data_5768 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Copper-CopAS46V from Bacillus subtilis ; _BMRB_accession_number 5768 _BMRB_flat_file_name bmr5768.str _Entry_type original _Submission_date 2003-04-11 _Accession_date 2003-04-11 _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 Ciofi-Baffoni S. . . 4 Gonnelli L. . . 5 Su X. C. . 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" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-08 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5769 'free form' stop_ _Original_release_date 2003-09-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Core Mutation Affecting the Folding Properties of a Soluble Domain of the ATPase Protein CopA from Bacillus subtilis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22770441 _PubMed_ID 12888353 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Ciofi-Baffoni S. . . 4 Gonnelli L. . . 5 Su X. C. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 331 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 473 _Page_last 484 _Year 2003 _Details . loop_ _Keyword CopA 'copper protein' folding mutation NMR 'P-type ATPase' stop_ save_ ################################## # Molecular system description # ################################## save_system_CopA _Saveframe_category molecular_system _Mol_system_name 'Potential copper-transporting ATPase' _Abbreviation_common CopA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CopA $CopA_mutation 'copper ion (I)' $CU1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CopA_mutation _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CPx-type ATPase CopA' _Name_variant S46V _Abbreviation_common CopA _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MLSEQKEIAMQVSGMTCAAC AARIEKGLKRMPGVTDANVN LATETVNVIYDPAETGTAAI QEKIEKLGYHVVIEGR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 SER 4 GLU 5 GLN 6 LYS 7 GLU 8 ILE 9 ALA 10 MET 11 GLN 12 VAL 13 SER 14 GLY 15 MET 16 THR 17 CYS 18 ALA 19 ALA 20 CYS 21 ALA 22 ALA 23 ARG 24 ILE 25 GLU 26 LYS 27 GLY 28 LEU 29 LYS 30 ARG 31 MET 32 PRO 33 GLY 34 VAL 35 THR 36 ASP 37 ALA 38 ASN 39 VAL 40 ASN 41 LEU 42 ALA 43 THR 44 GLU 45 THR 46 VAL 47 ASN 48 VAL 49 ILE 50 TYR 51 ASP 52 PRO 53 ALA 54 GLU 55 THR 56 GLY 57 THR 58 ALA 59 ALA 60 ILE 61 GLN 62 GLU 63 LYS 64 ILE 65 GLU 66 LYS 67 LEU 68 GLY 69 TYR 70 HIS 71 VAL 72 VAL 73 ILE 74 GLU 75 GLY 76 ARG stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 PDB 1OQ3 'A Core Mutation Affecting The Folding Properties Of A Soluble Domain Of The Atpase Protein Copa From Bacillus Subtilis' 98.68 76 100.00 100.00 6.78e-36 PDB 1OQ6 'Solution Structure Of Copper-S46v Copa From Bacillus Subtilis' 98.68 76 100.00 100.00 6.78e-36 BMRB 5769 'CPx-type