data_4720 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-2-- a Protein Inhibitor of Protein Phosphatase-1 ; _BMRB_accession_number 4720 _BMRB_flat_file_name bmr4720.str _Entry_type original _Submission_date 2000-04-13 _Accession_date 2000-04-17 _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 Huang Hsien-bin . . 2 Chen Yi-Chen . . 3 Tsai Li-huang . . 4 Wang Hui-chun . . 5 Lin Fang-Min . . 6 Horiuchi Atsuko . . 7 Greengard Paul . . 8 Nairn Angus C. . 9 Shiao Ming-Shi . . 10 Lin Ta-Hsien . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 605 "13C chemical shifts" 509 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-09-26 original author 'Original release' 2007-03-23 update BMRB 'Links to related BMRB entries inserted' stop_ loop_ _Related_BMRB_accession_number _Relationship 15179 'Inhibitor-2 residues 9 - 164' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-2-- a Protein Inhibitor of Protein Phosphatase-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20466532 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Hsien-bin . . 2 Chen Yi-Chen . . 3 Tsai Li-huang . . 4 Wang Hui-chun . . 5 Lin Fang-Min . . 6 Horiuchi Atsuko . . 7 Greengard Paul . . 8 Nairn Angus C. . 9 Shiao Ming-Shi . . 10 Lin Ta-Hsien . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 359 _Page_last 360 _Year 2000 _Details . loop_ _Keyword 'heteronuclear NMR' inhibitor-2 phosphorylation 'protein phosphatase-1' stop_ save_ ################################## # Molecular system description # ################################## save_system_I2 _Saveframe_category molecular_system _Mol_system_name 'Inhibitor-2 monomer' _Abbreviation_common I2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label inhibitor-2 $inhibitor-2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_inhibitor-2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Inhibitor-2 _Abbreviation_common I2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; MAASTASHRPIKGILKNKTS TTSSMVASAEQPRGNVDEEL SKKSQKWDEMNILATYHPAD KDYGLMKIDEPSTPYHSMMG DDEDACSDTEATEAMAPDIL ARKLAAAEGLEPKYRIQEQE SSGEEDSDLSPEEREKKRQF EMKRKLHYNEGLNIKLARQL ISKDLHDDDEDEE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ALA 4 SER 5 THR 6 ALA 7 SER 8 HIS 9 ARG 10 PRO 11 ILE 12 LYS 13 GLY 14 ILE 15 LEU 16 LYS 17 ASN 18 LYS 19 THR 20 SER 21 THR 22 THR 23 SER 24 SER 25 MET 26 VAL 27 ALA 28 SER 29 ALA 30 GLU 31 GLN 32 PRO 33 ARG 34 GLY 35 ASN 36 VAL 37 ASP 38 GLU 39 GLU 40 LEU 41 SER 42 LYS 43 LYS 44 SER 45 GLN 46 LYS 47 TRP 48 ASP 49 GLU 50 MET 51 ASN 52 ILE 53 LEU 54 ALA 55 THR 56 TYR 57 HIS 58 PRO 59 ALA 60 ASP 61 LYS 62 ASP 63 TYR 64 GLY 65 LEU 66 MET 67 LYS 68 ILE 69 ASP 70 GLU 71 PRO 72 SER 73 THR 74 PRO 75 TYR 76 HIS 77 SER 78 MET 79 MET 80 GLY 81 ASP 82 ASP 83 GLU 84 ASP 85 ALA 86 CYS 87 SER 88 ASP 89 THR 90 GLU 91 ALA 92 THR 93 GLU 94 ALA 95 MET 96 ALA 97 PRO 98 ASP 99 ILE 100 LEU 101 ALA 102 ARG 103 LYS 104 LEU 105 ALA 106 ALA 107 ALA 108 GLU 109 GLY 110 LEU 111 GLU 112 PRO 113 LYS 114 TYR 115 ARG 116 ILE 117 GLN 118 GLU 119 GLN 120 GLU 121 SER 122 SER 123 GLY 124 GLU 125 GLU 126 ASP 127 SER 128 ASP 129 LEU 130 SER 131 PRO 132 GLU 133 GLU 134 ARG 135 GLU 136 LYS 137 LYS 138 ARG 139 GLN 140 PHE 141 GLU 142 MET 143 LYS 144 ARG 145 LYS 146 LEU 147 HIS 148 TYR 149 ASN 150 GLU 151 GLY 152 LEU 153 ASN 154 ILE 155 LYS 156 LEU 157 ALA 158 ARG 159 GLN 160 LEU 161 ILE 162 SER 163 LYS 164 ASP 165 LEU 166 HIS 167 ASP 168 ASP 169 ASP 170 GLU 171 ASP 172 GLU 173 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 15179 Inhibitor-2 91.33 159 99.37 99.37 1.12e-109 DBJ BAI46858 "protein phosphatase 1, regulatory (inhibitor) subunit 2 [synthetic construct]" 100.00 205 100.00 100.00 6.22e-122 EMBL CAA55475 "inhibitor 2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 EMBL CAA82754 "IPP-2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 EMBL CAB41680 "inhibitor 2 of protein phosphatase 1 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 GB AAC51206 "protein phosphatase inhibitor 2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 GB AAH07655 "Protein phosphatase 1, regulatory (inhibitor) subunit 2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 GB AAL48322 "inhibitor-2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 GB ABW23430 "cardiac inhibitor-2 [Canis lupus familiaris]" 100.00 205 99.42 99.42 3.31e-121 GB ADQ32784 "protein phosphatase 1, regulatory (inhibitor) subunit 2 [synthetic construct]" 100.00 205 100.00 100.00 6.22e-122 PRF 2007253A "protein phosphatase inhibitor 2" 100.00 205 100.00 100.00 6.22e-122 REF NP_001247610 "protein phosphatase inhibitor 2 [Macaca mulatta]" 100.00 205 98.27 99.42 4.86e-120 REF NP_001278433 "protein phosphatase inhibitor 2 isoform 1 [Homo sapiens]" 100.58 206 98.85 99.43 1.64e-119 REF NP_001303254 "protein phosphatase inhibitor 2 isoform 4 [Homo sapiens]" 57.80 185 98.00 98.00 8.83e-60 REF NP_006232 "protein phosphatase inhibitor 2 isoform 2 [Homo sapiens]" 100.00 205 100.00 100.00 6.22e-122 REF XP_002814482 "PREDICTED: protein phosphatase inhibitor 2 [Pongo abelii]" 100.00 205 98.84 99.42 9.04e-121 SP P41236 "RecName: Full=Protein phosphatase inhibitor 2; Short=IPP-2" 100.00 205 100.00 100.00 6.22e-122 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Plasmid $inhibitor-2 'E. coli' 562 Eubacteria . Escherichia coli BL21 pET3a 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 $inhibitor-2 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET-3a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample-1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $inhibitor-2 1.6 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_exp1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 296 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_cs_set1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample-1 stop_ _Sample_conditions_label $exp1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name inhibitor-2 _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 ALA HA H 4.041 0.02 1 2 . 