data_5813 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The solution structure of the whole N-terminal domain of the ATPase CopA from Bacillus Subtilis. Implications for the function ; _BMRB_accession_number 5813 _BMRB_flat_file_name bmr5813.str _Entry_type original _Submission_date 2003-05-31 _Accession_date 2003-06-02 _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" 771 "13C chemical shifts" 552 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-12-18 original author 'original release' 2004-01-21 update BMRB 'update the citation' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural basis for the function of the N terminal domain of the ATPase CopA from Bacillus subtilis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14514665 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. Biol. Chem.' _Journal_volume 278 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 50506 _Page_last 50513 _Year 2003 _Details . loop_ _Keyword CopA copper folding interaction '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 $CopAab stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CopAab _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'copper-transporting ATPase CopA' _Abbreviation_common CopA _Molecular_mass 16380.7 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; MLSEQKEIAMQVSGMTCAAC AARIEKGLKRMPGVTDANVN LATETVNVIYDPAETGTAAI QEKIEKLGYHVVTEKAEFDI EGMTCAACANRIEKRLNKIE GVANAPVNFALETVTVEYNP KEASVSDLKEAVDKLGYKLK LKGEQDSIEGR ; 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 THR 74 GLU 75 LYS 76 ALA 77 GLU 78 PHE 79 ASP 80 ILE 81 GLU 82 GLY 83 MET 84 THR 85 CYS 86 ALA 87 ALA 88 CYS 89 ALA 90 ASN 91 ARG 92 ILE 93 GLU 94 LYS 95 ARG 96 LEU 97 ASN 98 LYS 99 ILE 100 GLU 101 GLY 102 VAL 103 ALA 104 ASN 105 ALA 106 PRO 107 VAL 108 ASN 109 PHE 110 ALA 111 LEU 112 GLU 113 THR 114 VAL 115 THR 116 VAL 117 GLU 118 TYR 119 ASN 120 PRO 121 LYS 122 GLU 123 ALA 124 SER 125 VAL 126 SER 127 ASP 128 LEU 129 LYS 130 GLU 131 ALA 132 VAL 133 ASP 134 LYS 135 LEU 136 GLY 137 TYR 138 LYS 139 LEU 140 LYS 141 LEU 142 LYS 143 GLY 144 GLU 145 GLN 146 ASP 147 SER 148 ILE 149 GLU 150 GLY 151 ARG stop_ _Sequence_homology_query_date . _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 1P6T 'Structure Characterization Of The Water Soluble Region Of P- Type Atpase Copa From Bacillus Subtilis' 99.34 151 100.00 100.00 2.17e-81 stop_ 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 $CopAab 'Bacillus subtilis' 224308 Bacteria . Bacillus subtilis 'BL21DE3 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_type _Vector_name $CopAab 'recombinant technology' 'E. coli' Escherichia coli PLYSS plasmide PET21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type bicell_solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CopAab 1.5 mM '[U-95% 13C; U-90% 15N]' phosphate 20 mM . H2O 90 % . D2O 10 % . DTT 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task processing stop_ _Details BRUKER save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Gunter, Mumenthaler, Wuthrich' save_ save_Xeasy _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'structure solution' stop_ _Details 'Xia, Bartels' 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 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _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_13C-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_CC(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_(H)CCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-TOCSY _Sample_label . save_ save_CBCANH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _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 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _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' 22 0.05 mM pH 7.0 0.1 n/a pressure 1 0.01 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 TMS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 TMS H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel 1.0 TMS N 15 'methyl protons' ppm 0.00 . 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 ; several unassigned signals were observed that may correspond to a minor conformation species ; 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 . 2 LEU C C 174.284 0.1 1 2 . 3 SER N N 116.612 0.1 1 3 . 3 SER H H 8.268 0.1 1 4 . 3 SER CA C 55.486 0.1 1 5 . 3 SER HA H 4.348 0.1 1 6 . 3 SER HB2 H 3.742 0.1 1 7 . 3 SER C C 171.457 0.1 1 8 . 4 GLU N N 122.652 0.1 1 9 . 4 GLU H H 8.401 0.1 1 10 . 4 GLU CA C 53.607 0.1 1 11 . 4 GLU HA H 4.218 0.1 1 12 . 4 GLU CB C 28.241 0.1 1 13 . 4 GLU HB2 H 1.904 0.1 1 14 . 4 GLU HB3 H 1.806 0.1 1 15 . 4 GLU CG C 33.565 0.1 1 16 . 4 GLU HG2 H 2.101 0.1 1 17 . 4 GLU HG3 H 2.042 0.1 1 18 . 4 GLU C C 172.726 0.1 1 19 . 5 GLN N N 118.947 0.1 1 20 . 5 GLN H H 7.970 0.1 1 21 . 5 GLN CA C 52.354 0.1 1 22 . 5 GLN HA H 4.430 0.1 1 23 . 5 GLN CB C 27.928 0.1 1 24 . 5 GLN HB2 H 1.777 0.1 1 25 . 5 GLN HB3 H 1.640 0.1 1 26 . 5 GLN CG C 31.686 0.1 1 27 . 5 GLN HG2 H 2.087 0.1 1 28 . 5 GLN HG3 H 2.016 0.1 1 29 . 5 GLN NE2 N 111.127 0.1 1 30 . 5 GLN HE21 H 7.326 0.1 1 31 . 5 GLN HE22 H 6.528 0.1 1 32 . 5 GLN C C 172.098 0.1 1 33 . 6 LYS N N 122.628 0.1 1 34 . 6 LYS H H 8.581 0.1 1 35 . 6 LYS CA C 51.415 0.1 1 36 . 6 LYS HA H 4.352 0.1 1 37 . 6 LYS CB C 32.939 0.1 1 38 . 6 LYS HB2 H 1.186 0.1 1 39 . 6 LYS HB3 H 0.683 0.1 1 40 . 6 LYS CG C 22.918 0.1 1 41 . 6 LYS HG2 H 1.103 0.1 1 42 . 6 LYS CD C 26.362 0.1 1 43 . 6 LYS HD2 H 1.580 0.1 1 44 . 6 LYS CE C 39.515 0.1 1 45 . 6 LYS HE2 H 2.920 0.1 1 46 . 6 LYS C C 174.067 0.1 1 47 . 7 GLU N N 120.161 0.1 1 48 . 7 GLU H H 8.119 0.1 1 49 . 7 GLU CA C 51.415 0.1 1 50 . 7 GLU HA H 5.476 0.1 1 51 . 7 GLU CB C 29.807 0.1 1 52 . 7 GLU HB2 H 1.827 0.1 1 53 . 7 GLU HB3 H 1.710 0.1 1 54 . 7 GLU CG C 33.565 0.1 1 55 . 7 GLU HG2 H 1.988 0.1 1 56 . 7 GLU C C 173.325 0.1 1 57 . 8 ILE N N 121.774 0.1 1 58 . 8 ILE H H 9.043 0.1 1 59 . 8 ILE CA C 55.799 0.1 1 60 . 8 ILE HA H 4.790 0.1 1 61 . 8 ILE CB C 39.828 0.1 1 62 . 8 ILE HB H 1.820 0.1 1 63 . 8 ILE HG2 H 0.865 0.1 1 64 . 8 ILE CG2 C 15.402 0.1 1 65 . 8 ILE CG1 C 25.423 0.1 1 66 . 8 ILE HG12 H 1.345 0.1 1 67 . 8 ILE HG13 H 1.035 0.1 1 68 . 8 ILE HD1 H 0.838 0.1 1 69 . 8 ILE CD1 C 11.957 0.1 1 70 . 8 ILE C C 169.091 0.1 1 71 . 9 ALA N N 127.425 0.1 1 72 . 9 ALA H H 8.389 0.1 1 73 . 9 ALA CA C 47.344 0.1 1 74 . 