ATPase CopA' 100.00 76 100.00 100.00 1.28e-36 PDB 1OPZ 'A Core Mutation Affecting The Folding Properties Of A Soluble Domain Of The Atpase Protein Copa From Bacillus Subtilis' 98.68 76 100.00 100.00 6.78e-36 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _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 16 11:21:40 2011 ; 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 _Strain _Gene_mnemonic $CopA_mutation 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis pLysS yvgX 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 $CopA_mutation '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 $CopA_mutation 1.2 mM [U-15N] phosphate 20 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task processing stop_ _Details Bruker save_ save_Xeasy _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'structure solution' stop_ _Details 'Xia, Bartels' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Gunter, Mumenthaler, Wuthrich' save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task refinement stop_ _Details 'Pearlman, Case, Caldwell, Ross, cheatham, Ferguson, Seibel, Singh, Weiner, Kollman.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ save_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HNHB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . 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' 20 . mM pH 7.0 0.1 n/a pressure 1 . atm temperature 298 0.1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TMS H 1 'methyl protons' ppm 0.00 external direct cylindrical external perpendicular 1.0 $entry_citation $entry_citation TMS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.10132912 $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 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CopA _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 SER N N 116.937 0.000 . 2 . 3 SER H H 8.270 0.000 . 3 . 3 SER HA H 4.346 0.000 . 4 . 3 SER HB2 H 3.746 0.001 . 5 . 4 GLU N N 122.747 0.000 . 6 . 4 GLU H H 8.384 0.000 . 7 . 4 GLU HA H 4.213 0.000 . 8 . 4 GLU HB2 H 1.902 0.000 . 9 . 4 GLU HB3 H 1.810 0.000 . 10 . 4 GLU HG2 H 2.119 0.000 . 11 . 4 GLU HG3 H 2.041 0.000 . 12 . 5 GLN N N 119.205 0.000 . 13 . 5 GLN H H 7.976 0.000 . 14 . 5 GLN HA H 4.406 0.000 . 15 . 5 GLN HB2 H 1.784 0.001 . 16 . 5 GLN HB3 H 1.647 0.000 . 17 . 5 GLN HG2 H 2.094 0.000 . 18 . 5 GLN HG3 H 2.015 0.000 . 19 . 5 GLN NE2 N 110.986 0.000 . 20 . 5 GLN HE21 H 7.311 0.001 . 21 . 5 GLN HE22 H 6.521 0.000 . 22 . 6 LYS N N 122.180 0.000 . 23 . 6 LYS H H 8.563 0.000 . 24 . 6 LYS HA H 4.377 0.000 . 25 . 6 LYS HB2 H 1.244 0.000 . 26 . 6 LYS HB3 H 0.640 0.000 . 27 . 6 LYS HG2 H 1.127 0.000 . 28 . 6 LYS HG3 H 1.084 0.000 . 29 . 6 LYS HD2 H 1.569 0.002 . 30 . 7 GLU N N 119.205 0.000 . 