data_18376 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Free MTIP(61-204) from Plasmodium falciparum ; _BMRB_accession_number 18376 _BMRB_flat_file_name bmr18376.str _Entry_type original _Submission_date 2012-04-03 _Accession_date 2012-04-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of free MTIP(61-204)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Douse Christopher H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 137 "13C chemical shifts" 422 "15N chemical shifts" 137 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-03-25 update BMRB 'update entry citation' 2012-04-16 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18377 MTIP(61-204)(61-204)/MyoA(799-818) stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22932904 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Douse Christopher H. . 2 Green Judith L. . 3 Salgado Paula S. . 4 Simpson Peter J. . 5 Thomas Jemima C. . 6 Langsley Gordon . . 7 Holder Anthony A. . 8 Tate Edward W. . 9 Cota Ernesto . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 287 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 36968 _Page_last 36977 _Year 2012 _Details . loop_ _Keyword dynamics 'light chain' malaria myosin Plasmodium stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MTIP(61-204) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MTIP(61-204) $MTIP(61-204) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MTIP(61-204) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MTIP(61-204) _Molecular_mass 17605 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 154 _Mol_residue_sequence ; RGSHHHHHHGSVADIQQLEE KVDESDVRIYFNEKSSGGKI SIDNASYNARKLGLAPSSID EKKIKELYGDNLTYEQYLEY LSICVHDKDNVEELIKMFAH FDNNCTGYLTKSQMKNILTT WGDALTDQEAIDALNAFSSE DNIDYKLFCEDILQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 51 ARG 2 52 GLY 3 53 SER 4 54 HIS 5 55 HIS 6 56 HIS 7 57 HIS 8 58 HIS 9 59 HIS 10 60 GLY 11 61 SER 12 62 VAL 13 63 ALA 14 64 ASP 15 65 ILE 16 66 GLN 17 67 GLN 18 68 LEU 19 69 GLU 20 70 GLU 21 71 LYS 22 72 VAL 23 73 ASP 24 74 GLU 25 75 SER 26 76 ASP 27 77 VAL 28 78 ARG 29 79 ILE 30 80 TYR 31 81 PHE 32 82 ASN 33 83 GLU 34 84 LYS 35 85 SER 36 86 SER 37 87 GLY 38 88 GLY 39 89 LYS 40 90 ILE 41 91 SER 42 92 ILE 43 93 ASP 44 94 ASN 45 95 ALA 46 96 SER 47 97 TYR 48 98 ASN 49 99 ALA 50 100 ARG 51 101 LYS 52 102 LEU 53 103 GLY 54 104 LEU 55 105 ALA 56 106 PRO 57 107 SER 58 108 SER 59 109 ILE 60 110 ASP 61 111 GLU 62 112 LYS 63 113 LYS 64 114 ILE 65 115 LYS 66 116 GLU 67 117 LEU 68 118 TYR 69 119 GLY 70 120 ASP 71 121 ASN 72 122 LEU 73 123 THR 74 124 TYR 75 125 GLU 76 126 GLN 77 127 TYR 78 128 LEU 79 129 GLU 80 130 TYR 81 131 LEU 82 132 SER 83 133 ILE 84 134 CYS 85 135 VAL 86 136 HIS 87 137 ASP 88 138 LYS 89 139 ASP 90 140 ASN 91 141 VAL 92 142 GLU 93 143 GLU 94 144 LEU 95 145 ILE 96 146 LYS 97 147 MET 98 148 PHE 99 149 ALA 100 150 HIS 101 151 PHE 102 152 ASP 103 153 ASN 104 154 ASN 105 155 CYS 106 156 THR 107 157 GLY 108 158 TYR 109 159 LEU 110 160 THR 111 161 LYS 112 162 SER 113 163 GLN 114 164 MET 115 165 LYS 116 166 ASN 117 167 ILE 118 168 LEU 119 169 THR 120 170 THR 121 171 TRP 122 172 GLY 123 173 ASP 124 174 ALA 125 175 LEU 126 176 THR 127 177 ASP 128 178 GLN 129 179 GLU 130 180 ALA 131 181 ILE 132 182 ASP 133 183 ALA 134 184 LEU 135 185 ASN 136 186 ALA 137 187 PHE 138 188 SER 139 189 SER 140 190 GLU 141 191 ASP 142 192 ASN 143 193 ILE 144 194 ASP 145 195 TYR 146 196 LYS 147 197 LEU 148 198 PHE 149 199 CYS 150 200 GLU 151 201 ASP 152 202 ILE 153 203 LEU 154 204 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-22 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18377 MTIP(61-204) 100.00 154 100.00 100.00 3.43e-108 PDB 2QAC "The Closed Mtip-myosina-tail