data_6622 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for HEWL-SMe ; _BMRB_accession_number 6622 _BMRB_flat_file_name bmr6622.str _Entry_type original _Submission_date 2005-05-10 _Accession_date 2005-05-10 _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 Schlorb Christian . . 2 Ackermann Katrin . . 3 Richter Christian . . 4 Wirmer Julia . . 5 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 402 "13C chemical shifts" 332 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlorb Christian . . 2 Ackermann Katrin . . 3 Richter Christian . . 4 Wirmer Julia . . 5 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 33 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 95 _Page_last 104 _Year 2005 _Details . loop_ _Keyword lysozyme 'inclusion bodies' 'non-native proteins' 'resonance assignment' 'isotope enrichment' 'tryptophan side chains' stop_ save_ ################################## # Molecular system description # ################################## save_system_HEWL-SMe _Saveframe_category molecular_system _Mol_system_name 'reduced and S-methylated hen egg white lysozyme' _Abbreviation_common HEWL-SMe _Enzyme_commission_number 3.2.1.17 loop_ _Mol_system_component_name _Mol_label hewl-sme $hewl-sme stop_ _System_molecular_weight . _System_physical_state reduced _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hewl-sme _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Hen egg white lysozyme' _Name_variant SMe _Abbreviation_common HEWL-SMe _Molecular_mass 14444.3 _Mol_thiol_state 'all other bound' _Details 'reduced disulfide bridges, all cysteins are S-methylated' ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRXELAAAMKRHGLDN YRGYSLGNWVXAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWXNDGRTPGSRNLXNIP XSALLSSDITASVNXAKKIV SDGNGMNAWVAWRNRXKGTD VQAWIRGXRL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 VAL 4 PHE 5 GLY 6 ARG 7 SMC 8 GLU 9 LEU 10 ALA 11 ALA 12 ALA 13 MET 14 LYS 15 ARG 16 HIS 17 GLY 18 LEU 19 ASP 20 ASN 21 TYR 22 ARG 23 GLY 24 TYR 25 SER 26 LEU 27 GLY 28 ASN 29 TRP 30 VAL 31 SMC 32 ALA 33 ALA 34 LYS 35 PHE 36 GLU 37 SER 38 ASN 39 PHE 40 ASN 41 THR 42 GLN 43 ALA 44 THR 45 ASN 46 ARG 47 ASN 48 THR 49 ASP 50 GLY 51 SER 52 THR 53 ASP 54 TYR 55 GLY 56 ILE 57 LEU 58 GLN 59 ILE 60 ASN 61 SER 62 ARG 63 TRP 64 TRP 65 SMC 66 ASN 67 ASP 68 GLY 69 ARG 70 THR 71 PRO 72 GLY 73 SER 74 ARG 75 ASN 76 LEU 77 SMC 78 ASN 79 ILE 80 PRO 81 SMC 82 SER 83 ALA 84 LEU 85 LEU 86 SER 87 SER 88 ASP 89 ILE 90 THR 91 ALA 92 SER 93 VAL 94 ASN 95 SMC 96 ALA 97 LYS 98 LYS 99 ILE 100 VAL 101 SER 102 ASP 103 GLY 104 ASN 105 GLY 106 MET 107 ASN 108 ALA 109 TRP 110 VAL 111 ALA 112 TRP 113 ARG 114 ASN 115 ARG 116 SMC 117 LYS 118 GLY 119 THR 120 ASP 121 VAL 122 GLN 123 ALA 124 TRP 125 ILE 126 ARG 127 GLY 128 SMC 129 ARG 130 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2005-12-09 save_ ###################### # Polymer residues # ###################### save_chem_comp_SMC _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common S-METHYLCYSTEINE _BMRB_code SMC _PDB_code SMC _Standard_residue_derivative . _Molecular_mass 135.185 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CS CS C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HCS1 HCS1 H . 0 . ? HCS2 HCS2 H . 0 . ? HCS3 HCS3 H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? SG SG S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB SG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING SG CS ? ? SING CS HCS1 ? ? SING CS HCS2 ? ? SING CS HCS3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hewl-sme Chicken 9031 Eukaryota Metazoa Gallus gallus 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 $hewl-sme 'recombinant technology' . . . . . 