data_19719 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignments of the PHIST domain of P. falciparum protein PFI1780w ; _BMRB_accession_number 19719 _BMRB_flat_file_name bmr19719.str _Entry_type original _Submission_date 2014-01-07 _Accession_date 2014-01-09 _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 Vakonakis Ioannis . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 404 "13C chemical shifts" 419 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-05-24 original BMRB . stop_ _Original_release_date 2016-05-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24983468 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oberli Alexander . . 2 Slater Leanne M . 3 Cutts Erin . . 4 Brand Francoise . . 5 Mundwiler-Pachlatko Esther . . 6 Rusch Sebastian . . 7 Masik Martin FG . 8 Erat Michele C . 9 Beck Hans-Peter . . 10 Vakonakis Ioannis . . stop_ _Journal_abbreviation 'FASEB J.' _Journal_name_full 'FASEB journal' _Journal_volume 28 _Journal_issue 10 _Journal_ISSN 0892-6638 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4420 _Page_last 4433 _Year 2014 _Details . loop_ _Keyword 'Structural and functional analysis' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PFI1780w-PHIST _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PHIST $PFI1780w 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_PFI1780w _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PFI1780w _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Structural protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; GPLGSYTAEEINEMINSSNE FINRNDMNIIFSYVHESERE KFKKVEENIFKFIQSIVETY KIPDEYKMRKFKFAHFEMQG YALKQEKFLLEYAFLSLNGK LCERKKFKEVLEYVKREWIE FRKSMFDVWKEKLASEFREH GEMLNQKRKLKQHEL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 GLY 2 -4 PRO 3 -3 LEU 4 -2 GLY 5 -1 SER 6 98 TYR 7 99 THR 8 100 ALA 9 101 GLU 10 102 GLU 11 103 ILE 12 104 ASN 13 105 GLU 14 106 MET 15 107 ILE 16 108 ASN 17 109 SER 18 110 SER 19 111 ASN 20 112 GLU 21 113 PHE 22 114 ILE 23 115 ASN 24 116 ARG 25 117 ASN 26 118 ASP 27 119 MET 28 120 ASN 29 121 ILE 30 122 ILE 31 123 PHE 32 124 SER 33 125 TYR 34 126 VAL 35 127 HIS 36 128 GLU 37 129 SER 38 130 GLU 39 131 ARG 40 132 GLU 41 133 LYS 42 134 PHE 43 135 LYS 44 136 LYS 45 137 VAL 46 138 GLU 47 139 GLU 48 140 ASN 49 141 ILE 50 142 PHE 51 143 LYS 52 144 PHE 53 145 ILE 54 146 GLN 55 147 SER 56 148 ILE 57 149 VAL 58 150 GLU 59 151 THR 60 152 TYR 61 153 LYS 62 154 ILE 63 155 PRO 64 156 ASP 65 157 GLU 66 158 TYR 67 159 LYS 68 160 MET 69 161 ARG 70 162 LYS 71 163 PHE 72 164 LYS 73 165 PHE 74 166 ALA 75 167 HIS 76 168 PHE 77 169 GLU 78 170 MET 79 171 GLN 80 172 GLY 81 173 TYR 82 174 ALA 83 175 LEU 84 176 LYS 85 177 GLN 86 178 GLU 87 179 LYS 88 180 PHE 89 181 LEU 90 182 LEU 91 183 GLU 92 184 TYR 93 185 ALA 94 186 PHE 95 187 LEU 96 188 SER 97 189 LEU 98 190 ASN 99 191 GLY 100 192 LYS 101 193 LEU 102 194 CYS 103 195 GLU 104 196 ARG 105 197 LYS 106 198 LYS 107 199 PHE 108 200 LYS 109 201 GLU 110 202 VAL 111 203 LEU 112 204 GLU 113 205 TYR 114 206 VAL 115 207 LYS 116 208 ARG 117 209 GLU 118 210 TRP 119 211 ILE 120 212 GLU 121 213 PHE 122 214 ARG 123 215 LYS 124 216 SER 125 217 MET 126 218 PHE 127 219 ASP 128 220 VAL 129 221 TRP 130 222 LYS 131 223 GLU 132 224 LYS 133 225 LEU 134 226 ALA 135 227 SER 136 228 GLU 137 229 PHE 138 230 ARG 139 231 GLU 140 232 HIS 141 233 GLY 142 234 GLU 143 235 MET 144 236 LEU 145 237 ASN 146 238 GLN 147 239 LYS 148 240 ARG 149 241 LYS 150 242 LEU 151 243 LYS 152 244 GLN 153 245 HIS 154 246 GLU 155 247 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP Q8I2F2 . . . . . . 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 _Gene_mnemonic $PFI1780w 'malaria parasite P. falciparum' 5833 Eukaryota . Plasmodium falciparum 3D7 pfi1780w 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 $PFI1780w 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pGEX-6P-2 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 $PFI1780w 0.2 mM '[U-99% 13C; U-99% 15N]' D2O 5 '% v/v' 'natural abundance' H2O 95 '% v/v' 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 0.02 '% w/v' 'natural abundance' DTT 2 mM 'natural abundance' DSS 0.1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task '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 'Bruker console and inverse TCI cryoprobe installed in Oxford Instruments superconducting magnet' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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 'ionic strength' 110 . mM pH 7 . pH pressure 1 . atm temperature 310.15 