2 ALA HB H 1.462 0.02 1 3 . 2 ALA C C 173.418 0.15 1 4 . 2 ALA CA C 51.562 0.15 1 5 . 2 ALA CB C 19.252 0.15 1 6 . 3 ALA H H 8.600 0.02 1 7 . 3 ALA HA H 4.314 0.02 1 8 . 3 ALA HB H 1.345 0.02 1 9 . 3 ALA C C 177.659 0.15 1 10 . 3 ALA CA C 52.328 0.15 1 11 . 3 ALA CB C 19.252 0.15 1 12 . 3 ALA N N 123.690 0.15 1 13 . 4 SER H H 8.447 0.02 1 14 . 4 SER HA H 4.431 0.02 1 15 . 4 SER HB2 H 3.845 0.02 1 16 . 4 SER HB3 H 3.845 0.02 1 17 . 4 SER C C 174.943 0.15 1 18 . 4 SER CA C 58.125 0.15 1 19 . 4 SER CB C 63.568 0.15 1 20 . 4 SER N N 115.627 0.15 1 21 . 5 THR H H 8.166 0.02 1 22 . 5 THR HA H 4.275 0.02 1 23 . 5 THR HB H 4.002 0.02 1 24 . 5 THR C C 174.289 0.15 1 25 . 5 THR CA C 61.625 0.15 1 26 . 5 THR CB C 69.471 0.15 1 27 . 5 THR N N 115.814 0.15 1 28 . 6 ALA H H 8.207 0.02 1 29 . 6 ALA HA H 4.275 0.02 1 30 . 6 ALA HB H 1.306 0.02 1 31 . 6 ALA C C 177.542 0.15 1 32 . 6 ALA CA C 52.546 0.15 1 33 . 6 ALA CB C 19.106 0.15 1 34 . 6 ALA N N 126.034 0.15 1 35 . 7 SER H H 8.142 0.02 1 36 . 7 SER HA H 4.311 0.02 1 37 . 7 SER HB2 H 3.741 0.02 1 38 . 7 SER HB3 H 3.741 0.02 1 39 . 7 SER C C 174.188 0.15 1 40 . 7 SER CA C 58.234 0.15 1 41 . 7 SER CB C 63.495 0.15 1 42 . 7 SER N N 114.689 0.15 1 43 . 8 HIS H H 8.383 0.02 1 44 . 8 HIS HA H 4.627 0.02 1 45 . 8 HIS HB2 H 3.142 0.02 1 46 . 8 HIS HB3 H 3.142 0.02 1 47 . 8 HIS C C 173.999 0.15 1 48 . 8 HIS CA C 55.063 0.15 1 49 . 8 HIS CB C 28.946 0.15 1 50 . 8 HIS N N 120.315 0.15 1 51 . 9 ARG H H 8.295 0.02 1 52 . 9 ARG HA H 4.546 0.02 1 53 . 9 ARG C C 173.970 0.15 1 54 . 9 ARG CA C 54.078 0.15 1 55 . 9 ARG CB C 29.893 0.15 1 56 . 9 ARG N N 123.503 0.15 1 57 . 10 PRO HA H 4.395 0.02 1 58 . 10 PRO HB2 H 2.205 0.02 1 59 . 10 PRO HB3 H 2.205 0.02 1 60 . 10 PRO HG2 H 1.775 0.02 1 61 . 10 PRO HG3 H 1.775 0.02 1 62 . 10 PRO C C 176.599 0.15 1 63 . 10 PRO CA C 62.938 0.15 1 64 . 10 PRO CB C 31.788 0.15 1 65 . 11 ILE H H 8.230 0.02 1 66 . 11 ILE HA H 4.041 0.02 1 67 . 11 ILE HB H 1.775 0.02 1 68 . 11 ILE C C 176.192 0.15 1 69 . 11 ILE CA C 60.969 0.15 1 70 . 11 ILE CB C 38.640 0.15 1 71 . 11 ILE N N 121.628 0.15 1 72 . 12 LYS H H 8.318 0.02 1 73 . 12 LYS HA H 4.236 0.02 1 74 . 12 LYS HB2 H 1.736 0.02 1 75 . 12 LYS HB3 H 1.736 0.02 1 76 . 12 LYS C C 176.626 0.15 1 77 . 12 LYS CA C 56.265 0.15 1 78 . 12 LYS CB C 33.028 0.15 1 79 . 12 LYS N N 125.378 0.15 1 80 . 13 GLY H H 8.324 0.02 1 81 . 13 GLY HA2 H 3.884 0.02 1 82 . 13 GLY HA3 H 3.884 0.02 1 83 . 13 GLY C C 173.694 0.15 1 84 . 13 GLY CA C 45.109 0.15 1 85 . 13 GLY N N 110.751 0.15 1 86 . 14 ILE H H 7.913 0.02 1 87 . 14 ILE HA H 4.119 0.02 1 88 . 14 ILE HB H 1.775 0.02 1 89 . 14 ILE C C 176.279 0.15 1 90 . 14 ILE CA C 60.969 0.15 1 91 . 14 ILE CB C 38.567 0.15 1 92 . 14 ILE N N 119.752 0.15 1 93 . 15 LEU H H 8.254 0.02 1 94 . 15 LEU HA H 4.275 0.02 1 95 . 15 LEU HB2 H 1.541 0.02 1 96 . 15 LEU HB3 H 1.541 0.02 1 97 . 15 LEU C C 176.962 0.15 1 98 . 15 LEU CA C 54.953 0.15 1 99 . 15 LEU CB C 41.920 0.15 1 100 . 15 LEU N N 126.128 0.15 1 101 . 16 LYS H H 8.242 0.02 1 102 . 16 LYS HA H 4.236 0.02 1 103 . 16 LYS HB2 H 1.736 0.02 1 104 . 16 LYS HB3 H 1.736 0.02 1 105 . 16 LYS C C 176.046 0.15 1 106 . 16 LYS CA C 56.156 0.15 1 107 . 16 LYS CB C 32.663 0.15 1 108 . 16 LYS N N 122.471 0.15 1 109 . 17 ASN H H 8.318 0.02 1 110 . 17 ASN HA H 4.587 0.02 1 111 . 17 ASN HB2 H 2.752 0.02 1 112 . 17 ASN HB3 H 2.752 0.02 1 113 . 17 ASN C C 175.001 0.15 1 114 . 17 ASN CA C 52.984 0.15 1 115 . 17 ASN CB C 38.786 0.15 1 116 . 17 ASN N N 119.659 0.15 1 117 . 18 LYS H H 8.295 0.02 1 118 . 18 LYS HA H 4.275 0.02 1 119 . 18 LYS HB2 H 1.775 0.02 1 120 . 18 LYS HB3 H 1.775 0.02 1 121 . 18 LYS C C 176.671 0.15 1 122 . 18 LYS CA C 56.484 0.15 1 123 . 18 LYS CB C 32.882 0.15 1 124 . 18 LYS N N 121.721 0.15 1 125 . 19 THR H H 8.148 0.02 1 126 . 19 THR HA H 4.353 0.02 1 127 . 19 THR C C 174.449 0.15 1 128 . 19 THR CA C 61.735 0.15 1 129 . 19 THR CB C 69.617 0.15 1 130 . 19 THR N N 115.064 0.15 1 131 . 20 SER H H 8.318 0.02 1 132 . 20 SER HA H 4.470 0.02 1 133 . 20 SER HB2 H 3.845 0.02 1 134 . 20 SER HB3 H 3.845 0.02 1 135 . 20 SER C C 174.689 0.15 1 136 . 20 SER CA C 58.276 0.15 1 137 . 20 SER CB C 63.591 0.15 1 138 . 20 SER N N 118.065 0.15 1 139 . 21 THR H H 8.236 0.02 1 140 . 21 THR HA H 4.392 0.02 1 141 . 21 THR HB H 4.242 0.02 1 142 . 21 THR HG2 H 1.167 0.02 1 143 . 21 THR C C 174.696 0.15 1 144 . 21 THR CA C 61.735 0.15 1 145 . 21 THR CB C 69.471 0.15 1 146 . 21 THR N N 115.814 0.15 1 147 . 22 THR H H 8.119 0.02 1 148 . 22 THR HA H 4.343 0.02 1 149 . 22 THR HB H 4.199 0.02 1 150 . 22 THR HG2 H 1.156 0.02 1 151 . 22 THR C C 174.798 0.15 1 152 . 22 THR CA C 61.844 0.15 1 153 . 22 THR CB C 69.471 0.15 1 154 . 22 THR N N 115.908 0.15 1 155 . 23 SER H H 8.283 0.02 1 156 . 23 SER HA H 4.431 0.02 1 157 . 23 SER HB2 H 3.845 0.02 1 158 . 23 SER HB3 H 3.845 0.02 1 159 . 23 SER C C 174.598 0.15 1 160 . 23 SER CA C 58.453 0.15 1 161 . 23 SER CB C 63.568 0.15 1 162 . 23 SER N N 118.065 0.15 1 163 . 24 SER H H 8.283 0.02 1 164 . 24 SER HA H 4.387 0.02 1 165 . 24 SER HB2 H 3.817 0.02 1 166 . 24 SER HB3 H 3.817 0.02 1 167 . 24 SER C C 174.318 0.15 1 168 . 24 SER CA C 58.453 0.15 1 169 . 24 SER CB C 63.568 0.15 1 170 . 24 SER N N 117.596 0.15 1 171 . 25 MET H H 8.242 0.02 1 172 . 25 MET HA H 4.431 0.02 1 173 . 25 MET HB2 H 1.970 0.02 1 174 . 25 MET HB3 H 1.970 0.02 1 175 . 25 MET C C 175.989 0.15 1 176 . 25 MET CA C 55.609 0.15 1 177 . 25 MET CB C 32.444 0.15 1 178 . 25 MET N N 122.096 0.15 1 179 . 26 VAL H H 7.972 0.02 1 180 . 26 VAL HA H 4.041 0.02 1 181 . 26 VAL HB H 1.970 0.02 1 182 . 26 VAL C C 175.727 0.15 1 183 . 26 VAL CA C 62.172 0.15 1 184 . 26 VAL CB C 32.590 0.15 1 185 . 26 VAL N N 121.065 0.15 1 186 . 27 ALA H H 8.318 0.02 1 187 . 27 ALA HA H 4.275 0.02 1 188 . 27 ALA HB H 1.345 0.02 1 189 . 