data_7428 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR ; _BMRB_accession_number 7428 _BMRB_flat_file_name bmr7428.str _Entry_type original _Submission_date 2008-07-02 _Accession_date 2008-07-02 _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 Chill Jordan H. . 2 Louis John M. . 3 Delaglio Frank . . 4 Bax Ad . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 139 "13C chemical shifts" 284 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-07 original author . stop_ _Original_release_date 2008-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17945182 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chill Jordan H. . 2 Louis John M. . 3 Delaglio Frank . . 4 Bax Ad . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta.' _Journal_volume 1768 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3260 _Page_last 3270 _Year 2007 _Details . loop_ _Keyword KcsA NMR 'potassium channel' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title 'NMR study of the tetrameric KcsA potassium channel in detergent micelles.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16522799 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chill Jordan H. . 2 Louis John M. . 3 Miller C. . . 4 Bax Ad . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full . _Journal_volume 15 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 684 _Page_last 698 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name KcsA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KcsA, 1' $KcsA 'KcsA, 2' $KcsA 'KcsA, 3' $KcsA 'KcsA, 4' $KcsA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_KcsA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common KcsA _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'selective conduction of K+ ions across the cell membrane' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 145 _Mol_residue_sequence ; LLGRHGSALHWRAAGAATVL LVIVLLAGSYLAVLAERGAP GAQLITYPRALWWSVETATT VGYGDLYPVTLWGRLVAVVV MVAGITSFGLVTAALATWFV GREQERRGHFVRHSEKAAEE AYTRTTRALHERFDRLERML DDNRR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 16 LEU 2 17 LEU 3 18 GLY 4 19 ARG 5 20 HIS 6 21 GLY 7 22 SER 8 23 ALA 9 24 LEU 10 25 HIS 11 26 TRP 12 27 ARG 13 28 ALA 14 29 ALA 15 30 GLY 16 31 ALA 17 32 ALA 18 33 THR 19 34 VAL 20 35 LEU 21 36 LEU 22 37 VAL 23 38 ILE 24 39 VAL 25 40 LEU 26 41 LEU 27 42 ALA 28 43 GLY 29 44 SER 30 45 TYR 31 46 LEU 32 47 ALA 33 48 VAL 34 49 LEU 35 50 ALA 36 51 GLU 37 52 ARG 38 53 GLY 39 54 ALA 40 55 PRO 41 56 GLY 42 57 ALA 43 58 GLN 44 59 LEU 45 60 ILE 46 61 THR 47 62 TYR 48 63 PRO 49 64 ARG 50 65 ALA 51 66 LEU 52 67 TRP 53 68 TRP 54 69 SER 55 70 VAL 56 71 GLU 57 72 THR 58 73 ALA 59 74 THR 60 75 THR 61 76 VAL 62 77 GLY 63 78 TYR 64 79 GLY 65 80 ASP 66 81 LEU 67 82 TYR 68 83 PRO 69 84 VAL 70 85 THR 71 86 LEU 72 87 TRP 73 88 GLY 74 89 ARG 75 90 LEU 76 91 VAL 77 92 ALA 78 93 VAL 79 94 VAL 80 95 VAL 81 96 MET 82 97 VAL 83 98 ALA 84 99 GLY 85 100 ILE 86 101 THR 87 102 SER 88 103 PHE 89 104 GLY 90 105 LEU 91 106 VAL 92 107 THR 93 108 ALA 94 109 ALA 95 110 LEU 96 111 ALA 97 112 THR 98 113 TRP 99 114 PHE 100 115 VAL 101 116 GLY 102 117 ARG 103 118 GLU 104 119 GLN 105 120 GLU 106 121 ARG 107 122 ARG 108 123 GLY 109 124 HIS 110 125 PHE 111 126 VAL 112 127 ARG 113 128 HIS 114 129 SER 115 130 GLU 116 131 LYS 117 132 ALA 118 133 ALA 119 134 GLU 120 135 GLU 121 136 ALA 122 137 TYR 123 138 THR 124 139 ARG 125 140 THR 126 141 THR 127 142 ARG 128 143 ALA 129 144 LEU 130 145 HIS 131 146 GLU 132 147 ARG 133 148 PHE 134 149 ASP 135 150 ARG 136 151 LEU 137 