data_7068 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure and intermolecular interactions of the Copper form of third metal-binding domain of ATP7A, the menkes disease protein ; _BMRB_accession_number 7068 _BMRB_flat_file_name bmr7068.str _Entry_type original _Submission_date 2006-04-10 _Accession_date 2006-04-12 _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 Cantini F. . . 4 DellaMalva N. . . 5 Rosato A. . . 6 Herrmann T. . . 7 Wuthrich K. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 424 "13C chemical shifts" 243 "15N chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-09-07 original author 'original release' 2008-07-07 update BMRB 'update entry citation' stop_ loop_ _Related_BMRB_accession_number _Relationship 7069 'Copper-transporting ATPase 1 (E.C.3.6.3.4)' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16873374 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Cantini F. . . 4 DellaMalva N. . . 5 Herrmann T. . . 6 Rosato A. . . 7 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 281 _Journal_issue 39 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 29141 _Page_last 29147 _Year 2006 _Details . loop_ _Keyword copper(I) 'Menkes disease-associated protein' NMR 'solution structure' SPINE 'Structural Genomics' 'Structural Proteomics in Europe' stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name 'Copper-transporting ATPase 1 (E.C.3.6.3.4)' _Abbreviation_common 'Copper-transporting ATPase 1 (E.C.3.6.3.4)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Copper-transporting ATPase 1' $ATPase_1 'COPPER (I) ION' $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_ATPase_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Copper-transporting ATPase 1' _Abbreviation_common 'Copper-transporting ATPase 1' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 90 _Mol_residue_sequence ; NDSTATFIIDGMHCKSCVSN IESTLSALQYVSSIVVSLEN RSAIVVYNASSVTPESLRKA IEAVSPGLYRVSITSEVEIE GRLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 ASP 3 SER 4 THR 5 ALA 6 THR 7 PHE 8 ILE 9 ILE 10 ASP 11 GLY 12 MET 13 HIS 14 CYS 15 LYS 16 SER 17 CYS 18 VAL 19 SER 20 ASN 21 ILE 22 GLU 23 SER 24 THR 25 LEU 26 SER 27 ALA 28 LEU 29 GLN 30 TYR 31 VAL 32 SER 33 SER 34 ILE 35 VAL 36 VAL 37 SER 38 LEU 39 GLU 40 ASN 41 ARG 42 SER 43 ALA 44 ILE 45 VAL 46 VAL 47 TYR 48 ASN 49 ALA 50 SER 51 SER 52 VAL 53 THR 54 PRO 55 GLU 56 SER 57 LEU 58 ARG 59 LYS 60 ALA 61 ILE 62 GLU 63 ALA 64 VAL 65 SER 66 PRO 67 GLY 68 LEU 69 TYR 70 ARG 71 VAL 72 SER 73 ILE 74 THR 75 SER 76 GLU 77 VAL 78 GLU 79 ILE 80 GLU 81 GLY 82 ARG 83 LEU 84 GLU 85 HIS 86 HIS 87 HIS 88 HIS 89 HIS 90 HIS 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 2GA7 'Solution Structure Of The Copper(I) Form Of The Third Metal- Binding Domain Of Atp7a Protein (Menkes Disease Protein)' 98.89 90 100.00 100.00 4.08e-43 PDB 2G9O 'Solution Structure Of The Apo Form Of The Third Metal- Binding Domain Of Atp7a Protein (Menkes Disease Protein)' 98.89 90 100.00 100.00 4.08e-43 BMRB 7069 'Copper-transporting ATPase 1 (E.C.3.6.3.4)' 100.00 90 100.00 100.00 7.82e-44 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 $ATPase_1 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_1 '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 1 mM . phosphate_buffer 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 0.5 mM [U-15N] phosphate_buffer 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 0.5 mM '[U-15N; U-13C]' phosphate_buffer 100 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 