9 ALA HA H 5.417 0.1 1 75 . 9 ALA HB H 1.134 0.1 1 76 . 9 ALA CB C 18.847 0.1 1 77 . 9 ALA C C 173.807 0.1 1 78 . 10 MET N N 116.690 0.1 1 79 . 10 MET H H 8.701 0.1 1 80 . 10 MET CA C 51.728 0.1 1 81 . 10 MET HA H 4.494 0.1 1 82 . 10 MET CB C 34.191 0.1 1 83 . 10 MET HB2 H 1.882 0.1 1 84 . 10 MET HB3 H 1.567 0.1 1 85 . 10 MET CG C 29.494 0.1 1 86 . 10 MET HG2 H 2.322 0.1 1 87 . 10 MET HG3 H 2.145 0.1 1 88 . 10 MET C C 171.073 0.1 1 89 . 11 GLN N N 125.597 0.1 1 90 . 11 GLN H H 9.688 0.1 1 91 . 11 GLN CA C 52.041 0.1 1 92 . 11 GLN HA H 4.986 0.1 1 93 . 11 GLN CB C 26.676 0.1 1 94 . 11 GLN HB2 H 1.968 0.1 1 95 . 11 GLN HB3 H 1.843 0.1 1 96 . 11 GLN CG C 31.373 0.1 1 97 . 11 GLN HG2 H 2.441 0.1 1 98 . 11 GLN HG3 H 2.132 0.1 1 99 . 11 GLN NE2 N 109.994 0.1 1 100 . 11 GLN HE21 H 7.438 0.1 1 101 . 11 GLN HE22 H 6.730 0.1 1 102 . 11 GLN C C 172.212 0.1 1 103 . 12 VAL N N 124.329 0.1 1 104 . 12 VAL H H 8.507 0.1 1 105 . 12 VAL CA C 57.364 0.1 1 106 . 12 VAL HA H 5.035 0.1 1 107 . 12 VAL CB C 32.939 0.1 1 108 . 12 VAL HB H 1.549 0.1 1 109 . 12 VAL HG1 H 0.670 0.1 1 110 . 12 VAL HG2 H 0.644 0.1 1 111 . 12 VAL CG1 C 19.473 0.1 1 112 . 12 VAL CG2 C 19.473 0.1 1 113 . 12 VAL C C 172.722 0.1 1 114 . 13 SER N N 122.065 0.1 1 115 . 13 SER H H 9.516 0.1 1 116 . 13 SER CA C 54.233 0.1 1 117 . 13 SER HA H 4.834 0.1 1 118 . 13 SER CB C 63.001 0.1 1 119 . 13 SER HB2 H 3.860 0.1 1 120 . 13 SER HB3 H 3.656 0.1 1 121 . 13 SER C C 171.575 0.1 1 122 . 14 GLY N N 108.729 0.1 1 123 . 14 GLY H H 8.536 0.1 1 124 . 14 GLY HA2 H 4.653 0.1 1 125 . 14 GLY C C 172.609 0.1 1 126 . 15 MET N N 120.645 0.1 1 127 . 15 MET H H 9.110 0.1 1 128 . 15 MET CA C 53.920 0.1 1 129 . 15 MET HA H 4.813 0.1 1 130 . 15 MET CB C 31.060 0.1 1 131 . 15 MET HB2 H 2.384 0.1 1 132 . 15 MET HB3 H 1.374 0.1 1 133 . 15 MET CG C 28.554 0.1 1 134 . 15 MET HG2 H 2.015 0.1 1 135 . 15 MET HG3 H 1.367 0.1 1 136 . 15 MET C C 175.206 0.1 1 137 . 16 THR N N 117.957 0.1 1 138 . 16 THR H H 10.267 0.1 1 139 . 16 THR CA C 59.870 0.1 1 140 . 16 THR HA H 4.506 0.1 1 141 . 16 THR CB C 68.325 0.1 1 142 . 16 THR HB H 4.257 0.1 1 143 . 16 THR HG2 H 1.121 0.1 1 144 . 16 THR CG2 C 18.847 0.1 1 145 . 16 THR C C 172.061 0.1 1 146 . 17 CYS N N 115.831 0.1 1 147 . 17 CYS H H 8.033 0.1 1 148 . 17 CYS CA C 53.920 0.1 1 149 . 17 CYS HA H 4.954 0.1 1 150 . 17 CYS CB C 28.241 0.1 1 151 . 17 CYS HB2 H 3.388 0.1 1 152 . 17 CYS HB3 H 3.000 0.1 1 153 . 18 ALA C C 171.453 0.1 1 154 . 19 ALA N N 121.827 0.1 1 155 . 19 ALA H H 8.406 0.1 1 156 . 19 ALA CA C 52.667 0.1 1 157 . 19 ALA HA H 4.147 0.1 1 158 . 19 ALA HB H 1.458 0.1 1 159 . 19 ALA CB C 15.402 0.1 1 160 . 19 ALA C C 178.005 0.1 1 161 . 20 CYS N N 121.937 0.1 1 162 . 20 CYS H H 7.667 0.1 1 163 . 20 CYS CA C 61.435 0.1 1 164 . 20 CYS HA H 3.930 0.1 1 165 . 20 CYS CB C 26.676 0.1 1 166 . 20 CYS HB2 H 3.187 0.1 1 167 . 20 CYS HB3 H 2.582 0.1 1 168 . 20 CYS C C 174.528 0.1 1 169 . 21 ALA N N 118.645 0.1 1 170 . 21 ALA H H 6.686 0.1 1 171 . 21 ALA CA C 52.354 0.1 1 172 . 21 ALA HA H 3.676 0.1 1 173 . 21 ALA HB H 1.313 0.1 1 174 . 21 ALA CB C 15.402 0.1 1 175 . 21 ALA C C 176.095 0.1 1 176 . 22 ALA N N 117.791 0.1 1 177 . 22 ALA H H 7.736 0.1 1 178 . 22 ALA CA C 52.041 0.1 1 179 . 22 ALA HA H 4.066 0.1 1 180 . 22 ALA HB H 1.376 0.1 1 181 . 22 ALA CB C 15.402 0.1 1 182 . 22 ALA C C 177.085 0.1 1 183 . 23 ARG N N 118.510 0.1 1 184 . 23 ARG H H 7.885 0.1 1 185 . 23 ARG CA C 56.738 0.1 1 186 . 23 ARG HA H 3.935 0.1 1 187 . 23 ARG CB C 27.302 0.1 1 188 . 23 ARG HB2 H 2.004 0.1 1 189 . 23 ARG HB3 H 1.952 0.1 1 190 . 23 ARG CG C 25.423 0.1 1 191 . 23 ARG HG2 H 1.796 0.1 1 192 . 23 ARG HG3 H 1.592 0.1 1 193 . 23 ARG CD C 41.081 0.1 1 194 . 23 ARG HD2 H 3.403 0.1 1 195 . 23 ARG HD3 H 3.298 0.1 1 196 . 23 ARG C C 177.144 0.1 1 197 . 24 ILE N N 120.069 0.1 1 198 . 24 ILE H H 7.808 0.1 1 199 . 24 ILE CA C 63.001 0.1 1 200 . 24 ILE HA H 3.432 0.1 1 201 . 24 ILE CB C 35.757 0.1 1 202 . 24 ILE HB H 1.533 0.1 1 203 . 24 ILE HG2 H 0.447 0.1 1 204 . 24 ILE CG2 C 15.089 0.1 1 205 . 24 ILE CG1 C 27.928 0.1 1 206 . 24 ILE HG12 H 1.460 0.1 1 207 . 24 ILE HG13 H 0.290 0.1 1 208 . 24 ILE HD1 H -0.100 0.1 1 209 . 24 ILE CD1 C 11.018 0.1 1 210 . 24 ILE C C 173.350 0.1 1 211 . 25 GLU N N 118.375 0.1 1 212 . 25 GLU H H 8.273 0.1 1 213 . 25 GLU CA C 58.304 0.1 1 214 . 25 GLU HA H 3.369 0.1 1 215 . 25 GLU CB C 27.302 0.1 1 216 . 25 GLU HB2 H 2.053 0.1 1 217 . 25 GLU HB3 H 1.819 0.1 1 218 . 25 GLU CG C 34.817 0.1 1 219 . 25 GLU HG2 H 2.434 0.1 1 220 . 25 GLU HG3 H 1.844 0.1 1 221 . 25 GLU C C 175.454 0.1 1 222 . 26 LYS N N 115.392 0.1 1 223 . 26 LYS H H 8.247 0.1 1 224 . 26 LYS CA C 56.738 0.1 1 225 . 26 LYS HA H 3.809 0.1 1 226 . 26 LYS CB C 29.494 0.1 1 227 . 26 LYS HB2 H 1.803 0.1 1 228 . 26 LYS HB3 H 1.677 0.1 1 229 . 26 LYS CG C 22.605 0.1 1 230 . 26 LYS HG2 H 1.491 0.1 1 231 . 26 LYS HG3 H 1.308 0.1 1 232 . 26 LYS HD2 H 1.526 0.1 1 233 . 26 LYS HE2 H 3.043 0.1 1 234 . 26 LYS HE3 H 2.852 0.1 1 235 . 26 LYS C C 176.612 0.1 1 236 . 27 GLY N N 104.469 0.1 1 237 . 27 GLY H H 7.808 0.1 1 238 . 27 GLY CA C 44.212 0.1 1 239 . 27 GLY HA2 H 3.714 0.1 1 240 . 27 GLY HA3 H 3.433 0.1 1 241 . 27 GLY C C 173.277 0.1 1 242 . 28 LEU N N 119.802 0.1 1 243 . 28 LEU H H 8.201 0.1 1 244 . 28 LEU CA C 54.859 0.1 1 245 . 28 LEU HA H 4.040 0.1 1 246 . 28 LEU CB C 39.515 0.1 1 247 . 28 LEU HB2 H 1.646 0.1 1 248 . 28 LEU HB3 H 0.977 0.1 1 249 . 28 LEU CG C 24.483 0.1 1 250 . 28 LEU HG H 0.470 0.1 1 251 . 28 LEU HD1 H 0.757 0.1 1 252 . 28 LEU HD2 H 0.725 0.1 1 253 . 28 LEU CD1 C 20.412 0.1 1 254 . 28 LEU CD2 C 20.412 0.1 1 255 . 28 LEU C C 175.755 0.1 1 256 . 29 LYS N N 114.809 0.1 1 257 . 29 LYS H H 7.979 0.1 1 258 . 29 LYS CA C 56.738 0.1 1 259 . 29 LYS HA H 3.711 0.1 1 260 . 29 LYS CB C 29.807 0.1 1 261 . 29 LYS HB2 H 1.822 0.1 1 262 . 29 LYS HB3 H 1.697 0.1 1 263 . 29 LYS CG C 25.110 0.1 1 264 . 29 LYS HG2 H 1.187 0.1 1 265 . 29 LYS CD C 26.989 0.1 1 266 . 29 LYS HD2 H 1.671 0.1 1 267 . 29 LYS CE C 39.202 0.1 1 268 . 29 LYS HE2 H 3.035 0.1 1 269 . 29 LYS C C 174.875 0.1 1 270 . 30 ARG N N 114.120 0.1 1 271 . 30 ARG H H 6.897 0.1 1 272 . 30 ARG CA C 52.980 0.1 1 273 . 30 ARG HA H 4.213 0.1 1 274 . 30 ARG CB C 28.241 0.1 1 275 . 30 ARG HB2 H 1.915 0.1 1 276 . 30 ARG HB3 H 1.801 0.1 1 277 . 30 ARG CG C 24.797 0.1 1 278 . 30 ARG HG2 H 1.735 0.1 1 279 . 30 ARG HG3 H 1.647 0.1 1 280 . 30 ARG CD C 40.767 0.1 1 281 . 