data_4060 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Multinuclear Backbone NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase/Protease I - A Member of a New Subclass of Lipolytic Enzymes ; _BMRB_accession_number 4060 _BMRB_flat_file_name bmr4060.str _Entry_type original _Submission_date 1997-09-20 _Accession_date 1997-12-31 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; E. coli thioesterase/protease I, a member of the new subclass of lipolytic enzymes, is a 183 amino acid protein of molecular weight 20.5 kDa. In this study, near complete resonance assignments of the backbone 1H, 13C and 15N nuclei have been obtained by analyzing a set of heteronuclear multi-dimensional NMR spectra. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Ta-Hsien . . 2 Chen Chinpan . . 3 Huang Rong-Fong . . 4 Lee Ya-Lin . . 5 Shaw Jei-Fu . . 6 Huang Tai-huang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 543 "13C chemical shifts" 506 "15N chemical shifts" 161 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-02-06 original author 'Original release.' 2002-07-17 update BMRB 'Modify the saveframe name.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Multinuclear Backbone NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase/Protease I - A Member of a New Subclass of Lipolytic Enzymes ; _Citation_status 'in press' _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Ta-Hsien . . 2 Chen Chinpan . . 3 Huang Rong-Fong . . 4 Lee Ya-Lin . . 5 Shaw Jei-Fu . . 6 Huang Tai-huang . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'Chemical Shift Indices' 'Heteronuclear triple resonance NMR' Lipase 'Lypolytic enzyme' 'Resonance Assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_thioesterase_protease_I _Saveframe_category molecular_system _Mol_system_name thioesterase/protease_I _Abbreviation_common thioesterase/protease_I _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label thioesterase/protease_I $thioesterase_protease_I stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'lipolytic enzyme' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_thioesterase_protease_I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common thioesterase/protease_I _Abbreviation_common thioesterase/protease_I _Molecular_mass 21000 _Mol_thiol_state . loop_ _Biological_function 'lipolytic enzyme' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; MADTLLILGDSLSAGYRMSA SAAWPALLNDKWQSKTSVVN ASISGDTSQQGLARLPALLK QHQPRWVLVELGGNDGLRGF QPQQTEQTLRQILQDVKAAN AEPLLMQIRLPANYGRRYNE AFSAIYPKLAKEFDVPLLPF FMEEVYLKPQWMQDDGIHPN RDAQPFIADWMAKQLQPLVN HDSHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 THR 5 LEU 6 LEU 7 ILE 8 LEU 9 GLY 10 ASP 11 SER 12 LEU 13 SER 14 ALA 15 GLY 16 TYR 17 ARG 18 MET 19 SER 20 ALA 21 SER 22 ALA 23 ALA 24 TRP 25 PRO 26 ALA 27 LEU 28 LEU 29 ASN 30 ASP 31 LYS 32 TRP 33 GLN 34 SER 35 LYS 36 THR 37 SER 38 VAL 39 VAL 40 ASN 41 ALA 42 SER 43 ILE 44 SER 45 GLY 46 ASP 47 THR 48 SER 49 GLN 50 GLN 51 GLY 52 LEU 53 ALA 54 ARG 55 LEU 56 PRO 57 ALA 58 LEU 59 LEU 60 LYS 61 GLN 62 HIS 63 GLN 64 PRO 65 ARG 66 TRP 67 VAL 68 LEU 69 VAL 70 GLU 71 LEU 72 GLY 73 GLY 74 ASN 75 ASP 76 GLY 77 LEU 78 ARG 79 GLY 80 PHE 81 GLN 82 PRO 83 GLN 84 GLN 85 THR 86 GLU 87 GLN 88 THR 89 LEU 90 ARG 91 GLN 92 ILE 93 LEU 94 GLN 95 ASP 96 VAL 97 LYS 98 ALA 99 ALA 100 ASN 101 ALA 102 GLU 103 PRO 104 LEU 105 LEU 106 MET 107 GLN 108 ILE 109 ARG 110 LEU 111 PRO 112 ALA 113 ASN 114 TYR 115 GLY 116 ARG 117 ARG 118 TYR 119 ASN 120 GLU 121 ALA 122 PHE 123 SER 124 ALA 125 ILE 126 TYR 127 PRO 128 LYS 129 LEU 130 ALA 131 LYS 132 GLU 133 PHE 134 ASP 135 VAL 136 PRO 137 LEU 138 LEU 139 PRO 140 PHE 141 PHE 142 MET 143 GLU 144 GLU 145 VAL 146 TYR 147 LEU 148 LYS 149 PRO 150 GLN 151 TRP 152 MET 153 GLN 154 ASP 155 ASP 156 GLY 157 ILE 158 HIS 159 PRO 160 ASN 161 ARG 162 ASP 163 ALA 164 GLN 165 PRO 166 PHE 167 ILE 168 ALA 169 ASP 170 TRP 171 MET 172 ALA 173 LYS 174 GLN 175 LEU 176 GLN 177 PRO 178 LEU 179 VAL 180 ASN 181 HIS 182 ASP 183 SER 184 HIS 185 HIS 186 HIS 187 HIS 188 HIS 189 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1IVN "E.Coli Thioesterase IPROTEASE ILYSOPHOSPHOLIASE L1" 100.53 190 98.95 98.95 1.38e-132 PDB 1J00 "E. Coli Thioesterase I/protease I/lysophospholipase L1 In Complexed With Diethyl Phosphono Moiety" 100.53 190 98.42 98.42 6.59e-132 PDB 1JRL "Crystal Structure Of E. Coli Lysophospholiase L1ACYL-Coa Thioesterase IPROTEASE I L109P MUTANT" 100.53 190 98.42 98.42 2.10e-131 PDB 1U8U "E. Coli Thioesterase IPROTEASE ILYSOPHOSPHOLIASE L1 IN COMPLEXED With Octanoic Acid" 100.53 190 98.95 98.95 1.38e-132 PDB 1V2G "The L109p Mutant Of E. Coli Thioesterase IPROTEASE ILYSOPHOSPHOLIPASE L1 (TAP) IN COMPLEXED WITH OCTANOIC Acid" 100.53 190 98.42 98.42 2.10e-131 DBJ BAA02475 "protease I [Escherichia coli]" 96.30 208 100.00 100.00 3.04e-128 DBJ BAB33980 "acyl-CoA thioesterase I [Escherichia coli O157:H7 str. Sakai]" 96.30 208 99.45 99.45 2.22e-127 DBJ BAE76273 "multifunctional acyl-CoA thioesterase I, protease I, and lysophospholipase L1 [Escherichia coli str. K12 substr. W3110]" 96.30 208 100.00 100.00 3.04e-128 DBJ BAG76043 "acyl-CoA thioesterase I [Escherichia coli SE11]" 96.30 207 100.00 100.00 3.10e-128 DBJ BAI23868 "multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [Escherichia coli O26:H11 str. 11368]" 96.30 208 100.00 100.00 3.04e-128 EMBL CAP75030 "acyl-CoA thioesterase I [Escherichia coli LF82]" 96.30 208 99.45 99.45 1.29e-127 EMBL CAQ30967 "multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [Escherichia coli BL21(DE3)]" 96.30 208 100.00 100.00 3.04e-128 EMBL CAQ88099 "multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [Escherichia fergusonii ATCC 35469]" 96.30 208 100.00 100.00 3.04e-128 EMBL CAQ97369 "multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [Escherichia