1.3 loop_ _Task collection stop_ _Details . save_ save_Xeasy _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'data analysis' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.5 loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Task 'structure solution' stop_ _Details 'Guntert, P. et al.' save_ save_AMBER _Saveframe_category software _Name AMBER _Version 8.0 loop_ _Task refinement stop_ _Details 'Case, D.A. et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _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 . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_h(CCH)-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name h(CCH)-TOCSY _Sample_label . save_ save_3D_13C-separated_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_15N-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . 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 CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name h(CCH)-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _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' 100 . mM pH 7 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label dioxane C 13 'methyl carbons' ppm 69.4 . direct . . . 1.0 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . . $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 '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 . 2 ASP H H 8.082 0.02 . 2 . 2 ASP HA H 4.716 0.02 . 3 . 2 ASP HB2 H 2.399 0.02 . 4 . 2 ASP HB3 H 2.262 0.02 . 5 . 2 ASP CA C 54.795 0.3 . 6 . 2 ASP CB C 41.960 0.3 . 7 . 2 ASP N N 120.474 0.2 . 8 . 3 SER H H 8.539 0.02 . 9 . 3 SER HA H 4.527 0.02 . 10 . 3 SER HB2 H 2.668 0.02 . 11 . 3 SER HB3 H 3.406 0.02 . 12 . 3 SER CA C 57.934 0.3 . 13 . 3 SER CB C 65.436 0.3 . 14 . 3 SER N N 118.290 0.2 . 15 . 4 THR H H 8.302 0.02 . 16 . 4 THR HA H 5.507 0.02 . 17 . 4 THR HB H 3.772 0.02 . 18 . 4 THR HG2 H 0.983 0.02 . 19 . 4 THR CA C 61.624 0.3 . 20 . 4 THR CB C 71.007 0.3 . 21 . 4 THR CG2 C 21.494 0.3 . 22 . 4 THR N N 115.753 0.2 . 23 . 5 ALA H H 9.605 0.02 . 24 . 5 ALA HA H 4.748 0.02 . 25 . 5 ALA HB H 1.103 0.02 . 26 . 5 ALA CA C 50.865 0.3 . 27 . 5 ALA CB C 22.841 0.3 . 28 . 5 ALA N N 130.325 0.2 . 29 . 6 THR H H 8.202 0.02 . 30 . 6 THR HA H 5.125 0.02 . 31 . 6 THR HB H 3.868 0.02 . 32 . 6 THR HG2 H 0.990 0.02 . 33 . 6 THR CA C 60.854 0.3 . 34 . 6 THR CB C 70.461 0.3 . 35 . 6 THR CG2 C 21.411 0.3 . 36 . 6 THR N N 113.684 0.2 . 37 . 7 PHE H H 8.930 0.02 . 38 . 7 PHE HA H 5.365 0.02 . 39 . 7 PHE HB2 H 2.907 0.02 . 40 . 7 PHE HB3 H 2.391 0.02 . 41 . 7 PHE HD1 H 6.809 0.02 . 42 . 7 PHE HD2 H 6.809 0.02 . 43 . 7 PHE HE1 H 6.862 0.02 . 44 . 7 PHE HE2 H 6.862 0.02 . 45 . 7 PHE CA C 55.915 0.3 . 46 . 7 PHE CB C 42.822 0.3 . 47 . 7 PHE N N 120.940 0.2 . 48 . 8 ILE H H 8.943 0.02 . 49 . 8 ILE HA H 4.911 0.02 . 50 . 8 ILE HB H 1.754 0.02 . 51 . 8 ILE HG12 H 1.407 0.02 . 52 . 8 ILE HG13 H 1.180 0.02 . 53 . 8 ILE HG2 H 0.872 0.02 . 54 . 8 ILE HD1 H 0.721 0.02 . 55 . 8 ILE CA C 59.215 0.3 . 56 . 8 ILE CB C 38.882 0.3 . 57 . 8 ILE CG1 C 27.425 0.3 . 58 . 8 ILE CG2 C 17.184 0.3 . 59 . 8 ILE CD1 C 11.589 0.3 . 60 . 8 ILE N N 122.788 0.2 . 61 . 9 ILE H H 8.645 0.02 . 62 . 9 ILE HA H 4.369 0.02 . 63 . 9 ILE HB H 1.395 0.02 . 64 . 9 ILE HG12 H 1.350 0.02 . 65 . 9 ILE HG13 H 0.690 0.02 . 66 . 9 ILE HG2 H 0.268 0.02 . 67 . 9 ILE HD1 H 0.598 0.02 . 68 . 9 ILE CA C 60.475 0.3 . 69 . 9 ILE CB C 39.973 0.3 . 70 . 9 ILE CG1 C 27.712 0.3 . 71 . 9 ILE CG2 C 18.014 0.3 . 72 . 9 ILE CD1 C 15.786 0.3 . 73 . 9 ILE N N 126.466 0.2 . 74 . 