data_19940 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts and structural constraints of outer membrane protein A ; _BMRB_accession_number 19940 _BMRB_flat_file_name bmr19940.str _Entry_type original _Submission_date 2014-04-24 _Accession_date 2014-04-24 _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 Arora Ashish . . 2 Abildgaard Frits . . 3 Bushweller John H. . 4 Cierpicki Tomasz . . 5 Liang Binyong . . 6 Tamm Lukas K. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 143 "13C chemical shifts" 463 "15N chemical shifts" 143 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-29 original author . stop_ _Original_release_date 2014-04-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of outer membrane protein A transmembrane domain by NMR spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arora Ashish . . 2 Abildgaard Frits . . 3 Bushweller John H. . 4 Tamm Lukas K. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 8 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 334 _Page_last 338 _Year 2001 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_2nd_paper _Saveframe_category citation _Citation_full . _Citation_title 'Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16569016 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 liang binyong . . 2 Bushweller John H. . 3 Tamm Lukas K. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full . _Journal_volume 128 _Journal_issue . _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 4389 _Page_last 4397 _Year 2006 _Details . save_ save_3rd_paper _Saveframe_category citation _Citation_full . _Citation_title 'Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16719475 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cierpicki Tomasz . . 2 liang binyong . . 3 Tamm Lukas K. . 4 Bushweller John H. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full . _Journal_volume 128 _Journal_issue . _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 6947 _Page_last 6951 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ompa _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ompa $OmpA 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_OmpA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common OmpA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; APKDNTWYTGAKLGFSQYHD TGFINNNGPTHENQLGAGAF GGYQVNPYVGFEMGYDFLGR MPYKGSVENGAYKAQGVQLT AKLGYPITDDLDIYTRLGGM VFRADTKSNVYGKNHDTGVS PVFAGGVEYAITPEIATRLE YQFTNNIGDAHTIGTRPDNG MLSLGVSYRFGQGEAA ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PRO 3 LYS 4 ASP 5 ASN 6 THR 7 TRP 8 TYR 9 THR 10 GLY 11 ALA 12 LYS 13 LEU 14 GLY 15 PHE 16 SER 17 GLN 18 TYR 19 HIS 20 ASP 21 THR 22 GLY 23 PHE 24 ILE 25 ASN 26 ASN 27 ASN 28 GLY 29 PRO 30 THR 31 HIS 32 GLU 33 ASN 34 GLN 35 LEU 36 GLY 37 ALA 38 GLY 39 ALA 40 PHE 41 GLY 42 GLY 43 TYR 44 GLN 45 VAL 46 ASN 47 PRO 48 TYR 49 VAL 50 