coli IAI1]" 96.30 208 100.00 100.00 3.04e-128 EMBL CAR01845 "multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 [Escherichia coli S88]" 96.30 208 100.00 100.00 3.04e-128 GB AAA24664 "acyl-coA thioesterase I [Escherichia coli str. K-12 substr. W3110]" 96.30 208 100.00 100.00 3.04e-128 GB AAB40248 "acyl-coA thioesterase I precursor [Escherichia coli]" 96.30 218 100.00 100.00 3.03e-128 GB AAC73596 "acyl-CoA thioesterase 1 and protease I and lysophospholipase L1 [Escherichia coli str. K-12 substr. MG1655]" 96.30 208 100.00 100.00 3.04e-128 GB AAG54851 "acyl-CoA thioesterase I; also functions as protease I [Escherichia coli O157:H7 str. EDL933]" 96.30 208 99.45 99.45 2.22e-127 GB AAN79092 "Acyl-CoA thioesterase I precursor [Escherichia coli CFT073]" 96.30 218 100.00 100.00 3.03e-128 REF NP_308584 "multifunctional acyl-CoA thioesterase I/protease I/lysophospholipase L1 [Escherichia coli O157:H7 str. Sakai]" 96.30 208 99.45 99.45 2.22e-127 REF NP_415027 "acyl-CoA thioesterase 1 and protease I and lysophospholipase L1 [Escherichia coli str. K-12 substr. MG1655]" 96.30 208 100.00 100.00 3.04e-128 REF WP_001295836 "MULTISPECIES: arylesterase [Bacteria]" 96.30 207 100.00 100.00 3.10e-128 REF WP_001297298 "arylesterase [Escherichia coli]" 96.30 208 100.00 100.00 3.04e-128 REF WP_001301605 "arylesterase [Escherichia coli]" 96.30 207 99.45 99.45 2.94e-127 SP P0ADA1 "RecName: Full=Acyl-CoA thioesterase I; AltName: Full=Lecithinase B; AltName: Full=Lysophospholipase L1; AltName: Full=Protease " 96.30 208 100.00 100.00 3.04e-128 SP P0ADA2 "RecName: Full=Acyl-CoA thioesterase I; AltName: Full=Lecithinase B; AltName: Full=Lysophospholipase L1; AltName: Full=Protease " 96.30 208 100.00 100.00 3.04e-128 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $thioesterase_protease_I 'E. coli' 562 . . 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_name $thioesterase_protease_I 'recombinant technology' 'E. coli' Escherichia coli . . 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 $thioesterase_protease_I 2 mM [U-15N] 'phosphate buffer' 50 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $thioesterase_protease_I 2 mM [U-13C] 'phosphate buffer' 50 mM . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $thioesterase_protease_I 2 mM [U-13C;U-15N] 'phosphate buffer' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.5 0.1 pH temperature 310 0.5 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 . C 13 . ppm . . . . . . . H 1 . ppm . . . . . . . N 15 . ppm . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_thioesterase_protease_I _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name thioesterase/protease_I _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 H H 7.51 0.01 1 2 . 2 ALA HA H 4.12 0.01 1 3 . 2 ALA HB H 1.45 0.01 2 4 . 2 ALA C C 173.87 0.01 1 5 . 2 ALA CA C 51.77 0.01 1 6 . 2 ALA CB C 19.80 0.01 1 7 . 2 ALA N N 117.61 0.01 1 8 . 3 ASP H H 8.72 0.01 1 9 . 3 ASP HA H 4.80 0.01 1 10 . 3 ASP HB2 H 2.87 0.01 2 11 . 3 ASP HB3 H 2.68 0.01 2 12 . 3 ASP C C 174.88 0.01 1 13 . 3 ASP CA C 54.2 0.01 1 14 . 3 ASP CB C 41.71 0.01 1 15 . 3 ASP N N 121.07 0.01 1 16 . 4 THR H H 8.62 0.01 1 17 . 4 THR HA H 5.18 0.01 1 18 . 4 THR HB H 3.93 0.01 1 19 . 4 THR C C 173.26 0.01 1 20 . 4 THR CA C 62.70 0.01 1 21 . 4 THR CB C 71.42 0.01 1 22 . 4 THR N N 117.32 0.01 1 23 . 5 LEU H H 9.54 0.01 1 24 . 5 LEU HA H 5.31 0.01 1 25 . 5 LEU HB2 H 2.08 0.01 2 26 . 5 LEU HB3 H 1.55 0.01 2 27 . 5 LEU C C 173.06 0.01 1 28 . 5 LEU CA C 53.70 0.01 1 29 . 5 LEU CB C 44.05 0.01 1 30 . 5 LEU N N 129.82 0.01 1 31 . 6 LEU H H 8.72 0.01 1 32 . 6 LEU HA H 5.31 0.01 1 33 . 6 LEU C C 174.38 0.01 1 34 . 6 LEU CA C 53.05 0.01 1 35 . 6 LEU N N 128.57 0.01 1 36 . 7 ILE H H 9.12 0.01 1 37 . 7 ILE HA H 4.43 0.01 1 38 . 7 ILE HB H 2.06 0.01 1 39 . 7 ILE C C 172.85 0.01 1 40 . 7 ILE CA C 60.25 0.01 1 41 . 7 ILE CB C 37.42 0.01 1 42 . 7 ILE N N 126.70 0.01 1 43 . 8 LEU H H 9.05 0.01 1 44 . 8 LEU HA H 4.64 0.01 1 45 . 8 LEU HB2 H 2.08 0.01 2 46 . 8 LEU C C 173.43 0.01 1 47 . 8 LEU CA C 52.83 0.01 1 48 . 8 LEU CB C 43.69 0.01 1 49 . 8 LEU N N 130.76 0.01 1 50 . 9 GLY H H 6.87 0.01 1 51 . 9 GLY HA2 H 5.52 0.01 2 52 . 9 GLY HA3 H 3.70 0.01 2 53 . 9 GLY C C 173.36 0.01 1 54 . 9 GLY CA C 45.00 0.01 1 55 . 9 GLY N N 111.7 0.01 1 56 . 10 ASP H H 7.75 0.01 1 57 . 10 ASP HA H 5.45 0.01 1 58 . 10 ASP C C 179.47 0.01 1 59 . 10 ASP CA C 51.48 0.01 1 60 . 10 ASP CB C 40.77 0.01 1 61 . 10 ASP N N 117.63 0.01 1 62 . 11 SER CA C 66.91 0.01 1 63 . 12 LEU H H 8.04 0.01 1 64 . 12 LEU HA H 4.64 0.01 1 65 . 12 LEU C C 179.46 0.01 1 66 . 12 LEU CA C 57.36 0.01 1 67 . 12 LEU CB C 40.34 0.01 1 68 . 12 LEU N N 118.01 0.01 1 69 . 13 SER H H 7.79 0.01 1 70 . 13 SER HA H 4.71 0.01 1 71 . 13 SER HB2 H 3.97 0.01 2 72 . 13 SER HB3 H 3.97 0.01 2 73 . 13 SER C C 172.85 0.01 1 74 . 13 SER CA C 60.14 0.01 1 75 . 13 SER CB C 64.63 0.01 1 76 . 13 SER N N 113.9 0.01 1 77 . 14 ALA H H 8.23 0.01 1 78 . 14 ALA HA H 3.86 0.01 1 79 . 14 ALA HB H 1.04 0.01 2 80 . 14 ALA C C 177.12 0.01 1 81 . 14 ALA CA C 53.30 0.01 1 82 . 14 ALA CB C 19.97 0.01 1 83 . 14 ALA N N 119.82 0.01 1 84 . 15 GLY H H 8.23 0.01 1 85 . 15 GLY HA2 H 3.96 0.01 2 86 . 15 GLY HA3 H 3.50 0.01 2 87 . 15 GLY C C 172.04 0.01 1 88 . 15 GLY CA C 45.00 0.01 1 89 . 15 GLY N N 102.32 0.01 1 90 . 16 TYR H H 8.26 0.01 1 91 . 16 TYR HA H 4.37 0.01 1 92 . 16 TYR HB2 H 2.57 0.01 2 93 . 16 TYR HB3 H 2.57 0.01 2 94 . 16 TYR C C 174.48 0.01 1 95 . 16 TYR CA C 57.75 0.01 1 96 . 16 TYR CB C 39.37 0.01 1 97 . 16 TYR N N 125.14 0.01 1 98 . 17 ARG H H 8.72 0.01 1 99 . 17 ARG HA H 3.47 0.01 1 100 . 17 ARG C C 174.42 0.01 1 101 . 17 ARG CA C 57.29 0.01 1 102 . 17 ARG CB C 26.62 0.01 1 103 . 17 ARG N N 122.63 0.01 1 104 . 18 MET H H 7.23 0.01 1 105 . 