27 ALA C C 177.610 0.15 1 190 . 27 ALA CA C 52.437 0.15 1 191 . 27 ALA CB C 19.033 0.15 1 192 . 27 ALA N N 127.722 0.15 1 193 . 28 SER H H 8.171 0.02 1 194 . 28 SER HA H 4.353 0.02 1 195 . 28 SER HB2 H 3.806 0.02 1 196 . 28 SER HB3 H 3.806 0.02 1 197 . 28 SER C C 174.289 0.15 1 198 . 28 SER CA C 58.234 0.15 1 199 . 28 SER CB C 63.568 0.15 1 200 . 28 SER N N 115.064 0.15 1 201 . 29 ALA H H 8.265 0.02 1 202 . 29 ALA HA H 4.274 0.02 1 203 . 29 ALA HB H 1.337 0.02 1 204 . 29 ALA C C 177.470 0.15 1 205 . 29 ALA CA C 52.437 0.15 1 206 . 29 ALA CB C 19.106 0.15 1 207 . 29 ALA N N 125.625 0.15 1 208 . 30 GLU H H 8.183 0.02 1 209 . 30 GLU HA H 4.210 0.02 1 210 . 30 GLU HB2 H 1.931 0.02 1 211 . 30 GLU HB3 H 1.931 0.02 1 212 . 30 GLU C C 176.105 0.15 1 213 . 30 GLU CA C 56.156 0.15 1 214 . 30 GLU CB C 30.112 0.15 1 215 . 30 GLU N N 119.471 0.15 1 216 . 31 GLN H H 8.236 0.02 1 217 . 31 GLN HA H 4.530 0.02 1 218 . 31 GLN C C 173.781 0.15 1 219 . 31 GLN CA C 53.422 0.15 1 220 . 31 GLN CB C 28.727 0.15 1 221 . 31 GLN N N 122.378 0.15 1 222 . 32 PRO HA H 4.353 0.02 1 223 . 32 PRO HB2 H 2.244 0.02 1 224 . 32 PRO HB3 H 2.244 0.02 1 225 . 32 PRO HG2 H 1.853 0.02 1 226 . 32 PRO HG3 H 1.853 0.02 1 227 . 32 PRO C C 176.874 0.15 1 228 . 32 PRO CA C 63.047 0.15 1 229 . 32 PRO CB C 31.861 0.15 1 230 . 33 ARG H H 8.453 0.02 1 231 . 33 ARG HA H 4.275 0.02 1 232 . 33 ARG HB2 H 1.775 0.02 1 233 . 33 ARG HB3 H 1.775 0.02 1 234 . 33 ARG C C 176.744 0.15 1 235 . 33 ARG CA C 55.937 0.15 1 236 . 33 ARG CB C 30.768 0.15 1 237 . 33 ARG N N 121.534 0.15 1 238 . 34 GLY H H 8.342 0.02 1 239 . 34 GLY HA2 H 3.884 0.02 1 240 . 34 GLY HA3 H 3.884 0.02 1 241 . 34 GLY C C 173.549 0.15 1 242 . 34 GLY CA C 44.999 0.15 1 243 . 34 GLY N N 109.439 0.15 1 244 . 35 ASN H H 8.336 0.02 1 245 . 35 ASN HA H 4.666 0.02 1 246 . 35 ASN HB2 H 2.712 0.02 1 247 . 35 ASN HB3 H 2.712 0.02 1 248 . 35 ASN C C 175.371 0.15 1 249 . 35 ASN CA C 53.093 0.15 1 250 . 35 ASN CB C 38.713 0.15 1 251 . 35 ASN N N 118.815 0.15 1 252 . 36 VAL H H 8.089 0.02 1 253 . 36 VAL HA H 4.002 0.02 1 254 . 36 VAL HB H 2.048 0.02 1 255 . 36 VAL C C 175.872 0.15 1 256 . 36 VAL CA C 62.610 0.15 1 257 . 36 VAL CB C 32.444 0.15 1 258 . 36 VAL N N 120.127 0.15 1 259 . 37 ASP H H 8.283 0.02 1 260 . 37 ASP HA H 4.524 0.02 1 261 . 37 ASP HB2 H 2.556 0.02 1 262 . 37 ASP HB3 H 2.556 0.02 1 263 . 37 ASP C C 176.689 0.15 1 264 . 37 ASP CA C 54.734 0.15 1 265 . 37 ASP CB C 40.754 0.15 1 266 . 37 ASP N N 122.94 0.15 1 267 . 38 GLU H H 8.283 0.15 1 268 . 38 GLU HA H 4.158 0.15 1 269 . 38 GLU HB2 H 1.970 0.02 1 270 . 38 GLU HB3 H 1.970 0.02 1 271 . 38 GLU C C 177.049 0.15 1 272 . 38 GLU CA C 57.389 0.15 1 273 . 38 GLU CB C 29.966 0.15 1 274 . 38 GLU N N 121.909 0.15 1 275 . 39 GLU H H 8.301 0.02 1 276 . 39 GLU HA H 4.119 0.02 1 277 . 39 GLU HB2 H 1.970 0.02 1 278 . 39 GLU HB3 H 1.970 0.02 1 279 . 39 GLU C C 177.397 0.15 1 280 . 39 GLU CA C 57.316 0.15 1 281 . 39 GLU CB C 29.564 0.15 1 282 . 39 GLU N N 120.596 0.15 1 283 . 40 LEU H H 8.060 0.02 1 284 . 40 LEU HA H 4.158 0.02 1 285 . 40 LEU HB2 H 1.580 0.02 1 286 . 40 LEU HB3 H 1.580 0.02 1 287 . 40 LEU C C 178.211 0.15 1 288 . 40 LEU CA C 56.105 0.15 1 289 . 40 LEU CB C 41.774 0.15 1 290 . 40 LEU N N 121.534 0.15 1 291 . 41 SER H H 8.078 0.02 1 292 . 41 SER HA H 4.275 0.02 1 293 . 41 SER HB2 H 3.845 0.02 1 294 . 41 SER HB3 H 3.845 0.02 1 295 . 41 SER C C 175.074 0.15 1 296 . 41 SER CA C 59.109 0.15 1 297 . 41 SER CB C 63.203 0.15 1 298 . 41 SER N N 115.158 0.15 1 299 . 42 LYS H H 7.960 0.02 1 300 . 42 LYS HA H 4.200 0.02 1 301 . 42 LYS HB2 H 1.770 0.02 1 302 . 42 LYS HB3 H 1.770 0.02 1 303 . 42 LYS C C 176.962 0.15 1 304 . 42 LYS CA C 56.812 0.15 1 305 . 42 LYS CB C 32.560 0.15 1 306 . 42 LYS N N 122.19 0.15 1 307 . 43 LYS H H 8.013 0.02 1 308 . 43 LYS HA H 4.236 0.02 1 309 . 43 LYS HB2 H 1.736 0.02 1 310 . 43 LYS HB3 H 1.736 0.02 1 311 . 43 LYS C C 176.758 0.15 1 312 . 43 LYS CA C 56.703 0.15 1 313 . 43 LYS CB C 32.517 0.15 1 314 . 43 LYS N N 120.878 0.15 1 315 . 44 SER H H 8.107 0.02 1 316 . 44 SER HA H 4.353 0.02 1 317 . 44 SER HB2 H 3.845 0.02 1 318 . 44 SER HB3 H 3.845 0.02 1 319 . 44 SER C C 174.567 0.15 1 320 . 44 SER CA C 58.563 0.15 1 321 . 44 SER CB C 63.422 0.15 1 322 . 44 SER N N 115.908 0.15 1 323 . 45 GLN H H 8.213 0.02 1 324 . 45 GLN HA H 4.210 0.02 1 325 . 45 GLN C C 175.930 0.15 1 326 . 45 GLN CA C 56.047 0.15 1 327 . 45 GLN CB C 29.029 0.15 1 328 . 45 GLN N N 122.003 0.15 1 329 . 46 LYS H H 8.142 0.02 1 330 . 46 LYS HA H 4.158 0.02 1 331 . 46 LYS HB2 H 1.658 0.02 1 332 . 46 LYS HB3 H 1.658 0.02 1 333 . 46 LYS C C 176.584 0.15 1 334 . 46 LYS CA C 56.300 0.15 1 335 . 46 LYS CB C 32.444 0.15 1 336 . 46 LYS N N 121.534 0.15 1 337 . 47 TRP H H 8.020 0.02 1 338 . 47 TRP HA H 4.525 0.02 1 339 . 47 TRP C C 176.264 0.15 1 340 . 47 TRP CA C 57.906 0.15 1 341 . 47 TRP CB C 29.237 0.15 1 342 . 47 TRP N N 121.721 0.15 1 343 . 48 ASP H H 8.113 0.02 1 344 . 48 ASP HA H 4.392 0.02 1 345 . 48 ASP HB2 H 2.478 0.02 1 346 . 48 ASP HB3 H 2.478 0.02 1 347 . 48 ASP C C 176.457 0.15 1 348 . 48 ASP CA C 54.524 0.15 1 349 . 48 ASP CB C 40.535 0.15 1 350 . 48 ASP N N 120.878 0.15 1 351 . 49 GLU H H 8.048 0.02 1 352 . 49 GLU HA H 4.050 0.02 1 353 . 49 GLU C C 176.799 0.15 1 354 . 49 GLU CA C 57.250 0.15 1 355 . 49 GLU CB C 29.602 0.15 1 356 . 49 GLU N N 120.315 0.15 1 357 . 50 MET H H 8.083 0.02 1 358 . 50 MET HA H 4.296 0.02 1 359 . 50 MET HB2 H 1.931 0.02 1 360 . 50 MET HB3 H 1.931 0.02 1 361 . 50 MET C C 176.323 0.15 1 362 . 50 MET CA C 56.047 0.15 1 363 . 50 MET CB C 32.299 0.15 1 364 . 50 MET N N 118.627 0.15 1 365 . 51 ASN H H 8.119 0.02 1 366 . 51 ASN HA H 4.509 0.02 1 367 . 51 ASN HB2 H 2.673 0.02 1 368 . 51 ASN HB3 H 2.673 0.02 1 369 . 51 ASN C C 175.408 0.15 1 370 . 51 ASN CA C 53.531 0.15 1 371 . 51 ASN CB C 38.494 0.15 1 372 . 51 ASN N N 118.909 0.15 1 373 . 52 ILE H H 7.979 0.02 1 374 . 52 ILE HA H 4.041 0.02 1 375 . 