Complex From The Malaria Parasite Invasion Machinery" 93.51 146 100.00 100.00 3.99e-99 PDB 4AOM "Mtip And Myoa Complex" 93.51 146 100.00 100.00 3.99e-99 PDB 4MZJ "Crystal Structure Of Mtip From Plasmodium Falciparum In Complex With Pgly[801,805], A Stapled Myoa Tail Peptide" 94.16 145 100.00 100.00 6.71e-100 PDB 4MZK "Crystal Structure Of Mtip From Plasmodium Falciparum In Complex With Pgly[807,811], A Stapled Myoa Tail Peptide" 94.16 145 100.00 100.00 6.71e-100 PDB 4MZL "Crystal Structure Of Mtip From Plasmodium Falciparum In Complex With Hbs Myoa, A Hydrogen Bond Surrogate Myoa Helix Mimetic" 94.16 145 100.00 100.00 6.71e-100 PDB 4R1E "Crystal Structure Of Mtip From Plasmodium Falciparum In Complex With A Peptide-fragment Chimera" 94.16 145 100.00 100.00 6.71e-100 EMBL CDO65736 "myosin A tail domain interacting protein [Plasmodium reichenowi]" 93.51 204 98.61 99.31 4.58e-97 GB AAN36529 "myosin A tail domain interacting protein [Plasmodium falciparum 3D7]" 93.51 204 100.00 100.00 3.34e-98 GB ETW17315 "hypothetical protein PFFVO_03747 [Plasmodium falciparum Vietnam Oak-Knoll (FVO)]" 93.51 204 99.31 100.00 1.27e-97 GB ETW29792 "hypothetical protein PFFCH_02759 [Plasmodium falciparum FCH/4]" 93.51 204 99.31 100.00 1.27e-97 GB ETW35145 "hypothetical protein PFTANZ_04108 [Plasmodium falciparum Tanzania (2000708)]" 93.51 281 99.31 100.00 1.48e-96 GB ETW41309 "hypothetical protein PFNF135_04294 [Plasmodium falciparum NF135/5.C10]" 93.51 204 100.00 100.00 3.34e-98 REF XP_001350849 "myosin A tail domain interacting protein [Plasmodium falciparum 3D7]" 93.51 204 100.00 100.00 3.34e-98 REF XP_012764323 "myosin A tail domain interacting protein [Plasmodium reichenowi]" 93.51 204 98.61 99.31 4.58e-97 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MTIP(61-204) 'malaria parasite P. falciparum' 5833 Eukaryota . Plasmodium falciparum 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 _Details $MTIP(61-204) 'recombinant technology' . Escherichia coli . pQE30 'non-cleavable N-terminal His6 tag' 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 $MTIP(61-204) 0.5 mM '[U-98% 13C; U-98% 15N]' 'MOPS buffer' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' TCEP 1 mM 'natural abundance' 'sodium azide' 0.005 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 water C 13 protons ppm 4.725 internal indirect . . . 0.251449530 water H 1 protons ppm 4.725 internal direct . . . 1 water N 15 protons ppm 4.725 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MTIP(61-204) _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 60 10 GLY C C 174.029 0.50 1 2 60 10 GLY CA C 45.400 0.50 1 3 61 11 SER H H 8.266 0.03 1 4 61 11 SER C C 174.770 0.50 1 5 61 11 SER CA C 58.088 0.50 1 6 61 11 SER CB C 64.160 0.50 1 7 61 11 SER N N 115.872 0.20 1 8 62 12 VAL H H 8.181 0.03 1 9 62 12 VAL C C 175.871 0.50 1 10 62 12 VAL CA C 62.759 0.50 1 11 62 12 VAL CB C 32.634 0.50 1 12 62 12 VAL N N 121.255 0.20 1 13 63 13 ALA H H 8.213 0.03 1 14 63 13 ALA C C 177.373 0.50 1 15 63 13 ALA CA C 52.717 0.50 1 16 63 13 ALA CB C 19.400 0.50 1 17 63 13 ALA N N 126.076 0.20 1 18 64 14 ASP H H 8.092 0.03 1 19 64 14 ASP C C 176.572 0.50 1 20 64 14 ASP CA C 54.508 0.50 1 21 64 14 ASP CB C 41.274 0.50 1 22 64 14 ASP N N 119.217 0.20 1 23 65 15 ILE H H 7.971 0.03 1 24 65 15 ILE C C 176.472 0.50 1 25 65 15 ILE CA C 61.747 0.50 1 26 65 15 ILE CB C 38.550 0.50 1 27 65 15 ILE N N 120.482 0.20 1 28 66 16 GLN H H 8.305 0.03 1 29 66 16 GLN C C 176.352 0.50 1 30 66 16 GLN CA C 56.921 0.50 1 31 66 16 GLN CB C 29.208 0.50 1 32 66 16 GLN N N 123.012 0.20 1 33 67 17 GLN H H 8.240 0.03 1 34 67 17 GLN C C 176.292 0.50 1 35 67 17 GLN CA C 56.376 0.50 1 36 67 17 GLN CB C 29.053 0.50 1 37 67 17 