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 $hewl-sme 0.5 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 700 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 0.1 pH temperature 293 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name hewl-sme _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 LYS H H 8.694 0.05 1 2 . 2 LYS C C 171.8758 0.2 1 3 . 2 LYS CA C 56.1468 0.2 1 4 . 2 LYS CB C 32.9638 0.2 1 5 . 2 LYS N N 126.101 0.1 1 6 . 3 VAL H H 8.26 0.05 1 7 . 3 VAL HA H 4.07 0.05 1 8 . 3 VAL HB H 1.946 0.05 1 9 . 3 VAL C C 176.3528 0.2 1 10 . 3 VAL CA C 61.7318 0.2 1 11 . 3 VAL CB C 32.8878 0.2 1 12 . 3 VAL N N 124.096 0.1 1 13 . 4 PHE H H 8.522 0.05 1 14 . 4 PHE HA H 4.623 0.05 1 15 . 4 PHE HB2 H 3.053 0.05 1 16 . 4 PHE HB3 H 3.053 0.05 1 17 . 4 PHE C C 175.5678 0.2 1 18 . 4 PHE CA C 57.7528 0.2 1 19 . 4 PHE CB C 39.7738 0.2 1 20 . 4 PHE N N 126.316 0.1 1 21 . 5 GLY H H 8.368 0.05 1 22 . 5 GLY HA2 H 3.913 0.05 1 23 . 5 GLY HA3 H 3.913 0.05 1 24 . 5 GLY C C 176.0848 0.2 1 25 . 5 GLY CA C 44.8998 0.2 1 26 . 5 GLY N N 111.865 0.1 1 27 . 6 ARG H H 8.279 0.05 1 28 . 6 ARG C C 173.8378 0.2 1 29 . 6 ARG CA C 56.2998 0.2 1 30 . 6 ARG CB C 30.5158 0.2 1 31 . 6 ARG N N 121.903 0.1 1 32 . 7 SMC HA H 4.541 0.05 1 33 . 7 SMC HB2 H 2.907 0.05 1 34 . 7 SMC HB3 H 2.907 0.05 1 35 . 8 GLU H H 8.527 0.05 1 36 . 8 GLU HA H 4.347 0.05 1 37 . 8 GLU HB2 H 2.0135 0.05 1 38 . 8 GLU HB3 H 2.0135 0.05 1 39 . 8 GLU C C 175.3718 0.2 1 40 . 8 GLU CA C 56.0698 0.2 1 41 . 8 GLU CB C 28.3738 0.2 1 42 . 8 GLU N N 124.525 0.1 1 43 . 9 LEU H H 8.206 0.05 1 44 . 9 LEU HA H 4.264 0.05 1 45 . 9 LEU HB2 H 1.595 0.05 1 46 . 9 LEU HB3 H 1.595 0.05 1 47 . 9 LEU C C 176.0848 0.2 1 48 . 9 LEU CA C 55.5338 0.2 1 49 . 9 LEU CB C 42.0688 0.2 1 50 . 9 LEU N N 124.481 0.1 1 51 . 10 ALA H H 8.247 0.05 1 52 . 10 ALA HA H 4.362 0.05 1 53 . 10 ALA HB H 1.385 0.05 1 54 . 10 ALA C C 177.4228 0.2 1 55 . 10 ALA CA C 53.0098 0.2 1 56 . 10 ALA CB C 18.6568 0.2 1 57 . 10 ALA N N 125.552 0.1 1 58 . 11 ALA H H 8.158 0.05 1 59 . 11 ALA HA H 4.205 0.05 1 60 . 11 ALA HB H 1.4 0.05 1 61 . 11 ALA C C 176.6378 0.2 1 62 . 11 ALA CA C 53.0858 0.2 1 63 . 11 ALA CB C 18.5808 0.2 1 64 . 11 ALA N N 123.273 0.1 1 65 . 12 ALA H H 8.18 0.05 1 66 . 12 ALA HA H 4.212 0.05 1 67 . 12 ALA HB H 1.393 0.05 1 68 . 12 ALA C C 178.3688 0.2 1 69 . 12 ALA CA C 53.1628 0.2 1 70 . 12 ALA CB C 18.6568 0.2 1 71 . 12 ALA N N 123.54 0.1 1 72 . 13 MET H H 8.116 0.05 1 73 . 13 MET C C 178.3688 0.2 1 74 . 13 MET CA C 56.0698 0.2 1 75 . 13 MET CB C 32.6578 0.2 1 76 . 13 MET N N 119.79 0.1 1 77 . 17 GLY H H 8.444 0.05 1 78 . 17 GLY HA2 H 3.943 0.05 1 79 . 17 GLY HA3 H 3.943 0.05 1 80 . 17 GLY C C 174.7478 0.2 1 81 . 17 GLY CA C 45.1288 0.2 1 82 . 17 GLY N N 111.287 0.1 1 83 . 18 LEU H H 8.223 0.05 1 84 . 18 LEU HA H 4.324 0.05 1 85 . 18 LEU HB2 H 1.572 0.05 1 86 . 18 LEU HB3 H 1.572 0.05 1 87 . 18 LEU C C 173.8908 0.2 1 88 . 18 LEU CA C 55.3808 0.2 1 89 . 18 LEU CB C 42.2978 0.2 1 90 . 18 LEU N N 122.759 0.1 1 91 . 19 ASP H H 8.525 0.05 1 92 . 19 ASP HA H 4.623 0.05 1 93 . 19 ASP HB2 H 2.769 0.05 1 94 . 19 ASP HB3 H 2.769 0.05 1 95 . 19 ASP C C 177.2628 0.2 1 96 . 19 ASP CA C 52.7798 0.2 1 97 . 19 ASP CB C 37.8608 0.2 1 98 . 19 ASP N N 120.514 0.1 1 99 . 20 ASN H H 8.309 0.05 1 100 . 20 ASN HA H 4.638 0.05 1 101 . 20 ASN HB2 H 2.686 0.05 1 102 . 20 ASN HB3 H 2.686 0.05 1 103 . 20 ASN C C 174.6938 0.2 1 104 . 20 ASN CA C 53.0098 0.2 1 105 . 20 ASN CB C 38.3958 0.2 1 106 . 20 ASN N N 120.22 0.1 1 107 . 21 TYR H H 8.069 0.05 1 108 . 21 TYR HA H 4.489 0.05 1 109 . 21 TYR HB2 H 2.963 0.05 1 110 . 21 TYR HB3 H 2.963 0.05 1 111 . 21 TYR C C 174.6938 0.2 1 112 . 21 TYR CA C 57.9058 0.2 1 113 . 21 TYR CB C 38.4728 0.2 1 114 . 21 TYR N N 121.777 0.1 1 115 . 22 ARG H H 8.247 0.05 1 116 . 22 ARG HA H 4.182 0.05 1 117 . 22 ARG HB2 H 1.673 0.05 1 118 . 22 ARG HB3 H 1.673 0.05 1 119 . 22 ARG C C 175.7458 0.2 1 120 . 22 ARG CA C 55.9938 0.2 1 121 . 22 ARG CB C 30.1328 0.2 1 122 . 22 ARG N N 124.602 0.1 1 123 . 