GLY 51 PHE 52 GLU 53 MET 54 GLY 55 TYR 56 ASP 57 PHE 58 LEU 59 GLY 60 ARG 61 MET 62 PRO 63 TYR 64 LYS 65 GLY 66 SER 67 VAL 68 GLU 69 ASN 70 GLY 71 ALA 72 TYR 73 LYS 74 ALA 75 GLN 76 GLY 77 VAL 78 GLN 79 LEU 80 THR 81 ALA 82 LYS 83 LEU 84 GLY 85 TYR 86 PRO 87 ILE 88 THR 89 ASP 90 ASP 91 LEU 92 ASP 93 ILE 94 TYR 95 THR 96 ARG 97 LEU 98 GLY 99 GLY 100 MET 101 VAL 102 PHE 103 ARG 104 ALA 105 ASP 106 THR 107 LYS 108 SER 109 ASN 110 VAL 111 TYR 112 GLY 113 LYS 114 ASN 115 HIS 116 ASP 117 THR 118 GLY 119 VAL 120 SER 121 PRO 122 VAL 123 PHE 124 ALA 125 GLY 126 GLY 127 VAL 128 GLU 129 TYR 130 ALA 131 ILE 132 THR 133 PRO 134 GLU 135 ILE 136 ALA 137 THR 138 ARG 139 LEU 140 GLU 141 TYR 142 GLN 143 PHE 144 THR 145 ASN 146 ASN 147 ILE 148 GLY 149 ASP 150 ALA 151 HIS 152 THR 153 ILE 154 GLY 155 THR 156 ARG 157 PRO 158 ASP 159 ASN 160 GLY 161 MET 162 LEU 163 SER 164 LEU 165 GLY 166 VAL 167 SER 168 TYR 169 ARG 170 PHE 171 GLY 172 GLN 173 GLY 174 GLU 175 ALA 176 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 19410 Escherichia_Coli_tOmpA 100.00 177 97.73 100.00 3.56e-122 PDB 1G90 "Nmr Solution Structure Of Outer Membrane Protein A Transmembrane Domain: 10 Conformers" 99.43 176 100.00 100.00 1.41e-123 PDB 2GE4 "High-Resolution Solution Structure Of Outer Membrane Protein A Transmembrane Domain" 100.00 177 100.00 100.00 2.87e-124 DBJ BAA35715 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K12 substr. W3110]" 100.00 346 97.73 100.00 1.57e-121 DBJ BAB34464 "outer membrane protein 3a [Escherichia coli O157:H7 str. Sakai]" 100.00 346 97.73 100.00 1.57e-121 DBJ BAG76542 "outer membrane protein OmpA [Escherichia coli SE11]" 100.00 346 97.73 100.00 1.57e-121 DBJ BAI24400 "outer membrane protein A [Escherichia coli O26:H11 str. 11368]" 100.00 346 97.73 100.00 1.57e-121 DBJ BAI29850 "outer membrane protein A [Escherichia coli O103:H2 str. 12009]" 100.00 346 97.73 100.00 1.57e-121 EMBL CAA23588 "ompA protein [Escherichia coli]" 100.00 346 97.73 100.00 1.57e-121 EMBL CAQ31485 "outer membrane protein 3a (II*;G;d) [Escherichia coli BL21(DE3)]" 100.00 346 97.73 100.00 1.57e-121 EMBL CAR02310 "outer membrane protein A (3a;II*;G;d) [Escherichia coli S88]" 100.00 346 97.16 100.00 1.33e-121 EMBL CAR12355 "outer membrane protein A (3a;II*;G;d) [Escherichia coli UMN026]" 100.00 346 97.16 100.00 2.29e-121 EMBL CAU96868 "outer membrane protein A (3a;II*;G;d) [Escherichia coli 55989]" 100.00 346 97.73 100.00 1.57e-121 GB AAC74043 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K-12 substr. MG1655]" 100.00 346 97.73 100.00 1.57e-121 GB AAF37887 "outer membrane protein A [Escherichia coli RS218]" 100.00 346 97.16 100.00 1.33e-121 GB AAG55443 "outer membrane protein 3a (II*;G;d) [Escherichia coli O157:H7 str. EDL933]" 100.00 346 97.73 100.00 1.57e-121 GB AAP74759 "outer membrane protein A precursor [Shigella sonnei]" 100.00 346 97.73 