data_4323 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N NMR backbone assignments of 37 kDa surface antigen OspC from Borrelia burgdorferi ; _BMRB_accession_number 4323 _BMRB_flat_file_name bmr4323.str _Entry_type original _Submission_date 1999-03-22 _Accession_date 1999-03-23 _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 Xiaolin . . 2 Link Karl . . 3 Koide Akiko . . 4 Dunn J. J. . 5 Luft B. J. . 6 Koide Shohei . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 495 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-15 original author . stop_ _Original_release_date 2000-12-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Huang, X., Link, K., Koide, A., Dunn, J.J., Luft, B.J., and Koide, S.,"1H, 13C, and 15N NMR Backbone Assignments of 37 kDa Surface Antigen OspC from Borrelia burgdorferi," J. Biomol. NMR 14, 283-284 (1999). ; _Citation_title ; 1H, 13C, 15N NMR backbone assignments of 37 kDa surface antigen OspC from Borrelia burgdorferi ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99410892 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Xiaolin . . 2 Link Karl . . 3 Koide Akiko . . 4 Dunn J. J. . 5 Luft B. J. . 6 Koide Shohei . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 14 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 283 _Page_last 284 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_OspC _Saveframe_category molecular_system _Mol_system_name 'outer surface protein C' _Abbreviation_common OspC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'OspC monomer 1' $OspC 'OspC monomer 2' $OspC stop_ _System_molecular_weight 37132 _System_physical_state Native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'OspC monomer 1' 1 'OspC monomer 2' stop_ _Database_query_date . _Details ; OspC exists a dimer in solution. The protein used for this study correspounds to residues 38-210 plus the first Met residue which comes from the expression vector. ; save_ ######################## # Monomeric polymers # ######################## save_OspC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'outer surface protein C' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 174 _Mol_residue_sequence ; MKGPNLTEISKKITDSNAVL LAVKEVEALLSSIDEIAAKA IGKKIHQNNGLDTENNHNGS LLAGAYAISTLIKQKLDGLK NEGLKEKIDAAKKCSETFTN KLKEKHTDLGKEGVTDADAK EAILKTNGTKTKGAEELGKL FESVEVLSKAAKEMLANSVK ELTSPVVAESPKKP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 37 MET 2 38 LYS 3 39 GLY 4 40 PRO 5 41 ASN 6 42 LEU 7 43 THR 8 44 GLU 9 45 ILE 10 46 SER 11 47 LYS 12 48 LYS 13 49 ILE 14 50 THR 15 51 ASP 16 52 SER 17 53 ASN 18 54 ALA 19 55 VAL 20 56 LEU 21 57 LEU 22 58 ALA 23 59 VAL 24 60 LYS 25 61 GLU 26 62 VAL 27 63 GLU 28 64 ALA 29 65 LEU 30 66 LEU 31 67 SER 32 68 SER 33 69 ILE 34 70 ASP 35 71 GLU 36 72 ILE 37 73 ALA 38 74 ALA 39 75 LYS 40 76 ALA 41 77 ILE 42 78 GLY 43 79 LYS 44 80 LYS 45 81 ILE 46 82 HIS 47 83 GLN 48 84 ASN 49 85 ASN 50 86 GLY 51 87 LEU 52 88 ASP 53 89 THR 54 90 GLU 55 91 ASN 56 92 ASN 57 93 HIS 58 94 ASN 59 95 GLY 60 96 SER 61 97 LEU 62 98 LEU 63 99 ALA 64 100 GLY 65 101 ALA 66 102 TYR 67 103 ALA 68 104 ILE 69 105 SER 70 106 THR 71 107 LEU 72 108 ILE 73 109 LYS 74 110 GLN 75 111 LYS 76 112 LEU 77 113 ASP 78 114 GLY 79 115 LEU 80 116 LYS 81 117 ASN 82 118 GLU 83 119 GLY 84 120 LEU 85 121 LYS 86 122 GLU 87 123 LYS 88 124 ILE 89 125 ASP 90 126 ALA 91 127 ALA 92 128 LYS 93 129 LYS 94 130 CYS 95 131 SER 96 132 GLU 97 133 THR 98 134 PHE 99 135 THR 100 136 ASN 101 137 LYS 102 138 LEU 103 139 LYS 104 140 GLU 105 141 LYS 106 142 HIS 107 143 THR 108 144 ASP 109 145 LEU 110 146 GLY 111 147 LYS 112 148 GLU 113 149 GLY 114 150 VAL 115 151 THR 116 152 ASP 117 153 ALA 118 154 ASP 119 155 ALA 120 156 LYS 121 157 GLU 122 158 ALA 123 159 ILE 124 160 LEU 125 161 LYS 126 162 THR 127 163 ASN 128 164 GLY 129 165 THR 130 166 LYS 131 167 THR 132 168 LYS 133 169 GLY 134 170 ALA 135 171 GLU 136 172 GLU 137 173 LEU 138 174 GLY 139 175 LYS 140 176 LEU 141 177 PHE 142 178 GLU 143 179 SER 144 180 VAL 145 181 GLU 146 182 VAL 147 183 LEU 148 184 SER 149 185 LYS 150 186 ALA 151 187 ALA 152 188 LYS 153 189 GLU 154 