152 GLU 138 153 ARG 139 154 MET 140 155 LEU 141 156 ASP 142 157 ASP 143 158 ASN 144 159 ARG 145 160 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15853 KcsA 100.00 145 100.00 100.00 1.85e-95 PDB 1BL8 "Potassium Channel (Kcsa) From Streptomyces Lividans" 66.90 97 98.97 98.97 9.21e-57 PDB 1F6G "Potassium Channel (Kcsa) Full-Length Fold" 100.00 160 97.93 97.93 2.83e-93 PDB 1J95 "Kcsa Potassium Channel With Tba (Tetrabutylammonium) And Potassium" 75.86 125 99.09 99.09 2.63e-67 PDB 1JVM "Kcsa Potassium Channel With Tba (Tetrabutylammonium) And Rubidium" 75.86 125 99.09 99.09 2.02e-67 PDB 1K4C "Potassium Channel Kcsa-Fab Complex In High Concentration Of K+" 75.17 124 99.08 99.08 2.37e-66 PDB 1K4D "Potassium Channel Kcsa-Fab Complex In Low Concentration Of K+" 75.17 124 99.08 99.08 2.37e-66 PDB 1R3I "Potassium Channel Kcsa-Fab Complex In Rb+" 75.17 124 99.08 99.08 2.37e-66 PDB 1R3J "Potassium Channel Kcsa-Fab Complex In High Concentration Of Tl+" 75.17 124 99.08 99.08 2.37e-66 PDB 1R3K "Potassium Channel Kcsa-Fab Complex In Low Concentration Of Tl+" 75.17 124 99.08 99.08 2.37e-66 PDB 1R3L "Potassium Channel Kcsa-Fab Complex In Cs+" 75.17 124 99.08 99.08 2.37e-66 PDB 1S5H "Potassium Channel Kcsa-Fab Complex T75c Mutant In K+" 75.17 124 99.08 99.08 2.27e-66 PDB 1ZWI "Structure Of Mutant Kcsa Potassium Channel" 70.34 103 98.04 98.04 7.95e-60 PDB 2ATK "Structure Of A Mutant Kcsa K+ Channel" 75.17 124 98.17 98.17 1.41e-65 PDB 2BOB "Potassium Channel Kcsa-Fab Complex In Thallium With Tetrabutylammonium (Tba)" 75.17 124 99.08 99.08 2.37e-66 PDB 2BOC "Potassium Channel Kcsa-Fab Complex In Thallium With Tetraethylarsonium (Teas)" 75.17 124 99.08 99.08 2.37e-66 PDB 2DWD "Crystal Structure Of Kcsa-Fab-Tba Complex In Tl+" 71.03 103 99.03 99.03 8.97e-62 PDB 2DWE "Crystal Structure Of Kcsa-Fab-Tba Complex In Rb+" 71.03 103 99.03 99.03 8.97e-62 PDB 2HJF "Potassium Channel Kcsa-Fab Complex With Tetrabutylammonium (Tba)" 71.03 103 99.03 99.03 8.97e-62 PDB 2HVJ "Crystal Structure Of Kcsa-fab-tba Complex In Low K+" 75.17 124 99.08 99.08 2.37e-66 PDB 2HVK "Crystal Structure Of The Kcsa-Fab-Tba Complex In High K+" 75.17 124 99.08 99.08 2.37e-66 PDB 2IH1 "Ion Selectivity In A Semi-Synthetic K+ Channel Locked In The Conductive Conformation" 73.79 122 97.20 98.13 4.70e-63 PDB 2IH3 "Ion Selectivity In A Semi-Synthetic K+ Channel Locked In The Conductive Conformation" 73.79 122 97.20 98.13 4.70e-63 PDB 2ITC "Potassium Channel Kcsa-Fab Complex In Sodium Chloride" 75.17 124 99.08 99.08 2.37e-66 PDB 2ITD "Potassium Channel Kcsa-Fab Complex In Barium Chloride" 75.17 124 99.08 99.08 2.37e-66 PDB 2JK5 "Potassium Channel Kcsa In Complex With Tetrabutylammonium In High K" 75.17 124 99.08 99.08 2.62e-66 PDB 2NLJ "Potassium Channel Kcsa(M96v)-Fab Complex In Kcl" 75.17 124 98.17 99.08 1.34e-65 PDB 2P7T "Crystal Structure Of Kcsa Mutant" 71.03 103 98.06 98.06 3.86e-61 PDB 2QTO "An Anisotropic Model For Potassium Channel Kcsa" 66.90 97 98.97 98.97 9.21e-57 PDB 2W0F "Potassium Channel Kcsa-fab Complex With Tetraoctylammonium" 75.17 124 99.08 99.08 2.62e-66 PDB 3EFF "The Crystal Structure Of Full-Length Kcsa In Its Closed Conformation" 95.86 139 100.00 100.00 3.61e-91 PDB 3F5W "Kcsa Potassium Channel In The Open-Inactivated State With 32 A Opening At T112" 65.52 104 97.89 97.89 4.80e-54 PDB 3F7V "Kcsa Potassium Channel In The Open-Inactivated State With 23 A Opening At T112" 65.52 104 97.89 97.89 4.80e-54 PDB 3F7Y "Kcsa Potassium Channel In The Partially Open State With 17 A Opening At T112" 65.52 