100.00 1.57e-121 GB AAQ96072 "outer membrane protein II, partial [Escherichia coli]" 50.00 157 97.73 100.00 3.36e-53 REF NP_309068 "outer membrane protein A [Escherichia coli O157:H7 str. Sakai]" 100.00 346 97.73 100.00 1.57e-121 REF NP_415477 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K-12 substr. MG1655]" 100.00 346 97.73 100.00 1.57e-121 REF WP_000315442 "membrane protein, partial [Escherichia coli]" 100.00 343 97.73 100.00 1.33e-121 REF WP_000630860 "membrane protein, partial [Escherichia coli]" 100.00 335 97.73 100.00 2.23e-121 REF WP_000750416 "MULTISPECIES: outer membrane protein A [Enterobacteriaceae]" 100.00 346 97.73 100.00 1.57e-121 SP P0A910 "RecName: Full=Outer membrane protein A; AltName: Full=Outer membrane protein II*; Flags: Precursor" 100.00 346 97.73 100.00 1.57e-121 SP P0A911 "RecName: Full=Outer membrane protein A; AltName: Full=Outer membrane protein II*; Flags: Precursor" 100.00 346 97.73 100.00 1.57e-121 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $OmpA 'E. coli' 562 Bacteria . Escherichia coli 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 $OmpA 'recombinant technology' . Escherichia coli . pET14b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $OmpA 1 mM '[U-13C; U-15N; U-2H]' NaCl 50 mM 'natural abundance' 'potassium phosphate' 10 mM 'natural abundance' NaN3 0.01 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.3 . pH pressure 1 . atm 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ompa _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 2 PRO C C 173.955 0.012 1 2 2 2 PRO CA C 61.638 0.046 1 3 2 2 PRO CB C 30.310 0.023 1 4 3 3 LYS H H 8.331 0.004 1 5 3 3 LYS C C 175.499 0.012 1 6 3 3 LYS CA C 55.980 0.046 1 7 3 3 LYS CB C 32.037 0.023 1 8 3 3 LYS N N 119.892 0.055 1 9 4 4 ASP H H 7.871 0.004 1 10 4 4 ASP C C 175.849 0.012 1 11 4 4 ASP CA C 55.522 0.046 1 12 4 4 ASP CB C 39.736 0.023 1 13 4 4 ASP N N 121.929 0.055 1 14 5 5 ASN H H 8.276 0.004 1 15 5 5 ASN C C 174.137 0.012 1 16 5 5 ASN CA C 54.234 0.046 1 17 5 5 ASN CB C 36.704 0.023 1 18 5 5 ASN N N 115.513 0.055 1 19 6 6 THR H H 6.807 0.004 1 20 6 6 THR C C 171.538 0.012 1 21 6 6 THR CA C 59.945 0.046 1 22 6 6 THR CB C 72.332 0.023 1 23 6 6 THR N N 106.580 0.055 1 24 7 7 TRP H H 8.200 0.004 1 25 7 7 TRP C C 176.492 0.012 1 26 7 7 TRP CA C 55.493 0.046 1 27 7 7 TRP CB C 32.556 0.023 1 28 7 7 TRP N N 118.858 0.055 1 29 8 8 TYR H H 8.769 0.004 1 30 8 8 TYR C C 174.418 0.012 1 31 8 8 TYR CA C 55.653 0.046 1 32 8 8 TYR CB C 41.111 0.023 1 33 8 8 TYR N N 117.024 0.055 1 34 9 9 THR H H 8.889 0.004 1 35 9 9 THR C C 172.706 0.012 1 36 9 9 THR CA C 59.618 0.046 1 37 9 9 THR CB C 71.506 0.023 1 38 9 9 THR N N 112.133 0.055 1 39 10 10 GLY H H 8.692 0.004 1 40 10 10 GLY C C 170.037 0.012 1 41 10 10 GLY CA C 46.122 0.046 1 42 10 10 GLY N N 113.199 0.055 1 43 11 11 ALA H H 8.317 0.004 1 44 11 11 