23 GLY H H 7.752 0.05 1 124 . 23 GLY HA2 H 3.808 0.05 1 125 . 23 GLY HA3 H 3.808 0.05 1 126 . 23 GLY C C 176.2278 0.2 1 127 . 23 GLY CA C 44.9758 0.2 1 128 . 23 GLY N N 109.957 0.1 1 129 . 24 TYR H H 7.948 0.05 1 130 . 24 TYR HA H 4.556 0.05 1 131 . 24 TYR HB2 H 2.9295 0.05 1 132 . 24 TYR HB3 H 2.9295 0.05 1 133 . 24 TYR C C 173.5518 0.2 1 134 . 24 TYR CA C 57.5998 0.2 1 135 . 24 TYR CB C 38.8548 0.2 1 136 . 24 TYR N N 120.984 0.1 1 137 . 25 SER H H 8.262 0.05 1 138 . 25 SER HA H 4.399 0.05 1 139 . 25 SER HB2 H 3.786 0.05 1 140 . 25 SER HB3 H 3.786 0.05 1 141 . 25 SER C C 175.7998 0.2 1 142 . 25 SER CA C 57.9828 0.2 1 143 . 25 SER CB C 40.9498 0.2 1 144 . 25 SER N N 118.764 0.1 1 145 . 26 LEU H H 8.218 0.05 1 146 . 26 LEU HA H 4.287 0.05 1 147 . 26 LEU HB2 H 1.595 0.05 1 148 . 26 LEU HB3 H 1.595 0.05 1 149 . 26 LEU C C 174.2478 0.2 1 150 . 26 LEU CA C 55.5338 0.2 1 151 . 26 LEU CB C 63.8738 0.2 1 152 . 26 LEU N N 125.152 0.1 1 153 . 27 GLY H H 8.194 0.05 1 154 . 27 GLY HA2 H 3.786 0.05 1 155 . 27 GLY HA3 H 3.786 0.05 1 156 . 27 GLY C C 177.6728 0.2 1 157 . 27 GLY CA C 45.2058 0.2 1 158 . 27 GLY N N 109.707 0.1 1 159 . 28 ASN H H 8.169 0.05 1 160 . 28 ASN HA H 4.668 0.05 1 161 . 28 ASN HB2 H 2.672 0.05 1 162 . 28 ASN HB3 H 2.672 0.05 1 163 . 28 ASN C C 173.7308 0.2 1 164 . 28 ASN CA C 53.0098 0.2 1 165 . 28 ASN CB C 38.6258 0.2 1 166 . 28 ASN N N 119.792 0.1 1 167 . 29 TRP H H 8.073 0.05 1 168 . 29 TRP HA H 4.616 0.05 1 169 . 29 TRP HB2 H 3.225 0.05 1 170 . 29 TRP HB3 H 3.225 0.05 1 171 . 29 TRP C C 174.8898 0.2 1 172 . 29 TRP CA C 57.5238 0.2 1 173 . 29 TRP CB C 29.2148 0.2 1 174 . 29 TRP N N 122.759 0.1 1 175 . 30 VAL H H 7.844 0.05 1 176 . 30 VAL HA H 3.92 0.05 1 177 . 30 VAL HB H 1.909 0.05 2 178 . 30 VAL C C 176.1568 0.2 1 179 . 30 VAL CA C 62.3438 0.2 1 180 . 30 VAL CB C 32.6578 0.2 1 181 . 30 VAL N N 122.832 0.1 1 182 . 31 SMC H H 8.134 0.05 1 183 . 31 SMC HA H 4.362 0.05 1 184 . 31 SMC HB2 H 2.8135 0.05 1 185 . 31 SMC HB3 H 2.8135 0.05 1 186 . 31 SMC C C 175.6748 0.2 1 187 . 31 SMC CA C 55.3048 0.2 1 188 . 31 SMC CB C 36.8658 0.2 1 189 . 31 SMC N N 123.881 0.1 1 190 . 32 ALA H H 8.385 0.05 1 191 . 32 ALA HA H 4.205 0.05 1 192 . 32 ALA HB H 1.37 0.05 1 193 . 32 ALA C C 174.8548 0.2 1 194 . 32 ALA CA C 52.9328 0.2 1 195 . 32 ALA CB C 18.8098 0.2 1 196 . 32 ALA N N 127.822 0.1 1 197 . 33 ALA H H 8.111 0.05 1 198 . 33 ALA HA H 4.182 0.05 1 199 . 33 ALA HB H 1.325 0.05 1 200 . 33 ALA C C 177.5118 0.2 1 201 . 33 ALA CA C 52.7798 0.2 1 202 . 33 ALA CB C 18.8098 0.2 1 203 . 33 ALA N N 123.62 0.1 1 204 . 34 LYS H H 8.027 0.05 1 205 . 34 LYS HA H 4.257 0.05 1 206 . 34 LYS HB2 H 1.774 0.05 1 207 . 34 LYS HB3 H 1.774 0.05 1 208 . 34 LYS C C 177.9398 0.2 1 209 . 34 LYS CA C 56.3758 0.2 1 210 . 34 LYS CB C 32.6578 0.2 1 211 . 34 LYS N N 120.477 0.1 1 212 . 36 GLU H H 8.278 0.05 1 213 . 36 GLU HA H 4.317 0.05 1 214 . 36 GLU HB2 H 1.972 0.05 1 215 . 36 GLU HB3 H 1.972 0.05 1 216 . 36 GLU C C 177.2088 0.2 1 217 . 36 GLU CA C 55.6108 0.2 1 218 . 36 GLU CB C 28.9858 0.2 1 219 . 36 GLU N N 122.503 0.1 1 220 . 37 SER H H 8.278 0.05 1 221 . 37 SER HA H 4.324 0.05 1 222 . 37 SER HB2 H 3.793 0.05 1 223 . 37 SER HB3 H 3.793 0.05 1 224 . 37 SER C C 175.7108 0.2 1 225 . 37 SER CA C 58.5948 0.2 1 226 . 37 SER CB C 63.5678 0.2 1 227 . 37 SER N N 117.805 0.1 1 228 . 38 ASN H H 8.347 0.05 1 229 . 38 ASN HA H 4.646 0.05 1 230 . 38 ASN HB2 H 2.686 0.05 1 231 . 38 ASN HB3 H 2.686 0.05 1 232 . 38 ASN C C 174.1948 0.2 1 233 . 38 ASN CA C 53.0098 0.2 1 234 . 38 ASN CB C 38.8548 0.2 1 235 . 38 ASN N N 121.285 0.1 1 236 . 39 PHE H H 8.149 0.05 1 237 . 39 PHE HA H 4.549 0.05 1 238 . 39 PHE HB2 H 3.038 0.05 1 239 . 39 PHE HB3 H 3.038 0.05 1 240 . 39 PHE C C 174.9438 0.2 1 241 . 39 PHE CA C 58.0588 0.2 1 242 . 39 PHE CB C 39.0848 0.2 1 243 . 39 PHE N N 121.464 0.1 1 244 . 40 ASN H H 8.345 0.05 1 245 . 