52 ILE HB H 1.814 0.02 1 376 . 52 ILE C C 176.511 0.15 1 377 . 52 ILE CA C 61.844 0.15 1 378 . 52 ILE CB C 38.414 0.15 1 379 . 52 ILE N N 120.596 0.15 1 380 . 53 LEU H H 8.066 0.02 1 381 . 53 LEU HA H 4.236 0.02 1 382 . 53 LEU HB2 H 1.541 0.02 1 383 . 53 LEU HB3 H 1.541 0.02 1 384 . 53 LEU C C 177.267 0.15 1 385 . 53 LEU CA C 55.390 0.15 1 386 . 53 LEU CB C 41.774 0.15 1 387 . 53 LEU N N 123.878 0.15 1 388 . 54 ALA H H 7.984 0.02 1 389 . 54 ALA HA H 4.236 0.02 1 390 . 54 ALA HB H 1.345 0.02 1 391 . 54 ALA C C 177.702 0.15 1 392 . 54 ALA CA C 52.765 0.15 1 393 . 54 ALA CB C 19.033 0.15 1 394 . 54 ALA N N 123.315 0.15 1 395 . 55 THR H H 7.784 0.02 1 396 . 55 THR HA H 4.178 0.02 1 397 . 55 THR HB H 4.158 0.02 1 398 . 55 THR C C 173.825 0.15 1 399 . 55 THR CA C 61.735 0.15 1 400 . 55 THR CB C 69.544 0.15 1 401 . 55 THR N N 111.595 0.15 1 402 . 56 TYR H H 7.954 0.02 1 403 . 56 TYR HA H 4.431 0.02 1 404 . 56 TYR HB2 H 2.869 0.02 1 405 . 56 TYR HB3 H 2.869 0.02 1 406 . 56 TYR C C 174.623 0.15 1 407 . 56 TYR CA C 57.687 0.15 1 408 . 56 TYR CB C 38.731 0.15 1 409 . 56 TYR N N 122.753 0.15 1 410 . 57 HIS H H 8.160 0.02 1 411 . 57 HIS HA H 4.787 0.02 1 412 . 57 HIS C C 171.501 0.15 1 413 . 57 HIS CA C 52.546 0.15 1 414 . 57 HIS CB C 28.727 0.15 1 415 . 57 HIS N N 122.753 0.15 1 416 . 58 PRO HA H 4.197 0.02 1 417 . 58 PRO HB2 H 2.205 0.02 1 418 . 58 PRO HB3 H 2.205 0.02 1 419 . 58 PRO HG2 H 1.853 0.02 1 420 . 58 PRO HG3 H 1.853 0.02 1 421 . 58 PRO C C 176.511 0.15 1 422 . 58 PRO CA C 63.047 0.15 1 423 . 58 PRO CB C 31.861 0.15 1 424 . 59 ALA H H 8.394 0.02 1 425 . 59 ALA HA H 4.237 0.02 1 426 . 59 ALA HB H 1.327 0.02 1 427 . 59 ALA C C 177.455 0.15 1 428 . 59 ALA CA C 52.437 0.15 1 429 . 59 ALA CB C 19.033 0.15 1 430 . 59 ALA N N 123.784 0.15 1 431 . 60 ASP H H 8.177 0.02 1 432 . 60 ASP HA H 4.470 0.02 1 433 . 60 ASP HB2 H 2.595 0.02 1 434 . 60 ASP HB3 H 2.595 0.02 1 435 . 60 ASP C C 176.221 0.15 1 436 . 60 ASP CA C 54.297 0.15 1 437 . 60 ASP CB C 40.899 0.15 1 438 . 60 ASP N N 119.096 0.15 1 439 . 61 LYS H H 8.066 0.02 1 440 . 61 LYS HA H 4.158 0.02 1 441 . 61 LYS HB2 H 1.580 0.02 1 442 . 61 LYS HB3 H 1.580 0.02 1 443 . 61 LYS C C 175.77 0.15 1 444 . 61 LYS CA C 56.375 0.15 1 445 . 61 LYS CB C 32.663 0.15 1 446 . 61 LYS N N 120.69 0.15 1 447 . 62 ASP H H 8.142 0.02 1 448 . 62 ASP HA H 4.509 0.02 1 449 . 62 ASP HB2 H 2.634 0.02 1 450 . 62 ASP HB3 H 2.517 0.02 1 451 . 62 ASP C C 176.021 0.15 1 452 . 62 ASP CA C 53.968 0.15 1 453 . 62 ASP CB C 40.681 0.15 1 454 . 62 ASP N N 120.221 0.15 1 455 . 63 TYR H H 8.025 0.02 1 456 . 63 TYR HA H 4.342 0.02 1 457 . 63 TYR HB2 H 3.025 0.02 1 458 . 63 TYR HB3 H 2.869 0.02 1 459 . 63 TYR C C 176.518 0.15 1 460 . 63 TYR CA C 58.672 0.15 1 461 . 63 TYR CB C 38.203 0.15 1 462 . 63 TYR N N 121.253 0.15 1 463 . 64 GLY H H 8.312 0.02 1 464 . 64 GLY C C 174.13 0.15 1 465 . 64 GLY CA C 45.437 0.15 1 466 . 64 GLY N N 109.626 0.15 1 467 . 65 LEU H H 7.819 0.02 1 468 . 65 LEU HA H 4.275 0.02 1 469 . 65 LEU HB2 H 1.526 0.02 1 470 . 65 LEU HB3 H 1.526 0.02 1 471 . 65 LEU C C 177.223 0.15 1 472 . 65 LEU CA C 55.127 0.15 1 473 . 65 LEU CB C 42.145 0.15 1 474 . 65 LEU N N 120.971 0.15 1 475 . 66 MET H H 8.148 0.02 1 476 . 66 MET HA H 4.353 0.02 1 477 . 66 MET HB2 H 1.970 0.02 1 478 . 66 MET HB3 H 1.970 0.02 1 479 . 66 MET C C 175.655 0.15 1 480 . 66 MET CA C 55.281 0.15 1 481 . 66 MET CB C 32.590 0.15 1 482 . 66 MET N N 120.409 0.15 1 483 . 67 LYS H H 8.189 0.02 1 484 . 67 LYS HA H 4.263 0.02 1 485 . 67 LYS C C 176.09 0.15 1 486 . 67 LYS CA C 56.047 0.15 1 487 . 67 LYS CB C 32.633 0.15 1 488 . 67 LYS N N 122.846 0.15 1 489 . 68 ILE H H 8.113 0.02 1 490 . 68 ILE HA H 4.119 0.02 1 491 . 68 ILE HB H 1.775 0.02 1 492 . 68 ILE C C 175.553 0.15 1 493 . 68 ILE CA C 60.860 0.15 1 494 . 68 ILE CB C 38.786 0.15 1 495 . 68 ILE N N 122.284 0.15 1 496 . 69 ASP H H 8.330 0.02 1 497 . 69 ASP HA H 4.548 0.02 1 498 . 69 ASP HB2 H 2.556 0.02 1 499 . 69 ASP HB3 H 2.556 0.02 1 500 . 69 ASP C C 175.35 0.15 1 501 . 69 ASP CA C 53.968 0.15 1 502 . 69 ASP CB C 40.899 0.15 1 503 . 69 ASP N N 124.065 0.15 1 504 . 70 GLU H H 8.101 0.02 1 505 . 70 GLU HA H 4.536 0.02 1 506 . 70 GLU C C 174.246 0.15 1 507 . 70 GLU CA C 54.078 0.15 1 508 . 70 GLU CB C 29.675 0.15 1 509 . 70 GLU N N 122.096 0.15 1 510 . 71 PRO HA H 4.353 0.02 1 511 . 71 PRO HB2 H 2.205 0.02 1 512 . 71 PRO HB3 H 2.205 0.02 1 513 . 71 PRO C C 176.816 0.15 1 514 . 71 PRO CA C 63.157 0.15 1 515 . 71 PRO CB C 31.861 0.15 1 516 . 72 SER H H 8.371 0.02 1 517 . 72 SER HA H 4.392 0.02 1 518 . 72 SER HB2 H 3.806 0.02 1 519 . 72 SER HB3 H 3.806 0.02 1 520 . 72 SER C C 174.246 0.15 1 521 . 72 SER CA C 58.234 0.15 1 522 . 72 SER CB C 63.786 0.15 1 523 . 72 SER N N 115.814 0.15 1 524 . 73 THR H H 8.042 0.02 1 525 . 73 THR HA H 4.552 0.02 1 526 . 73 THR HB H 4.256 0.02 1 527 . 73 THR C C 172.736 0.15 1 528 . 73 THR CA C 59.547 0.15 1 529 . 73 THR CB C 69.617 0.15 1 530 . 73 THR N N 117.596 0.15 1 531 . 74 PRO HA H 4.314 0.02 1 532 . 74 PRO HB2 H 2.127 0.02 1 533 . 74 PRO HB3 H 2.127 0.02 1 534 . 74 PRO C C 176.352 0.15 1 535 . 74 PRO CA C 63.157 0.15 1 536 . 74 PRO CB C 31.716 0.15 1 537 . 75 TYR H H 8.083 0.02 1 538 . 75 TYR HA H 4.408 0.02 1 539 . 75 TYR C C 175.364 0.15 1 540 . 75 TYR CA C 57.997 0.15 1 541 . 75 TYR CB C 38.567 0.15 1 542 . 75 TYR N N 120.502 0.15 1 543 . 76 HIS H H 8.113 0.02 1 544 . 76 HIS HA H 4.548 0.02 1 545 . 76 HIS HB2 H 3.064 0.02 1 546 . 76 HIS HB3 H 3.064 0.02 1 547 . 76 HIS C C 173.665 0.15 1 548 . 76 HIS CA C 54.895 0.15 1 549 . 76 HIS CB C 29.237 0.15 1 550 . 76 HIS N N 120.971 0.15 1 551 . 77 SER H H 8.295 0.02 1 552 . 77 SER HA H 4.314 0.02 1 553 . 77 SER HB2 H 3.806 0.02 1 554 . 77 SER HB3 H 3.806 0.02 1 555 . 77 SER C C 174.522 0.15 1 556 . 77 SER CA C 58.276 0.15 1 557 . 77 SER CB C 63.495 0.15 1 558 . 77 SER N N 117.315 0.15 1 559 . 78 MET H H 8.459 0.02 1 560 . 78 MET HA H 4.431 0.02 1 561 . 