104 97.89 97.89 4.80e-54 PDB 3FB5 "Kcsa Potassium Channel In The Partially Open State With 14.5 A Opening At T112" 65.52 104 97.89 97.89 4.80e-54 PDB 3FB6 "Kcsa Potassium Channel In The Partially Open State With 16 A Opening At T112" 65.52 104 97.89 97.89 4.80e-54 PDB 3FB7 "Open Kcsa Potassium Channel In The Presence Of Rb+ Ion" 65.52 104 97.89 97.89 4.80e-54 PDB 3FB8 "Kcsa Potassium Channel In The Open-Conductive State With 20 At T112 In The Presence Of Rb+ Ion" 65.52 104 97.89 97.89 4.80e-54 PDB 3GB7 "Potassium Channel Kcsa-Fab Complex In Li+" 75.17 124 99.08 99.08 2.37e-66 PDB 3HPL "Kcsa E71h-F103a Mutant In The Closed State" 75.17 124 97.25 97.25 3.40e-64 PDB 3IGA "Potassium Channel Kcsa-fab Complex In Li+ And K+" 75.17 124 99.08 99.08 2.37e-66 PDB 3OGC "Kcsa E71a Variant In Presence Of Na+" 75.17 131 99.08 99.08 9.90e-66 PDB 3OR6 "On The Structural Basis Of Modal Gating Behavior In K+channels - E71q" 71.03 103 98.06 99.03 2.03e-61 PDB 3OR7 "On The Structural Basis Of Modal Gating Behavior In K+channels - E71i" 71.03 103 98.06 98.06 1.47e-60 PDB 3STL "Kcsa Potassium Channel Mutant Y82c With Cadmium Bound" 71.03 103 99.03 99.03 3.66e-61 PDB 3STZ "Kcsa Potassium Channel Mutant Y82c With Nitroxide Spin Label" 70.34 102 99.02 99.02 1.68e-60 PDB 4LBE "Structure Of Kcsa With R122a Mutation" 75.17 130 99.08 99.08 1.07e-65 PDB 4LCU "Structure Of Kcsa With E118a Mutation" 75.17 131 99.08 99.08 9.90e-66 PDB 4MSW "Y78 Ester Mutant Of Kcsa In High K+" 71.03 103 99.03 99.03 4.54e-61 PDB 4UUJ "Potassium Channel Kcsa-fab With Tetrahexylammonium" 71.72 111 99.04 99.04 1.15e-62 EMBL CAA86025 "potassium channel protein [Streptomyces lividans 1326]" 100.00 160 100.00 100.00 1.39e-95 EMBL CAC16993 "voltage-gated potassium channel [Streptomyces coelicolor A3(2)]" 100.00 160 100.00 100.00 1.39e-95 GB AIJ11233 "Voltage-gated potassium channel [Streptomyces lividans TK24]" 100.00 157 100.00 100.00 1.00e-95 GB EFD64549 "voltage-gated potassium channel [Streptomyces lividans TK24]" 100.00 160 100.00 100.00 1.39e-95 GB EOY52587 "Voltage-gated potassium channel [Streptomyces lividans 1326]" 100.00 157 100.00 100.00 1.00e-95 REF NP_631700 "voltage-gated potassium channel [Streptomyces coelicolor A3(2)]" 100.00 160 100.00 100.00 1.39e-95 REF WP_003971485 "voltage-gated potassium channel [Streptomyces coelicolor]" 100.00 160 100.00 100.00 1.39e-95 REF WP_016328171 "Voltage-gated potassium channel [Streptomyces lividans]" 100.00 157 100.00 100.00 1.00e-95 REF WP_030864493 "voltage-gated potassium channel [Streptomyces violaceoruber]" 100.00 157 97.93 99.31 4.82e-94 SP P0A333 "RecName: Full=pH-gated potassium channel KcsA [Streptomyces coelicolor A3(2)]" 100.00 160 100.00 100.00 1.39e-95 SP P0A334 "RecName: Full=pH-gated potassium channel KcsA; AltName: Full=Streptomyces lividans K+ channel; Short=SKC1 [Streptomyces lividan" 100.00 160 100.00 100.00 1.39e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $KcsA . 1902 bacteria . Streptomyces coelicolor 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 $KcsA 'recombinant technology' . Escherichia coli . pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_4_for_TableS5 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $KcsA 0.5-0.6 mM 'natural abundance' MES 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe_NMRDraw _Saveframe_category software _Name NMRPipe/NMRDraw _Version . loop_ _Vendor _Address _Electronic_address NIH . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_4_for_TableS5 save_ save_3D_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_4_for_TableS5 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_4_for_TableS5 save_ ####################### # Sample conditions # ####################### save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6 . pH pressure 14.1 . Torr temperature 323 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HN(CA)CO' '3D HNCA' stop_ loop_ _Sample_label $sample_4_for_TableS5 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'KcsA, 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 16 1 LEU H H 8.22 0.02 1 2 16 1 LEU C C 177.4 0.1 1 3 16 1 LEU CA C 56.5 0.1 1 4 16 1 LEU N N 122.6 0.02 1 5 17 2 LEU H H 7.68 0.02 1 6 17 2 LEU C C 177.8 0.1 1 7 17 2 LEU CA C 54.9 0.1 1 8 17 2 LEU N N 117.6 0.02 1 9 18 3 GLY H H 7.95 0.02 1 10 18 3 GLY C C 175.2 0.1 1 11 18 3 GLY CA C 45.5 0.1 1 12 18 3 GLY N N 107.9 0.02 1 13 19 4 ARG H H 7.78 0.02 1 14 19 4 ARG C C 177 0.1 1 15 19 4 ARG CA C 56.4 0.1 1 16 19 4 ARG N N 119.5 0.02 1 17 20 5 HIS H H 8.2 0.02 1 18 20 5 HIS C C 175.2 0.1 1 19 20 5 HIS CA C 55.4 0.1 1 20 20 5 HIS N N 117.4 0.02 1 21 21 6 GLY H H 8.05 0.02 1 22 21 6 GLY C C 174.6 0.1 1 23 21 6 GLY CA C 45.6 0.1 1 24 21 6 GLY N N 109.1 0.02 1 25 22 7 SER H H 7.83 0.02 1 26 22 7 SER C C 174.6 0.1 1 27 22 7 SER CA C 58.4 0.1 1 28 22 7 SER N N 115.6 0.02 1 29 23 8 ALA H H 7.94 0.02 1 30 23 8 ALA C C 177.4 0.1 1 31 23 8 ALA CA C 52.5 0.1 1 32 23 8 ALA N N 124.9 0.02 1 33 24 9 LEU H H 7.54 0.02 1 34 24 9 LEU C C 176.8 0.1 1 35 24 9 LEU CA C 54.9 0.1 1 36 24 9 LEU N N 118.7 0.02 1 37 25 10 HIS H H 7.77 0.02 1 38 25 10 HIS C C 174.4 0.1 1 39 25 10 HIS CA C 54.6 0.1 1 40 25 10 HIS N N 117.9 0.02 1 41 26 11 TRP H H 7.68 0.02 1 42 26 11 TRP C C 176.8 0.1 1 43 26 11 TRP CA C 57.9 0.1 1 44 26 11 TRP N N 121.6 0.02 1 45 27 12 ARG H H 7.73 0.02 1 46 27 12 ARG C C 176.5 0.1 1 47 27 12 ARG CA C 56.2 0.1 1 48 27 12 ARG N N 120.1 0.02 1 49 28 13 ALA H H 7.81 0.02 1 50 28 13 ALA C C 178.5 0.1 1 51 28 13 ALA CA C 53.6 0.1 1 52 28 13 ALA N N 123.4 0.02 1 53 29 14 ALA H H 7.83 0.02 1 54 29 14 ALA C C 179 0.1 1 55 29 14 ALA CA C 53.3 0.1 1 56 29 14 ALA N N 119.2 0.02 1 57 30 15 GLY H H 7.76 0.02 1 58 30 15 GLY C C 174.7 0.1 1 59 30 15 GLY CA C 46.2 0.1 1 60 30 15 GLY N N 107.8 0.02 1 61 31 16 ALA H H 8.08 0.02 1 62 31 16 ALA C C 179.2 0.1 1 63 31 16 ALA CA C 55 0.1 1 64 31 16 ALA N N 123.6 0.02 1 65 32 17 ALA H H 8.07 0.02 1 66 32 17 ALA C C 178.6 0.1 1 67 32 17 ALA CA C 54.8 0.1 1 68 32 17 ALA N N 118.1 0.02 1 69 33 18 THR H H 7.48 0.02 1 70 33 18 THR C C 176.2 0.1 1 71 33 18 THR CA C 67.1 0.1 1 72 33 18 THR N N 114.6 0.02 1 73 34 19 VAL H H 7.73 0.02 1 74 34 19 VAL C C 177.1 0.1 1 75 34 19 VAL CA C 67 0.1 1 76 34 19 VAL N N 121.1 0.02 1 77 35 20 LEU H H 7.75 0.02 1 78 35 20 LEU C C 176.9 0.1 1 79 35 20 LEU CA C 58 0.1 1 80 35 20 LEU N N 119.3 0.02 1 81 36 21 LEU H H 7.85 0.02 1 82 36 21 LEU C C 178.2 0.1 1 83 36 21 LEU CA C 57.9 0.1 1 84 36 21 LEU N N 117.6 0.02 1 85 37 22 VAL H H 8.26 0.02 1 86 37 22 VAL C C 177.9 0.1 1 87 37 22 VAL CA C 67.4 0.1 1 88 37 22 VAL N N 117.5 0.02 1 89 38 23 ILE H H 8.26 0.02 1 90 38 23 ILE C C 177.8 0.1 1 91 38 23 ILE CA C 66 0.1 1 92 38 23 ILE N N 120 0.02 1 93 39 24 VAL H H 8.21 0.02 1 94 39 24 VAL C C 178.7 0.1 1 95 39 24 VAL CA C 67 0.1 1 96 39 24 VAL N N 119.8 0.02 1 97 40 25 LEU H H 8.46 0.02 1 98 40 25 LEU C C 180.8 0.1 1 99 40 25 LEU CA C 57.8 0.1 1 100 40 25 LEU N N 118.3 0.02 1 101 41 26 LEU H H 8.77 0.02 1 102 41 26 LEU C C 180.5 0.1 1 103 41 26 LEU CA C 57.8 0.1 1 104 41 26 LEU N N 120.8 0.02 1 105 42 27 ALA