data_25196 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; haloSRC assignment ; _BMRB_accession_number 25196 _BMRB_flat_file_name bmr25196.str _Entry_type original _Submission_date 2014-09-02 _Accession_date 2014-09-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR assignment of halophilic disordered peptide haloSrc' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ortega Gabriel . . 2 Millet Oscar . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 81 "13C chemical shifts" 217 "15N chemical shifts" 81 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-09-23 update BMRB 'update entry citation' 2014-10-02 original author 'original release' stop_ _Original_release_date 2016-09-28 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Halophilic Protein Adaptation Results from Synergistic Residue-Ion Interactions in the Folded and Unfolded States ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26628359 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ortega Gabriel . . 2 Diercks Tammo . . 3 Millet Oscar . . stop_ _Journal_abbreviation 'Chem. Biol.' _Journal_volume 22 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1597 _Page_last 1607 _Year 2015 _Details . loop_ _Keyword Halophilia KCl Protein Stability acidic aminoacid archaea disordered electrostatic halophilic protein salt unfolded stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name haloSRC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label haloSRC $haloSRC stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'designed halophilic sequence derived from unique domain of human SRC kinase' 'lipid binding activity' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_haloSRC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common haloSRC _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'designed halophilic sequence from unique domine of SRC Kinase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; MASNDSKPSDASQRRRSLET AENVHGAGGGATPASQTPSE PASADGHDGPSAAFAPAAAE PDLFGGFNSSDTVTSPQRAG PEAGGSAWSHPQFEK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 SER 4 4 ASN 5 5 ASP 6 6 SER 7 7 LYS 8 8 PRO 9 9 SER 10 10 ASP 11 11 ALA 12 12 SER 13 13 GLN 14 14 ARG 15 15 ARG 16 16 ARG 17 17 SER 18 18 LEU 19 19 GLU 20 20 THR 21 21 ALA 22 22 GLU 23 23 ASN 24 24 VAL 25 25 HIS 26 26 GLY 27 27 ALA 28 28 GLY 29 29 GLY 30 30 GLY 31 31 ALA 32 32 THR 33 33 PRO 34 34 ALA 35 35 SER 36 36 GLN 37 37 THR 38 38 PRO 39 39 SER 40 40 GLU 41 41 PRO 42 42 ALA 43 43 SER 44 44 ALA 45 45 ASP 46 46 GLY 47 47 HIS 48 48 ASP 49 49 GLY 50 50 PRO 51 51 SER 52 52 ALA 53 53 ALA 54 54 PHE 55 55 ALA 56 56 PRO 57 57 ALA 58 58 ALA 59 59 ALA 60 60 GLU 61 61 PRO 62 62 ASP 63 63 LEU 64 64 PHE 65 65 GLY 66 66 GLY 67 67 PHE 68 68 ASN 69 69 SER 70 70 SER 71 71 ASP 72 72 THR 73 73 VAL 74 74 THR 75 75 SER 76 76 PRO 77 77 GLN 78 78 ARG 79 79 ALA 80 80 GLY 81 81 PRO 82 82 GLU 83 83 ALA 84 84 GLY 85 85 GLY 86 86 SER 87 87 ALA 88 88 TRP 89 89 