data_5213 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ ; _BMRB_accession_number 5213 _BMRB_flat_file_name bmr5213.str _Entry_type original _Submission_date 2001-11-20 _Accession_date 2001-11-20 _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 Markey J. . . 5 Ruiz-Duenas J. F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 373 "15N chemical shifts" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-02-14 original BMRB . stop_ _Original_release_date 2001-11-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21614397 _PubMed_ID 11747441 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 Markey J. . . 5 Ruiz-Duenas F. J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 15660 _Page_last 15668 _Year 2001 _Details . loop_ _Keyword beta-alpha-beta-beta-alpha-beta stop_ save_ ################################## # Molecular system description # ################################## save_system_CopZ _Saveframe_category molecular_system _Mol_system_name 'CopZ from Bacillus subtilis' _Abbreviation_common CopZ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CopZ from Bacillus subtilis' $CopZ 'COPPER (I) ION' $entity_CU1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'copper-transport in Bacillus subtilis' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CopZ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CopZ from Bacillus subtilis' _Abbreviation_common CopZ _Molecular_mass 7826 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; MEQKTLQVEGMSCQHCVKAV ETSVGELDGVSAVHVNLEAG KVDVSFDADKVSVKDIADAI EDQGYDVAKIEGR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLN 4 LYS 5 THR 6 LEU 7 GLN 8 VAL 9 GLU 10 GLY 11 MET 12 SER 13 CYS 14 GLN 15 HIS 16 CYS 17 VAL 18 LYS 19 ALA 20 VAL 21 GLU 22 THR 23 SER 24 VAL 25 GLY 26 GLU 27 LEU 28 ASP 29 GLY 30 VAL 31 SER 32 ALA 33 VAL 34 HIS 35 VAL 36 ASN 37 LEU 38 GLU 39 ALA 40 GLY 41 LYS 42 VAL 43 ASP 44 VAL 45 SER 46 PHE 47 ASP 48 ALA 49 ASP 50 LYS 51 VAL 52 SER 53 VAL 54 LYS 55 ASP 56 ILE 57 ALA 58 ASP 59 ALA 60 ILE 61 GLU 62 ASP 63 GLN 64 GLY 65 TYR 66 ASP 67 VAL 68 ALA 69 LYS 70 ILE 71 GLU 72 GLY 73 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'COPPER (I) ION' _BMRB_code CU1 _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 1 . ? 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 $CopZ 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $CopZ 'recombinant technology' 'B. subtilis' Bacillus subtilis . plasmid pET21 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 $CopZ 2 mM '[U-99% 15N]' $entity_CU1 2 mM . 'phosphate buffer' 100 mM . DTT trace mM . D2O 10 % . H2O 90 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CopZ 2 mM . $entity_CU1 2 mM . 