GLN N N 120.427 0.20 1 38 68 18 LEU H H 8.115 0.03 1 39 68 18 LEU C C 177.553 0.50 1 40 68 18 LEU CA C 55.987 0.50 1 41 68 18 LEU CB C 42.442 0.50 1 42 68 18 LEU N N 122.558 0.20 1 43 69 19 GLU H H 8.300 0.03 1 44 69 19 GLU C C 176.492 0.50 1 45 69 19 GLU CA C 57.466 0.50 1 46 69 19 GLU CB C 30.220 0.50 1 47 69 19 GLU N N 120.235 0.20 1 48 70 20 GLU H H 8.189 0.03 1 49 70 20 GLU C C 176.412 0.50 1 50 70 20 GLU CA C 56.999 0.50 1 51 70 20 GLU CB C 30.143 0.50 1 52 70 20 GLU N N 120.719 0.20 1 53 71 21 LYS H H 8.220 0.03 1 54 71 21 LYS C C 176.412 0.50 1 55 71 21 LYS CA C 55.909 0.50 1 56 71 21 LYS CB C 33.490 0.50 1 57 71 21 LYS N N 121.643 0.20 1 58 72 22 VAL H H 8.138 0.03 1 59 72 22 VAL C C 175.231 0.50 1 60 72 22 VAL CA C 61.903 0.50 1 61 72 22 VAL CB C 33.101 0.50 1 62 72 22 VAL N N 120.600 0.20 1 63 73 23 ASP H H 8.432 0.03 1 64 73 23 ASP C C 176.072 0.50 1 65 73 23 ASP CA C 54.274 0.50 1 66 73 23 ASP CB C 41.586 0.50 1 67 73 23 ASP N N 123.696 0.20 1 68 74 24 GLU H H 8.482 0.03 1 69 74 24 GLU C C 176.392 0.50 1 70 74 24 GLU CA C 57.154 0.50 1 71 74 24 GLU CB C 30.065 0.50 1 72 74 24 GLU N N 123.495 0.20 1 73 75 25 SER H H 8.319 0.03 1 74 75 25 SER C C 175.391 0.50 1 75 75 25 SER CA C 59.256 0.50 1 76 75 25 SER CB C 63.927 0.50 1 77 75 25 SER N N 116.163 0.20 1 78 76 26 ASP H H 8.288 0.03 1 79 76 26 ASP C C 176.752 0.50 1 80 76 26 ASP CA C 57.388 0.50 1 81 76 26 ASP CB C 39.795 0.50 1 82 76 26 ASP N N 123.422 0.20 1 83 77 27 VAL H H 7.783 0.03 1 84 77 27 VAL C C 178.855 0.50 1 85 77 27 VAL CA C 67.040 0.50 1 86 77 27 VAL CB C 32.556 0.50 1 87 77 27 VAL N N 116.773 0.20 1 88 78 28 ARG H H 7.519 0.03 1 89 78 28 ARG C C 177.834 0.50 1 90 78 28 ARG CA C 58.088 0.50 1 91 78 28 ARG CB C 30.220 0.50 1 92 78 28 ARG N N 121.619 0.20 1 93 79 29 ILE H H 8.455 0.03 1 94 79 29 ILE C C 179.616 0.50 1 95 79 29 ILE CA C 65.483 0.50 1 96 79 29 ILE CB C 37.771 0.50 1 97 79 29 ILE N N 122.338 0.20 1 98 80 30 TYR H H 8.791 0.03 1 99 80 30 TYR C C 180.497 0.50 1 100 80 30 TYR CA C 57.777 0.50 1 101 80 30 TYR CB C 35.202 0.50 1 102 80 30 TYR N N 117.075 0.20 1 103 81 31 PHE H H 7.571 0.03 1 104 81 31 PHE C C 176.752 0.50 1 105 81 31 PHE CA C 62.603 0.50 1 106 81 31 PHE CB C 39.095 0.50 1 107 81 31 PHE N N 121.089 0.20 1 108 82 32 ASN H H 8.900 0.03 1 109 82 32 ASN C C 177.733 0.50 1 110 82 32 ASN CA C 55.831 0.50 1 111 82 32 ASN CB C 37.460 0.50 1 112 82 32 ASN N N 120.206 0.20 1 113 83 33 GLU H H 8.068 0.03 1 114 83 33 GLU C C 177.934 0.50 1 115 83 33 GLU CA C 58.789 0.50 1 116 83 33 GLU CB C 30.921 0.50 1 117 83 33 GLU N N 117.448 0.20 1 118 84 34 LYS H H 6.934 0.03 1 119 84 34 LYS C C 175.992 0.50 1 120 84 34 LYS CA C 53.963 0.50 1 121 84 34 LYS CB C 34.735 0.50 1 122 84 34 LYS N N 113.152 0.20 1 123 85 35 SER H H 7.675 0.03 1 124 85 35 SER C C 173.689 0.50 1 125 85 35 SER CA C 57.933 0.50 1 126 85 35 SER CB C 64.549 0.50 1 127 85 35 SER N N 116.835 0.20 1 128 86 36 SER H H 8.875 0.03 1 129 86 36 SER C C 176.312 0.50 1 130 86 36 SER CA C 57.855 0.50 1 131 86 36 SER CB C 64.004 0.50 1 132 86 36 SER N N 114.322 0.20 1 133 87 37 GLY C C 175.671 0.50 1 134 87 37 GLY CA C 47.190 0.50 1 135 88 38 GLY H H 8.752 0.03 1 136 88 38 GLY C C 173.369 0.50 1 137 88 38 GLY CA C 45.089 0.50 1 138 88 38 GLY N N 105.169 0.20 1 139 89 39 LYS H H 7.422 0.03 1 140 89 39 LYS C C 174.290 0.50 1 141 89 39 LYS CA C 54.430 0.50 1 142 89 39 LYS CB C 37.616 0.50 1 143 89 39 LYS N N 117.096 0.20 1 144 90 40 ILE H H 9.657 0.03 1 145 90 40 ILE C C 173.008 0.50 1 146 90 40 ILE CA C 58.088 0.50 1 147 90 40 ILE CB C 42.364 0.50 1 148 90 40 ILE N N 121.194 0.20 1 149 91 41 SER H H 8.766 0.03 1 150 91 41 SER C C 176.012 0.50 1 151 91 41 SER CA C 57.388 0.50 1 152 91 41 SER CB C 64.939 