10 ASP H H 8.971 0.02 . 75 . 10 ASP HA H 4.950 0.02 . 76 . 10 ASP HB2 H 2.764 0.02 . 77 . 10 ASP HB3 H 2.610 0.02 . 78 . 10 ASP CA C 54.222 0.3 . 79 . 10 ASP CB C 43.211 0.3 . 80 . 10 ASP N N 127.394 0.2 . 81 . 11 GLY H H 8.322 0.02 . 82 . 11 GLY HA2 H 5.070 0.02 . 83 . 11 GLY HA3 H 3.606 0.02 . 84 . 11 GLY CA C 45.178 0.3 . 85 . 11 GLY N N 110.517 0.2 . 86 . 12 MET H H 8.401 0.02 . 87 . 12 MET HA H 5.364 0.02 . 88 . 12 MET HB2 H 1.621 0.02 . 89 . 12 MET CA C 57.456 0.3 . 90 . 12 MET CB C 34.379 0.3 . 91 . 12 MET N N 119.309 0.2 . 92 . 15 LYS HA H 3.939 0.02 . 93 . 15 LYS HB2 H 1.800 0.02 . 94 . 15 LYS HB3 H 1.800 0.02 . 95 . 15 LYS HG2 H 1.612 0.02 . 96 . 15 LYS HG3 H 1.612 0.02 . 97 . 15 LYS HD2 H 1.517 0.02 . 98 . 15 LYS HD3 H 1.360 0.02 . 99 . 15 LYS HE2 H 2.926 0.02 . 100 . 15 LYS HE3 H 2.926 0.02 . 101 . 15 LYS CA C 59.975 0.3 . 102 . 15 LYS CB C 32.056 0.3 . 103 . 15 LYS CG C 29.320 0.3 . 104 . 15 LYS CD C 25.359 0.3 . 105 . 15 LYS CE C 38.980 0.3 . 106 . 16 SER H H 9.297 0.02 . 107 . 16 SER HA H 4.365 0.02 . 108 . 16 SER HB2 H 3.795 0.02 . 109 . 16 SER HB3 H 3.924 0.02 . 110 . 16 SER CA C 62.175 0.3 . 111 . 16 SER CB C 62.500 0.3 . 112 . 16 SER N N 120.017 0.2 . 113 . 17 CYS H H 7.962 0.02 . 114 . 17 CYS HA H 3.810 0.02 . 115 . 17 CYS HB2 H 3.198 0.02 . 116 . 17 CYS HB3 H 2.611 0.02 . 117 . 17 CYS CA C 64.689 0.3 . 118 . 17 CYS CB C 29.867 0.3 . 119 . 17 CYS N N 124.512 0.2 . 120 . 18 VAL H H 6.421 0.02 . 121 . 18 VAL HA H 3.152 0.02 . 122 . 18 VAL HB H 2.210 0.02 . 123 . 18 VAL HG1 H 0.934 0.02 . 124 . 18 VAL HG2 H 0.822 0.02 . 125 . 18 VAL CA C 66.557 0.3 . 126 . 18 VAL CB C 31.702 0.3 . 127 . 18 VAL CG1 C 22.991 0.3 . 128 . 18 VAL CG2 C 20.780 0.3 . 129 . 18 VAL N N 116.246 0.2 . 130 . 19 SER H H 7.571 0.02 . 131 . 19 SER HA H 4.222 0.02 . 132 . 19 SER HB2 H 3.869 0.02 . 133 . 19 SER HB3 H 3.869 0.02 . 134 . 19 SER CA C 61.278 0.3 . 135 . 19 SER CB C 62.729 0.3 . 136 . 19 SER N N 111.562 0.2 . 137 . 20 ASN H H 8.541 0.02 . 138 . 20 ASN HA H 4.482 0.02 . 139 . 20 ASN HB2 H 2.900 0.02 . 140 . 20 ASN HB3 H 2.661 0.02 . 141 . 20 ASN HD21 H 7.469 0.02 . 142 . 20 ASN HD22 H 6.875 0.02 . 143 . 20 ASN CA C 55.982 0.3 . 144 . 20 ASN CB C 37.647 0.3 . 145 . 20 ASN N N 121.196 0.2 . 146 . 20 ASN ND2 N 111.250 0.2 . 147 . 21 ILE H H 8.180 0.02 . 148 . 21 ILE HA H 3.617 0.02 . 149 . 21 ILE HB H 1.671 0.02 . 150 . 21 ILE HG12 H 0.559 0.02 . 151 . 21 ILE HG13 H 0.559 0.02 . 152 . 21 ILE HG2 H 0.585 0.02 . 153 . 21 ILE HD1 H 0.211 0.02 . 154 . 21 ILE CA C 66.863 0.3 . 155 . 21 ILE CB C 38.677 0.3 . 156 . 21 ILE CG1 C 30.196 0.3 . 157 . 21 ILE CG2 C 18.668 0.3 . 158 . 21 ILE CD1 C 14.098 0.3 . 159 . 21 ILE N N 121.925 0.2 . 160 . 22 GLU H H 8.538 0.02 . 161 . 22 GLU HA H 3.736 0.02 . 162 . 22 GLU HB2 H 1.938 0.02 . 163 . 22 GLU HB3 H 1.909 0.02 . 164 . 22 GLU HG2 H 2.513 0.02 . 165 . 22 GLU HG3 H 2.058 0.02 . 166 . 22 GLU CA C 60.708 0.3 . 167 . 22 GLU CB C 29.666 0.3 . 168 . 22 GLU CG C 38.382 0.3 . 169 . 22 GLU N N 117.263 0.2 . 170 . 23 SER H H 8.746 0.02 . 171 . 23 SER HA H 3.934 0.02 . 172 . 23 SER HB2 H 4.025 0.02 . 173 . 23 SER HB3 H 4.025 0.02 . 174 . 23 SER CA C 61.999 0.3 . 175 . 23 SER CB C 62.707 0.3 . 176 . 23 SER N N 114.885 0.2 . 177 . 24 THR H H 7.600 0.02 . 178 . 24 THR HA H 3.847 0.02 . 179 . 24 THR HB H 4.001 0.02 . 180 . 24 THR HG2 H 1.076 0.02 . 181 . 24 THR CA C 66.842 0.3 . 182 . 24 THR CB C 68.602 0.3 . 183 . 24 THR CG2 C 21.096 0.3 . 184 . 24 THR N N 117.924 0.2 . 185 . 25 LEU H H 7.894 0.02 . 186 . 25 LEU HA H 3.946 0.02 . 187 . 