40 ASN HA H 4.698 0.05 1 246 . 40 ASN HB2 H 2.754 0.05 1 247 . 40 ASN HB3 H 2.754 0.05 1 248 . 40 ASN C C 175.5148 0.2 1 249 . 40 ASN CA C 53.1628 0.2 1 250 . 40 ASN CB C 38.5488 0.2 1 251 . 40 ASN N N 121.253 0.1 1 252 . 41 THR H H 8.113 0.05 1 253 . 41 THR C C 175.4608 0.2 1 254 . 41 THR CA C 65.8628 0.2 1 255 . 41 THR N N 115.617 0.1 1 256 . 42 GLN H H 8.329 0.05 1 257 . 42 GLN HA H 4.302 0.05 1 258 . 42 GLN HB2 H 2.04 0.05 1 259 . 42 GLN HB3 H 2.04 0.05 1 260 . 42 GLN C C 174.7478 0.2 1 261 . 42 GLN CA C 56.1468 0.2 1 262 . 42 GLN CB C 29.0618 0.2 1 263 . 42 GLN N N 123.222 0.1 1 264 . 43 ALA H H 8.28 0.05 1 265 . 43 ALA HA H 4.317 0.05 1 266 . 43 ALA HB H 1.385 0.05 1 267 . 43 ALA C C 175.9068 0.2 1 268 . 43 ALA CA C 52.7798 0.2 1 269 . 43 ALA CB C 18.8868 0.2 1 270 . 43 ALA N N 125.984 0.1 1 271 . 44 THR H H 8.101 0.05 1 272 . 44 THR HA H 4.302 0.05 1 273 . 44 THR C C 177.9938 0.2 1 274 . 44 THR CA C 61.9608 0.2 1 275 . 44 THR CB C 69.6888 0.2 1 276 . 44 THR N N 113.869 0.1 1 277 . 45 ASN H H 8.382 0.05 1 278 . 45 ASN HA H 4.683 0.05 1 279 . 45 ASN HB2 H 2.757 0.05 1 280 . 45 ASN HB3 H 2.757 0.05 1 281 . 45 ASN C C 174.3728 0.2 1 282 . 45 ASN CA C 53.0858 0.2 1 283 . 45 ASN CB C 38.1668 0.2 1 284 . 45 ASN N N 121.973 0.1 1 285 . 46 ARG H H 8.337 0.05 1 286 . 46 ARG HA H 4.317 0.05 1 287 . 46 ARG HB2 H 1.7925 0.05 1 288 . 46 ARG HB3 H 1.7925 0.05 1 289 . 46 ARG C C 175.1398 0.2 1 290 . 46 ARG CA C 56.2228 0.2 1 291 . 46 ARG CB C 30.5158 0.2 1 292 . 46 ARG N N 122.548 0.1 1 293 . 47 ASN H H 8.494 0.05 1 294 . 47 ASN HA H 4.736 0.05 1 295 . 47 ASN HB2 H 2.799 0.05 1 296 . 47 ASN HB3 H 2.799 0.05 1 297 . 47 ASN C C 176.0498 0.2 1 298 . 47 ASN CA C 53.2388 0.2 1 299 . 47 ASN CB C 38.5488 0.2 1 300 . 47 ASN N N 120.729 0.1 1 301 . 48 THR H H 8.178 0.05 1 302 . 48 THR HA H 4.302 0.05 1 303 . 48 THR C C 175.7108 0.2 1 304 . 48 THR CA C 62.0378 0.2 1 305 . 48 THR CB C 69.5358 0.2 1 306 . 48 THR N N 115.183 0.1 1 307 . 49 ASP H H 8.494 0.05 1 308 . 49 ASP HA H 4.758 0.05 1 309 . 49 ASP HB2 H 2.881 0.05 1 310 . 49 ASP HB3 H 2.881 0.05 1 311 . 49 ASP C C 174.6938 0.2 1 312 . 49 ASP CA C 52.9328 0.2 1 313 . 49 ASP CB C 37.8608 0.2 1 314 . 49 ASP N N 122.014 0.1 1 315 . 50 GLY H H 8.41 0.05 1 316 . 50 GLY HA2 H 3.965 0.05 1 317 . 50 GLY HA3 H 3.965 0.05 1 318 . 50 GLY C C 175.6388 0.2 1 319 . 50 GLY CA C 45.3588 0.2 1 320 . 50 GLY N N 110.487 0.1 1 321 . 51 SER H H 8.17 0.05 1 322 . 51 SER HA H 4.481 0.05 1 323 . 51 SER HB2 H 3.876 0.05 1 324 . 51 SER HB3 H 3.876 0.05 1 325 . 51 SER C C 174.2838 0.2 1 326 . 51 SER CA C 58.3648 0.2 1 327 . 51 SER CB C 63.7968 0.2 1 328 . 51 SER N N 116.645 0.1 1 329 . 52 THR H H 8.211 0.05 1 330 . 52 THR HA H 4.272 0.05 1 331 . 52 THR HB H 4.085 0.05 2 332 . 52 THR C C 174.8898 0.2 1 333 . 52 THR CA C 61.8848 0.2 1 334 . 52 THR CB C 69.5358 0.2 1 335 . 52 THR N N 116.746 0.1 1 336 . 53 ASP H H 8.38 0.05 1 337 . 53 ASP HA H 4.683 0.05 1 338 . 53 ASP HB2 H 2.716 0.05 1 339 . 53 ASP HB3 H 2.716 0.05 1 340 . 53 ASP C C 174.3188 0.2 1 341 . 53 ASP CA C 52.7798 0.2 1 342 . 53 ASP CB C 38.0898 0.2 1 343 . 53 ASP N N 122.101 0.1 1 344 . 54 TYR H H 8.131 0.05 1 345 . 54 TYR HA H 4.459 0.05 1 346 . 54 TYR HB2 H 2.9895 0.05 1 347 . 54 TYR HB3 H 2.9895 0.05 1 348 . 54 TYR C C 174.7298 0.2 1 349 . 54 TYR CA C 58.5178 0.2 1 350 . 54 TYR CB C 38.3198 0.2 1 351 . 54 TYR N N 121.989 0.1 1 352 . 55 GLY H H 8.278 0.05 1 353 . 55 GLY HA2 H 3.868 0.05 1 354 . 55 GLY HA3 H 3.868 0.05 1 355 . 55 GLY C C 176.3708 0.2 1 356 . 55 GLY CA C 45.2818 0.2 1 357 . 55 GLY N N 110.882 0.1 1 358 . 56 ILE H H 7.838 0.05 1 359 . 56 ILE HA H 4.145 0.05 1 360 . 56 ILE HB H 1.856 0.05 1 361 . 56 ILE C C 174.1768 0.2 1 362 . 56 ILE CA C 61.4258 0.2 1 363 . 56 ILE CB C 38.3958 0.2 1 364 . 56 ILE N N 120.783 0.1 1 365 . 58 GLN HA H 4.287 0.05 1 366 . 58 GLN HB2 H 1.9795 0.05 1 367 . 58 GLN HB3 H 1.9795 0.05 1 368 . 