0.50 1 153 91 41 SER N N 124.383 0.20 1 154 92 42 ILE H H 8.029 0.03 1 155 92 42 ILE C C 177.293 0.50 1 156 92 42 ILE CA C 64.627 0.50 1 157 92 42 ILE CB C 36.526 0.50 1 158 92 42 ILE N N 120.956 0.20 1 159 93 43 ASP H H 8.392 0.03 1 160 93 43 ASP C C 179.756 0.50 1 161 93 43 ASP CA C 57.855 0.50 1 162 93 43 ASP CB C 40.418 0.50 1 163 93 43 ASP N N 116.964 0.20 1 164 94 44 ASN H H 7.883 0.03 1 165 94 44 ASN C C 177.193 0.50 1 166 94 44 ASN CA C 55.052 0.50 1 167 94 44 ASN CB C 37.538 0.50 1 168 94 44 ASN N N 118.227 0.20 1 169 95 45 ALA H H 9.163 0.03 1 170 95 45 ALA C C 179.836 0.50 1 171 95 45 ALA CA C 56.765 0.50 1 172 95 45 ALA CB C 18.700 0.50 1 173 95 45 ALA N N 127.085 0.20 1 174 96 46 SER H H 9.382 0.03 1 175 96 46 SER C C 175.691 0.50 1 176 96 46 SER CA C 62.837 0.50 1 177 96 46 SER CB C 62.992 0.50 1 178 96 46 SER N N 116.812 0.20 1 179 97 47 TYR H H 8.015 0.03 1 180 97 47 TYR C C 178.274 0.50 1 181 97 47 TYR CA C 61.825 0.50 1 182 97 47 TYR CB C 38.005 0.50 1 183 97 47 TYR N N 123.474 0.20 1 184 98 48 ASN H H 8.512 0.03 1 185 98 48 ASN C C 176.993 0.50 1 186 98 48 ASN CA C 55.520 0.50 1 187 98 48 ASN CB C 37.460 0.50 1 188 98 48 ASN N N 120.689 0.20 1 189 99 49 ALA H H 8.840 0.03 1 190 99 49 ALA C C 179.455 0.50 1 191 99 49 ALA CA C 56.220 0.50 1 192 99 49 ALA CB C 17.532 0.50 1 193 99 49 ALA N N 122.104 0.20 1 194 100 50 ARG H H 8.043 0.03 1 195 100 50 ARG C C 181.318 0.50 1 196 100 50 ARG CA C 59.334 0.50 1 197 100 50 ARG CB C 29.753 0.50 1 198 100 50 ARG N N 117.294 0.20 1 199 101 51 LYS H H 7.897 0.03 1 200 101 51 LYS C C 178.474 0.50 1 201 101 51 LYS CA C 59.801 0.50 1 202 101 51 LYS CB C 32.089 0.50 1 203 101 51 LYS N N 123.130 0.20 1 204 102 52 LEU H H 7.772 0.03 1 205 102 52 LEU C C 176.572 0.50 1 206 102 52 LEU CA C 55.442 0.50 1 207 102 52 LEU CB C 42.442 0.50 1 208 102 52 LEU N N 118.542 0.20 1 209 103 53 GLY H H 7.851 0.03 1 210 103 53 GLY C C 174.370 0.50 1 211 103 53 GLY CA C 45.244 0.50 1 212 103 53 GLY N N 106.631 0.20 1 213 104 54 LEU H H 8.107 0.03 1 214 104 54 LEU C C 175.311 0.50 1 215 104 54 LEU CA C 53.651 0.50 1 216 104 54 LEU CB C 42.598 0.50 1 217 104 54 LEU N N 120.518 0.20 1 218 105 55 ALA H H 8.520 0.03 1 219 105 55 ALA C C 173.829 0.50 1 220 105 55 ALA CA C 49.448 0.50 1 221 105 55 ALA CB C 19.089 0.50 1 222 105 55 ALA N N 121.111 0.20 1 223 106 56 PRO C C 177.373 0.50 1 224 106 56 PRO CA C 63.226 0.50 1 225 106 56 PRO CB C 32.400 0.50 1 226 107 57 SER H H 9.836 0.03 1 227 107 57 SER C C 175.651 0.50 1 228 107 57 SER CA C 56.220 0.50 1 229 107 57 SER CB C 67.274 0.50 1 230 107 57 SER N N 121.476 0.20 1 231 108 58 SER C C 177.193 0.50 1 232 108 58 SER CA C 61.513 0.50 1 233 108 58 SER CB C 62.525 0.50 1 234 109 59 ILE H H 7.769 0.03 1 235 109 59 ILE C C 177.633 0.50 1 236 109 59 ILE CA C 63.927 0.50 1 237 109 59 ILE CB C 37.693 0.50 1 238 109 59 ILE N N 122.297 0.20 1 239 110 60 ASP H H 7.540 0.03 1 240 110 60 ASP C C 178.054 0.50 1 241 110 60 ASP CA C 58.011 0.50 1 242 110 60 ASP CB C 41.119 0.50 1 243 110 60 ASP N N 123.494 0.20 1 244 111 61 GLU H H 7.777 0.03 1 245 111 61 GLU C C 178.454 0.50 1 246 111 61 GLU CA C 59.567 0.50 1 247 111 61 GLU CB C 29.831 0.50 1 248 111 61 GLU N N 117.766 0.20 1 249 112 62 LYS H H 7.908 0.03 1 250 112 62 LYS C C 178.795 0.50 1 251 112 62 LYS CA C 59.567 0.50 1 252 112 62 LYS CB C 32.634 0.50 1 253 112 62 LYS N N 119.190 0.20 1 254 113 63 LYS H H 8.130 0.03 1 255 113 63 LYS C C 179.315 0.50 1 256 113 63 LYS CA C 59.334 0.50 1 257 113 63 LYS CB C 32.322 0.50 1 258 113 63 LYS N N 118.886 0.20 1 259 114 64 ILE H H 7.935 0.03 1 260 114 64 ILE C C 176.772 0.50 1 261 114 64 ILE CA C 60.891 0.50 1 262 114 64 ILE CB C 39.172 0.50 1 263 114 64 ILE N N 119.095 0.20 1 264 115 