30 ARG HD2 H 3.082 0.1 1 282 . 30 ARG C C 173.903 0.1 1 283 . 31 MET N N 123.050 0.1 1 284 . 31 MET H H 7.756 0.1 1 285 . 31 MET CA C 51.728 0.1 1 286 . 31 MET HA H 4.445 0.1 1 287 . 31 MET CB C 30.747 0.1 1 288 . 31 MET HB2 H 2.105 0.1 1 289 . 31 MET HB3 H 2.043 0.1 1 290 . 31 MET CG C 29.181 0.1 1 291 . 31 MET HG2 H 2.627 0.1 1 292 . 31 MET HG3 H 2.445 0.1 1 293 . 32 PRO CD C 48.283 0.1 1 294 . 32 PRO CA C 61.122 0.1 1 295 . 32 PRO HA H 4.225 0.1 1 296 . 32 PRO CB C 28.868 0.1 1 297 . 32 PRO HB2 H 2.235 0.1 1 298 . 32 PRO CG C 25.110 0.1 1 299 . 32 PRO HG2 H 2.075 0.1 1 300 . 32 PRO HG3 H 1.912 0.1 1 301 . 32 PRO HD2 H 4.002 0.1 1 302 . 32 PRO HD3 H 3.564 0.1 1 303 . 32 PRO C C 174.204 0.1 1 304 . 33 GLY N N 110.418 0.1 1 305 . 33 GLY H H 8.500 0.1 1 306 . 33 GLY CA C 43.273 0.1 1 307 . 33 GLY HA2 H 4.195 0.1 1 308 . 33 GLY HA3 H 3.680 0.1 1 309 . 33 GLY C C 170.962 0.1 1 310 . 34 VAL N N 120.489 0.1 1 311 . 34 VAL H H 7.554 0.1 1 312 . 34 VAL CA C 60.809 0.1 1 313 . 34 VAL HA H 4.057 0.1 1 314 . 34 VAL CB C 29.181 0.1 1 315 . 34 VAL HB H 2.328 0.1 1 316 . 34 VAL HG1 H 0.739 0.1 1 317 . 34 VAL HG2 H 0.615 0.1 1 318 . 34 VAL CG1 C 20.412 0.1 1 319 . 34 VAL CG2 C 19.160 0.1 1 320 . 34 VAL C C 173.301 0.1 1 321 . 35 THR N N 124.879 0.1 1 322 . 35 THR H H 9.132 0.1 1 323 . 35 THR CA C 60.809 0.1 1 324 . 35 THR HA H 4.133 0.1 1 325 . 35 THR CB C 66.446 0.1 1 326 . 35 THR HB H 3.768 0.1 1 327 . 35 THR HG2 H 1.023 0.1 1 328 . 35 THR CG2 C 19.160 0.1 1 329 . 35 THR C C 171.680 0.1 1 330 . 36 ASP N N 117.810 0.1 1 331 . 36 ASP H H 8.015 0.1 1 332 . 36 ASP HA H 4.620 0.1 1 333 . 36 ASP CB C 41.081 0.1 1 334 . 36 ASP HB2 H 2.518 0.1 1 335 . 36 ASP HB3 H 2.274 0.1 1 336 . 36 ASP C C 170.532 0.1 1 337 . 37 ALA N N 120.908 0.1 1 338 . 37 ALA H H 8.181 0.1 1 339 . 37 ALA CA C 48.909 0.1 1 340 . 37 ALA HA H 5.088 0.1 1 341 . 37 ALA HB H 1.121 0.1 1 342 . 37 ALA CB C 20.412 0.1 1 343 . 37 ALA C C 171.897 0.1 1 344 . 38 ASN N N 117.241 0.1 1 345 . 38 ASN H H 8.698 0.1 1 346 . 38 ASN CA C 49.849 0.1 1 347 . 38 ASN HA H 4.954 0.1 1 348 . 38 ASN CB C 40.454 0.1 1 349 . 38 ASN HB2 H 2.468 0.1 1 350 . 38 ASN ND2 N 114.387 0.1 1 351 . 38 ASN HD21 H 7.658 0.1 1 352 . 38 ASN HD22 H 6.635 0.1 1 353 . 38 ASN C C 170.773 0.1 1 354 . 39 VAL N N 125.897 0.1 1 355 . 39 VAL H H 9.751 0.1 1 356 . 39 VAL CA C 58.617 0.1 1 357 . 39 VAL HA H 4.342 0.1 1 358 . 39 VAL CB C 30.120 0.1 1 359 . 39 VAL HB H 1.848 0.1 1 360 . 39 VAL HG1 H 0.829 0.1 1 361 . 39 VAL HG2 H 0.574 0.1 1 362 . 39 VAL CG1 C 19.473 0.1 1 363 . 39 VAL CG2 C 18.847 0.1 1 364 . 39 VAL C C 171.530 0.1 1 365 . 40 ASN N N 126.746 0.1 1 366 . 40 ASN H H 8.879 0.1 1 367 . 40 ASN CA C 48.596 0.1 1 368 . 40 ASN HA H 4.765 0.1 1 369 . 40 ASN CB C 36.383 0.1 1 370 . 40 ASN HB2 H 3.053 0.1 1 371 . 40 ASN HB3 H 2.392 0.1 1 372 . 40 ASN ND2 N 111.552 0.1 1 373 . 40 ASN HD21 H 7.355 0.1 1 374 . 40 ASN HD22 H 6.843 0.1 1 375 . 40 ASN C C 172.411 0.1 1 376 . 41 LEU N N 125.451 0.1 1 377 . 41 LEU H H 8.756 0.1 1 378 . 41 LEU CA C 55.172 0.1 1 379 . 41 LEU HA H 3.710 0.1 1 380 . 41 LEU CB C 39.828 0.1 1 381 . 41 LEU HB2 H 1.538 0.1 1 382 . 41 LEU HB3 H 1.389 0.1 1 383 . 41 LEU CG C 24.170 0.1 1 384 . 41 LEU HG H 1.435 0.1 1 385 . 41 LEU HD1 H 0.658 0.1 1 386 . 41 LEU HD2 H 0.620 0.1 1 387 . 41 LEU CD1 C 21.665 0.1 1 388 . 41 LEU CD2 C 21.978 0.1 1 389 . 41 LEU C C 176.071 0.1 1 390 . 42 ALA N N 119.244 0.1 1 391 . 42 ALA H H 8.017 0.1 1 392 . 42 ALA CA C 52.354 0.1 1 393 . 42 ALA HA H 4.021 0.1 1 394 . 42 ALA HB H 1.411 0.1 1 395 . 42 ALA CB C 15.715 0.1 1 396 . 42 ALA C C 177.052 0.1 1 397 . 43 THR N N 104.050 0.1 1 398 . 43 THR H H 7.213 0.1 1 399 . 43 THR CA C 57.678 0.1 1 400 . 43 THR HA H 4.339 0.1 1 401 . 43 THR CB C 66.133 0.1 1 402 . 43 THR HB H 4.379 0.1 1 403 . 43 THR HG2 H 0.962 0.1 1 404 . 43 THR CG2 C 18.534 0.1 1 405 . 43 THR C C 172.004 0.1 1 406 . 44 GLU N N 120.337 0.1 1 407 . 44 GLU H H 7.799 0.1 1 408 . 44 GLU CA C 55.172 0.1 1 409 . 44 GLU HA H 3.370 0.1 1 410 . 44 GLU CB C 24.483 0.1 1 411 . 44 GLU HB2 H 2.06 0.1 1 412 . 44 GLU HB3 H 1.66 0.1 1 413 . 44 GLU CG C 35.131 0.1 1 414 . 44 GLU HG2 H 2.059 0.1 1 415 . 44 GLU HG3 H 1.664 0.1 1 416 . 44 GLU C C 170.707 0.1 1 417 . 45 THR N N 110.133 0.1 1 418 . 45 THR H H 7.613 0.1 1 419 . 45 THR CA C 58.930 0.1 1 420 . 45 THR HA H 5.086 0.1 1 421 . 45 THR CB C 69.264 0.1 1 422 . 45 THR HB H 3.658 0.1 1 423 . 45 THR HG2 H 0.956 0.1 1 424 . 45 THR CG2 C 18.534 0.1 1 425 . 45 THR C C 170.314 0.1 1 426 . 46 VAL N N 125.582 0.1 1 427 . 46 VAL H H 9.250 0.1 1 428 . 46 VAL CA C 57.364 0.1 1 429 . 46 VAL HA H 4.589 0.1 1 430 . 46 VAL CB C 31.999 0.1 1 431 . 46 VAL HB H 1.644 0.1 1 432 . 46 VAL HG1 H 0.651 0.1 1 433 . 46 VAL HG2 H 0.560 0.1 1 434 . 46 VAL C C 170.082 0.1 1 435 . 46 VAL CG2 C 17.907 0.1 1 436 . 46 VAL CG1 C 19.473 0.1 1 437 . 47 ASN N N 126.063 0.1 1 438 . 47 ASN H H 8.699 0.1 1 439 . 47 ASN CA C 49.849 0.1 1 440 . 47 ASN HA H 5.575 0.1 1 441 . 47 ASN CB C 38.575 0.1 1 442 . 47 ASN HB2 H 2.538 0.1 1 443 . 47 ASN HB3 H 2.472 0.1 1 444 . 47 ASN ND2 N 112.403 0.1 1 445 . 47 ASN HD21 H 7.568 0.1 1 446 . 47 ASN HD22 H 6.706 0.1 1 447 . 47 ASN C C 171.958 0.1 1 448 . 48 VAL N N 123.755 0.1 1 449 . 48 VAL H H 9.203 0.1 1 450 . 48 VAL HA H 4.624 0.1 1 451 . 48 VAL CB C 32.625 0.1 1 452 . 48 VAL HB H 1.863 0.1 1 453 . 48 VAL HG1 H 0.989 0.1 1 454 . 48 VAL HG2 H 0.722 0.1 1 455 . 48 VAL CG1 C 20.412 0.1 1 456 . 48 VAL CG2 C 20.412 0.1 1 457 . 48 VAL C C 170.800 0.1 1 458 . 49 ILE N N 127.322 0.1 1 459 . 49 ILE H H 8.465 0.1 1 460 . 49 ILE CA C 57.364 0.1 1 461 . 49 ILE HA H 5.125 0.1 1 462 . 49 ILE CB C 36.383 0.1 1 463 . 49 ILE HB H 1.457 0.1 1 464 . 49 ILE HG2 H 0.712 0.1 1 465 . 49 ILE CG2 C 15.402 0.1 1 466 . 49 ILE CG1 C 24.797 0.1 1 467 . 49 ILE HG12 H 1.448 0.1 1 468 . 49 ILE HG13 H 0.867 0.1 1 469 . 49 ILE HD1 H 0.662 0.1 1 470 . 49 ILE CD1 C 10.705 0.1 1 471 . 49 ILE C C 172.814 0.1 1 472 . 50 TYR N N 124.475 0.1 1 473 . 50 TYR H H 9.344 0.1 1 474 . 50 TYR CA C 52.667 0.1 1 475 . 50 TYR HA H 5.487 0.1 1 476 . 50 TYR CB C 39.515 0.1 1 477 . 50 TYR HB2 H 2.641 0.1 1 478 . 50 TYR HB3 H 2.460 0.1 1 479 . 50 TYR HD2 H 6.498 0.1 1 480 . 50 TYR HE2 H 6.385 0.1 1 481 . 50 TYR C C 168.602 0.1 1 482 . 51 ASP N N 119.180 0.1 1 483 . 51 ASP H H 8.794 0.1 1 484 . 51 ASP CA C 47.030 0.1 1 485 . 51 ASP HA H 5.010 0.1 1 486 . 