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_ _Software_label $TOPSPIN $NMRPipe $PIPP stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HN(CO)CA' '3D HBHA(CO)NH' '3D HN(CA)CO' '3D HNCO' 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 PHIST _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 -4 2 PRO HA H 4.486 0.02 1 2 -4 2 PRO HB2 H 2.371 0.02 2 3 -4 2 PRO HB3 H 1.98 0.02 2 4 -4 2 PRO C C 177.18 0.1 1 5 -4 2 PRO CA C 63.86 0.1 1 6 -4 2 PRO CB C 32.42 0.1 1 7 -3 3 LEU H H 8.566 0.02 1 8 -3 3 LEU HA H 4.354 0.02 1 9 -3 3 LEU HB2 H 1.666 0.02 2 10 -3 3 LEU HB3 H 1.666 0.02 2 11 -3 3 LEU C C 177.76 0.1 1 12 -3 3 LEU CA C 55.9 0.1 1 13 -3 3 LEU CB C 41.82 0.1 1 14 -3 3 LEU N N 120.88 0.1 1 15 -2 4 GLY H H 8.137 0.02 1 16 -2 4 GLY HA2 H 3.972 0.02 2 17 -2 4 GLY HA3 H 3.972 0.02 2 18 -2 4 GLY C C 174.05 0.1 1 19 -2 4 GLY CA C 45.4 0.1 1 20 -2 4 GLY N N 107.9 0.1 1 21 -1 5 SER H H 7.86 0.02 1 22 -1 5 SER HA H 4.513 0.02 1 23 -1 5 SER HB2 H 3.738 0.02 2 24 -1 5 SER HB3 H 3.738 0.02 2 25 -1 5 SER C C 173.47 0.1 1 26 -1 5 SER CA C 58.2 0.1 1 27 -1 5 SER CB C 64.35 0.1 1 28 -1 5 SER N N 115.46 0.1 1 29 98 6 TYR H H 8.117 0.02 1 30 98 6 TYR HA H 4.83 0.02 1 31 98 6 TYR C C 176.18 0.1 1 32 98 6 TYR CA C 57.92 0.1 1 33 98 6 TYR CB C 41.34 0.1 1 34 98 6 TYR N N 121.15 0.1 1 35 99 7 THR H H 8.848 0.02 1 36 99 7 THR C C 175.07 0.1 1 37 99 7 THR CA C 60.12 0.1 1 38 99 7 THR CB C 71.61 0.1 1 39 99 7 THR N N 112.8 0.1 1 40 100 8 ALA H H 8.761 0.02 1 41 100 8 ALA HA H 3.731 0.02 1 42 100 8 ALA HB H 1.475 0.02 1 43 100 8 ALA C C 180.41 0.1 1 44 100 8 ALA CA C 55.52 0.1 1 45 100 8 ALA CB C 18.21 0.1 1 46 100 8 ALA N N 123.2 0.1 1 47 101 9 GLU H H 8.581 0.02 1 48 101 9 GLU HA H 4.009 0.02 1 49 101 9 GLU HB2 H 2.026 0.02 2 50 101 9 GLU HB3 H 2.026 0.02 2 51 101 9 GLU C C 179.27 0.1 1 52 101 9 GLU CA C 60.32 0.1 1 53 101 9 GLU CB C 29.12 0.1 1 54 101 9 GLU N N 116.92 0.1 1 55 102 10 GLU H H 7.774 0.02 1 56 102 10 GLU HA H 3.991 0.02 1 57 102 10 GLU C C 179.74 0.1 1 58 102 10 GLU CA C 59.36 0.1 1 59 102 10 GLU CB C 30.36 0.1 1 60 102 10 GLU N N 121.13 0.1 1 61 103 11 ILE H H 7.821 0.02 1 62 103 11 ILE HA H 3.612 0.02 1 63 103 11 ILE C C 178.33 0.1 1 64 103 11 ILE CA C 62.02 0.1 1 65 103 11 ILE N N 120.96 0.1 1 66 104 12 ASN H H 8.244 0.02 1 67 104 12 ASN HA H 4.345 0.02 1 68 104 12 ASN HB2 H 2.791 0.02 2 69 104 12 ASN HB3 H 2.791 0.02 2 70 104 12 ASN C C 177.85 0.1 1 71 104 12 ASN CA C 56.81 0.1 1 72 104 12 ASN CB C 38.21 0.1 1 73 104 12 ASN N N 118.87 0.1 1 74 105 13 GLU H H 7.913 0.02 1 75 105 13 GLU HA H 4.007 0.02 1 76 105 13 GLU HB2 H 2.099 0.02 2 77 105 13 GLU HB3 H 2.099 0.02 2 78 105 13 GLU C C 178.84 0.1 1 79 105 13 GLU CA C 59.12 0.1 1 80 105 13 GLU CB C 29.32 0.1 1 81 105 13 GLU N N 119.55 0.1 1 82 106 14 MET H H 7.625 0.02 1 83 106 14 MET HA H 4.045 0.02 1 84 106 14 MET C C 179.19 0.1 1 85 106 14 MET CA C 59.14 0.1 1 86 106 14 MET CB C 34.66 0.1 1 87 106 14 MET N N 118.3 0.1 1 88 107 15 ILE H H 8.196 0.02 1 89 107 15 ILE HA H 3.41 0.02 1 90 107 15 ILE C C 177.14 0.1 1 91 107 15 ILE CA C 66.33 0.1 1 92 107 15 ILE CB C 38.59 0.1 1 93 107 15 ILE N N 119.68 0.1 1 94 108 16 ASN H H 7.735 0.02 1 95 108 16 ASN HA H 4.729 0.02 1 96 108 16 ASN HB2 H 2.939 0.02 2 97 108 16 ASN HB3 H 2.611 0.02 2 98 108 16 ASN C C 174.21 0.1 1 99 108 16 ASN CA C 53.76 0.1 1 100 108 16 ASN CB C 38.81 0.1 1 101 108 16 ASN N N 114.49 0.1 1 102 109 17 SER H H 6.773 0.02 1 103 109 17 SER C C 174.75 0.1 1 104 109 17 SER CA C 58.51 0.1 1 105 109 17 SER CB C 63.97 0.1 1 106 109 17 SER N N 114.42 0.1 1 107 110 18 SER H H 8.421 0.02 1 108 110 18 SER HA H 4.333 0.02 1 109 110 18 SER HB2 H 3.997 0.02 2 110 110 18 SER HB3 H 3.997 0.02 2 111 110 18 SER C C 174.83 0.1 1 112 110 18 SER CA C 58.81 0.1 1 113 110 18 SER CB C 63.48 0.1 1 114 110 18 SER N N 119.4 0.1 1 115 111 19 ASN H H 8.009 0.02 1 116 111 19 ASN C C 176.48 0.1 1 117 111 19 ASN CA C 53.98 0.1 1 118 111 19 ASN CB C 38.6 0.1 1 119 111 19 ASN N N 122.64 0.1 1 120 112 20 GLU H H 8.972 0.02 1 121 112 20 GLU HA H 3.895 0.02 1 122 112 20 GLU HB2 H 1.697 0.02 2 123 112 20 GLU HB3 H 1.923 0.02 2 124 112 20 GLU C C 176.35 0.1 1 125 112 20 GLU CA C 59.38 0.1 1 126 112 20 GLU CB C 30.25 0.1 1 127 112 20 GLU N N 126.28 0.1 1 128 113 21 PHE H H 8.446 0.02 1 129 113 21 PHE HA H 5.392 0.02 1 130 113 21 PHE C C 174.46 0.1 1 131 113 21 PHE CA C 56.51 0.1 1 132 113 21 PHE CB C 42.68 0.1 1 133 113 21 PHE N N 116.93 0.1 1 134 114 22 ILE H H 9.359 0.02 1 135 114 22 ILE HA H 4.778 0.02 1 136 114 22 ILE C C 172.63 0.1 1 137 114 22 ILE CA C 58.97 0.1 1 138 114 22 ILE CB C 43.01 0.1 