65 LYS H H 7.884 0.03 1 265 115 65 LYS C C 180.477 0.50 1 266 115 65 LYS CA C 58.633 0.50 1 267 115 65 LYS CB C 32.711 0.50 1 268 115 65 LYS N N 123.915 0.20 1 269 116 66 GLU H H 8.049 0.03 1 270 116 66 GLU C C 178.154 0.50 1 271 116 66 GLU CA C 59.256 0.50 1 272 116 66 GLU CB C 29.364 0.50 1 273 116 66 GLU N N 119.558 0.20 1 274 117 67 LEU H H 7.272 0.03 1 275 117 67 LEU C C 178.975 0.50 1 276 117 67 LEU CA C 57.466 0.50 1 277 117 67 LEU CB C 42.675 0.50 1 278 117 67 LEU N N 117.423 0.20 1 279 118 68 TYR H H 8.047 0.03 1 280 118 68 TYR C C 175.871 0.50 1 281 118 68 TYR CA C 56.999 0.50 1 282 118 68 TYR CB C 41.430 0.50 1 283 118 68 TYR N N 114.788 0.20 1 284 119 69 GLY H H 8.411 0.03 1 285 119 69 GLY C C 171.466 0.50 1 286 119 69 GLY CA C 44.699 0.50 1 287 119 69 GLY N N 110.811 0.20 1 288 120 70 ASP H H 7.738 0.03 1 289 120 70 ASP C C 176.152 0.50 1 290 120 70 ASP CA C 55.753 0.50 1 291 120 70 ASP CB C 42.208 0.50 1 292 120 70 ASP N N 113.167 0.20 1 293 121 71 ASN H H 7.878 0.03 1 294 121 71 ASN C C 173.389 0.50 1 295 121 71 ASN CA C 52.094 0.50 1 296 121 71 ASN CB C 42.675 0.50 1 297 121 71 ASN N N 115.878 0.20 1 298 122 72 LEU H H 9.523 0.03 1 299 122 72 LEU C C 178.194 0.50 1 300 122 72 LEU CA C 54.118 0.50 1 301 122 72 LEU CB C 44.077 0.50 1 302 122 72 LEU N N 122.029 0.20 1 303 123 73 THR H H 8.347 0.03 1 304 123 73 THR C C 174.650 0.50 1 305 123 73 THR CA C 61.280 0.50 1 306 123 73 THR CB C 70.855 0.50 1 307 123 73 THR N N 112.008 0.20 1 308 124 74 TYR H H 9.287 0.03 1 309 124 74 TYR C C 176.893 0.50 1 310 124 74 TYR CA C 63.070 0.50 1 311 124 74 TYR CB C 37.693 0.50 1 312 124 74 TYR N N 121.079 0.20 1 313 125 75 GLU H H 8.765 0.03 1 314 125 75 GLU C C 179.756 0.50 1 315 125 75 GLU CA C 61.046 0.50 1 316 125 75 GLU CB C 28.819 0.50 1 317 125 75 GLU N N 115.839 0.20 1 318 126 76 GLN H H 7.236 0.03 1 319 126 76 GLN C C 177.673 0.50 1 320 126 76 GLN CA C 58.011 0.50 1 321 126 76 GLN CB C 27.885 0.50 1 322 126 76 GLN N N 120.770 0.20 1 323 127 77 TYR H H 8.729 0.03 1 324 127 77 TYR C C 176.212 0.50 1 325 127 77 TYR CA C 60.112 0.50 1 326 127 77 TYR CB C 37.226 0.50 1 327 127 77 TYR N N 123.643 0.20 1 328 128 78 LEU H H 8.201 0.03 1 329 128 78 LEU C C 180.537 0.50 1 330 128 78 LEU CA C 58.011 0.50 1 331 128 78 LEU CB C 41.196 0.50 1 332 128 78 LEU N N 119.946 0.20 1 333 129 79 GLU H H 7.567 0.03 1 334 129 79 GLU C C 179.315 0.50 1 335 129 79 GLU CA C 59.645 0.50 1 336 129 79 GLU CB C 29.286 0.50 1 337 129 79 GLU N N 120.633 0.20 1 338 130 80 TYR H H 8.624 0.03 1 339 130 80 TYR C C 177.253 0.50 1 340 130 80 TYR CA C 60.190 0.50 1 341 130 80 TYR CB C 37.771 0.50 1 342 130 80 TYR N N 121.390 0.20 1 343 131 81 LEU H H 8.241 0.03 1 344 131 81 LEU C C 178.975 0.50 1 345 131 81 LEU CA C 58.088 0.50 1 346 131 81 LEU CB C 40.651 0.50 1 347 131 81 LEU N N 117.902 0.20 1 348 132 82 SER H H 7.560 0.03 1 349 132 82 SER C C 177.073 0.50 1 350 132 82 SER CA C 61.513 0.50 1 351 132 82 SER CB C 63.460 0.50 1 352 132 82 SER N N 112.242 0.20 1 353 133 83 ILE H H 7.891 0.03 1 354 133 83 ILE C C 177.493 0.50 1 355 133 83 ILE CA C 64.549 0.50 1 356 133 83 ILE CB C 38.316 0.50 1 357 133 83 ILE N N 121.788 0.20 1 358 134 84 CYS H H 7.261 0.03 1 359 134 84 CYS C C 173.929 0.50 1 360 134 84 CYS CA C 61.513 0.50 1 361 134 84 CYS CB C 27.652 0.50 1 362 134 84 CYS N N 116.331 0.20 1 363 135 85 VAL H H 7.196 0.03 1 364 135 85 VAL C C 175.811 0.50 1 365 135 85 VAL CA C 63.537 0.50 1 366 135 85 VAL CB C 31.855 0.50 1 367 135 85 VAL N N 118.868 0.20 1 368 136 86 HIS H H 7.986 0.03 1 369 136 86 HIS C C 174.650 0.50 1 370 136 86 HIS CA C 55.987 0.50 1 371 136 86 HIS CB C 28.741 0.50 1 372 136 86 HIS N N 118.970 0.20 1 373 137 87 ASP H H 8.475 0.03 1 374 137 87 ASP CA