190 MET 155 191 LEU 156 192 ALA 157 193 ASN 158 194 SER 159 195 VAL 160 196 LYS 161 197 GLU 162 198 LEU 163 199 THR 164 200 SER 165 201 PRO 166 202 VAL 167 203 VAL 168 204 ALA 169 205 GLU 170 206 SER 171 207 PRO 172 208 LYS 173 209 LYS 174 210 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1GGQ "Outer Surface Protein C (ospc) Of Borrelia Burgdorferi Strain B31" 100.00 174 100.00 100.00 4.74e-115 DBJ BAA08457 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 EMBL CAA49306 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 EMBL CAA52001 "outer surface protein C, partial [Borrelia burgdorferi]" 96.55 178 98.21 98.81 1.01e-106 EMBL CAA59254 "outer surface protein C, partial [Borrelia burgdorferi]" 95.98 177 98.80 99.40 2.84e-108 EMBL CAG44432 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 EMBL CAG44433 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 GB AAA16058 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 GB AAB06569 "outer surface protein, partial [Borrelia burgdorferi]" 100.00 191 99.43 100.00 4.63e-114 GB AAB36995 "outer surface protein C, partial [Borrelia burgdorferi]" 100.00 192 99.43 100.00 6.22e-114 GB AAB81889 "outer surface protein C, partial [Borrelia burgdorferi]" 86.21 175 99.33 100.00 6.64e-96 GB AAB81894 "outer surface protein C, partial [Borrelia burgdorferi]" 96.55 182 99.40 100.00 2.79e-109 PRF 2003376B "outer surface protein [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 REF NP_047005 "outer surface protein C [Borrelia burgdorferi B31]" 100.00 210 99.43 100.00 7.22e-114 REF WP_010890595 "outer surface protein C [Borrelia burgdorferi]" 100.00 210 99.43 100.00 7.22e-114 SP Q07337 "RecName: Full=Outer surface protein C; Short=PC; Flags: Precursor" 100.00 210 99.43 100.00 7.22e-114 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 $OspC spirochete 139 Eubacteria . Borrelia burgdorferi B31 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 _Vendor_name _Details $OspC 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET24-OspC Novagen 'natural source' 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 $OspC 1.0 mM '[U-99% 13C; U-98% 15N; U-95% 2H]' 'sodium phosphate' 20 mM . 'sodium chloride' 100 mM . EDTA 0.10 mM . DTT 1.0 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_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 120 . mM pH 6.0 0.05 n/a pressure 1.0 . atm temperature 308 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 _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.25144954 DSS H 1 'methyl protons' ppm 0 external direct . . . . DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.10132900 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_one _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 'OspC monomer 1' _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 . 3 GLY N N 111.520 0.1 1 2 . 3 GLY H H 8.304 0.01 1 3 . 3 GLY CA C 44.069 0.5 1 4 . 4 PRO CA C 62.291 0.5 1 5 . 4 PRO CB C 31.507 0.5 1 6 . 4 PRO C C 176.190 0.5 1 7 . 5 ASN N N 120.902 0.1 1 8 . 5 ASN H H 8.754 0.01 1 9 . 5 ASN CA C 51.943 0.5 1 10 . 5 ASN CB C 37.122 0.5 1 11 . 5 ASN C C 175.808 0.5 1 12 . 6 LEU N N 124.514 0.1 1 13 . 6 LEU H H 8.468 0.01 1 14 . 6 LEU CA C 57.602 0.5 1 15 . 6 LEU CB C 40.136 0.5 1 16 . 6 LEU C C 179.163 0.5 1 17 . 7 THR N N 117.464 0.1 1 18 . 7 THR H H 8.177 0.01 1 19 . 7 THR CA C 66.226 0.5 1 20 . 7 THR CB C 67.825 0.5 1 21 . 7 THR C C 176.795 0.5 1 22 . 8 GLU N N 123.908 0.1 1 23 . 8 GLU H H 7.635 0.01 1 24 . 8 GLU CA C 58.599 0.5 1 25 . 8 GLU CB C 28.854 0.5 1 26 . 8 GLU C C 179.534 0.5 1 27 . 9 ILE N N 121.363 0.1 1 28 . 9 ILE H H 8.393 0.01 1 29 . 9 ILE CA C 64.805 0.5 1 30 . 9 ILE CB C 37.468 0.5 1 31 . 9 ILE C C 177.761 0.5 1 32 . 10 SER N N 115.668 0.1 1 33 . 10 SER H H 8.221 0.01 1 34 . 10 SER CA C 62.161 0.5 1 35 . 10 SER C C 176.067 0.5 1 36 . 11 LYS N N 122.905 0.1 1 37 . 11 LYS H H 7.294 0.01 1 38 . 11 LYS CA C 58.768 0.5 1 39 . 11 LYS CB C 31.326 0.5 1 40 . 11 LYS C C 177.832 0.5 1 41 . 12 LYS N N 120.461 0.1 1 42 . 12 LYS H H 7.920 0.01 1 43 . 12 LYS CA C 59.593 0.5 1 44 . 12 LYS CB C 31.326 0.5 1 45 . 