1 139 114 22 ILE N N 121.26 0.1 1 140 115 23 ASN H H 8.813 0.02 1 141 115 23 ASN C C 175.79 0.1 1 142 115 23 ASN CA C 51.9 0.1 1 143 115 23 ASN CB C 39.76 0.1 1 144 115 23 ASN N N 125.79 0.1 1 145 116 24 ARG H H 8.066 0.02 1 146 116 24 ARG HA H 4.002 0.02 1 147 116 24 ARG C C 177.52 0.1 1 148 116 24 ARG CA C 59.2 0.1 1 149 116 24 ARG CB C 29.99 0.1 1 150 116 24 ARG N N 119.39 0.1 1 151 117 25 ASN H H 8.393 0.02 1 152 117 25 ASN HA H 4.416 0.02 1 153 117 25 ASN HB2 H 2.77 0.02 2 154 117 25 ASN HB3 H 2.77 0.02 2 155 117 25 ASN C C 177.34 0.1 1 156 117 25 ASN CA C 57.07 0.1 1 157 117 25 ASN CB C 38.56 0.1 1 158 117 25 ASN N N 118.26 0.1 1 159 118 26 ASP H H 8.331 0.02 1 160 118 26 ASP HA H 4.288 0.02 1 161 118 26 ASP C C 178.58 0.1 1 162 118 26 ASP CA C 57.17 0.1 1 163 118 26 ASP CB C 39.29 0.1 1 164 118 26 ASP N N 120.54 0.1 1 165 119 27 MET H H 7.992 0.02 1 166 119 27 MET HA H 3.438 0.02 1 167 119 27 MET C C 177.37 0.1 1 168 119 27 MET CA C 60.78 0.1 1 169 119 27 MET N N 117.41 0.1 1 170 120 28 ASN H H 8.37 0.02 1 171 120 28 ASN HA H 3.876 0.02 1 172 120 28 ASN C C 178.96 0.1 1 173 120 28 ASN CA C 56.64 0.1 1 174 120 28 ASN CB C 38.26 0.1 1 175 120 28 ASN N N 116.73 0.1 1 176 121 29 ILE H H 7.992 0.02 1 177 121 29 ILE HA H 3.701 0.02 1 178 121 29 ILE C C 178.34 0.1 1 179 121 29 ILE CA C 65.48 0.1 1 180 121 29 ILE N N 122.73 0.1 1 181 122 30 ILE H H 8.146 0.02 1 182 122 30 ILE HA H 3.566 0.02 1 183 122 30 ILE C C 178.35 0.1 1 184 122 30 ILE CA C 66.29 0.1 1 185 122 30 ILE N N 119.72 0.1 1 186 123 31 PHE H H 9.098 0.02 1 187 123 31 PHE HA H 4.29 0.02 1 188 123 31 PHE C C 177.66 0.1 1 189 123 31 PHE CA C 62.11 0.1 1 190 123 31 PHE CB C 38.04 0.1 1 191 123 31 PHE N N 116.4 0.1 1 192 124 32 SER H H 8.359 0.02 1 193 124 32 SER C C 176.56 0.1 1 194 124 32 SER CA C 62.67 0.1 1 195 124 32 SER N N 114.18 0.1 1 196 125 33 TYR H H 8.095 0.02 1 197 125 33 TYR HA H 3.988 0.02 1 198 125 33 TYR C C 178.32 0.1 1 199 125 33 TYR CA C 62.21 0.1 1 200 125 33 TYR N N 123.47 0.1 1 201 126 34 VAL H H 8.764 0.02 1 202 126 34 VAL HA H 3.555 0.02 1 203 126 34 VAL C C 178.19 0.1 1 204 126 34 VAL CA C 66.86 0.1 1 205 126 34 VAL CB C 31.8 0.1 1 206 126 34 VAL N N 121.83 0.1 1 207 127 35 HIS H H 8.775 0.02 1 208 127 35 HIS HA H 4.255 0.02 1 209 127 35 HIS C C 178.16 0.1 1 210 127 35 HIS CA C 60.37 0.1 1 211 127 35 HIS N N 118.61 0.1 1 212 128 36 GLU H H 8.086 0.02 1 213 128 36 GLU HA H 3.945 0.02 1 214 128 36 GLU C C 179.26 0.1 1 215 128 36 GLU CA C 60.3 0.1 1 216 128 36 GLU CB C 29.37 0.1 1 217 128 36 GLU N N 119.33 0.1 1 218 129 37 SER H H 8.023 0.02 1 219 129 37 SER HA H 4.045 0.02 1 220 129 37 SER HB2 H 3.752 0.02 2 221 129 37 SER HB3 H 3.752 0.02 2 222 129 37 SER C C 177.86 0.1 1 223 129 37 SER CA C 61.41 0.1 1 224 129 37 SER CB C 62.82 0.1 1 225 129 37 SER N N 115.14 0.1 1 226 130 38 GLU H H 8.425 0.02 1 227 130 38 GLU HA H 3.729 0.02 1 228 130 38 GLU C C 180.16 0.1 1 229 130 38 GLU CA C 58.6 0.1 1 230 130 38 GLU N N 121.73 0.1 1 231 131 39 ARG H H 8.279 0.02 1 232 131 39 ARG HA H 3.798 0.02 1 233 131 39 ARG C C 180.32 0.1 1 234 131 39 ARG CA C 60.22 0.1 1 235 131 39 ARG CB C 29.78 0.1 1 236 131 39 ARG N N 122.06 0.1 1 237 132 40 GLU H H 7.783 0.02 1 238 132 40 GLU HA H 4.125 0.02 1 239 132 40 GLU HB2 H 2.154 0.02 2 240 132 40 GLU HB3 H 2.154 0.02 2 241 132 40 GLU C C 179.82 0.1 1 242 132 40 GLU CA C 59.62 0.1 1 243 132 40 GLU CB C 29.01 0.1 1 244 132 40 GLU N N 121.44 0.1 1 245 133 41 LYS H H 7.618 0.02 1 246 133 41 LYS HA H 4.03 0.02 1 247 133 41 LYS C C 179.83 0.1 1 248 133 41 LYS CA C 59.61 0.1 1 249 133 41 LYS N N 118.92 0.1 1 250 134 42 PHE H H 8.241 0.02 1 251 134 42 PHE HA H 3.392 0.02 1 252 134 42 PHE C C 176.35 0.1 1 253 134 42 PHE CA C 61.42 0.1 1 254 134 42 PHE CB C 38.44 0.1 1 255 134 42 PHE N N 120.47 0.1 1 256 135 43 LYS H H 7.701 0.02 1 257 135 43 LYS HA H 3.96 0.02 1 258 135 43 LYS HB2 H 1.98 0.02 2 259 135 43 LYS HB3 H 1.98 0.02 2 260 135 43 LYS C C 178.99 0.1 1 261 135 43 LYS CA C 60.07 0.1 1 262 135 43 LYS CB C 32.01 0.1 1 263 135 43 LYS N N 119.64 0.1 1 264 136 44 LYS H H 7.176 0.02 1 265 136 44 LYS HA H 4.051 0.02 1 266 136 44 LYS HB2 H 1.891 0.02 2 267 136 44 LYS HB3 H 1.891 0.02 2 268 136 44 LYS C C 178.54 0.1 1 269 136 44 LYS CA C 58.09 0.1 1 270 136 44 LYS CB C 31.61 0.1 1 271 136 44 LYS N N 117.05 0.1 1 272 137 45 VAL H H 7.152 0.02 1 273 137 45 VAL HA H 3.591 0.02 1 274 137 45 VAL C C 177.75 0.1 1 275 137 45 VAL CA C 66.54 0.1 1 276 137 45 VAL CB C 30.82 0.1 1 277 137 45 VAL N N 120.53 0.1 1 278 138 46 GLU H H 7.438 0.02 1 279 138 46 GLU HA H 3.165 0.02 1 280 