data_6129 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure and backbone dynamics of the Cu(I) and apo-forms of the second metal-binding domain of the Menkes protein ATP7A ; _BMRB_accession_number 6129 _BMRB_flat_file_name bmr6129.str _Entry_type original _Submission_date 2004-03-03 _Accession_date 2004-03-03 _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 Banci L. . . 2 Bertini I. . . 3 'Del Conte' R. . . 4 D'Onofrio M. . . 5 Rosato A. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 435 "13C chemical shifts" 248 "15N chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-05-15 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6130 'same protein in simple form' stop_ _Original_release_date 2004-05-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15035611 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 'Del Conte' R. . . 4 D'Onofrio M. . . 5 Rosato A. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3396 _Page_last 3403 _Year 2004 _Details . loop_ _Keyword 'copper homeostasis' Menkes 'metal transport' stop_ save_ ################################## # Molecular system description # ################################## save_system_ATPase _Saveframe_category molecular_system _Mol_system_name 'Copper-transporting ATPase 1 (E.C.3.6.3.4)' _Abbreviation_common ATPase _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Copper-transporting ATPase 1' $ATPase 'COPPER (I) ION' $CU stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ATPase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ATPase _Abbreviation_common ATPase _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; GEVVLKMKVEGMTCHSCTST IEGKIGKLQGVQRIKVSLDN QEATIVYQPHLISVEEMKKQ IEAMGFPAFVKKIEGR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLU 3 VAL 4 VAL 5 LEU 6 LYS 7 MET 8 LYS 9 VAL 10 GLU 11 GLY 12 MET 13 THR 14 CYS 15 HIS 16 SER 17 CYS 18 THR 19 SER 20 THR 21 ILE 22 GLU 23 GLY 24 LYS 25 ILE 26 GLY 27 LYS 28 LEU 29 GLN 30 GLY 31 VAL 32 GLN 33 ARG 34 ILE 35 LYS 36 VAL 37 SER 38 LEU 39 ASP 40 ASN 41 GLN 42 GLU 43 ALA 44 THR 45 ILE 46 VAL 47 TYR 48 GLN 49 PRO 50 HIS 51 LEU 52 ILE 53 SER 54 VAL 55 GLU 56 GLU 57 MET 58 LYS 59 LYS 60 GLN 61 ILE 62 GLU 63 ALA 64 MET 65 GLY 66 PHE 67 PRO 68 ALA 69 PHE 70 VAL 71 LYS 72 LYS 73 ILE 74 GLU 75 GLY 76 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 6022 MNKr2 94.74 84 100.00 100.00 2.72e-43 BMRB 6130 ATPase 100.00 76 100.00 100.00 2.91e-46 PDB 1Q8L "Second Metal Binding Domain Of The Menkes Atpase" 94.74 84 100.00 100.00 2.72e-43 PDB 1S6O "Solution Structure And Backbone Dynamics Of The Apo-Form Of The Second Metal-Binding Domain Of The Menkes Protein Atp7a" 100.00 76 100.00 100.00 2.91e-46 PDB 1S6U "Solution Structure And Backbone Dynamics Of The Cu(I) Form Of The Second Metal-Binding Domain Of The Menkes Protein Atp7a" 100.00 76 100.00 100.00 2.91e-46 stop_ save_ ############# # Ligands # ############# save_CU _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU (COPPER (II) ION)" _BMRB_code . _PDB_code CU _Molecular_mass 63.546 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 23 09:31:38 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ATPase 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 _Vector_name $ATPase 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ATPase 1 mM . $CU 1 mM . phosphate 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ATPase 1 mM [U-15N] $CU 1 mM . phosphate 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ATPase 1 mM '[U-13C; U-15N]' $CU 1 mM . phosphate 100 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task refinement 'structure solution' stop_ _Details Guentert save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save_[1H-1H]-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name [1H-1H]-NOESY _Sample_label . save_ save_13C-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _Sample_label . save_ save_15N-NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label . save_ save_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label . C 13 . ppm . . . . . . $entry_citation $entry_citation . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Copper-transporting ATPase 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY CA C 41.18 . . 2 . 1 GLY HA2 H 3.954 . . 3 . 1 GLY HA3 H 4.000 . . 4 . 2 GLU H H 8.314 . . 5 . 2 GLU N N 118.43 . . 6 . 2 GLU CA C 53.50 . . 7 . 2 GLU CB C 29.05 . . 8 . 2 GLU HA H 4.434 . . 9 . 2 GLU HB2 H 1.719 . . 10 . 2 GLU CG C 34.10 . . 11 . 2 GLU HG2 H 2.026 . . 12 . 2 GLU HG3 H 1.976 . . 13 . 3 VAL H H 8.463 . . 14 . 3 VAL N N 122.68 . . 15 . 3 VAL CA C 58.81 . . 16 . 3 VAL CB C 31.44 . . 17 . 3 VAL HA H 4.170 . . 18 . 3 VAL HB H 1.201 . . 19 . 3 VAL CG1 C 20.11 . . 20 . 3 VAL HG1 H 0.733 . . 21 . 3 VAL CG2 C 19.13 . . 22 . 3 VAL HG2 H 0.541 . . 23 . 4 VAL H H 8.276 . . 24 . 4 VAL N N 122.68 . . 25 . 4 VAL CA C 58.91 . . 26 . 4 VAL CB C 31.07 . . 27 . 4 VAL HA H 4.810 . . 28 . 4 VAL HB H 1.870 . . 29 . 4 VAL CG1 C 19.06 . . 30 . 4 VAL HG1 H 0.848 . . 31 . 4 VAL CG2 C 18.82 . . 32 . 4 VAL HG2 H 0.744 . . 33 . 5 LEU H H 9.721 . . 34 . 5 LEU N N 130.61 . . 35 . 5 LEU CA C 50.86 . . 36 . 5 LEU CB C 44.01 . . 37 . 5 LEU HB3 H 1.635 . . 38 . 5 LEU HA H 4.962 . . 39 . 5 LEU HB2 H 1.813 . . 40 . 5 LEU CD1 C 25.13 . . 41 . 5 LEU HD1 H 0.720 . . 42 . 5 LEU CD2 C 22.52 . . 43 . 5 LEU HD2 H 0.951 . . 44 . 5 LEU CG C 25.43 . . 45 . 5 LEU HG H 1.378 . . 46 . 6 LYS H H 8.803 . . 47 . 6 LYS N N 123.53 . . 48 . 6 LYS CA C 51.92 . . 49 . 6 LYS CB C 32.22 . . 50 . 6 LYS HB3 H 1.674 . . 51 . 6 LYS HA H 5.385 . . 52 . 6 LYS HB2 H 1.495 . . 53 . 6 LYS CD C 26.81 . . 54 . 6 LYS HD2 H 1.432 . . 55 . 6 LYS HD3 H 1.620 . . 56 . 6 LYS CG C 22.82 . . 57 . 6 LYS HG2 H 1.361 . . 58 . 6 LYS CE C 39.69 . . 59 . 6 LYS HE2 H 2.777 . . 60 . 7 MET H H 9.060 . . 61 . 7 MET N N 121.54 . . 62 . 7 MET CA C 51.21 . . 63 . 7 MET CB C 35.10 . . 64 . 7 MET HB3 H 1.471 . . 65 . 7 MET HA H 5.062 . . 66 . 7 MET HB2 H 1.884 . . 67 . 7 MET CG C 29.94 . . 68 . 7 MET HG2 H 2.227 . . 69 . 7 MET HG3 H 2.074 . . 70 . 7 MET HE H 1.543 . . 71 . 8 LYS H H 9.246 . . 72 . 8 LYS N N 126.64 . . 73 . 8 LYS CA C 53.213 . . 74 . 8 LYS CB C 31.05 . . 75 . 8 LYS HB3 H 1.632 . . 76 . 8 LYS HA H 4.841 . . 77 . 8 LYS HB2 H 1.765 . . 78 . 8 LYS CD C 26.65 . . 79 . 8 LYS HD2 H 1.711 . . 80 . 8 LYS HD3 H 1.577 . . 81 . 8 LYS CG C 22.69 . . 82 . 8 LYS HE2 H 2.903 . . 83 . 8 LYS HE3 H 2.817 . . 84 . 8 LYS HG2 H 1.575 . . 