59 ILE H H 8.109 0.05 1 369 . 59 ILE HA H 4.003 0.05 1 370 . 59 ILE HB H 1.804 0.05 1 371 . 59 ILE C C 176.1568 0.2 1 372 . 59 ILE CA C 61.6548 0.2 1 373 . 59 ILE CB C 38.4728 0.2 1 374 . 59 ILE N N 122.677 0.1 1 375 . 60 ASN H H 8.354 0.05 1 376 . 60 ASN HA H 4.683 0.05 1 377 . 60 ASN HB2 H 2.769 0.05 1 378 . 60 ASN HB3 H 2.769 0.05 1 379 . 60 ASN C C 176.0318 0.2 1 380 . 60 ASN CA C 53.1628 0.2 1 381 . 60 ASN CB C 38.5488 0.2 1 382 . 60 ASN N N 122.667 0.1 1 383 . 61 SER H H 8.228 0.05 1 384 . 61 SER HA H 4.272 0.05 1 385 . 61 SER HB2 H 3.827 0.05 1 386 . 61 SER HB3 H 3.827 0.05 1 387 . 61 SER C C 177.6908 0.2 1 388 . 61 SER CA C 58.5948 0.2 1 389 . 61 SER CB C 63.6438 0.2 1 390 . 61 SER N N 117.288 0.1 1 391 . 62 ARG H H 8.194 0.05 1 392 . 62 ARG HA H 4.01 0.05 1 393 . 62 ARG HB2 H 1.43 0.05 1 394 . 62 ARG HB3 H 1.43 0.05 1 395 . 62 ARG C C 174.8188 0.2 1 396 . 62 ARG CA C 56.2228 0.2 1 397 . 62 ARG CB C 29.6738 0.2 1 398 . 62 ARG N N 123.046 0.1 1 399 . 63 TRP H H 7.786 0.05 1 400 . 63 TRP HA H 4.541 0.05 1 401 . 63 TRP HB2 H 3.217 0.05 1 402 . 63 TRP HB3 H 3.217 0.05 1 403 . 63 TRP C C 176.3348 0.2 1 404 . 63 TRP CA C 57.5998 0.2 1 405 . 63 TRP CB C 29.2148 0.2 1 406 . 63 TRP N N 121.586 0.1 1 407 . 64 TRP H H 7.398 0.05 1 408 . 64 TRP HA H 4.466 0.05 1 409 . 64 TRP HB2 H 2.9595 0.05 1 410 . 64 TRP HB3 H 2.9595 0.05 1 411 . 64 TRP C C 176.1208 0.2 1 412 . 64 TRP CA C 57.3708 0.2 1 413 . 64 TRP CB C 28.9858 0.2 1 414 . 64 TRP N N 121.604 0.1 1 415 . 65 SMC H H 7.728 0.05 1 416 . 65 SMC C C 175.7638 0.2 1 417 . 65 SMC CA C 55.3048 0.2 1 418 . 65 SMC CB C 36.8658 0.2 1 419 . 65 SMC N N 121.93 0.1 1 420 . 66 ASN HA H 4.623 0.05 1 421 . 66 ASN HB2 H 2.761 0.05 1 422 . 66 ASN HB3 H 2.761 0.05 1 423 . 67 ASP H H 8.352 0.05 1 424 . 67 ASP HA H 4.631 0.05 1 425 . 67 ASP HB2 H 2.866 0.05 1 426 . 67 ASP HB3 H 2.866 0.05 1 427 . 67 ASP C C 175.0508 0.2 1 428 . 67 ASP CA C 53.2388 0.2 1 429 . 67 ASP CB C 37.8608 0.2 1 430 . 67 ASP N N 119.96 0.1 1 431 . 68 GLY H H 8.331 0.05 1 432 . 68 GLY HA2 H 3.838 0.05 1 433 . 68 GLY HA3 H 3.838 0.05 1 434 . 68 GLY C C 175.4788 0.2 1 435 . 68 GLY CA C 45.4348 0.2 1 436 . 68 GLY N N 109.57 0.1 1 437 . 69 ARG H H 7.964 0.05 1 438 . 69 ARG HA H 4.407 0.05 1 439 . 69 ARG HB2 H 1.804 0.05 1 440 . 69 ARG HB3 H 1.804 0.05 1 441 . 69 ARG C C 173.5518 0.2 1 442 . 69 ARG CA C 55.9168 0.2 1 443 . 69 ARG CB C 30.7458 0.2 1 444 . 69 ARG N N 120.86 0.1 1 445 . 70 THR H H 8.247 0.05 1 446 . 70 THR C C 174.7828 0.2 1 447 . 70 THR CA C 59.6658 0.2 1 448 . 70 THR CB C 69.4588 0.2 1 449 . 70 THR N N 118.291 0.1 1 450 . 71 PRO HA H 4.706 0.05 1 451 . 72 GLY H H 8.485 0.1 1 452 . 72 GLY HA2 H 3.943 0.05 1 453 . 72 GLY HA3 H 3.943 0.05 1 454 . 72 GLY C C 175.9778 0.2 1 455 . 72 GLY CA C 45.1288 0.2 1 456 . 72 GLY N N 110.548 0.1 1 457 . 73 SER H H 8.115 0.05 1 458 . 73 SER HA H 4.414 0.05 1 459 . 73 SER HB2 H 3.868 0.05 1 460 . 73 SER HB3 H 3.868 0.05 1 461 . 73 SER C C 174.2838 0.2 1 462 . 73 SER CA C 58.5948 0.2 1 463 . 73 SER CB C 63.8738 0.2 1 464 . 73 SER N N 116.612 0.1 1 465 . 74 ARG H H 8.42 0.05 1 466 . 74 ARG HA H 4.317 0.05 1 467 . 74 ARG HB2 H 1.763 0.05 1 468 . 74 ARG HB3 H 1.763 0.05 1 469 . 74 ARG C C 174.6938 0.2 1 470 . 74 ARG CA C 56.1468 0.2 1 471 . 74 ARG CB C 30.5158 0.2 1 472 . 74 ARG N N 123.693 0.1 1 473 . 75 ASN H H 8.424 0.05 1 474 . 75 ASN HA H 4.661 0.05 1 475 . 75 ASN HB2 H 2.765 0.05 1 476 . 75 ASN HB3 H 2.765 0.05 1 477 . 75 ASN C C 175.8708 0.2 1 478 . 75 ASN CA C 53.1628 0.2 1 479 . 75 ASN CB C 38.5488 0.2 1 480 . 75 ASN N N 120.726 0.1 1 481 . 77 SMC H H 8.295 0.05 1 482 . 77 SMC HA H 4.406 0.05 1 483 . 77 SMC HB2 H 2.8735 0.05 1 484 . 77 SMC HB3 H 2.8735 0.05 1 485 . 77 SMC C C 177.1198 0.2 1 486 . 77 SMC CA C 55.3048 0.2 1 487 . 77 SMC CB C 37.0958 0.2 1 488 . 77 SMC N N 120.911 0.1 1 489 . 78 ASN H H 8.507 0.05 1 490 . 