'phosphate buffer' 100 mM . DTT trace mM . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'solution structure calculation' stop_ _Details 'Guenter et al. 1997' save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task 'NMR experiments collection' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details 'Eccles et al. 1991' save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task 'solution structure refinement' stop_ _Details 'Pearlman et al. 1997' save_ save_molmol _Saveframe_category software _Name Molmol _Version 2.4 loop_ _Task 'data analysis' stop_ _Details 'Koradi et al. 1996' save_ save_CORMA _Saveframe_category software _Name CORMA _Version . loop_ _Task 'data analysis' stop_ _Details 'Borgias et al. 1989' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_TOSCY-HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOSCY-HMQC' _Sample_label . save_ save_3D_NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _Sample_label . save_ save_3D_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_2D_TOSCY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOSCY' _Sample_label . save_ save_2D_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details 'The samples were kept under reduction conditions with DTT in an inert atmophere.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.01 na pressure 1 . atm temperature 300 0.5 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 TMS H 1 'methyl protons' ppm 0.0 . direct . . . 1.000000000 TMS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D TOSCY-HMQC' '3D NOESY-HSQC' '3D HNHA' '2D TOSCY' '2D NOESY' '2D HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CopZ from Bacillus subtilis' _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 MET HA H 4.047 0.05 1 2 . 1 MET HB2 H 1.901 0.05 1 3 . 1 MET HB3 H 1.910 0.05 1 4 . 1 MET HG2 H 2.401 0.05 1 5 . 1 MET HG3 H 2.410 0.05 1 6 . 2 GLU N N 124.775 0.05 1 7 . 2 GLU H H 8.774 0.05 1 8 . 2 GLU HA H 4.308 0.05 1 9 . 2 GLU HB2 H 1.910 0.05 1 10 . 2 GLU HB3 H 1.840 0.05 1 11 . 2 GLU HG2 H 1.140 0.05 1 12 . 2 GLU HG3 H 0.843 0.05 1 13 . 3 GLN N N 119.957 0.05 1 14 . 3 GLN H H 8.271 0.05 1 15 . 3 GLN HA H 5.462 0.05 1 16 . 3 GLN HB2 H 1.889 0.05 1 17 . 3 GLN HB3 H 1.785 0.05 1 18 . 3 GLN HG2 H 2.120 0.05 1 19 . 3 GLN HG3 H 2.208 0.05 1 20 . 4 LYS N N 122.366 0.05 1 21 . 4 LYS H H 8.845 0.05 1 22 . 4 LYS HA H 4.804 0.05 1 23 . 4 LYS HB2 H 1.726 0.05 1 24 . 4 LYS HB3 H 1.730 0.05 1 25 . 4 LYS HG2 H 1.255 0.05 2 26 . 4 LYS HG3 H 1.260 0.05 2 27 . 4 LYS HD2 H 1.450 0.05 1 28 . 5 THR N N 118.925 0.05 1 29 . 