85 . 8 LYS HG3 H 1.330 . . 86 . 8 LYS CE C 39.79 . . 87 . 9 VAL H H 7.903 . . 88 . 9 VAL N N 126.08 . . 89 . 9 VAL CA C 58.99 . . 90 . 9 VAL CB C 31.76 . . 91 . 9 VAL HA H 4.743 . . 92 . 9 VAL HB H 1.439 . . 93 . 9 VAL CG1 C 18.81 . . 94 . 9 VAL HG1 H 0.636 . . 95 . 9 VAL CG2 C 20.23 . . 96 . 9 VAL HG2 H 0.671 . . 97 . 10 GLU H H 9.017 . . 98 . 10 GLU N N 126.08 . . 99 . 10 GLU CA C 53.02 . . 100 . 10 GLU CB C 29.57 . . 101 . 10 GLU HB3 H 2.085 . . 102 . 10 GLU HA H 4.505 . . 103 . 10 GLU HB2 H 1.867 . . 104 . 10 GLU CG C 34.93 . . 105 . 10 GLU HG2 H 2.271 . . 106 . 10 GLU HG3 H 2.148 . . 107 . 11 GLY H H 8.152 . . 108 . 11 GLY N N 102.55 . . 109 . 11 GLY CA C 43.37 . . 110 . 11 GLY HA2 H 3.613 . . 111 . 11 GLY HA3 H 4.342 . . 112 . 12 MET H H 8.876 . . 113 . 12 MET N N 119.28 . . 114 . 12 MET CA C 53.74 . . 115 . 12 MET CB C 31.75 . . 116 . 12 MET HB3 H 1.306 . . 117 . 12 MET HA H 4.897 . . 118 . 12 MET HB2 H 2.381 . . 119 . 12 MET CG C 28.42 . . 120 . 12 MET HG2 H 2.031 . . 121 . 12 MET HG3 H 1.259 . . 122 . 13 THR H H 9.095 . . 123 . 13 THR N N 113.61 . . 124 . 13 THR CA C 59.54 . . 125 . 13 THR CB C 68.86 . . 126 . 13 THR HA H 4.527 . . 127 . 13 THR HB H 4.363 . . 128 . 13 THR CG2 C 19.25 . . 129 . 13 THR HG2 H 1.098 . . 130 . 14 CYS H H 8.007 . . 131 . 14 CYS N N 117.29 . . 132 . 14 CYS CA C 55.01 . . 133 . 14 CYS CB C 29.28 . . 134 . 14 CYS HB3 H 3.206 . . 135 . 14 CYS HA H 4.814 . . 136 . 14 CYS HB2 H 3.317 . . 137 . 15 HIS CA C 56.63 . . 138 . 15 HIS CB C 27.20 . . 139 . 15 HIS HB3 H 3.105 . . 140 . 15 HIS HA H 4.664 . . 141 . 15 HIS HB2 H 3.211 . . 142 . 16 SER H H 9.456 . . 143 . 16 SER N N 120.98 . . 144 . 16 SER CA C 56.77 . . 145 . 16 SER CB C 59.77 . . 146 . 16 SER HB3 H 3.895 . . 147 . 16 SER HA H 4.340 . . 148 . 16 SER HB2 H 3.972 . . 149 . 17 CYS H H 8.150 . . 150 . 17 CYS N N 124.94 . . 151 . 17 CYS CA C 61.40 . . 152 . 17 CYS CB C 27.18 . . 153 . 17 CYS HB3 H 2.547 . . 154 . 17 CYS HA H 3.922 . . 155 . 17 CYS HB2 H 3.226 . . 156 . 18 THR H H 6.886 . . 157 . 18 THR N N 107.09 . . 158 . 18 THR CA C 62.89 . . 159 . 18 THR CB C 64.47 . . 160 . 18 THR HA H 3.500 . . 161 . 18 THR HB H 4.017 . . 162 . 18 THR CG2 C 20.99 . . 163 . 18 THR HG2 H 1.139 . . 164 . 19 SER H H 7.609 . . 165 . 19 SER N N 117.01 . . 166 . 19 SER CA C 58.91 . . 167 . 19 SER CB C 60.33 . . 168 . 19 SER HB3 H 3.831 . . 169 . 19 SER HA H 4.175 . . 170 . 19 SER HB2 H 3.884 . . 171 . 20 THR H H 7.944 . . 172 . 20 THR N N 120.69 . . 173 . 20 THR CA C 64.37 . . 174 . 20 THR CB C 66.22 . . 175 . 20 THR HA H 3.944 . . 176 . 20 THR HB H 4.300 . . 177 . 20 THR CG2 C 19.00 . . 178 . 20 THR HG2 H 1.337 . . 179 . 21 ILE H H 7.481 . . 180 . 21 ILE N N 121.26 . . 181 . 21 ILE CA C 63.94 . . 182 . 21 ILE CB C 36.15 . . 183 . 21 ILE HA H 3.434 . . 184 . 21 ILE HB H 1.470 . . 185 . 21 ILE CG1 C 26.84 . . 186 . 21 ILE HG12 H 1.610 . . 187 . 21 ILE HG13 H 0.608 . . 188 . 21 ILE CG2 C 15.27 . . 189 . 21 ILE HG2 H 0.575 . . 190 . 21 ILE CD1 C 11.93 . . 191 . 21 ILE HD1 H -0.085 . . 192 . 22 GLU H H 8.250 . . 193 . 22 GLU N N 117.01 . . 194 . 22 GLU CA C 57.53 . . 195 . 22 GLU CB C 27.10 . . 196 . 22 GLU HB3 H 1.834 . . 197 . 22 GLU HA H 3.575 . . 198 . 22 GLU HB2 H 2.011 . . 