C 54.585 0.50 1 375 137 87 ASP CB C 41.196 0.50 1 376 137 87 ASP N N 120.638 0.20 1 377 138 88 LYS H H 8.307 0.03 1 378 138 88 LYS C C 176.492 0.50 1 379 138 88 LYS CA C 56.609 0.50 1 380 138 88 LYS CB C 32.867 0.50 1 381 138 88 LYS N N 120.907 0.20 1 382 139 89 ASP H H 8.383 0.03 1 383 139 89 ASP C C 176.372 0.50 1 384 139 89 ASP CA C 54.897 0.50 1 385 139 89 ASP CB C 40.963 0.50 1 386 139 89 ASP N N 120.877 0.20 1 387 140 90 ASN H H 8.376 0.03 1 388 140 90 ASN C C 176.812 0.50 1 389 140 90 ASN CA C 54.196 0.50 1 390 140 90 ASN CB C 38.861 0.50 1 391 140 90 ASN N N 119.188 0.20 1 392 141 91 VAL H H 8.370 0.03 1 393 141 91 VAL C C 176.412 0.50 1 394 141 91 VAL CA C 65.795 0.50 1 395 141 91 VAL CB C 31.777 0.50 1 396 141 91 VAL N N 122.200 0.20 1 397 142 92 GLU H H 8.242 0.03 1 398 142 92 GLU C C 179.235 0.50 1 399 142 92 GLU CA C 59.957 0.50 1 400 142 92 GLU CB C 29.208 0.50 1 401 142 92 GLU N N 120.290 0.20 1 402 143 93 GLU H H 7.891 0.03 1 403 143 93 GLU C C 178.675 0.50 1 404 143 93 GLU CA C 58.867 0.50 1 405 143 93 GLU CB C 29.987 0.50 1 406 143 93 GLU N N 117.849 0.20 1 407 144 94 LEU H H 7.581 0.03 1 408 144 94 LEU C C 178.174 0.50 1 409 144 94 LEU CA C 57.699 0.50 1 410 144 94 LEU CB C 41.508 0.50 1 411 144 94 LEU N N 121.812 0.20 1 412 145 95 ILE H H 8.270 0.03 1 413 145 95 ILE C C 178.194 0.50 1 414 145 95 ILE CA C 66.495 0.50 1 415 145 95 ILE CB C 38.005 0.50 1 416 145 95 ILE N N 118.290 0.20 1 417 146 96 LYS H H 7.606 0.03 1 418 146 96 LYS C C 179.015 0.50 1 419 146 96 LYS CA C 59.723 0.50 1 420 146 96 LYS CB C 32.556 0.50 1 421 146 96 LYS N N 118.014 0.20 1 422 147 97 MET H H 7.583 0.03 1 423 147 97 MET C C 178.294 0.50 1 424 147 97 MET CA C 58.244 0.50 1 425 147 97 MET CB C 31.777 0.50 1 426 147 97 MET N N 119.400 0.20 1 427 148 98 PHE H H 7.756 0.03 1 428 148 98 PHE C C 177.733 0.50 1 429 148 98 PHE CA C 61.046 0.50 1 430 148 98 PHE CB C 38.939 0.50 1 431 148 98 PHE N N 117.059 0.20 1 432 149 99 ALA H H 8.455 0.03 1 433 149 99 ALA C C 180.336 0.50 1 434 149 99 ALA CA C 54.663 0.50 1 435 149 99 ALA CB C 18.310 0.50 1 436 149 99 ALA N N 119.740 0.20 1 437 150 100 HIS H H 7.594 0.03 1 438 150 100 HIS C C 176.292 0.50 1 439 150 100 HIS CA C 59.100 0.50 1 440 150 100 HIS CB C 29.987 0.50 1 441 150 100 HIS N N 116.660 0.20 1 442 151 101 PHE H H 7.620 0.03 1 443 151 101 PHE C C 175.371 0.50 1 444 151 101 PHE CA C 59.801 0.50 1 445 151 101 PHE CB C 39.717 0.50 1 446 151 101 PHE N N 114.542 0.20 1 447 152 102 ASP H H 7.735 0.03 1 448 152 102 ASP C C 176.792 0.50 1 449 152 102 ASP CA C 51.861 0.50 1 450 152 102 ASP CB C 39.172 0.50 1 451 152 102 ASP N N 121.629 0.20 1 452 154 104 ASN C C 174.049 0.50 1 453 154 104 ASN CA C 53.029 0.50 1 454 154 104 ASN CB C 38.316 0.50 1 455 155 105 CYS H H 8.263 0.03 1 456 155 105 CYS C C 175.131 0.50 1 457 155 105 CYS CA C 60.268 0.50 1 458 155 105 CYS CB C 25.083 0.50 1 459 155 105 CYS N N 117.580 0.20 1 460 156 106 THR H H 9.691 0.03 1 461 156 106 THR C C 177.093 0.50 1 462 156 106 THR CA C 63.460 0.50 1 463 156 106 THR CB C 70.855 0.50 1 464 156 106 THR N N 112.776 0.20 1 465 157 107 GLY H H 10.310 0.03 1 466 157 107 GLY C C 172.548 0.50 1 467 157 107 GLY CA C 44.855 0.50 1 468 157 107 GLY N N 112.441 0.20 1 469 158 108 TYR H H 8.189 0.03 1 470 158 108 TYR C C 174.730 0.50 1 471 158 108 TYR CA C 56.298 0.50 1 472 158 108 TYR CB C 42.675 0.50 1 473 158 108 TYR N N 118.419 0.20 1 474 159 109 LEU H H 8.534 0.03 1 475 159 109 LEU C C 176.412 0.50 1 476 159 109 LEU CA C 53.496 0.50 1 477 159 109 LEU CB C 47.969 0.50 1 478 159 109 LEU N N 118.887 0.20 1 479 160 110 THR H H 8.730 0.03 1 480 160 110 THR C C 176.973 0.50 1 481 160 110 THR CA C 61.280 0.50 1 482 160 110 THR CB C 71.322 0.50 1 483 160 