5 THR H H 8.716 0.05 1 30 . 5 THR HA H 5.187 0.05 1 31 . 5 THR HB H 3.640 0.05 1 32 . 5 THR HG2 H 1.070 0.05 1 33 . 6 LEU N N 126.496 0.05 1 34 . 6 LEU H H 9.696 0.05 1 35 . 6 LEU HA H 4.698 0.05 1 36 . 6 LEU HB2 H 2.915 0.05 1 37 . 6 LEU HB3 H 2.920 0.05 1 38 . 6 LEU HG H 2.513 0.05 1 39 . 7 GLN N N 125.808 0.05 1 40 . 7 GLN H H 9.159 0.05 1 41 . 7 GLN HA H 4.785 0.05 1 42 . 7 GLN HB2 H 1.926 0.05 1 43 . 7 GLN HB3 H 2.108 0.05 1 44 . 7 GLN HG2 H 2.257 0.05 1 45 . 7 GLN HG3 H 2.228 0.05 1 46 . 8 VAL N N 127.184 0.05 1 47 . 8 VAL H H 8.778 0.05 1 48 . 8 VAL HA H 4.966 0.05 1 49 . 8 VAL HB H 1.520 0.05 1 50 . 8 VAL HG1 H 0.810 0.05 1 51 . 8 VAL HG2 H 0.696 0.05 1 52 . 9 GLU N N 127.873 0.05 1 53 . 9 GLU H H 9.511 0.05 1 54 . 9 GLU HA H 4.688 0.05 1 55 . 9 GLU HB2 H 2.206 0.05 1 56 . 9 GLU HB3 H 2.112 0.05 1 57 . 9 GLU HG2 H 1.901 0.05 1 58 . 9 GLU HG3 H 1.910 0.05 1 59 . 10 GLY N N 108.257 0.05 1 60 . 10 GLY H H 8.499 0.05 1 61 . 10 GLY HA2 H 3.697 0.05 1 62 . 10 GLY HA3 H 3.700 0.05 1 63 . 11 MET N N 121.334 0.05 1 64 . 11 MET H H 8.926 0.05 1 65 . 11 MET HA H 4.716 0.05 1 66 . 11 MET HB2 H 2.209 0.05 1 67 . 11 MET HB3 H 2.156 0.05 1 68 . 11 MET HG2 H 1.789 0.05 1 69 . 11 MET HG3 H 1.205 0.05 1 70 . 11 MET HE H 3.163 0.05 1 71 . 12 SER N N 121.334 0.05 1 72 . 12 SER H H 8.040 0.05 1 73 . 12 SER HA H 5.133 0.05 1 74 . 12 SER HB2 H 3.410 0.05 1 75 . 12 SER HB3 H 3.391 0.05 1 76 . 12 SER HG H 4.201 0.05 1 77 . 13 CYS N N 118.925 0.05 1 78 . 13 CYS H H 10.196 0.05 1 79 . 13 CYS HA H 4.751 0.05 1 80 . 13 CYS HB2 H 3.410 0.05 1 81 . 13 CYS HB3 H 2.399 0.05 1 82 . 14 GLN N N 116.860 0.05 1 83 . 14 GLN H H 8.856 0.05 1 84 . 14 GLN HA H 3.934 0.05 1 85 . 14 GLN HB2 H 1.854 0.05 1 86 . 14 GLN HB3 H 1.861 0.05 1 87 . 14 GLN HG2 H 2.108 0.05 1 88 . 14 GLN HG3 H 2.120 0.05 1 89 . 15 HIS N N 123.399 0.05 1 90 . 15 HIS H H 9.444 0.05 1 91 . 15 HIS HA H 4.348 0.05 1 92 . 15 HIS HB2 H 3.175 0.05 1 93 . 15 HIS HB3 H 3.182 0.05 1 94 . 15 HIS HD2 H 7.730 0.05 1 95 . 15 HIS HE1 H 7.570 0.05 1 96 . 16 CYS N N 124.431 0.05 1 97 . 16 CYS H H 8.033 0.05 1 98 . 16 CYS HA H 4.197 0.05 1 99 . 16 CYS HB2 H 3.411 0.05 1 100 . 16 CYS HB3 H 2.715 0.05 1 101 . 17 VAL N N 116.516 0.05 1 102 . 17 VAL H H 7.040 0.05 1 103 . 17 VAL HA H 3.087 0.05 1 104 . 17 VAL HB H 2.117 0.05 1 105 . 17 VAL HG1 H 0.848 0.05 2 106 . 17 VAL HG2 H 0.716 0.05 2 107 . 18 LYS N N 116.860 0.05 1 108 . 18 LYS H H 7.583 0.05 1 109 . 18 LYS HA H 4.040 0.05 1 110 . 18 LYS HB2 H 1.799 0.05 1 111 . 18 LYS HB3 H 1.809 0.05 1 112 . 18 LYS HG2 H 1.395 0.05 1 113 . 18 LYS HG3 H 1.408 0.05 1 114 . 18 LYS HD2 H 1.600 0.05 1 115 . 