199 . 22 GLU CG C 35.26 . . 200 . 22 GLU HG2 H 2.484 . . 201 . 22 GLU HG3 H 1.955 . . 202 . 23 GLY H H 8.314 . . 203 . 23 GLY N N 105.39 . . 204 . 23 GLY CA C 44.32 . . 205 . 23 GLY HA2 H 3.698 . . 206 . 23 GLY HA3 H 3.769 . . 207 . 24 LYS H H 7.493 . . 208 . 24 LYS N N 118.43 . . 209 . 24 LYS CA C 55.99 . . 210 . 24 LYS CB C 30.68 . . 211 . 24 LYS HB3 H 1.743 . . 212 . 24 LYS HA H 4.125 . . 213 . 24 LYS HB2 H 1.846 . . 214 . 24 LYS CD C 26.37 . . 215 . 24 LYS HD2 H 1.717 . . 216 . 24 LYS CG C 22.68 . . 217 . 24 LYS HG2 H 1.448 . . 218 . 24 LYS HG3 H 1.395 . . 219 . 24 LYS CE C 39.71 . . 220 . 24 LYS HE2 H 2.954 . . 221 . 25 ILE H H 8.311 . . 222 . 25 ILE N N 116.73 . . 223 . 25 ILE CA C 57.99 . . 224 . 25 ILE CB C 31.66 . . 225 . 25 ILE HA H 3.721 . . 226 . 25 ILE HB H 1.974 . . 227 . 25 ILE CG1 C 25.77 . . 228 . 25 ILE HG12 H 1.819 . . 229 . 25 ILE HG13 H 0.888 . . 230 . 25 ILE CG2 C 16.20 . . 231 . 25 ILE HG2 H 0.702 . . 232 . 25 ILE CD1 C 6.94 . . 233 . 25 ILE HD1 H 0.522 . . 234 . 26 GLY H H 7.675 . . 235 . 26 GLY N N 102.27 . . 236 . 26 GLY CA C 43.77 . . 237 . 26 GLY HA2 H 3.658 . . 238 . 26 GLY HA3 H 3.753 . . 239 . 27 LYS H H 6.554 . . 240 . 27 LYS N N 114.46 . . 241 . 27 LYS CA C 53.18 . . 242 . 27 LYS CB C 30.72 . . 243 . 27 LYS HB3 H 1.694 . . 244 . 27 LYS HA H 4.308 . . 245 . 27 LYS HB2 H 1.904 . . 246 . 27 LYS CD C 26.66 . . 247 . 27 LYS HD2 H 1.627 . . 248 . 27 LYS CG C 22.52 . . 249 . 27 LYS HG2 H 1.561 . . 250 . 27 LYS HG3 H 1.444 . . 251 . 27 LYS CE C 39.77 . . 252 . 27 LYS HE2 H 2.944 . . 253 . 28 LEU H H 7.377 . . 254 . 28 LEU N N 120.69 . . 255 . 28 LEU CA C 52.41 . . 256 . 28 LEU CB C 38.71 . . 257 . 28 LEU HB3 H 1.178 . . 258 . 28 LEU HA H 4.113 . . 259 . 28 LEU HB2 H 1.823 . . 260 . 28 LEU CD1 C 23.63 . . 261 . 28 LEU HD1 H 0.753 . . 262 . 28 LEU CD2 C 19.52 . . 263 . 28 LEU HD2 H 0.760 . . 264 . 28 LEU CG C 23.77 . . 265 . 28 LEU HG H 1.921 . . 266 . 29 GLN H H 8.563 . . 267 . 29 GLN N N 123.81 . . 268 . 29 GLN CA C 55.03 . . 269 . 29 GLN CB C 25.81 . . 270 . 29 GLN HA H 3.950 . . 271 . 29 GLN HB2 H 1.943 . . 272 . 29 GLN CG C 31.77 . . 273 . 29 GLN HG2 H 2.330 . . 274 . 29 GLN HG3 H 2.239 . . 275 . 29 GLN NE2 N 111.13 . . 276 . 29 GLN HE21 H 7.445 . . 277 . 29 GLN HE22 H 6.757 . . 278 . 30 GLY H H 8.521 . . 279 . 30 GLY N N 109.64 . . 280 . 30 GLY CA C 43.76 . . 281 . 30 GLY HA2 H 3.457 . . 282 . 30 GLY HA3 H 4.240 . . 283 . 31 VAL H H 7.597 . . 284 . 31 VAL N N 120.13 . . 285 . 31 VAL CA C 61.46 . . 286 . 31 VAL CB C 28.65 . . 287 . 31 VAL HA H 3.906 . . 288 . 31 VAL HB H 2.189 . . 289 . 31 VAL CG1 C 20.20 . . 290 . 31 VAL HG1 H 0.790 . . 291 . 31 VAL CG2 C 19.02 . . 292 . 31 VAL HG2 H 0.657 . . 293 . 32 GLN H H 9.155 . . 294 . 32 GLN N N 127.21 . . 295 . 32 GLN CA C 54.23 . . 296 . 32 GLN CB C 28.05 . . 297 . 32 GLN HB3 H 1.963 . . 298 . 32 GLN HA H 4.284 . . 299 . 32 GLN HB2 H 1.643 . . 300 . 32 GLN CG C 31.47 . . 301 . 32 GLN HG2 H 2.283 . . 302 . 32 GLN HG3 H 2.090 . . 303 . 32 GLN NE2 N 111.41 . . 304 . 32 GLN HE21 H 7.245 . . 305 . 32 GLN HE22 H 6.723 . . 306 . 33 ARG H H 7.673 . . 307 . 33 ARG N N 115.02 . . 308 . 33 ARG CA C 53.15 . . 309 . 33 ARG CB C 30.96 . . 310 . 33 ARG HA H 4.514 . . 311 . 