51 ASP CB C 39.515 0.1 1 487 . 51 ASP HB2 H 2.962 0.1 1 488 . 51 ASP HB3 H 2.472 0.1 1 489 . 52 PRO CD C 48.596 0.1 1 490 . 52 PRO CA C 60.496 0.1 1 491 . 52 PRO HA H 5.099 0.1 1 492 . 52 PRO CB C 29.807 0.1 1 493 . 52 PRO HB2 H 2.157 0.1 1 494 . 52 PRO CG C 24.170 0.1 1 495 . 52 PRO HG2 H 1.891 0.1 1 496 . 52 PRO HG3 H 1.690 0.1 1 497 . 52 PRO HD2 H 3.989 0.1 1 498 . 52 PRO HD3 H 3.579 0.1 1 499 . 52 PRO C C 174.342 0.1 1 500 . 53 ALA N N 120.772 0.1 1 501 . 53 ALA H H 8.543 0.1 1 502 . 53 ALA CA C 50.475 0.1 1 503 . 53 ALA HA H 4.249 0.1 1 504 . 53 ALA HB H 1.380 0.1 1 505 . 53 ALA CB C 16.028 0.1 1 506 . 53 ALA C C 175.824 0.1 1 507 . 54 GLU N N 115.547 0.1 1 508 . 54 GLU H H 7.780 0.1 1 509 . 54 GLU CA C 53.293 0.1 1 510 . 54 GLU HA H 4.395 0.1 1 511 . 54 GLU CB C 31.373 0.1 1 512 . 54 GLU HB2 H 1.929 0.1 1 513 . 54 GLU HB3 H 1.770 0.1 1 514 . 54 GLU CG C 32.939 0.1 1 515 . 54 GLU HG2 H 2.110 0.1 1 516 . 54 GLU HG3 H 1.944 0.1 1 517 . 54 GLU C C 172.814 0.1 1 518 . 55 THR N N 114.104 0.1 1 519 . 55 THR H H 8.017 0.1 1 520 . 55 THR HA H 4.484 0.1 1 521 . 55 THR CB C 65.506 0.1 1 522 . 55 THR HB H 4.129 0.1 1 523 . 55 THR HG2 H 0.867 0.1 1 524 . 55 THR HG1 H 5.347 0.1 1 525 . 55 THR CG2 C 16.341 0.1 1 526 . 55 THR C C 169.179 0.1 1 527 . 55 THR CA C 57.364 0.1 1 528 . 56 GLY N N 104.889 0.1 1 529 . 56 GLY H H 7.880 0.1 1 530 . 56 GLY CA C 42.333 0.1 1 531 . 56 GLY HA2 H 4.177 0.1 1 532 . 56 GLY HA3 H 3.889 0.1 1 533 . 56 GLY C C 170.267 0.1 1 534 . 57 THR N N 110.418 0.1 1 535 . 57 THR H H 8.302 0.1 1 536 . 57 THR CA C 63.314 0.1 1 537 . 57 THR HA H 3.333 0.1 1 538 . 57 THR CB C 65.193 0.1 1 539 . 57 THR HB H 3.997 0.1 1 540 . 57 THR HG2 H 1.109 0.1 1 541 . 57 THR CG2 C 20.099 0.1 1 542 . 57 THR C C 173.764 0.1 1 543 . 58 ALA N N 124.182 0.1 1 544 . 58 ALA H H 8.448 0.1 1 545 . 58 ALA CA C 52.667 0.1 1 546 . 58 ALA HA H 3.997 0.1 1 547 . 58 ALA HB H 1.284 0.1 1 548 . 58 ALA CB C 14.776 0.1 1 549 . 58 ALA C C 177.399 0.1 1 550 . 59 ALA N N 120.623 0.1 1 551 . 59 ALA H H 7.692 0.1 1 552 . 59 ALA CA C 51.728 0.1 1 553 . 59 ALA HA H 3.998 0.1 1 554 . 59 ALA HB H 1.292 0.1 1 555 . 59 ALA CB C 15.089 0.1 1 556 . 59 ALA C C 178.140 0.1 1 557 . 60 ILE N N 120.356 0.1 1 558 . 60 ILE H H 7.481 0.1 1 559 . 60 ILE CA C 63.001 0.1 1 560 . 60 ILE HA H 3.215 0.1 1 561 . 60 ILE CB C 35.757 0.1 1 562 . 60 ILE HB H 1.458 0.1 1 563 . 60 ILE HG2 H 0.617 0.1 1 564 . 60 ILE CG2 C 15.089 0.1 1 565 . 60 ILE CG1 C 26.676 0.1 1 566 . 60 ILE HG12 H 1.469 0.1 1 567 . 60 ILE HG13 H 0.479 0.1 1 568 . 60 ILE HD1 H -0.058 0.1 1 569 . 60 ILE CD1 C 11.018 0.1 1 570 . 60 ILE C C 173.949 0.1 1 571 . 61 GLN N N 118.093 0.1 1 572 . 61 GLN H H 8.235 0.1 1 573 . 61 GLN CA C 57.051 0.1 1 574 . 61 GLN HA H 3.619 0.1 1 575 . 61 GLN CB C 25.110 0.1 1 576 . 61 GLN HB2 H 2.009 0.1 1 577 . 61 GLN CG C 31.060 0.1 1 578 . 61 GLN HG2 H 2.294 0.1 1 579 . 61 GLN HG3 H 2.136 0.1 1 580 . 61 GLN NE2 N 109.002 0.1 1 581 . 61 GLN HE21 H 7.073 0.1 1 582 . 61 GLN HE22 H 6.603 0.1 1 583 . 61 GLN C C 174.875 0.1 1 584 . 62 GLU N N 117.682 0.1 1 585 . 62 GLU H H 8.019 0.1 1 586 . 62 GLU CA C 56.425 0.1 1 587 . 62 GLU HA H 3.936 0.1 1 588 . 62 GLU CB C 26.676 0.1 1 589 . 62 GLU HB2 H 1.997 0.1 1 590 . 62 GLU CG C 33.565 0.1 1 591 . 62 GLU HG2 H 2.305 0.1 1 592 . 62 GLU C C 175.547 0.1 1 593 . 63 LYS N N 119.499 0.1 1 594 . 63 LYS H H 7.624 0.1 1 595 . 63 LYS CA C 55.172 0.1 1 596 . 63 LYS HA H 3.949 0.1 1 597 . 63 LYS CB C 27.302 0.1 1 598 . 63 LYS HB2 H 1.979 0.1 1 599 . 63 LYS HB3 H 1.804 0.1 1 600 . 63 LYS CG C 22.605 0.1 1 601 . 63 LYS HG2 H 1.563 0.1 1 602 . 63 LYS HG3 H 1.477 0.1 1 603 . 63 LYS CD C 26.362 0.1 1 604 . 63 LYS HD2 H 1.596 0.1 1 605 . 63 LYS HE2 H 2.811 0.1 1 606 . 63 LYS HE3 H 2.654 0.1 1 607 . 63 LYS C C 175.130 0.1 1 608 . 64 ILE N N 117.940 0.1 1 609 . 64 ILE H H 7.533 0.1 1 610 . 64 ILE CA C 63.628 0.1 1 611 . 64 ILE HA H 3.301 0.1 1 612 . 64 ILE CB C 34.817 0.1 1 613 . 64 ILE HB H 1.851 0.1 1 614 . 64 ILE HG2 H 0.662 0.1 1 615 . 64 ILE CG2 C 16.028 0.1 1 616 . 64 ILE CG1 C 27.302 0.1 1 617 . 64 ILE HG12 H 1.803 0.1 1 618 . 64 ILE HG13 H 0.622 0.1 1 619 . 64 ILE HD1 H 0.555 0.1 1 620 . 64 ILE CD1 C 11.331 0.1 1 621 . 64 ILE C C 175.014 0.1 1 622 . 65 GLU N N 118.094 0.1 1 623 . 65 GLU H H 7.869 0.1 1 624 . 65 GLU HA H 4.644 0.1 1 625 . 65 GLU CB C 26.049 0.1 1 626 . 65 GLU HB2 H 2.121 0.1 1 627 . 65 GLU HB3 H 1.992 0.1 1 628 . 65 GLU CG C 33.878 0.1 1 629 . 65 GLU HG2 H 2.431 0.1 1 630 . 65 GLU HG3 H 2.316 0.1 1 631 . 65 GLU C C 179.714 0.1 1 632 . 66 LYS N N 122.495 0.1 1 633 . 66 LYS H H 8.659 0.1 1 634 . 66 LYS CA C 55.799 0.1 1 635 . 66 LYS HA H 3.960 0.1 1 636 . 66 LYS CB C 29.494 0.1 1 637 . 66 LYS HB2 H 1.970 0.1 1 638 . 66 LYS HB3 H 1.820 0.1 1 639 . 66 LYS HG2 H 1.536 0.1 1 640 . 66 LYS HG3 H 1.451 0.1 1 641 . 66 LYS CD C 26.362 0.1 1 642 . 66 LYS HD2 H 1.565 0.1 1 643 . 66 LYS HE2 H 2.833 0.1 1 644 . 66 LYS C C 176.519 0.1 1 645 . 67 LEU N N 118.096 0.1 1 646 . 67 LEU H H 7.865 0.1 1 647 . 67 LEU CA C 52.980 0.1 1 648 . 67 LEU HA H 4.138 0.1 1 649 . 67 LEU CB C 39.828 0.1 1 650 . 67 LEU HB2 H 2.193 0.1 1 651 . 67 LEU HB3 H 1.481 0.1 1 652 . 67 LEU CG C 23.857 0.1 1 653 . 67 LEU HG H 1.898 0.1 1 654 . 67 LEU HD1 H 0.800 0.1 1 655 . 67 LEU HD2 H 0.760 0.1 1 656 . 67 LEU CD1 C 20.099 0.1 1 657 . 67 LEU CD2 C 20.099 0.1 1 658 . 67 LEU C C 173.589 0.1 1 659 . 68 GLY N N 104.032 0.1 1 660 . 68 GLY H H 7.635 0.1 1 661 . 68 GLY CA C 41.707 0.1 1 662 . 68 GLY HA2 H 3.875 0.1 1 663 . 68 GLY HA3 H 3.360 0.1 1 664 . 68 GLY C C 170.344 0.1 1 665 . 69 TYR N N 119.790 0.1 1 666 . 69 TYR H H 7.243 0.1 1 667 . 69 TYR CA C 53.607 0.1 1 668 . 69 TYR HA H 4.581 0.1 1 669 . 69 TYR CB C 37.010 0.1 1 670 . 69 TYR HB2 H 3.063 0.1 1 671 . 69 TYR HB3 H 2.186 0.1 1 672 . 69 TYR HD2 H 6.670 0.1 1 673 . 69 TYR C C 170.194 0.1 1 674 . 70 HIS N N 114.259 0.1 1 675 . 70 HIS H H 7.659 0.1 1 676 . 70 HIS CA C 51.728 0.1 1 677 . 70 HIS HA H 5.055 0.1 1 678 . 70 HIS CB C 28.241 0.1 1 679 . 70 HIS HB2 H 3.032 0.1 1 680 . 70 HIS HB3 H 2.893 0.1 1 681 . 70 HIS HD2 H 6.955 0.1 1 682 . 70 HIS C C 171.100 0.1 1 683 . 71 VAL N N 125.890 0.1 1 684 . 71 VAL H H 8.863 0.1 1 685 . 71 VAL CA C 60.183 0.1 1 686 . 71 VAL HA H 4.230 0.1 1 687 . 71 VAL CB C 29.181 0.1 1 688 . 71 VAL HB H 1.841 0.1 1 689 . 71 VAL HG1 H 0.863 0.1 1 690 . 71 VAL HG2 H 0.777 0.1 1 691 . 