12 LYS C C 181.065 0.5 1 46 . 13 ILE N N 122.430 0.1 1 47 . 13 ILE H H 8.697 0.01 1 48 . 13 ILE CA C 65.556 0.5 1 49 . 13 ILE CB C 37.286 0.5 1 50 . 13 ILE C C 177.501 0.5 1 51 . 14 THR N N 116.930 0.1 1 52 . 14 THR H H 8.362 0.01 1 53 . 14 THR CA C 66.844 0.5 1 54 . 14 THR CB C 67.809 0.5 1 55 . 14 THR C C 177.991 0.5 1 56 . 15 ASP N N 124.926 0.1 1 57 . 15 ASP H H 9.029 0.01 1 58 . 15 ASP CA C 57.241 0.5 1 59 . 15 ASP CB C 39.596 0.5 1 60 . 15 ASP C C 179.340 0.5 1 61 . 16 SER N N 117.426 0.1 1 62 . 16 SER H H 8.375 0.01 1 63 . 16 SER CA C 62.070 0.5 1 64 . 16 SER C C 177.048 0.5 1 65 . 17 ASN N N 123.415 0.1 1 66 . 17 ASN H H 8.840 0.01 1 67 . 17 ASN CA C 56.778 0.5 1 68 . 17 ASN CB C 38.563 0.5 1 69 . 17 ASN C C 175.921 0.5 1 70 . 18 ALA N N 121.414 0.1 1 71 . 18 ALA H H 7.834 0.01 1 72 . 18 ALA CA C 55.253 0.5 1 73 . 18 ALA CB C 17.096 0.5 1 74 . 18 ALA C C 181.260 0.5 1 75 . 19 VAL N N 119.415 0.1 1 76 . 19 VAL H H 7.535 0.01 1 77 . 19 VAL CA C 65.365 0.5 1 78 . 19 VAL CB C 30.839 0.5 1 79 . 19 VAL C C 177.033 0.5 1 80 . 20 LEU N N 121.918 0.1 1 81 . 20 LEU H H 7.960 0.01 1 82 . 20 LEU CA C 57.833 0.5 1 83 . 20 LEU CB C 40.630 0.5 1 84 . 20 LEU C C 178.580 0.5 1 85 . 21 LEU N N 119.467 0.1 1 86 . 21 LEU H H 8.629 0.01 1 87 . 21 LEU CA C 57.786 0.5 1 88 . 21 LEU CB C 40.995 0.5 1 89 . 21 LEU C C 178.484 0.5 1 90 . 22 ALA N N 121.822 0.1 1 91 . 22 ALA H H 7.342 0.01 1 92 . 22 ALA CA C 54.312 0.5 1 93 . 22 ALA CB C 18.069 0.5 1 94 . 22 ALA C C 181.401 0.5 1 95 . 23 VAL N N 120.405 0.1 1 96 . 23 VAL H H 8.429 0.01 1 97 . 23 VAL CA C 66.399 0.5 1 98 . 23 VAL CB C 30.596 0.5 1 99 . 23 VAL C C 177.608 0.5 1 100 . 24 LYS N N 122.850 0.1 1 101 . 24 LYS H H 8.906 0.01 1 102 . 24 LYS CA C 56.598 0.5 1 103 . 24 LYS CB C 29.562 0.5 1 104 . 24 LYS C C 177.874 0.5 1 105 . 25 GLU N N 118.915 0.1 1 106 . 25 GLU H H 7.779 0.01 1 107 . 25 GLU CA C 59.363 0.5 1 108 . 25 GLU CB C 29.197 0.5 1 109 . 25 GLU C C 177.509 0.5 1 110 . 26 VAL N N 118.415 0.1 1 111 . 26 VAL H H 7.141 0.01 1 112 . 26 VAL CA C 66.981 0.5 1 113 . 26 VAL CB C 30.353 0.5 1 114 . 26 VAL C C 177.489 0.5 1 115 . 27 GLU N N 120.912 0.1 1 116 . 27 GLU H H 8.643 0.01 1 117 . 27 GLU CA C 59.757 0.5 1 118 . 27 GLU CB C 29.806 0.5 1 119 . 27 GLU C C 179.056 0.5 1 120 . 28 ALA N N 122.999 0.1 1 121 . 28 ALA H H 8.680 0.01 1 122 . 28 ALA CA C 53.934 0.5 1 123 . 28 ALA CB C 19.438 0.5 1 124 . 28 ALA C C 180.746 0.5 1 125 . 29 LEU N N 121.366 0.1 1 126 . 29 LEU H H 8.269 0.01 1 127 . 29 LEU CA C 57.786 0.5 1 128 . 29 LEU CB C 41.056 0.5 1 129 . 29 LEU C C 180.908 0.5 1 130 . 30 LEU N N 122.464 0.1 1 131 . 30 LEU H H 8.255 0.01 1 132 . 30 LEU CA C 58.072 0.5 1 133 . 30 LEU CB C 39.536 0.5 1 134 . 30 LEU C C 179.319 0.5 1 135 . 31 SER N N 117.947 0.1 1 136 . 31 SER H H 8.486 0.01 1 137 . 31 SER CA C 61.697 0.5 1 138 . 31 SER C C 176.808 0.5 1 139 . 32 SER N N 121.909 0.1 1 140 . 32 SER H H 8.153 0.01 1 141 . 32 SER CA C 62.633 0.5 1 142 . 32 SER C C 175.568 0.5 1 143 . 33 ILE N N 123.423 0.1 1 144 . 33 ILE H H 7.305 0.01 1 145 . 33 ILE CA C 65.489 0.5 1 146 . 33 ILE CB C 36.617 0.5 1 147 . 33 ILE C C 177.195 0.5 1 148 . 34 ASP N N 119.662 0.1 1 149 . 34 ASP H H 7.948 0.01 1 150 . 34 ASP CA C 57.017 0.5 1 151 . 34 ASP CB C 40.569 0.5 1 152 . 34 ASP C C 178.557 0.5 1 153 . 35 GLU N N 120.894 0.1 1 154 . 35 GLU H H 8.409 0.01 1 155 . 35 GLU CA C 58.691 0.5 1 156 . 35 GLU CB C 28.468 0.5 1 157 . 35 GLU C C 179.473 0.5 1 158 . 36 ILE N N 114.903 0.1 1 159 . 36 ILE H H 8.174 0.01 1 160 . 36 ILE CA C 65.220 0.5 1 161 . 36 ILE CB C 35.583 0.5 1 162 . 36 ILE C C 178.067 0.5 1 163 . 37 ALA N N 123.981 0.1 1 164 . 37 ALA H H 8.416 0.01 1 165 . 37 ALA CA C 53.587 0.5 1 166 . 37 ALA CB C 20.015 0.5 1 167 . 37 ALA C C 178.000 0.5 1 168 . 38 ALA N N 116.889 0.1 1 169 . 38 ALA H H 8.136 0.01 1 170 . 38 ALA CA C 53.553 0.5 1 171 . 38 ALA CB C 18.434 0.5 1 172 . 38 ALA C C 180.025 0.5 1 173 . 39 LYS N N 112.265 0.1 1 174 . 39 LYS H H 8.148 0.01 1 175 . 39 LYS CA C 55.037 0.5 1 176 . 39 LYS CB C 33.760 0.5 1 177 . 39 LYS C C 176.958 0.5 1 178 . 40 ALA N N 117.910 0.1 1 179 . 40 ALA H H 8.003 0.01 1 180 . 