78 MET HB2 H 2.009 0.02 1 562 . 78 MET HB3 H 2.009 0.02 1 563 . 78 MET C C 176.119 0.15 1 564 . 78 MET CA C 55.500 0.15 1 565 . 78 MET CB C 32.372 0.15 1 566 . 78 MET N N 122.284 0.15 1 567 . 79 MET H H 8.277 0.02 1 568 . 79 MET HA H 4.431 0.02 1 569 . 79 MET HB2 H 1.970 0.02 1 570 . 79 MET HB3 H 1.970 0.02 1 571 . 79 MET C C 176.482 0.15 1 572 . 79 MET CA C 55.500 0.15 1 573 . 79 MET CB C 40.754 0.15 1 574 . 79 MET N N 120.409 0.15 1 575 . 80 GLY H H 8.306 0.02 1 576 . 80 GLY HA2 H 3.906 0.02 1 577 . 80 GLY HA3 H 3.906 0.02 1 578 . 80 GLY C C 173.738 0.15 1 579 . 80 GLY CA C 45.218 0.15 1 580 . 80 GLY N N 110.001 0.15 1 581 . 81 ASP H H 8.218 0.02 1 582 . 81 ASP HA H 4.587 0.02 1 583 . 81 ASP HB2 H 2.634 0.02 1 584 . 81 ASP HB3 H 2.634 0.02 1 585 . 81 ASP C C 175.887 0.15 1 586 . 81 ASP CA C 54.250 0.15 1 587 . 81 ASP CB C 40.899 0.15 1 588 . 81 ASP N N 120.221 0.15 1 589 . 82 ASP H H 8.301 0.02 1 590 . 82 ASP HA H 4.587 0.02 1 591 . 82 ASP HB2 H 2.634 0.02 1 592 . 82 ASP HB3 H 2.634 0.02 1 593 . 82 ASP C C 176.277 0.15 1 594 . 82 ASP CA C 54.187 0.15 1 595 . 82 ASP CB C 40.789 0.15 1 596 . 82 ASP N N 120.034 0.15 1 597 . 83 GLU H H 8.277 0.02 1 598 . 83 GLU HA H 4.158 0.02 1 599 . 83 GLU HB2 H 1.931 0.02 1 600 . 83 GLU HB3 H 1.931 0.02 1 601 . 83 GLU C C 176.265 0.15 1 602 . 83 GLU CA C 56.812 0.15 1 603 . 83 GLU CB C 29.749 0.15 1 604 . 83 GLU N N 120.784 0.15 1 605 . 84 ASP H H 8.269 0.02 1 606 . 84 ASP HA H 4.509 0.02 1 607 . 84 ASP HB2 H 2.634 0.02 1 608 . 84 ASP HB3 H 2.634 0.02 1 609 . 84 ASP C C 175.945 0.15 1 610 . 84 ASP CA C 54.324 0.15 1 611 . 84 ASP CB C 40.681 0.15 1 612 . 84 ASP N N 120.690 0.15 1 613 . 85 ALA H H 8.060 0.02 1 614 . 85 ALA HA H 4.236 0.02 1 615 . 85 ALA HB H 1.345 0.02 1 616 . 85 ALA C C 177.659 0.15 1 617 . 85 ALA CA C 52.546 0.15 1 618 . 85 ALA CB C 19.106 0.15 1 619 . 85 ALA N N 124.065 0.15 1 620 . 86 CYS H H 8.271 0.02 1 621 . 86 CYS HA H 4.431 0.02 1 622 . 86 CYS HB2 H 2.869 0.02 1 623 . 86 CYS HB3 H 2.869 0.02 1 624 . 86 CYS C C 174.632 0.15 1 625 . 86 CYS CA C 58.453 0.15 1 626 . 86 CYS CB C 27.707 0.15 1 627 . 86 CYS N N 118.065 0.15 1 628 . 87 SER H H 8.318 0.02 1 629 . 87 SER HA H 4.431 0.02 1 630 . 87 SER HB2 H 3.845 0.02 1 631 . 87 SER HB3 H 3.845 0.02 1 632 . 87 SER C C 174.207 0.15 1 633 . 87 SER CA C 58.344 0.15 1 634 . 87 SER CB C 63.640 0.15 1 635 . 87 SER N N 118.158 0.15 1 636 . 88 ASP H H 8.330 0.02 1 637 . 88 ASP HA H 4.627 0.02 1 638 . 88 ASP HB2 H 2.634 0.02 1 639 . 88 ASP HB3 H 2.634 0.02 1 640 . 88 ASP C C 176.395 0.15 1 641 . 88 ASP CA C 54.406 0.15 1 642 . 88 ASP CB C 40.681 0.15 1 643 . 88 ASP N N 122.378 0.15 1 644 . 89 THR H H 8.054 0.02 1 645 . 89 THR HA H 4.226 0.02 1 646 . 89 THR C C 174.740 0.15 1 647 . 89 THR CA C 62.281 0.15 1 648 . 89 THR CB C 69.471 0.15 1 649 . 89 THR N N 114.221 0.15 1 650 . 90 GLU H H 8.270 0.02 1 651 . 90 GLU HA H 4.197 0.02 1 652 . 90 GLU HB2 H 1.970 0.02 1 653 . 90 GLU HB3 H 1.970 0.02 1 654 . 90 GLU C C 176.308 0.15 1 655 . 90 GLU CA C 56.594 0.15 1 656 . 90 GLU CB C 29.675 0.15 1 657 . 90 GLU N N 122.659 0.15 1 658 . 91 ALA H H 8.189 0.02 1 659 . 91 ALA HA H 4.275 0.02 1 660 . 91 ALA HB H 1.345 0.02 1 661 . 91 ALA C C 178.022 0.15 1 662 . 91 ALA CA C 52.656 0.15 1 663 . 91 ALA CB C 18.887 0.15 1 664 . 91 ALA N N 124.628 0.15 1 665 . 92 THR H H 8.001 0.02 1 666 . 92 THR HA H 4.221 0.02 1 667 . 92 THR C C 174.914 0.15 1 668 . 92 THR CA C 62.172 0.15 1 669 . 92 THR CB C 69.617 0.15 1 670 . 92 THR N N 113.095 0.15 1 671 . 93 GLU H H 8.283 0.02 1 672 . 93 GLU HA H 4.197 0.02 1 673 . 93 GLU HB2 H 1.931 0.02 1 674 . 93 GLU HB3 H 1.931 0.02 1 675 . 93 GLU C C 176.134 0.15 1 676 . 93 GLU CA C 56.594 0.15 1 677 . 93 GLU CB C 29.675 0.15 1 678 . 93 GLU N N 122.659 0.15 1 679 . 94 ALA H H 8.125 0.02 1 680 . 94 ALA HA H 4.197 0.02 1 681 . 94 ALA HB H 1.345 0.02 1 682 . 94 ALA C C 177.441 0.15 1 683 . 94 ALA CA C 52.437 0.15 1 684 . 94 ALA CB C 18.960 0.15 1 685 . 94 ALA N N 124.159 0.15 1 686 . 95 MET H H 8.060 0.02 1 687 . 95 MET HA H 4.353 0.02 1 688 . 95 MET HB2 H 1.931 0.02 1 689 . 95 MET HB3 H 1.931 0.02 1 690 . 95 MET C C 175.379 0.15 1 691 . 95 MET CA C 54.953 0.15 1 692 . 95 MET CB C 33.232 0.15 1 693 . 95 MET N N 118.909 0.15 1 694 . 96 ALA H H 8.148 0.02 1 695 . 96 ALA HA H 4.488 0.02 1 696 . 96 ALA HB H 1.383 0.02 1 697 . 96 ALA C C 175.945 0.15 1 698 . 96 ALA CA C 51.015 0.15 1 699 . 96 ALA CB C 17.867 0.15 1 700 . 96 ALA N N 126.222 0.15 1 701 . 97 PRO HA H 4.275 0.02 1 702 . 97 PRO HB2 H 2.244 0.02 1 703 . 97 PRO HB3 H 2.244 0.02 1 704 . 97 PRO C C 177.528 0.15 1 705 . 97 PRO CA C 64.250 0.15 1 706 . 97 PRO CB C 31.788 0.15 1 707 . 98 ASP H H 8.430 0.02 1 708 . 98 ASP HA H 4.470 0.02 1 709 . 98 ASP HB2 H 2.634 0.02 1 710 . 98 ASP HB3 H 2.634 0.02 1 711 . 98 ASP C C 177.158 0.15 1 712 . 98 ASP CA C 55.062 0.15 1 713 . 98 ASP CB C 40.171 0.15 1 714 . 98 ASP N N 118.158 0.15 1 715 . 99 ILE H H 7.655 0.02 1 716 . 99 ILE HA H 3.855 0.02 1 717 . 99 ILE HB H 1.907 0.02 1 718 . 99 ILE C C 177.528 0.15 1 719 . 99 ILE CA C 62.828 0.15 1 720 . 99 ILE CB C 37.765 0.15 1 721 . 99 ILE N N 121.159 0.15 1 722 . 100 LEU H H 7.966 0.02 1 723 . 100 LEU HA H 4.092 0.02 1 724 . 100 LEU C C 178.094 0.15 1 725 . 100 LEU CA C 56.812 0.15 1 726 . 100 LEU CB C 41.410 0.15 1 727 . 100 LEU N N 122.378 0.15 1 728 . 101 ALA H H 7.948 0.02 1 729 . 101 ALA HA H 4.080 0.02 1 730 . 101 ALA HB H 1.384 0.02 1 731 . 101 ALA C C 179.401 0.15 1 732 . 101 ALA CA C 53.968 0.15 1 733 . 101 ALA CB C 18.304 0.15 1 734 . 101 ALA N N 121.346 0.15 1 735 . 102 ARG H H 7.784 0.02 1 736 . 102 ARG HA H 4.080 0.02 1 737 . 102 ARG HB2 H 1.580 0.02 1 738 . 102 ARG HB3 H 1.580 0.02 1 739 . 102 ARG C C 177.702 0.15 1 740 . 102 ARG CA C 57.797 0.15 1 741 . 102 ARG CB C 30.258 0.15 1 742 . 102 ARG N N 118.440 0.15 1 743 . 103 LYS H H 8.048 0.02 1 744 . 103 LYS HA H 4.119 0.02 1 745 . 103 LYS C C 178.044 0.15 1 746 . 