71 VAL CG1 C 20.412 0.1 1 692 . 71 VAL CG2 C 18.847 0.1 1 693 . 71 VAL C C 172.823 0.1 1 694 . 72 VAL N N 129.553 0.1 1 695 . 72 VAL H H 8.587 0.1 1 696 . 72 VAL CA C 60.809 0.1 1 697 . 72 VAL HA H 3.764 0.1 1 698 . 72 VAL CB C 29.494 0.1 1 699 . 72 VAL HB H 1.705 0.1 1 700 . 72 VAL HG1 H 0.823 0.1 1 701 . 72 VAL HG2 H 0.747 0.1 1 702 . 72 VAL CG1 C 18.534 0.1 1 703 . 72 VAL CG2 C 18.220 0.1 1 704 . 72 VAL C C 172.840 0.1 1 705 . 73 THR N N 116.557 0.1 1 706 . 73 THR H H 7.749 0.1 1 707 . 73 THR CA C 56.738 0.1 1 708 . 73 THR HA H 4.520 0.1 1 709 . 73 THR CB C 68.638 0.1 1 710 . 73 THR HB H 4.009 0.1 1 711 . 73 THR HG2 H 0.883 0.1 1 712 . 73 THR CG2 C 19.160 0.1 1 713 . 73 THR C C 170.701 0.1 1 714 . 74 GLU N N 120.337 0.1 1 715 . 74 GLU H H 8.587 0.1 1 716 . 74 GLU CA C 51.415 0.1 1 717 . 74 GLU HA H 4.446 0.1 1 718 . 74 GLU CB C 30.433 0.1 1 719 . 74 GLU HB2 H 1.483 0.1 1 720 . 74 GLU CG C 33.565 0.1 1 721 . 74 GLU HG2 H 1.958 0.1 1 722 . 74 GLU C C 176.936 0.1 1 723 . 75 LYS N N 118.805 0.1 1 724 . 75 LYS H H 8.255 0.1 1 725 . 75 LYS CA C 51.728 0.1 1 726 . 75 LYS HA H 5.535 0.1 1 727 . 75 LYS CB C 32.939 0.1 1 728 . 75 LYS HB2 H 1.506 0.1 1 729 . 75 LYS HB3 H 1.388 0.1 1 730 . 75 LYS CG C 22.918 0.1 1 731 . 75 LYS HG2 H 1.275 0.1 1 732 . 75 LYS HG3 H 1.049 0.1 1 733 . 75 LYS CD C 26.989 0.1 1 734 . 75 LYS HD2 H 1.454 0.1 1 735 . 75 LYS HE2 H 2.734 0.1 1 736 . 75 LYS C C 173.298 0.1 1 737 . 76 ALA N N 126.017 0.1 1 738 . 76 ALA H H 8.929 0.1 1 739 . 76 ALA CA C 47.970 0.1 1 740 . 76 ALA HA H 4.556 0.1 1 741 . 76 ALA HB H 1.066 0.1 1 742 . 76 ALA CB C 19.786 0.1 1 743 . 76 ALA C C 171.195 0.1 1 744 . 77 GLU N N 122.635 0.1 1 745 . 77 GLU H H 8.348 0.1 1 746 . 77 GLU CA C 52.354 0.1 1 747 . 77 GLU HA H 4.848 0.1 1 748 . 77 GLU CB C 29.181 0.1 1 749 . 77 GLU HB2 H 1.765 0.1 1 750 . 77 GLU HB3 H 1.684 0.1 1 751 . 77 GLU CG C 33.565 0.1 1 752 . 77 GLU HG2 H 2.089 0.1 1 753 . 77 GLU HG3 H 2.022 0.1 1 754 . 77 GLU C C 171.726 0.1 1 755 . 78 PHE N N 119.516 0.1 1 756 . 78 PHE H H 8.967 0.1 1 757 . 78 PHE CA C 53.607 0.1 1 758 . 78 PHE HA H 5.269 0.1 1 759 . 78 PHE CB C 39.828 0.1 1 760 . 78 PHE HB2 H 2.847 0.1 1 761 . 78 PHE HB3 H 2.618 0.1 1 762 . 78 PHE HD2 H 6.873 0.1 1 763 . 78 PHE C C 174.140 0.1 1 764 . 79 ASP N N 120.763 0.1 1 765 . 79 ASP H H 9.145 0.1 1 766 . 79 ASP CA C 52.041 0.1 1 767 . 79 ASP HA H 5.198 0.1 1 768 . 79 ASP CB C 40.454 0.1 1 769 . 79 ASP HB2 H 2.761 0.1 1 770 . 79 ASP HB3 H 2.371 0.1 1 771 . 79 ASP C C 172.899 0.1 1 772 . 80 ILE N N 118.813 0.1 1 773 . 80 ILE H H 8.155 0.1 1 774 . 80 ILE CA C 57.364 0.1 1 775 . 80 ILE HA H 4.793 0.1 1 776 . 80 ILE CB C 38.262 0.1 1 777 . 80 ILE HB H 1.129 0.1 1 778 . 80 ILE HG12 H 0.607 0.1 1 779 . 80 ILE HG13 H 1.323 0.1 1 780 . 80 ILE CG2 C 15.402 0.1 1 781 . 80 ILE CG1 C 25.110 0.1 1 782 . 80 ILE HD1 H 0.509 0.1 1 783 . 80 ILE CD1 C 12.584 0.1 1 784 . 80 ILE C C 174.081 0.1 1 785 . 81 GLU N N 129.161 0.1 1 786 . 81 GLU H H 9.413 0.1 1 787 . 81 GLU HA H 4.772 0.1 1 788 . 81 GLU CB C 30.120 0.1 1 789 . 81 GLU HB2 H 1.942 0.1 1 790 . 81 GLU HB3 H 1.802 0.1 1 791 . 81 GLU CG C 33.565 0.1 1 792 . 81 GLU HG2 H 2.071 0.1 1 793 . 81 GLU C C 173.643 0.1 1 794 . 82 GLY N N 109.846 0.1 1 795 . 82 GLY H H 8.755 0.1 1 796 . 82 GLY CA C 42.646 0.1 1 797 . 82 GLY HA2 H 4.638 0.1 1 798 . 82 GLY HA3 H 3.690 0.1 1 799 . 82 GLY C C 172.868 0.1 1 800 . 83 MET N N 119.649 0.1 1 801 . 83 MET H H 9.039 0.1 1 802 . 83 MET HA H 4.656 0.1 1 803 . 83 MET HB2 H 2.407 0.1 1 804 . 83 MET HB3 H 1.476 0.1 1 805 . 83 MET HG2 H 1.892 0.1 1 806 . 83 MET HG3 H 1.814 0.1 1 807 . 83 MET C C 175.159 0.1 1 808 . 84 THR N N 118.805 0.1 1 809 . 84 THR H H 10.473 0.1 1 810 . 84 THR CA C 59.557 0.1 1 811 . 84 THR HA H 4.656 0.1 1 812 . 84 THR CB C 68.325 0.1 1 813 . 84 THR HB H 4.298 0.1 1 814 . 84 THR HG2 H 1.188 0.1 1 815 . 84 THR C C 172.026 0.1 1 816 . 85 CYS N N 117.962 0.1 1 817 . 85 CYS H H 8.462 0.1 1 818 . 85 CYS CA C 53.920 0.1 1 819 . 85 CYS HA H 4.783 0.1 1 820 . 85 CYS CB C 27.928 0.1 1 821 . 85 CYS HB2 H 3.349 0.1 1 822 . 85 CYS HB3 H 2.824 0.1 1 823 . 85 CYS C C 173.407 0.1 1 824 . 86 ALA N N 124.979 0.1 1 825 . 86 ALA H H 8.152 0.1 1 826 . 86 ALA C C 174.283 0.1 1 827 . 87 ALA N N 119.425 0.1 1 828 . 87 ALA H H 8.088 0.1 1 829 . 87 ALA HA H 4.022 0.1 1 830 . 87 ALA HB H 1.409 0.1 1 831 . 87 ALA CB C 16.028 0.1 1 832 . 87 ALA C C 177.988 0.1 1 833 . 88 CYS N N 121.805 0.1 1 834 . 88 CYS H H 7.785 0.1 1 835 . 88 CYS CA C 61.749 0.1 1 836 . 88 CYS HA H 3.740 0.1 1 837 . 88 CYS CB C 26.989 0.1 1 838 . 88 CYS HB2 H 3.206 0.1 1 839 . 88 CYS HB3 H 2.492 0.1 1 840 . 88 CYS C C 174.653 0.1 1 841 . 89 ALA N N 118.794 0.1 1 842 . 89 ALA H H 6.531 0.1 1 843 . 89 ALA CA C 52.354 0.1 1 844 . 89 ALA HA H 3.763 0.1 1 845 . 89 ALA HB H 1.422 0.1 1 846 . 89 ALA CB C 16.028 0.1 1 847 . 89 ALA C C 176.337 0.1 1 848 . 90 ASN N N 114.826 0.1 1 849 . 90 ASN H H 7.359 0.1 1 850 . 90 ASN CA C 53.607 0.1 1 851 . 90 ASN HA H 4.367 0.1 1 852 . 90 ASN CB C 36.383 0.1 1 853 . 90 ASN HB2 H 2.698 0.1 1 854 . 90 ASN ND2 N 111.836 0.1 1 855 . 90 ASN HD21 H 7.642 0.1 1 856 . 90 ASN HD22 H 6.887 0.1 1 857 . 90 ASN C C 174.114 0.1 1 858 . 91 ARG N N 119.236 0.1 1 859 . 91 ARG H H 7.937 0.1 1 860 . 91 ARG CA C 56.738 0.1 1 861 . 91 ARG HA H 3.896 0.1 1 862 . 91 ARG CB C 27.928 0.1 1 863 . 91 ARG HB2 H 1.943 0.1 1 864 . 91 ARG HB3 H 1.825 0.1 1 865 . 91 ARG CG C 24.797 0.1 1 866 . 91 ARG HG2 H 1.798 0.1 1 867 . 91 ARG HG3 H 1.597 0.1 1 868 . 91 ARG HD3 H 3.258 0.1 1 869 . 92 ILE N N 119.913 0.1 1 870 . 92 ILE H H 7.872 0.1 1 871 . 92 ILE CA C 63.314 0.1 1 872 . 92 ILE HA H 3.203 0.1 1 873 . 92 ILE CB C 36.070 0.1 1 874 . 92 ILE HB H 1.577 0.1 1 875 . 92 ILE HG2 H 0.492 0.1 1 876 . 92 ILE CG2 C 14.463 0.1 1 877 . 92 ILE CG1 C 28.241 0.1 1 878 . 92 ILE HG12 H 1.450 0.1 1 879 . 92 ILE HG13 H 0.291 0.1 1 880 . 92 ILE HD1 H 0.023 0.1 1 881 . 92 ILE CD1 C 11.018 0.1 1 882 . 93 GLU N N 120.763 0.1 1 883 . 93 GLU H H 8.223 0.1 1 884 . 93 GLU CA C 57.678 0.1 1 885 . 93 GLU HA H 3.712 0.1 1 886 . 93 GLU CB C 27.302 0.1 1 887 . 93 GLU HB2 H 2.247 0.1 1 888 . 93 GLU HB3 H 1.920 0.1 1 889 . 93 GLU CG C 32.939 0.1 1 890 . 93 GLU HG2 H 2.520 0.1 1 891 . 93 GLU HG3 H 2.060 0.1 1 892 . 93 GLU C C 176.304 0.1 1 893 . 94 LYS N N 116.097 0.1 1 894 . 94 LYS H H 8.277 0.1 1 895 . 94 LYS CA C 56.738 0.1 1 896 . 94 LYS HA H 3.914 0.1 1 897 . 