31 . 7 GLU H H 8.049 0.000 . 32 . 7 GLU HA H 5.489 0.004 . 33 . 7 GLU HB2 H 1.827 0.002 . 34 . 7 GLU HB3 H 1.749 0.000 . 35 . 7 GLU HG2 H 2.000 0.002 . 36 . 8 ILE N N 121.848 0.012 . 37 . 8 ILE H H 9.094 0.001 . 38 . 8 ILE HA H 4.701 0.000 . 39 . 8 ILE HB H 1.854 0.000 . 40 . 8 ILE HG2 H 0.880 0.002 . 41 . 8 ILE HG12 H 1.405 0.000 . 42 . 8 ILE HD1 H 1.077 0.000 . 43 . 9 ALA N N 127.282 0.000 . 44 . 9 ALA H H 8.154 0.000 . 45 . 9 ALA HA H 5.378 0.000 . 46 . 9 ALA HB H 1.159 0.000 . 47 . 10 MET N N 119.951 0.014 . 48 . 10 MET H H 8.903 0.000 . 49 . 10 MET HA H 4.613 0.000 . 50 . 10 MET HB2 H 1.789 0.000 . 51 . 10 MET HB3 H 1.619 0.000 . 52 . 10 MET HG2 H 2.383 0.001 . 53 . 10 MET HG3 H 2.181 0.001 . 54 . 11 GLN N N 123.977 0.016 . 55 . 11 GLN H H 8.903 0.000 . 56 . 11 GLN HA H 4.914 0.000 . 57 . 11 GLN HB2 H 2.003 0.002 . 58 . 11 GLN HG2 H 2.160 0.000 . 59 . 11 GLN NE2 N 111.269 0.000 . 60 . 11 GLN HE21 H 7.516 0.000 . 61 . 11 GLN HE22 H 6.837 0.001 . 62 . 12 VAL N N 123.597 0.000 . 63 . 12 VAL H H 8.439 0.000 . 64 . 12 VAL HA H 4.956 0.000 . 65 . 12 VAL HB H 1.550 0.000 . 66 . 12 VAL HG1 H 0.781 0.000 . 67 . 12 VAL HG2 H 0.666 0.001 . 68 . 13 SER N N 122.200 0.000 . 69 . 13 SER H H 9.448 0.000 . 70 . 13 SER HA H 4.819 0.004 . 71 . 13 SER HB2 H 3.842 0.000 . 72 . 13 SER HB3 H 3.698 0.000 . 73 . 14 GLY N N 109.002 0.000 . 74 . 14 GLY H H 8.546 0.000 . 75 . 14 GLY HA2 H 4.650 0.000 . 76 . 14 GLY HA3 H 3.651 0.000 . 77 . 15 MET N N 120.480 0.000 . 78 . 15 MET H H 9.178 0.000 . 79 . 15 MET HA H 4.751 0.000 . 80 . 15 MET HB2 H 2.485 0.000 . 81 . 15 MET HB3 H 1.300 0.000 . 82 . 15 MET HG2 H 2.022 0.009 . 83 . 15 MET HG3 H 1.664 0.000 . 84 . 16 THR N N 115.378 0.000 . 85 . 16 THR H H 9.109 0.002 . 86 . 16 THR HA H 4.474 0.000 . 87 . 16 THR HB H 3.213 0.000 . 88 . 16 THR HG2 H 1.097 0.000 . 89 . 17 CYS N N 115.662 0.000 . 90 . 17 CYS H H 7.915 0.000 . 91 . 17 CYS HA H 4.870 0.000 . 92 . 17 CYS HB2 H 3.324 0.000 . 93 . 17 CYS HB3 H 3.116 0.000 . 94 . 19 ALA N N 124.022 0.000 . 95 . 19 ALA H H 9.120 0.000 . 96 . 19 ALA HA H 4.212 0.000 . 97 . 19 ALA HB H 1.436 0.004 . 98 . 20 CYS N N 122.605 0.000 . 99 . 20 CYS H H 8.133 0.000 . 100 . 20 CYS HA H 3.984 0.000 . 101 . 20 CYS HB2 H 3.201 0.005 . 102 . 20 CYS HB3 H 2.503 0.003 . 103 . 21 ALA N N 118.779 0.000 . 104 . 21 ALA H H 6.524 0.000 . 105 . 21 ALA HA H 3.699 0.000 . 106 . 21 ALA HB H 1.317 0.001 . 107 . 22 ALA N N 117.504 0.000 . 108 . 22 ALA H H 7.576 0.000 . 109 . 22 ALA HA H 4.071 0.000 . 110 . 22 ALA HB H 1.377 0.000 . 111 . 23 ARG N N 117.504 0.000 . 112 . 23 ARG H H 7.718 0.000 . 113 . 23 ARG HA H 3.946 0.000 . 114 . 23 ARG HB2 H 1.997 0.000 . 115 . 23 ARG HG2 H 1.824 0.000 . 116 . 23 ARG HG3 H 1.571 0.000 . 117 . 