H H 8.82 0.02 1 106 42 27 ALA C C 180 0.1 1 107 42 27 ALA CA C 54.7 0.1 1 108 42 27 ALA N N 121.5 0.02 1 109 43 28 GLY H H 8.9 0.02 1 110 43 28 GLY C C 175.4 0.1 1 111 43 28 GLY CA C 47 0.1 1 112 43 28 GLY N N 106.6 0.02 1 113 44 29 SER H H 7.7 0.02 1 114 44 29 SER C C 175.2 0.1 1 115 44 29 SER CA C 62.8 0.1 1 116 44 29 SER N N 115.6 0.02 1 117 45 30 TYR H H 7.47 0.02 1 118 45 30 TYR C C 177.1 0.1 1 119 45 30 TYR CA C 61.2 0.1 1 120 45 30 TYR N N 121.4 0.02 1 121 46 31 LEU H H 7.95 0.02 1 122 46 31 LEU C C 178.2 0.1 1 123 46 31 LEU CA C 57.1 0.1 1 124 46 31 LEU N N 116.4 0.02 1 125 47 32 ALA H H 8.09 0.02 1 126 47 32 ALA C C 178.8 0.1 1 127 47 32 ALA CA C 55.4 0.1 1 128 47 32 ALA N N 120 0.02 1 129 48 33 VAL H H 7.22 0.02 1 130 48 33 VAL C C 178.6 0.1 1 131 48 33 VAL CA C 65 0.1 1 132 48 33 VAL N N 116.3 0.02 1 133 49 34 LEU H H 7.41 0.02 1 134 49 34 LEU C C 179.4 0.1 1 135 49 34 LEU CA C 57.4 0.1 1 136 49 34 LEU N N 119.5 0.02 1 137 50 35 ALA H H 7.76 0.02 1 138 50 35 ALA C C 179.3 0.1 1 139 50 35 ALA CA C 54.1 0.1 1 140 50 35 ALA N N 118.1 0.02 1 141 51 36 GLU H H 7.82 0.02 1 142 51 36 GLU C C 177.9 0.1 1 143 51 36 GLU CA C 57.4 0.1 1 144 51 36 GLU N N 114.9 0.02 1 145 52 37 ARG H H 7.93 0.02 1 146 52 37 ARG C C 177.9 0.1 1 147 52 37 ARG CA C 59.3 0.1 1 148 52 37 ARG N N 116.9 0.02 1 149 53 38 GLY H H 8.3 0.02 1 150 53 38 GLY C C 174.6 0.1 1 151 53 38 GLY CA C 44.5 0.1 1 152 53 38 GLY N N 110.6 0.02 1 153 54 39 ALA H H 7.67 0.02 1 154 54 39 ALA C C 176.4 0.1 1 155 54 39 ALA CA C 49.7 0.1 1 156 54 39 ALA N N 126.4 0.02 1 157 55 40 PRO C C 178.3 0.1 1 158 55 40 PRO CA C 63.2 0.1 1 159 56 41 GLY H H 8.5 0.02 1 160 56 41 GLY C C 174.4 0.1 1 161 56 41 GLY CA C 44.9 0.1 1 162 56 41 GLY N N 111.7 0.02 1 163 57 42 ALA H H 7.29 0.02 1 164 57 42 ALA C C 177.5 0.1 1 165 57 42 ALA CA C 52.9 0.1 1 166 57 42 ALA N N 121.9 0.02 1 167 58 43 GLN H H 8.63 0.02 1 168 58 43 GLN C C 176.9 0.1 1 169 58 43 GLN CA C 54.7 0.1 1 170 58 43 GLN N N 116.4 0.02 1 171 59 44 LEU H H 7.85 0.02 1 172 59 44 LEU C C 174.6 0.1 1 173 59 44 LEU CA C 53 0.1 1 174 59 44 LEU N N 125.1 0.02 1 175 60 45 ILE H H 6.88 0.02 1 176 60 45 ILE C C 175.9 0.1 1 177 60 45 ILE CA C 61.3 0.1 1 178 60 45 ILE N N 107.1 0.02 1 179 61 46 THR H H 7.15 0.02 1 180 61 46 THR C C 173.9 0.1 1 181 61 46 THR CA C 58.2 0.1 1 182 61 46 THR N N 109.9 0.02 1 183 62 47 TYR H H 8.98 0.02 1 184 62 47 TYR CA C 63.3 0.1 1 185 62 47 TYR N N 122.4 0.02 1 186 63 48 PRO C C 177.9 0.1 1 187 63 48 PRO CA C 66.4 0.1 1 188 64 49 ARG H H 6.74 0.02 1 189 64 49 ARG C C 178.5 0.1 1 190 64 49 ARG CA C 58.9 0.1 1 191 64 49 ARG N N 113.8 0.02 1 192 65 50 ALA H H 7.79 0.02 1 193 65 50 ALA C C 178.9 0.1 1 194 65 50 ALA CA C 54.8 0.1 1 195 65 50 ALA N N 120.6 0.02 1 196 66 51 LEU H H 8.58 0.02 1 197 66 51 LEU C C 180 0.1 1 198 66 51 LEU CA C 57.2 0.1 1 199 66 51 LEU N N 122.8 0.02 1 200 67 52 TRP H H 7.86 0.02 1 201 67 52 TRP C C 176.8 0.1 1 202 67 52 TRP CA C 59.5 0.1 1 203 67 52 TRP N N 121.4 0.02 1 204 68 53 TRP H H 8.33 0.02 1 205 68 53 TRP C C 180.2 0.1 1 206 68 53 TRP CA C 59.8 0.1 1 207 68 53 TRP N N 120.3 0.02 1 208 69 54 SER H H 9.41 0.02 1 209 69 54 SER C C 176.2 0.1 1 210 69 54 SER CA C 63.2 0.1 1 211 69 54 SER N N 124.5 0.02 1 212 70 55 VAL H H 7.66 0.02 1 213 70 55 VAL C C 178.1 0.1 1 214 70 55 VAL CA C 66 0.1 1 215 70 55 VAL N N 124.8 0.02 1 216 71 56 GLU H H 7.98 0.02 1 217 71 56 GLU C C 180.2 0.1 1 218 71 56 GLU CA C 58.5 0.1 1 219 71 56 GLU N N 120.1 0.02 1 220 72 57 THR H H 7.89 0.02 1 221 72 57 THR C C 173.6 0.1 1 222 72 57 THR CA