78 ASN HA H 4.691 0.05 1 491 . 78 ASN HB2 H 2.739 0.05 1 492 . 78 ASN HB3 H 2.739 0.05 1 493 . 78 ASN C C 174.5868 0.2 1 494 . 78 ASN CA C 52.7798 0.2 1 495 . 78 ASN CB C 38.4728 0.2 1 496 . 78 ASN N N 122.289 0.1 1 497 . 79 ILE H H 8.02 0.05 1 498 . 79 ILE C C 174.4088 0.2 1 499 . 79 ILE CA C 58.5948 0.2 1 500 . 79 ILE CB C 38.3958 0.2 1 501 . 79 ILE N N 123.874 0.1 1 502 . 80 PRO HA H 4.414 0.05 1 503 . 80 PRO HB2 H 2.253 0.05 1 504 . 80 PRO HB3 H 2.253 0.05 1 505 . 81 SMC H H 8.499 0.05 1 506 . 81 SMC HA H 4.444 0.05 1 507 . 81 SMC HB2 H 2.911 0.05 1 508 . 81 SMC HB3 H 2.911 0.05 1 509 . 81 SMC C C 176.7628 0.2 1 510 . 81 SMC CA C 56.0698 0.2 1 511 . 81 SMC CB C 36.7898 0.2 1 512 . 81 SMC N N 121.597 0.1 1 513 . 82 SER H H 8.515 0.05 1 514 . 82 SER HA H 4.347 0.05 1 515 . 82 SER HB2 H 3.876 0.05 1 516 . 82 SER HB3 H 3.876 0.05 1 517 . 82 SER C C 175.6568 0.2 1 518 . 82 SER CA C 58.9768 0.2 1 519 . 82 SER CB C 63.4148 0.2 1 520 . 82 SER N N 119.152 0.1 1 521 . 83 ALA H H 8.212 0.05 1 522 . 83 ALA HA H 4.302 0.05 1 523 . 83 ALA HB H 1.378 0.05 1 524 . 83 ALA C C 174.5508 0.2 1 525 . 83 ALA CA C 52.7798 0.2 1 526 . 83 ALA CB C 18.9628 0.2 1 527 . 83 ALA N N 126.924 0.1 1 528 . 84 LEU H H 7.96 0.05 1 529 . 84 LEU HA H 4.287 0.05 1 530 . 84 LEU HB2 H 1.587 0.05 1 531 . 84 LEU HB3 H 1.587 0.05 1 532 . 84 LEU C C 177.7798 0.2 1 533 . 84 LEU CA C 55.3048 0.2 1 534 . 84 LEU CB C 41.9918 0.2 1 535 . 84 LEU N N 121.347 0.1 1 536 . 85 LEU H H 8.045 0.05 1 537 . 85 LEU HA H 4.362 0.05 1 538 . 85 LEU HB2 H 1.617 0.05 1 539 . 85 LEU HB3 H 1.617 0.05 1 540 . 85 LEU C C 177.5478 0.2 1 541 . 85 LEU CA C 55.2278 0.2 1 542 . 85 LEU CB C 42.0688 0.2 1 543 . 85 LEU N N 123.152 0.1 1 544 . 86 SER H H 8.231 0.05 1 545 . 86 SER HA H 4.407 0.05 1 546 . 86 SER HB2 H 3.876 0.05 1 547 . 86 SER HB3 H 3.876 0.05 1 548 . 86 SER C C 177.6728 0.2 1 549 . 86 SER CA C 58.5948 0.2 1 550 . 86 SER CB C 63.5678 0.2 1 551 . 86 SER N N 117.118 0.1 1 552 . 87 SER H H 8.247 0.05 1 553 . 87 SER HA H 4.451 0.05 1 554 . 87 SER HB2 H 3.876 0.05 1 555 . 87 SER HB3 H 3.876 0.05 1 556 . 87 SER C C 176.2638 0.2 1 557 . 87 SER CA C 58.5948 0.2 1 558 . 87 SER CB C 63.6438 0.2 1 559 . 87 SER N N 118.286 0.1 1 560 . 88 ASP H H 8.406 0.05 1 561 . 88 ASP C C 174.3548 0.2 1 562 . 88 ASP CA C 53.0098 0.2 1 563 . 88 ASP CB C 37.9368 0.2 1 564 . 88 ASP N N 121.982 0.1 1 565 . 90 THR H H 8.174 0.05 1 566 . 90 THR C C 176.5488 0.2 1 567 . 90 THR CA C 61.8848 0.2 1 568 . 90 THR CB C 69.5358 0.2 1 569 . 90 THR N N 119.199 0.1 1 570 . 91 ALA H H 8.262 0.05 1 571 . 91 ALA HA H 4.332 0.05 1 572 . 91 ALA HB H 1.393 0.05 1 573 . 91 ALA C C 174.2658 0.2 1 574 . 91 ALA CA C 52.5508 0.2 1 575 . 91 ALA CB C 18.9628 0.2 1 576 . 91 ALA N N 127.486 0.1 1 577 . 92 SER H H 8.285 0.05 1 578 . 92 SER C C 177.7618 0.2 1 579 . 92 SER CA C 58.3648 0.2 1 580 . 92 SER CB C 63.7208 0.2 1 581 . 92 SER N N 116.474 0.1 1 582 . 94 ASN H H 8.477 0.05 1 583 . 94 ASN HA H 4.661 0.05 1 584 . 94 ASN HB2 H 2.709 0.05 1 585 . 94 ASN HB3 H 2.709 0.05 1 586 . 94 ASN C C 175.9598 0.2 1 587 . 94 ASN CA C 45.7788 0.2 1 588 . 94 ASN N N 122.757 0.1 1 589 . 95 SMC H H 8.22 0.05 1 590 . 95 SMC HA H 4.459 0.05 1 591 . 95 SMC HB2 H 2.907 0.05 1 592 . 95 SMC HB3 H 2.907 0.05 1 593 . 95 SMC C C 174.0698 0.2 1 594 . 95 SMC N N 121.732 0.1 1 595 . 96 ALA H H 8.382 0.05 1 596 . 96 ALA HA H 4.302 0.05 1 597 . 96 ALA HB H 1.385 0.05 1 598 . 96 ALA C C 174.8548 0.2 1 599 . 96 ALA CA C 52.5508 0.2 1 600 . 96 ALA CB C 18.8098 0.2 1 601 . 96 ALA N N 127.044 0.1 1 602 . 97 LYS H H 8.122 0.05 1 603 . 97 LYS HA H 4.242 0.05 1 604 . 97 LYS HB2 H 1.774 0.05 1 605 . 97 LYS HB3 H 1.774 0.05 1 606 . 97 LYS C C 176.6378 0.2 1 607 . 97 LYS CA C 56.3758 0.2 1 608 . 97 LYS CB C 32.6578 0.2 1 609 . 97 LYS N N 123.138 0.1 1 610 . 98 LYS H H 8.262 0.05 1 611 . 98 LYS HA H 4.287 0.05 1 612 . 98 LYS HB2 H 1.744 0.05 1 613 . 