94 LYS CB C 29.807 0.1 1 898 . 94 LYS HB2 H 1.797 0.1 1 899 . 94 LYS HB3 H 1.682 0.1 1 900 . 94 LYS CG C 22.918 0.1 1 901 . 94 LYS HG2 H 1.494 0.1 1 902 . 94 LYS HG3 H 1.361 0.1 1 903 . 94 LYS CD C 26.049 0.1 1 904 . 94 LYS HD2 H 1.557 0.1 1 905 . 94 LYS HE2 H 2.874 0.1 1 906 . 94 LYS C C 176.607 0.1 1 907 . 95 ARG N N 117.086 0.1 1 908 . 95 ARG H H 7.549 0.1 1 909 . 95 ARG CA C 54.233 0.1 1 910 . 95 ARG HA H 4.196 0.1 1 911 . 95 ARG HB2 H 1.569 0.1 1 912 . 95 ARG CG C 22.605 0.1 1 913 . 95 ARG HG2 H 1.267 0.1 1 914 . 95 ARG HD2 H 1.473 0.1 1 915 . 95 ARG C C 176.910 0.1 1 916 . 96 LEU N N 119.227 0.1 1 917 . 96 LEU H H 8.441 0.1 1 918 . 96 LEU CA C 55.172 0.1 1 919 . 96 LEU HA H 3.851 0.1 1 920 . 96 LEU CB C 39.515 0.1 1 921 . 96 LEU HB2 H 1.822 0.1 1 922 . 96 LEU HB3 H 0.909 0.1 1 923 . 96 LEU CG C 24.170 0.1 1 924 . 96 LEU HG H 0.461 0.1 1 925 . 96 LEU HD1 H 0.598 0.1 1 926 . 96 LEU HD2 H 0.569 0.1 1 927 . 96 LEU CD2 C 21.039 0.1 1 928 . 96 LEU C C 175.293 0.1 1 929 . 97 ASN N N 112.698 0.1 1 930 . 97 ASN H H 7.763 0.1 1 931 . 97 ASN CA C 52.667 0.1 1 932 . 97 ASN HA H 4.225 0.1 1 933 . 97 ASN CB C 36.696 0.1 1 934 . 97 ASN HB2 H 2.631 0.1 1 935 . 97 ASN ND2 N 110.844 0.1 1 936 . 97 ASN HD21 H 7.099 0.1 1 937 . 97 ASN HD22 H 7.013 0.1 1 938 . 97 ASN C C 173.104 0.1 1 939 . 98 LYS N N 116.233 0.1 1 940 . 98 LYS H H 7.083 0.1 1 941 . 98 LYS CA C 53.607 0.1 1 942 . 98 LYS HA H 4.208 0.1 1 943 . 98 LYS CB C 30.433 0.1 1 944 . 98 LYS HB2 H 1.914 0.1 1 945 . 98 LYS HB3 H 1.765 0.1 1 946 . 98 LYS CG C 22.605 0.1 1 947 . 98 LYS HG2 H 1.556 0.1 1 948 . 98 LYS HG3 H 1.489 0.1 1 949 . 98 LYS HD2 H 1.578 0.1 1 950 . 98 LYS HE3 H 2.885 0.1 1 951 . 98 LYS C C 174.384 0.1 1 952 . 99 ILE N N 123.185 0.1 1 953 . 99 ILE H H 7.358 0.1 1 954 . 99 ILE CA C 59.243 0.1 1 955 . 99 ILE HA H 3.822 0.1 1 956 . 99 ILE CB C 34.504 0.1 1 957 . 99 ILE HB H 1.993 0.1 1 958 . 99 ILE HG2 H 0.733 0.1 1 959 . 99 ILE CG2 C 13.523 0.1 1 960 . 99 ILE CG1 C 24.797 0.1 1 961 . 99 ILE HG12 H 1.691 0.1 1 962 . 99 ILE HG13 H 1.004 0.1 1 963 . 99 ILE HD1 H 0.667 0.1 1 964 . 99 ILE CD1 C 12.270 0.1 1 965 . 99 ILE C C 173.980 0.1 1 966 . 100 GLU N N 130.595 0.1 1 967 . 100 GLU H H 8.860 0.1 1 968 . 100 GLU CA C 56.112 0.1 1 969 . 100 GLU HA H 3.935 0.1 1 970 . 100 GLU CB C 26.049 0.1 1 971 . 100 GLU HB2 H 1.994 0.1 1 972 . 100 GLU CG C 33.565 0.1 1 973 . 100 GLU HG2 H 2.314 0.1 1 974 . 100 GLU C C 173.676 0.1 1 975 . 101 GLY N N 109.170 0.1 1 976 . 101 GLY H H 8.588 0.1 1 977 . 101 GLY CA C 42.646 0.1 1 978 . 101 GLY HA2 H 4.300 0.1 1 979 . 101 GLY HA3 H 3.884 0.1 1 980 . 101 GLY C C 172.801 0.1 1 981 . 102 VAL N N 123.056 0.1 1 982 . 102 VAL H H 8.003 0.1 1 983 . 102 VAL CA C 61.435 0.1 1 984 . 102 VAL HA H 3.930 0.1 1 985 . 102 VAL CB C 29.181 0.1 1 986 . 102 VAL HB H 2.322 0.1 1 987 . 102 VAL HG1 H 0.642 0.1 1 988 . 102 VAL HG2 H 0.622 0.1 1 989 . 102 VAL CG1 C 18.847 0.1 1 990 . 102 VAL CG2 C 18.847 0.1 1 991 . 102 VAL C C 172.194 0.1 1 992 . 103 ALA N N 131.171 0.1 1 993 . 103 ALA H H 9.169 0.1 1 994 . 103 ALA CA C 50.475 0.1 1 995 . 103 ALA HA H 4.382 0.1 1 996 . 103 ALA HB H 1.219 0.1 1 997 . 103 ALA CB C 17.594 0.1 1 998 . 103 ALA C C 174.586 0.1 1 999 . 104 ASN N N 112.127 0.1 1 1000 . 104 ASN H H 7.557 0.1 1 1001 . 104 ASN HA H 4.692 0.1 1 1002 . 104 ASN CB C 38.888 0.1 1 1003 . 104 ASN HB2 H 2.814 0.1 1 1004 . 104 ASN HB3 H 2.611 0.1 1 1005 . 104 ASN ND2 N 114.103 0.1 1 1006 . 104 ASN HD21 H 7.416 0.1 1 1007 . 104 ASN HD22 H 6.957 0.1 1 1008 . 104 ASN C C 170.039 0.1 1 1009 . 105 ALA N N 123.758 0.1 1 1010 . 105 ALA H H 8.880 0.1 1 1011 . 105 ALA CA C 47.970 0.1 1 1012 . 105 ALA HA H 4.900 0.1 1 1013 . 105 ALA HB H 1.054 0.1 1 1014 . 105 ALA CB C 18.220 0.1 1 1015 . 106 PRO CD C 46.717 0.1 1 1016 . 106 PRO CA C 59.557 0.1 1 1017 . 106 PRO HA H 4.383 0.1 1 1018 . 106 PRO CB C 27.928 0.1 1 1019 . 106 PRO HB2 H 1.995 0.1 1 1020 . 106 PRO HB3 H 1.861 0.1 1 1021 . 106 PRO CG C 25.110 0.1 1 1022 . 106 PRO HG2 H 1.844 0.1 1 1023 . 106 PRO HD2 H 3.818 0.1 1 1024 . 106 PRO HD3 H 3.491 0.1 1 1025 . 106 PRO C C 174.855 0.1 1 1026 . 107 VAL N N 129.311 0.1 1 1027 . 107 VAL H H 8.303 0.1 1 1028 . 107 VAL CA C 59.870 0.1 1 1029 . 107 VAL HA H 3.803 0.1 1 1030 . 107 VAL CB C 29.494 0.1 1 1031 . 107 VAL HB H 1.942 0.1 1 1032 . 107 VAL HG1 H 0.846 0.1 1 1033 . 107 VAL HG2 H 0.628 0.1 1 1034 . 107 VAL CG1 C 18.847 0.1 1 1035 . 107 VAL CG2 C 17.594 0.1 1 1036 . 107 VAL C C 172.430 0.1 1 1037 . 108 ASN N N 127.177 0.1 1 1038 . 108 ASN H H 9.075 0.1 1 1039 . 108 ASN CA C 48.596 0.1 1 1040 . 108 ASN HA H 4.763 0.1 1 1041 . 108 ASN CB C 36.383 0.1 1 1042 . 108 ASN HB2 H 3.168 0.1 1 1043 . 108 ASN HB3 H 2.455 0.1 1 1044 . 108 ASN ND2 N 112.969 0.1 1 1045 . 108 ASN HD21 H 7.680 0.1 1 1046 . 108 ASN HD22 H 6.805 0.1 1 1047 . 108 ASN C C 171.083 0.1 1 1048 . 109 PHE N N 125.053 0.1 1 1049 . 109 PHE H H 8.777 0.1 1 1050 . 109 PHE CA C 58.304 0.1 1 1051 . 109 PHE HA H 3.930 0.1 1 1052 . 109 PHE CB C 36.696 0.1 1 1053 . 109 PHE HB2 H 3.061 0.1 1 1054 . 109 PHE HB3 H 2.860 0.1 1 1055 . 109 PHE HD2 H 7.078 0.1 1 1056 . 109 PHE HE2 H 7.014 0.1 1 1057 . 109 PHE C C 173.568 0.1 1 1058 . 110 ALA N N 119.767 0.1 1 1059 . 110 ALA H H 8.117 0.1 1 1060 . 110 ALA CA C 52.041 0.1 1 1061 . 110 ALA HA H 3.596 0.1 1 1062 . 110 ALA HB H 1.328 0.1 1 1063 . 110 ALA CB C 15.402 0.1 1 1064 . 110 ALA C C 176.809 0.1 1 1065 . 111 LEU N N 113.098 0.1 1 1066 . 111 LEU H H 7.214 0.1 1 1067 . 111 LEU CA C 51.101 0.1 1 1068 . 111 LEU HA H 4.190 0.1 1 1069 . 111 LEU CB C 39.202 0.1 1 1070 . 111 LEU HB2 H 1.474 0.1 1 1071 . 111 LEU HB3 H 1.238 0.1 1 1072 . 111 LEU CG C 24.170 0.1 1 1073 . 111 LEU HG H 1.436 0.1 1 1074 . 111 LEU HD1 H 0.722 0.1 1 1075 . 111 LEU HD2 H 0.648 0.1 1 1076 . 111 LEU CD1 C 22.918 0.1 1 1077 . 111 LEU CD2 C 19.160 0.1 1 1078 . 111 LEU C C 174.720 0.1 1 1079 . 112 GLU N N 116.501 0.1 1 1080 . 112 GLU H H 7.709 0.1 1 1081 . 112 GLU CA C 54.546 0.1 1 1082 . 112 GLU HA H 3.306 0.1 1 1083 . 112 GLU CB C 24.170 0.1 1 1084 . 112 GLU HB2 H 2.290 0.1 1 1085 . 112 GLU HB3 H 2.193 0.1 1 1086 . 112 GLU CG C 35.131 0.1 1 1087 . 112 GLU HG2 H 1.900 0.1 1 1088 . 112 GLU HG3 H 1.745 0.1 1 1089 . 112 GLU C C 171.976 0.1 1 1090 . 113 THR N N 107.721 0.1 1 1091 . 113 THR H H 7.720 0.1 1 1092 . 113 THR CA C 56.425 0.1 1 1093 . 113 THR HA H 5.478 0.1 1 1094 . 