103 LYS CA C 57.797 0.15 1 747 . 103 LYS CB C 32.517 0.15 1 748 . 103 LYS N N 121.440 0.15 1 749 . 104 LEU H H 8.142 0.02 1 750 . 104 LEU HA H 4.158 0.02 1 751 . 104 LEU HB2 H 1.658 0.02 1 752 . 104 LEU HB3 H 1.658 0.02 1 753 . 104 LEU HG H 1.502 0.02 1 754 . 104 LEU C C 178.007 0.15 1 755 . 104 LEU CA C 56.300 0.15 1 756 . 104 LEU CB C 41.774 0.15 1 757 . 104 LEU N N 121.44 0.15 1 758 . 105 ALA H H 7.931 0.02 1 759 . 105 ALA HA H 4.167 0.02 1 760 . 105 ALA HB H 1.374 0.02 1 761 . 105 ALA C C 178.383 0.15 1 762 . 105 ALA CA C 53.203 0.15 1 763 . 105 ALA CB C 18.523 0.15 1 764 . 105 ALA N N 122.753 0.15 1 765 . 106 ALA H H 7.902 0.02 1 766 . 106 ALA HA H 4.197 0.02 1 767 . 106 ALA HB H 1.405 0.02 1 768 . 106 ALA C C 178.181 0.15 1 769 . 106 ALA CA C 52.977 0.15 1 770 . 106 ALA CB C 18.523 0.15 1 771 . 106 ALA N N 121.534 0.15 1 772 . 107 ALA H H 7.907 0.02 1 773 . 107 ALA HA H 4.041 0.02 1 774 . 107 ALA HB H 1.970 0.02 1 775 . 107 ALA C C 178.065 0.15 1 776 . 107 ALA CA C 52.875 0.15 1 777 . 107 ALA CB C 18.699 0.15 1 778 . 107 ALA N N 121.909 0.15 1 779 . 108 GLU H H 8.078 0.02 1 780 . 108 GLU HA H 4.230 0.02 1 781 . 108 GLU HB2 H 1.970 0.02 1 782 . 108 GLU HB3 H 1.970 0.02 1 783 . 108 GLU C C 176.965 0.15 1 784 . 108 GLU CA C 56.703 0.15 1 785 . 108 GLU CB C 29.968 0.15 1 786 . 108 GLU N N 118.721 0.15 1 787 . 109 GLY H H 8.160 0.02 1 788 . 109 GLY HA2 H 3.884 0.02 1 789 . 109 GLY HA3 H 3.884 0.02 1 790 . 109 GLY C C 173.97 0.15 1 791 . 109 GLY CA C 45.327 0.15 1 792 . 109 GLY N N 108.595 0.15 1 793 . 110 LEU H H 7.884 0.02 1 794 . 110 LEU HA H 4.307 0.02 1 795 . 110 LEU C C 177.049 0.15 1 796 . 110 LEU CA C 54.734 0.15 1 797 . 110 LEU CB C 42.430 0.15 1 798 . 110 LEU N N 120.784 0.15 1 799 . 111 GLU H H 8.265 0.02 1 800 . 111 GLU HA H 4.199 0.02 1 801 . 111 GLU C C 174.420 0.15 1 802 . 111 GLU CA C 54.515 0.15 1 803 . 111 GLU CB C 29.165 0.15 1 804 . 111 GLU N N 122.378 0.15 1 805 . 112 PRO HB2 H 2.166 0.02 1 806 . 112 PRO HB3 H 2.166 0.02 1 807 . 112 PRO C C 176.847 0.15 1 808 . 112 PRO CA C 63.375 0.15 1 809 . 112 PRO CB C 31.753 0.15 1 810 . 113 LYS H H 8.242 0.02 1 811 . 113 LYS HA H 4.109 0.02 1 812 . 113 LYS C C 176.25 0.15 1 813 . 113 LYS CA C 56.496 0.15 1 814 . 113 LYS CB C 32.421 0.15 1 815 . 113 LYS N N 120.034 0.15 1 816 . 114 TYR H H 7.896 0.02 1 817 . 114 TYR HA H 4.509 0.02 1 818 . 114 TYR HB2 H 3.025 0.02 1 819 . 114 TYR HB3 H 2.791 0.02 1 820 . 114 TYR C C 175.35 0.15 1 821 . 114 TYR CA C 57.469 0.15 1 822 . 114 TYR CB C 38.567 0.15 1 823 . 114 TYR N N 119.565 0.15 1 824 . 115 ARG H H 8.037 0.02 1 825 . 115 ARG HA H 4.236 0.02 1 826 . 115 ARG HB2 H 1.650 0.02 1 827 . 115 ARG HB3 H 1.650 0.02 1 828 . 115 ARG C C 175.814 0.15 1 829 . 115 ARG CA C 55.828 0.15 1 830 . 115 ARG CB C 30.768 0.15 1 831 . 115 ARG N N 122.284 0.15 1 832 . 116 ILE H H 8.078 0.02 1 833 . 116 ILE HA H 4.002 0.02 1 834 . 116 ILE HB H 1.775 0.02 1 835 . 116 ILE C C 176.148 0.15 1 836 . 116 ILE CA C 61.297 0.15 1 837 . 116 ILE CB C 38.421 0.15 1 838 . 116 ILE N N 122.096 0.15 1 839 . 117 GLN H H 8.371 0.02 1 840 . 117 GLN HA H 4.236 0.02 1 841 . 117 GLN HB2 H 1.980 0.02 1 842 . 117 GLN HB3 H 1.980 0.02 1 843 . 117 GLN C C 175.829 0.15 1 844 . 117 GLN CA C 55.937 0.15 1 845 . 117 GLN CB C 29.237 0.15 1 846 . 117 GLN N N 123.972 0.15 1 847 . 118 GLU H H 8.389 0.02 1 848 . 118 GLU HA H 4.205 0.02 1 849 . 118 GLU HB2 H 1.983 0.02 1 850 . 118 GLU HB3 H 1.983 0.02 1 851 . 118 GLU C C 176.308 0.15 1 852 . 118 GLU CA C 56.594 0.15 1 853 . 118 GLU CB C 29.854 0.15 1 854 . 118 GLU N N 122.284 0.15 1 855 . 119 GLN H H 8.318 0.02 1 856 . 119 GLN HA H 4.275 0.02 1 857 . 119 GLN HB2 H 2.009 0.02 1 858 . 119 GLN HB3 H 2.009 0.02 1 859 . 119 GLN C C 175.864 0.15 1 860 . 119 GLN CA C 55.828 0.15 1 861 . 119 GLN CB C 29.383 0.15 1 862 . 119 GLN N N 120.69 0.15 1 863 . 120 GLU H H 8.424 0.02 1 864 . 120 GLU HA H 4.236 0.02 1 865 . 120 GLU HB2 H 1.970 0.02 1 866 . 120 GLU HB3 H 1.970 0.02 1 867 . 120 GLU C C 176.366 0.15 1 868 . 120 GLU CA C 56.484 0.15 1 869 . 120 GLU CB C 29.893 0.15 1 870 . 120 GLU N N 122.19 0.15 1 871 . 121 SER H H 8.336 0.02 1 872 . 121 SER HA H 4.431 0.02 1 873 . 121 SER HB2 H 3.845 0.02 1 874 . 121 SER HB3 H 3.845 0.02 1 875 . 121 SER C C 174.594 0.15 1 876 . 121 SER CA C 58.016 0.15 1 877 . 121 SER CB C 63.64 0.15 1 878 . 121 SER N N 116.846 0.15 1 879 . 122 SER H H 8.447 0.02 1 880 . 122 SER HA H 4.431 0.02 1 881 . 122 SER HB2 H 3.845 0.02 1 882 . 122 SER HB3 H 3.845 0.02 1 883 . 122 SER C C 174.972 0.15 1 884 . 122 SER CA C 58.453 0.15 1 885 . 122 SER CB C 63.859 0.15 1 886 . 122 SER N N 118.158 0.15 1 887 . 123 GLY H H 8.406 0.02 1 888 . 123 GLY HA2 H 3.932 0.02 1 889 . 123 GLY HA3 H 3.932 0.02 1 890 . 123 GLY C C 174.144 0.15 1 891 . 123 GLY CA C 45.218 0.15 1 892 . 123 GLY N N 110.845 0.15 1 893 . 124 GLU H H 8.230 0.02 1 894 . 124 GLU HA H 4.236 0.02 1 895 . 124 GLU HB2 H 1.853 0.02 1 896 . 124 GLU HB3 H 1.853 0.02 1 897 . 124 GLU HG2 H 2.009 0.02 1 898 . 124 GLU HG3 H 2.009 0.02 1 899 . 124 GLU C C 176.613 0.15 1 900 . 124 GLU CA C 56.375 0.15 1 901 . 124 GLU CB C 29.837 0.15 1 902 . 124 GLU N N 120.221 0.15 1 903 . 125 GLU H H 8.535 0.02 1 904 . 125 GLU HA H 4.236 0.02 1 905 . 125 GLU HB2 H 1.970 0.02 1 906 . 125 GLU HB3 H 1.970 0.02 1 907 . 125 GLU C C 176.395 0.15 1 908 . 125 GLU CA C 56.594 0.15 1 909 . 125 GLU CB C 29.893 0.15 1 910 . 125 GLU N N 121.628 0.15 1 911 . 126 ASP H H 8.383 0.02 1 912 . 126 ASP HA H 4.548 0.02 1 913 . 126 ASP HB2 H 2.644 0.02 1 914 . 126 ASP HB3 H 2.644 0.02 1 915 . 126 ASP C C 176.584 0.15 1 916 . 126 ASP CA C 54.491 0.15 1 917 . 126 ASP CB C 40.471 0.15 1 918 . 126 ASP N N 120.878 0.15 1 919 . 127 SER H H 8.101 0.02 1 920 . 127 SER HA H 4.236 0.02 1 921 . 127 SER HB2 H 4.025 0.02 1 922 . 127 SER HB3 H 4.025 0.02 1 923 . 127 SER C C 174.289 0.15 1 924 . 127 SER CA C 59.328 0.15 1 925 . 127 SER CB C 63.422 0.15 1 926 . 