33 ARG HB2 H 1.654 . . 312 . 33 ARG CG C 24.54 . . 313 . 33 ARG HG2 H 1.480 . . 314 . 33 ARG HG3 H 1.423 . . 315 . 33 ARG CD C 41.06 . . 316 . 33 ARG HD2 H 3.091 . . 317 . 34 ILE H H 8.517 . . 318 . 34 ILE N N 119.28 . . 319 . 34 ILE CA C 56.36 . . 320 . 34 ILE CB C 37.66 . . 321 . 34 ILE HA H 5.196 . . 322 . 34 ILE HB H 1.654 . . 323 . 34 ILE CG1 C 26.90 . . 324 . 34 ILE HG12 H 1.362 . . 325 . 34 ILE HG13 H 0.67 . . 326 . 34 ILE CG2 C 11.99 . . 327 . 34 ILE HG2 H 0.865 . . 328 . 34 ILE CD1 C 11.85 . . 329 . 34 ILE HD1 H 0.552 . . 330 . 35 LYS H H 8.317 . . 331 . 35 LYS N N 126.08 . . 332 . 35 LYS CA C 51.47 . . 333 . 35 LYS CB C 33.01 . . 334 . 35 LYS HB3 H 1.571 . . 335 . 35 LYS HA H 4.657 . . 336 . 35 LYS HB2 H 1.675 . . 337 . 35 LYS CD C 26.04 . . 338 . 35 LYS HD2 H 1.680 . . 339 . 35 LYS HD3 H 1.667 . . 340 . 35 LYS CG C 22.04 . . 341 . 35 LYS HG2 H 1.251 . . 342 . 35 LYS CE C 39.72 . . 343 . 35 LYS HE2 H 2.875 . . 344 . 36 VAL H H 10.129 . . 345 . 36 VAL N N 128.63 . . 346 . 36 VAL CA C 58.94 . . 347 . 36 VAL CB C 30.08 . . 348 . 36 VAL HA H 4.542 . . 349 . 36 VAL HB H 1.802 . . 350 . 36 VAL CG1 C 19.40 . . 351 . 36 VAL HG1 H 0.725 . . 352 . 36 VAL CG2 C 20.35 . . 353 . 36 VAL HG2 H 0.584 . . 354 . 37 SER H H 8.708 . . 355 . 37 SER N N 120.41 . . 356 . 37 SER CA C 52.79 . . 357 . 37 SER CB C 62.08 . . 358 . 37 SER HB3 H 3.816 . . 359 . 37 SER HA H 4.724 . . 360 . 37 SER HB2 H 3.752 . . 361 . 38 LEU H H 9.098 . . 362 . 38 LEU N N 130.05 . . 363 . 38 LEU CA C 55.25 . . 364 . 38 LEU CB C 39.76 . . 365 . 38 LEU HB3 H 1.224 . . 366 . 38 LEU HA H 3.837 . . 367 . 38 LEU HB2 H 1.640 . . 368 . 38 LEU CD1 C 21.15 . . 369 . 38 LEU HD1 H 0.510 . . 370 . 38 LEU CD2 C 22.80 . . 371 . 38 LEU HD2 H 0.419 . . 372 . 38 LEU CG C 23.83 . . 373 . 38 LEU HG H 1.343 . . 374 . 39 ASP H H 8.390 . . 375 . 39 ASP N N 117.01 . . 376 . 39 ASP CA C 54.72 . . 377 . 39 ASP CB C 37.76 . . 378 . 39 ASP HB3 H 2.311 . . 379 . 39 ASP HA H 4.128 . . 380 . 39 ASP HB2 H 2.495 . . 381 . 40 ASN H H 7.605 . . 382 . 40 ASN N N 112.47 . . 383 . 40 ASN CA C 49.73 . . 384 . 40 ASN CB C 36.18 . . 385 . 40 ASN HB3 H 2.408 . . 386 . 40 ASN HA H 4.682 . . 387 . 40 ASN HB2 H 2.663 . . 388 . 40 ASN ND2 N 111.84 . . 389 . 40 ASN HD21 H 7.304 . . 390 . 40 ASN HD22 H 6.739 . . 391 . 41 GLN H H 7.524 . . 392 . 41 GLN N N 117.01 . . 393 . 41 GLN CA C 54.50 . . 394 . 41 GLN CB C 23.84 . . 395 . 41 GLN HB3 H 2.319 . . 396 . 41 GLN HA H 3.518 . . 397 . 41 GLN HB2 H 2.224 . . 398 . 41 GLN CG C 32.20 . . 399 . 41 GLN HG2 H 2.288 . . 400 . 41 GLN HG3 H 2.204 . . 401 . 41 GLN NE2 N 111.84 . . 402 . 41 GLN HE21 H 7.543 . . 403 . 41 GLN HE22 H 6.830 . . 404 . 42 GLU H H 7.549 . . 405 . 42 GLU N N 114.74 . . 406 . 42 GLU CA C 52.26 . . 407 . 42 GLU CB C 33.04 . . 408 . 42 GLU HB3 H 1.628 . . 409 . 42 GLU HA H 5.401 . . 410 . 42 GLU HB2 H 1.725 . . 411 . 42 GLU CG C 34.84 . . 412 . 42 GLU HG2 H 1.974 . . 413 . 42 GLU HG3 H 1.851 . . 414 . 43 ALA H H 9.367 . . 415 . 43 ALA N N 126.64 . . 416 . 43 ALA CA C 47.41 . . 417 . 43 ALA CB C 19.19 . . 418 . 43 ALA HA H 5.126 . . 419 . 43 ALA HB H 1.003 . . 420 . 44 THR H H 8.932 . . 421 . 44 THR N N 119.84 . . 422 . 44 THR CA C 60.30 . . 423 . 44 THR CB C 67.09 . . 424 . 