23 ARG HD2 H 3.319 0.001 . 118 . 24 ILE N N 119.913 0.000 . 119 . 24 ILE H H 7.664 0.000 . 120 . 24 ILE HA H 3.423 0.001 . 121 . 24 ILE HB H 1.520 0.000 . 122 . 24 ILE HG2 H 0.313 0.000 . 123 . 24 ILE HG12 H 0.854 0.000 . 124 . 24 ILE HG13 H 0.463 0.002 . 125 . 24 ILE HD1 H -0.092 0.000 . 126 . 25 GLU N N 118.354 0.000 . 127 . 25 GLU H H 8.272 0.000 . 128 . 25 GLU HA H 3.389 0.004 . 129 . 25 GLU HB2 H 2.041 0.000 . 130 . 25 GLU HB3 H 1.833 0.000 . 131 . 25 GLU HG2 H 2.445 0.000 . 132 . 26 LYS N N 115.469 0.000 . 133 . 26 LYS H H 8.242 0.000 . 134 . 26 LYS HA H 3.813 0.000 . 135 . 26 LYS HB2 H 1.801 0.000 . 136 . 26 LYS HB3 H 1.683 0.000 . 137 . 26 LYS HG2 H 1.304 0.000 . 138 . 26 LYS HD2 H 1.561 0.001 . 139 . 26 LYS HD3 H 1.484 0.009 . 140 . 26 LYS HE2 H 2.933 0.000 . 141 . 26 LYS HE3 H 2.845 0.000 . 142 . 27 GLY N N 104.325 0.000 . 143 . 27 GLY H H 7.767 0.000 . 144 . 27 GLY HA2 H 3.726 0.000 . 145 . 27 GLY HA3 H 3.439 0.000 . 146 . 28 LEU N N 119.953 0.011 . 147 . 28 LEU H H 8.221 0.000 . 148 . 28 LEU HA H 4.046 0.000 . 149 . 28 LEU HB2 H 1.650 0.000 . 150 . 28 LEU HB3 H 0.998 0.000 . 151 . 28 LEU HG H 1.108 0.000 . 152 . 28 LEU HD1 H 0.745 0.007 . 153 . 28 LEU HD2 H 0.480 0.002 . 154 . 29 LYS N N 114.642 0.000 . 155 . 29 LYS H H 7.969 0.000 . 156 . 29 LYS HA H 3.734 0.000 . 157 . 29 LYS HB2 H 1.826 0.002 . 158 . 29 LYS HB3 H 1.700 0.000 . 159 . 29 LYS HG2 H 1.458 0.000 . 160 . 29 LYS HD2 H 1.186 0.002 . 161 . 29 LYS HE2 H 3.344 0.000 . 162 . 29 LYS HE3 H 3.029 0.000 . 163 . 30 ARG N N 114.288 0.000 . 164 . 30 ARG H H 6.878 0.000 . 165 . 30 ARG HA H 4.236 0.000 . 166 . 30 ARG HB2 H 1.928 0.000 . 167 . 30 ARG HB3 H 1.675 0.000 . 168 . 30 ARG HG2 H 1.778 0.000 . 169 . 30 ARG HD2 H 3.088 0.002 . 170 . 31 MET N N 123.144 0.000 . 171 . 31 MET H H 7.768 0.000 . 172 . 31 MET HA H 4.448 0.000 . 173 . 31 MET HB2 H 2.048 0.001 . 174 . 31 MET HB3 H 2.126 0.000 . 175 . 31 MET HG2 H 2.633 0.001 . 176 . 31 MET HG3 H 2.460 0.000 . 177 . 32 PRO HA H 4.204 0.000 . 178 . 32 PRO HB2 H 2.247 0.000 . 179 . 32 PRO HB3 H 2.101 0.000 . 180 . 32 PRO HG2 H 1.923 0.000 . 181 . 32 PRO HG3 H 1.831 0.000 . 182 . 32 PRO HD2 H 4.011 0.005 . 183 . 32 PRO HD3 H 3.560 0.000 . 184 . 33 GLY N N 110.419 0.000 . 185 . 33 GLY H H 8.498 0.000 . 186 . 33 GLY HA2 H 4.145 0.000 . 187 . 33 GLY HA3 H 3.692 0.000 . 188 . 34 VAL N N 120.622 0.000 . 189 . 34 VAL H H 7.556 0.001 . 190 . 34 VAL HA H 4.048 0.000 . 191 . 34 VAL HB H 2.346 0.003 . 192 . 34 VAL HG1 H 0.746 0.000 . 193 . 34 VAL HG2 H 0.609 0.000 . 194 . 35 THR N N 124.916 0.000 . 195 . 35 THR H H 9.112 0.000 . 196 . 35 THR HA H 4.128 0.000 . 197 . 35 THR HB H 3.769 0.000 . 198 . 35 THR HG2 H 1.017 0.000 . 199 . 36 ASP N N 117.945 0.007 . 200 . 36 ASP H H 8.004 0.000 . 