127 SER N N 115.439 0.15 1 927 . 128 ASP H H 8.383 0.02 1 928 . 128 ASP HA H 4.587 0.02 1 929 . 128 ASP HB2 H 2.634 0.02 1 930 . 128 ASP HB3 H 2.634 0.02 1 931 . 128 ASP C C 175.742 0.15 1 932 . 128 ASP CA C 54.137 0.15 1 933 . 128 ASP CB C 40.471 0.15 1 934 . 128 ASP N N 120.878 0.15 1 935 . 129 LEU H H 7.591 0.02 1 936 . 129 LEU HA H 4.392 0.02 1 937 . 129 LEU HB2 H 1.619 0.02 1 938 . 129 LEU HB3 H 1.619 0.02 1 939 . 129 LEU C C 177.107 0.15 1 940 . 129 LEU CA C 54.297 0.15 1 941 . 129 LEU CB C 43.232 0.15 1 942 . 129 LEU N N 120.69 0.15 1 943 . 130 SER H H 8.746 0.02 1 944 . 130 SER HA H 4.664 0.02 1 945 . 130 SER C C 172.982 0.15 1 946 . 130 SER CA C 56.482 0.15 1 947 . 130 SER CB C 62.62 0.15 1 948 . 130 SER N N 119.565 0.15 1 949 . 131 PRO HA H 4.119 0.02 1 950 . 131 PRO HB2 H 1.892 0.02 1 951 . 131 PRO HB3 H 1.892 0.02 1 952 . 131 PRO C C 179.314 0.15 1 953 . 131 PRO CA C 65.891 0.15 1 954 . 131 PRO CB C 31.570 0.15 1 955 . 132 GLU H H 8.753 0.02 1 956 . 132 GLU HA H 4.039 0.02 1 957 . 132 GLU C C 179.154 0.15 1 958 . 132 GLU CA C 59.656 0.15 1 959 . 132 GLU CB C 28.727 0.15 1 960 . 132 GLU N N 117.596 0.15 1 961 . 133 GLU H H 7.808 0.02 1 962 . 133 GLU HA H 4.002 0.02 1 963 . 133 GLU C C 179.297 0.15 1 964 . 133 GLU CA C 58.672 0.15 1 965 . 133 GLU CB C 29.808 0.15 1 966 . 133 GLU N N 120.784 0.15 1 967 . 134 ARG H H 8.600 0.02 1 968 . 134 ARG HA H 3.845 0.02 1 969 . 134 ARG HB2 H 1.853 0.02 1 970 . 134 ARG HB3 H 1.853 0.02 1 971 . 134 ARG C C 178.632 0.15 1 972 . 134 ARG CA C 58.672 0.15 1 973 . 134 ARG CB C 29.893 0.15 1 974 . 134 ARG N N 120.784 0.15 1 975 . 135 GLU H H 7.948 0.02 1 976 . 135 GLU HA H 4.197 0.02 1 977 . 135 GLU HB2 H 2.009 0.02 1 978 . 135 GLU HB3 H 2.009 0.02 1 979 . 135 GLU C C 178.167 0.15 1 980 . 135 GLU CA C 58.344 0.15 1 981 . 135 GLU CB C 28.581 0.15 1 982 . 135 GLU N N 120.127 0.15 1 983 . 136 LYS H H 7.761 0.02 1 984 . 136 LYS HA H 3.964 0.002 1 985 . 136 LYS C C 179.011 0.15 1 986 . 136 LYS CA C 59.219 0.15 1 987 . 136 LYS CB C 32.157 0.15 1 988 . 136 LYS N N 120.034 0.15 1 989 . 137 LYS H H 7.872 0.02 1 990 . 137 LYS HA H 4.080 0.02 1 991 . 137 LYS HB2 H 1.814 0.02 1 992 . 137 LYS HB3 H 1.814 0.02 1 993 . 137 LYS C C 178.109 0.15 1 994 . 137 LYS CA C 59.097 0.15 1 995 . 137 LYS CB C 32.248 0.15 1 996 . 137 LYS N N 119.94 0.15 1 997 . 138 ARG H H 7.984 0.02 1 998 . 138 ARG HA H 4.041 0.02 1 999 . 138 ARG HB2 H 1.931 0.02 1 1000 . 138 ARG HB3 H 1.931 0.02 1 1001 . 138 ARG C C 178.843 0.15 1 1002 . 138 ARG CA C 58.891 0.15 1 1003 . 138 ARG CB C 30.185 0.15 1 1004 . 138 ARG N N 120.034 0.15 1 1005 . 139 GLN H H 8.183 0.02 1 1006 . 139 GLN HA H 4.002 0.02 1 1007 . 139 GLN C C 178.022 0.15 1 1008 . 139 GLN CA C 58.344 0.15 1 1009 . 139 GLN CB C 28.071 0.15 1 1010 . 139 GLN N N 118.065 0.15 1 1011 . 140 PHE H H 8.083 0.02 1 1012 . 140 PHE HA H 4.275 0.02 1 1013 . 140 PHE HB2 H 3.220 0.02 1 1014 . 140 PHE HB3 H 3.220 0.02 1 1015 . 140 PHE C C 177.614 0.15 1 1016 . 140 PHE CA C 60.422 0.15 1 1017 . 140 PHE CB C 38.786 0.15 1 1018 . 140 PHE N N 120.315 0.15 1 1019 . 141 GLU H H 8.265 0.02 1 1020 . 141 GLU HA H 3.962 0.02 1 1021 . 141 GLU HB2 H 2.048 0.02 1 1022 . 141 GLU HB3 H 2.048 0.02 1 1023 . 141 GLU C C 178.37 0.15 1 1024 . 141 GLU CA C 58.234 0.15 1 1025 . 141 GLU CB C 29.237 0.15 1 1026 . 141 GLU N N 119.377 0.15 1 1027 . 142 MET H H 8.037 0.02 1 1028 . 142 MET HA H 4.158 0.02 1 1029 . 142 MET C C 177.68 0.15 1 1030 . 142 MET CA C 57.578 0.15 1 1031 . 142 MET CB C 32.258 0.15 1 1032 . 142 MET N N 118.815 0.15 1 1033 . 143 LYS H H 7.802 0.02 1 1034 . 143 LYS HA H 4.000 0.02 1 1035 . 143 LYS HB2 H 1.736 0.02 1 1036 . 143 LYS HB3 H 1.736 0.02 1 1037 . 143 LYS C C 177.688 0.15 1 1038 . 143 LYS CA C 57.984 0.15 1 1039 . 143 LYS CB C 32.226 0.15 1 1040 . 143 LYS N N 119.471 0.15 1 1041 . 144 ARG H H 7.784 0.02 1 1042 . 144 ARG HA H 4.002 0.02 1 1043 . 144 ARG HB2 H 1.814 0.02 1 1044 . 144 ARG HB3 H 1.814 0.02 1 1045 . 144 ARG HG2 H 1.658 0.02 1 1046 . 144 ARG HG3 H 1.658 0.02 1 1047 . 144 ARG C C 177.238 0.15 1 1048 . 144 ARG CA C 57.469 0.15 1 1049 . 144 ARG CB C 32.226 0.15 1 1050 . 144 ARG N N 119.659 0.15 1 1051 . 145 LYS H H 7.860 0.02 1 1052 . 145 LYS HA H 4.080 0.02 1 1053 . 145 LYS HB2 H 1.775 0.02 1 1054 . 145 LYS HB3 H 1.775 0.02 1 1055 . 145 LYS C C 176.991 0.15 1 1056 . 145 LYS CA C 57.250 0.15 1 1057 . 145 LYS CB C 32.421 0.15 1 1058 . 145 LYS N N 119.940 0.15 1 1059 . 146 LEU H H 7.831 0.02 1 1060 . 146 LEU HA H 4.158 0.02 1 1061 . 146 LEU HB2 H 1.580 0.02 1 1062 . 146 LEU HB3 H 1.580 0.02 1 1063 . 146 LEU C C 177.372 0.15 1 1064 . 146 LEU CA C 55.719 0.15 1 1065 . 146 LEU CB C 41.993 0.15 1 1066 . 146 LEU N N 120.596 0.15 1 1067 . 147 HIS H H 8.142 0.02 1 1068 . 147 HIS HA H 4.548 0.02 1 1069 . 147 HIS HB2 H 3.142 0.02 1 1070 . 147 HIS HB3 H 3.142 0.02 1 1071 . 147 HIS C C 174.594 0.15 1 1072 . 147 HIS CA C 55.500 0.15 1 1073 . 147 HIS CB C 28.509 0.15 1 1074 . 147 HIS N N 117.127 0.15 1 1075 . 148 TYR H H 8.095 0.02 1 1076 . 148 TYR HA H 4.353 0.02 1 1077 . 148 TYR HB2 H 2.947 0.02 1 1078 . 148 TYR HB3 H 2.947 0.02 1 1079 . 148 TYR C C 175.683 0.15 1 1080 . 148 TYR CA C 58.563 0.15 1 1081 . 148 TYR CB C 38.494 0.15 1 1082 . 148 TYR N N 121.159 0.15 1 1083 . 149 ASN H H 8.324 0.02 1 1084 . 149 ASN HA H 4.450 0.02 1 1085 . 149 ASN HB2 H 2.752 0.02 1 1086 . 149 ASN HB3 H 2.752 0.02 1 1087 . 149 ASN C C 175.166 0.15 1 1088 . 149 ASN CA C 53.422 0.15 1 1089 . 149 ASN CB C 38.494 0.15 1 1090 . 149 ASN N N 120.221 0.15 1 1091 . 150 GLU H H 8.189 0.02 1 1092 . 150 GLU HA H 4.119 0.02 1 1093 . 150 GLU HB2 H 1.970 0.02 1 1094 . 150 GLU HB3 H 1.970 0.02 1 1095 . 150 GLU C C 176.962 0.15 1 1096 . 150 GLU CA C 57.250 0.15 1 1097 . 150 GLU CB C 29.675 0.15 1 1098 . 150 GLU N N 120.878 0.15 1 1099 . 151 GLY H H 8.259 0.02 1 1100 . 151 GLY HA2 H 3.845 0.02 1 1101 . 151 GLY HA3 H 3.845 0.02 1 1102 . 