110 THR N N 110.493 0.20 1 484 161 111 LYS H H 8.630 0.03 1 485 161 111 LYS C C 178.635 0.50 1 486 161 111 LYS CA C 61.903 0.50 1 487 161 111 LYS CB C 32.867 0.50 1 488 161 111 LYS N N 120.959 0.20 1 489 162 112 SER H H 8.722 0.03 1 490 162 112 SER C C 176.993 0.50 1 491 162 112 SER CA C 62.447 0.50 1 492 162 112 SER CB C 62.447 0.50 1 493 162 112 SER N N 113.369 0.20 1 494 163 113 GLN H H 7.702 0.03 1 495 163 113 GLN C C 179.175 0.50 1 496 163 113 GLN CA C 59.178 0.50 1 497 163 113 GLN CB C 29.909 0.50 1 498 163 113 GLN N N 121.240 0.20 1 499 164 114 MET H H 8.628 0.03 1 500 164 114 MET C C 178.134 0.50 1 501 164 114 MET CA C 57.699 0.50 1 502 164 114 MET CB C 32.400 0.50 1 503 164 114 MET N N 116.328 0.20 1 504 165 115 LYS H H 8.629 0.03 1 505 165 115 LYS C C 177.834 0.50 1 506 165 115 LYS CA C 60.813 0.50 1 507 165 115 LYS CB C 31.388 0.50 1 508 165 115 LYS N N 120.320 0.20 1 509 166 116 ASN H H 7.554 0.03 1 510 166 116 ASN C C 177.053 0.50 1 511 166 116 ASN CA C 56.220 0.50 1 512 166 116 ASN CB C 38.238 0.50 1 513 166 116 ASN N N 117.350 0.20 1 514 167 117 ILE H H 7.737 0.03 1 515 167 117 ILE C C 178.114 0.50 1 516 167 117 ILE CA C 65.250 0.50 1 517 167 117 ILE CB C 39.095 0.50 1 518 167 117 ILE N N 120.772 0.20 1 519 168 118 LEU H H 8.647 0.03 1 520 168 118 LEU CA C 58.088 0.50 1 521 168 118 LEU CB C 42.753 0.50 1 522 168 118 LEU N N 118.883 0.20 1 523 169 119 THR H H 7.851 0.03 1 524 169 119 THR C C 175.731 0.50 1 525 169 119 THR CA C 63.460 0.50 1 526 169 119 THR CB C 69.921 0.50 1 527 169 119 THR N N 106.248 0.20 1 528 170 120 THR H H 7.573 0.03 1 529 170 120 THR C C 174.550 0.50 1 530 170 120 THR CA C 64.004 0.50 1 531 170 120 THR CB C 70.465 0.50 1 532 170 120 THR N N 114.258 0.20 1 533 171 121 TRP H H 8.030 0.03 1 534 171 121 TRP C C 175.971 0.50 1 535 171 121 TRP CA C 58.244 0.50 1 536 171 121 TRP CB C 29.831 0.50 1 537 171 121 TRP N N 122.759 0.20 1 538 172 122 GLY H H 8.045 0.03 1 539 172 122 GLY C C 173.969 0.50 1 540 172 122 GLY CA C 46.178 0.50 1 541 172 122 GLY N N 108.617 0.20 1 542 173 123 ASP H H 8.006 0.03 1 543 173 123 ASP C C 175.731 0.50 1 544 173 123 ASP CA C 53.963 0.50 1 545 173 123 ASP CB C 40.418 0.50 1 546 173 123 ASP N N 122.327 0.20 1 547 174 124 ALA H H 7.700 0.03 1 548 174 124 ALA C C 177.473 0.50 1 549 174 124 ALA CA C 53.963 0.50 1 550 174 124 ALA CB C 19.167 0.50 1 551 174 124 ALA N N 122.604 0.20 1 552 175 125 LEU H H 7.938 0.03 1 553 175 125 LEU C C 177.633 0.50 1 554 175 125 LEU CA C 54.585 0.50 1 555 175 125 LEU CB C 43.999 0.50 1 556 175 125 LEU N N 120.235 0.20 1 557 176 126 THR H H 8.493 0.03 1 558 176 126 THR C C 175.030 0.50 1 559 176 126 THR CA C 61.358 0.50 1 560 176 126 THR CB C 71.088 0.50 1 561 176 126 THR N N 111.980 0.20 1 562 177 127 ASP H H 8.606 0.03 1 563 177 127 ASP C C 177.633 0.50 1 564 177 127 ASP CA C 57.933 0.50 1 565 177 127 ASP CB C 41.041 0.50 1 566 177 127 ASP N N 120.374 0.20 1 567 178 128 GLN H H 8.368 0.03 1 568 178 128 GLN C C 179.716 0.50 1 569 178 128 GLN CA C 58.088 0.50 1 570 178 128 GLN CB C 28.741 0.50 1 571 178 128 GLN N N 117.313 0.20 1 572 179 129 GLU H H 7.796 0.03 1 573 179 129 GLU C C 179.996 0.50 1 574 179 129 GLU CA C 59.490 0.50 1 575 179 129 GLU CB C 30.532 0.50 1 576 179 129 GLU N N 118.079 0.20 1 577 180 130 ALA H H 8.414 0.03 1 578 180 130 ALA C C 178.454 0.50 1 579 180 130 ALA CA C 55.597 0.50 1 580 180 130 ALA CB C 19.011 0.50 1 581 180 130 ALA N N 121.622 0.20 1 582 181 131 ILE H H 8.179 0.03 1 583 181 131 ILE C C 178.114 0.50 1 584 181 131 ILE CA C 64.472 0.50 1 585 181 131 ILE CB C 38.550 0.50 1 586 181 131 ILE N N 117.978 0.20 1 587 182 132 ASP H H 8.546 0.03 1 588 182 132 ASP C C 179.616 0.50 1 589 182 132 ASP CA C 57.699 0.50 1 590 182 132 