25 LEU HB2 H 1.828 0.02 . 188 . 25 LEU HB3 H 1.318 0.02 . 189 . 25 LEU HG H 1.514 0.02 . 190 . 25 LEU HD1 H 0.557 0.02 . 191 . 25 LEU HD2 H 0.628 0.02 . 192 . 25 LEU CA C 57.339 0.3 . 193 . 25 LEU CB C 41.185 0.3 . 194 . 25 LEU CG C 30.268 0.3 . 195 . 25 LEU CD1 C 23.827 0.3 . 196 . 25 LEU CD2 C 24.153 0.3 . 197 . 25 LEU N N 121.900 0.2 . 198 . 26 SER H H 8.030 0.02 . 199 . 26 SER HA H 4.027 0.02 . 200 . 26 SER HB2 H 3.893 0.02 . 201 . 26 SER HB3 H 3.811 0.02 . 202 . 26 SER CA C 61.473 0.3 . 203 . 26 SER CB C 62.880 0.3 . 204 . 26 SER N N 111.223 0.2 . 205 . 27 ALA H H 6.708 0.02 . 206 . 27 ALA HA H 4.118 0.02 . 207 . 27 ALA HB H 1.366 0.02 . 208 . 27 ALA CA C 52.626 0.3 . 209 . 27 ALA CB C 18.995 0.3 . 210 . 27 ALA N N 119.932 0.2 . 211 . 28 LEU H H 7.211 0.02 . 212 . 28 LEU HA H 4.032 0.02 . 213 . 28 LEU HB2 H 1.669 0.02 . 214 . 28 LEU HB3 H 1.669 0.02 . 215 . 28 LEU HG H 0.838 0.02 . 216 . 28 LEU HD1 H 0.702 0.02 . 217 . 28 LEU CA C 54.501 0.3 . 218 . 28 LEU CB C 41.326 0.3 . 219 . 28 LEU CG C 25.192 0.3 . 220 . 28 LEU CD1 C 22.059 0.3 . 221 . 28 LEU N N 119.559 0.2 . 222 . 30 TYR HB2 H 3.492 0.02 . 223 . 30 TYR HB3 H 3.070 0.02 . 224 . 30 TYR HD1 H 6.972 0.02 . 225 . 30 TYR HD2 H 6.972 0.02 . 226 . 30 TYR HE1 H 6.708 0.02 . 227 . 30 TYR HE2 H 6.708 0.02 . 228 . 31 VAL H H 7.139 0.02 . 229 . 31 VAL HA H 4.272 0.02 . 230 . 31 VAL HB H 2.187 0.02 . 231 . 31 VAL HG1 H 0.764 0.02 . 232 . 31 VAL HG2 H 0.634 0.02 . 233 . 31 VAL CA C 62.786 0.3 . 234 . 31 VAL CB C 32.985 0.3 . 235 . 31 VAL CG1 C 23.307 0.3 . 236 . 31 VAL CG2 C 21.471 0.3 . 237 . 31 VAL N N 122.338 0.2 . 238 . 32 SER H H 9.105 0.02 . 239 . 32 SER HA H 4.509 0.02 . 240 . 32 SER HB2 H 3.684 0.02 . 241 . 32 SER HB3 H 3.610 0.02 . 242 . 32 SER CA C 59.293 0.3 . 243 . 32 SER CB C 63.621 0.3 . 244 . 32 SER N N 123.017 0.2 . 245 . 33 SER H H 7.734 0.02 . 246 . 33 SER HA H 4.568 0.02 . 247 . 33 SER HB2 H 3.741 0.02 . 248 . 33 SER HB3 H 3.632 0.02 . 249 . 33 SER CA C 58.042 0.3 . 250 . 33 SER CB C 64.687 0.3 . 251 . 33 SER N N 113.808 0.2 . 252 . 34 ILE H H 8.313 0.02 . 253 . 34 ILE HA H 5.259 0.02 . 254 . 34 ILE HB H 1.707 0.02 . 255 . 34 ILE HG12 H 1.370 0.02 . 256 . 34 ILE HG13 H 0.901 0.02 . 257 . 34 ILE HG2 H 0.633 0.02 . 258 . 34 ILE HD1 H 0.215 0.02 . 259 . 34 ILE CA C 59.339 0.3 . 260 . 34 ILE CB C 40.589 0.3 . 261 . 34 ILE CG1 C 29.352 0.3 . 262 . 34 ILE CG2 C 15.842 0.3 . 263 . 34 ILE N N 120.078 0.2 . 264 . 35 VAL H H 8.182 0.02 . 265 . 35 VAL HA H 4.391 0.02 . 266 . 35 VAL HB H 1.805 0.02 . 267 . 35 VAL HG1 H 0.837 0.02 . 268 . 35 VAL HG2 H 0.790 0.02 . 269 . 35 VAL CA C 61.059 0.3 . 270 . 35 VAL CB C 35.002 0.3 . 271 . 35 VAL CG1 C 20.907 0.3 . 272 . 35 VAL CG2 C 20.585 0.3 . 273 . 35 VAL N N 125.383 0.2 . 274 . 36 VAL H H 9.737 0.02 . 275 . 36 VAL HA H 4.763 0.02 . 276 . 36 VAL HB H 2.020 0.02 . 277 . 36 VAL HG1 H 0.824 0.02 . 278 . 36 VAL HG2 H 0.756 0.02 . 279 . 36 VAL CA C 60.887 0.3 . 280 . 36 VAL CB C 32.877 0.3 . 281 . 36 VAL CG1 C 23.380 0.3 . 282 . 36 VAL CG2 C 21.908 0.3 . 283 . 36 VAL N N 131.476 0.2 . 284 . 37 SER H H 8.771 0.02 . 285 . 37 SER HA H 4.766 0.02 . 286 . 37 SER HB2 H 3.829 0.02 . 287 . 37 SER HB3 H 3.705 0.02 . 288 . 37 SER CA C 55.176 0.3 . 289 . 37 SER CB C 64.070 0.3 . 290 . 37 SER N N 120.580 0.2 . 291 . 38 LEU H H 8.944 0.02 . 292 . 38 LEU HA H 4.679 0.02 . 293 . 38 LEU HB2 H 1.631 0.02 . 294 . 38 LEU HB3 H 1.349 0.02 . 295 . 38 LEU HG H 1.397 0.02 . 296 . 38 LEU HD1 H 0.630 0.02 . 297 . 38 LEU HD2 H 0.583 0.02 . 298 . 38 LEU CA C 57.947 0.3 . 299 . 