SER 90 90 HIS 91 91 PRO 92 92 GLN 93 93 PHE 94 94 GLU 95 95 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $haloSRC Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name _Details $haloSRC 'recombinant technology' . Escherichia coli BL21 DE3 pET16b 'NcoI - BamHI' 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 $haloSRC 1 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' PMSF 1 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' 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_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 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 800 _Details Cryoprobe 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_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0 0.1 mM pH 7.5 0.1 pH pressure 1 . atm temperature 280 0.05 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 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(COCA)CB' '2D 1H-13C HSQC' '3D HN(CA)CO' 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 haloSRC _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 3 SER C C 173.67 . . 2 3 3 SER CA C 57.67 . . 3 3 3 SER CB C 62.67 . . 4 4 4 ASN H H 8.456 . . 5 4 4 ASN CA C 52.67 . . 6 4 4 ASN CB C 37.67 . . 7 4 4 ASN N N 120.3 . . 8 5 5 ASP H H 8.012 . . 9 5 5 ASP C C 175.67 . . 10 5 5 ASP CA C 53.67 . . 11 5 5 ASP CB C 40.67 . . 12 5 5 ASP N N 120.3 . . 13 6 6 SER H H 8.030 . . 14 6 6 SER CA C 57.67 . . 15 6 6 SER CB C 62.67 . . 16 6 6 SER N N 115.9 . . 17 7 7 LYS H H 8.147 . . 18 7 7 LYS CA C 53.67 . . 19 7 7 LYS CB C 31.67 . . 20 7 7 LYS N N 124.1 . . 21 8 8 PRO CA C 62.67 . . 22 8 8 PRO CB C 31.67 . . 23 9 9 SER H H 8.317 . . 24 9 9 SER C C 173.67 . . 25 9 9 SER CA C 57.67 . . 26 9 9 SER CB C 62.67 . . 27 9 9 SER N N 116.0 . . 28 10 10 ASP H H 8.180 . . 29 10 10 ASP C C 176.67 . . 30 10 10 ASP CA C 53.67 . . 31 10 10 ASP CB C 40.67 . . 32 10 10 ASP N N 122.6 . . 33 11 11 ALA H H 8.213 . . 34 11 11 ALA C C 178.67 . . 35 11 11 ALA CA C 52.67 . . 36 11 11 ALA CB C 17.67 . . 37 11 11 ALA N N 124.3 . . 38 12 12 SER H H 8.125 . . 39 12 12 SER C C 174.67 . . 40 12 12 SER CA C 58.67 . . 41 12 12 SER CB C 62.67 . . 42 12 12 SER N N 114.5 . . 43 13 13 GLN H H 7.921 . . 44 13 13 GLN CA C 55.67 . . 45 13 13 GLN CB C 28.67 . . 46 13 13 GLN N N 121.4 . . 47 14 14 ARG H H 7.929 . . 48 14 14 ARG CA C 55.67 . . 49 14 14 ARG CB C 29.67 . . 50 14 14 ARG N N 121.2 . . 51 15 15 ARG H H 8.087 . . 52 15 15 ARG C C 175.67 . . 53 15 15 ARG CA C 55.67 . . 54 15 15 ARG CB C 29.67 . . 55 15 15 ARG N N 121.8 . . 56 16 16 ARG H H 8.175 . . 57 16 16 ARG C C 176.67 . . 58 16 16 ARG CA C 55.67 . . 59 16 16 ARG CB C 29.67 . . 60 16 16 ARG N N 122.0 . . 61 17 17 SER H H 8.177 . . 62 17 17 SER CA C 57.67 . . 63 17 17 SER CB C 62.67 . . 64 17 17 SER N N 116.8 . . 65 18 18 LEU H H 8.045 . . 66 18 18 LEU CA C 54.67 . . 67 18 18 LEU CB C 41.67 . . 68 18 18 LEU N N 123.4 . . 69 19 19 GLU H H 8.117 . . 70 19 19 GLU CA C 55.67 . . 