18 LYS HD3 H 1.580 0.05 1 116 . 18 LYS HE2 H 4.130 0.05 1 117 . 18 LYS HE3 H 4.141 0.05 1 118 . 18 LYS NZ N 124.090 0.05 1 119 . 18 LYS HZ H 8.390 0.05 1 120 . 19 ALA N N 123.399 0.05 1 121 . 19 ALA H H 8.028 0.05 1 122 . 19 ALA HA H 4.016 0.05 1 123 . 19 ALA HB H 1.556 0.05 1 124 . 20 VAL N N 118.925 0.05 1 125 . 20 VAL H H 7.862 0.05 1 126 . 20 VAL HA H 3.335 0.05 1 127 . 20 VAL HB H 1.860 0.05 1 128 . 20 VAL HG1 H 0.743 0.05 2 129 . 20 VAL HG2 H 0.550 0.05 2 130 . 21 GLU N N 117.893 0.05 1 131 . 21 GLU H H 8.776 0.05 1 132 . 21 GLU HA H 3.488 0.05 1 133 . 21 GLU HB2 H 2.075 0.05 1 134 . 21 GLU HB3 H 2.080 0.05 1 135 . 21 GLU HG2 H 2.374 0.05 1 136 . 21 GLU HG3 H 2.381 0.05 1 137 . 22 THR N N 113.419 0.05 1 138 . 22 THR H H 8.395 0.05 1 139 . 22 THR HA H 3.819 0.05 1 140 . 22 THR HB H 4.097 0.05 1 141 . 22 THR HG2 H 1.109 0.05 1 142 . 23 SER N N 115.484 0.05 1 143 . 23 SER H H 7.565 0.05 1 144 . 23 SER HA H 4.041 0.05 1 145 . 23 SER HB2 H 3.739 0.05 1 146 . 23 SER HB3 H 3.749 0.05 1 147 . 24 VAL N N 118.925 0.05 1 148 . 24 VAL H H 8.074 0.05 1 149 . 24 VAL HA H 3.454 0.05 1 150 . 24 VAL HB H 1.829 0.05 1 151 . 24 VAL HG1 H 0.709 0.05 1 152 . 24 VAL HG2 H 0.678 0.05 1 153 . 25 GLY N N 103.439 0.05 1 154 . 25 GLY H H 7.471 0.05 1 155 . 25 GLY HA2 H 3.705 0.05 1 156 . 25 GLY HA3 H 3.536 0.05 1 157 . 26 GLU N N 115.484 0.05 1 158 . 26 GLU H H 7.044 0.05 1 159 . 26 GLU HA H 4.087 0.05 1 160 . 26 GLU HB2 H 1.992 0.05 1 161 . 26 GLU HB3 H 1.909 0.05 1 162 . 26 GLU HG2 H 2.386 0.05 2 163 . 26 GLU HG3 H 2.247 0.05 2 164 . 27 LEU N N 120.907 0.05 1 165 . 27 LEU H H 7.278 0.05 1 166 . 27 LEU HA H 4.069 0.05 1 167 . 27 LEU HB2 H 1.942 0.05 2 168 . 27 LEU HB3 H 1.822 0.05 2 169 . 27 LEU HG H 1.080 0.05 1 170 . 27 LEU HD1 H 0.710 0.05 1 171 . 27 LEU HD2 H 0.648 0.05 1 172 . 28 ASP N N 125.119 0.05 1 173 . 28 ASP H H 8.445 0.05 1 174 . 28 ASP HA H 4.259 0.05 1 175 . 28 ASP HB2 H 2.598 0.05 2 176 . 28 ASP HB3 H 2.515 0.05 2 177 . 29 GLY N N 109.978 0.05 1 178 . 29 GLY H H 8.357 0.05 1 179 . 29 GLY HA2 H 4.423 0.05 2 180 . 29 GLY HA3 H 3.555 0.05 2 181 . 30 VAL N N 123.055 0.05 1 182 . 30 VAL H H 7.815 0.05 1 183 . 30 VAL HA H 4.031 0.05 1 184 . 30 VAL HB H 2.226 0.05 1 185 . 30 VAL HG1 H 0.765 0.05 1 186 . 30 VAL HG2 H 0.780 0.05 1 187 . 31 SER N N 123.399 0.05 1 188 . 31 SER H H 9.021 0.05 1 189 . 31 SER HA H 4.575 0.05 1 190 . 31 SER HB2 H 3.737 0.05 2 191 . 31 SER HB3 H 3.602 0.05 2 192 . 32 ALA N N 122.022 0.05 1 193 . 32 ALA H H 7.674 0.05 1 194 . 32 ALA HA H 4.543 0.05 1 195 . 32 ALA HB H 1.273 0.05 1 196 . 33 VAL N N 118.581 0.05 1 197 . 33 VAL H H 8.207 0.05 1 198 . 