138 46 GLU HB2 H 1.764 0.02 2 281 138 46 GLU HB3 H 1.764 0.02 2 282 138 46 GLU C C 176.91 0.1 1 283 138 46 GLU CA C 60.28 0.1 1 284 138 46 GLU CB C 29.53 0.1 1 285 138 46 GLU N N 118.2 0.1 1 286 139 47 GLU H H 7.696 0.02 1 287 139 47 GLU HA H 3.803 0.02 1 288 139 47 GLU HB2 H 2.081 0.02 2 289 139 47 GLU HB3 H 2.081 0.02 2 290 139 47 GLU C C 179.21 0.1 1 291 139 47 GLU CA C 59.67 0.1 1 292 139 47 GLU CB C 29.7 0.1 1 293 139 47 GLU N N 116.27 0.1 1 294 140 48 ASN H H 8.079 0.02 1 295 140 48 ASN HA H 4.59 0.02 1 296 140 48 ASN HB2 H 3.068 0.02 2 297 140 48 ASN HB3 H 2.83 0.02 2 298 140 48 ASN C C 179.17 0.1 1 299 140 48 ASN CA C 56.05 0.1 1 300 140 48 ASN CB C 38.09 0.1 1 301 140 48 ASN N N 118.48 0.1 1 302 141 49 ILE H H 8.398 0.02 1 303 141 49 ILE HA H 3.488 0.02 1 304 141 49 ILE C C 177.69 0.1 1 305 141 49 ILE CA C 66.75 0.1 1 306 141 49 ILE N N 123.82 0.1 1 307 142 50 PHE H H 8.396 0.02 1 308 142 50 PHE HA H 4.035 0.02 1 309 142 50 PHE C C 179.7 0.1 1 310 142 50 PHE CA C 61.12 0.1 1 311 142 50 PHE N N 118.09 0.1 1 312 143 51 LYS H H 8.117 0.02 1 313 143 51 LYS HA H 4.199 0.02 1 314 143 51 LYS HB2 H 2.044 0.02 2 315 143 51 LYS HB3 H 2.044 0.02 2 316 143 51 LYS C C 179.21 0.1 1 317 143 51 LYS CA C 59.78 0.1 1 318 143 51 LYS CB C 32.68 0.1 1 319 143 51 LYS N N 119.92 0.1 1 320 144 52 PHE H H 7.826 0.02 1 321 144 52 PHE HA H 4.456 0.02 1 322 144 52 PHE C C 178.37 0.1 1 323 144 52 PHE CA C 61.69 0.1 1 324 144 52 PHE CB C 38.9 0.1 1 325 144 52 PHE N N 121.08 0.1 1 326 145 53 ILE H H 8.457 0.02 1 327 145 53 ILE HA H 3.673 0.02 1 328 145 53 ILE C C 177.99 0.1 1 329 145 53 ILE CA C 61.25 0.1 1 330 145 53 ILE N N 118.66 0.1 1 331 146 54 GLN H H 8.376 0.02 1 332 146 54 GLN HA H 4.015 0.02 1 333 146 54 GLN C C 177.25 0.1 1 334 146 54 GLN CA C 58.72 0.1 1 335 146 54 GLN CB C 27.39 0.1 1 336 146 54 GLN N N 122.11 0.1 1 337 147 55 SER H H 7.499 0.02 1 338 147 55 SER HA H 3.941 0.02 1 339 147 55 SER C C 176.78 0.1 1 340 147 55 SER CA C 62.04 0.1 1 341 147 55 SER N N 113.25 0.1 1 342 148 56 ILE H H 7.377 0.02 1 343 148 56 ILE HA H 3.936 0.02 1 344 148 56 ILE C C 178.24 0.1 1 345 148 56 ILE CA C 65.19 0.1 1 346 148 56 ILE N N 125.36 0.1 1 347 149 57 VAL H H 8.009 0.02 1 348 149 57 VAL HA H 3.697 0.02 1 349 149 57 VAL C C 178.49 0.1 1 350 149 57 VAL CA C 66.88 0.1 1 351 149 57 VAL N N 120.36 0.1 1 352 150 58 GLU H H 8.152 0.02 1 353 150 58 GLU HA H 4.212 0.02 1 354 150 58 GLU HB2 H 2.129 0.02 2 355 150 58 GLU HB3 H 2.129 0.02 2 356 150 58 GLU C C 179.41 0.1 1 357 150 58 GLU CA C 59.12 0.1 1 358 150 58 GLU CB C 29.53 0.1 1 359 150 58 GLU N N 117.19 0.1 1 360 151 59 THR H H 7.929 0.02 1 361 151 59 THR HA H 4.149 0.02 1 362 151 59 THR HB H 3.834 0.02 1 363 151 59 THR C C 175.69 0.1 1 364 151 59 THR CA C 66.88 0.1 1 365 151 59 THR CB C 69.04 0.1 1 366 151 59 THR N N 117.08 0.1 1 367 152 60 TYR H H 7.661 0.02 1 368 152 60 TYR C C 173.8 0.1 1 369 152 60 TYR CA C 59.19 0.1 1 370 152 60 TYR N N 115.44 0.1 1 371 153 61 LYS H H 7.929 0.02 1 372 153 61 LYS HA H 4.029 0.02 1 373 153 61 LYS HB2 H 1.877 0.02 2 374 153 61 LYS HB3 H 1.877 0.02 2 375 153 61 LYS C C 176.63 0.1 1 376 153 61 LYS CA C 56.78 0.1 1 377 153 61 LYS CB C 29.01 0.1 1 378 153 61 LYS N N 119.77 0.1 1 379 154 62 ILE H H 8.102 0.02 1 380 154 62 ILE C C 174.03 0.1 1 381 154 62 ILE CA C 59.63 0.1 1 382 154 62 ILE N N 121.8 0.1 1 383 155 63 PRO HA H 4.484 0.02 1 384 155 63 PRO C C 177.23 0.1 1 385 155 63 PRO CA C 63.2 0.1 1 386 155 63 PRO CB C 33.17 0.1 1 387 156 64 ASP H H 8.729 0.02 1 388 156 64 ASP HA H 4.315 0.02 1 389 156 64 ASP HB2 H 2.647 0.02 2 390 156 64 ASP HB3 H 2.647 0.02 2 391 156 64 ASP C C 178.04 0.1 1 392 156 64 ASP CA C 57.81 0.1 1 393 156 64 ASP CB C 40.8 0.1 1 394 156 64 ASP N N 123.14 0.1 1 395 157 65 GLU H H 8.974 0.02 1 396 157 65 GLU HA H 3.987 0.02 1 397 157 65 GLU C C 178.34 0.1 1 398 157 65 GLU CA C 60.32 0.1 1 399 157 65 GLU CB C 28.72 0.1 1 400 157 65 GLU N N 117.95 0.1 1 401 158 66 TYR H H 6.839 0.02 1 402 158 66 TYR HA H 3.876 0.02 1 403 158 66 TYR C C 176.35 0.1 1 404 158 66 TYR CA C 61.36 0.1 1 405 158 66 TYR CB C 38.45 0.1 1 406 158 66 TYR N N 119.22 0.1 1 407 159 67 LYS H H 7.476 0.02 1 408 159 67 LYS HA H 3.587 0.02 1 409 159 67 LYS C C 176.82 0.1 1 410 159 67 LYS CA C 59.82 0.1 1 411 159 67 LYS CB C 32.87 0.1 1 412 159 67 LYS N N 118.29 0.1 1 413 160 68 MET H H 8.725 0.02 1 414 160 68 MET HA H 4.043 0.02 1 415 160 68 MET HB2 H 2.013 0.02 2 416 160 68 MET HB3 H 2.013 0.02 2 417 160 68 MET C C 179.27 0.1 1 418 160 68 MET CA C 58 0.1 1 419 160 68 MET CB C 31.27 0.1 1 420 160 68 MET N N 114.21 0.1 