71 19 19 GLU CB C 29.67 . . 72 19 19 GLU N N 120.9 . . 73 20 20 THR H H 7.917 . . 74 20 20 THR C C 173.67 . . 75 20 20 THR CA C 60.67 . . 76 20 20 THR CB C 68.67 . . 77 20 20 THR N N 114.6 . . 78 21 21 ALA H H 8.106 . . 79 21 21 ALA C C 176.67 . . 80 21 21 ALA CA C 51.67 . . 81 21 21 ALA CB C 18.67 . . 82 21 21 ALA N N 126.0 . . 83 22 22 GLU H H 8.169 . . 84 22 22 GLU CA C 55.67 . . 85 22 22 GLU CB C 29.67 . . 86 22 22 GLU N N 119.5 . . 87 23 23 ASN H H 8.202 . . 88 23 23 ASN CA C 52.67 . . 89 23 23 ASN CB C 37.67 . . 90 23 23 ASN N N 119.5 . . 91 24 24 VAL H H 7.854 . . 92 24 24 VAL CA C 61.67 . . 93 24 24 VAL CB C 31.67 . . 94 24 24 VAL N N 120.2 . . 95 25 25 HIS H H 8.247 . . 96 25 25 HIS CA C 55.67 . . 97 25 25 HIS CB C 29.67 . . 98 25 25 HIS N N 122.1 . . 99 26 26 GLY H H 8.146 . . 100 26 26 GLY CA C 44.67 . . 101 26 26 GLY N N 110.2 . . 102 27 27 ALA H H 8.123 . . 103 27 27 ALA C C 177.67 . . 104 27 27 ALA CA C 51.67 . . 105 27 27 ALA CB C 18.67 . . 106 27 27 ALA N N 123.7 . . 107 28 28 GLY H H 8.330 . . 108 28 28 GLY CA C 44.67 . . 109 28 28 GLY N N 108.3 . . 110 29 29 GLY CA C 44.67 . . 111 30 30 GLY H H 8.124 . . 112 30 30 GLY C C 172.67 . . 113 30 30 GLY CA C 44.67 . . 114 30 30 GLY N N 108.6 . . 115 31 31 ALA H H 8.022 . . 116 31 31 ALA C C 176.67 . . 117 31 31 ALA CA C 51.67 . . 118 31 31 ALA CB C 18.67 . . 119 31 31 ALA N N 123.4 . . 120 32 32 THR H H 8.115 . . 121 32 32 THR CA C 58.67 . . 122 32 32 THR CB C 68.67 . . 123 32 32 THR N N 116.7 . . 124 33 33 PRO C C 175.67 . . 125 33 33 PRO CA C 62.67 . . 126 33 33 PRO CB C 31.67 . . 127 34 34 ALA H H 8.298 . . 128 34 34 ALA C C 177.67 . . 129 34 34 ALA CA C 51.67 . . 130 34 34 ALA CB C 18.67 . . 131 34 34 ALA N N 124.4 . . 132 35 35 SER H H 8.114 . . 133 35 35 SER C C 173.67 . . 134 35 35 SER CA C 57.67 . . 135 35 35 SER CB C 62.67 . . 136 35 35 SER N N 114.7 . . 137 36 36 GLN H H 8.211 . . 138 36 36 GLN C C 174.67 . . 139 36 36 GLN CA C 54.67 . . 140 36 36 GLN CB C 28.67 . . 141 36 36 GLN N N 122.0 . . 142 37 37 THR H H 8.120 . . 143 37 37 THR C C 171.67 . . 144 37 37 THR CA C 59.67 . . 145 37 37 THR CB C 68.67 . . 146 37 37 THR N N 118.7 . . 147 38 38 PRO C C 173.67 . . 148 38 38 PRO CA C 62.67 . . 149 38 38 PRO CB C 31.67 . . 150 39 39 SER H H 8.297 . . 151 39 39 SER C C 173.67 . . 152 39 39 SER CA C 57.67 . . 153 39 39 SER CB C 62.67 . . 154 39 39 SER N N 116.8 . . 155 40 40 GLU H H 8.191 . . 156 40 40 GLU C C 173.67 . . 157 40 40 GLU CA C 53.67 . . 158 40 40 GLU CB C 28.67 . . 159 40 40 GLU N N 123.6 . . 160 41 41 PRO C C 175.67 . . 161 41 41 PRO CA C 62.67 . . 162 41 41 PRO CB C 31.67 . . 163 42 42 ALA H H 8.318 . . 164 42 42 ALA C C 177.67 . . 165 42 42 ALA CA C 51.67 . . 166 42 42 ALA CB C 18.67 . . 167 42 42 ALA N N 124.4 . . 168 43 43 SER H H 8.170 . . 169 43 43 SER C C 173.67 . . 170 43 43 SER CA C 57.67 . . 171 43 43 SER CB C 62.67 . . 172 43 43 SER N N 115.3 . . 173 44 44 ALA H H 8.320 . . 174 44 44 ALA CA C 51.67 . . 