33 VAL HA H 4.789 0.05 1 199 . 33 VAL HB H 1.830 0.05 1 200 . 33 VAL HG1 H 0.688 0.05 1 201 . 33 VAL HG2 H 0.690 0.05 1 202 . 34 HIS N N 124.775 0.05 1 203 . 34 HIS H H 8.974 0.05 1 204 . 34 HIS HA H 4.965 0.05 1 205 . 34 HIS HB2 H 2.996 0.05 1 206 . 34 HIS HB3 H 3.010 0.05 1 207 . 34 HIS HD2 H 6.990 0.05 1 208 . 35 VAL N N 127.528 0.05 1 209 . 35 VAL H H 9.333 0.05 1 210 . 35 VAL HA H 4.232 0.05 1 211 . 35 VAL HB H 1.947 0.05 1 212 . 35 VAL HG1 H 0.808 0.05 2 213 . 35 VAL HG2 H 0.663 0.05 2 214 . 36 ASN N N 125.808 0.05 1 215 . 36 ASN H H 8.816 0.05 1 216 . 36 ASN HA H 4.773 0.05 1 217 . 36 ASN HB2 H 2.840 0.05 1 218 . 36 ASN HB3 H 2.588 0.05 1 219 . 37 LEU N N 125.464 0.05 1 220 . 37 LEU H H 8.688 0.05 1 221 . 37 LEU HA H 3.615 0.05 1 222 . 37 LEU HB2 H 1.571 0.05 1 223 . 37 LEU HB3 H 1.534 0.05 1 224 . 37 LEU HG H 1.228 0.05 1 225 . 37 LEU HD1 H 0.484 0.05 1 226 . 37 LEU HD2 H 0.508 0.05 1 227 . 38 GLU N N 118.581 0.05 1 228 . 38 GLU H H 8.581 0.05 1 229 . 38 GLU HA H 3.811 0.05 1 230 . 38 GLU HB2 H 2.009 0.05 2 231 . 38 GLU HB3 H 1.923 0.05 2 232 . 38 GLU HG2 H 2.240 0.05 1 233 . 38 GLU HG3 H 2.178 0.05 1 234 . 39 ALA N N 116.860 0.05 1 235 . 39 ALA H H 7.391 0.05 1 236 . 39 ALA HA H 4.300 0.05 1 237 . 39 ALA HB H 1.176 0.05 1 238 . 40 GLY N N 108.945 0.05 1 239 . 40 GLY H H 7.794 0.05 1 240 . 40 GLY HA2 H 3.969 0.05 2 241 . 40 GLY HA3 H 3.429 0.05 2 242 . 41 LYS N N 114.795 0.05 1 243 . 41 LYS H H 7.398 0.05 1 244 . 41 LYS HA H 5.203 0.05 1 245 . 41 LYS HB2 H 1.591 0.05 1 246 . 41 LYS HB3 H 1.438 0.05 1 247 . 41 LYS HG2 H 1.074 0.05 1 248 . 41 LYS HG3 H 1.081 0.05 1 249 . 41 LYS HD2 H 1.303 0.05 1 250 . 41 LYS HD3 H 1.307 0.05 1 251 . 42 VAL N N 122.366 0.05 1 252 . 42 VAL H H 9.153 0.05 1 253 . 42 VAL HA H 4.575 0.05 1 254 . 42 VAL HB H 1.933 0.05 1 255 . 42 VAL HG1 H 0.730 0.05 1 256 . 42 VAL HG2 H 0.540 0.05 1 257 . 43 ASP N N 129.249 0.05 1 258 . 43 ASP H H 9.207 0.05 1 259 . 43 ASP HA H 5.482 0.05 1 260 . 43 ASP HB2 H 2.581 0.05 1 261 . 43 ASP HB3 H 2.593 0.05 1 262 . 44 VAL N N 123.399 0.05 1 263 . 44 VAL H H 9.211 0.05 1 264 . 44 VAL HA H 4.976 0.05 1 265 . 44 VAL HB H 2.094 0.05 1 266 . 44 VAL HG1 H 0.986 0.05 1 267 . 44 VAL HG2 H 0.834 0.05 1 268 . 45 SER N N 122.711 0.05 1 269 . 45 SER H H 8.779 0.05 1 270 . 45 SER HA H 5.784 0.05 1 271 . 45 SER HB2 H 3.728 0.05 1 272 . 45 SER HB3 H 3.761 0.05 1 273 . 46 PHE N N 122.022 0.05 1 274 . 46 PHE H H 9.148 0.05 1 275 . 46 PHE HA H 5.342 0.05 1 276 . 46 PHE HB2 H 2.818 0.05 1 277 . 46 PHE HB3 H 2.504 0.05 1 278 . 46 PHE HD1 H 6.782 0.05 1 279 . 46 PHE HE1 H 7.020 0.05 1 280 . 46 PHE HZ H 7.150 0.05 1 281 . 