44 THR HA H 4.895 . . 425 . 44 THR HB H 3.891 . . 426 . 44 THR CG2 C 18.77 . . 427 . 44 THR HG2 H 0.987 . . 428 . 45 ILE H H 9.575 . . 429 . 45 ILE N N 128.91 . . 430 . 45 ILE CA C 58.05 . . 431 . 45 ILE CB C 39.40 . . 432 . 45 ILE HA H 4.683 . . 433 . 45 ILE HB H 1.559 . . 434 . 45 ILE CG1 C 25.57 . . 435 . 45 ILE HG12 H 1.332 . . 436 . 45 ILE HG13 H 0.605 . . 437 . 45 ILE CG2 C 16.72 . . 438 . 45 ILE HG2 H 0.908 . . 439 . 45 ILE CD1 C 11.76 . . 440 . 45 ILE HD1 H 0.606 . . 441 . 46 VAL H H 8.940 . . 442 . 46 VAL N N 128.06 . . 443 . 46 VAL CA C 59.04 . . 444 . 46 VAL CB C 29.96 . . 445 . 46 VAL HA H 5.141 . . 446 . 46 VAL HB H 1.812 . . 447 . 46 VAL CG1 C 18.39 . . 448 . 46 VAL HG1 H 0.860 . . 449 . 46 VAL CG2 C 18.95 . . 450 . 46 VAL HG2 H 0.787 . . 451 . 47 TYR H H 9.278 . . 452 . 47 TYR N N 125.79 . . 453 . 47 TYR CA C 52.54 . . 454 . 47 TYR CB C 39.40 . . 455 . 47 TYR HB3 H 2.575 . . 456 . 47 TYR HA H 5.619 . . 457 . 47 TYR HB2 H 2.641 . . 458 . 47 TYR HD1 H 6.764 . . 459 . 47 TYR HD2 H 6.764 . . 460 . 47 TYR HE1 H 6.521 . . 461 . 47 TYR HE2 H 6.521 . . 462 . 48 GLN H H 8.588 . . 463 . 48 GLN N N 118.71 . . 464 . 48 GLN CA C 49.55 . . 465 . 48 GLN CB C 27.42 . . 466 . 48 GLN HB3 H 1.932 . . 467 . 48 GLN HA H 4.981 . . 468 . 48 GLN HB2 H 1.992 . . 469 . 48 GLN CG C 31.43 . . 470 . 48 GLN HG2 H 2.300 . . 471 . 48 GLN HG3 H 2.229 . . 472 . 48 GLN NE2 N 110.56 . . 473 . 48 GLN HE21 H 7.403 . . 474 . 48 GLN HE22 H 6.671 . . 475 . 49 PRO CA C 61.50 . . 476 . 49 PRO CB C 29.89 . . 477 . 49 PRO HB3 H 2.050 . . 478 . 49 PRO HA H 5.004 . . 479 . 49 PRO HB2 H 2.265 . . 480 . 49 PRO HD2 H 4.037 . . 481 . 49 PRO HD3 H 3.502 . . 482 . 49 PRO CG C 24.75 . . 483 . 49 PRO HG2 H 1.956 . . 484 . 49 PRO HG3 H 1.737 . . 485 . 50 HIS H H 8.223 . . 486 . 50 HIS N N 113.89 . . 487 . 50 HIS CA C 54.91 . . 488 . 50 HIS CB C 26.88 . . 489 . 50 HIS HB3 H 2.838 . . 490 . 50 HIS HA H 4.679 . . 491 . 50 HIS HB2 H 3.159 . . 492 . 50 HIS HD2 H 6.840 . . 493 . 51 LEU H H 7.541 . . 494 . 51 LEU N N 119.28 . . 495 . 51 LEU CA C 52.42 . . 496 . 51 LEU CB C 42.83 . . 497 . 51 LEU HB3 H 1.048 . . 498 . 51 LEU HA H 4.304 . . 499 . 51 LEU HB2 H 1.490 . . 500 . 51 LEU CD1 C 23.02 . . 501 . 51 LEU HD1 H 0.667 . . 502 . 51 LEU CD2 C 23.53 . . 503 . 51 LEU HD2 H 0.296 . . 504 . 51 LEU CG C 20.30 . . 505 . 51 LEU HG H 0.645 . . 506 . 52 ILE H H 7.743 . . 507 . 52 ILE N N 119.28 . . 508 . 52 ILE CA C 57.98 . . 509 . 52 ILE CB C 37.72 . . 510 . 52 ILE HA H 4.383 . . 511 . 52 ILE HB H 2.052 . . 512 . 52 ILE CG1 C 27.16 . . 513 . 52 ILE HG12 H 1.523 . . 514 . 52 ILE HG13 H 1.253 . . 515 . 52 ILE CG2 C 13.53 . . 516 . 52 ILE HG2 H 0.721 . . 517 . 52 ILE CD1 C 12.88 . . 518 . 52 ILE HD1 H 0.756 . . 519 . 53 SER H H 7.386 . . 520 . 53 SER N N 116.44 . . 521 . 53 SER CA C 52.87 . . 522 . 53 SER CB C 65.06 . . 523 . 53 SER HB3 H 3.856 . . 524 . 53 SER HA H 4.975 . . 525 . 53 SER HB2 H 4.257 . . 526 . 54 VAL H H 8.325 . . 527 . 54 VAL N N 120.41 . . 528 . 54 VAL CA C 64.32 . . 529 . 54 VAL CB C 29.01 . . 530 . 54 VAL HA H 3.086 . . 531 . 54 VAL HB H 1.817 . . 532 . 54 VAL CG1 C 20.78 . . 533 . 54 VAL HG1 H 0.947 . . 534 . 54 VAL CG2 C 19.87 . . 535 . 54 VAL HG2 H 0.775 . . 536 . 55 GLU H H 8.509 . . 