18 MET HA H 2.91 0.01 1 106 . 18 MET C C 173.67 0.01 1 107 . 18 MET CA C 53.82 0.01 1 108 . 18 MET CB C 35.07 0.01 1 109 . 18 MET N N 111.07 0.01 1 110 . 19 SER H H 8.39 0.01 1 111 . 19 SER HA H 4.31 0.01 1 112 . 19 SER HB2 H 3.90 0.01 2 113 . 19 SER HB3 H 3.81 0.01 2 114 . 19 SER C C 175.49 0.01 1 115 . 19 SER CA C 58.00 0.01 1 116 . 19 SER CB C 63.62 0.01 1 117 . 19 SER N N 115.13 0.01 1 118 . 20 ALA H H 8.77 0.01 1 119 . 20 ALA HA H 4.03 0.01 1 120 . 20 ALA HB H 1.44 0.01 2 121 . 20 ALA C C 180.47 0.01 1 122 . 20 ALA CA C 55.28 0.01 1 123 . 20 ALA CB C 18.21 0.01 1 124 . 20 ALA N N 127.30 0.01 1 125 . 21 SER H H 7.86 0.01 1 126 . 21 SER HA H 3.95 0.01 1 127 . 21 SER HB2 H 3.82 0.01 2 128 . 21 SER HB3 H 3.82 0.01 2 129 . 21 SER C C 173.46 0.01 1 130 . 21 SER CA C 62.67 0.01 1 131 . 21 SER CB C 59.4 0.01 1 132 . 21 SER N N 108.88 0.01 1 133 . 22 ALA H H 7.50 0.01 1 134 . 22 ALA HA H 4.26 0.01 1 135 . 22 ALA HB H 1.34 0.01 2 136 . 22 ALA C C 176.61 0.01 1 137 . 22 ALA CA C 50.95 0.01 1 138 . 22 ALA CB C 19.91 0.01 1 139 . 22 ALA N N 121.7 0.01 1 140 . 23 ALA H H 6.88 0.01 1 141 . 23 ALA HA H 4.18 0.01 1 142 . 23 ALA HB H 1.08 0.01 2 143 . 23 ALA C C 179.05 0.01 1 144 . 23 ALA CA C 51.43 0.01 1 145 . 23 ALA CB C 19.85 0.01 1 146 . 23 ALA N N 118.26 0.01 1 147 . 24 TRP H H 8.98 0.01 1 148 . 24 TRP HA H 4.65 0.01 1 149 . 24 TRP HB2 H 3.17 0.01 2 150 . 24 TRP HB3 H 3.05 0.01 2 151 . 24 TRP C C 174.6 0.01 1 152 . 24 TRP CA C 61.12 0.01 1 153 . 24 TRP N N 118.01 0.01 1 154 . 25 PRO C C 178.13 0.01 1 155 . 25 PRO CA C 66.07 0.01 1 156 . 26 ALA H H 7.20 0.01 1 157 . 26 ALA HA H 4.00 0.01 1 158 . 26 ALA HB H 1.46 0.01 2 159 . 26 ALA C C 180.17 0.01 1 160 . 26 ALA CA C 54.32 0.01 1 161 . 26 ALA CB C 18.27 0.01 1 162 . 26 ALA N N 118.88 0.01 1 163 . 27 LEU H H 7.13 0.01 1 164 . 27 LEU HA H 4.10 0.01 1 165 . 27 LEU HB2 H 1.67 0.01 2 166 . 27 LEU HB3 H 1.36 0.01 2 167 . 27 LEU C C 180.37 0.01 1 168 . 27 LEU CA C 56.79 0.01 1 169 . 27 LEU CB C 40.10 0.01 1 170 . 27 LEU N N 117.32 0.01 1 171 . 28 LEU H H 8.41 0.01 1 172 . 28 LEU HA H 3.68 0.01 1 173 . 28 LEU HB2 H 1.74 0.01 2 174 . 28 LEU C C 177.42 0.01 1 175 . 28 LEU CA C 57.24 0.01 1 176 . 28 LEU CB C 42.17 0.01 1 177 . 28 LEU N N 121.07 0.01 1 178 . 29 ASN H H 8.01 0.01 1 179 . 29 ASN HA H 4.30 0.01 1 180 . 29 ASN HB2 H 3.01 0.01 2 181 . 29 ASN HB3 H 2.81 0.01 2 182 . 29 ASN C C 177.12 0.01 1 183 . 29 ASN CA C 57.30 0.01 1 184 . 29 ASN CB C 39.38 0.01 1 185 . 29 ASN N N 115.76 0.01 1 186 . 30 ASP H H 7.72 0.01 1 187 . 30 ASP HA H 4.44 0.01 1 188 . 30 ASP HB2 H 2.84 0.01 2 189 . 30 ASP HB3 H 2.82 0.01 2 190 . 30 ASP C C 174.78 0.01 1 191 . 30 ASP CA C 56.24 0.01 1 192 . 30 ASP CB C 38.89 0.01 1 193 . 30 ASP N N 115.76 0.01 1 194 . 31 LYS H H 7.67 0.01 1 195 . 31 LYS HA H 4.16 0.01 1 196 . 31 LYS HB2 H 1.78 0.01 2 197 . 31 LYS HB3 H 1.47 0.01 2 198 . 31 LYS C C 178.54 0.01 1 199 . 31 LYS CA C 58.37 0.01 1 200 . 31 LYS CB C 33.06 0.01 1 201 . 31 LYS N N 118.57 0.01 1 202 . 32 TRP H H 8.10 0.01 1 203 . 32 TRP HA H 4.97 0.01 1 204 . 32 TRP HB2 H 3.58 0.01 1 205 . 32 TRP HB3 H 3.26 0.01 1 206 . 32 TRP C C 176.81 0.01 1 207 . 32 TRP CA C 55.43 0.01 1 208 . 32 TRP CB C 30.23 0.01 1 209 . 32 TRP N N 117.38 0.01 1 210 . 33 GLN H H 8.01 0.01 1 211 . 33 GLN HA H 4.29 0.01 1 212 . 33 GLN C C 175.90 0.01 1 213 . 33 GLN CA C 58.2 0.01 1 214 . 33 GLN CB C 28.00 0.01 1 215 . 33 GLN N N 118.26 0.01 1 216 . 34 SER H H 8.55 0.01 1 217 . 34 SER HA H 4.16 0.01 1 218 . 34 SER HB2 H 3.96 0.01 2 219 . 34 SER HB3 H 3.84 0.01 2 220 . 34 SER C C 174.17 0.01 1 221 . 34 SER CA C 60.61 0.01 1 222 . 34 SER CB C 62.77 0.01 1 223 . 34 SER N N 114.20 0.01 1 224 . 35 LYS H H 8.47 0.01 1 225 . 35 LYS HA H 4.37 0.01 1 226 . 35 LYS HB2 H 1.68 0.01 1 227 . 35 LYS HB3 H 1.31 0.01 1 228 . 35 LYS C C 176.51 0.01 1 229 . 35 LYS CA C 57.63 0.01 1 230 . 35 LYS CB C 33.92 0.01 1 231 . 35 LYS N N 120.45 0.01 1 232 . 36 THR H H 7.85 0.01 1 233 . 36 THR HA H 4.60 0.01 1 234 . 36 THR HB H 3.64 0.01 1 235 . 36 THR C C 173.06 0.01 1 236 . 36 THR CA C 62.11 0.01 1 237 . 36 THR CB C 71.83 0.01 1 238 . 36 THR N N 116.07 0.01 1 239 . 37 SER H H 8.66 0.01 1 240 . 37 SER HA H 4.72 0.01 1 241 . 37 SER HB2 H 3.83 0.01 2 242 . 37 SER HB3 H 3.83 0.01 2 243 . 37 SER C C 173.46 0.01 1 244 . 37 SER CA C 57.93 0.01 1 245 . 37 SER CB C 63.74 0.01 1 246 . 37 SER N N 120.45 0.01 1 247 . 38 VAL H H 8.61 0.01 1 248 . 38 VAL HA H 4.89 0.01 1 249 . 38 VAL HB H 1.90 0.01 1 250 . 38 VAL C C 175.49 0.01 1 251 . 38 VAL CA C 61.37 0.01 1 252 . 38 VAL CB C 32.82 0.01 1 253 . 38 VAL N N 125.76 0.01 1 254 . 39 VAL H H 8.88 0.01 1 255 . 39 VAL HA H 3.96 0.01 1 256 . 39 VAL HB H 1.42 0.01 1 257 . 39 VAL C C 173.97 0.01 1 258 . 39 VAL CA C 60.68 0.01 1 259 . 39 VAL CB C 33.49 0.01 1 260 . 39 VAL N N 128.57 0.01 1 261 . 40 ASN H H 9.14 0.01 1 262 . 40 ASN HA H 4.71 0.01 1 263 . 40 ASN HB2 H 3.05 0.01 1 264 . 40 ASN HB3 H 2.14 0.01 1 265 . 40 ASN C C 173.97 0.01 1 266 . 40 ASN CA C 51.39 0.01 1 267 . 40 ASN CB C 37.92 0.01 1 268 . 40 ASN N N 126.39 0.01 1 269 . 41 ALA H H 8.87 0.01 1 270 . 41 ALA HA H 4.76 0.01 1 271 . 41 ALA HB H 1.27 0.01 2 272 . 41 ALA C C 176.61 0.01 1 273 . 41 ALA CA C 50.18 0.01 1 274 . 41 ALA CB C 20.29 0.01 1 275 . 41 ALA N N 132.32 0.01 1 276 . 42 SER H H 7.27 0.01 1 277 . 42 SER HA H 4.84 0.01 1 278 . 42 SER HB2 H 3.02 0.01 1 279 . 42 SER HB3 H 3.02 0.01 1 280 . 42 SER C C 172.74 0.01 1 281 . 42 SER CA C 58.75 0.01 1 282 . 42 SER CB C 63.82 0.01 1 283 . 42 SER N N 116.38 0.01 1 284 . 43 ILE H H 7.59 0.01 1 285 . 43 ILE HA H 4.14 0.01 1 286 . 43 ILE HB H 1.70 0.01 1 287 . 43 ILE C C 176.20 0.01 1 288 . 43 ILE CA C 59.47 0.01 1 289 . 43 ILE CB C 40.05 0.01 1 290 . 43 ILE N N 122.63 0.01 1 291 . 44 SER H H 8.91 0.01 1 292 . 44 SER HA H 3.84 0.01 1 293 . 44 SER CA C 61.19 0.01 1 294 . 