47 ASP N N 118.925 0.05 1 282 . 47 ASP H H 8.340 0.05 1 283 . 47 ASP HA H 4.658 0.05 1 284 . 47 ASP HB2 H 2.868 0.05 1 285 . 47 ASP HB3 H 2.542 0.05 1 286 . 48 ALA N N 129.593 0.05 1 287 . 48 ALA H H 8.626 0.05 1 288 . 48 ALA HA H 5.075 0.05 1 289 . 48 ALA HB H 1.417 0.05 1 290 . 49 ASP N N 115.828 0.05 1 291 . 49 ASP H H 8.486 0.05 1 292 . 49 ASP HA H 4.530 0.05 1 293 . 49 ASP HB2 H 2.712 0.05 1 294 . 49 ASP HB3 H 2.568 0.05 1 295 . 50 LYS N N 117.549 0.05 1 296 . 50 LYS H H 7.837 0.05 1 297 . 50 LYS HA H 4.318 0.05 1 298 . 50 LYS HB2 H 1.787 0.05 1 299 . 50 LYS HB3 H 1.698 0.05 1 300 . 50 LYS HG2 H 1.247 0.05 1 301 . 50 LYS HG3 H 1.256 0.05 1 302 . 50 LYS HD2 H 1.474 0.05 1 303 . 50 LYS HD3 H 1.464 0.05 1 304 . 51 VAL N N 120.302 0.05 1 305 . 51 VAL H H 8.142 0.05 1 306 . 51 VAL HA H 4.371 0.05 1 307 . 51 VAL HB H 2.292 0.05 1 308 . 51 VAL HG1 H 0.964 0.05 1 309 . 51 VAL HG2 H 0.720 0.05 1 310 . 52 SER N N 117.893 0.05 1 311 . 52 SER H H 8.291 0.05 1 312 . 52 SER HA H 5.112 0.05 1 313 . 52 SER HB2 H 4.177 0.05 1 314 . 52 SER HB3 H 3.833 0.05 1 315 . 53 VAL N N 116.860 0.05 1 316 . 53 VAL H H 8.597 0.05 1 317 . 53 VAL HA H 3.472 0.05 1 318 . 53 VAL HB H 2.091 0.05 1 319 . 53 VAL HG1 H 1.057 0.05 2 320 . 53 VAL HG2 H 1.001 0.05 2 321 . 54 LYS N N 119.613 0.05 1 322 . 54 LYS H H 7.714 0.05 1 323 . 54 LYS HA H 3.934 0.05 1 324 . 54 LYS HB2 H 1.640 0.05 1 325 . 54 LYS HB3 H 1.714 0.05 1 326 . 54 LYS HG2 H 1.327 0.05 1 327 . 54 LYS HG3 H 1.337 0.05 1 328 . 54 LYS HD2 H 1.470 0.05 1 329 . 54 LYS HD3 H 1.480 0.05 1 330 . 55 ASP N N 118.237 0.05 1 331 . 55 ASP H H 7.496 0.05 1 332 . 55 ASP HA H 4.080 0.05 1 333 . 55 ASP HB2 H 2.940 0.05 1 334 . 55 ASP HB3 H 2.441 0.05 1 335 . 56 ILE N N 119.613 0.05 1 336 . 56 ILE H H 7.321 0.05 1 337 . 56 ILE HA H 3.117 0.05 1 338 . 56 ILE HB H 1.396 0.05 1 339 . 56 ILE HG2 H -0.021 0.05 1 340 . 56 ILE HG12 H 0.205 0.05 1 341 . 56 ILE HG13 H 0.216 0.05 1 342 . 56 ILE HD1 H -0.238 0.05 1 343 . 57 ALA N N 120.990 0.05 1 344 . 57 ALA H H 8.229 0.05 1 345 . 57 ALA HA H 3.597 0.05 1 346 . 57 ALA HB H 1.446 0.05 1 347 . 58 ASP N N 116.860 0.05 1 348 . 58 ASP H H 8.753 0.05 1 349 . 58 ASP HA H 4.172 0.05 1 350 . 58 ASP HB2 H 2.692 0.05 1 351 . 58 ASP HB3 H 2.540 0.05 1 352 . 59 ALA N N 121.678 0.05 1 353 . 59 ALA H H 7.408 0.05 1 354 . 59 ALA HA H 4.070 0.05 1 355 . 59 ALA HB H 1.302 0.05 1 356 . 60 ILE N N 118.237 0.05 1 357 . 60 ILE H H 7.554 0.05 1 358 . 60 ILE HA H 3.330 0.05 1 359 . 60 ILE HB H 1.714 0.05 1 360 . 60 ILE HG12 H 0.701 0.05 1 361 . 60 ILE HG13 H 0.710 0.05 1 362 . 60 ILE HG2 H 0.352 0.05 1 363 . 60 ILE HD1 H 0.116 0.05 1 364 . 