537 . 55 GLU N N 117.29 . . 538 . 55 GLU CA C 57.91 . . 539 . 55 GLU CB C 26.20 . . 540 . 55 GLU HB3 H 1.955 . . 541 . 55 GLU HA H 3.703 . . 542 . 55 GLU HB2 H 1.802 . . 543 . 55 GLU CG C 34.44 . . 544 . 55 GLU HG2 H 2.337 . . 545 . 55 GLU HG3 H 2.163 . . 546 . 56 GLU H H 7.690 . . 547 . 56 GLU N N 119.56 . . 548 . 56 GLU CA C 56.55 . . 549 . 56 GLU CB C 27.21 . . 550 . 56 GLU HB3 H 2.052 . . 551 . 56 GLU HA H 3.934 . . 552 . 56 GLU HB2 H 1.832 . . 553 . 56 GLU CG C 33.55 . . 554 . 56 GLU HG2 H 2.317 . . 555 . 56 GLU HG3 H 2.056 . . 556 . 57 MET H H 7.402 . . 557 . 57 MET N N 117.29 . . 558 . 57 MET CA C 58.47 . . 559 . 57 MET CB C 30.70 . . 560 . 57 MET HB3 H 1.283 . . 561 . 57 MET HA H 3.480 . . 562 . 57 MET HB2 H 1.873 . . 563 . 57 MET CG C 30.46 . . 564 . 57 MET HG2 H 2.361 . . 565 . 57 MET HG3 H 1.776 . . 566 . 58 LYS H H 8.318 . . 567 . 58 LYS N N 117.86 . . 568 . 58 LYS CA C 58.03 . . 569 . 58 LYS CB C 30.99 . . 570 . 58 LYS HB3 H 1.395 . . 571 . 58 LYS HA H 3.443 . . 572 . 58 LYS HB2 H 1.777 . . 573 . 58 LYS CD C 27.69 . . 574 . 58 LYS HD2 H 1.482 . . 575 . 58 LYS CG C 22.32 . . 576 . 58 LYS HG2 H 1.202 . . 577 . 58 LYS HG3 H 1.135 . . 578 . 58 LYS CE C 39.65 . . 579 . 58 LYS HE2 H 2.956 . . 580 . 59 LYS H H 7.933 . . 581 . 59 LYS N N 117.01 . . 582 . 59 LYS CA C 56.92 . . 583 . 59 LYS CB C 29.86 . . 584 . 59 LYS HB3 H 1.820 . . 585 . 59 LYS HA H 3.964 . . 586 . 59 LYS HB2 H 1.757 . . 587 . 59 LYS CD C 26.98 . . 588 . 59 LYS HD2 H 1.595 . . 589 . 59 LYS CG C 22.54 . . 590 . 59 LYS HG2 H 1.504 . . 591 . 59 LYS HG3 H 1.306 . . 592 . 59 LYS CE C 39.60 . . 593 . 59 LYS HE2 H 2.850 . . 594 . 60 GLN H H 7.871 . . 595 . 60 GLN N N 117.01 . . 596 . 60 GLN CA C 56.38 . . 597 . 60 GLN CB C 24.82 . . 598 . 60 GLN HB3 H 1.944 . . 599 . 60 GLN HA H 3.905 . . 600 . 60 GLN HB2 H 1.790 . . 601 . 60 GLN CG C 30.98 . . 602 . 60 GLN HG2 H 2.482 . . 603 . 60 GLN HG3 H 2.286 . . 604 . 60 GLN NE2 N 111.13 . . 605 . 60 GLN HE21 H 7.685 . . 606 . 60 GLN HE22 H 6.588 . . 607 . 61 ILE H H 7.746 . . 608 . 61 ILE N N 120.69 . . 609 . 61 ILE CA C 64.25 . . 610 . 61 ILE CB C 36.25 . . 611 . 61 ILE HA H 3.615 . . 612 . 61 ILE HB H 1.674 . . 613 . 61 ILE CG1 C 27.97 . . 614 . 61 ILE HG12 H 1.864 . . 615 . 61 ILE HG13 H 0.518 . . 616 . 61 ILE CG2 C 15.65 . . 617 . 61 ILE HG2 H 1.056 . . 618 . 61 ILE CD1 C 10.80 . . 619 . 61 ILE HD1 H 0.465 . . 620 . 62 GLU H H 8.361 . . 621 . 62 GLU N N 118.71 . . 622 . 62 GLU CA C 56.85 . . 623 . 62 GLU CB C 26.28 . . 624 . 62 GLU HB3 H 1.674 . . 625 . 62 GLU HA H 4.080 . . 626 . 62 GLU HB2 H 1.952 . . 627 . 62 GLU CG C 34.91 . . 628 . 62 GLU HG2 H 2.590 . . 629 . 62 GLU HG3 H 2.460 . . 630 . 63 ALA H H 8.158 . . 631 . 63 ALA N N 122.11 . . 632 . 63 ALA CA C 51.82 . . 633 . 63 ALA CB C 15.58 . . 634 . 63 ALA HA H 4.028 . . 635 . 63 ALA HB H 1.369 . . 636 . 64 MET H H 7.438 . . 637 . 64 MET N N 114.74 . . 638 . 64 MET CA C 54.15 . . 639 . 64 MET CB C 31.64 . . 640 . 64 MET HB3 H 2.334 . . 641 . 64 MET HA H 4.158 . . 642 . 64 MET HB2 H 2.553 . . 643 . 64 MET CG C 30.18 . . 644 . 64 MET HG2 H 2.842 . . 645 . 64 MET HG3 H 2.550 . . 646 . 64 MET HE H 2.051 . . 647 . 65 GLY H H 7.736 . . 648 . 65 GLY N N 103.97 . . 649 . 