44 SER CB C 62.90 0.01 1 295 . 44 SER N N 122.63 0.01 1 296 . 45 GLY H H 8.77 0.01 1 297 . 45 GLY HA2 H 4.76 0.01 2 298 . 45 GLY HA3 H 3.86 0.01 2 299 . 45 GLY C C 174.88 0.01 1 300 . 45 GLY CA C 45.19 0.01 1 301 . 45 GLY N N 106.07 0.01 1 302 . 46 ASP H H 7.27 0.01 1 303 . 46 ASP HA H 4.72 0.01 1 304 . 46 ASP C C 179.25 0.01 1 305 . 46 ASP CA C 55.98 0.01 1 306 . 46 ASP CB C 40.56 0.01 1 307 . 46 ASP N N 119.51 0.01 1 308 . 47 THR H H 8.65 0.01 1 309 . 47 THR HA H 4.42 0.01 1 310 . 47 THR HB H 4.61 0.01 1 311 . 47 THR C C 176.19 0.01 1 312 . 47 THR CA C 59.96 0.01 1 313 . 47 THR CB C 71.92 0.01 1 314 . 47 THR N N 113.57 0.01 1 315 . 48 SER H H 8.82 0.01 1 316 . 48 SER HA H 4.62 0.01 1 317 . 48 SER HB2 H 4.00 0.01 2 318 . 48 SER HB3 H 3.86 0.01 2 319 . 48 SER C C 176.31 0.01 1 320 . 48 SER CA C 62.74 0.01 1 321 . 48 SER CB C 60.28 0.01 1 322 . 48 SER N N 110.13 0.01 1 323 . 49 GLN H H 7.23 0.01 1 324 . 49 GLN HA H 3.77 0.01 1 325 . 49 GLN HB2 H 2.32 0.01 1 326 . 49 GLN HB3 H 2.02 0.01 1 327 . 49 GLN C C 178.24 0.01 1 328 . 49 GLN CA C 59.37 0.01 1 329 . 49 GLN CB C 28.82 0.01 1 330 . 49 GLN N N 120.51 0.01 1 331 . 50 GLN H H 7.67 0.01 1 332 . 50 GLN HA H 4.01 0.01 1 333 . 50 GLN HB2 H 2.41 0.01 2 334 . 50 GLN HB3 H 2.04 0.01 2 335 . 50 GLN C C 179.15 0.01 1 336 . 50 GLN CA C 59.06 0.01 1 337 . 50 GLN CB C 29.55 0.01 1 338 . 50 GLN N N 120.45 0.01 1 339 . 51 GLY H H 8.27 0.01 1 340 . 51 GLY HA2 H 3.73 0.01 2 341 . 51 GLY HA3 H 3.44 0.01 2 342 . 51 GLY C C 174.68 0.01 1 343 . 51 GLY CA C 47.24 0.01 1 344 . 51 GLY N N 107.01 0.01 1 345 . 52 LEU H H 8.11 0.01 1 346 . 52 LEU HA H 3.92 0.01 1 347 . 52 LEU C C 178.74 0.01 1 348 . 52 LEU CA C 57.79 0.01 1 349 . 52 LEU CB C 40.65 0.01 1 350 . 52 LEU N N 120.45 0.01 1 351 . 53 ALA H H 7.74 0.01 1 352 . 53 ALA HA H 4.03 0.01 1 353 . 53 ALA HB H 1.50 0.01 1 354 . 53 ALA C C 179.56 0.01 1 355 . 53 ALA CA C 54.67 0.01 1 356 . 53 ALA CB C 18.22 0.01 1 357 . 53 ALA N N 119.20 0.01 1 358 . 54 ARG H H 7.20 0.01 1 359 . 54 ARG HA H 4.34 0.01 1 360 . 54 ARG HB2 H 1.93 0.01 2 361 . 54 ARG C C 178.64 0.01 1 362 . 54 ARG CA C 56.71 0.01 1 363 . 54 ARG CB C 31.25 0.01 1 364 . 54 ARG N N 112.95 0.01 1 365 . 55 LEU H H 7.52 0.01 1 366 . 55 LEU HA H 4.18 0.01 1 367 . 55 LEU C C 173.83 0.01 1 368 . 55 LEU CA C 59.19 0.01 1 369 . 55 LEU CB C 39.82 0.01 1 370 . 55 LEU N N 118.88 0.01 1 371 . 56 PRO HA H 3.55 0.01 1 372 . 56 PRO C C 179.66 0.01 1 373 . 56 PRO CA C 67.06 0.01 1 374 . 56 PRO CB C 30.83 0.01 1 375 . 57 ALA H H 8.01 0.01 1 376 . 57 ALA HA H 4.10 0.01 1 377 . 57 ALA HB H 1.42 0.01 1 378 . 57 ALA C C 180.57 0.01 1 379 . 57 ALA CA C 55.10 0.01 1 380 . 57 ALA CB C 18.53 0.01 1 381 . 57 ALA N N 117.90 0.01 1 382 . 58 LEU H H 7.49 0.01 1 383 . 58 LEU HA H 4.14 0.01 1 384 . 58 LEU HB2 H 2.22 0.01 2 385 . 58 LEU C C 180.27 0.01 1 386 . 58 LEU CA C 52.68 0.01 1 387 . 58 LEU N N 117.63 0.01 1 388 . 59 LEU H H 8.44 0.01 1 389 . 59 LEU HA H 3.79 0.01 1 390 . 59 LEU C C 179.86 0.01 1 391 . 59 LEU CA C 57.68 0.01 1 392 . 59 LEU CB C 40.60 0.01 1 393 . 59 LEU N N 117.95 0.01 1 394 . 60 LYS H H 7.60 0.01 1 395 . 60 LYS HA H 4.01 0.01 1 396 . 60 LYS HB2 H 1.83 0.01 2 397 . 60 LYS HB3 H 1.44 0.01 2 398 . 60 LYS C C 178.03 0.01 1 399 . 60 LYS CA C 58.71 0.01 1 400 . 60 LYS CB C 32.76 0.01 1 401 . 60 LYS N N 118.88 0.01 1 402 . 61 GLN H H 7.97 0.01 1 403 . 61 GLN HA H 3.92 0.01 1 404 . 61 GLN HB2 H 1.65 0.01 2 405 . 61 GLN HB3 H 1.50 0.01 2 406 . 61 GLN C C 177.63 0.01 1 407 . 61 GLN CA C 58.02 0.01 1 408 . 61 GLN CB C 29.37 0.01 1 409 . 61 GLN N N 115.13 0.01 1 410 . 62 HIS H H 7.92 0.01 1 411 . 62 HIS HA H 4.70 0.01 1 412 . 62 HIS HB2 H 3.02 0.01 2 413 . 62 HIS HB3 H 2.85 0.01 2 414 . 62 HIS C C 173.26 0.01 1 415 . 62 HIS CA C 55.94 0.01 1 416 . 62 HIS CB C 30.60 0.01 1 417 . 62 HIS N N 110.13 0.01 1 418 . 63 GLN H H 7.89 0.01 1 419 . 63 GLN HA H 4.13 0.01 1 420 . 63 GLN HB2 H 2.12 0.01 2 421 . 63 GLN HB3 H 1.97 0.01 2 422 . 63 GLN C C 172.71 0.01 1 423 . 63 GLN CA C 55.90 0.01 1 424 . 63 GLN CB C 28.20 0.01 1 425 . 63 GLN N N 113.88 0.01 1 426 . 64 PRO HA H 4.32 0.01 1 427 . 64 PRO C C 175.09 0.01 1 428 . 64 PRO CA C 62.54 0.01 1 429 . 65 ARG H H 8.34 0.01 1 430 . 65 ARG HA H 4.16 0.01 1 431 . 65 ARG C C 176.31 0.01 1 432 . 65 ARG CA C 56.49 0.01 1 433 . 65 ARG CB C 29.83 0.01 1 434 . 65 ARG N N 118.57 0.01 1 435 . 66 TRP H H 7.59 0.01 1 436 . 66 TRP HA H 5.60 0.01 1 437 . 66 TRP HB2 H 3.15 0.01 2 438 . 66 TRP HB3 H 3.02 0.01 2 439 . 66 TRP C C 175.39 0.01 1 440 . 66 TRP CA C 56.50 0.01 1 441 . 66 TRP CB C 32.59 0.01 1 442 . 66 TRP N N 115.13 0.01 1 443 . 67 VAL H H 8.47 0.01 1 444 . 67 VAL HA H 5.17 0.01 1 445 . 67 VAL HB H 1.81 0.01 1 446 . 67 VAL C C 173.97 0.01 1 447 . 67 VAL CA C 60.08 0.01 1 448 . 67 VAL CB C 34.98 0.01 1 449 . 67 VAL N N 120.76 0.01 1 450 . 68 LEU H H 9.30 0.01 1 451 . 68 LEU C C 173.77 0.01 1 452 . 68 LEU CA C 53.99 0.01 1 453 . 68 LEU CB C 43.61 0.01 1 454 . 68 LEU N N 128.89 0.01 1 455 . 69 VAL H H 9.16 0.01 1 456 . 69 VAL HA H 4.29 0.01 1 457 . 69 VAL HB H 2.23 0.01 1 458 . 69 VAL C C 174.07 0.01 1 459 . 69 VAL CA C 62.49 0.01 1 460 . 69 VAL CB C 32.96 0.01 1 461 . 69 VAL N N 127.95 0.01 1 462 . 70 GLU H H 8.83 0.01 1 463 . 70 GLU HA H 5.01 0.01 1 464 . 70 GLU HB2 H 2.30 0.01 1 465 . 70 GLU C C 171.74 0.01 1 466 . 70 GLU CA C 54.80 0.01 1 467 . 70 GLU N N 134.20 0.01 1 468 . 71 LEU H H 8.66 0.01 1 469 . 71 LEU HA H 4.62 0.01 1 470 . 71 LEU C C 177.35 0.01 1 471 . 71 LEU CA C 53.79 0.01 1 472 . 71 LEU CB C 50.41 0.01 1 473 . 71 LEU N N 117.01 0.01 1 474 . 72 GLY H H 8.74 0.01 1 475 . 72 GLY HA2 H 4.80 0.01 2 476 . 72 GLY HA3 H 3.86 0.01 2 477 . 72 GLY C C 176.31 0.01 1 478 . 72 GLY CA C 44.07 0.01 1 479 . 72 GLY N N 106.07 0.01 1 480 . 73 GLY H H 9.43 0.01 1 481 . 73 GLY HA2 H 4.14 0.01 2 482 . 