113 THR CB C 70.517 0.1 1 1095 . 113 THR HB H 4.133 0.1 1 1096 . 113 THR HG2 H 1.101 0.1 1 1097 . 113 THR CG2 C 18.534 0.1 1 1098 . 113 THR C C 170.108 0.1 1 1099 . 114 VAL N N 116.668 0.1 1 1100 . 114 VAL H H 8.585 0.1 1 1101 . 114 VAL HA H 4.632 0.1 1 1102 . 114 VAL CB C 32.312 0.1 1 1103 . 114 VAL HB H 1.992 0.1 1 1104 . 114 VAL HG1 H 0.655 0.1 1 1105 . 114 VAL HG2 H 0.454 0.1 1 1106 . 114 VAL CG1 C 16.655 0.1 1 1107 . 114 VAL CG2 C 18.847 0.1 1 1108 . 114 VAL C C 169.500 0.1 1 1109 . 115 THR N N 125.469 0.1 1 1110 . 115 THR H H 7.840 0.1 1 1111 . 115 THR CA C 58.617 0.1 1 1112 . 115 THR HA H 5.110 0.1 1 1113 . 115 THR CB C 66.759 0.1 1 1114 . 115 THR HB H 3.875 0.1 1 1115 . 115 THR HG2 H 0.946 0.1 1 1116 . 115 THR CG2 C 18.847 0.1 1 1117 . 115 THR C C 171.015 0.1 1 1118 . 116 VAL N N 126.605 0.1 1 1119 . 116 VAL H H 9.325 0.1 1 1120 . 116 VAL HA H 4.659 0.1 1 1121 . 116 VAL CB C 31.373 0.1 1 1122 . 116 VAL HB H 2.084 0.1 1 1123 . 116 VAL HG1 H 1.037 0.1 1 1124 . 116 VAL HG2 H 0.923 0.1 1 1125 . 116 VAL CG1 C 20.412 0.1 1 1126 . 116 VAL CG2 C 20.412 0.1 1 1127 . 116 VAL C C 171.959 0.1 1 1128 . 117 GLU N N 128.582 0.1 1 1129 . 117 GLU H H 8.716 0.1 1 1130 . 117 GLU CA C 51.728 0.1 1 1131 . 117 GLU HA H 5.520 0.1 1 1132 . 117 GLU CB C 28.554 0.1 1 1133 . 117 GLU HB2 H 2.005 0.1 1 1134 . 117 GLU HB3 H 1.825 0.1 1 1135 . 117 GLU CG C 33.252 0.1 1 1136 . 117 GLU HG2 H 2.114 0.1 1 1137 . 117 GLU C C 173.272 0.1 1 1138 . 118 TYR N N 123.185 0.1 1 1139 . 118 TYR H H 9.444 0.1 1 1140 . 118 TYR CA C 52.354 0.1 1 1141 . 118 TYR HA H 5.492 0.1 1 1142 . 118 TYR CB C 39.202 0.1 1 1143 . 118 TYR HB2 H 2.753 0.1 1 1144 . 118 TYR HB3 H 2.610 0.1 1 1145 . 118 TYR HD2 H 6.723 0.1 1 1146 . 118 TYR HE2 H 6.549 0.1 1 1147 . 118 TYR C C 169.016 0.1 1 1148 . 119 ASN N N 118.226 0.1 1 1149 . 119 ASN H H 8.818 0.1 1 1150 . 119 ASN CA C 46.717 0.1 1 1151 . 119 ASN HA H 4.997 0.1 1 1152 . 119 ASN CB C 39.202 0.1 1 1153 . 119 ASN HB2 H 3.212 0.1 1 1154 . 119 ASN HB3 H 3.091 0.1 1 1155 . 119 ASN ND2 N 114.103 0.1 1 1156 . 119 ASN HD21 H 8.601 0.1 1 1157 . 119 ASN HD22 H 8.001 0.1 1 1158 . 120 PRO CD C 48.596 0.1 1 1159 . 120 PRO CA C 60.809 0.1 1 1160 . 120 PRO HA H 5.234 0.1 1 1161 . 120 PRO CB C 29.807 0.1 1 1162 . 120 PRO HB2 H 2.162 0.1 1 1163 . 120 PRO HB3 H 2.086 0.1 1 1164 . 120 PRO CG C 24.170 0.1 1 1165 . 120 PRO HG2 H 1.854 0.1 1 1166 . 120 PRO HD2 H 4.114 0.1 1 1167 . 120 PRO HD3 H 3.751 0.1 1 1168 . 120 PRO C C 172.863 0.1 1 1169 . 121 LYS N N 115.830 0.1 1 1170 . 121 LYS H H 7.723 0.1 1 1171 . 121 LYS CA C 53.293 0.1 1 1172 . 121 LYS HA H 4.242 0.1 1 1173 . 121 LYS CB C 28.554 0.1 1 1174 . 121 LYS HB2 H 1.903 0.1 1 1175 . 121 LYS HB3 H 1.792 0.1 1 1176 . 121 LYS CG C 22.605 0.1 1 1177 . 121 LYS HG2 H 1.366 0.1 1 1178 . 121 LYS HG3 H 1.258 0.1 1 1179 . 121 LYS CD C 26.049 0.1 1 1180 . 121 LYS HD2 H 1.572 0.1 1 1181 . 121 LYS HD3 H 1.483 0.1 1 1182 . 121 LYS C C 174.249 0.1 1 1183 . 122 GLU N N 116.232 0.1 1 1184 . 122 GLU H H 7.599 0.1 1 1185 . 122 GLU CA C 53.293 0.1 1 1186 . 122 GLU HA H 4.500 0.1 1 1187 . 122 GLU CB C 31.373 0.1 1 1188 . 122 GLU HB2 H 2.116 0.1 1 1189 . 122 GLU HB3 H 1.694 0.1 1 1190 . 122 GLU CG C 33.565 0.1 1 1191 . 122 GLU HG2 H 2.178 0.1 1 1192 . 122 GLU HG3 H 1.965 0.1 1 1193 . 122 GLU C C 173.474 0.1 1 1194 . 123 ALA N N 121.345 0.1 1 1195 . 123 ALA H H 8.045 0.1 1 1196 . 123 ALA CA C 48.283 0.1 1 1197 . 123 ALA HA H 4.745 0.1 1 1198 . 123 ALA HB H 1.219 0.1 1 1199 . 123 ALA CB C 18.847 0.1 1 1200 . 123 ALA C C 171.251 0.1 1 1201 . 124 SER N N 111.711 0.1 1 1202 . 124 SER H H 8.300 0.1 1 1203 . 124 SER CA C 52.667 0.1 1 1204 . 124 SER HA H 4.881 0.1 1 1205 . 124 SER CB C 64.880 0.1 1 1206 . 124 SER HB2 H 4.083 0.1 1 1207 . 124 SER HB3 H 3.809 0.1 1 1208 . 124 SER C C 172.565 0.1 1 1209 . 125 VAL N N 119.939 0.1 1 1210 . 125 VAL H H 8.666 0.1 1 1211 . 125 VAL CA C 64.880 0.1 1 1212 . 125 VAL HA H 3.337 0.1 1 1213 . 125 VAL CB C 28.554 0.1 1 1214 . 125 VAL HB H 2.043 0.1 1 1215 . 125 VAL HG1 H 1.043 0.1 1 1216 . 125 VAL HG2 H 1.002 0.1 1 1217 . 125 VAL CG1 C 20.412 0.1 1 1218 . 125 VAL CG2 C 18.847 0.1 1 1219 . 125 VAL C C 175.359 0.1 1 1220 . 126 SER N N 113.950 0.1 1 1221 . 126 SER H H 8.179 0.1 1 1222 . 126 SER CA C 59.557 0.1 1 1223 . 126 SER HA H 3.986 0.1 1 1224 . 126 SER CB C 59.557 0.1 1 1225 . 126 SER HB2 H 3.775 0.1 1 1226 . 126 SER C C 173.814 0.1 1 1227 . 127 ASP N N 121.070 0.1 1 1228 . 127 ASP H H 7.487 0.1 1 1229 . 127 ASP CA C 54.859 0.1 1 1230 . 127 ASP HA H 4.219 0.1 1 1231 . 127 ASP CB C 38.262 0.1 1 1232 . 127 ASP HB2 H 2.863 0.1 1 1233 . 127 ASP HB3 H 2.549 0.1 1 1234 . 127 ASP C C 176.388 0.1 1 1235 . 128 LEU N N 118.380 0.1 1 1236 . 128 LEU H H 7.347 0.1 1 1237 . 128 LEU CA C 54.859 0.1 1 1238 . 128 LEU HA H 3.536 0.1 1 1239 . 128 LEU CB C 37.636 0.1 1 1240 . 128 LEU HB2 H 1.759 0.1 1 1241 . 128 LEU HB3 H 0.696 0.1 1 1242 . 128 LEU CG C 22.605 0.1 1 1243 . 128 LEU HG H 0.349 0.1 1 1244 . 128 LEU HD1 H 0.567 0.1 1 1245 . 128 LEU HD2 H 0.388 0.1 1 1246 . 128 LEU CD1 C 21.039 0.1 1 1247 . 128 LEU CD2 C 20.099 0.1 1 1248 . 128 LEU C C 174.879 0.1 1 1249 . 129 LYS N N 115.093 0.1 1 1250 . 129 LYS H H 7.896 0.1 1 1251 . 129 LYS CA C 57.678 0.1 1 1252 . 129 LYS HA H 3.480 0.1 1 1253 . 129 LYS CB C 30.433 0.1 1 1254 . 129 LYS HB2 H 1.875 0.1 1 1255 . 129 LYS HB3 H 1.700 0.1 1 1256 . 129 LYS CG C 22.918 0.1 1 1257 . 129 LYS HG2 H 1.520 0.1 1 1258 . 129 LYS HG3 H 1.240 0.1 1 1259 . 129 LYS CD C 27.615 0.1 1 1260 . 129 LYS HD2 H 1.657 0.1 1 1261 . 129 LYS CE C 38.888 0.1 1 1262 . 129 LYS HE2 H 2.962 0.1 1 1263 . 129 LYS C C 171.218 0.1 1 1264 . 130 GLU N N 119.216 0.1 1 1265 . 130 GLU H H 8.245 0.1 1 1266 . 130 GLU HA H 4.228 0.1 1 1267 . 130 GLU CB C 26.676 0.1 1 1268 . 130 GLU HB2 H 2.038 0.1 1 1269 . 130 GLU HB3 H 1.900 0.1 1 1270 . 130 GLU CG C 33.565 0.1 1 1271 . 130 GLU HG2 H 2.320 0.1 1 1272 . 130 GLU HG3 H 2.171 0.1 1 1273 . 130 GLU C C 175.394 0.1 1 1274 . 131 ALA N N 118.512 0.1 1 1275 . 131 ALA H H 7.391 0.1 1 1276 . 131 ALA CA C 52.041 0.1 1 1277 . 131 ALA HA H 3.925 0.1 1 1278 . 131 ALA HB H 1.269 0.1 1 1279 . 131 ALA CB C 15.402 0.1 1 1280 . 131 ALA C C 177.550 0.1 1 1281 . 132 VAL N N 115.392 0.1 1 1282 . 132 VAL H H 7.165 0.1 1 1283 . 132 VAL CA C 63.628 0.1 1 1284 . 132 VAL HA H 3.521 0.1 1 1285 . 132 VAL CB C 29.181 0.1 1 1286 . 132 VAL HB H 1.788 0.1 1 1287 . 