65 GLY CA C 41.79 . . 650 . 65 GLY HA2 H 3.299 . . 651 . 65 GLY HA3 H 3.788 . . 652 . 66 PHE H H 6.700 . . 653 . 66 PHE N N 120.41 . . 654 . 66 PHE CA C 52.01 . . 655 . 66 PHE CB C 37.68 . . 656 . 66 PHE HB3 H 3.196 . . 657 . 66 PHE HA H 5.056 . . 658 . 66 PHE HB2 H 2.523 . . 659 . 66 PHE HD1 H 7.122 . . 660 . 66 PHE HD2 H 7.122 . . 661 . 67 PRO CA C 61.07 . . 662 . 67 PRO CB C 29.94 . . 663 . 67 PRO HB3 H 1.742 . . 664 . 67 PRO HA H 4.097 . . 665 . 67 PRO HB2 H 2.178 . . 666 . 67 PRO HD2 H 3.825 . . 667 . 67 PRO HD3 H 3.502 . . 668 . 67 PRO CG C 25.51 . . 669 . 67 PRO HG2 H 2.016 . . 670 . 67 PRO HG3 H 1.773 . . 671 . 68 ALA H H 7.960 . . 672 . 68 ALA N N 123.81 . . 673 . 68 ALA CA C 47.83 . . 674 . 68 ALA CB C 20.18 . . 675 . 68 ALA HA H 5.443 . . 676 . 68 ALA HB H 1.168 . . 677 . 69 PHE H H 8.630 . . 678 . 69 PHE N N 116.16 . . 679 . 69 PHE CA C 53.67 . . 680 . 69 PHE CB C 39.90 . . 681 . 69 PHE HB3 H 3.013 . . 682 . 69 PHE HA H 4.681 . . 683 . 69 PHE HB2 H 2.695 . . 684 . 69 PHE HD1 H 6.981 . . 685 . 69 PHE HD2 H 6.981 . . 686 . 69 PHE HE1 H 7.144 . . 687 . 69 PHE HE2 H 7.144 . . 688 . 70 VAL H H 8.963 . . 689 . 70 VAL N N 124.94 . . 690 . 70 VAL CA C 62.49 . . 691 . 70 VAL CB C 29.75 . . 692 . 70 VAL HA H 3.676 . . 693 . 70 VAL HB H 1.925 . . 694 . 70 VAL CG1 C 19.88 . . 695 . 70 VAL HG1 H 0.865 . . 696 . 70 VAL CG2 C 18.47 . . 697 . 70 VAL HG2 H 0.815 . . 698 . 71 LYS H H 8.694 . . 699 . 71 LYS N N 127.78 . . 700 . 71 LYS CA C 54.61 . . 701 . 71 LYS CB C 31.20 . . 702 . 71 LYS HB3 H 1.516 . . 703 . 71 LYS HA H 4.400 . . 704 . 71 LYS HB2 H 1.685 . . 705 . 71 LYS CD C 27.13 . . 706 . 71 LYS HD2 H 1.536 . . 707 . 71 LYS CG C 22.66 . . 708 . 71 LYS HG2 H 1.479 . . 709 . 71 LYS HG3 H 1.326 . . 710 . 71 LYS CE C 39.43 . . 711 . 71 LYS HE2 H 2.815 . . 712 . 72 LYS H H 7.966 . . 713 . 72 LYS N N 119.28 . . 714 . 72 LYS CA C 53.84 . . 715 . 72 LYS CB C 32.61 . . 716 . 72 LYS HA H 4.362 . . 717 . 72 LYS HB2 H 1.647 . . 718 . 72 LYS CD C 26.85 . . 719 . 72 LYS HD2 H 1.612 . . 720 . 72 LYS CG C 22.41 . . 721 . 72 LYS HG2 H 1.314 . . 722 . 72 LYS CE C 39.74 . . 723 . 72 LYS HE2 H 2.890 . . 724 . 73 ILE H H 8.375 . . 725 . 73 ILE N N 123.81 . . 726 . 73 ILE CA C 58.77 . . 727 . 73 ILE CB C 37.34 . . 728 . 73 ILE HA H 4.532 . . 729 . 73 ILE HB H 1.668 . . 730 . 73 ILE CG1 C 25.58 . . 731 . 73 ILE HG12 H 1.468 . . 732 . 73 ILE HG13 H 1.052 . . 733 . 73 ILE CG2 C 15.50 . . 734 . 73 ILE HG2 H 0.842 . . 735 . 73 ILE CD1 C 11.57 . . 736 . 73 ILE HD1 H 0.869 . . 737 . 74 GLU H H 8.934 . . 738 . 74 GLU N N 126.08 . . 739 . 74 GLU CA C 53.47 . . 740 . 74 GLU CB C 29.23 . . 741 . 74 GLU HB3 H 1.968 . . 742 . 74 GLU HA H 4.456 . . 743 . 74 GLU HB2 H 1.864 . . 744 . 74 GLU CG C 33.8 . . 745 . 74 GLU HG2 H 2.149 . . 746 . 75 GLY H H 8.496 . . 747 . 75 GLY N N 110.49 . . 748 . 75 GLY CA C 42.83 . . 749 . 75 GLY HA2 H 3.881 . . 750 . 75 GLY HA3 H 3.993 . . 751 . 76 ARG H H 7.761 . . 752 . 76 ARG N N 124.66 . . 753 . 76 ARG CA C 54.98 . . 754 . 76 ARG CB C 29.14 . . 755 . 76 ARG HB3 H 1.589 . . 756 . 76 ARG HA H 4.105 . . 757 . 76 ARG HB2 H 1.735 . . 758 . 76 ARG CG C 24.77 . . 759 . 76 ARG HG2 H 1.502 . . 760 . 76 ARG CD C 41.09 . . 761 . 76 ARG HD2 H 3.092 . . stop_ save_