1 421 161 69 ARG H H 7.413 0.02 1 422 161 69 ARG HA H 4.048 0.02 1 423 161 69 ARG C C 179.15 0.1 1 424 161 69 ARG CA C 59.68 0.1 1 425 161 69 ARG CB C 30.06 0.1 1 426 161 69 ARG N N 119.9 0.1 1 427 162 70 LYS H H 7.87 0.02 1 428 162 70 LYS HA H 4.192 0.02 1 429 162 70 LYS C C 180.32 0.1 1 430 162 70 LYS CA C 57.48 0.1 1 431 162 70 LYS CB C 31.41 0.1 1 432 162 70 LYS N N 118.14 0.1 1 433 163 71 PHE H H 9.052 0.02 1 434 163 71 PHE C C 178.36 0.1 1 435 163 71 PHE CA C 58.1 0.1 1 436 163 71 PHE CB C 36.24 0.1 1 437 163 71 PHE N N 120.36 0.1 1 438 164 72 LYS H H 8.119 0.02 1 439 164 72 LYS C C 178.73 0.1 1 440 164 72 LYS CA C 57.92 0.1 1 441 164 72 LYS N N 121.19 0.1 1 442 165 73 PHE HA H 4.515 0.02 1 443 165 73 PHE HB2 H 3.391 0.02 2 444 165 73 PHE HB3 H 3.391 0.02 2 445 165 73 PHE C C 178.13 0.1 1 446 165 73 PHE CA C 61.26 0.1 1 447 165 73 PHE CB C 38.88 0.1 1 448 166 74 ALA H H 8.727 0.02 1 449 166 74 ALA HA H 4.215 0.02 1 450 166 74 ALA HB H 1.89 0.02 1 451 166 74 ALA C C 178.76 0.1 1 452 166 74 ALA CA C 55.27 0.1 1 453 166 74 ALA CB C 19.13 0.1 1 454 166 74 ALA N N 121.57 0.1 1 455 167 75 HIS H H 8.785 0.02 1 456 167 75 HIS HA H 4.379 0.02 1 457 167 75 HIS C C 176.82 0.1 1 458 167 75 HIS CA C 59.67 0.1 1 459 167 75 HIS CB C 29.15 0.1 1 460 167 75 HIS N N 117.23 0.1 1 461 168 76 PHE H H 7.854 0.02 1 462 168 76 PHE HA H 4.032 0.02 1 463 168 76 PHE HB2 H 3.229 0.02 2 464 168 76 PHE HB3 H 3.229 0.02 2 465 168 76 PHE C C 179.19 0.1 1 466 168 76 PHE CA C 61.59 0.1 1 467 168 76 PHE CB C 38.44 0.1 1 468 168 76 PHE N N 117.36 0.1 1 469 169 77 GLU H H 8.322 0.02 1 470 169 77 GLU HA H 4.016 0.02 1 471 169 77 GLU C C 179.86 0.1 1 472 169 77 GLU CA C 59.74 0.1 1 473 169 77 GLU CB C 30.58 0.1 1 474 169 77 GLU N N 121.19 0.1 1 475 170 78 MET H H 8.781 0.02 1 476 170 78 MET HA H 3.614 0.02 1 477 170 78 MET C C 178.68 0.1 1 478 170 78 MET CA C 61.35 0.1 1 479 170 78 MET N N 119.03 0.1 1 480 171 79 GLN H H 8.302 0.02 1 481 171 79 GLN HA H 3.883 0.02 1 482 171 79 GLN C C 178.63 0.1 1 483 171 79 GLN CA C 58.85 0.1 1 484 171 79 GLN CB C 28.53 0.1 1 485 171 79 GLN N N 117.58 0.1 1 486 172 80 GLY H H 7.763 0.02 1 487 172 80 GLY C C 177.3 0.1 1 488 172 80 GLY CA C 47.35 0.1 1 489 172 80 GLY N N 107.23 0.1 1 490 173 81 TYR H H 7.846 0.02 1 491 173 81 TYR HA H 4.343 0.02 1 492 173 81 TYR C C 178.71 0.1 1 493 173 81 TYR CA C 62.21 0.1 1 494 173 81 TYR CB C 38.08 0.1 1 495 173 81 TYR N N 121.24 0.1 1 496 174 82 ALA H H 8.248 0.02 1 497 174 82 ALA HA H 3.924 0.02 1 498 174 82 ALA HB H 1.266 0.02 1 499 174 82 ALA C C 179.45 0.1 1 500 174 82 ALA CA C 55.62 0.1 1 501 174 82 ALA CB C 17.19 0.1 1 502 174 82 ALA N N 123.96 0.1 1 503 175 83 LEU H H 8.342 0.02 1 504 175 83 LEU HA H 4.125 0.02 1 505 175 83 LEU C C 179.77 0.1 1 506 175 83 LEU CA C 58.1 0.1 1 507 175 83 LEU CB C 41.51 0.1 1 508 175 83 LEU N N 119.93 0.1 1 509 176 84 LYS H H 7.624 0.02 1 510 176 84 LYS HA H 3.999 0.02 1 511 176 84 LYS C C 178.71 0.1 1 512 176 84 LYS CA C 59.74 0.1 1 513 176 84 LYS CB C 29.13 0.1 1 514 176 84 LYS N N 119.76 0.1 1 515 177 85 GLN H H 8.417 0.02 1 516 177 85 GLN C C 178.86 0.1 1 517 177 85 GLN CA C 58.69 0.1 1 518 177 85 GLN N N 119.61 0.1 1 519 178 86 GLU H H 7.963 0.02 1 520 178 86 GLU HA H 3.881 0.02 1 521 178 86 GLU C C 178.8 0.1 1 522 178 86 GLU CA C 59.62 0.1 1 523 178 86 GLU N N 119.8 0.1 1 524 179 87 LYS H H 8.066 0.02 1 525 179 87 LYS HA H 4.097 0.02 1 526 179 87 LYS HB2 H 1.994 0.02 2 527 179 87 LYS HB3 H 1.994 0.02 2 528 179 87 LYS C C 178.74 0.1 1 529 179 87 LYS CA C 60.27 0.1 1 530 179 87 LYS N N 119.39 0.1 1 531 180 88 PHE H H 7.863 0.02 1 532 180 88 PHE C C 178.14 0.1 1 533 180 88 PHE CA C 61.41 0.1 1 534 180 88 PHE N N 118.16 0.1 1 535 181 89 LEU C C 180.55 0.1 1 536 181 89 LEU CA C 57.36 0.1 1 537 182 90 LEU H H 8.5 0.02 1 538 182 90 LEU CA C 58.18 0.1 1 539 182 90 LEU N N 123.33 0.1 1 540 184 92 TYR HA H 3.799 0.02 1 541 184 92 TYR C C 178.66 0.1 1 542 184 92 TYR CA C 61.65 0.1 1 543 184 92 TYR CB C 38.5 0.1 1 544 185 93 ALA H H 7.879 0.02 1 545 185 93 ALA HA H 3.645 0.02 1 546 185 93 ALA HB H 0.959 0.02 1 547 185 93 ALA C C 178.59 0.1 1 548 185 93 ALA CA C 55.29 0.1 1 549 185 93 ALA CB C 18.57 0.1 1 550 185 93 ALA N N 121.35 0.1 1 551 186 94 PHE H H 7.883 0.02 1 552 186 94 PHE HA H 4.397 0.02 1 553 186 94 PHE C C 177.64 0.1 1 554 186 94 PHE CA C 60.52 0.1 1 555 186 94 PHE CB C 38.27 0.1 1 556 186 94 PHE N N 115.51 0.1 1 557 187 95 LEU H H 7.926 0.02 1 558 187 95 LEU HA H 4.107 0.02 1 559 187 95 LEU C C 179.2 0.1 1 560 187 95 LEU CA C 57.3 0.1 1 561 187 95 LEU CB C 42.08 0.1 1 562 187 