40 ALA CA C 51.746 0.5 1 181 . 40 ALA CB C 19.650 0.5 1 182 . 40 ALA C C 176.077 0.5 1 183 . 41 ILE N N 119.452 0.1 1 184 . 41 ILE H H 6.617 0.01 1 185 . 41 ILE CA C 63.241 0.5 1 186 . 41 ILE CB C 36.799 0.5 1 187 . 41 ILE C C 178.356 0.5 1 188 . 42 GLY N N 119.913 0.1 1 189 . 42 GLY H H 9.744 0.01 1 190 . 42 GLY CA C 47.474 0.5 1 191 . 42 GLY C C 176.397 0.5 1 192 . 43 LYS N N 119.419 0.1 1 193 . 43 LYS H H 7.853 0.01 1 194 . 43 LYS CA C 53.062 0.5 1 195 . 43 LYS CB C 36.677 0.5 1 196 . 43 LYS C C 175.037 0.5 1 197 . 44 LYS N N 115.438 0.1 1 198 . 44 LYS H H 8.930 0.01 1 199 . 44 LYS CA C 53.103 0.5 1 200 . 44 LYS CB C 35.644 0.5 1 201 . 44 LYS C C 174.505 0.5 1 202 . 45 ILE N N 123.021 0.1 1 203 . 45 ILE H H 8.645 0.01 1 204 . 45 ILE CA C 62.557 0.5 1 205 . 45 ILE CB C 37.772 0.5 1 206 . 45 ILE C C 173.945 0.5 1 207 . 46 HIS N N 127.054 0.1 1 208 . 46 HIS H H 7.789 0.01 1 209 . 46 HIS CA C 55.574 0.5 1 210 . 46 HIS CB C 35.446 0.5 1 211 . 46 HIS C C 174.573 0.5 1 212 . 47 GLN N N 124.992 0.1 1 213 . 47 GLN H H 7.957 0.01 1 214 . 47 GLN CA C 58.103 0.5 1 215 . 47 GLN CB C 27.556 0.5 1 216 . 47 GLN C C 174.743 0.5 1 217 . 48 ASN N N 114.440 0.1 1 218 . 48 ASN H H 8.290 0.01 1 219 . 48 ASN CA C 53.962 0.5 1 220 . 48 ASN CB C 40.265 0.5 1 221 . 48 ASN C C 176.533 0.5 1 222 . 49 ASN N N 120.452 0.1 1 223 . 49 ASN H H 10.010 0.01 1 224 . 49 ASN CA C 52.986 0.5 1 225 . 49 ASN CB C 38.137 0.5 1 226 . 49 ASN C C 176.164 0.5 1 227 . 50 GLY N N 113.517 0.1 1 228 . 50 GLY H H 7.787 0.01 1 229 . 50 GLY CA C 47.423 0.5 1 230 . 50 GLY C C 172.569 0.5 1 231 . 51 LEU N N 119.424 0.1 1 232 . 51 LEU H H 7.213 0.01 1 233 . 51 LEU CA C 52.731 0.5 1 234 . 51 LEU CB C 45.191 0.5 1 235 . 51 LEU C C 176.062 0.5 1 236 . 52 ASP N N 122.396 0.1 1 237 . 52 ASP H H 9.214 0.01 1 238 . 52 ASP CA C 51.595 0.5 1 239 . 52 ASP CB C 45.313 0.5 1 240 . 52 ASP C C 175.027 0.5 1 241 . 53 THR N N 118.850 0.1 1 242 . 53 THR H H 8.667 0.01 1 243 . 53 THR CA C 64.851 0.5 1 244 . 53 THR CB C 69.367 0.5 1 245 . 53 THR C C 174.323 0.5 1 246 . 54 GLU N N 129.554 0.1 1 247 . 54 GLU H H 8.620 0.01 1 248 . 54 GLU CA C 55.997 0.5 1 249 . 54 GLU CB C 28.833 0.5 1 250 . 54 GLU C C 173.608 0.5 1 251 . 55 ASN N N 123.975 0.1 1 252 . 55 ASN H H 8.693 0.01 1 253 . 55 ASN CA C 56.290 0.5 1 254 . 55 ASN CB C 40.752 0.5 1 255 . 55 ASN C C 176.174 0.5 1 256 . 56 ASN N N 113.899 0.1 1 257 . 56 ASN H H 9.934 0.01 1 258 . 56 ASN CA C 54.247 0.5 1 259 . 56 ASN CB C 34.427 0.5 1 260 . 56 ASN C C 173.539 0.5 1 261 . 57 HIS N N 118.025 0.1 1 262 . 57 HIS H H 8.715 0.01 1 263 . 57 HIS CA C 54.638 0.5 1 264 . 57 HIS CB C 28.589 0.5 1 265 . 57 HIS C C 177.290 0.5 1 266 . 58 ASN N N 114.436 0.1 1 267 . 58 ASN H H 8.385 0.01 1 268 . 58 ASN CA C 55.490 0.5 1 269 . 58 ASN CB C 40.326 0.5 1 270 . 58 ASN C C 175.291 0.5 1 271 . 59 GLY N N 112.915 0.1 1 272 . 59 GLY H H 8.922 0.01 1 273 . 59 GLY CA C 49.627 0.5 1 274 . 59 GLY C C 177.855 0.5 1 275 . 60 SER N N 122.375 0.1 1 276 . 60 SER H H 10.187 0.01 1 277 . 60 SER CA C 60.944 0.5 1 278 . 60 SER CB C 62.219 0.5 1 279 . 60 SER C C 177.334 0.5 1 280 . 61 LEU N N 127.667 0.1 1 281 . 61 LEU H H 7.880 0.01 1 282 . 61 LEU CA C 58.451 0.5 1 283 . 61 LEU CB C 41.238 0.5 1 284 . 61 LEU C C 178.640 0.5 1 285 . 62 LEU N N 121.915 0.1 1 286 . 62 LEU H H 8.268 0.01 1 287 . 62 LEU CA C 55.426 0.5 1 288 . 62 LEU CB C 38.927 0.5 1 289 . 62 LEU C C 179.033 0.5 1 290 . 63 ALA N N 124.404 0.1 1 291 . 63 ALA H H 8.456 0.01 1 292 . 63 ALA CA C 54.976 0.5 1 293 . 63 ALA CB C 17.157 0.5 1 294 . 63 ALA C C 179.764 0.5 1 295 . 64 GLY N N 107.462 0.1 1 296 . 64 GLY H H 8.505 0.01 1 297 . 64 GLY CA C 47.125 0.5 1 298 . 64 GLY C C 174.497 0.5 1 299 . 65 ALA N N 124.909 0.1 1 300 . 65 ALA H H 8.805 0.01 1 301 . 65 ALA CA C 55.195 0.5 1 302 . 65 ALA CB C 17.096 0.5 1 303 . 65 ALA C C 179.174 0.5 1 304 . 66 TYR N N 120.912 0.1 1 305 . 66 TYR H H 9.050 0.01 1 306 . 66 TYR CA C 62.062 0.5 1 307 . 66 TYR CB C 37.590 0.5 1 308 . 66 TYR C C 178.861 0.5 1 309 . 67 ALA N N 125.006 0.1 1 310 . 67 ALA H H 8.771 0.01 1 311 . 67 ALA CA C 54.639 0.5 1 312 . 