ALA C C 174.667 0.012 1 45 11 11 ALA CA C 50.089 0.046 1 46 11 11 ALA CB C 22.366 0.023 1 47 11 11 ALA N N 119.242 0.055 1 48 12 12 LYS H H 8.959 0.004 1 49 12 12 LYS C C 173.050 0.012 1 50 12 12 LYS CA C 53.956 0.046 1 51 12 12 LYS CB C 36.984 0.023 1 52 12 12 LYS N N 116.667 0.055 1 53 13 13 LEU H H 8.596 0.004 1 54 13 13 LEU C C 175.287 0.012 1 55 13 13 LEU CA C 53.499 0.046 1 56 13 13 LEU CB C 46.158 0.023 1 57 13 13 LEU N N 120.550 0.055 1 58 14 14 GLY H H 8.554 0.004 1 59 14 14 GLY C C 171.308 0.012 1 60 14 14 GLY CA C 45.842 0.046 1 61 14 14 GLY N N 108.603 0.055 1 62 15 15 PHE H H 8.589 0.004 1 63 15 15 PHE C C 174.549 0.012 1 64 15 15 PHE CA C 55.900 0.046 1 65 15 15 PHE CB C 41.647 0.023 1 66 15 15 PHE N N 118.314 0.055 1 67 17 17 GLN C C 174.906 0.012 1 68 17 17 GLN CA C 54.681 0.046 1 69 17 17 GLN CB C 31.032 0.023 1 70 18 18 TYR H H 8.461 0.004 1 71 18 18 TYR C C 175.244 0.012 1 72 18 18 TYR CA C 57.567 0.046 1 73 18 18 TYR CB C 39.034 0.023 1 74 18 18 TYR N N 123.421 0.055 1 75 19 19 HIS C C 173.723 0.012 1 76 19 19 HIS CA C 54.875 0.046 1 77 19 19 HIS CB C 30.441 0.023 1 78 20 20 ASP H H 8.302 0.004 1 79 20 20 ASP C C 176.299 0.012 1 80 20 20 ASP CA C 53.968 0.046 1 81 20 20 ASP CB C 41.403 0.023 1 82 20 20 ASP N N 122.777 0.055 1 83 21 21 THR H H 8.062 0.004 1 84 21 21 THR C C 175.209 0.012 1 85 21 21 THR CA C 61.828 0.046 1 86 21 21 THR CB C 69.082 0.023 1 87 21 21 THR N N 114.277 0.055 1 88 22 22 GLY H H 8.311 0.004 1 89 22 22 GLY C C 173.901 0.012 1 90 22 22 GLY CA C 45.256 0.046 1 91 22 22 GLY N N 110.877 0.055 1 92 23 23 PHE H H 7.875 0.004 1 93 23 23 PHE C C 175.488 0.012 1 94 23 23 PHE CA C 57.627 0.046 1 95 23 23 PHE CB C 38.849 0.023 1 96 23 23 PHE N N 120.325 0.055 1 97 24 24 ILE H H 7.775 0.004 1 98 24 24 ILE C C 175.414 0.012 1 99 24 24 ILE CA C 60.689 0.046 1 100 24 24 ILE CB C 37.952 0.023 1 101 24 24 ILE N N 121.405 0.055 1 102 25 25 ASN H H 8.146 0.004 1 103 25 25 ASN C C 174.563 0.012 1 104 25 25 ASN CA C 52.925 0.046 1 105 25 25 ASN CB C 38.771 0.023 1 106 25 25 ASN N N 122.315 0.055 1 107 26 26 ASN H H 8.183 0.004 1 108 26 26 ASN C C 173.889 0.012 1 109 26 26 ASN CA C 53.007 0.046 1 110 26 26 ASN CB C 38.694 0.023 1 111 26 26 ASN N N 120.508 0.055 1 112 27 27 ASN H H 7.790 0.004 1 113 27 27 ASN C C 169.947 0.012 1 114 27 27 ASN CA C 54.645 0.046 1 115 27 27 ASN CB C 40.266 0.023 1 116 27 27 ASN N N 124.556 0.055 1 117 29 29 PRO C C 177.221 0.012 1 118 29 29 PRO CA C 62.888 0.046 1 119 29 29 PRO CB C 31.240 0.023 1 120 30 30 THR H H 8.001 0.004 1 121 30 30 THR C C 174.300 0.012 1 122 30 30 THR CA C 61.582 0.046 1 123 30 30 THR CB C 69.236 0.023 1 124 30 30 THR N N 114.151 0.055 1 125 31 31 HIS H H 8.156 0.004 1 126 31 31 HIS C C 174.271 0.012 1 127 31 31 HIS CA C 55.246 0.046 1 128 31 31 HIS CB C 29.474 0.023 1 129 31 31 HIS N N 120.795 0.055 1 130 32 32 GLU H H 8.269 