61 GLU N N 119.269 0.05 1 365 . 61 GLU H H 8.578 0.05 1 366 . 61 GLU HA H 4.607 0.05 1 367 . 61 GLU HB2 H 2.012 0.05 1 368 . 61 GLU HB3 H 2.021 0.05 1 369 . 61 GLU HG2 H 2.699 0.05 1 370 . 61 GLU HG3 H 2.508 0.05 1 371 . 62 ASP N N 121.334 0.05 1 372 . 62 ASP H H 8.596 0.05 1 373 . 62 ASP HA H 4.383 0.05 1 374 . 62 ASP HB2 H 2.766 0.05 2 375 . 62 ASP HB3 H 2.530 0.05 2 376 . 63 GLN N N 114.107 0.05 1 377 . 63 GLN H H 7.308 0.05 1 378 . 63 GLN HA H 4.124 0.05 1 379 . 63 GLN HB2 H 2.194 0.05 1 380 . 63 GLN HB3 H 2.183 0.05 1 381 . 63 GLN HG2 H 2.680 0.05 1 382 . 63 GLN HG3 H 2.690 0.05 1 383 . 63 GLN HE21 H 6.690 0.05 1 384 . 63 GLN HE22 H 6.810 0.05 1 385 . 64 GLY N N 104.816 0.05 1 386 . 64 GLY H H 7.819 0.05 1 387 . 64 GLY HA2 H 3.785 0.05 1 388 . 64 GLY HA3 H 3.433 0.05 1 389 . 65 TYR N N 119.269 0.05 1 390 . 65 TYR H H 6.451 0.05 1 391 . 65 TYR HA H 4.744 0.05 1 392 . 65 TYR HB2 H 3.089 0.05 1 393 . 65 TYR HB3 H 2.088 0.05 1 394 . 65 TYR HE1 H 6.810 0.05 1 395 . 65 TYR HD1 H 6.680 0.05 1 396 . 66 ASP N N 118.237 0.05 1 397 . 66 ASP H H 7.972 0.05 1 398 . 66 ASP HA H 4.957 0.05 1 399 . 66 ASP HB2 H 2.516 0.05 1 400 . 66 ASP HB3 H 2.391 0.05 1 401 . 67 VAL N N 124.431 0.05 1 402 . 67 VAL H H 9.475 0.05 1 403 . 67 VAL HA H 4.334 0.05 1 404 . 67 VAL HB H 2.118 0.05 1 405 . 67 VAL HG1 H 0.998 0.05 1 406 . 67 VAL HG2 H 0.959 0.05 1 407 . 68 ALA N N 132.002 0.05 1 408 . 68 ALA H H 8.797 0.05 1 409 . 68 ALA HA H 4.259 0.05 1 410 . 68 ALA HB H 1.277 0.05 1 411 . 69 LYS N N 115.828 0.05 1 412 . 69 LYS H H 7.720 0.05 1 413 . 69 LYS HA H 4.280 0.05 1 414 . 69 LYS HB2 H 1.670 0.05 1 415 . 69 LYS HB3 H 1.680 0.05 1 416 . 69 LYS HG2 H 1.284 0.05 1 417 . 69 LYS HG3 H 1.289 0.05 1 418 . 69 LYS HD2 H 1.530 0.05 1 419 . 69 LYS HD3 H 1.540 0.05 1 420 . 70 ILE N N 123.399 0.05 1 421 . 70 ILE H H 8.276 0.05 1 422 . 70 ILE HA H 4.202 0.05 1 423 . 70 ILE HB H 1.466 0.05 1 424 . 70 ILE HG12 H 0.647 0.05 1 425 . 70 ILE HG13 H 0.656 0.05 1 426 . 70 ILE HG2 H 0.338 0.05 1 427 . 71 GLU N N 126.152 0.05 1 428 . 71 GLU H H 8.696 0.05 1 429 . 71 GLU HA H 4.359 0.05 1 430 . 71 GLU HB2 H 1.945 0.05 2 431 . 71 GLU HB3 H 1.848 0.05 2 432 . 71 GLU HG2 H 2.093 0.05 1 433 . 71 GLU HG3 H 2.085 0.05 1 434 . 72 GLY N N 109.978 0.05 1 435 . 72 GLY H H 8.469 0.05 1 436 . 72 GLY HA2 H 4.012 0.05 2 437 . 72 GLY HA3 H 3.942 0.05 2 438 . 73 ARG N N 125.808 0.05 1 439 . 73 ARG H H 7.885 0.05 1 440 . 73 ARG HA H 4.059 0.05 1 441 . 73 ARG HB2 H 1.748 0.05 1 442 . 73 ARG HB3 H 1.592 0.05 1 443 . 73 ARG HG2 H 1.476 0.05 1 444 . 73 ARG HG3 H 1.486 0.05 1 445 . 73 ARG HD2 H 3.068 0.05 1 446 . 73 ARG HD3 H 3.077 0.05 1 stop_ save_