67 ALA CB C 17.096 0.5 1 313 . 67 ALA C C 180.751 0.5 1 314 . 68 ILE N N 120.899 0.1 1 315 . 68 ILE H H 8.678 0.01 1 316 . 68 ILE CA C 65.617 0.5 1 317 . 68 ILE CB C 36.799 0.5 1 318 . 68 ILE C C 177.804 0.5 1 319 . 69 SER N N 119.009 0.1 1 320 . 69 SER H H 8.679 0.01 1 321 . 69 SER CA C 62.211 0.5 1 322 . 69 SER CB C 61.367 0.5 1 323 . 69 SER C C 176.861 0.5 1 324 . 70 THR N N 118.419 0.1 1 325 . 70 THR H H 7.981 0.01 1 326 . 70 THR CA C 65.014 0.5 1 327 . 70 THR CB C 67.756 0.5 1 328 . 70 THR C C 176.507 0.5 1 329 . 71 LEU N N 129.410 0.1 1 330 . 71 LEU H H 7.638 0.01 1 331 . 71 LEU CA C 57.369 0.5 1 332 . 71 LEU CB C 40.646 0.5 1 333 . 71 LEU C C 178.420 0.5 1 334 . 72 ILE N N 120.368 0.1 1 335 . 72 ILE H H 8.380 0.01 1 336 . 72 ILE CA C 66.204 0.5 1 337 . 72 ILE CB C 37.164 0.5 1 338 . 72 ILE C C 176.879 0.5 1 339 . 73 LYS N N 120.258 0.1 1 340 . 73 LYS H H 7.132 0.01 1 341 . 73 LYS CA C 59.377 0.5 1 342 . 73 LYS CB C 30.998 0.5 1 343 . 73 LYS C C 178.489 0.5 1 344 . 74 GLN N N 118.949 0.1 1 345 . 74 GLN H H 7.783 0.01 1 346 . 74 GLN CA C 58.614 0.5 1 347 . 74 GLN CB C 28.103 0.5 1 348 . 74 GLN C C 179.879 0.5 1 349 . 75 LYS N N 120.318 0.1 1 350 . 75 LYS H H 8.465 0.01 1 351 . 75 LYS CA C 57.287 0.5 1 352 . 75 LYS CB C 30.414 0.5 1 353 . 75 LYS C C 180.827 0.5 1 354 . 76 LEU N N 121.826 0.1 1 355 . 76 LEU H H 8.407 0.01 1 356 . 76 LEU CA C 57.532 0.5 1 357 . 76 LEU CB C 41.360 0.5 1 358 . 76 LEU C C 179.005 0.5 1 359 . 77 ASP N N 119.438 0.1 1 360 . 77 ASP H H 8.513 0.01 1 361 . 77 ASP CA C 56.383 0.5 1 362 . 77 ASP CB C 39.961 0.5 1 363 . 77 ASP C C 177.763 0.5 1 364 . 78 GLY N N 104.941 0.1 1 365 . 78 GLY H H 7.441 0.01 1 366 . 78 GLY CA C 44.419 0.5 1 367 . 78 GLY C C 173.475 0.5 1 368 . 79 LEU N N 124.466 0.1 1 369 . 79 LEU H H 7.259 0.01 1 370 . 79 LEU CA C 54.666 0.5 1 371 . 79 LEU CB C 41.421 0.5 1 372 . 79 LEU C C 175.142 0.5 1 373 . 80 LYS N N 125.728 0.1 1 374 . 80 LYS H H 8.417 0.01 1 375 . 80 LYS CA C 54.327 0.5 1 376 . 80 LYS CB C 32.603 0.5 1 377 . 80 LYS C C 175.658 0.5 1 378 . 81 ASN N N 122.360 0.1 1 379 . 81 ASN H H 7.895 0.01 1 380 . 81 ASN CA C 54.638 0.5 1 381 . 81 ASN CB C 40.995 0.5 1 382 . 81 ASN C C 174.198 0.5 1 383 . 82 GLU N N 128.900 0.1 1 384 . 82 GLU H H 9.000 0.01 1 385 . 82 GLU CA C 59.343 0.5 1 386 . 82 GLU CB C 28.772 0.5 1 387 . 82 GLU C C 178.688 0.5 1 388 . 83 GLY N N 108.787 0.1 1 389 . 83 GLY H H 8.177 0.01 1 390 . 83 GLY CA C 46.323 0.5 1 391 . 83 GLY C C 175.781 0.5 1 392 . 84 LEU N N 118.913 0.1 1 393 . 84 LEU H H 7.880 0.01 1 394 . 84 LEU CA C 53.308 0.5 1 395 . 84 LEU CB C 41.603 0.5 1 396 . 84 LEU C C 177.349 0.5 1 397 . 85 LYS N N 123.514 0.1 1 398 . 85 LYS H H 7.375 0.01 1 399 . 85 LYS CA C 60.885 0.5 1 400 . 85 LYS CB C 32.299 0.5 1 401 . 85 LYS C C 177.142 0.5 1 402 . 86 GLU N N 118.347 0.1 1 403 . 86 GLU H H 8.830 0.01 1 404 . 86 GLU CA C 59.634 0.5 1 405 . 86 GLU CB C 28.407 0.5 1 406 . 86 GLU C C 179.897 0.5 1 407 . 87 LYS N N 120.015 0.1 1 408 . 87 LYS H H 7.529 0.01 1 409 . 87 LYS CA C 58.398 0.5 1 410 . 87 LYS CB C 32.603 0.5 1 411 . 87 LYS C C 180.037 0.5 1 412 . 88 ILE N N 124.934 0.1 1 413 . 88 ILE H H 8.623 0.01 1 414 . 88 ILE CA C 65.779 0.5 1 415 . 88 ILE CB C 37.468 0.5 1 416 . 88 ILE C C 177.692 0.5 1 417 . 89 ASP N N 121.421 0.1 1 418 . 89 ASP H H 8.842 0.01 1 419 . 89 ASP CA C 57.299 0.5 1 420 . 89 ASP CB C 39.232 0.5 1 421 . 89 ASP C C 179.233 0.5 1 422 . 90 ALA N N 122.863 0.1 1 423 . 90 ALA H H 7.734 0.01 1 424 . 90 ALA CA C 54.773 0.5 1 425 . 90 ALA CB C 17.400 0.5 1 426 . 90 ALA C C 180.201 0.5 1 427 . 91 ALA N N 122.852 0.1 1 428 . 91 ALA H H 7.474 0.01 1 429 . 91 ALA CA C 54.390 0.5 1 430 . 91 ALA CB C 17.096 0.5 1 431 . 91 ALA C C 179.536 0.5 1 432 . 92 LYS N N 120.536 0.1 1 433 . 92 LYS H H 8.873 0.01 1 434 . 92 LYS CA C 60.218 0.5 1 435 . 92 LYS CB C 31.511 0.5 1 436 . 92 LYS C C 179.245 0.5 1 437 . 93 LYS N N 121.408 0.1 1 438 . 93 LYS H H 8.106 0.01 1 439 . 93 LYS CA C 58.816 0.5 1 440 . 93 LYS CB C 30.779 0.5 1 441 . 93 LYS C C 180.183 0.5 1 442 . 94 CYS N N 118.903 0.1 1 443 . 94 CYS H H 8.227 0.01 1 444 . 94 CYS CA C 63.534 0.5 1 445 . 