38 LEU CB C 42.152 0.3 . 300 . 38 LEU CG C 26.765 0.3 . 301 . 38 LEU CD1 C 25.360 0.3 . 302 . 38 LEU CD2 C 23.710 0.3 . 303 . 38 LEU N N 130.046 0.2 . 304 . 39 GLU H H 8.855 0.02 . 305 . 39 GLU HA H 3.853 0.02 . 306 . 39 GLU HB2 H 1.861 0.02 . 307 . 39 GLU HB3 H 1.791 0.02 . 308 . 39 GLU HG2 H 2.270 0.02 . 309 . 39 GLU HG3 H 2.155 0.02 . 310 . 39 GLU CA C 60.048 0.3 . 311 . 39 GLU CB C 29.156 0.3 . 312 . 39 GLU CG C 36.565 0.3 . 313 . 39 GLU N N 117.755 0.2 . 314 . 40 ASN H H 7.624 0.02 . 315 . 40 ASN HA H 4.737 0.02 . 316 . 40 ASN HB2 H 2.795 0.02 . 317 . 40 ASN HB3 H 2.551 0.02 . 318 . 40 ASN HD21 H 7.365 0.02 . 319 . 40 ASN HD22 H 6.872 0.02 . 320 . 40 ASN CA C 52.555 0.3 . 321 . 40 ASN CB C 38.822 0.3 . 322 . 40 ASN N N 113.180 0.2 . 323 . 40 ASN ND2 N 112.648 0.2 . 324 . 41 ARG H H 7.625 0.02 . 325 . 41 ARG HA H 3.682 0.02 . 326 . 41 ARG HB2 H 2.177 0.02 . 327 . 41 ARG HB3 H 2.107 0.02 . 328 . 41 ARG HG2 H 1.607 0.02 . 329 . 41 ARG HG3 H 1.522 0.02 . 330 . 41 ARG HD2 H 3.285 0.02 . 331 . 41 ARG HD3 H 3.262 0.02 . 332 . 41 ARG CA C 57.337 0.3 . 333 . 41 ARG CB C 27.131 0.3 . 334 . 41 ARG CG C 28.217 0.3 . 335 . 41 ARG CD C 44.157 0.3 . 336 . 41 ARG N N 117.482 0.2 . 337 . 42 SER H H 7.912 0.02 . 338 . 42 SER HA H 5.675 0.02 . 339 . 42 SER HB2 H 3.779 0.02 . 340 . 42 SER HB3 H 3.540 0.02 . 341 . 42 SER CA C 56.392 0.3 . 342 . 42 SER CB C 68.228 0.3 . 343 . 42 SER N N 108.771 0.2 . 344 . 43 ALA H H 8.696 0.02 . 345 . 43 ALA HA H 5.339 0.02 . 346 . 43 ALA HB H 1.144 0.02 . 347 . 43 ALA CA C 50.667 0.3 . 348 . 43 ALA CB C 23.452 0.3 . 349 . 43 ALA N N 119.059 0.2 . 350 . 44 ILE H H 8.523 0.02 . 351 . 44 ILE HA H 4.806 0.02 . 352 . 44 ILE HB H 1.599 0.02 . 353 . 44 ILE HG12 H 0.987 0.02 . 354 . 44 ILE HG13 H 0.987 0.02 . 355 . 44 ILE HG2 H 0.740 0.02 . 356 . 44 ILE CA C 61.063 0.3 . 357 . 44 ILE CB C 40.300 0.3 . 358 . 44 ILE CG1 C 27.459 0.3 . 359 . 44 ILE CG2 C 17.217 0.3 . 360 . 44 ILE CD1 C 13.851 0.3 . 361 . 44 ILE N N 122.230 0.2 . 362 . 45 VAL H H 9.409 0.02 . 363 . 45 VAL HA H 4.903 0.02 . 364 . 45 VAL HB H 2.095 0.02 . 365 . 45 VAL HG1 H 1.062 0.02 . 366 . 45 VAL HG2 H 0.805 0.02 . 367 . 45 VAL CA C 61.009 0.3 . 368 . 45 VAL CB C 35.699 0.3 . 369 . 45 VAL CG1 C 23.405 0.3 . 370 . 45 VAL CG2 C 21.947 0.3 . 371 . 45 VAL N N 129.080 0.2 . 372 . 46 VAL H H 8.893 0.02 . 373 . 46 VAL HA H 5.191 0.02 . 374 . 46 VAL HB H 1.942 0.02 . 375 . 46 VAL HG1 H 0.760 0.02 . 376 . 46 VAL HG2 H 0.802 0.02 . 377 . 46 VAL CA C 61.427 0.3 . 378 . 46 VAL CB C 32.055 0.3 . 379 . 46 VAL CG1 C 21.620 0.3 . 380 . 46 VAL CG2 C 20.728 0.3 . 381 . 46 VAL N N 129.574 0.2 . 382 . 47 TYR H H 9.232 0.02 . 383 . 47 TYR HA H 5.577 0.02 . 384 . 47 TYR HB2 H 2.859 0.02 . 385 . 47 TYR HB3 H 2.659 0.02 . 386 . 47 TYR HD1 H 6.759 0.02 . 387 . 47 TYR HD2 H 6.759 0.02 . 388 . 47 TYR HE1 H 6.498 0.02 . 389 . 47 TYR HE2 H 6.498 0.02 . 390 . 47 TYR CA C 55.209 0.3 . 391 . 47 TYR CB C 42.525 0.3 . 392 . 47 TYR N N 125.016 0.2 . 393 . 48 ASN H H 8.305 0.02 . 394 . 48 ASN HA H 4.759 0.02 . 395 . 48 ASN HB2 H 3.004 0.02 . 396 . 48 ASN HB3 H 2.867 0.02 . 397 . 48 ASN HD21 H 7.762 0.02 . 398 . 48 ASN HD22 H 6.905 0.02 . 399 . 48 ASN CA C 52.390 0.3 . 400 . 48 ASN CB C 38.451 0.3 . 401 . 48 ASN N N 116.806 0.2 . 402 . 48 ASN ND2 N 111.881 0.2 . 403 . 49 ALA H H 8.468 0.02 . 404 . 49 ALA HA H 4.665 0.02 . 405 . 49 ALA HB H 1.371 0.02 . 406 . 49 ALA CA C 53.601 0.3 . 407 . 49 ALA CB C 18.977 0.3 . 408 . 49 ALA N N 129.385 0.2 . 409 . 50 SER H H 8.329 0.02 . 410 . 50 SER HA H 4.354 0.02 . 