ASP CB C 39.873 0.50 1 591 182 132 ASP N N 120.774 0.20 1 592 183 133 ALA H H 8.130 0.03 1 593 183 133 ALA C C 180.877 0.50 1 594 183 133 ALA CA C 55.130 0.50 1 595 183 133 ALA CB C 18.077 0.50 1 596 183 133 ALA N N 122.969 0.20 1 597 184 134 LEU H H 8.251 0.03 1 598 184 134 LEU C C 178.514 0.50 1 599 184 134 LEU CA C 58.088 0.50 1 600 184 134 LEU CB C 41.975 0.50 1 601 184 134 LEU N N 118.984 0.20 1 602 185 135 ASN H H 8.596 0.03 1 603 185 135 ASN C C 177.153 0.50 1 604 185 135 ASN CA C 54.819 0.50 1 605 185 135 ASN CB C 37.382 0.50 1 606 185 135 ASN N N 116.583 0.20 1 607 186 136 ALA H H 7.946 0.03 1 608 186 136 ALA C C 178.554 0.50 1 609 186 136 ALA CA C 53.729 0.50 1 610 186 136 ALA CB C 18.077 0.50 1 611 186 136 ALA N N 121.249 0.20 1 612 187 137 PHE H H 7.651 0.03 1 613 187 137 PHE C C 175.811 0.50 1 614 187 137 PHE CA C 60.502 0.50 1 615 187 137 PHE CB C 41.041 0.50 1 616 187 137 PHE N N 118.029 0.20 1 617 188 138 SER H H 8.135 0.03 1 618 188 138 SER C C 179.195 0.50 1 619 188 138 SER CA C 57.621 0.50 1 620 188 138 SER CB C 65.483 0.50 1 621 188 138 SER N N 110.269 0.20 1 622 189 139 SER C C 174.770 0.50 1 623 189 139 SER CA C 59.334 0.50 1 624 189 139 SER CB C 63.615 0.50 1 625 190 140 GLU H H 8.370 0.03 1 626 190 140 GLU C C 175.571 0.50 1 627 190 140 GLU CA C 55.753 0.50 1 628 190 140 GLU CB C 30.765 0.50 1 629 190 140 GLU N N 122.485 0.20 1 630 191 141 ASP H H 8.233 0.03 1 631 191 141 ASP C C 175.491 0.50 1 632 191 141 ASP CA C 56.298 0.50 1 633 191 141 ASP CB C 42.598 0.50 1 634 191 141 ASP N N 117.157 0.20 1 635 192 142 ASN H H 7.472 0.03 1 636 192 142 ASN C C 174.109 0.50 1 637 192 142 ASN CA C 52.406 0.50 1 638 192 142 ASN CB C 39.328 0.50 1 639 192 142 ASN N N 114.184 0.20 1 640 193 143 ILE H H 9.405 0.03 1 641 193 143 ILE C C 174.810 0.50 1 642 193 143 ILE CA C 58.867 0.50 1 643 193 143 ILE CB C 38.939 0.50 1 644 193 143 ILE N N 124.914 0.20 1 645 194 144 ASP H H 8.696 0.03 1 646 194 144 ASP C C 175.491 0.50 1 647 194 144 ASP CA C 52.639 0.50 1 648 194 144 ASP CB C 40.262 0.50 1 649 194 144 ASP N N 127.294 0.20 1 650 195 145 TYR H H 6.899 0.03 1 651 195 145 TYR C C 176.812 0.50 1 652 195 145 TYR CA C 59.412 0.50 1 653 195 145 TYR CB C 36.759 0.50 1 654 195 145 TYR N N 124.922 0.20 1 655 196 146 LYS H H 8.024 0.03 1 656 196 146 LYS C C 178.334 0.50 1 657 196 146 LYS CA C 61.046 0.50 1 658 196 146 LYS CB C 31.544 0.50 1 659 196 146 LYS N N 126.106 0.20 1 660 197 147 LEU H H 7.581 0.03 1 661 197 147 LEU C C 179.335 0.50 1 662 197 147 LEU CA C 57.621 0.50 1 663 197 147 LEU CB C 41.819 0.50 1 664 197 147 LEU N N 120.441 0.20 1 665 198 148 PHE H H 8.240 0.03 1 666 198 148 PHE C C 176.913 0.50 1 667 198 148 PHE CA C 61.591 0.50 1 668 198 148 PHE CB C 39.172 0.50 1 669 198 148 PHE N N 119.815 0.20 1 670 199 149 CYS H H 7.955 0.03 1 671 199 149 CYS CA C 64.160 0.50 1 672 199 149 CYS CB C 27.496 0.50 1 673 199 149 CYS N N 116.111 0.20 1 674 200 150 GLU C C 177.834 0.50 1 675 200 150 GLU CA C 59.178 0.50 1 676 200 150 GLU CB C 29.909 0.50 1 677 201 151 ASP H H 8.007 0.03 1 678 201 151 ASP C C 177.733 0.50 1 679 201 151 ASP CA C 56.298 0.50 1 680 201 151 ASP CB C 41.975 0.50 1 681 201 151 ASP N N 117.023 0.20 1 682 202 152 ILE H H 7.644 0.03 1 683 202 152 ILE C C 176.893 0.50 1 684 202 152 ILE CA C 61.513 0.50 1 685 202 152 ILE CB C 37.538 0.50 1 686 202 152 ILE N N 115.906 0.20 1 687 203 153 LEU H H 7.175 0.03 1 688 203 153 LEU C C 176.172 0.50 1 689 203 153 LEU CA C 55.130 0.50 1 690 203 153 LEU CB C 42.053 0.50 1 691 203 153 LEU N N 119.520 0.20 1 692 204 154 GLN H H 7.340 0.03 1 693 204 154 GLN C C 180.557 0.50 1 694 204 154 GLN CA C 58.011 0.50 1 695 204 154 GLN CB C 30.454 0.50 1 696 204 154 GLN N N 123.613 0.20 1 stop_ save_