C 67.2 0.1 1 223 72 57 THR N N 119.6 0.02 1 224 73 58 ALA H H 7.57 0.02 1 225 73 58 ALA C C 177.1 0.1 1 226 73 58 ALA CA C 54.8 0.1 1 227 73 58 ALA N N 120.8 0.02 1 228 74 59 THR H H 6.98 0.02 1 229 74 59 THR C C 178 0.1 1 230 74 59 THR CA C 61.5 0.1 1 231 74 59 THR N N 100.1 0.02 1 232 75 60 THR H H 7.3 0.02 1 233 75 60 THR C C 173.6 0.1 1 234 75 60 THR CA C 62.2 0.1 1 235 75 60 THR N N 116 0.02 1 236 76 61 VAL H H 7.09 0.02 1 237 76 61 VAL C C 176.4 0.1 1 238 76 61 VAL CA C 65.2 0.1 1 239 76 61 VAL N N 119.7 0.02 1 240 77 62 GLY H H 8.16 0.02 1 241 77 62 GLY C C 175.7 0.1 1 242 77 62 GLY CA C 47.8 0.1 1 243 77 62 GLY N N 107.1 0.02 1 244 78 63 TYR H H 6.09 0.02 1 245 78 63 TYR C C 178 0.1 1 246 78 63 TYR CA C 56.9 0.1 1 247 78 63 TYR N N 117.4 0.02 1 248 79 64 GLY H H 8.96 0.02 1 249 79 64 GLY C C 174.4 0.1 1 250 79 64 GLY CA C 47.1 0.1 1 251 79 64 GLY N N 102.2 0.02 1 252 80 65 ASP H H 9.61 0.02 1 253 80 65 ASP CA C 54.4 0.1 1 254 80 65 ASP N N 115.6 0.02 1 255 83 68 PRO C C 176.1 0.1 1 256 83 68 PRO CA C 61.1 0.1 1 257 84 69 VAL H H 10.75 0.02 1 258 84 69 VAL C C 176.7 0.1 1 259 84 69 VAL CA C 61 0.1 1 260 84 69 VAL N N 116.4 0.02 1 261 85 70 THR H H 8.7 0.02 1 262 85 70 THR C C 174.7 0.1 1 263 85 70 THR CA C 60 0.1 1 264 85 70 THR N N 116.8 0.02 1 265 86 71 LEU H H 8.05 0.02 1 266 86 71 LEU C C 178.7 0.1 1 267 86 71 LEU CA C 58.4 0.1 1 268 86 71 LEU N N 123.6 0.02 1 269 87 72 TRP H H 7.17 0.02 1 270 87 72 TRP C C 178.7 0.1 1 271 87 72 TRP CA C 59 0.1 1 272 87 72 TRP N N 116 0.02 1 273 88 73 GLY H H 8.42 0.02 1 274 88 73 GLY C C 176.6 0.1 1 275 88 73 GLY CA C 46 0.1 1 276 88 73 GLY N N 107.6 0.02 1 277 89 74 ARG H H 7.77 0.02 1 278 89 74 ARG C C 178 0.1 1 279 89 74 ARG CA C 59.6 0.1 1 280 89 74 ARG N N 123.3 0.02 1 281 90 75 LEU H H 7.87 0.02 1 282 90 75 LEU C C 179.8 0.1 1 283 90 75 LEU CA C 58.2 0.1 1 284 90 75 LEU N N 120 0.02 1 285 91 76 VAL H H 8.23 0.02 1 286 91 76 VAL C C 178.8 0.1 1 287 91 76 VAL CA C 66.5 0.1 1 288 91 76 VAL N N 119.1 0.02 1 289 92 77 ALA H H 8.44 0.02 1 290 92 77 ALA C C 179.2 0.1 1 291 92 77 ALA CA C 55.7 0.1 1 292 92 77 ALA N N 121 0.02 1 293 93 78 VAL H H 8.21 0.02 1 294 93 78 VAL C C 177.8 0.1 1 295 93 78 VAL CA C 67.5 0.1 1 296 93 78 VAL N N 119 0.02 1 297 94 79 VAL H H 7.55 0.02 1 298 94 79 VAL C C 178 0.1 1 299 94 79 VAL CA C 67 0.1 1 300 94 79 VAL N N 119.9 0.02 1 301 95 80 VAL H H 8.43 0.02 1 302 95 80 VAL C C 179.4 0.1 1 303 95 80 VAL CA C 67.2 0.1 1 304 95 80 VAL N N 120.1 0.02 1 305 96 81 MET H H 9.16 0.02 1 306 96 81 MET C C 177.6 0.1 1 307 96 81 MET CA C 59.7 0.1 1 308 96 81 MET N N 120.6 0.02 1 309 97 82 VAL H H 8.33 0.02 1 310 97 82 VAL C C 178.2 0.1 1 311 97 82 VAL CA C 67.5 0.1 1 312 97 82 VAL N N 117 0.02 1 313 98 83 ALA H H 8.61 0.02 1 314 98 83 ALA C C 180.1 0.1 1 315 98 83 ALA CA C 54.2 0.1 1 316 98 83 ALA N N 119.8 0.02 1 317 99 84 GLY H H 8.85 0.02 1 318 99 84 GLY C C 174.6 0.1 1 319 99 84 GLY CA C 46.7 0.1 1 320 99 84 GLY N N 112.1 0.02 1 321 100 85 ILE H H 8.5 0.02 1 322 100 85 ILE C C 181 0.1 1 323 100 85 ILE CA C 65.6 0.1 1 324 100 85 ILE N N 124 0.02 1 325 101 86 THR H H 6.85 0.02 1 326 101 86 THR C C 177.6 0.1 1 327 101 86 THR CA C 67.1 0.1 1 328 101 86 THR N N 114.9 0.02 1 329 102 87 SER H H 7.69 0.02 1 330 102 87 SER C C 176.5 0.1 1 331 102 87 SER CA C 62.8 0.1 1 332 102 87 SER N N 116.3 0.02 1 333 103 88 PHE H H 9.09 0.02 1 334 103 88 PHE C C 177.8 0.1 1 335 103 88 PHE CA C 62 0.1 1 336 103 88 PHE N N 124.4 0.02 1 337 104 89 GLY H H 8.14 0.02 1 338 104 89 GLY C C 177.1 0.1 1 339 104 89 GLY CA C 