175 44 44 ALA CB C 18.67 . . 176 44 44 ALA N N 126.4 . . 177 45 45 ASP H H 8.034 . . 178 45 45 ASP C C 175.67 . . 179 45 45 ASP CA C 53.67 . . 180 45 45 ASP CB C 40.67 . . 181 45 45 ASP N N 118.9 . . 182 46 46 GLY H H 8.081 . . 183 46 46 GLY C C 173.67 . . 184 46 46 GLY CA C 44.67 . . 185 46 46 GLY N N 108.8 . . 186 47 47 HIS H H 8.084 . . 187 47 47 HIS C C 173.67 . . 188 47 47 HIS CA C 55.67 . . 189 47 47 HIS CB C 28.67 . . 190 47 47 HIS N N 118.5 . . 191 48 48 ASP H H 8.250 . . 192 48 48 ASP C C 175.67 . . 193 48 48 ASP CA C 53.67 . . 194 48 48 ASP CB C 40.67 . . 195 48 48 ASP N N 121.0 . . 196 49 49 GLY H H 7.961 . . 197 49 49 GLY CA C 43.67 . . 198 49 49 GLY N N 109.0 . . 199 50 50 PRO C C 176.67 . . 200 50 50 PRO CA C 62.67 . . 201 50 50 PRO CB C 31.67 . . 202 51 51 SER H H 8.279 . . 203 51 51 SER C C 173.67 . . 204 51 51 SER CA C 57.67 . . 205 51 51 SER CB C 62.67 . . 206 51 51 SER N N 116.2 . . 207 52 52 ALA H H 8.128 . . 208 52 52 ALA C C 176.67 . . 209 52 52 ALA CA C 51.67 . . 210 52 52 ALA CB C 18.67 . . 211 52 52 ALA N N 126.0 . . 212 53 53 ALA H H 7.942 . . 213 53 53 ALA CA C 51.67 . . 214 53 53 ALA CB C 18.67 . . 215 53 53 ALA N N 122.6 . . 216 54 54 PHE H H 7.874 . . 217 54 54 PHE CA C 56.67 . . 218 54 54 PHE CB C 38.67 . . 219 54 54 PHE N N 119.3 . . 220 55 55 ALA H H 7.934 . . 221 55 55 ALA CA C 49.67 . . 222 55 55 ALA CB C 17.67 . . 223 55 55 ALA N N 127.5 . . 224 56 56 PRO C C 175.67 . . 225 56 56 PRO CA C 61.67 . . 226 56 56 PRO CB C 31.67 . . 227 57 57 ALA H H 8.224 . . 228 57 57 ALA CA C 51.67 . . 229 57 57 ALA CB C 18.67 . . 230 57 57 ALA N N 124.5 . . 231 58 58 ALA H H 8.029 . . 232 58 58 ALA C C 176.67 . . 233 58 58 ALA CA C 51.67 . . 234 58 58 ALA CB C 18.67 . . 235 58 58 ALA N N 123.0 . . 236 59 59 ALA H H 8.115 . . 237 59 59 ALA C C 176.67 . . 238 59 59 ALA CA C 51.67 . . 239 59 59 ALA CB C 18.67 . . 240 59 59 ALA N N 123.7 . . 241 60 60 GLU H H 8.214 . . 242 60 60 GLU CA C 53.67 . . 243 60 60 GLU CB C 28.67 . . 244 60 60 GLU N N 121.7 . . 245 61 61 PRO CA C 62.67 . . 246 61 61 PRO CB C 31.67 . . 247 62 62 ASP H H 8.228 . . 248 62 62 ASP CA C 53.67 . . 249 62 62 ASP CB C 40.67 . . 250 62 62 ASP N N 120.3 . . 251 63 63 LEU H H 7.998 . . 252 63 63 LEU CA C 54.67 . . 253 63 63 LEU CB C 41.67 . . 254 63 63 LEU N N 122.9 . . 255 64 64 PHE H H 8.137 . . 256 64 64 PHE CA C 56.67 . . 257 64 64 PHE CB C 38.67 . . 258 64 64 PHE N N 119.9 . . 259 65 65 GLY H H 8.066 . . 260 65 65 GLY CA C 44.67 . . 261 65 65 GLY N N 110.6 . . 262 66 66 GLY H H 7.729 . . 263 66 66 GLY CA C 44.67 . . 264 66 66 GLY N N 108.1 . . 265 67 67 PHE H H 7.952 . . 266 67 67 PHE CA C 56.67 . . 267 67 67 PHE CB C 38.67 . . 268 67 67 PHE N N 119.7 . . 269 68 68 ASN H H 8.293 . . 270 68 68 ASN CA C 52.67 . . 271 68 68 ASN CB C 38.67 . . 272 68 68 ASN N N 120.9 . . 273 69 69 SER H H 8.169 . . 274 69 69 SER CA C 57.67 . . 275 69 69 SER CB C 62.67 . . 276 69 69 SER N N 117.0 . . 277 70 70 SER H H 8.207 . . 