0.004 1 131 32 32 GLU C C 175.820 0.012 1 132 32 32 GLU CA C 55.869 0.046 1 133 32 32 GLU CB C 30.463 0.023 1 134 32 32 GLU N N 121.609 0.055 1 135 33 33 ASN H H 8.491 0.004 1 136 33 33 ASN C C 174.649 0.012 1 137 33 33 ASN CA C 53.253 0.046 1 138 33 33 ASN CB C 39.569 0.023 1 139 33 33 ASN N N 120.951 0.055 1 140 34 34 GLN H H 8.616 0.004 1 141 34 34 GLN C C 174.541 0.012 1 142 34 34 GLN CA C 54.503 0.046 1 143 34 34 GLN CB C 31.112 0.023 1 144 34 34 GLN N N 120.197 0.055 1 145 35 35 LEU H H 8.419 0.004 1 146 35 35 LEU C C 175.915 0.012 1 147 35 35 LEU CA C 54.370 0.046 1 148 35 35 LEU CB C 43.276 0.023 1 149 35 35 LEU N N 124.149 0.055 1 150 36 36 GLY H H 8.520 0.004 1 151 36 36 GLY C C 171.748 0.012 1 152 36 36 GLY CA C 43.652 0.046 1 153 36 36 GLY N N 110.263 0.055 1 154 37 37 ALA H H 8.657 0.004 1 155 37 37 ALA C C 175.580 0.012 1 156 37 37 ALA CA C 50.792 0.046 1 157 37 37 ALA CB C 23.079 0.023 1 158 37 37 ALA N N 120.759 0.055 1 159 38 38 GLY H H 8.344 0.004 1 160 38 38 GLY C C 171.034 0.012 1 161 38 38 GLY CA C 46.732 0.046 1 162 38 38 GLY N N 105.297 0.055 1 163 39 39 ALA H H 8.880 0.004 1 164 39 39 ALA C C 176.609 0.012 1 165 39 39 ALA CA C 49.922 0.046 1 166 39 39 ALA CB C 22.405 0.023 1 167 39 39 ALA N N 120.333 0.055 1 168 40 40 PHE H H 8.800 0.004 1 169 40 40 PHE C C 173.347 0.012 1 170 40 40 PHE CA C 56.002 0.046 1 171 40 40 PHE CB C 42.102 0.023 1 172 40 40 PHE N N 120.104 0.055 1 173 41 41 GLY H H 9.127 0.004 1 174 41 41 GLY C C 170.681 0.012 1 175 41 41 GLY CA C 44.953 0.046 1 176 41 41 GLY N N 107.678 0.055 1 177 42 42 GLY H H 8.355 0.004 1 178 42 42 GLY C C 169.368 0.012 1 179 42 42 GLY CA C 45.856 0.046 1 180 42 42 GLY N N 109.433 0.055 1 181 43 43 TYR H H 8.381 0.004 1 182 43 43 TYR C C 173.713 0.012 1 183 43 43 TYR CA C 55.384 0.046 1 184 43 43 TYR CB C 42.430 0.023 1 185 43 43 TYR N N 119.169 0.055 1 186 44 44 GLN H H 8.482 0.004 1 187 44 44 GLN C C 175.150 0.012 1 188 44 44 GLN CA C 54.631 0.046 1 189 44 44 GLN CB C 28.203 0.023 1 190 44 44 GLN N N 130.006 0.055 1 191 45 45 VAL H H 8.786 0.004 1 192 45 45 VAL C C 174.999 0.012 1 193 45 45 VAL CA C 64.801 0.046 1 194 45 45 VAL CB C 31.874 0.023 1 195 45 45 VAL N N 128.641 0.055 1 196 46 46 ASN H H 8.038 0.004 1 197 46 46 ASN C C 172.384 0.012 1 198 46 46 ASN CA C 51.424 0.046 1 199 46 46 ASN CB C 37.285 0.023 1 200 46 46 ASN N N 117.151 0.055 1 201 47 47 PRO C C 174.296 0.012 1 202 47 47 PRO CA C 65.422 0.046 1 203 48 48 TYR H H 7.564 0.004 1 204 48 48 TYR C C 176.107 0.012 1 205 48 48 TYR CA C 55.948 0.046 1 206 48 48 TYR CB C 39.886 0.023 1 207 48 48 TYR N N 111.181 0.055 1 208 49 49 VAL H H 7.277 0.004 1 209 49 49 VAL C C 173.773 0.012 1 210 49 49 VAL CA C 60.546 0.046 1 211 49 49 VAL CB C 34.530 0.023 1 212 49 49 VAL N N 117.337 0.055 1 213 50 50 GLY H H 8.796 0.004 1 214 50 50 GLY C C 170.631 0.012 1 215 50 50 GLY CA C 44.133 