151 GLY C C 174.334 0.15 1 1103 . 151 GLY CA C 45.546 0.15 1 1104 . 151 GLY N N 108.689 0.15 1 1105 . 152 LEU H H 7.849 0.02 1 1106 . 152 LEU HA H 4.197 0.02 1 1107 . 152 LEU HB2 H 1.526 0.02 1 1108 . 152 LEU HB3 H 1.526 0.02 1 1109 . 152 LEU C C 177.15 0.15 1 1110 . 152 LEU CA C 55.500 0.15 1 1111 . 152 LEU CB C 42.211 0.15 1 1112 . 152 LEU N N 121.159 0.15 1 1113 . 153 ASN H H 8.289 0.02 1 1114 . 153 ASN HA H 4.550 0.02 1 1115 . 153 ASN HB2 H 2.760 0.02 1 1116 . 153 ASN HB3 H 2.760 0.02 1 1117 . 153 ASN C C 175.553 0.15 1 1118 . 153 ASN CA C 53.531 0.15 1 1119 . 153 ASN CB C 38.275 0.15 1 1120 . 153 ASN N N 118.909 0.15 1 1121 . 154 ILE H H 7.896 0.02 1 1122 . 154 ILE HA H 4.002 0.02 1 1123 . 154 ILE HB H 1.775 0.02 1 1124 . 154 ILE C C 176.294 0.15 1 1125 . 154 ILE CA C 61.844 0.15 1 1126 . 154 ILE CB C 38.203 0.15 1 1127 . 154 ILE N N 121.065 0.15 1 1128 . 155 LYS H H 8.113 0.02 1 1129 . 155 LYS HA H 4.158 0.02 1 1130 . 155 LYS HB2 H 1.736 0.02 1 1131 . 155 LYS HB3 H 1.736 0.02 1 1132 . 155 LYS C C 177.136 0.15 1 1133 . 155 LYS CA C 57.141 0.15 1 1134 . 155 LYS CB C 32.444 0.15 1 1135 . 155 LYS N N 123.597 0.15 1 1136 . 156 LEU H H 8.001 0.02 1 1137 . 156 LEU HA H 4.197 0.02 1 1138 . 156 LEU HB2 H 1.541 0.02 1 1139 . 156 LEU HB3 H 1.541 0.02 1 1140 . 156 LEU C C 177.426 0.15 1 1141 . 156 LEU CA C 55.390 0.15 1 1142 . 156 LEU CB C 41.993 0.15 1 1143 . 156 LEU N N 121.909 0.15 1 1144 . 157 ALA H H 8.078 0.02 1 1145 . 157 ALA HA H 4.167 0.02 1 1146 . 157 ALA HB H 1.348 0.02 1 1147 . 157 ALA C C 178.152 0.15 1 1148 . 157 ALA CA C 53.093 0.15 1 1149 . 157 ALA CB C 18.814 0.15 1 1150 . 157 ALA N N 123.69 0.15 1 1151 . 158 ARG HA H 4.353 0.02 1 1152 . 158 ARG HB2 H 1.736 0.02 1 1153 . 158 ARG HB3 H 1.736 0.02 1 1154 . 158 ARG C C 176.616 0.15 1 1155 . 158 ARG CA C 56.627 0.15 1 1156 . 158 ARG CB C 30.418 0.15 1 1157 . 159 GLN H H 8.160 0.02 1 1158 . 159 GLN HA H 4.210 0.02 1 1159 . 159 GLN HB2 H 2.021 0.02 1 1160 . 159 GLN HB3 H 2.021 0.02 1 1161 . 159 GLN C C 175.993 0.15 1 1162 . 159 GLN CA C 56.209 0.15 1 1163 . 159 GLN CB C 29.092 0.15 1 1164 . 159 GLN N N 120.221 0.15 1 1165 . 160 LEU H H 8.095 0.02 1 1166 . 160 LEU HA H 4.275 0.02 1 1167 . 160 LEU HB2 H 2.517 0.02 1 1168 . 160 LEU HB3 H 2.517 0.02 1 1169 . 160 LEU HG H 1.541 0.02 1 1170 . 160 LEU C C 177.238 0.15 1 1171 . 160 LEU CA C 55.281 0.15 1 1172 . 160 LEU CB C 41.993 0.15 1 1173 . 160 LEU N N 122.378 0.15 1 1174 . 161 ILE H H 7.919 0.02 1 1175 . 161 ILE HA H 4.119 0.02 1 1176 . 161 ILE HB H 1.814 0.02 1 1177 . 161 ILE C C 176.076 0.15 1 1178 . 161 ILE CA C 60.969 0.15 1 1179 . 161 ILE CB C 38.567 0.15 1 1180 . 161 ILE N N 120.502 0.15 1 1181 . 162 SER H H 8.195 0.02 1 1182 . 162 SER HA H 4.353 0.02 1 1183 . 162 SER HB2 H 3.806 0.02 1 1184 . 162 SER HB3 H 3.806 0.02 1 1185 . 162 SER C C 174.478 0.15 1 1186 . 162 SER CA C 58.234 0.15 1 1187 . 162 SER CB C 63.495 0.15 1 1188 . 162 SER N N 119.19 0.15 1 1189 . 163 LYS H H 8.248 0.02 1 1190 . 163 LYS HA H 4.236 0.02 1 1191 . 163 LYS HB2 H 1.736 0.02 1 1192 . 163 LYS HB3 H 1.736 0.02 1 1193 . 163 LYS C C 175.976 0.15 1 1194 . 163 LYS CA C 56.484 0.15 1 1195 . 163 LYS CB C 32.736 0.15 1 1196 . 163 LYS N N 123.222 0.15 1 1197 . 164 ASP H H 8.236 0.02 1 1198 . 164 ASP HA H 4.509 0.02 1 1199 . 164 ASP HB2 H 2.292 0.02 1 1200 . 164 ASP HB3 H 2.292 0.02 1 1201 . 164 ASP C C 175.576 0.15 1 1202 . 164 ASP CA C 54.152 0.15 1 1203 . 164 ASP CB C 40.827 0.15 1 1204 . 164 ASP N N 120.596 0.15 1 1205 . 165 LEU H H 7.978 0.02 1 1206 . 165 LEU HA H 4.197 0.02 1 1207 . 165 LEU HB2 H 1.462 0.02 1 1208 . 165 LEU HB3 H 1.462 0.02 1 1209 . 165 LEU C C 176.962 0.15 1 1210 . 165 LEU CA C 55.062 0.15 1 1211 . 165 LEU CB C 42.066 0.15 1 1212 . 165 LEU N N 121.909 0.15 1 1213 . 166 HIS H H 8.435 0.02 1 1214 . 166 HIS HA H 4.587 0.02 1 1215 . 166 HIS HB2 H 3.181 0.02 1 1216 . 166 HIS HB3 H 3.181 0.02 1 1217 . 166 HIS C C 174.057 0.15 1 1218 . 166 HIS CA C 55.172 0.15 1 1219 . 166 HIS CB C 28.873 0.15 1 1220 . 166 HIS N N 118.627 0.15 1 1221 . 167 ASP H H 8.330 0.02 1 1222 . 167 ASP HA H 4.548 0.02 1 1223 . 167 ASP HB2 H 2.595 0.02 1 1224 . 167 ASP HB3 H 2.595 0.02 1 1225 . 167 ASP C C 175.732 0.15 1 1226 . 167 ASP CA C 54.297 0.15 1 1227 . 167 ASP CB C 40.827 0.15 1 1228 . 167 ASP N N 121.815 0.15 1 1229 . 168 ASP H H 8.330 0.02 1 1230 . 168 ASP HA H 4.548 0.02 1 1231 . 168 ASP HB2 H 2.614 0.02 1 1232 . 168 ASP HB3 H 2.614 0.02 1 1233 . 168 ASP C C 175.76 0.15 1 1234 . 168 ASP CA C 54.297 0.15 1 1235 . 168 ASP CB C 40.754 0.15 1 1236 . 168 ASP N N 120.315 0.15 1 1237 . 169 ASP H H 8.207 0.02 1 1238 . 169 ASP HA H 4.548 0.02 1 1239 . 169 ASP HB2 H 2.634 0.02 1 1240 . 169 ASP HB3 H 2.634 0.02 1 1241 . 169 ASP C C 176.165 0.15 1 1242 . 169 ASP CA C 54.297 0.15 1 1243 . 169 ASP CB C 40.681 0.15 1 1244 . 169 ASP N N 120.127 0.15 1 1245 . 170 GLU H H 8.190 0.02 1 1246 . 170 GLU HA H 4.236 0.02 1 1247 . 170 GLU HB2 H 2.009 0.02 1 1248 . 170 GLU HB3 H 2.009 0.02 1 1249 . 170 GLU C C 176.021 0.15 1 1250 . 170 GLU CA C 56.333 0.15 1 1251 . 170 GLU CB C 29.748 0.15 1 1252 . 170 GLU N N 120.409 0.15 1 1253 . 171 ASP H H 8.283 0.02 1 1254 . 171 ASP HA H 4.548 0.02 1 1255 . 171 ASP HB2 H 2.634 0.02 1 1256 . 171 ASP HB3 H 2.634 0.02 1 1257 . 171 ASP C C 175.757 0.15 1 1258 . 171 ASP CA C 54.187 0.15 1 1259 . 171 ASP CB C 40.781 0.15 1 1260 . 171 ASP N N 120.878 0.15 1 1261 . 172 GLU H H 8.195 0.02 1 1262 . 172 GLU HA H 4.275 0.02 1 1263 . 172 GLU HB2 H 1.853 0.02 1 1264 . 172 GLU HB3 H 1.853 0.02 1 1265 . 172 GLU HG2 H 2.048 0.02 1 1266 . 172 GLU HG3 H 2.048 0.02 1 1267 . 172 GLU C C 175.372 0.15 1 1268 . 172 GLU CA C 56.047 0.15 1 1269 . 172 GLU CB C 30.039 0.15 1 1270 . 172 GLU N N 121.159 0.15 1 1271 . 173 GLU H H 7.960 0.02 2 1272 . 173 GLU HA H 4.071 0.02 1 1273 . 173 GLU C C 180.833 0.15 1 1274 . 173 GLU CA C 57.797 0.15 1 1275 . 173 GLU CB C 30.622 0.15 1 1276 . 173 GLU N N 126.691 0.15 1 stop_ save_