 205 VAL HG1 H 1.03 0.01 2 1279 . 205 VAL HG2 H 0.90 0.01 2 1280 . 205 VAL N N 121.4 0.1 1 1281 . 205 VAL CA C 64.2 0.1 1 1282 . 205 VAL CB C 29.9 0.1 1 1283 . 206 ARG H H 7.97 0.01 1 1284 . 206 ARG HA H 3.60 0.01 1 1285 . 206 ARG HB2 H 1.56 0.01 2 1286 . 206 ARG HB3 H 1.38 0.01 2 1287 . 206 ARG N N 118.2 0.1 1 1288 . 206 ARG CA C 57.4 0.1 1 1289 . 206 ARG CB C 27.4 0.1 1 1290 . 207 ALA H H 7.28 0.01 1 1291 . 207 ALA HA H 4.18 0.01 1 1292 . 207 ALA HB H 1.51 0.01 1 1293 . 207 ALA N N 120.5 0.1 1 1294 . 207 ALA CA C 52.5 0.1 1 1295 . 207 ALA CB C 16.2 0.1 1 1296 . 208 ASP H H 8.23 0.01 1 1297 . 208 ASP HA H 4.43 0.01 1 1298 . 208 ASP HB2 H 3.03 0.01 2 1299 . 208 ASP HB3 H 2.54 0.01 2 1300 . 208 ASP N N 121.2 0.1 1 1301 . 208 ASP CA C 55.3 0.1 1 1302 . 208 ASP CB C 37.4 0.1 1 1303 . 209 LEU H H 8.54 0.01 1 1304 . 209 LEU HA H 3.96 0.01 1 1305 . 209 LEU HB2 H 2.31 0.01 2 1306 . 209 LEU HB3 H 1.35 0.01 2 1307 . 209 LEU N N 120.5 0.1 1 1308 . 209 LEU CA C 55.6 0.1 1 1309 . 209 LEU CB C 40.0 0.1 1 1310 . 210 GLU H H 8.42 0.01 1 1311 . 210 GLU HA H 4.19 0.01 1 1312 . 210 GLU HB2 H 2.24 0.01 2 1313 . 210 GLU HB3 H 2.05 0.01 2 1314 . 210 GLU N N 118.8 0.1 1 1315 . 210 GLU CA C 57.0 0.1 1 1316 . 210 GLU CB C 27.4 0.1 1 1317 . 211 LYS H H 7.70 0.01 1 1318 . 211 LYS HA H 4.12 0.01 1 1319 . 211 LYS HB2 H 1.99 0.01 1 1320 . 211 LYS HB3 H 1.99 0.01 1 1321 . 211 LYS N N 118.9 0.1 1 1322 . 211 LYS CA C 56.3 0.1 1 1323 . 211 LYS CB C 30.0 0.1 1 1324 . 212 ILE H H 7.64 0.01 1 1325 . 212 ILE HA H 3.72 0.01 1 1326 . 212 ILE HB H 1.63 0.01 1 1327 . 212 ILE N N 119.2 0.1 1 1328 . 212 ILE CA C 62.2 0.1 1 1329 . 212 ILE CB C 37.4 0.1 1 1330 . 213 LEU H H 8.14 0.01 1 1331 . 213 LEU HA H 3.69 0.01 1 1332 . 213 LEU HB2 H 1.83 0.01 2 1333 . 213 LEU HB3 H 0.91 0.01 2 1334 . 213 LEU HG H 1.37 0.01 1 1335 . 213 LEU HD1 H -0.12 0.01 1 1336 . 213 LEU HD2 H 0.56 0.01 1 1337 . 213 LEU N N 117.3 0.1 1 1338 . 213 LEU CA C 53.5 0.1 1 1339 . 213 LEU CB C 39.1 0.1 1 1340 . 214 GLY H H 7.68 0.01 1 1341 . 214 GLY HA2 H 3.99 0.01 2 1342 . 214 GLY HA3 H 3.72 0.01 2 1343 . 214 GLY N N 112.6 0.1 1 1344 . 214 GLY CA C 44.1 0.1 1 stop_ save_