278 70 70 SER C C 173.67 . . 279 70 70 SER CA C 57.67 . . 280 70 70 SER CB C 62.67 . . 281 70 70 SER N N 117.5 . . 282 71 71 ASP H H 8.050 . . 283 71 71 ASP C C 175.67 . . 284 71 71 ASP CA C 53.67 . . 285 71 71 ASP CB C 40.67 . . 286 71 71 ASP N N 121.9 . . 287 72 72 THR H H 7.876 . . 288 72 72 THR C C 173.67 . . 289 72 72 THR CA C 61.67 . . 290 72 72 THR CB C 68.67 . . 291 72 72 THR N N 114.4 . . 292 73 73 VAL H H 8.004 . . 293 73 73 VAL C C 175.67 . . 294 73 73 VAL CA C 61.67 . . 295 73 73 VAL CB C 31.67 . . 296 73 73 VAL N N 123.0 . . 297 74 74 THR H H 8.093 . . 298 74 74 THR C C 173.67 . . 299 74 74 THR CA C 60.67 . . 300 74 74 THR CB C 68.67 . . 301 74 74 THR N N 118.2 . . 302 75 75 SER H H 8.142 . . 303 75 75 SER C C 171.67 . . 304 75 75 SER CA C 55.67 . . 305 75 75 SER CB C 62.67 . . 306 75 75 SER N N 119.7 . . 307 76 76 PRO CA C 62.67 . . 308 76 76 PRO CB C 31.67 . . 309 77 77 GLN H H 8.262 . . 310 77 77 GLN CA C 54.67 . . 311 77 77 GLN CB C 28.67 . . 312 77 77 GLN N N 120.5 . . 313 78 78 ARG H H 8.182 . . 314 78 78 ARG CA C 54.67 . . 315 78 78 ARG CB C 30.67 . . 316 78 78 ARG N N 122.9 . . 317 79 79 ALA H H 8.224 . . 318 79 79 ALA CA C 51.67 . . 319 79 79 ALA CB C 18.67 . . 320 79 79 ALA N N 125.8 . . 321 80 80 GLY H H 8.086 . . 322 80 80 GLY CA C 43.67 . . 323 80 80 GLY N N 108.7 . . 324 81 81 PRO CA C 62.67 . . 325 81 81 PRO CB C 31.67 . . 326 82 82 GLU H H 8.516 . . 327 82 82 GLU CA C 55.67 . . 328 82 82 GLU CB C 28.67 . . 329 82 82 GLU N N 120.7 . . 330 83 83 ALA H H 8.070 . . 331 83 83 ALA CA C 51.67 . . 332 83 83 ALA CB C 18.67 . . 333 83 83 ALA N N 124.9 . . 334 84 84 GLY H H 8.091 . . 335 84 84 GLY CA C 44.67 . . 336 84 84 GLY N N 107.9 . . 337 85 85 GLY H H 8.029 . . 338 85 85 GLY C C 173.67 . . 339 85 85 GLY CA C 44.67 . . 340 85 85 GLY N N 108.5 . . 341 86 86 SER H H 8.105 . . 342 86 86 SER C C 173.67 . . 343 86 86 SER CA C 57.67 . . 344 86 86 SER CB C 62.67 . . 345 86 86 SER N N 115.5 . . 346 87 87 ALA H H 8.165 . . 347 87 87 ALA CA C 51.67 . . 348 87 87 ALA CB C 17.67 . . 349 87 87 ALA N N 125.3 . . 350 88 88 TRP H H 7.748 . . 351 88 88 TRP CA C 56.67 . . 352 88 88 TRP CB C 28.67 . . 353 88 88 TRP N N 119.2 . . 354 89 89 SER H H 7.625 . . 355 89 89 SER CA C 57.67 . . 356 89 89 SER CB C 62.67 . . 357 89 89 SER N N 117.2 . . 358 90 90 HIS H H 7.893 . . 359 90 90 HIS CA C 53.67 . . 360 90 90 HIS CB C 28.67 . . 361 90 90 HIS N N 121.7 . . 362 91 91 PRO CA C 62.67 . . 363 91 91 PRO CB C 31.67 . . 364 92 92 GLN H H 8.477 . . 365 92 92 GLN CA C 54.67 . . 366 92 92 GLN CB C 28.67 . . 367 92 92 GLN N N 120.6 . . 368 93 93 PHE H H 8.009 . . 369 93 93 PHE CA C 56.67 . . 370 93 93 PHE CB C 38.67 . . 371 93 93 PHE N N 120.5 . . 372 94 94 GLU H H 8.127 . . 373 94 94 GLU CA C 55.67 . . 374 94 94 GLU CB C 29.67 . . 375 94 94 GLU N N 122.8 . . 376 95 95 LYS H H 7.742 . . 377 95 95 LYS CA C 56.67 . . 378 95 95 LYS CB C 32.67 . . 379 95 95 LYS N N 127.2 . . stop_ save_