95 LEU N N 119.15 0.1 1 563 188 96 SER H H 7.334 0.02 1 564 188 96 SER HA H 4.241 0.02 1 565 188 96 SER HB2 H 3.602 0.02 2 566 188 96 SER HB3 H 3.602 0.02 2 567 188 96 SER C C 174.42 0.1 1 568 188 96 SER CA C 60.65 0.1 1 569 188 96 SER CB C 64.32 0.1 1 570 188 96 SER N N 112.23 0.1 1 571 189 97 LEU H H 7.688 0.02 1 572 189 97 LEU HA H 4.662 0.02 1 573 189 97 LEU C C 175.33 0.1 1 574 189 97 LEU CA C 53.5 0.1 1 575 189 97 LEU CB C 43.24 0.1 1 576 189 97 LEU N N 122.14 0.1 1 577 190 98 ASN H H 7.818 0.02 1 578 190 98 ASN HA H 4.658 0.02 1 579 190 98 ASN HB2 H 2.751 0.02 2 580 190 98 ASN HB3 H 2.751 0.02 2 581 190 98 ASN C C 175.46 0.1 1 582 190 98 ASN CA C 53.67 0.1 1 583 190 98 ASN CB C 39.67 0.1 1 584 190 98 ASN N N 118.85 0.1 1 585 191 99 GLY H H 7.985 0.02 1 586 191 99 GLY C C 173.72 0.1 1 587 191 99 GLY CA C 44.7 0.1 1 588 191 99 GLY N N 109.03 0.1 1 589 192 100 LYS H H 9.485 0.02 1 590 192 100 LYS HA H 4.097 0.02 1 591 192 100 LYS HB2 H 1.828 0.02 2 592 192 100 LYS HB3 H 1.828 0.02 2 593 192 100 LYS C C 176.44 0.1 1 594 192 100 LYS CB C 33.08 0.1 1 595 192 100 LYS N N 125.87 0.1 1 596 193 101 LEU H H 7.637 0.02 1 597 193 101 LEU HA H 4.726 0.02 1 598 193 101 LEU HB2 H 1.4 0.02 2 599 193 101 LEU HB3 H 1.4 0.02 2 600 193 101 LEU C C 175.99 0.1 1 601 193 101 LEU CA C 54.41 0.1 1 602 193 101 LEU CB C 44.7 0.1 1 603 193 101 LEU N N 118.33 0.1 1 604 194 102 CYS H H 8.833 0.02 1 605 194 102 CYS HA H 4.887 0.02 1 606 194 102 CYS HB2 H 2.727 0.02 2 607 194 102 CYS HB3 H 2.727 0.02 2 608 194 102 CYS C C 173.99 0.1 1 609 194 102 CYS CA C 57.74 0.1 1 610 194 102 CYS CB C 30.98 0.1 1 611 194 102 CYS N N 120.85 0.1 1 612 195 103 GLU H H 9.456 0.02 1 613 195 103 GLU C C 177.61 0.1 1 614 195 103 GLU CA C 57.9 0.1 1 615 195 103 GLU N N 125.9 0.1 1 616 196 104 ARG H H 9.274 0.02 1 617 196 104 ARG HA H 3.894 0.02 1 618 196 104 ARG C C 177.91 0.1 1 619 196 104 ARG CA C 60.75 0.1 1 620 196 104 ARG N N 130.54 0.1 1 621 197 105 LYS H H 8.948 0.02 1 622 197 105 LYS HA H 4.046 0.02 1 623 197 105 LYS HB2 H 1.948 0.02 2 624 197 105 LYS HB3 H 1.948 0.02 2 625 197 105 LYS C C 178.61 0.1 1 626 197 105 LYS CA C 60.29 0.1 1 627 197 105 LYS CB C 32.49 0.1 1 628 197 105 LYS N N 118.07 0.1 1 629 198 106 LYS H H 6.813 0.02 1 630 198 106 LYS HB2 H 2.01 0.02 2 631 198 106 LYS HB3 H 2.01 0.02 2 632 198 106 LYS C C 178.58 0.1 1 633 198 106 LYS CA C 58.33 0.1 1 634 198 106 LYS CB C 32.25 0.1 1 635 198 106 LYS N N 119.23 0.1 1 636 199 107 PHE H H 8.059 0.02 1 637 199 107 PHE HA H 4.318 0.02 1 638 199 107 PHE C C 176.17 0.1 1 639 199 107 PHE CA C 61.29 0.1 1 640 199 107 PHE CB C 38.92 0.1 1 641 199 107 PHE N N 119.97 0.1 1 642 200 108 LYS H H 8.652 0.02 1 643 200 108 LYS HA H 3.457 0.02 1 644 200 108 LYS HB2 H 1.894 0.02 2 645 200 108 LYS HB3 H 1.894 0.02 2 646 200 108 LYS C C 178.56 0.1 1 647 200 108 LYS CA C 60.59 0.1 1 648 200 108 LYS CB C 32.23 0.1 1 649 200 108 LYS N N 118.99 0.1 1 650 201 109 GLU H H 7.47 0.02 1 651 201 109 GLU HA H 4.121 0.02 1 652 201 109 GLU C C 179.89 0.1 1 653 201 109 GLU CA C 59.76 0.1 1 654 201 109 GLU CB C 29.75 0.1 1 655 201 109 GLU N N 119.3 0.1 1 656 202 110 VAL H H 8.041 0.02 1 657 202 110 VAL HA H 4.187 0.02 1 658 202 110 VAL C C 177.81 0.1 1 659 202 110 VAL CA C 66.46 0.1 1 660 202 110 VAL N N 122.26 0.1 1 661 203 111 LEU H H 8.772 0.02 1 662 203 111 LEU HA H 4.05 0.02 1 663 203 111 LEU C C 178.36 0.1 1 664 203 111 LEU CA C 58.49 0.1 1 665 203 111 LEU CB C 41.27 0.1 1 666 203 111 LEU N N 121.75 0.1 1 667 204 112 GLU H H 8.119 0.02 1 668 204 112 GLU HA H 4.044 0.02 1 669 204 112 GLU HB2 H 2.144 0.02 2 670 204 112 GLU HB3 H 2.144 0.02 2 671 204 112 GLU C C 179.12 0.1 1 672 204 112 GLU CA C 59.42 0.1 1 673 204 112 GLU CB C 29.05 0.1 1 674 204 112 GLU N N 117.24 0.1 1 675 205 113 TYR H H 7.865 0.02 1 676 205 113 TYR HA H 4.208 0.02 1 677 205 113 TYR C C 177.08 0.1 1 678 205 113 TYR CA C 61.94 0.1 1 679 205 113 TYR CB C 38.22 0.1 1 680 205 113 TYR N N 122 0.1 1 681 206 114 VAL H H 8.777 0.02 1 682 206 114 VAL HA H 3.606 0.02 1 683 206 114 VAL C C 177.49 0.1 1 684 206 114 VAL CA C 66.75 0.1 1 685 206 114 VAL N N 119.02 0.1 1 686 207 115 LYS H H 8.224 0.02 1 687 207 115 LYS HA H 4.148 0.02 1 688 207 115 LYS C C 179.13 0.1 1 689 207 115 LYS CA C 58.53 0.1 1 690 207 115 LYS CB C 36.26 0.1 1 691 207 115 LYS N N 119 0.1 1 692 208 116 ARG H H 8.509 0.02 1 693 208 116 ARG HA H 4.068 0.02 1 694 208 116 ARG HB2 H 1.971 0.02 2 695 208 116 ARG HB3 H 1.971 0.02 2 696 208 116 ARG C C 179.24 0.1 1 697 208 116 ARG CA C 59.92 0.1 1 698 208 116 ARG CB C 29.73 0.1 1 699 208 116 ARG N N 