94 CYS CB C 26.643 0.5 1 446 . 94 CYS C C 178.243 0.5 1 447 . 95 SER N N 120.083 0.1 1 448 . 95 SER H H 8.696 0.01 1 449 . 95 SER CA C 61.507 0.5 1 450 . 95 SER CB C 62.279 0.5 1 451 . 95 SER C C 176.292 0.5 1 452 . 96 GLU N N 122.852 0.1 1 453 . 96 GLU H H 8.078 0.01 1 454 . 96 GLU CA C 58.882 0.5 1 455 . 96 GLU CB C 29.197 0.5 1 456 . 96 GLU C C 178.325 0.5 1 457 . 97 THR N N 115.416 0.1 1 458 . 97 THR H H 8.324 0.01 1 459 . 97 THR CA C 66.127 0.5 1 460 . 97 THR CB C 68.239 0.5 1 461 . 97 THR C C 176.958 0.5 1 462 . 98 PHE N N 122.877 0.1 1 463 . 98 PHE H H 7.825 0.01 1 464 . 98 PHE CA C 60.268 0.5 1 465 . 98 PHE CB C 38.198 0.5 1 466 . 98 PHE C C 174.987 0.5 1 467 . 99 THR N N 116.460 0.1 1 468 . 99 THR H H 8.131 0.01 1 469 . 99 THR CA C 67.152 0.5 1 470 . 99 THR CB C 68.445 0.5 1 471 . 99 THR C C 176.295 0.5 1 472 . 100 ASN N N 117.399 0.1 1 473 . 100 ASN H H 8.454 0.01 1 474 . 100 ASN CA C 55.170 0.5 1 475 . 100 ASN CB C 36.921 0.5 1 476 . 100 ASN C C 178.014 0.5 1 477 . 101 LYS N N 125.167 0.1 1 478 . 101 LYS H H 7.903 0.01 1 479 . 101 LYS CA C 56.679 0.5 1 480 . 101 LYS CB C 29.258 0.5 1 481 . 101 LYS C C 177.063 0.5 1 482 . 102 LEU N N 117.028 0.1 1 483 . 102 LEU H H 7.364 0.01 1 484 . 102 LEU CA C 57.486 0.5 1 485 . 102 LEU CB C 40.813 0.5 1 486 . 102 LEU C C 178.683 0.5 1 487 . 103 LYS N N 113.890 0.1 1 488 . 103 LYS H H 7.137 0.01 1 489 . 103 LYS CA C 57.481 0.5 1 490 . 103 LYS CB C 31.558 0.5 1 491 . 103 LYS C C 179.739 0.5 1 492 . 104 GLU N N 121.413 0.1 1 493 . 104 GLU H H 8.294 0.01 1 494 . 104 GLU CA C 58.503 0.5 1 495 . 104 GLU CB C 29.137 0.5 1 496 . 104 GLU C C 179.269 0.5 1 497 . 105 LYS N N 117.081 0.1 1 498 . 105 LYS H H 7.555 0.01 1 499 . 105 LYS CA C 52.728 0.5 1 500 . 105 LYS CB C 28.285 0.5 1 501 . 105 LYS C C 177.321 0.5 1 502 . 106 HIS N N 120.478 0.1 1 503 . 106 HIS H H 7.675 0.01 1 504 . 106 HIS CA C 58.965 0.5 1 505 . 106 HIS CB C 28.954 0.5 1 506 . 106 HIS C C 176.070 0.5 1 507 . 107 THR N N 118.041 0.1 1 508 . 107 THR H H 7.452 0.01 1 509 . 107 THR CA C 65.596 0.5 1 510 . 107 THR CB C 67.321 0.5 1 511 . 107 THR C C 174.996 0.5 1 512 . 108 ASP N N 117.986 0.1 1 513 . 108 ASP H H 7.148 0.01 1 514 . 108 ASP CA C 55.255 0.5 1 515 . 108 ASP CB C 42.333 0.5 1 516 . 108 ASP C C 176.743 0.5 1 517 . 109 LEU N N 114.409 0.1 1 518 . 109 LEU H H 8.012 0.01 1 519 . 109 LEU CA C 54.457 0.5 1 520 . 109 LEU CB C 42.576 0.5 1 521 . 109 LEU C C 176.144 0.5 1 522 . 110 GLY N N 111.946 0.1 1 523 . 110 GLY H H 8.548 0.01 1 524 . 110 GLY CA C 47.435 0.5 1 525 . 110 GLY C C 173.133 0.5 1 526 . 111 LYS N N 116.947 0.1 1 527 . 111 LYS H H 7.390 0.01 1 528 . 111 LYS CA C 54.076 0.5 1 529 . 111 LYS CB C 31.691 0.5 1 530 . 111 LYS C C 174.859 0.5 1 531 . 112 GLU N N 119.067 0.1 1 532 . 112 GLU H H 9.106 0.01 1 533 . 112 GLU CA C 58.610 0.5 1 534 . 112 GLU CB C 26.887 0.5 1 535 . 112 GLU C C 179.945 0.5 1 536 . 113 GLY N N 111.446 0.1 1 537 . 113 GLY H H 8.267 0.01 1 538 . 113 GLY CA C 46.509 0.5 1 539 . 113 GLY C C 174.603 0.5 1 540 . 114 VAL N N 121.865 0.1 1 541 . 114 VAL H H 6.815 0.01 1 542 . 114 VAL CA C 62.282 0.5 1 543 . 114 VAL CB C 32.664 0.5 1 544 . 114 VAL C C 178.374 0.5 1 545 . 115 THR N N 122.590 0.1 1 546 . 115 THR H H 8.861 0.01 1 547 . 115 THR CA C 61.225 0.5 1 548 . 115 THR CB C 69.315 0.5 1 549 . 115 THR C C 174.812 0.5 1 550 . 116 ASP N N 124.932 0.1 1 551 . 116 ASP H H 9.359 0.01 1 552 . 116 ASP CA C 56.989 0.5 1 553 . 116 ASP CB C 38.988 0.5 1 554 . 116 ASP C C 177.909 0.5 1 555 . 117 ALA N N 119.760 0.1 1 556 . 117 ALA H H 8.184 0.01 1 557 . 117 ALA CA C 54.904 0.5 1 558 . 117 ALA CB C 17.643 0.5 1 559 . 117 ALA C C 180.272 0.5 1 560 . 118 ASP N N 120.419 0.1 1 561 . 118 ASP H H 7.802 0.01 1 562 . 118 ASP CA C 56.928 0.5 1 563 . 118 ASP CB C 38.794 0.5 1 564 . 118 ASP C C 177.496 0.5 1 565 . 119 ALA N N 120.435 0.1 1 566 . 119 ALA H H 8.393 0.01 1 567 . 119 ALA CA C 54.751 0.5 1 568 . 119 ALA CB C 17.765 0.5 1 569 . 119 ALA C C 180.062 0.5 1 570 . 120 LYS N N 118.909 0.1 1 571 . 120 LYS H H 8.217 0.01 1 572 . 120 LYS CA C 59.730 0.5 1 573 . 120 LYS CB C 31.812 0.5 1 574 . 120 LYS C C 177.887 0.5 1 575 . 