46.6 0.1 1 340 104 89 GLY N N 106.9 0.02 1 341 105 90 LEU H H 7.31 0.02 1 342 105 90 LEU C C 179.9 0.1 1 343 105 90 LEU CA C 57.4 0.1 1 344 105 90 LEU N N 122.5 0.02 1 345 106 91 VAL H H 7.65 0.02 1 346 106 91 VAL C C 178.2 0.1 1 347 106 91 VAL CA C 66.7 0.1 1 348 106 91 VAL N N 121.8 0.02 1 349 107 92 THR H H 8.11 0.02 1 350 107 92 THR C C 177.8 0.1 1 351 107 92 THR CA C 65 0.1 1 352 107 92 THR N N 110.8 0.02 1 353 108 93 ALA H H 7.6 0.02 1 354 108 93 ALA C C 181 0.1 1 355 108 93 ALA CA C 54.8 0.1 1 356 108 93 ALA N N 124.7 0.02 1 357 109 94 ALA H H 7.68 0.02 1 358 109 94 ALA C C 181.2 0.1 1 359 109 94 ALA CA C 54.7 0.1 1 360 109 94 ALA N N 122.7 0.02 1 361 110 95 LEU H H 8.27 0.02 1 362 110 95 LEU C C 178.7 0.1 1 363 110 95 LEU CA C 57.7 0.1 1 364 110 95 LEU N N 120.7 0.02 1 365 111 96 ALA H H 8.53 0.02 1 366 111 96 ALA C C 179.8 0.1 1 367 111 96 ALA CA C 55.6 0.1 1 368 111 96 ALA N N 122.1 0.02 1 369 112 97 THR H H 7.92 0.02 1 370 112 97 THR C C 177.3 0.1 1 371 112 97 THR CA C 66.3 0.1 1 372 112 97 THR N N 114.1 0.02 1 373 113 98 TRP H H 8.15 0.02 1 374 113 98 TRP C C 178.5 0.1 1 375 113 98 TRP CA C 61.3 0.1 1 376 113 98 TRP N N 125.1 0.02 1 377 114 99 PHE H H 8.63 0.02 1 378 114 99 PHE C C 178.2 0.1 1 379 114 99 PHE CA C 61.3 0.1 1 380 114 99 PHE N N 119.7 0.02 1 381 115 100 VAL H H 8.19 0.02 1 382 115 100 VAL C C 178.8 0.1 1 383 115 100 VAL CA C 65.5 0.1 1 384 115 100 VAL N N 117.7 0.02 1 385 116 101 GLY H H 7.63 0.02 1 386 116 101 GLY C C 176 0.1 1 387 116 101 GLY CA C 46.1 0.1 1 388 116 101 GLY N N 107.5 0.02 1 389 117 102 ARG H H 7.24 0.02 1 390 117 102 ARG C C 177.2 0.1 1 391 117 102 ARG CA C 56.5 0.1 1 392 117 102 ARG N N 121.2 0.02 1 393 118 103 GLU H H 7.87 0.02 1 394 118 103 GLU C C 177 0.1 1 395 118 103 GLU CA C 57 0.1 1 396 118 103 GLU N N 120.9 0.02 1 397 119 104 GLN C C 177.6 0.1 1 398 119 104 GLN CA C 57.1 0.1 1 399 120 105 GLU H H 7.9 0.02 1 400 120 105 GLU C C 177.6 0.1 1 401 120 105 GLU CA C 56.9 0.1 1 402 120 105 GLU N N 119 0.02 1 403 121 106 ARG H H 7.9 0.1 1 404 121 106 ARG C C 177 0.1 1 405 121 106 ARG CA C 56.8 0.1 1 406 121 106 ARG N N 119.2 0.1 1 407 122 107 ARG H H 7.82 0.1 1 408 122 107 ARG C C 177.3 0.1 1 409 122 107 ARG CA C 56.8 0.1 1 410 122 107 ARG N N 120.4 0.1 1 411 123 108 GLY H H 7.97 0.1 1 412 123 108 GLY C C 174.5 0.1 1 413 123 108 GLY CA C 45.4 0.1 1 414 123 108 GLY N N 108.9 0.1 1 415 124 109 HIS H H 7.86 0.1 1 416 124 109 HIS C C 174.7 0.1 1 417 124 109 HIS CA C 55.7 0.1 1 418 124 109 HIS N N 117.3 0.1 1 419 125 110 PHE H H 7.96 0.1 1 420 125 110 PHE C C 176 0.1 1 421 125 110 PHE CA C 58.7 0.1 1 422 125 110 PHE N N 120.2 0.1 1 423 126 111 VAL H H 7.54 0.1 1 424 126 111 VAL C C 176.2 0.1 1 425 126 111 VAL CA C 62.5 0.1 1 426 126 111 VAL N N 119.7 0.1 1 427 127 112 ARG H H 7.77 0.1 1 428 127 112 ARG C C 176.9 0.1 1 429 127 112 ARG CA C 56.5 0.1 1 430 127 112 ARG N N 121.8 0.1 1 431 128 113 HIS H H 8.05 0.1 1 432 128 113 HIS C C 175 0.1 1 433 128 113 HIS CA C 55.8 0.1 1 434 128 113 HIS N N 118.2 0.1 1 435 129 114 SER H H 7.93 0.1 1 436 129 114 SER C C 175.1 0.1 1 437 129 114 SER CA C 58.7 0.1 1 438 129 114 SER N N 116 0.1 1 439 130 115 GLU H H 8.21 0.1 1 440 130 115 GLU C C 177.1 0.1 1 441 130 115 GLU CA C 57.2 0.1 1 442 130 115 GLU N N 122.9 0.1 1 443 131 116 LYS H H 7.86 0.1 1 444 131 116 LYS C C 177.4 0.1 1 445 131 116 LYS CA C 56.9 0.1 1 446 131 116 LYS N N 120.8 0.1 1 447 132 117 ALA H H 7.86 0.1 1 448 132 117 ALA C C 178.6 0.1 1 449 132 117 ALA CA C 53.3 0.1 1 450 132 117 ALA N N 123.5 0.1 1 451 133 118 ALA H H 7.86 