0.046 1 216 50 50 GLY N N 115.384 0.055 1 217 51 51 PHE H H 8.753 0.004 1 218 51 51 PHE C C 173.595 0.012 1 219 51 51 PHE CA C 56.650 0.046 1 220 51 51 PHE CB C 42.924 0.023 1 221 51 51 PHE N N 117.914 0.055 1 222 52 52 GLU H H 9.027 0.004 1 223 52 52 GLU C C 174.815 0.012 1 224 52 52 GLU CA C 54.968 0.046 1 225 52 52 GLU CB C 34.066 0.023 1 226 52 52 GLU N N 119.851 0.055 1 227 53 53 MET H H 9.339 0.004 1 228 53 53 MET C C 174.782 0.012 1 229 53 53 MET CA C 53.326 0.046 1 230 53 53 MET CB C 36.247 0.023 1 231 53 53 MET N N 124.592 0.055 1 232 54 54 GLY H H 8.769 0.004 1 233 54 54 GLY C C 170.813 0.012 1 234 54 54 GLY CA C 44.892 0.046 1 235 54 54 GLY N N 109.020 0.055 1 236 55 55 TYR H H 8.786 0.004 1 237 55 55 TYR C C 173.539 0.012 1 238 55 55 TYR CA C 56.090 0.046 1 239 55 55 TYR CB C 41.840 0.023 1 240 55 55 TYR N N 123.746 0.055 1 241 56 56 ASP H H 8.579 0.004 1 242 56 56 ASP C C 173.984 0.012 1 243 56 56 ASP CA C 53.139 0.046 1 244 56 56 ASP CB C 43.172 0.023 1 245 56 56 ASP N N 126.840 0.055 1 246 57 57 PHE H H 9.017 0.004 1 247 57 57 PHE CA C 56.463 0.046 1 248 57 57 PHE CB C 40.194 0.023 1 249 57 57 PHE N N 119.936 0.055 1 250 59 59 GLY C C 173.980 0.012 1 251 59 59 GLY CA C 45.181 0.046 1 252 60 60 ARG H H 7.884 0.004 1 253 60 60 ARG C C 176.160 0.012 1 254 60 60 ARG CA C 55.835 0.046 1 255 60 60 ARG CB C 30.188 0.023 1 256 60 60 ARG N N 120.814 0.055 1 257 62 62 PRO C C 175.745 0.012 1 258 62 62 PRO CA C 62.660 0.046 1 259 62 62 PRO CB C 30.633 0.023 1 260 63 63 TYR H H 7.759 0.004 1 261 63 63 TYR C C 175.449 0.012 1 262 63 63 TYR CA C 57.543 0.046 1 263 63 63 TYR CB C 38.078 0.023 1 264 63 63 TYR N N 119.247 0.055 1 265 64 64 LYS H H 8.104 0.004 1 266 64 64 LYS C C 176.577 0.012 1 267 64 64 LYS CA C 55.944 0.046 1 268 64 64 LYS CB C 31.949 0.023 1 269 64 64 LYS N N 123.040 0.055 1 270 65 65 GLY H H 7.947 0.004 1 271 65 65 GLY C C 173.940 0.012 1 272 65 65 GLY CA C 45.176 0.046 1 273 65 65 GLY N N 109.841 0.055 1 274 66 66 SER H H 7.968 0.004 1 275 66 66 SER C C 174.555 0.012 1 276 66 66 SER CA C 57.801 0.046 1 277 66 66 SER CB C 63.406 0.023 1 278 66 66 SER N N 115.885 0.055 1 279 67 67 VAL H H 7.893 0.004 1 280 67 67 VAL C C 175.807 0.012 1 281 67 67 VAL CA C 61.783 0.046 1 282 67 67 VAL CB C 32.016 0.023 1 283 67 67 VAL N N 120.738 0.055 1 284 68 68 GLU H H 8.162 0.004 1 285 68 68 GLU C C 175.178 0.012 1 286 68 68 GLU CA C 56.182 0.046 1 287 68 68 GLU CB C 29.648 0.023 1 288 68 68 GLU N N 123.719 0.055 1 289 69 69 ASN H H 7.791 0.004 1 290 69 69 ASN C C 169.791 0.012 1 291 69 69 ASN CA C 54.603 0.046 1 292 69 69 ASN CB C 40.588 0.023 1 293 69 69 ASN N N 125.691 0.055 1 294 70 70 GLY C C 173.868 0.012 1 295 70 70 GLY CA C 45.284 0.046 1 296 71 71 ALA H H 8.023 0.004 1 297 71 71 ALA C C 176.964 0.012 1 298 71 71 ALA CA C 52.045 0.046 1 299 71 71 ALA CB C 19.178 0.023 1 300 71 71 ALA N N 