98 LYS HB3 H 1.744 0.05 1 614 . 98 LYS C C 176.3348 0.2 1 615 . 98 LYS CA C 56.2228 0.2 1 616 . 98 LYS CB C 32.8878 0.2 1 617 . 98 LYS N N 124.306 0.1 1 618 . 99 ILE H H 8.269 0.05 1 619 . 99 ILE HA H 4.152 0.05 1 620 . 99 ILE HB H 1.826 0.05 1 621 . 99 ILE C C 176.2278 0.2 1 622 . 99 ILE CA C 60.8898 0.2 1 623 . 99 ILE CB C 38.3198 0.2 1 624 . 99 ILE N N 124.603 0.1 1 625 . 100 VAL H H 8.34 0.05 1 626 . 100 VAL HA H 4.152 0.05 1 627 . 100 VAL HB H 2.043 0.05 1 628 . 100 VAL C C 176.2458 0.2 1 629 . 100 VAL CA C 62.2668 0.2 1 630 . 100 VAL CB C 32.6578 0.2 1 631 . 100 VAL N N 126.405 0.1 1 632 . 101 SER H H 8.447 0.05 1 633 . 101 SER HB2 H 3.823 0.05 1 634 . 101 SER HB3 H 3.823 0.05 1 635 . 101 SER C C 175.9598 0.2 1 636 . 101 SER CA C 58.0588 0.2 1 637 . 101 SER CB C 63.7968 0.2 1 638 . 101 SER N N 120.906 0.1 1 639 . 102 ASP H H 8.583 0.05 1 640 . 102 ASP HA H 4.706 0.05 1 641 . 102 ASP HB2 H 2.911 0.05 1 642 . 102 ASP HB3 H 2.911 0.05 1 643 . 102 ASP C C 174.3368 0.2 1 644 . 102 ASP CA C 52.7798 0.2 1 645 . 102 ASP CB C 38.0138 0.2 1 646 . 102 ASP N N 122.63 0.1 1 647 . 103 GLY H H 8.393 0.05 1 648 . 103 GLY HA2 H 3.928 0.05 1 649 . 103 GLY HA3 H 3.928 0.05 1 650 . 103 GLY C C 175.6388 0.2 1 651 . 103 GLY CA C 45.2818 0.2 1 652 . 103 GLY N N 110.631 0.1 1 653 . 104 ASN H H 8.359 0.05 1 654 . 104 ASN HA H 4.706 0.05 1 655 . 104 ASN HB2 H 2.814 0.05 1 656 . 104 ASN HB3 H 2.814 0.05 1 657 . 104 ASN C C 174.0518 0.2 1 658 . 104 ASN CA C 53.2388 0.2 1 659 . 104 ASN CB C 38.6258 0.2 1 660 . 104 ASN N N 119.712 0.1 1 661 . 105 GLY H H 8.474 0.05 1 662 . 105 GLY HA2 H 3.928 0.05 1 663 . 105 GLY HA3 H 3.928 0.05 1 664 . 105 GLY C C 175.9958 0.2 1 665 . 105 GLY CA C 45.5118 0.2 1 666 . 105 GLY N N 110.362 0.1 1 667 . 106 MET H H 8.215 0.05 1 668 . 106 MET HA H 4.407 0.05 1 669 . 106 MET HB2 H 2.021 0.05 1 670 . 106 MET HB3 H 2.021 0.05 1 671 . 106 MET C C 174.5868 0.2 1 672 . 106 MET CA C 55.9168 0.2 1 673 . 106 MET CB C 32.1988 0.2 1 674 . 106 MET N N 121 0.1 1 675 . 107 ASN H H 8.407 0.05 1 676 . 107 ASN HA H 4.586 0.05 1 677 . 107 ASN HB2 H 2.709 0.05 1 678 . 107 ASN HB3 H 2.709 0.05 1 679 . 107 ASN C C 176.3888 0.2 1 680 . 107 ASN CA C 53.7748 0.2 1 681 . 107 ASN CB C 38.3958 0.2 1 682 . 107 ASN N N 120.44 0.1 1 683 . 108 ALA H H 8.218 0.05 1 684 . 108 ALA HA H 4.197 0.05 1 685 . 108 ALA HB H 1.31 0.05 1 686 . 108 ALA C C 175.5498 0.2 1 687 . 108 ALA CA C 53.3918 0.2 1 688 . 108 ALA CB C 18.6568 0.2 1 689 . 108 ALA N N 124.94 0.1 1 690 . 109 TRP H H 8.049 0.05 1 691 . 109 TRP HA H 4.504 0.05 1 692 . 109 TRP HB2 H 3.292 0.05 1 693 . 109 TRP HB3 H 3.292 0.05 1 694 . 109 TRP C C 178.0118 0.2 1 695 . 109 TRP CA C 58.4418 0.2 1 696 . 109 TRP CB C 28.9858 0.2 1 697 . 109 TRP N N 120.908 0.1 1 698 . 110 VAL H H 7.793 0.05 1 699 . 110 VAL HA H 3.711 0.05 1 700 . 110 VAL HB H 1.879 0.05 1 701 . 110 VAL C C 176.7988 0.2 1 702 . 110 VAL CA C 63.5678 0.2 1 703 . 110 VAL CB C 32.3518 0.2 1 704 . 110 VAL N N 122.188 0.1 1 705 . 111 ALA H H 8.015 0.05 1 706 . 111 ALA HA H 4.063 0.05 1 707 . 111 ALA HB H 1.348 0.05 1 708 . 111 ALA C C 176.4058 0.2 1 709 . 111 ALA CA C 53.5448 0.2 1 710 . 111 ALA CB C 18.5038 0.2 1 711 . 111 ALA N N 125.597 0.1 1 712 . 112 TRP H H 7.899 0.05 1 713 . 112 TRP HA H 4.414 0.05 1 714 . 112 TRP HB2 H 3.292 0.05 1 715 . 112 TRP HB3 H 3.292 0.05 1 716 . 112 TRP C C 178.6358 0.2 1 717 . 112 TRP CA C 58.5178 0.2 1 718 . 112 TRP CB C 28.9088 0.2 1 719 . 112 TRP N N 120.354 0.1 1 720 . 113 ARG H H 7.984 0.05 1 721 . 113 ARG HA H 3.905 0.05 1 722 . 113 ARG HB2 H 1.5575 0.05 1 723 . 113 ARG HB3 H 1.5575 0.05 1 724 . 113 ARG C C 177.1558 0.2 1 725 . 113 ARG CA C 57.2178 0.2 1 726 . 113 ARG CB C 29.8268 0.2 1 727 . 113 ARG N N 121.937 0.1 1 728 . 114 ASN H H 8.063 0.05 1 729 . 114 ASN HA H 4.571 0.05 1 730 . 114 ASN HB2 H 2.7575 0.05 1 731 . 114 ASN HB3 H 2.7575 0.05 1 732 . 