120.64 0.1 1 700 209 117 GLU H H 8.474 0.02 1 701 209 117 GLU HA H 3.899 0.02 1 702 209 117 GLU C C 180.82 0.1 1 703 209 117 GLU CA C 58.8 0.1 1 704 209 117 GLU N N 119.85 0.1 1 705 210 118 TRP H H 8.241 0.02 1 706 210 118 TRP C C 179.2 0.1 1 707 210 118 TRP CA C 61.44 0.1 1 708 210 118 TRP CB C 30.39 0.1 1 709 210 118 TRP N N 121.27 0.1 1 710 211 119 ILE H H 7.768 0.02 1 711 211 119 ILE HA H 3.722 0.02 1 712 211 119 ILE C C 179.22 0.1 1 713 211 119 ILE CA C 66.45 0.1 1 714 211 119 ILE N N 120.27 0.1 1 715 212 120 GLU H H 8.13 0.02 1 716 212 120 GLU HA H 4.114 0.02 1 717 212 120 GLU C C 179.19 0.1 1 718 212 120 GLU CA C 59.09 0.1 1 719 212 120 GLU CB C 29.14 0.1 1 720 212 120 GLU N N 119.46 0.1 1 721 213 121 PHE H H 8.563 0.02 1 722 213 121 PHE HA H 4.328 0.02 1 723 213 121 PHE C C 177.1 0.1 1 724 213 121 PHE CA C 61.4 0.1 1 725 213 121 PHE CB C 39.49 0.1 1 726 213 121 PHE N N 121.88 0.1 1 727 214 122 ARG H H 8.569 0.02 1 728 214 122 ARG HA H 3.827 0.02 1 729 214 122 ARG C C 178.54 0.1 1 730 214 122 ARG CA C 62.1 0.1 1 731 214 122 ARG N N 118.49 0.1 1 732 215 123 LYS H H 7.979 0.02 1 733 215 123 LYS HA H 4.089 0.02 1 734 215 123 LYS HB2 H 1.98 0.02 2 735 215 123 LYS HB3 H 1.98 0.02 2 736 215 123 LYS C C 178.54 0.1 1 737 215 123 LYS CA C 59.93 0.1 1 738 215 123 LYS CB C 32.71 0.1 1 739 215 123 LYS N N 119.58 0.1 1 740 216 124 SER H H 8.334 0.02 1 741 216 124 SER HA H 3.944 0.02 1 742 216 124 SER HB2 H 4.325 0.02 2 743 216 124 SER HB3 H 4.325 0.02 2 744 216 124 SER C C 176.83 0.1 1 745 216 124 SER CA C 61.58 0.1 1 746 216 124 SER CB C 63.03 0.1 1 747 216 124 SER N N 114.7 0.1 1 748 217 125 MET H H 8.47 0.02 1 749 217 125 MET HA H 4.364 0.02 1 750 217 125 MET C C 178.39 0.1 1 751 217 125 MET CA C 57.48 0.1 1 752 217 125 MET CB C 32.22 0.1 1 753 217 125 MET N N 118.47 0.1 1 754 218 126 PHE H H 7.823 0.02 1 755 218 126 PHE HA H 4.096 0.02 1 756 218 126 PHE HB2 H 3.282 0.02 2 757 218 126 PHE HB3 H 3.282 0.02 2 758 218 126 PHE C C 175.8 0.1 1 759 218 126 PHE CA C 61.69 0.1 1 760 218 126 PHE CB C 39.05 0.1 1 761 218 126 PHE N N 117.96 0.1 1 762 219 127 ASP H H 7.688 0.02 1 763 219 127 ASP HA H 4.144 0.02 1 764 219 127 ASP HB2 H 2.718 0.02 2 765 219 127 ASP HB3 H 2.718 0.02 2 766 219 127 ASP C C 179.45 0.1 1 767 219 127 ASP CA C 57.9 0.1 1 768 219 127 ASP CB C 40.72 0.1 1 769 219 127 ASP N N 117 0.1 1 770 220 128 VAL H H 8.417 0.02 1 771 220 128 VAL HA H 3.613 0.02 1 772 220 128 VAL C C 179.39 0.1 1 773 220 128 VAL CA C 66.22 0.1 1 774 220 128 VAL N N 118.32 0.1 1 775 221 129 TRP H H 8.673 0.02 1 776 221 129 TRP HA H 4.033 0.02 1 777 221 129 TRP C C 178.53 0.1 1 778 221 129 TRP CA C 62.66 0.1 1 779 221 129 TRP CB C 28.68 0.1 1 780 221 129 TRP N N 119.99 0.1 1 781 222 130 LYS H H 8.329 0.02 1 782 222 130 LYS HA H 3.893 0.02 1 783 222 130 LYS HB2 H 1.296 0.02 2 784 222 130 LYS HB3 H 1.296 0.02 2 785 222 130 LYS C C 177.51 0.1 1 786 222 130 LYS CA C 61.05 0.1 1 787 222 130 LYS CB C 31.27 0.1 1 788 222 130 LYS N N 119.94 0.1 1 789 223 131 GLU H H 6.913 0.02 1 790 223 131 GLU HA H 4.165 0.02 1 791 223 131 GLU HB2 H 2.018 0.02 2 792 223 131 GLU HB3 H 2.018 0.02 2 793 223 131 GLU C C 179.22 0.1 1 794 223 131 GLU CA C 58.84 0.1 1 795 223 131 GLU CB C 29.37 0.1 1 796 223 131 GLU N N 116.09 0.1 1 797 224 132 LYS H H 8.137 0.02 1 798 224 132 LYS HA H 4.034 0.02 1 799 224 132 LYS HB2 H 1.559 0.02 2 800 224 132 LYS HB3 H 1.559 0.02 2 801 224 132 LYS C C 179.38 0.1 1 802 224 132 LYS CA C 59.79 0.1 1 803 224 132 LYS CB C 33.52 0.1 1 804 224 132 LYS N N 120.64 0.1 1 805 225 133 LEU H H 8.386 0.02 1 806 225 133 LEU HA H 4.504 0.02 1 807 225 133 LEU HB2 H 1.54 0.02 2 808 225 133 LEU HB3 H 1.54 0.02 2 809 225 133 LEU C C 179.14 0.1 1 810 225 133 LEU CA C 57.95 0.1 1 811 225 133 LEU CB C 42.51 0.1 1 812 225 133 LEU N N 116.84 0.1 1 813 226 134 ALA H H 8.649 0.02 1 814 226 134 ALA HA H 4.042 0.02 1 815 226 134 ALA HB H 1.687 0.02 1 816 226 134 ALA C C 179.91 0.1 1 817 226 134 ALA CA C 56.65 0.1 1 818 226 134 ALA CB C 18.56 0.1 1 819 226 134 ALA N N 122.55 0.1 1 820 227 135 SER H H 8.156 0.02 1 821 227 135 SER HA H 4.271 0.02 1 822 227 135 SER HB2 H 4.113 0.02 2 823 227 135 SER HB3 H 4.113 0.02 2 824 227 135 SER C C 177.14 0.1 1 825 227 135 SER CA C 62.07 0.1 1 826 227 135 SER CB C 62.94 0.1 1 827 227 135 SER N N 112.31 0.1 1 828 228 136 GLU H H 7.868 0.02 1 829 228 136 GLU HA H 4.223 0.02 1 830 228 136 GLU C C 179.83 0.1 1 831 228 136 GLU CA C 60.02 0.1 1 832 228 136 GLU CB C 30 0.1 1 833 228 136 GLU N N 121.56 0.1 1 834 229 137 PHE H H 9.207 0.02 1 835 229 137 PHE HA H 4.283 0.02 1 836 229 