201 . 36 ASP HA H 4.617 0.000 . 202 . 36 ASP HB2 H 2.524 0.002 . 203 . 36 ASP HB3 H 2.272 0.000 . 204 . 37 ALA N N 121.047 0.000 . 205 . 37 ALA H H 8.155 0.000 . 206 . 37 ALA HA H 5.110 0.000 . 207 . 37 ALA HB H 1.122 0.000 . 208 . 38 ASN N N 117.235 0.008 . 209 . 38 ASN H H 8.708 0.000 . 210 . 38 ASN HA H 4.947 0.000 . 211 . 38 ASN HB2 H 2.477 0.000 . 212 . 38 ASN ND2 N 114.245 0.000 . 213 . 38 ASN HD21 H 7.586 0.002 . 214 . 38 ASN HD22 H 6.646 0.002 . 215 . 39 VAL N N 126.006 0.000 . 216 . 39 VAL H H 9.783 0.000 . 217 . 39 VAL HA H 4.346 0.000 . 218 . 39 VAL HB H 1.848 0.000 . 219 . 39 VAL HG1 H 0.840 0.004 . 220 . 39 VAL HG2 H 0.581 0.000 . 221 . 40 ASN N N 126.715 0.000 . 222 . 40 ASN H H 8.919 0.000 . 223 . 40 ASN HA H 4.777 0.000 . 224 . 40 ASN HB2 H 3.040 0.005 . 225 . 40 ASN HB3 H 2.394 0.000 . 226 . 40 ASN ND2 N 111.926 0.000 . 227 . 40 ASN HD21 H 7.353 0.000 . 228 . 40 ASN HD22 H 6.842 0.000 . 229 . 41 LEU N N 125.388 0.000 . 230 . 41 LEU H H 8.768 0.000 . 231 . 41 LEU HA H 3.721 0.000 . 232 . 41 LEU HB2 H 1.512 0.000 . 233 . 41 LEU HB3 H 1.436 0.000 . 234 . 41 LEU HG H 1.395 0.000 . 235 . 41 LEU HD1 H 0.635 0.000 . 236 . 41 LEU HD2 H 0.553 0.000 . 237 . 42 ALA N N 119.488 0.000 . 238 . 42 ALA H H 8.027 0.000 . 239 . 42 ALA HA H 4.051 0.000 . 240 . 42 ALA HB H 1.410 0.000 . 241 . 43 THR N N 104.184 0.000 . 242 . 43 THR H H 7.208 0.000 . 243 . 43 THR HA H 4.340 0.002 . 244 . 43 THR HB H 4.419 0.000 . 245 . 43 THR HG2 H 0.959 0.000 . 246 . 44 GLU N N 119.913 0.000 . 247 . 44 GLU H H 7.759 0.000 . 248 . 44 GLU HA H 3.368 0.000 . 249 . 44 GLU HB2 H 2.429 0.006 . 250 . 44 GLU HB3 H 2.210 0.000 . 251 . 44 GLU HG2 H 2.049 0.000 . 252 . 45 THR N N 110.034 0.010 . 253 . 45 THR H H 7.624 0.000 . 254 . 45 THR HA H 5.077 0.002 . 255 . 45 THR HB H 3.610 0.000 . 256 . 45 THR HG2 H 0.949 0.000 . 257 . 46 VAL N N 124.798 0.000 . 258 . 46 VAL H H 9.245 0.000 . 259 . 46 VAL HA H 4.526 0.007 . 260 . 46 VAL HB H 1.652 0.000 . 261 . 46 VAL HG1 H 0.955 0.000 . 262 . 46 VAL HG2 H 0.555 0.000 . 263 . 47 ASN N N 126.573 0.000 . 264 . 47 ASN H H 8.732 0.000 . 265 . 47 ASN HA H 5.511 0.004 . 266 . 47 ASN HB2 H 2.523 0.000 . 267 . 47 ASN ND2 N 112.119 0.000 . 268 . 47 ASN HD21 H 7.433 0.000 . 269 . 47 ASN HD22 H 6.780 0.000 . 270 . 48 VAL N N 124.164 0.000 . 271 . 48 VAL H H 9.150 0.000 . 272 . 48 VAL HA H 4.629 0.000 . 273 . 48 VAL HB H 1.866 0.000 . 274 . 48 VAL HG1 H 0.994 0.001 . 275 . 48 VAL HG2 H 0.730 0.007 . 276 . 49 ILE N N 127.707 0.000 . 277 . 49 ILE H H 8.452 0.000 . 278 . 49 ILE HA H 5.121 0.003 . 279 . 49 ILE HB H 1.460 0.000 . 280 . 49 ILE HG2 H 0.746 0.000 . 281 . 49 ILE HG12 H 0.884 0.003 . 282 . 49 ILE HD1 H 0.674 0.000 . 283 . 50 TYR N N 124.325 0.000 . 284 . 