121 GLU N N 114.438 0.1 1 576 . 121 GLU H H 7.302 0.01 1 577 . 121 GLU CA C 59.148 0.5 1 578 . 121 GLU CB C 30.292 0.5 1 579 . 121 GLU C C 176.217 0.5 1 580 . 122 ALA N N 123.040 0.1 1 581 . 122 ALA H H 7.526 0.01 1 582 . 122 ALA CA C 52.923 0.5 1 583 . 122 ALA CB C 21.413 0.5 1 584 . 122 ALA C C 177.331 0.5 1 585 . 123 ILE N N 100.910 0.1 1 586 . 123 ILE H H 7.461 0.01 1 587 . 123 ILE CA C 59.510 0.5 1 588 . 123 ILE CB C 40.159 0.5 1 589 . 123 ILE C C 173.038 0.5 1 590 . 124 LEU N N 123.895 0.1 1 591 . 124 LEU H H 8.107 0.01 1 592 . 124 LEU CA C 52.604 0.5 1 593 . 124 LEU CB C 42.090 0.5 1 594 . 124 LEU C C 176.009 0.5 1 595 . 125 LYS N N 126.501 0.1 1 596 . 125 LYS H H 9.522 0.01 1 597 . 125 LYS CA C 58.761 0.5 1 598 . 125 LYS CB C 30.657 0.5 1 599 . 125 LYS C C 175.125 0.5 1 600 . 126 THR N N 106.482 0.1 1 601 . 126 THR H H 6.777 0.01 1 602 . 126 THR CA C 59.929 0.5 1 603 . 126 THR CB C 67.935 0.5 1 604 . 126 THR C C 174.916 0.5 1 605 . 127 ASN N N 123.423 0.1 1 606 . 127 ASN H H 7.812 0.01 1 607 . 127 ASN CA C 53.971 0.5 1 608 . 127 ASN CB C 39.718 0.5 1 609 . 127 ASN C C 175.689 0.5 1 610 . 128 GLY N N 109.137 0.1 1 611 . 128 GLY H H 8.114 0.01 1 612 . 128 GLY CA C 46.624 0.5 1 613 . 128 GLY C C 174.318 0.5 1 614 . 129 THR N N 112.887 0.1 1 615 . 129 THR H H 7.018 0.01 1 616 . 129 THR CA C 60.306 0.5 1 617 . 129 THR CB C 69.206 0.5 1 618 . 129 THR C C 175.351 0.5 1 619 . 130 LYS N N 126.856 0.1 1 620 . 130 LYS H H 9.033 0.01 1 621 . 130 LYS CA C 54.919 0.5 1 622 . 130 LYS CB C 33.394 0.5 1 623 . 130 LYS C C 177.847 0.5 1 624 . 131 THR N N 110.352 0.1 1 625 . 131 THR H H 8.550 0.01 1 626 . 131 THR CA C 63.190 0.5 1 627 . 131 THR CB C 69.782 0.5 1 628 . 131 THR C C 175.564 0.5 1 629 . 132 LYS N N 119.901 0.1 1 630 . 132 LYS H H 7.468 0.01 1 631 . 132 LYS CA C 55.173 0.5 1 632 . 132 LYS CB C 31.752 0.5 1 633 . 132 LYS C C 172.287 0.5 1 634 . 133 GLY N N 105.405 0.1 1 635 . 133 GLY H H 8.510 0.01 1 636 . 133 GLY CA C 45.121 0.5 1 637 . 133 GLY C C 177.095 0.5 1 638 . 134 ALA N N 123.430 0.1 1 639 . 134 ALA H H 8.802 0.01 1 640 . 134 ALA CA C 55.089 0.5 1 641 . 134 ALA CB C 16.974 0.5 1 642 . 134 ALA C C 180.448 0.5 1 643 . 135 GLU N N 121.936 0.1 1 644 . 135 GLU H H 8.049 0.01 1 645 . 135 GLU CA C 58.633 0.5 1 646 . 135 GLU CB C 28.589 0.5 1 647 . 135 GLU C C 178.557 0.5 1 648 . 136 GLU N N 123.902 0.1 1 649 . 136 GLU H H 9.453 0.01 1 650 . 136 GLU CA C 60.830 0.5 1 651 . 136 GLU CB C 27.251 0.5 1 652 . 136 GLU C C 180.546 0.5 1 653 . 137 LEU N N 125.333 0.1 1 654 . 137 LEU H H 8.902 0.01 1 655 . 137 LEU CA C 57.177 0.5 1 656 . 137 LEU CB C 39.292 0.5 1 657 . 137 LEU C C 178.795 0.5 1 658 . 138 GLY N N 107.903 0.1 1 659 . 138 GLY H H 8.053 0.01 1 660 . 138 GLY CA C 47.244 0.5 1 661 . 138 GLY C C 176.691 0.5 1 662 . 139 LYS N N 121.896 0.1 1 663 . 139 LYS H H 7.760 0.01 1 664 . 139 LYS CA C 58.229 0.5 1 665 . 139 LYS CB C 30.993 0.5 1 666 . 139 LYS C C 179.629 0.5 1 667 . 140 LEU N N 123.896 0.1 1 668 . 140 LEU H H 8.057 0.01 1 669 . 140 LEU CA C 57.474 0.5 1 670 . 140 LEU CB C 40.205 0.5 1 671 . 140 LEU C C 178.332 0.5 1 672 . 141 PHE N N 121.478 0.1 1 673 . 141 PHE H H 8.856 0.01 1 674 . 141 PHE CA C 62.492 0.5 1 675 . 141 PHE CB C 38.076 0.5 1 676 . 141 PHE C C 178.329 0.5 1 677 . 142 GLU N N 119.409 0.1 1 678 . 142 GLU H H 8.129 0.01 1 679 . 142 GLU CA C 59.244 0.5 1 680 . 142 GLU CB C 28.954 0.5 1 681 . 142 GLU C C 178.855 0.5 1 682 . 143 SER N N 115.962 0.1 1 683 . 143 SER H H 8.255 0.01 1 684 . 143 SER CA C 61.592 0.5 1 685 . 143 SER CB C 62.584 0.5 1 686 . 143 SER C C 178.241 0.5 1 687 . 144 VAL N N 126.610 0.1 1 688 . 144 VAL H H 8.200 0.01 1 689 . 144 VAL CA C 66.053 0.5 1 690 . 144 VAL CB C 30.049 0.5 1 691 . 144 VAL C C 176.614 0.5 1 692 . 145 GLU N N 125.042 0.1 1 693 . 145 GLU H H 8.433 0.01 1 694 . 145 GLU CA C 59.283 0.5 1 695 . 145 GLU CB C 28.164 0.5 1 696 . 145 GLU C C 179.367 0.5 1 697 . 146 VAL N N 119.763 0.1 1 698 . 146 VAL H H 7.785 0.01 1 699 . 146 VAL CA C 66.066 0.5 1 700 . 146 VAL CB C 31.083 0.5 1 701 . 146 VAL C C 179.043 0.5 1 702 . 147 LEU N N 122.891 0.1 1 703 . 147 LEU H H 7.292 0.01 1 704 . 