132 VAL HG1 H 0.773 0.1 1 1288 . 132 VAL HG2 H 0.749 0.1 1 1289 . 132 VAL CG1 C 21.978 0.1 1 1290 . 132 VAL CG2 C 20.412 0.1 1 1291 . 132 VAL C C 174.578 0.1 1 1292 . 133 ASP N N 123.608 0.1 1 1293 . 133 ASP H H 8.410 0.1 1 1294 . 133 ASP CA C 54.233 0.1 1 1295 . 133 ASP HA H 4.875 0.1 1 1296 . 133 ASP CB C 38.888 0.1 1 1297 . 133 ASP HB2 H 2.780 0.1 1 1298 . 133 ASP HB3 H 2.655 0.1 1 1299 . 133 ASP C C 178.341 0.1 1 1300 . 134 LYS N N 116.388 0.1 1 1301 . 134 LYS H H 7.574 0.1 1 1302 . 134 LYS HA H 3.953 0.1 1 1303 . 134 LYS CB C 29.494 0.1 1 1304 . 134 LYS HB2 H 1.952 0.1 1 1305 . 134 LYS HB3 H 1.796 0.1 1 1306 . 134 LYS CG C 22.918 0.1 1 1307 . 134 LYS HG2 H 1.478 0.1 1 1308 . 134 LYS HD2 H 1.598 0.1 1 1309 . 134 LYS C C 175.293 0.1 1 1310 . 135 LEU N N 116.936 0.1 1 1311 . 135 LEU H H 7.391 0.1 1 1312 . 135 LEU HA H 4.183 0.1 1 1313 . 135 LEU CB C 41.081 0.1 1 1314 . 135 LEU HB2 H 2.045 0.1 1 1315 . 135 LEU HB3 H 1.769 0.1 1 1316 . 135 LEU CG C 23.231 0.1 1 1317 . 135 LEU HG H 0.853 0.1 1 1318 . 135 LEU HD1 H 0.795 0.1 1 1319 . 135 LEU HD2 H 0.771 0.1 1 1320 . 135 LEU CD1 C 20.726 0.1 1 1321 . 135 LEU C C 173.744 0.1 1 1322 . 136 GLY N N 103.044 0.1 1 1323 . 136 GLY H H 7.623 0.1 1 1324 . 136 GLY CA C 41.707 0.1 1 1325 . 136 GLY HA2 H 3.898 0.1 1 1326 . 136 GLY HA3 H 3.503 0.1 1 1327 . 136 GLY C C 170.640 0.1 1 1328 . 137 TYR N N 118.513 0.1 1 1329 . 137 TYR H H 6.996 0.1 1 1330 . 137 TYR CA C 52.667 0.1 1 1331 . 137 TYR HA H 4.899 0.1 1 1332 . 137 TYR CB C 37.323 0.1 1 1333 . 137 TYR HB2 H 3.092 0.1 1 1334 . 137 TYR HB3 H 2.128 0.1 1 1335 . 137 TYR HD2 H 6.591 0.1 1 1336 . 137 TYR HE2 H 6.839 0.1 1 1337 . 137 TYR C C 170.611 0.1 1 1338 . 138 LYS N N 116.531 0.1 1 1339 . 138 LYS H H 8.035 0.1 1 1340 . 138 LYS HA H 4.728 0.1 1 1341 . 138 LYS CB C 33.565 0.1 1 1342 . 138 LYS HB2 H 1.600 0.1 1 1343 . 138 LYS HB3 H 1.542 0.1 1 1344 . 138 LYS CG C 21.978 0.1 1 1345 . 138 LYS HG2 H 1.280 0.1 1 1346 . 138 LYS HG3 H 1.160 0.1 1 1347 . 138 LYS CD C 26.676 0.1 1 1348 . 138 LYS HD2 H 1.566 0.1 1 1349 . 138 LYS HD3 H 1.484 0.1 1 1350 . 138 LYS CE C 39.515 0.1 1 1351 . 138 LYS HE2 H 2.822 0.1 1 1352 . 138 LYS C C 172.464 0.1 1 1353 . 139 LEU N N 123.472 0.1 1 1354 . 139 LEU H H 8.810 0.1 1 1355 . 139 LEU CA C 50.475 0.1 1 1356 . 139 LEU HA H 4.912 0.1 1 1357 . 139 LEU CB C 40.767 0.1 1 1358 . 139 LEU HB2 H 1.163 0.1 1 1359 . 139 LEU HB3 H 1.057 0.1 1 1360 . 139 LEU CG C 22.918 0.1 1 1361 . 139 LEU HG H 1.099 0.1 1 1362 . 139 LEU HD1 H 0.124 0.1 1 1363 . 139 LEU HD2 H -0.222 0.1 1 1364 . 139 LEU CD1 C 21.039 0.1 1 1365 . 139 LEU CD2 C 21.039 0.1 1 1366 . 139 LEU C C 173.508 0.1 1 1367 . 140 LYS N N 122.204 0.1 1 1368 . 140 LYS H H 8.938 0.1 1 1369 . 140 LYS HA H 4.618 0.1 1 1370 . 140 LYS CB C 31.999 0.1 1 1371 . 140 LYS HB2 H 1.742 0.1 1 1372 . 140 LYS HB3 H 1.603 0.1 1 1373 . 140 LYS CG C 21.352 0.1 1 1374 . 140 LYS HG2 H 1.279 0.1 1 1375 . 140 LYS HG3 H 1.233 0.1 1 1376 . 140 LYS CD C 26.362 0.1 1 1377 . 140 LYS HD2 H 1.543 0.1 1 1378 . 140 LYS HE2 H 2.775 0.1 1 1379 . 140 LYS C C 173.137 0.1 1 1380 . 141 LEU N N 128.026 0.1 1 1381 . 141 LEU H H 9.000 0.1 1 1382 . 141 LEU CA C 52.980 0.1 1 1383 . 141 LEU HA H 4.025 0.1 1 1384 . 141 LEU CB C 39.828 0.1 1 1385 . 141 LEU HB2 H 1.584 0.1 1 1386 . 141 LEU HB3 H 1.296 0.1 1 1387 . 141 LEU CG C 24.483 0.1 1 1388 . 141 LEU HG H 1.469 0.1 1 1389 . 141 LEU HD1 H 0.612 0.1 1 1390 . 141 LEU HD2 H 0.552 0.1 1 1391 . 141 LEU CD1 C 22.918 0.1 1 1392 . 141 LEU CD2 C 21.665 0.1 1 1393 . 141 LEU C C 174.851 0.1 1 1394 . 142 LYS N N 126.455 0.1 1 1395 . 142 LYS H H 8.460 0.1 1 1396 . 142 LYS CA C 54.859 0.1 1 1397 . 142 LYS HA H 4.067 0.1 1 1398 . 142 LYS CB C 29.494 0.1 1 1399 . 142 LYS HB2 H 1.584 0.1 1 1400 . 142 LYS HB3 H 1.467 0.1 1 1401 . 142 LYS HG2 H 1.252 0.1 1 1402 . 142 LYS CD C 26.362 0.1 1 1403 . 142 LYS HD2 H 1.469 0.1 1 1404 . 142 LYS CE C 38.888 0.1 1 1405 . 142 LYS HE2 H 2.783 0.1 1 1406 . 142 LYS C C 174.947 0.1 1 1407 . 143 GLY N N 111.119 0.1 1 1408 . 143 GLY H H 8.593 0.1 1 1409 . 143 GLY CA C 42.959 0.1 1 1410 . 143 GLY HA2 H 3.963 0.1 1 1411 . 143 GLY HA3 H 3.725 0.1 1 1412 . 143 GLY C C 171.771 0.1 1 1413 . 144 GLU N N 120.206 0.1 1 1414 . 144 GLU H H 7.905 0.1 1 1415 . 144 GLU CA C 54.233 0.1 1 1416 . 144 GLU HA H 4.153 0.1 1 1417 . 144 GLU CB C 27.615 0.1 1 1418 . 144 GLU HB2 H 1.948 0.1 1 1419 . 144 GLU CG C 33.878 0.1 1 1420 . 144 GLU HG2 H 2.181 0.1 1 1421 . 144 GLU C C 173.918 0.1 1 1422 . 145 GLN N N 120.965 0.1 1 1423 . 145 GLN H H 8.477 0.1 1 1424 . 145 GLN CA C 52.980 0.1 1 1425 . 145 GLN HA H 4.261 0.1 1 1426 . 145 GLN CB C 26.676 0.1 1 1427 . 145 GLN HB2 H 2.022 0.1 1 1428 . 145 GLN HB3 H 1.880 0.1 1 1429 . 145 GLN CG C 30.747 0.1 1 1430 . 145 GLN HG2 H 2.272 0.1 1 1431 . 145 GLN NE2 N 112.261 0.1 1 1432 . 145 GLN HE21 H 7.477 0.1 1 1433 . 145 GLN HE22 H 6.791 0.1 1 1434 . 145 GLN C C 172.992 0.1 1 1435 . 146 ASP N N 121.220 0.1 1 1436 . 146 ASP H H 8.301 0.1 1 1437 . 146 ASP CA C 52.041 0.1 1 1438 . 146 ASP HA H 4.481 0.1 1 1439 . 146 ASP CB C 38.262 0.1 1 1440 . 146 ASP HB2 H 2.580 0.1 1 1441 . 146 ASP HB3 H 2.498 0.1 1 1442 . 146 ASP C C 173.512 0.1 1 1443 . 147 SER N N 115.408 0.1 1 1444 . 147 SER H H 8.155 0.1 1 1445 . 147 SER HA H 4.359 0.1 1 1446 . 147 SER CB C 61.122 0.1 1 1447 . 147 SER HB2 H 3.757 0.1 1 1448 . 147 SER C C 171.925 0.1 1 1449 . 148 ILE N N 122.077 0.1 1 1450 . 148 ILE H H 8.118 0.1 1 1451 . 148 ILE HA H 4.081 0.1 1 1452 . 148 ILE HB H 1.779 0.1 1 1453 . 148 ILE HG2 H 0.791 0.1 1 1454 . 148 ILE HG12 H 1.328 0.1 1 1455 . 148 ILE HG13 H 1.079 0.1 1 1456 . 148 ILE HD1 H 0.760 0.1 1 1457 . 148 ILE C C 173.676 0.1 1 1458 . 149 GLU N N 123.642 0.1 1 1459 . 149 GLU H H 8.344 0.1 1 1460 . 149 GLU HA H 4.140 0.1 1 1461 . 149 GLU HB2 H 1.926 0.1 1 1462 . 149 GLU HB3 H 1.819 0.1 1 1463 . 149 GLU HG2 H 2.153 0.1 1 1464 . 149 GLU C C 174.519 0.1 1 1465 . 150 GLY N N 109.969 0.1 1 1466 . 150 GLY H H 8.329 0.1 1 1467 . 150 GLY HA2 H 3.821 0.1 1 1468 . 150 GLY C C 170.645 0.1 1 1469 . 151 ARG N N 125.173 0.1 1 1470 . 151 ARG H H 7.640 0.1 1 1471 . 151 ARG HA H 4.100 0.1 1 1472 . 151 ARG HB2 H 1.755 0.1 1 1473 . 151 ARG HB3 H 1.598 0.1 1 1474 . 151 ARG HG2 H 1.64 0.1 1 1475 . 151 ARG HG3 H 1.75 0.1 1 1476 . 151 ARG HD2 H 3.06 0.1 1 1477 . 151 ARG HD3 H 1.635 0.1 1 1478 . 151 ARG CG C 24.52 0.1 1 1479 . 151 ARG CD C 40.69 0.1 1 stop_ save_