0.1 1 452 133 118 ALA C C 178.6 0.1 1 453 133 118 ALA CA C 53.5 0.1 1 454 133 118 ALA N N 121.7 0.1 1 455 134 119 GLU H H 7.94 0.1 1 456 134 119 GLU C C 178.1 0.1 1 457 134 119 GLU CA C 57.7 0.1 1 458 134 119 GLU N N 118.2 0.1 1 459 135 120 GLU H H 8 0.1 1 460 135 120 GLU C C 177.4 0.1 1 461 135 120 GLU CA C 57.3 0.1 1 462 135 120 GLU N N 120.2 0.1 1 463 136 121 ALA H H 7.99 0.1 1 464 136 121 ALA C C 179 0.1 1 465 136 121 ALA CA C 53.7 0.1 1 466 136 121 ALA N N 123.1 0.1 1 467 137 122 TYR H H 8.07 0.1 1 468 137 122 TYR C C 177.2 0.1 1 469 137 122 TYR CA C 59.4 0.1 1 470 137 122 TYR N N 119.5 0.1 1 471 138 123 THR H H 7.94 0.1 1 472 138 123 THR C C 175.7 0.1 1 473 138 123 THR CA C 63.6 0.1 1 474 138 123 THR N N 115.7 0.1 1 475 139 124 ARG H H 7.98 0.1 1 476 139 124 ARG C C 177.9 0.1 1 477 139 124 ARG CA C 57.6 0.1 1 478 139 124 ARG N N 122 0.1 1 479 140 125 THR H H 7.84 0.1 1 480 140 125 THR C C 175.8 0.1 1 481 140 125 THR CA C 64.3 0.1 1 482 140 125 THR N N 115 0.1 1 483 141 126 THR H H 7.88 0.1 1 484 141 126 THR C C 176.3 0.1 1 485 141 126 THR CA C 63.9 0.1 1 486 141 126 THR N N 114.5 0.1 1 487 142 127 ARG H H 7.82 0.1 1 488 142 127 ARG C C 177.6 0.1 1 489 142 127 ARG CA C 57.7 0.1 1 490 142 127 ARG N N 122.9 0.1 1 491 143 128 ALA H H 7.81 0.1 1 492 143 128 ALA C C 179.7 0.1 1 493 143 128 ALA CA C 53.7 0.1 1 494 143 128 ALA N N 123.1 0.1 1 495 144 129 LEU H H 7.92 0.1 1 496 144 129 LEU C C 178.5 0.1 1 497 144 129 LEU CA C 57.1 0.1 1 498 144 129 LEU N N 118.8 0.1 1 499 145 130 HIS H H 8.03 0.1 1 500 145 130 HIS C C 176.6 0.1 1 501 145 130 HIS CA C 58.1 0.1 1 502 145 130 HIS N N 116.6 0.1 1 503 146 131 GLU H H 7.97 0.1 1 504 146 131 GLU C C 178.4 0.1 1 505 146 131 GLU CA C 58.2 0.1 1 506 146 131 GLU N N 118.7 0.1 1 507 147 132 ARG H H 7.64 0.1 1 508 147 132 ARG C C 177.1 0.1 1 509 147 132 ARG CA C 56.5 0.1 1 510 147 132 ARG N N 119.1 0.1 1 511 148 133 PHE H H 7.9 0.1 1 512 148 133 PHE C C 176.8 0.1 1 513 148 133 PHE CA C 58.7 0.1 1 514 148 133 PHE N N 119.2 0.1 1 515 149 134 ASP H H 8.02 0.1 1 516 149 134 ASP C C 178.3 0.1 1 517 149 134 ASP CA C 57 0.1 1 518 149 134 ASP N N 120 0.1 1 519 150 135 ARG H H 7.74 0.1 1 520 150 135 ARG C C 178.6 0.1 1 521 150 135 ARG CA C 56.5 0.1 1 522 150 135 ARG N N 119.3 0.1 1 523 151 136 LEU H H 7.57 0.1 1 524 151 136 LEU C C 178.4 0.1 1 525 151 136 LEU CA C 57.2 0.1 1 526 151 136 LEU N N 120.3 0.1 1 527 152 137 GLU H H 8.07 0.1 1 528 152 137 GLU C C 178.4 0.1 1 529 152 137 GLU CA C 58.9 0.1 1 530 152 137 GLU N N 118.1 0.1 1 531 153 138 ARG H H 7.66 0.1 1 532 153 138 ARG C C 178.4 0.1 1 533 153 138 ARG CA C 58.3 0.1 1 534 153 138 ARG N N 118.4 0.1 1 535 154 139 MET H H 7.68 0.1 1 536 154 139 MET C C 177.9 0.1 1 537 154 139 MET CA C 57.7 0.1 1 538 154 139 MET N N 118.8 0.1 1 539 155 140 LEU H H 7.73 0.1 1 540 155 140 LEU C C 178.5 0.1 1 541 155 140 LEU CA C 57.8 0.1 1 542 155 140 LEU N N 119.4 0.1 1 543 156 141 ASP H H 7.89 0.1 1 544 156 141 ASP C C 177.5 0.1 1 545 156 141 ASP CA C 55.4 0.1 1 546 156 141 ASP N N 119 0.1 1 547 157 142 ASP H H 8 0.1 1 548 157 142 ASP C C 176.9 0.1 1 549 157 142 ASP CA C 55.2 0.1 1 550 157 142 ASP N N 119.2 0.1 1 551 158 143 ASN H H 7.85 0.1 1 552 158 143 ASN C C 175.3 0.1 1 553 158 143 ASN CA C 53.8 0.1 1 554 158 143 ASN N N 117.6 0.1 1 555 159 144 ARG H H 7.67 0.1 1 556 159 144 ARG C C 175.9 0.1 1 557 159 144 ARG CA C 56.3 0.1 1 558 159 144 ARG N N 120 0.1 1 559 160 145 ARG H H 7.57 0.1 1 560 160 145 ARG C C 181.1 0.1 1 561 160 145 ARG CA C 57.1 0.1 1 562 160 145 ARG N N 126.1 0.1 1 stop_ save_