411 . 50 SER HB2 H 3.901 0.02 . 412 . 50 SER HB3 H 3.866 0.02 . 413 . 50 SER CA C 60.442 0.3 . 414 . 50 SER CB C 63.338 0.3 . 415 . 50 SER N N 112.469 0.2 . 416 . 52 VAL H H 7.624 0.02 . 417 . 52 VAL HA H 4.355 0.02 . 418 . 52 VAL HB H 1.795 0.02 . 419 . 52 VAL HG1 H 0.749 0.02 . 420 . 52 VAL CA C 60.527 0.3 . 421 . 52 VAL CB C 34.945 0.3 . 422 . 52 VAL CG1 C 20.709 0.3 . 423 . 52 VAL N N 119.697 0.2 . 424 . 53 THR H H 7.088 0.02 . 425 . 53 THR HA H 5.025 0.02 . 426 . 53 THR HB H 4.617 0.02 . 427 . 53 THR HG2 H 1.219 0.02 . 428 . 53 THR CA C 58.114 0.3 . 429 . 53 THR CB C 69.883 0.3 . 430 . 53 THR CG2 C 21.745 0.3 . 431 . 53 THR N N 111.232 0.2 . 432 . 54 PRO HA H 3.849 0.02 . 433 . 54 PRO HB2 H 2.046 0.02 . 434 . 54 PRO HB3 H 1.911 0.02 . 435 . 54 PRO HG2 H 2.236 0.02 . 436 . 54 PRO HG3 H 1.860 0.02 . 437 . 54 PRO HD2 H 3.869 0.02 . 438 . 54 PRO HD3 H 3.818 0.02 . 439 . 54 PRO CA C 65.895 0.3 . 440 . 54 PRO CB C 31.801 0.3 . 441 . 54 PRO CG C 28.392 0.3 . 442 . 54 PRO CD C 50.692 0.3 . 443 . 55 GLU H H 8.024 0.02 . 444 . 55 GLU HA H 4.365 0.02 . 445 . 55 GLU HB2 H 1.642 0.02 . 446 . 55 GLU HB3 H 1.642 0.02 . 447 . 55 GLU HG2 H 2.374 0.02 . 448 . 55 GLU HG3 H 2.042 0.02 . 449 . 55 GLU CA C 58.775 0.3 . 450 . 55 GLU CB C 28.944 0.3 . 451 . 55 GLU CG C 34.706 0.3 . 452 . 55 GLU N N 117.158 0.2 . 453 . 56 SER H H 7.727 0.02 . 454 . 56 SER HA H 3.981 0.02 . 455 . 56 SER HB2 H 3.753 0.02 . 456 . 56 SER HB3 H 3.873 0.02 . 457 . 56 SER CA C 61.852 0.3 . 458 . 56 SER CB C 62.715 0.3 . 459 . 56 SER N N 115.728 0.2 . 460 . 57 LEU H H 7.562 0.02 . 461 . 57 LEU HA H 3.731 0.02 . 462 . 57 LEU HB2 H 1.945 0.02 . 463 . 57 LEU HB3 H 0.716 0.02 . 464 . 57 LEU HG H 1.399 0.02 . 465 . 57 LEU HD1 H 0.506 0.02 . 466 . 57 LEU HD2 H 0.073 0.02 . 467 . 57 LEU CA C 57.640 0.3 . 468 . 57 LEU CB C 42.587 0.3 . 469 . 57 LEU CG C 25.282 0.3 . 470 . 57 LEU CD1 C 23.100 0.3 . 471 . 57 LEU CD2 C 24.955 0.3 . 472 . 57 LEU N N 122.181 0.2 . 473 . 58 ARG H H 8.396 0.02 . 474 . 58 ARG HA H 3.107 0.02 . 475 . 58 ARG HB2 H 2.233 0.02 . 476 . 58 ARG HB3 H 1.817 0.02 . 477 . 58 ARG HG2 H 1.268 0.02 . 478 . 58 ARG HG3 H 1.349 0.02 . 479 . 58 ARG HD2 H 3.526 0.02 . 480 . 58 ARG HD3 H 3.526 0.02 . 481 . 58 ARG CA C 59.969 0.3 . 482 . 58 ARG CB C 30.440 0.3 . 483 . 58 ARG CG C 26.591 0.3 . 484 . 58 ARG CD C 42.368 0.3 . 485 . 58 ARG N N 120.729 0.2 . 486 . 59 LYS H H 7.711 0.02 . 487 . 59 LYS HA H 3.776 0.02 . 488 . 59 LYS HB2 H 1.760 0.02 . 489 . 59 LYS HB3 H 1.732 0.02 . 490 . 59 LYS HG2 H 1.594 0.02 . 491 . 59 LYS HG3 H 1.594 0.02 . 492 . 59 LYS HD2 H 1.354 0.02 . 493 . 59 LYS HD3 H 1.607 0.02 . 494 . 59 LYS HE2 H 2.871 0.02 . 495 . 59 LYS HE3 H 2.871 0.02 . 496 . 59 LYS CA C 59.356 0.3 . 497 . 59 LYS CB C 32.320 0.3 . 498 . 59 LYS CG C 29.105 0.3 . 499 . 59 LYS CD C 25.636 0.3 . 500 . 59 LYS CE C 38.939 0.3 . 501 . 59 LYS N N 116.207 0.2 . 502 . 60 ALA H H 7.841 0.02 . 503 . 60 ALA HA H 3.980 0.02 . 504 . 60 ALA HB H 1.333 0.02 . 505 . 60 ALA CA C 54.939 0.3 . 506 . 60 ALA CB C 17.513 0.3 . 507 . 60 ALA N N 123.116 0.2 . 508 . 61 ILE H H 7.727 0.02 . 509 . 61 ILE HA H 3.416 0.02 . 510 . 61 ILE HB H 1.515 0.02 . 511 . 61 ILE HG12 H 0.197 0.02 . 512 . 61 ILE HG13 H 0.197 0.02 . 513 . 61 ILE HG2 H 0.497 0.02 . 514 . 61 ILE HD1 H -0.207 0.02 . 515 . 61 ILE CA C 65.618 0.3 . 516 . 61 ILE CB C 37.367 0.3 . 517 . 61 ILE CG1 C 29.711 0.3 . 518 . 61 ILE CG2 C 18.888 0.3 . 519 . 61 ILE CD1 C 12.241 0.3 . 520 . 61 ILE N N 116.737 0.2 . 521 . 62 GLU H H 7.563 0.02 . 522 . 62 GLU HA H 3.749 0.02 . 