123.406 0.055 1 301 72 72 TYR H H 8.023 0.004 1 302 72 72 TYR C C 174.924 0.012 1 303 72 72 TYR CA C 57.274 0.046 1 304 72 72 TYR CB C 38.661 0.023 1 305 72 72 TYR N N 119.865 0.055 1 306 73 73 LYS H H 8.086 0.004 1 307 73 73 LYS C C 174.909 0.012 1 308 73 73 LYS CA C 55.486 0.046 1 309 73 73 LYS CB C 33.235 0.023 1 310 73 73 LYS N N 123.632 0.055 1 311 77 77 VAL C C 173.855 0.012 1 312 77 77 VAL CA C 59.419 0.046 1 313 77 77 VAL CB C 34.329 0.023 1 314 78 78 GLN H H 9.272 0.004 1 315 78 78 GLN C C 174.068 0.012 1 316 78 78 GLN CA C 52.223 0.046 1 317 78 78 GLN CB C 33.810 0.023 1 318 78 78 GLN N N 122.006 0.055 1 319 79 79 LEU H H 8.389 0.004 1 320 79 79 LEU C C 175.342 0.012 1 321 79 79 LEU CA C 54.047 0.046 1 322 79 79 LEU CB C 44.654 0.023 1 323 79 79 LEU N N 123.890 0.055 1 324 80 80 THR H H 9.058 0.004 1 325 80 80 THR C C 173.350 0.012 1 326 80 80 THR CA C 58.886 0.046 1 327 80 80 THR CB C 72.917 0.023 1 328 80 80 THR N N 112.529 0.055 1 329 81 81 ALA H H 8.656 0.004 1 330 81 81 ALA C C 174.975 0.012 1 331 81 81 ALA CA C 50.385 0.046 1 332 81 81 ALA CB C 19.166 0.023 1 333 81 81 ALA N N 122.467 0.055 1 334 82 82 LYS H H 8.820 0.004 1 335 82 82 LYS C C 174.099 0.012 1 336 82 82 LYS CA C 54.054 0.046 1 337 82 82 LYS CB C 32.704 0.023 1 338 82 82 LYS N N 125.249 0.055 1 339 83 83 LEU H H 8.877 0.004 1 340 83 83 LEU C C 175.667 0.012 1 341 83 83 LEU CA C 52.395 0.046 1 342 83 83 LEU CB C 42.460 0.023 1 343 83 83 LEU N N 131.186 0.055 1 344 84 84 GLY H H 9.242 0.004 1 345 84 84 GLY C C 170.267 0.012 1 346 84 84 GLY CA C 45.164 0.046 1 347 84 84 GLY N N 111.602 0.055 1 348 85 85 TYR H H 8.801 0.004 1 349 85 85 TYR C C 174.065 0.012 1 350 85 85 TYR CA C 54.327 0.046 1 351 85 85 TYR CB C 43.245 0.023 1 352 85 85 TYR N N 116.939 0.055 1 353 86 86 PRO C C 175.192 0.012 1 354 86 86 PRO CA C 61.198 0.046 1 355 86 86 PRO CB C 29.692 0.023 1 356 87 87 ILE H H 8.458 0.004 1 357 87 87 ILE C C 176.746 0.012 1 358 87 87 ILE CA C 62.877 0.046 1 359 87 87 ILE CB C 37.889 0.023 1 360 87 87 ILE N N 128.156 0.055 1 361 88 88 THR H H 8.080 0.004 1 362 88 88 THR C C 174.249 0.012 1 363 88 88 THR CA C 58.963 0.046 1 364 88 88 THR CB C 71.239 0.023 1 365 88 88 THR N N 108.871 0.055 1 366 89 89 ASP H H 8.342 0.004 1 367 89 89 ASP C C 175.795 0.012 1 368 89 89 ASP CA C 56.579 0.046 1 369 89 89 ASP CB C 40.077 0.023 1 370 89 89 ASP N N 117.312 0.055 1 371 90 90 ASP H H 7.781 0.004 1 372 90 90 ASP C C 173.922 0.012 1 373 90 90 ASP CA C 53.443 0.046 1 374 90 90 ASP CB C 42.626 0.023 1 375 90 90 ASP N N 113.538 0.055 1 376 91 91 LEU H H 7.372 0.004 1 377 91 91 LEU C C 174.037 0.012 1 378 91 91 LEU CA C 54.061 0.046 1 379 91 91 LEU CB C 45.102 0.023 1 380 91 91 LEU N N 124.508 0.055 1 381 92 92 ASP H H 8.990 0.004 1 382 92 92 ASP C C 176.382 0.012 1 383 92 92 ASP CA C 52.857 0.046 1 384 92 92 ASP CB C 44.200 0.023 1 385 92 92 ASP N N 