50 TYR H H 9.311 0.000 . 285 . 50 TYR HA H 5.490 0.000 . 286 . 50 TYR HB2 H 2.646 0.000 . 287 . 50 TYR HB3 H 2.469 0.000 . 288 . 50 TYR HD1 H 6.500 0.002 . 289 . 50 TYR HE1 H 6.392 0.000 . 290 . 51 ASP N N 119.205 0.000 . 291 . 51 ASP H H 8.847 0.000 . 292 . 51 ASP HA H 5.004 0.000 . 293 . 51 ASP HB2 H 2.956 0.001 . 294 . 51 ASP HB3 H 2.474 0.000 . 295 . 52 PRO HA H 5.081 0.000 . 296 . 52 PRO HB2 H 2.141 0.000 . 297 . 52 PRO HG2 H 1.915 0.002 . 298 . 52 PRO HG3 H 1.681 0.000 . 299 . 52 PRO HD2 H 4.022 0.004 . 300 . 52 PRO HD3 H 3.563 0.003 . 301 . 53 ALA N N 120.901 0.000 . 302 . 53 ALA H H 8.548 0.000 . 303 . 53 ALA HA H 4.240 0.000 . 304 . 53 ALA HB H 1.380 0.000 . 305 . 54 GLU N N 115.477 0.019 . 306 . 54 GLU H H 7.742 0.000 . 307 . 54 GLU HA H 4.403 0.000 . 308 . 54 GLU HB2 H 1.930 0.000 . 309 . 54 GLU HB3 H 1.758 0.000 . 310 . 54 GLU HG2 H 2.116 0.000 . 311 . 55 THR N N 114.055 0.011 . 312 . 55 THR H H 8.008 0.000 . 313 . 55 THR HA H 4.486 0.001 . 314 . 55 THR HB H 4.127 0.000 . 315 . 55 THR HG2 H 0.864 0.000 . 316 . 55 THR HG1 H 5.352 0.000 . 317 . 56 GLY N N 104.959 0.000 . 318 . 56 GLY H H 7.896 0.003 . 319 . 56 GLY HA2 H 4.138 0.000 . 320 . 56 GLY HA3 H 3.878 0.000 . 321 . 57 THR N N 110.037 0.000 . 322 . 57 THR H H 8.191 0.000 . 323 . 57 THR HA H 3.312 0.002 . 324 . 57 THR HB H 3.968 0.000 . 325 . 57 THR HG2 H 1.076 0.000 . 326 . 58 ALA N N 124.207 0.000 . 327 . 58 ALA H H 8.366 0.000 . 328 . 58 ALA HA H 3.994 0.000 . 329 . 58 ALA HB H 1.267 0.000 . 330 . 59 ALA N N 120.664 0.000 . 331 . 59 ALA H H 7.675 0.000 . 332 . 59 ALA HB H 1.291 0.000 . 333 . 60 ILE N N 120.313 0.009 . 334 . 60 ILE H H 7.473 0.000 . 335 . 60 ILE HA H 3.215 0.000 . 336 . 60 ILE HB H 1.462 0.000 . 337 . 60 ILE HG2 H 0.473 0.000 . 338 . 60 ILE HG12 H 1.785 0.002 . 339 . 60 ILE HG13 H 0.639 0.000 . 340 . 60 ILE HD1 H -0.059 0.003 . 341 . 61 GLN N N 118.067 0.001 . 342 . 61 GLN H H 8.208 0.000 . 343 . 61 GLN HA H 3.636 0.000 . 344 . 61 GLN HB2 H 2.008 0.000 . 345 . 61 GLN HG2 H 2.286 0.000 . 346 . 61 GLN HG3 H 2.138 0.000 . 347 . 61 GLN NE2 N 109.143 0.000 . 348 . 61 GLN HE21 H 7.186 0.000 . 349 . 61 GLN HE22 H 6.564 0.001 . 350 . 62 GLU N N 117.476 0.000 . 351 . 62 GLU H H 8.017 0.000 . 352 . 62 GLU HA H 3.956 0.004 . 353 . 62 GLU HB2 H 2.069 0.000 . 354 . 62 GLU HB3 H 1.982 0.000 . 355 . 62 GLU HG2 H 2.282 0.000 . 356 . 63 LYS N N 119.602 0.000 . 357 . 63 LYS H H 7.632 0.000 . 358 . 63 LYS HA H 3.964 0.006 . 359 . 63 LYS HB2 H 1.964 0.001 . 360 . 63 LYS HB3 H 1.803 0.001 . 361 . 63 LYS HG2 H 1.472 0.000 . 362 . 63 LYS HG3 H 1.093 0.005 . 363 . 63 LYS HD2 H 1.600 0.001 . 364 . 63 LYS HE2 H 2.799 0.002 . 365 . 63 LYS HE3 H 2.666 0.000 . 366 . 64 ILE N N 117.712 0.000 . 367 . 64 ILE H H 7.535 0.000 . 