73 GLY HA3 H 3.69 0.01 2 483 . 73 GLY C C 176.31 0.01 1 484 . 73 GLY CA C 47.14 0.01 1 485 . 73 GLY N N 111.07 0.01 1 486 . 74 ASN H H 8.39 0.01 1 487 . 74 ASN HA H 4.95 0.01 1 488 . 74 ASN HB2 H 2.83 0.01 2 489 . 74 ASN HB3 H 2.50 0.01 2 490 . 74 ASN C C 175.49 0.01 1 491 . 74 ASN CA C 53.53 0.01 1 492 . 74 ASN CB C 38.90 0.01 1 493 . 74 ASN N N 113.26 0.01 1 494 . 75 ASP H H 7.89 0.01 1 495 . 75 ASP HA H 3.82 0.01 1 496 . 75 ASP HB2 H 3.09 0.01 2 497 . 75 ASP C C 178.54 0.01 1 498 . 75 ASP CA C 58.09 0.01 1 499 . 75 ASP CB C 38.67 0.01 1 500 . 75 ASP N N 122.32 0.01 1 501 . 76 GLY H H 9.02 0.01 1 502 . 76 GLY HA2 H 3.64 0.01 2 503 . 76 GLY HA3 H 3.05 0.01 2 504 . 76 GLY C C 177.22 0.01 1 505 . 76 GLY CA C 46.96 0.01 1 506 . 76 GLY N N 108.57 0.01 1 507 . 77 LEU H H 7.47 0.01 1 508 . 77 LEU HA H 4.06 0.01 1 509 . 77 LEU HB2 H 1.80 0.01 2 510 . 77 LEU HB3 H 1.63 0.01 2 511 . 77 LEU C C 178.34 0.01 1 512 . 77 LEU CA C 56.80 0.01 1 513 . 77 LEU CB C 53.70 0.01 1 514 . 77 LEU N N 121.70 0.01 1 515 . 78 ARG H H 7.09 0.01 1 516 . 78 ARG HA H 4.36 0.01 1 517 . 78 ARG HB2 H 2.07 0.01 2 518 . 78 ARG HB3 H 1.58 0.01 2 519 . 78 ARG C C 176.10 0.01 1 520 . 78 ARG CA C 53.70 0.01 1 521 . 78 ARG CB C 29.46 0.01 1 522 . 78 ARG N N 114.51 0.01 1 523 . 79 GLY H H 7.63 0.01 1 524 . 79 GLY HA2 H 4.04 0.01 2 525 . 79 GLY HA3 H 3.67 0.01 2 526 . 79 GLY C C 177.93 0.01 1 527 . 79 GLY CA C 45.56 0.01 1 528 . 79 GLY N N 105.76 0.01 1 529 . 80 PHE H H 7.79 0.01 1 530 . 80 PHE HA H 4.73 0.01 1 531 . 80 PHE HB2 H 2.94 0.01 2 532 . 80 PHE HB3 H 2.89 0.01 2 533 . 80 PHE C C 178.03 0.01 1 534 . 80 PHE CA C 56.61 0.01 1 535 . 80 PHE CB C 38.38 0.01 1 536 . 80 PHE N N 118.57 0.01 1 537 . 81 GLN H H 9.39 0.01 1 538 . 81 GLN HA H 4.78 0.01 1 539 . 81 GLN HB2 H 1.92 0.01 1 540 . 81 GLN HB3 H 1.92 0.01 1 541 . 81 GLN C C 176.25 0.01 1 542 . 81 GLN CA C 54.37 0.01 1 543 . 81 GLN CB C 27.48 0.01 1 544 . 81 GLN N N 124.51 0.01 1 545 . 82 PRO HA H 4.00 0.01 1 546 . 82 PRO C C 177.02 0.01 1 547 . 82 PRO CA C 66.80 0.01 1 548 . 82 PRO CB C 31.43 0.01 1 549 . 83 GLN H H 8.99 0.01 1 550 . 83 GLN HA H 4.07 0.01 1 551 . 83 GLN HB2 H 2.03 0.01 2 552 . 83 GLN HB3 H 2.03 0.01 2 553 . 83 GLN C C 176.92 0.01 1 554 . 83 GLN CA C 59.10 0.01 1 555 . 83 GLN CB C 27.55 0.01 1 556 . 83 GLN N N 113.57 0.01 1 557 . 84 GLN H H 7.61 0.01 1 558 . 84 GLN HA H 4.18 0.01 1 559 . 84 GLN HB2 H 2.27 0.01 1 560 . 84 GLN HB3 H 2.05 0.01 1 561 . 84 GLN C C 179.05 0.01 1 562 . 84 GLN CA C 58.75 0.01 1 563 . 84 GLN CB C 28.44 0.01 1 564 . 84 GLN N N 118.57 0.01 1 565 . 85 THR H H 7.85 0.01 1 566 . 85 THR HA H 3.82 0.01 1 567 . 85 THR HB H 4.16 0.01 1 568 . 85 THR C C 175.49 0.01 1 569 . 85 THR CA C 68.32 0.01 1 570 . 85 THR N N 120.45 0.01 1 571 . 86 GLU H H 8.71 0.01 1 572 . 86 GLU HA H 3.50 0.01 1 573 . 86 GLU C C 177.04 0.01 1 574 . 86 GLU CA C 60.48 0.01 1 575 . 86 GLU CB C 28.97 0.01 1 576 . 86 GLU N N 119.88 0.01 1 577 . 87 GLN H H 7.84 0.01 1 578 . 87 GLN HA H 4.01 0.01 1 579 . 87 GLN HB2 H 2.21 0.01 2 580 . 87 GLN HB3 H 2.08 0.01 2 581 . 87 GLN C C 178.45 0.01 1 582 . 87 GLN CA C 58.44 0.01 1 583 . 87 GLN CB C 27.98 0.01 1 584 . 87 GLN N N 116.13 0.01 1 585 . 88 THR H H 8.11 0.01 1 586 . 88 THR HA H 3.89 0.01 1 587 . 88 THR HB H 4.23 0.01 1 588 . 88 THR CA C 66.68 0.01 1 589 . 88 THR CB C 67.91 0.01 1 590 . 88 THR N N 117.32 0.01 1 591 . 89 LEU H H 8.65 0.01 1 592 . 89 LEU HA H 3.82 0.01 1 593 . 89 LEU C C 178.54 0.01 1 594 . 89 LEU CA C 57.89 0.01 1 595 . 89 LEU CB C 42.46 0.01 1 596 . 89 LEU N N 120.13 0.01 1 597 . 90 ARG H H 8.50 0.01 1 598 . 90 ARG HA H 3.58 0.01 1 599 . 90 ARG HB2 H 2.02 0.01 1 600 . 90 ARG C C 177.22 0.01 1 601 . 90 ARG CA C 60.50 0.01 1 602 . 90 ARG CB C 29.70 0.01 1 603 . 90 ARG N N 118.88 0.01 1 604 . 91 GLN H H 7.46 0.01 1 605 . 91 GLN HA H 3.97 0.01 1 606 . 91 GLN HB2 H 2.32 0.01 2 607 . 91 GLN HB3 H 2.13 0.01 2 608 . 91 GLN C C 178.44 0.01 1 609 . 91 GLN CA C 58.75 0.01 1 610 . 91 GLN CB C 29.00 0.01 1 611 . 91 GLN N N 117.01 0.01 1 612 . 92 ILE H H 8.04 0.01 1 613 . 92 ILE HA H 3.40 0.01 1 614 . 92 ILE HB H 2.14 0.01 1 615 . 92 ILE C C 177.12 0.01 1 616 . 92 ILE CA C 65.97 0.01 1 617 . 92 ILE CB C 37.61 0.01 1 618 . 92 ILE N N 119.51 0.01 1 619 . 93 LEU H H 8.19 0.01 1 620 . 93 LEU HA H 3.42 0.01 1 621 . 93 LEU HB2 H 2.24 0.01 2 622 . 93 LEU HB3 H 1.95 0.01 2 623 . 93 LEU C C 178.64 0.01 1 624 . 93 LEU CA C 58.88 0.01 1 625 . 93 LEU CB C 39.58 0.01 1 626 . 93 LEU N N 118.57 0.01 1 627 . 94 GLN H H 8.21 0.01 1 628 . 94 GLN HA H 3.97 0.01 1 629 . 94 GLN HB2 H 2.30 0.01 2 630 . 94 GLN HB3 H 2.07 0.01 2 631 . 94 GLN C C 178.95 0.01 1 632 . 94 GLN CA C 59.02 0.01 1 633 . 94 GLN N N 117.01 0.01 1 634 . 95 ASP H H 8.45 0.01 1 635 . 95 ASP HA H 4.26 0.01 1 636 . 95 ASP HB2 H 3.12 0.01 1 637 . 95 ASP C C 178.13 0.01 1 638 . 95 ASP CA C 55.40 0.01 1 639 . 95 ASP CB C 36.69 0.01 1 640 . 95 ASP N N 118.88 0.01 1 641 . 96 VAL H H 8.27 0.01 1 642 . 96 VAL HA H 3.36 0.01 1 643 . 96 VAL HB H 2.04 0.01 1 644 . 96 VAL C C 177.42 0.01 1 645 . 96 VAL CA C 67.53 0.01 1 646 . 96 VAL CB C 31.69 0.01 1 647 . 96 VAL N N 119.20 0.01 1 648 . 97 LYS H H 8.04 0.01 1 649 . 97 LYS HA H 4.45 0.01 1 650 . 97 LYS HB2 H 1.95 0.01 2 651 . 97 LYS HB3 H 1.53 0.01 2 652 . 97 LYS C C 180.98 0.01 1 653 . 97 LYS CA C 59.50 0.01 1 654 . 97 LYS CB C 31.59 0.01 1 655 . 97 LYS N N 117.01 0.01 1 656 . 98 ALA H H 8.39 0.01 1 657 . 98 ALA HA H 4.22 0.01 1 658 . 98 ALA HB H 1.50 0.01 1 659 . 98 ALA C C 177.83 0.01 1 660 . 98 ALA CA C 54.14 0.01 1 661 . 98 ALA CB C 18.32 0.01 1 662 . 98 ALA N N 121.38 0.01 1 663 . 99 ALA H H 7.30 0.01 1 664 . 99 ALA HA H 4.45 0.01 1 665 . 99 ALA HB H 1.44 0.01 1 666 . 99 ALA C C 176.10 0.01 1 667 . 99 ALA CA C 51.10 0.01 1 668 . 99 ALA CB C 19.20 0.01 1 669 . 99 ALA N N 119.51 0.01 1 670 . 100 ASN H H 8.14 0.01 1 671 . 