137 PHE C C 177.97 0.1 1 837 229 137 PHE CA C 62.41 0.1 1 838 229 137 PHE CB C 39.05 0.1 1 839 229 137 PHE N N 119.09 0.1 1 840 230 138 ARG H H 8.728 0.02 1 841 230 138 ARG HA H 3.643 0.02 1 842 230 138 ARG HB2 H 2.004 0.02 2 843 230 138 ARG HB3 H 2.004 0.02 2 844 230 138 ARG C C 177.65 0.1 1 845 230 138 ARG CA C 60.48 0.1 1 846 230 138 ARG CB C 30 0.1 1 847 230 138 ARG N N 119.62 0.1 1 848 231 139 GLU H H 7.941 0.02 1 849 231 139 GLU HA H 3.945 0.02 1 850 231 139 GLU HB2 H 2.162 0.02 2 851 231 139 GLU HB3 H 2.162 0.02 2 852 231 139 GLU C C 179.3 0.1 1 853 231 139 GLU CA C 59.85 0.1 1 854 231 139 GLU CB C 29.44 0.1 1 855 231 139 GLU N N 118.23 0.1 1 856 232 140 HIS H H 7.909 0.02 1 857 232 140 HIS HA H 4.164 0.02 1 858 232 140 HIS C C 177.43 0.1 1 859 232 140 HIS CA C 60.04 0.1 1 860 232 140 HIS CB C 30.25 0.1 1 861 232 140 HIS N N 119.63 0.1 1 862 233 141 GLY H H 8.556 0.02 1 863 233 141 GLY HA2 H 3.278 0.02 2 864 233 141 GLY HA3 H 3.278 0.02 2 865 233 141 GLY C C 175.54 0.1 1 866 233 141 GLY CA C 47.23 0.1 1 867 233 141 GLY N N 105.96 0.1 1 868 234 142 GLU H H 8.364 0.02 1 869 234 142 GLU HA H 3.998 0.02 1 870 234 142 GLU HB2 H 2.033 0.02 2 871 234 142 GLU HB3 H 2.033 0.02 2 872 234 142 GLU C C 179.6 0.1 1 873 234 142 GLU CA C 59.47 0.1 1 874 234 142 GLU CB C 29.13 0.1 1 875 234 142 GLU N N 121.15 0.1 1 876 235 143 MET H H 7.61 0.02 1 877 235 143 MET HA H 4.106 0.02 1 878 235 143 MET HB2 H 2.154 0.02 2 879 235 143 MET HB3 H 2.154 0.02 2 880 235 143 MET C C 179.28 0.1 1 881 235 143 MET CA C 59.06 0.1 1 882 235 143 MET CB C 30.94 0.1 1 883 235 143 MET N N 121.12 0.1 1 884 236 144 LEU H H 8.243 0.02 1 885 236 144 LEU HA H 3.865 0.02 1 886 236 144 LEU C C 179.91 0.1 1 887 236 144 LEU CA C 57.78 0.1 1 888 236 144 LEU CB C 41.3 0.1 1 889 236 144 LEU N N 120.75 0.1 1 890 237 145 ASN H H 8.26 0.02 1 891 237 145 ASN HA H 4.521 0.02 1 892 237 145 ASN HB2 H 2.98 0.02 2 893 237 145 ASN HB3 H 2.98 0.02 2 894 237 145 ASN C C 177.7 0.1 1 895 237 145 ASN CA C 55.57 0.1 1 896 237 145 ASN CB C 39.99 0.1 1 897 237 145 ASN N N 117.79 0.1 1 898 238 146 GLN H H 7.92 0.02 1 899 238 146 GLN HA H 4.138 0.02 1 900 238 146 GLN HB2 H 2.229 0.02 2 901 238 146 GLN HB3 H 2.229 0.02 2 902 238 146 GLN C C 178.2 0.1 1 903 238 146 GLN CA C 58.66 0.1 1 904 238 146 GLN CB C 28.39 0.1 1 905 238 146 GLN N N 119.65 0.1 1 906 239 147 LYS H H 7.997 0.02 1 907 239 147 LYS HA H 4.116 0.02 1 908 239 147 LYS HB2 H 1.937 0.02 2 909 239 147 LYS HB3 H 1.937 0.02 2 910 239 147 LYS C C 178.72 0.1 1 911 239 147 LYS CA C 58.63 0.1 1 912 239 147 LYS CB C 32.5 0.1 1 913 239 147 LYS N N 119.47 0.1 1 914 240 148 ARG H H 8.107 0.02 1 915 240 148 ARG HA H 4.146 0.02 1 916 240 148 ARG HB2 H 1.953 0.02 2 917 240 148 ARG HB3 H 1.953 0.02 2 918 240 148 ARG C C 177.67 0.1 1 919 240 148 ARG CA C 58.32 0.1 1 920 240 148 ARG CB C 30.73 0.1 1 921 240 148 ARG N N 119.04 0.1 1 922 241 149 LYS H H 7.724 0.02 1 923 241 149 LYS HA H 4.198 0.02 1 924 241 149 LYS HB2 H 1.895 0.02 2 925 241 149 LYS HB3 H 1.895 0.02 2 926 241 149 LYS C C 177.29 0.1 1 927 241 149 LYS CA C 57.81 0.1 1 928 241 149 LYS CB C 32.67 0.1 1 929 241 149 LYS N N 119.4 0.1 1 930 242 150 LEU H H 7.742 0.02 1 931 242 150 LEU HA H 4.294 0.02 1 932 242 150 LEU HB2 H 1.747 0.02 2 933 242 150 LEU HB3 H 1.612 0.02 2 934 242 150 LEU C C 177.58 0.1 1 935 242 150 LEU CA C 55.76 0.1 1 936 242 150 LEU CB C 42.36 0.1 1 937 242 150 LEU N N 120.47 0.1 1 938 243 151 LYS H H 7.996 0.02 1 939 243 151 LYS HA H 4.275 0.02 1 940 243 151 LYS HB2 H 1.829 0.02 2 941 243 151 LYS HB3 H 1.829 0.02 2 942 243 151 LYS C C 176.63 0.1 1 943 243 151 LYS CA C 56.39 0.1 1 944 243 151 LYS CB C 32.59 0.1 1 945 243 151 LYS N N 120.13 0.1 1 946 244 152 GLN H H 8.161 0.02 1 947 244 152 GLN HA H 4.258 0.02 1 948 244 152 GLN HB2 H 2.016 0.02 2 949 244 152 GLN HB3 H 2.016 0.02 2 950 244 152 GLN C C 175.75 0.1 1 951 244 152 GLN CA C 56.44 0.1 1 952 244 152 GLN CB C 29.35 0.1 1 953 244 152 GLN N N 119.99 0.1 1 954 245 153 HIS H H 8.162 0.02 1 955 245 153 HIS HA H 4.64 0.02 1 956 245 153 HIS C C 174.87 0.1 1 957 245 153 HIS CA C 56.35 0.1 1 958 245 153 HIS CB C 30.56 0.1 1 959 245 153 HIS N N 118.96 0.1 1 960 246 154 GLU H H 8.194 0.02 1 961 246 154 GLU HA H 4.311 0.02 1 962 246 154 GLU HB2 H 2.076 0.02 2 963 246 154 GLU HB3 H 1.926 0.02 2 964 246 154 GLU C C 175.22 0.1 1 965 246 154 GLU CA C 56.67 0.1 1 966 246 154 GLU CB C 30.6 0.1 1 967 246 154 GLU N N 122.02 0.1 1 968 247 155 LEU H H 7.764 0.02 1 969 247 155 LEU C C 182.27 0.1 1 970 247 155 LEU CA C 56.81 0.1 1 971 247 155 LEU N N 128.45 0.1 1 stop_ save_