523 . 62 GLU HB2 H 2.064 0.02 . 524 . 62 GLU HB3 H 1.992 0.02 . 525 . 62 GLU HG2 H 2.470 0.02 . 526 . 62 GLU HG3 H 2.138 0.02 . 527 . 62 GLU CA C 61.213 0.3 . 528 . 62 GLU CB C 29.621 0.3 . 529 . 62 GLU CG C 38.514 0.3 . 530 . 62 GLU N N 118.048 0.2 . 531 . 63 ALA H H 7.677 0.02 . 532 . 63 ALA HA H 4.056 0.02 . 533 . 63 ALA HB H 1.385 0.02 . 534 . 63 ALA CA C 53.087 0.3 . 535 . 63 ALA CB C 18.345 0.3 . 536 . 63 ALA N N 116.466 0.2 . 537 . 64 VAL H H 7.606 0.02 . 538 . 64 VAL HA H 3.567 0.02 . 539 . 64 VAL HB H 2.243 0.02 . 540 . 64 VAL HG1 H 1.147 0.02 . 541 . 64 VAL HG2 H 0.902 0.02 . 542 . 64 VAL CA C 66.111 0.3 . 543 . 64 VAL CB C 31.308 0.3 . 544 . 64 VAL CG1 C 23.776 0.3 . 545 . 64 VAL CG2 C 22.267 0.3 . 546 . 64 VAL N N 119.986 0.2 . 547 . 65 SER H H 6.501 0.02 . 548 . 65 SER HA H 4.395 0.02 . 549 . 65 SER HB2 H 2.802 0.02 . 550 . 65 SER HB3 H 2.711 0.02 . 551 . 65 SER CA C 55.496 0.3 . 552 . 65 SER CB C 62.632 0.3 . 553 . 65 SER N N 109.658 0.2 . 554 . 66 PRO HA H 4.171 0.02 . 555 . 66 PRO HB2 H 2.152 0.02 . 556 . 66 PRO HB3 H 1.809 0.02 . 557 . 66 PRO HG2 H 2.005 0.02 . 558 . 66 PRO HG3 H 1.863 0.02 . 559 . 66 PRO HD2 H 3.433 0.02 . 560 . 66 PRO HD3 H 3.399 0.02 . 561 . 66 PRO CA C 64.495 0.3 . 562 . 66 PRO CB C 31.949 0.3 . 563 . 66 PRO CG C 27.636 0.3 . 564 . 66 PRO CD C 50.254 0.3 . 565 . 67 GLY H H 8.778 0.02 . 566 . 67 GLY HA2 H 3.614 0.02 . 567 . 67 GLY HA3 H 4.105 0.02 . 568 . 67 GLY CA C 45.479 0.3 . 569 . 67 GLY N N 113.882 0.2 . 570 . 68 LEU H H 7.894 0.02 . 571 . 68 LEU HA H 4.357 0.02 . 572 . 68 LEU HB2 H 1.201 0.02 . 573 . 68 LEU HB3 H 1.089 0.02 . 574 . 68 LEU HG H 1.292 0.02 . 575 . 68 LEU HD1 H 0.680 0.02 . 576 . 68 LEU HD2 H 0.750 0.02 . 577 . 68 LEU CA C 55.911 0.3 . 578 . 68 LEU CB C 43.509 0.3 . 579 . 68 LEU CG C 27.142 0.3 . 580 . 68 LEU CD1 C 24.826 0.3 . 581 . 68 LEU CD2 C 23.669 0.3 . 582 . 68 LEU N N 121.876 0.2 . 583 . 69 TYR H H 7.387 0.02 . 584 . 69 TYR HA H 5.679 0.02 . 585 . 69 TYR HB2 H 2.841 0.02 . 586 . 69 TYR HB3 H 2.713 0.02 . 587 . 69 TYR HD1 H 6.879 0.02 . 588 . 69 TYR HD2 H 6.879 0.02 . 589 . 69 TYR HE1 H 6.598 0.02 . 590 . 69 TYR HE2 H 6.598 0.02 . 591 . 69 TYR CA C 53.724 0.3 . 592 . 69 TYR CB C 39.116 0.3 . 593 . 69 TYR N N 115.002 0.2 . 594 . 70 ARG H H 8.607 0.02 . 595 . 70 ARG HA H 4.759 0.02 . 596 . 70 ARG HB2 H 1.788 0.02 . 597 . 70 ARG HB3 H 1.689 0.02 . 598 . 70 ARG HG2 H 1.497 0.02 . 599 . 70 ARG HG3 H 1.534 0.02 . 600 . 70 ARG HD2 H 3.104 0.02 . 601 . 70 ARG HD3 H 3.068 0.02 . 602 . 70 ARG CA C 55.195 0.3 . 603 . 70 ARG CB C 32.033 0.3 . 604 . 70 ARG CG C 26.878 0.3 . 605 . 70 ARG CD C 43.343 0.3 . 606 . 70 ARG N N 123.751 0.2 . 607 . 71 VAL H H 9.974 0.02 . 608 . 71 VAL HA H 5.199 0.02 . 609 . 71 VAL HB H 1.896 0.02 . 610 . 71 VAL HG1 H 0.816 0.02 . 611 . 71 VAL HG2 H 0.924 0.02 . 612 . 71 VAL CA C 61.181 0.3 . 613 . 71 VAL CB C 33.656 0.3 . 614 . 71 VAL CG1 C 23.572 0.3 . 615 . 71 VAL CG2 C 23.092 0.3 . 616 . 71 VAL N N 128.851 0.2 . 617 . 72 SER H H 9.209 0.02 . 618 . 72 SER HA H 4.953 0.02 . 619 . 72 SER HB2 H 3.777 0.02 . 620 . 72 SER HB3 H 3.671 0.02 . 621 . 72 SER CA C 56.709 0.3 . 622 . 72 SER CB C 65.902 0.3 . 623 . 72 SER N N 122.522 0.2 . 624 . 73 ILE H H 8.928 0.02 . 625 . 73 ILE HA H 4.146 0.02 . 626 . 73 ILE HB H 1.626 0.02 . 627 . 73 ILE HG12 H 0.909 0.02 . 628 . 73 ILE HG13 H 1.513 0.02 . 629 . 73 ILE HG2 H 0.738 0.02 . 630 . 73 ILE HD1 H 0.832 0.02 . 631 . 73 ILE CA C 61.972 0.3 . 632 . 73 ILE CB C 39.350 0.3 . 633 . 73 ILE CG1 C 28.883 0.3 . 634 . 