368 . 64 ILE HA H 3.329 0.001 . 369 . 64 ILE HB H 1.843 0.000 . 370 . 64 ILE HG2 H 0.627 0.000 . 371 . 64 ILE HG12 H 0.885 0.000 . 372 . 64 ILE HG13 H 0.750 0.002 . 373 . 64 ILE HD1 H 0.684 0.000 . 374 . 65 GLU N N 118.185 0.000 . 375 . 65 GLU H H 7.896 0.000 . 376 . 65 GLU HA H 4.629 0.000 . 377 . 65 GLU HB2 H 2.128 0.004 . 378 . 65 GLU HB3 H 1.982 0.003 . 379 . 65 GLU HG2 H 2.462 0.000 . 380 . 65 GLU HG3 H 2.329 0.000 . 381 . 66 LYS N N 122.557 0.011 . 382 . 66 LYS H H 8.660 0.000 . 383 . 66 LYS HA H 3.969 0.000 . 384 . 66 LYS HB2 H 1.965 0.000 . 385 . 66 LYS HB3 H 1.832 0.002 . 386 . 66 LYS HG2 H 1.452 0.000 . 387 . 66 LYS HD2 H 1.546 0.002 . 388 . 66 LYS HE2 H 2.881 0.000 . 389 . 66 LYS HE3 H 2.832 0.000 . 390 . 67 LEU N N 118.303 0.000 . 391 . 67 LEU H H 7.853 0.000 . 392 . 67 LEU HA H 4.149 0.000 . 393 . 67 LEU HB2 H 2.223 0.001 . 394 . 67 LEU HB3 H 1.495 0.000 . 395 . 67 LEU HG H 1.926 0.002 . 396 . 67 LEU HD1 H 0.779 0.000 . 397 . 67 LEU HD2 H 0.753 0.000 . 398 . 68 GLY N N 104.132 0.000 . 399 . 68 GLY H H 7.647 0.000 . 400 . 68 GLY HA2 H 3.870 0.000 . 401 . 68 GLY HA3 H 3.361 0.000 . 402 . 69 TYR N N 119.720 0.000 . 403 . 69 TYR H H 7.166 0.000 . 404 . 69 TYR HA H 4.578 0.000 . 405 . 69 TYR HB2 H 3.083 0.000 . 406 . 69 TYR HB3 H 2.189 0.000 . 407 . 69 TYR HD1 H 6.691 0.002 . 408 . 69 TYR HE1 H 6.697 0.000 . 409 . 70 HIS N N 114.996 0.000 . 410 . 70 HIS H H 7.694 0.000 . 411 . 70 HIS HA H 5.067 0.000 . 412 . 70 HIS HB2 H 3.022 0.000 . 413 . 70 HIS HB3 H 2.886 0.000 . 414 . 71 VAL N N 125.034 0.000 . 415 . 71 VAL H H 8.856 0.000 . 416 . 71 VAL HA H 4.367 0.000 . 417 . 71 VAL HB H 1.852 0.000 . 418 . 71 VAL HG1 H 0.887 0.001 . 419 . 71 VAL HG2 H 0.784 0.001 . 420 . 72 VAL N N 128.340 0.000 . 421 . 72 VAL H H 8.454 0.000 . 422 . 72 VAL HA H 3.824 0.000 . 423 . 72 VAL HB H 1.758 0.003 . 424 . 72 VAL HG1 H 0.773 0.000 . 425 . 72 VAL HG2 H 0.695 0.000 . 426 . 73 ILE N N 126.715 0.000 . 427 . 73 ILE H H 8.197 0.000 . 428 . 73 ILE HA H 4.160 0.001 . 429 . 73 ILE HB H 1.734 0.000 . 430 . 73 ILE HG2 H 0.779 0.000 . 431 . 73 ILE HG12 H 1.341 0.000 . 432 . 73 ILE HG13 H 1.056 0.000 . 433 . 73 ILE HD1 H 0.711 0.002 . 434 . 74 GLU N N 125.742 0.000 . 435 . 74 GLU H H 8.548 0.002 . 436 . 74 GLU HA H 4.156 0.000 . 437 . 74 GLU HB2 H 1.959 0.002 . 438 . 74 GLU HB3 H 1.875 0.001 . 439 . 74 GLU HG2 H 2.168 0.000 . 440 . 75 GLY N N 110.273 0.000 . 441 . 75 GLY H H 8.438 0.000 . 442 . 75 GLY HA2 H 3.840 0.000 . 443 . 75 GLY HA3 H 3.775 0.000 . 444 . 76 ARG N N 125.273 0.008 . 445 . 76 ARG H H 7.720 0.000 . 446 . 76 ARG HA H 4.140 0.000 . 447 . 76 ARG HB2 H 1.762 0.000 . 448 . 76 ARG HB3 H 1.620 0.000 . 449 . 76 ARG HG2 H 1.487 0.000 . 450 . 76 ARG HD2 H 3.078 0.000 . stop_ save_