114 ASN C C 176.5668 0.2 1 733 . 114 ASN CA C 53.4688 0.2 1 734 . 114 ASN CB C 38.3958 0.2 1 735 . 114 ASN N N 118.93 0.1 1 736 . 115 ARG H H 7.899 0.05 1 737 . 115 ARG HA H 4.227 0.05 1 738 . 115 ARG HB2 H 1.767 0.05 1 739 . 115 ARG HB3 H 1.767 0.05 1 740 . 115 ARG C C 175.4608 0.2 1 741 . 115 ARG CA C 56.7588 0.2 1 742 . 115 ARG CB C 30.2098 0.2 1 743 . 115 ARG N N 121.682 0.1 1 744 . 116 SMC H H 8.203 0.05 1 745 . 116 SMC HA H 4.429 0.05 1 746 . 116 SMC HB2 H 2.802 0.05 1 747 . 116 SMC HB3 H 2.802 0.05 1 748 . 116 SMC C C 176.3528 0.2 1 749 . 116 SMC CA C 55.6868 0.2 1 750 . 116 SMC CB C 36.7898 0.2 1 751 . 116 SMC N N 121.249 0.1 1 752 . 117 LYS H H 8.374 0.05 1 753 . 117 LYS HA H 4.257 0.05 1 754 . 117 LYS HB2 H 1.7815 0.05 1 755 . 117 LYS HB3 H 1.7815 0.05 1 756 . 117 LYS C C 175.1398 0.2 1 757 . 117 LYS CA C 56.2228 0.2 1 758 . 117 LYS CB C 32.5048 0.2 1 759 . 117 LYS N N 124.394 0.1 1 760 . 118 GLY H H 8.36 0.05 1 761 . 118 GLY HA2 H 3.98 0.05 1 762 . 118 GLY HA3 H 3.98 0.05 1 763 . 118 GLY C C 176.8698 0.2 1 764 . 118 GLY CA C 45.1288 0.2 1 765 . 118 GLY N N 110.957 0.1 1 766 . 119 THR H H 8.069 0.05 1 767 . 119 THR HA H 4.347 0.05 1 768 . 119 THR HB H 4.227 0.05 1 769 . 119 THR C C 174.1768 0.2 1 770 . 119 THR CA C 61.9608 0.2 1 771 . 119 THR CB C 69.6888 0.2 1 772 . 119 THR N N 114.419 0.1 1 773 . 120 ASP H H 8.549 0.05 1 774 . 120 ASP HA H 4.728 0.05 1 775 . 120 ASP HB2 H 2.933 0.05 1 776 . 120 ASP HB3 H 2.933 0.05 1 777 . 120 ASP C C 174.3548 0.2 1 778 . 120 ASP CA C 52.7038 0.2 1 779 . 120 ASP CB C 37.7838 0.2 1 780 . 120 ASP N N 122.659 0.1 1 781 . 121 VAL H H 8.098 0.05 1 782 . 121 VAL HA H 3.95 0.05 1 783 . 121 VAL HB H 2.013 0.05 1 784 . 121 VAL C C 175.1218 0.2 1 785 . 121 VAL CA C 62.8788 0.2 1 786 . 121 VAL CB C 32.1988 0.2 1 787 . 121 VAL N N 122.073 0.1 1 788 . 122 GLN H H 8.365 0.05 1 789 . 122 GLN HA H 4.16 0.05 1 790 . 122 GLN HB2 H 1.879 0.05 1 791 . 122 GLN HB3 H 1.879 0.05 1 792 . 122 GLN C C 176.2638 0.2 1 793 . 122 GLN CA C 56.2998 0.2 1 794 . 122 GLN CB C 28.6798 0.2 1 795 . 122 GLN N N 124.294 0.1 1 796 . 123 ALA H H 8.144 0.05 1 797 . 123 ALA HA H 4.205 0.05 1 798 . 123 ALA HB H 1.318 0.05 1 799 . 123 ALA C C 175.9068 0.2 1 800 . 123 ALA CA C 52.8568 0.2 1 801 . 123 ALA CB C 18.8868 0.2 1 802 . 123 ALA N N 125.331 0.1 1 803 . 124 TRP H H 7.984 0.05 1 804 . 124 TRP HA H 4.608 0.05 1 805 . 124 TRP HB2 H 3.217 0.05 1 806 . 124 TRP HB3 H 3.217 0.05 1 807 . 124 TRP C C 177.5118 0.2 1 808 . 124 TRP CA C 57.4468 0.2 1 809 . 124 TRP CB C 29.1388 0.2 1 810 . 124 TRP N N 120.864 0.1 1 811 . 125 ILE H H 7.899 0.05 1 812 . 125 ILE HA H 3.988 0.05 1 813 . 125 ILE HB H 1.722 0.05 1 814 . 125 ILE C C 176.3528 0.2 1 815 . 125 ILE CA C 61.4258 0.2 1 816 . 125 ILE CB C 38.6258 0.2 1 817 . 125 ILE N N 123.791 0.1 1 818 . 126 ARG H H 8.173 0.05 1 819 . 126 ARG HA H 4.107 0.05 1 820 . 126 ARG HB2 H 1.767 0.05 1 821 . 126 ARG HB3 H 1.767 0.05 1 822 . 126 ARG C C 175.9428 0.2 1 823 . 126 ARG CA C 56.6058 0.2 1 824 . 126 ARG CB C 30.1328 0.2 1 825 . 126 ARG N N 125.17 0.1 1 826 . 127 GLY H H 8.302 0.05 1 827 . 127 GLY HA2 H 3.928 0.05 1 828 . 127 GLY HA3 H 3.928 0.05 1 829 . 127 GLY C C 176.7268 0.2 1 830 . 127 GLY CA C 45.0528 0.2 1 831 . 127 GLY N N 110.634 0.1 1 832 . 128 SMC H H 8.129 0.05 1 833 . 128 SMC HA H 4.474 0.05 1 834 . 128 SMC HB2 H 2.814 0.05 1 835 . 128 SMC HB3 H 2.814 0.05 1 836 . 128 SMC C C 173.8558 0.2 1 837 . 128 SMC CA C 55.3808 0.2 1 838 . 128 SMC CB C 37.2488 0.2 1 839 . 128 SMC N N 120.957 0.1 1 840 . 129 ARG H H 8.507 0.05 1 841 . 129 ARG HA H 4.279 0.05 1 842 . 129 ARG C C 174.7118 0.2 1 843 . 129 ARG CA C 55.7638 0.2 1 844 . 129 ARG CB C 30.4388 0.2 1 845 . 129 ARG N N 124.985 0.1 1 846 . 130 LEU H H 8.337 0.05 1 847 . 130 LEU C C 175.7818 0.2 1 848 . 130 LEU CA C 54.2338 0.2 1 849 . 130 LEU CB C 41.7628 0.2 1 850 . 130 LEU N N 125.97 0.1 1 stop_ save_