100 ASN HA H 4.29 0.01 1 672 . 100 ASN HB2 H 3.06 0.01 2 673 . 100 ASN HB3 H 2.81 0.01 2 674 . 100 ASN C C 173.06 0.01 1 675 . 100 ASN CA C 54.24 0.01 1 676 . 100 ASN CB C 36.55 0.01 1 677 . 100 ASN N N 112.95 0.01 1 678 . 101 ALA H H 7.42 0.01 1 679 . 101 ALA HA H 4.58 0.01 1 680 . 101 ALA HB H 0.90 0.01 1 681 . 101 ALA C C 175.49 0.01 1 682 . 101 ALA CA C 49.22 0.01 1 683 . 101 ALA CB C 21.65 0.01 1 684 . 101 ALA N N 118.26 0.01 1 685 . 102 GLU H H 8.18 0.01 1 686 . 102 GLU HA H 5.04 0.01 1 687 . 102 GLU HB2 H 2.10 0.01 2 688 . 102 GLU HB3 H 2.10 0.01 2 689 . 102 GLU C C 174.49 0.01 1 690 . 102 GLU CA C 51.90 0.01 1 691 . 102 GLU CB C 30.87 0.01 1 692 . 102 GLU N N 120.45 0.01 1 693 . 103 PRO HA H 5.12 0.01 1 694 . 103 PRO C C 174.27 0.01 1 695 . 103 PRO CA C 61.08 0.01 1 696 . 103 PRO CB C 31.83 0.01 1 697 . 104 LEU H H 8.91 0.01 1 698 . 104 LEU HA H 4.60 0.01 1 699 . 104 LEU HB2 H 1.82 0.01 2 700 . 104 LEU HB3 H 1.12 0.01 2 701 . 104 LEU C C 175.09 0.01 1 702 . 104 LEU CA C 53.37 0.01 1 703 . 104 LEU CB C 43.90 0.01 1 704 . 104 LEU N N 119.20 0.01 1 705 . 105 LEU H H 8.45 0.01 1 706 . 105 LEU HA H 4.82 0.01 1 707 . 105 LEU HB2 H 2.08 0.01 2 708 . 105 LEU HB3 H 1.02 0.01 2 709 . 105 LEU C C 173.87 0.01 1 710 . 105 LEU CA C 53.90 0.01 1 711 . 105 LEU CB C 45.49 0.01 1 712 . 105 LEU N N 124.51 0.01 1 713 . 106 MET H H 8.04 0.01 1 714 . 106 MET HA H 4.80 0.01 1 715 . 106 MET HB2 H 2.06 0.01 1 716 . 106 MET C C 174.03 0.01 1 717 . 106 MET CA C 54.71 0.01 1 718 . 106 MET CB C 35.14 0.01 1 719 . 106 MET N N 124.51 0.01 1 720 . 107 GLN H H 8.59 0.01 1 721 . 107 GLN HA H 3.06 0.01 1 722 . 107 GLN C C 172.26 0.01 1 723 . 107 GLN CA C 56.54 0.01 1 724 . 107 GLN N N 125.82 0.01 1 725 . 108 ILE HA H 3.01 0.01 1 726 . 108 ILE HB H 1.53 0.01 1 727 . 108 ILE CA C 56.53 0.01 1 728 . 108 ILE CB C 36.64 0.01 1 729 . 109 ARG HA H 3.50 0.01 1 730 . 109 ARG C C 177.12 0.01 1 731 . 109 ARG CA C 65.13 0.01 1 732 . 109 ARG CB C 31.03 0.01 1 733 . 110 LEU H H 7.21 0.01 1 734 . 110 LEU HA H 4.25 0.01 1 735 . 110 LEU HB2 H 1.67 0.01 2 736 . 110 LEU HB3 H 1.27 0.01 2 737 . 110 LEU C C 178.03 0.01 1 738 . 110 LEU CA C 55.74 0.01 1 739 . 110 LEU CB C 42.43 0.01 1 740 . 110 LEU N N 114.51 0.01 1 741 . 111 PRO HA H 4.26 0.01 1 742 . 111 PRO C C 176.61 0.01 1 743 . 111 PRO CA C 62.21 0.01 1 744 . 111 PRO CB C 31.56 0.01 1 745 . 112 ALA H H 8.10 0.01 1 746 . 112 ALA HA H 3.94 0.01 1 747 . 112 ALA HB H 1.19 0.01 2 748 . 112 ALA C C 178.13 0.01 1 749 . 112 ALA CA C 53.21 0.01 1 750 . 112 ALA CB C 18.59 0.01 1 751 . 112 ALA N N 122.01 0.01 1 752 . 113 ASN H H 8.18 0.01 1 753 . 113 ASN HA H 4.41 0.01 1 754 . 113 ASN HB2 H 2.64 0.01 2 755 . 113 ASN HB3 H 2.62 0.01 2 756 . 113 ASN C C 175.60 0.01 1 757 . 113 ASN CA C 54.00 0.01 1 758 . 113 ASN CB C 37.01 0.01 1 759 . 113 ASN N N 112.32 0.01 1 760 . 114 TYR H H 7.68 0.01 1 761 . 114 TYR HA H 4.46 0.01 1 762 . 114 TYR HB2 H 3.05 0.01 2 763 . 114 TYR HB3 H 2.85 0.01 2 764 . 114 TYR C C 176.81 0.01 1 765 . 114 TYR CA C 57.47 0.01 1 766 . 114 TYR CB C 37.74 0.01 1 767 . 114 TYR N N 119.82 0.01 1 768 . 115 GLY H H 7.92 0.01 1 769 . 115 GLY HA2 H 4.37 0.01 2 770 . 115 GLY HA3 H 3.86 0.01 2 771 . 115 GLY C C 173.66 0.01 1 772 . 115 GLY CA C 44.43 0.01 1 773 . 115 GLY N N 106.70 0.01 1 774 . 116 ARG H H 8.43 0.01 1 775 . 116 ARG HA H 4.06 0.01 1 776 . 116 ARG C C 178.03 0.01 1 777 . 116 ARG CA C 59.57 0.01 1 778 . 116 ARG CB C 30.51 0.01 1 779 . 116 ARG N N 120.45 0.01 1 780 . 117 ARG H H 8.48 0.01 1 781 . 117 ARG HA H 4.61 0.01 1 782 . 117 ARG C C 179.35 0.01 1 783 . 117 ARG CA C 59.41 0.01 1 784 . 117 ARG CB C 29.43 0.01 1 785 . 117 ARG N N 117.95 0.01 1 786 . 118 TYR H H 8.45 0.01 1 787 . 118 TYR HA H 4.09 0.01 1 788 . 118 TYR HB2 H 3.07 0.01 2 789 . 118 TYR HB3 H 2.86 0.01 2 790 . 118 TYR C C 176.81 0.01 1 791 . 118 TYR CA C 61.68 0.01 1 792 . 118 TYR CB C 38.22 0.01 1 793 . 118 TYR N N 120.13 0.01 1 794 . 119 ASN H H 8.52 0.01 1 795 . 119 ASN HA H 4.29 0.01 1 796 . 119 ASN HB2 H 2.97 0.01 2 797 . 119 ASN HB3 H 2.83 0.01 2 798 . 119 ASN C C 178.74 0.01 1 799 . 119 ASN CA C 56.95 0.01 1 800 . 119 ASN CB C 38.05 0.01 1 801 . 119 ASN N N 117.32 0.01 1 802 . 120 GLU H H 8.65 0.01 1 803 . 120 GLU HA H 4.08 0.01 1 804 . 120 GLU HB2 H 2.12 0.01 2 805 . 120 GLU HB3 H 2.12 0.01 2 806 . 120 GLU C C 178.64 0.01 1 807 . 120 GLU CA C 55.16 0.01 1 808 . 120 GLU CB C 32.06 0.01 1 809 . 120 GLU N N 119.20 0.01 1 810 . 121 ALA H H 7.54 0.01 1 811 . 121 ALA HA H 4.13 0.01 1 812 . 121 ALA HB H 1.44 0.01 1 813 . 121 ALA C C 179.66 0.01 1 814 . 121 ALA CA C 54.51 0.01 1 815 . 121 ALA CB C 18.25 0.01 1 816 . 121 ALA N N 121.01 0.01 1 817 . 122 PHE H H 9.09 0.01 1 818 . 122 PHE HA H 3.92 0.01 1 819 . 122 PHE HB2 H 2.86 0.01 2 820 . 122 PHE HB3 H 2.36 0.01 2 821 . 122 PHE C C 177.02 0.01 1 822 . 122 PHE CA C 61.12 0.01 1 823 . 122 PHE CB C 40.37 0.01 1 824 . 122 PHE N N 117.63 0.01 1 825 . 123 SER H H 8.41 0.01 1 826 . 123 SER HA H 4.11 0.01 1 827 . 123 SER HB2 H 1.99 0.01 1 828 . 123 SER C C 176.51 0.01 1 829 . 123 SER CA C 62.52 0.01 1 830 . 123 SER CB C 57.22 0.01 1 831 . 123 SER N N 111.70 0.01 1 832 . 124 ALA H H 7.20 0.01 1 833 . 124 ALA HA H 4.16 0.01 1 834 . 124 ALA HB H 1.49 0.01 1 835 . 124 ALA C C 178.64 0.01 1 836 . 124 ALA CA C 53.38 0.01 1 837 . 124 ALA CB C 18.36 0.01 1 838 . 124 ALA N N 118.88 0.01 1 839 . 125 ILE H H 7.46 0.01 1 840 . 125 ILE HA H 3.32 0.01 1 841 . 125 ILE HB H 1.35 0.01 1 842 . 125 ILE C C 176.51 0.01 1 843 . 125 ILE CA C 65.16 0.01 1 844 . 125 ILE CB C 38.12 0.01 1 845 . 125 ILE N N 116.38 0.01 1 846 . 126 TYR H H 6.70 0.01 1 847 . 126 TYR HA H 3.84 0.01 1 848 . 126 TYR HB2 H 3.13 0.01 2 849 . 126 TYR HB3 H 2.69 0.01 2 850 . 126 TYR C C 174.29 0.01 1 851 . 126 TYR CA C 64.21 0.01 1 852 . 126 TYR CB C 35.78 0.01 1 853 . 