147 LEU CA C 57.690 0.5 1 705 . 147 LEU CB C 41.299 0.5 1 706 . 147 LEU C C 176.888 0.5 1 707 . 148 SER N N 115.919 0.1 1 708 . 148 SER H H 9.032 0.01 1 709 . 148 SER CA C 61.197 0.5 1 710 . 148 SER CB C 62.462 0.5 1 711 . 148 SER C C 177.045 0.5 1 712 . 149 LYS N N 120.924 0.1 1 713 . 149 LYS H H 8.356 0.01 1 714 . 149 LYS CA C 59.711 0.5 1 715 . 149 LYS CB C 31.630 0.5 1 716 . 149 LYS C C 179.194 0.5 1 717 . 150 ALA N N 121.603 0.1 1 718 . 150 ALA H H 7.677 0.01 1 719 . 150 ALA CA C 54.262 0.5 1 720 . 150 ALA CB C 17.886 0.5 1 721 . 150 ALA C C 180.539 0.5 1 722 . 151 ALA N N 123.424 0.1 1 723 . 151 ALA H H 8.698 0.01 1 724 . 151 ALA CA C 54.533 0.5 1 725 . 151 ALA CB C 17.400 0.5 1 726 . 151 ALA C C 179.725 0.5 1 727 . 152 LYS N N 121.335 0.1 1 728 . 152 LYS H H 8.790 0.01 1 729 . 152 LYS CA C 59.929 0.5 1 730 . 152 LYS CB C 31.569 0.5 1 731 . 152 LYS C C 179.735 0.5 1 732 . 153 GLU N N 121.803 0.1 1 733 . 153 GLU H H 8.010 0.01 1 734 . 153 GLU CA C 58.693 0.5 1 735 . 153 GLU CB C 28.650 0.5 1 736 . 153 GLU C C 178.077 0.5 1 737 . 154 MET N N 119.921 0.1 1 738 . 154 MET H H 7.848 0.01 1 739 . 154 MET CA C 58.961 0.5 1 740 . 154 MET CB C 32.299 0.5 1 741 . 154 MET C C 179.734 0.5 1 742 . 155 LEU N N 121.390 0.1 1 743 . 155 LEU H H 7.566 0.01 1 744 . 155 LEU CA C 57.355 0.5 1 745 . 155 LEU CB C 40.083 0.5 1 746 . 155 LEU C C 178.512 0.5 1 747 . 156 ALA N N 123.338 0.1 1 748 . 156 ALA H H 8.478 0.01 1 749 . 156 ALA CA C 55.022 0.5 1 750 . 156 ALA CB C 17.157 0.5 1 751 . 156 ALA C C 181.065 0.5 1 752 . 157 ASN N N 117.429 0.1 1 753 . 157 ASN H H 8.864 0.01 1 754 . 157 ASN CA C 55.289 0.5 1 755 . 157 ASN CB C 37.164 0.5 1 756 . 157 ASN C C 177.874 0.5 1 757 . 158 SER N N 118.915 0.1 1 758 . 158 SER H H 7.779 0.01 1 759 . 158 SER CA C 62.295 0.5 1 760 . 158 SER C C 174.994 0.5 1 761 . 159 VAL N N 120.450 0.1 1 762 . 159 VAL H H 7.913 0.01 1 763 . 159 VAL CA C 65.412 0.5 1 764 . 159 VAL CB C 30.909 0.5 1 765 . 159 VAL C C 179.522 0.5 1 766 . 160 LYS N N 122.344 0.1 1 767 . 160 LYS H H 8.163 0.01 1 768 . 160 LYS CA C 58.599 0.5 1 769 . 160 LYS CB C 31.508 0.5 1 770 . 160 LYS C C 178.146 0.5 1 771 . 161 GLU N N 118.891 0.1 1 772 . 161 GLU H H 7.390 0.01 1 773 . 161 GLU CA C 58.651 0.5 1 774 . 161 GLU CB C 29.015 0.5 1 775 . 161 GLU C C 177.667 0.5 1 776 . 162 LEU N N 115.619 0.1 1 777 . 162 LEU H H 7.645 0.01 1 778 . 162 LEU CA C 56.524 0.5 1 779 . 162 LEU CB C 41.664 0.5 1 780 . 162 LEU C C 176.924 0.5 1 781 . 163 THR N N 104.914 0.1 1 782 . 163 THR H H 7.318 0.01 1 783 . 163 THR CA C 60.427 0.5 1 784 . 163 THR CB C 69.223 0.5 1 785 . 163 THR C C 174.634 0.5 1 786 . 164 SER N N 119.894 0.1 1 787 . 164 SER H H 7.718 0.01 1 788 . 164 SER CA C 56.356 0.5 1 789 . 164 SER CB C 62.938 0.5 1 790 . 164 SER C C 172.272 0.5 1 791 . 165 PRO CA C 62.858 0.5 1 792 . 165 PRO CB C 31.448 0.5 1 793 . 165 PRO C C 176.860 0.5 1 794 . 166 VAL N N 121.414 0.1 1 795 . 166 VAL H H 8.183 0.01 1 796 . 166 VAL CA C 62.070 0.5 1 797 . 166 VAL CB C 31.752 0.5 1 798 . 166 VAL C C 176.231 0.5 1 799 . 167 VAL N N 125.326 0.1 1 800 . 167 VAL H H 8.107 0.01 1 801 . 167 VAL CA C 61.535 0.5 1 802 . 167 VAL CB C 32.056 0.5 1 803 . 167 VAL C C 175.554 0.5 1 804 . 168 ALA N N 128.876 0.1 1 805 . 168 ALA H H 8.274 0.01 1 806 . 168 ALA CA C 51.885 0.5 1 807 . 168 ALA CB C 18.738 0.5 1 808 . 168 ALA C C 177.289 0.5 1 809 . 169 GLU N N 121.497 0.1 1 810 . 169 GLU H H 8.272 0.01 1 811 . 169 GLU CA C 55.764 0.5 1 812 . 169 GLU CB C 29.927 0.5 1 813 . 169 GLU C C 176.233 0.5 1 814 . 170 SER N N 119.844 0.1 1 815 . 170 SER H H 8.369 0.01 1 816 . 170 SER CA C 56.192 0.5 1 817 . 170 SER CB C 62.741 0.5 1 818 . 170 SER C C 172.614 0.5 1 819 . 171 PRO CA C 62.774 0.5 1 820 . 171 PRO CB C 31.265 0.5 1 821 . 171 PRO C C 176.765 0.5 1 822 . 172 LYS N N 122.908 0.1 1 823 . 172 LYS H H 8.278 0.01 1 824 . 172 LYS CA C 55.680 0.5 1 825 . 172 LYS CB C 32.238 0.5 1 826 . 172 LYS C C 176.208 0.5 1 827 . 173 LYS N N 125.887 0.1 1 828 . 173 LYS H H 8.238 0.01 1 829 . 173 LYS CA C 53.611 0.5 1 830 . 173 LYS CB C 31.569 0.5 1 831 . 173 LYS C C 173.609 0.5 1 stop_ save_