73 ILE CG2 C 17.468 0.3 . 635 . 73 ILE CD1 C 14.220 0.3 . 636 . 73 ILE N N 124.236 0.2 . 637 . 74 THR H H 8.410 0.02 . 638 . 74 THR HA H 4.433 0.02 . 639 . 74 THR HB H 4.038 0.02 . 640 . 74 THR HG2 H 0.995 0.02 . 641 . 74 THR CA C 61.474 0.3 . 642 . 74 THR CB C 69.741 0.3 . 643 . 74 THR CG2 C 21.947 0.3 . 644 . 74 THR N N 120.570 0.2 . 645 . 75 SER H H 7.966 0.02 . 646 . 75 SER HA H 4.439 0.02 . 647 . 75 SER HB2 H 3.852 0.02 . 648 . 75 SER HB3 H 3.789 0.02 . 649 . 75 SER CA C 57.963 0.3 . 650 . 75 SER CB C 63.994 0.3 . 651 . 75 SER N N 116.979 0.2 . 652 . 76 GLU H H 8.407 0.02 . 653 . 76 GLU HA H 4.217 0.02 . 654 . 76 GLU HB2 H 1.893 0.02 . 655 . 76 GLU HB3 H 1.893 0.02 . 656 . 76 GLU HG2 H 2.059 0.02 . 657 . 76 GLU HG3 H 2.071 0.02 . 658 . 76 GLU CA C 56.888 0.3 . 659 . 76 GLU CB C 30.620 0.3 . 660 . 76 GLU CG C 36.395 0.3 . 661 . 76 GLU N N 121.881 0.2 . 662 . 77 VAL H H 8.100 0.02 . 663 . 77 VAL HA H 4.034 0.02 . 664 . 77 VAL HB H 1.978 0.02 . 665 . 77 VAL HG1 H 0.862 0.02 . 666 . 77 VAL HG2 H 0.842 0.02 . 667 . 77 VAL CA C 62.414 0.3 . 668 . 77 VAL CB C 33.176 0.3 . 669 . 77 VAL CG1 C 21.108 0.3 . 670 . 77 VAL CG2 C 20.735 0.3 . 671 . 77 VAL N N 120.194 0.2 . 672 . 78 GLU H H 8.375 0.02 . 673 . 78 GLU HA H 4.254 0.02 . 674 . 78 GLU HB2 H 1.859 0.02 . 675 . 78 GLU HB3 H 1.981 0.02 . 676 . 78 GLU HG2 H 2.115 0.02 . 677 . 78 GLU HG3 H 2.185 0.02 . 678 . 78 GLU CA C 56.740 0.3 . 679 . 78 GLU CB C 30.360 0.3 . 680 . 78 GLU CG C 36.303 0.3 . 681 . 78 GLU N N 124.601 0.2 . 682 . 79 ILE H H 8.154 0.02 . 683 . 79 ILE HA H 4.057 0.02 . 684 . 79 ILE HB H 1.755 0.02 . 685 . 79 ILE HG12 H 1.382 0.02 . 686 . 79 ILE HG13 H 1.104 0.02 . 687 . 79 ILE HG2 H 0.802 0.02 . 688 . 79 ILE HD1 H 0.755 0.02 . 689 . 79 ILE CA C 61.511 0.3 . 690 . 79 ILE CB C 38.929 0.3 . 691 . 79 ILE CG1 C 27.038 0.3 . 692 . 79 ILE CG2 C 17.261 0.3 . 693 . 79 ILE CD1 C 13.215 0.3 . 694 . 79 ILE N N 122.316 0.2 . 695 . 80 GLU H H 8.411 0.02 . 696 . 80 GLU HA H 4.149 0.02 . 697 . 80 GLU HB2 H 1.930 0.02 . 698 . 80 GLU HB3 H 1.852 0.02 . 699 . 80 GLU HG2 H 2.171 0.02 . 700 . 80 GLU HG3 H 2.171 0.02 . 701 . 80 GLU CA C 57.302 0.3 . 702 . 80 GLU CB C 30.114 0.3 . 703 . 80 GLU CG C 36.310 0.3 . 704 . 80 GLU N N 124.618 0.2 . 705 . 81 GLY H H 8.385 0.02 . 706 . 81 GLY HA2 H 3.808 0.02 . 707 . 81 GLY HA3 H 3.808 0.02 . 708 . 81 GLY CA C 45.692 0.3 . 709 . 81 GLY N N 109.928 0.2 . 710 . 82 ARG H H 7.997 0.02 . 711 . 82 ARG HA H 4.680 0.02 . 712 . 82 ARG HB2 H 1.722 0.02 . 713 . 82 ARG HB3 H 1.638 0.02 . 714 . 82 ARG HG2 H 1.488 0.02 . 715 . 82 ARG HG3 H 1.439 0.02 . 716 . 82 ARG HD2 H 3.045 0.02 . 717 . 82 ARG HD3 H 3.045 0.02 . 718 . 82 ARG CA C 56.330 0.3 . 719 . 82 ARG CB C 30.899 0.3 . 720 . 82 ARG CG C 27.124 0.3 . 721 . 82 ARG CD C 43.354 0.3 . 722 . 82 ARG N N 120.190 0.2 . 723 . 83 LEU H H 8.209 0.02 . 724 . 83 LEU HA H 4.197 0.02 . 725 . 83 LEU HB2 H 1.490 0.02 . 726 . 83 LEU HB3 H 1.381 0.02 . 727 . 83 LEU HG H 1.449 0.02 . 728 . 83 LEU HD1 H 0.828 0.02 . 729 . 83 LEU HD2 H 0.777 0.02 . 730 . 83 LEU CA C 55.261 0.3 . 731 . 83 LEU CB C 42.492 0.3 . 732 . 83 LEU CG C 26.949 0.3 . 733 . 83 LEU CD1 C 24.966 0.3 . 734 . 83 LEU CD2 C 23.599 0.3 . 735 . 83 LEU N N 122.913 0.2 . 736 . 84 GLU H H 8.288 0.02 . 737 . 84 GLU HA H 4.079 0.02 . 738 . 84 GLU HB2 H 1.822 0.02 . 739 . 84 GLU HB3 H 1.776 0.02 . 740 . 84 GLU HG2 H 1.823 0.02 . 741 . 84 GLU HG3 H 1.722 0.02 . 742 . 84 GLU CA C 56.689 0.3 . 743 . 84 GLU CB C 30.487 0.3 . 744 . 84 GLU CG C 36.218 0.3 . 745 . 84 GLU N N 121.222 0.2 . stop_ save_