126 TYR N N 113.26 0.01 1 854 . 127 PRO HA H 4.15 0.01 1 855 . 127 PRO C C 179.15 0.01 1 856 . 127 PRO CA C 65.33 0.01 1 857 . 127 PRO CB C 30.30 0.01 1 858 . 128 LYS H H 6.84 0.01 1 859 . 128 LYS HA H 3.99 0.01 1 860 . 128 LYS HB2 H 1.85 0.01 1 861 . 128 LYS C C 179.35 0.01 1 862 . 128 LYS CA C 59.76 0.01 1 863 . 128 LYS CB C 32.17 0.01 1 864 . 128 LYS N N 117.01 0.01 1 865 . 129 LEU H H 8.30 0.01 1 866 . 129 LEU HA H 4.18 0.01 1 867 . 129 LEU HB2 H 1.74 0.01 2 868 . 129 LEU HB3 H 1.14 0.01 2 869 . 129 LEU C C 176.71 0.01 1 870 . 129 LEU CA C 57.38 0.01 1 871 . 129 LEU CB C 42.18 0.01 1 872 . 129 LEU N N 118.88 0.01 1 873 . 130 ALA H H 8.33 0.01 1 874 . 130 ALA HA H 4.04 0.01 1 875 . 130 ALA HB H 2.56 0.01 1 876 . 130 ALA C C 179.86 0.01 1 877 . 130 ALA CA C 55.49 0.01 1 878 . 130 ALA CB C 18.25 0.01 1 879 . 130 ALA N N 120.76 0.01 1 880 . 131 LYS H H 7.65 0.01 1 881 . 131 LYS HA H 4.23 0.01 1 882 . 131 LYS HB2 H 1.94 0.01 2 883 . 131 LYS HB3 H 1.61 0.01 2 884 . 131 LYS C C 179.35 0.01 1 885 . 131 LYS CA C 58.48 0.01 1 886 . 131 LYS CB C 32.51 0.01 1 887 . 131 LYS N N 115.45 0.01 1 888 . 132 GLU H H 8.27 0.01 1 889 . 132 GLU HA H 3.83 0.01 1 890 . 132 GLU HB2 H 1.61 0.01 2 891 . 132 GLU HB3 H 1.61 0.01 2 892 . 132 GLU C C 178.03 0.01 1 893 . 132 GLU CA C 59.07 0.01 1 894 . 132 GLU CB C 29.73 0.01 1 895 . 132 GLU N N 119.82 0.01 1 896 . 133 PHE H H 8.07 0.01 1 897 . 133 PHE HA H 4.30 0.01 1 898 . 133 PHE HB2 H 3.15 0.01 2 899 . 133 PHE HB3 H 2.77 0.01 2 900 . 133 PHE C C 174.27 0.01 1 901 . 133 PHE CA C 59.00 0.01 1 902 . 133 PHE CB C 40.37 0.01 1 903 . 133 PHE N N 112.01 0.01 1 904 . 134 ASP H H 7.96 0.01 1 905 . 134 ASP HA H 4.46 0.01 1 906 . 134 ASP HB2 H 3.29 0.01 2 907 . 134 ASP HB3 H 2.55 0.01 2 908 . 134 ASP C C 174.68 0.01 1 909 . 134 ASP CA C 54.35 0.01 1 910 . 134 ASP CB C 37.31 0.01 1 911 . 134 ASP N N 121.70 0.01 1 912 . 135 VAL H H 8.39 0.01 1 913 . 135 VAL HA H 4.99 0.01 1 914 . 135 VAL HB H 2.56 0.01 1 915 . 135 VAL C C 173.03 0.01 1 916 . 135 VAL CA C 57.21 0.01 1 917 . 135 VAL CB C 31.84 0.01 1 918 . 135 VAL N N 112.01 0.01 1 919 . 136 PRO HA H 4.23 0.01 1 920 . 136 PRO C C 174.07 0.01 1 921 . 136 PRO CA C 63.54 0.01 1 922 . 136 PRO CB C 32.79 0.01 1 923 . 137 LEU H H 8.01 0.01 1 924 . 137 LEU HA H 5.29 0.01 1 925 . 137 LEU HB2 H 1.89 0.01 1 926 . 137 LEU C C 176.88 0.01 1 927 . 137 LEU CA C 52.17 0.01 1 928 . 137 LEU CB C 43.61 0.01 1 929 . 137 LEU N N 122.70 0.01 1 930 . 138 LEU H H 9.23 0.01 1 931 . 138 LEU HA H 4.82 0.01 1 932 . 138 LEU HB2 H 1.74 0.01 1 933 . 138 LEU C C 173.58 0.01 1 934 . 138 LEU CA C 51.94 0.01 1 935 . 138 LEU CB C 42.58 0.01 1 936 . 138 LEU N N 129.57 0.01 1 937 . 139 PRO HA H 4.55 0.01 1 938 . 139 PRO C C 174.78 0.01 1 939 . 139 PRO CA C 61.81 0.01 1 940 . 139 PRO CB C 31.98 0.01 1 941 . 140 PHE H H 8.65 0.01 1 942 . 140 PHE HA H 4.83 0.01 1 943 . 140 PHE HB2 H 3.04 0.01 2 944 . 140 PHE HB3 H 3.04 0.01 2 945 . 140 PHE C C 179.21 0.01 1 946 . 140 PHE CA C 54.52 0.01 1 947 . 140 PHE N N 117.70 0.01 1 948 . 141 PHE H H 6.86 0.01 1 949 . 141 PHE HA H 4.35 0.01 1 950 . 141 PHE HB2 H 3.18 0.01 2 951 . 141 PHE HB3 H 3.00 0.01 2 952 . 141 PHE C C 175.27 0.01 1 953 . 141 PHE N N 125.82 0.01 1 954 . 142 MET HA H 4.34 0.01 1 955 . 142 MET C C 176.61 0.01 1 956 . 142 MET CA C 53.17 0.01 1 957 . 142 MET CB C 28.50 0.01 1 958 . 143 GLU H H 7.02 0.01 1 959 . 143 GLU HA H 4.00 0.01 1 960 . 143 GLU HB2 H 2.14 0.01 2 961 . 143 GLU HB3 H 1.98 0.01 2 962 . 143 GLU C C 178.13 0.01 1 963 . 143 GLU CA C 58.84 0.01 1 964 . 143 GLU CB C 28.17 0.01 1 965 . 143 GLU N N 115.76 0.01 1 966 . 144 GLU H H 7.16 0.01 1 967 . 144 GLU HA H 4.16 0.01 1 968 . 144 GLU HB2 H 2.10 0.01 2 969 . 144 GLU HB3 H 1.07 0.01 2 970 . 144 GLU C C 176.61 0.01 1 971 . 144 GLU CA C 56.87 0.01 1 972 . 144 GLU CB C 29.24 0.01 1 973 . 144 GLU N N 112.63 0.01 1 974 . 145 VAL H H 6.90 0.01 1 975 . 145 VAL HA H 3.79 0.01 1 976 . 145 VAL HB H 1.80 0.01 1 977 . 145 VAL C C 179.05 0.01 1 978 . 145 VAL CA C 64.65 0.01 1 979 . 145 VAL CB C 32.03 0.01 1 980 . 145 VAL N N 118.57 0.01 1 981 . 146 TYR H H 7.83 0.01 1 982 . 146 TYR HA H 4.49 0.01 1 983 . 146 TYR C C 177.01 0.01 1 984 . 146 TYR CA C 58.54 0.01 1 985 . 146 TYR CB C 38.45 0.01 1 986 . 146 TYR N N 113.95 0.01 1 987 . 147 LEU H H 8.10 0.01 1 988 . 147 LEU HA H 4.18 0.01 1 989 . 147 LEU HB2 H 1.57 0.01 2 990 . 147 LEU HB3 H 1.50 0.01 2 991 . 147 LEU C C 177.37 0.01 1 992 . 147 LEU CA C 55.44 0.01 1 993 . 147 LEU CB C 41.98 0.01 1 994 . 147 LEU N N 122.38 0.01 1 995 . 148 LYS H H 7.99 0.01 1 996 . 148 LYS HA H 4.11 0.01 1 997 . 148 LYS C C 176.08 0.01 1 998 . 148 LYS CA C 56.16 0.01 1 999 . 148 LYS CB C 29.41 0.01 1 1000 . 148 LYS N N 118.95 0.01 1 1001 . 149 PRO C C 178.95 0.01 1 1002 . 149 PRO CA C 65.47 0.01 1 1003 . 149 PRO CB C 31.63 0.01 1 1004 . 150 GLN H H 9.09 0.01 1 1005 . 150 GLN HA H 4.26 0.01 1 1006 . 150 GLN HB2 H 1.96 0.01 1 1007 . 150 GLN C C 176.51 0.01 1 1008 . 150 GLN CA C 57.37 0.01 1 1009 . 150 GLN CB C 26.64 0.01 1 1010 . 150 GLN N N 114.82 0.01 1 1011 . 151 TRP H H 8.52 0.01 1 1012 . 151 TRP HA H 5.31 0.01 1 1013 . 151 TRP HB2 H 3.42 0.01 2 1014 . 151 TRP HB3 H 3.41 0.01 2 1015 . 151 TRP C C 175.29 0.01 1 1016 . 151 TRP CA C 54.34 0.01 1 1017 . 151 TRP CB C 31.36 0.01 1 1018 . 151 TRP N N 122.63 0.01 1 1019 . 152 MET H H 7.36 0.01 1 1020 . 152 MET HA H 5.32 0.01 1 1021 . 152 MET HB2 H 2.03 0.01 1 1022 . 152 MET C C 177.83 0.01 1 1023 . 152 MET CA C 51.90 0.01 1 1024 . 152 MET CB C 32.03 0.01 1 1025 . 152 MET N N 117.63 0.01 1 1026 . 153 GLN H H 8.66 0.01 1 1027 . 153 GLN HA H 4.59 0.01 1 1028 . 153 GLN HB2 H 2.20 0.01 2 1029 . 153 GLN HB3 H 1.35 0.01 2 1030 . 153 GLN C C 177.32 0.01 1 1031 . 153 GLN CA C 56.62 0.01 1 1032 . 153 GLN CB C 28.30 0.01 1 1033 . 153 GLN N N 117.32 0.01 1 1034 . 154 ASP H H 8.98 0.01 1 1035 . 154 ASP HA H 4.31 0.01 1 1036 . 154 ASP HB2 H 2.84 0.01 1 1037 . 154 ASP C C 175.80 0.01 1 1038 . 154 ASP CA C 55.75 0.01 1 1039 . 154 ASP CB C 39.17 0.01 1 1040 . 154 ASP N N 120.13 0.01 1 1041 . 155 ASP H H 7.27 0.01 1 1042 . 155 ASP HA H 4.41 0.01 1 1043 . 155 ASP HB2 H 3.04 0.01 1 1044 . 155 ASP HB3 H 2.88 0.01 1 1045 . 155 ASP C C 177.12 0.01 1 1046 . 155 ASP CA C 53.49 0.01 1 1047 . 155 ASP CB C 39.97 0.01 1 1048 . 155 ASP N N 114.82 0.01 1 1049 . 156 GLY H H 8.16 0.01 1 1050 . 156 GLY HA2 H 4.02 0.01 2 1051 . 156 GLY HA3 H 3.66 0.01 2 1052 . 156 GLY C C 172.95 0.01 1 1053 . 156 GLY CA C 46.09 0.01 1 1054 . 156 GLY N N 107.63 0.01 1 1055 . 157 ILE H H 8.47 0.01 1 1056 . 157 ILE HA H 4.03 0.01 1 1057 . 157 ILE HB H 0.93 0.01 1 1058 . 157 ILE C C 175.09 0.01 1 1059 . 157 ILE CA C 61.36 0.01 1 1060 . 157 ILE CB C 41.88 0.01 1 1061 . 157 ILE N N 117.63 0.01 1 1062 . 158 HIS H H 8.69 0.01 1 1063 . 158 HIS HA H 4.76 0.01 1 1064 . 158 HIS HB2 H 3.26 0.01 2 1065 . 158 HIS HB3 H 4.07 0.01 2 1066 . 158 HIS C C 171.88 0.01 1 1067 . 158 HIS CA C 55.47 0.01 1 1068 . 158 HIS CB C 29.30 0.01 1 1069 . 158 HIS N N 115.76 0.01 1 1070 . 159 PRO HA H 3.50 0.01 1 1071 . 159 PRO C C 177.12 0.01 1 1072 . 159 PRO CA C 64.74 0.01 1 1073 . 159 PRO CB C 32.03 0.01 1 1074 . 160 ASN H H 7.82 0.01 1 1075 . 160 ASN HA H 4.25 0.01 1 1076 . 160 ASN C C 178.03 0.01 1 1077 . 160 ASN CA C 58.54 0.01 1 1078 . 160 ASN CB C 38.45 0.01 1 1079 . 160 ASN N N 113.95 0.01 1 1080 . 161 ARG H H 7.38 0.01 1 1081 . 161 ARG HA H 3.55 0.01 . 1082 . 161 ARG C C 175.49 0.01 1 1083 . 161 ARG CA C 61.12 0.01 1 1084 . 161 ARG CB C 31.25 0.01 1 1085 . 161 ARG N N 112.01 0.01 1 1086 . 162 ASP H H 7.46 0.01 1 1087 . 162 ASP HA H 4.56 0.01 1 1088 . 162 ASP HB2 H 2.67 0.01 2 1089 . 162 ASP HB3 H 2.55 0.01 2 1090 . 162 ASP C C 174.99 0.01 1 1091 . 162 ASP CA C 53.03 0.01 1 1092 . 162 ASP CB C 38.63 0.01 1 1093 . 162 ASP N N 118.26 0.01 1 1094 . 164 GLN H H 8.41 0.01 1 1095 . 164 GLN HA H 4.22 0.01 1 1096 . 164 GLN C C 176.20 0.01 1 1097 . 164 GLN CA C 54.45 0.01 1 1098 . 164 GLN CB C 40.39 0.01 1 1099 . 164 GLN N N 120.19 0.01 1 1100 . 165 PRO HA H 3.62 0.01 1 1101 . 165 PRO C C 178.54 0.01 1 1102 . 165 PRO CA C 66.40 0.01 1 1103 . 165 PRO CB C 30.50 0.01 1 1104 . 166 PHE H H 7.17 0.01 1 1105 . 166 PHE HA H 4.05 0.01 1 1106 . 166 PHE HB2 H 2.67 0.01 2 1107 . 166 PHE HB3 H 2.34 0.01 2 1108 . 166 PHE C C 177.53 0.01 1 1109 . 166 PHE CA C 60.89 0.01 1 1110 . 166 PHE CB C 38.33 0.01 1 1111 . 166 PHE N N 117.32 0.01 1 1112 . 167 ILE H H 7.79 0.01 1 1113 . 167 ILE HA H 2.78 0.01 1 1114 . 167 ILE HB H 1.14 0.01 1 1115 . 167 ILE C C 177.42 0.01 1 1116 . 167 ILE CA C 65.26 0.01 1 1117 . 167 ILE CB C 38.18 0.01 1 1118 . 167 ILE N N 119.20 0.01 1 1119 . 168 ALA H H 8.44 0.01 1 1120 . 168 ALA HA H 4.37 0.01 1 1121 . 168 ALA HB H 1.67 0.01 1 1122 . 168 ALA C C 178.44 0.01 1 1123 . 168 ALA CA C 55.90 0.01 1 1124 . 168 ALA CB C 18.67 0.01 1 1125 . 168 ALA N N 119.82 0.01 1 1126 . 169 ASP H H 7.70 0.01 1 1127 . 169 ASP HA H 4.14 0.01 1 1128 . 169 ASP HB2 H 2.63 0.01 2 1129 . 169 ASP HB3 H 2.56 0.01 2 1130 . 169 ASP C C 177.63 0.01 1 1131 . 169 ASP CA C 57.02 0.01 1 1132 . 169 ASP CB C 40.24 0.01 1 1133 . 169 ASP N N 117.32 0.01 1 1134 . 170 TRP H H 8.43 0.01 1 1135 . 170 TRP HA H 3.73 0.01 1 1136 . 170 TRP HB2 H 2.89 0.01 2 1137 . 170 TRP C C 179.46 0.01 1 1138 . 170 TRP CA C 61.76 0.01 1 1139 . 170 TRP CB C 28.97 0.01 1 1140 . 170 TRP N N 122.63 0.01 1 1141 . 171 MET H H 8.95 0.01 1 1142 . 171 MET HA H 4.07 0.01 1 1143 . 171 MET C C 178.44 0.01 1 1144 . 171 MET CA C 55.54 0.01 1 1145 . 171 MET CB C 29.41 0.01 1 1146 . 171 MET N N 117.01 0.01 1 1147 . 172 ALA H H 8.34 0.01 1 1148 . 172 ALA HA H 3.76 0.01 1 1149 . 172 ALA HB H 1.29 0.01 1 1150 . 172 ALA C C 179.66 0.01 1 1151 . 172 ALA CA C 55.49 0.01 1 1152 . 172 ALA CB C 16.79 0.01 1 1153 . 172 ALA N N 122.01 0.01 1 1154 . 173 LYS H H 7.35 0.01 1 1155 . 173 LYS HA H 3.90 0.01 1 1156 . 173 LYS HB2 H 1.65 0.01 1 1157 . 173 LYS C C 179.35 0.01 1 1158 . 173 LYS CA C 58.93 0.01 1 1159 . 173 LYS CB C 32.00 0.01 1 1160 . 173 LYS N N 115.76 0.01 1 1161 . 174 GLN H H 7.53 0.01 1 1162 . 174 GLN HA H 3.67 0.01 1 1163 . 174 GLN HB2 H 1.80 0.01 1 1164 . 174 GLN HB3 H 1.46 0.01 1 1165 . 174 GLN C C 177.93 0.01 1 1166 . 174 GLN N N 115.45 0.01 1 1167 . 175 LEU H H 8.34 0.01 1 1168 . 175 LEU HA H 4.11 0.01 1 1169 . 175 LEU HB2 H 1.99 0.01 1 1170 . 175 LEU HB3 H 1.31 0.01 1 1171 . 175 LEU C C 178.24 0.01 1 1172 . 175 LEU CA C 55.84 0.01 1 1173 . 175 LEU CB C 43.25 0.01 1 1174 . 176 GLN H H 8.05 0.01 1 1175 . 176 GLN HA H 3.91 0.01 1 1176 . 176 GLN C C 173.94 0.01 1 1177 . 176 GLN CA C 61.19 0.01 1 1178 . 176 GLN N N 120.76 0.01 1 1179 . 177 PRO HA H 4.50 0.01 1 1180 . 177 PRO C C 177.12 0.01 1 1181 . 177 PRO CA C 61.68 0.01 1 1182 . 177 PRO CB C 32.22 0.01 1 1183 . 178 LEU H H 6.86 0.01 1 1184 . 178 LEU HA H 4.09 0.01 1 1185 . 178 LEU HB2 H 1.56 0.01 1 1186 . 178 LEU C C 176.92 0.01 1 1187 . 178 LEU CA C 51.09 0.01 1 1188 . 178 LEU N N 112.95 0.01 1 1189 . 179 VAL H H 8.79 0.01 1 1190 . 179 VAL HA H 3.58 0.01 1 1191 . 179 VAL HB H 1.18 0.01 1 1192 . 179 VAL C C 178.74 0.01 1 1193 . 179 VAL CA C 59.87 0.01 1 1194 . 179 VAL CB C 30.44 0.01 1 1195 . 179 VAL N N 119.82 0.01 1 1196 . 180 ASN H H 7.96 0.01 1 1197 . 180 ASN HA H 4.35 0.01 1 1198 . 180 ASN HB2 H 2.90 0.01 2 1199 . 180 ASN HB3 H 2.80 0.01 2 1200 . 180 ASN C C 176.31 0.01 1 1201 . 180 ASN CA C 56.14 0.01 1 1202 . 180 ASN CB C 39.48 0.01 1 1203 . 180 ASN N N 119.82 0.01 1 1204 . 181 HIS H H 7.45 0.01 1 1205 . 181 HIS HA H 2.81 0.01 1 1206 . 181 HIS HB2 H 1.38 0.01 1 1207 . 181 HIS C C 178.27 0.01 1 1208 . 181 HIS CA C 55.93 0.01 1 1209 . 181 HIS CB C 28.86 0.01 1 1210 . 181 HIS N N 117.63 0.01 1 stop_ save_