124.036 0.055 1 386 93 93 ILE H H 8.263 0.004 1 387 93 93 ILE C C 173.755 0.012 1 388 93 93 ILE CA C 59.459 0.046 1 389 93 93 ILE CB C 39.565 0.023 1 390 93 93 ILE N N 119.989 0.055 1 391 94 94 TYR H H 8.716 0.004 1 392 94 94 TYR C C 172.450 0.012 1 393 94 94 TYR CA C 56.469 0.046 1 394 94 94 TYR CB C 41.657 0.023 1 395 94 94 TYR N N 122.140 0.055 1 396 95 95 THR H H 9.268 0.004 1 397 95 95 THR C C 173.956 0.012 1 398 95 95 THR CA C 58.419 0.046 1 399 95 95 THR CB C 71.827 0.023 1 400 95 95 THR N N 111.256 0.055 1 401 96 96 ARG H H 8.683 0.004 1 402 96 96 ARG C C 175.161 0.012 1 403 96 96 ARG CA C 54.131 0.046 1 404 96 96 ARG CB C 32.322 0.023 1 405 96 96 ARG N N 120.756 0.055 1 406 97 97 LEU H H 8.495 0.004 1 407 97 97 LEU C C 175.835 0.012 1 408 97 97 LEU CA C 53.447 0.046 1 409 97 97 LEU CB C 45.375 0.023 1 410 97 97 LEU N N 119.913 0.055 1 411 98 98 GLY H H 8.174 0.004 1 412 98 98 GLY C C 171.313 0.012 1 413 98 98 GLY CA C 46.486 0.046 1 414 98 98 GLY N N 109.092 0.055 1 415 99 99 GLY H H 8.278 0.004 1 416 99 99 GLY C C 169.620 0.012 1 417 99 99 GLY CA C 44.214 0.046 1 418 99 99 GLY N N 109.801 0.055 1 419 100 100 MET H H 9.018 0.004 1 420 100 100 MET C C 174.048 0.012 1 421 100 100 MET CA C 53.507 0.046 1 422 100 100 MET CB C 36.492 0.023 1 423 100 100 MET N N 120.848 0.055 1 424 101 101 VAL H H 8.896 0.004 1 425 101 101 VAL C C 174.591 0.012 1 426 101 101 VAL CA C 59.695 0.046 1 427 101 101 VAL CB C 32.661 0.023 1 428 101 101 VAL N N 125.135 0.055 1 429 102 102 PHE H H 8.547 0.004 1 430 102 102 PHE C C 174.594 0.012 1 431 102 102 PHE CA C 56.401 0.046 1 432 102 102 PHE CB C 41.355 0.023 1 433 102 102 PHE N N 124.120 0.055 1 434 103 103 ARG H H 8.730 0.004 1 435 103 103 ARG C C 175.495 0.012 1 436 103 103 ARG CA C 55.032 0.046 1 437 103 103 ARG CB C 31.823 0.023 1 438 103 103 ARG N N 120.515 0.055 1 439 104 104 ALA H H 8.805 0.004 1 440 104 104 ALA C C 176.528 0.012 1 441 104 104 ALA CA C 51.292 0.046 1 442 104 104 ALA CB C 20.165 0.023 1 443 104 104 ALA N N 128.271 0.055 1 444 105 105 ASP H H 8.362 0.004 1 445 105 105 ASP C C 176.265 0.012 1 446 105 105 ASP CA C 53.940 0.046 1 447 105 105 ASP CB C 41.526 0.023 1 448 105 105 ASP N N 121.705 0.055 1 449 106 106 THR H H 8.023 0.004 1 450 106 106 THR C C 174.737 0.012 1 451 106 106 THR CA C 61.369 0.046 1 452 106 106 THR CB C 69.389 0.023 1 453 106 106 THR N N 114.899 0.055 1 454 107 107 LYS H H 8.185 0.004 1 455 107 107 LYS C C 176.685 0.012 1 456 107 107 LYS CA C 56.350 0.046 1 457 107 107 LYS CB C 31.930 0.023 1 458 107 107 LYS N N 122.635 0.055 1 459 108 108 SER H H 7.985 0.004 1 460 108 108 SER C C 174.489 0.012 1 461 108 108 SER CA C 57.947 0.046 1 462 108 108 SER CB C 63.310 0.023 1 463 108 108 SER N N 115.963 0.055 1 464 109 109 ASN C C 175.421 0.012 1 465 109 109 ASN CA C 53.322 0.046 1 466 109 109 ASN CB C 38.272 0.023 1 467 110 110 VAL H H 7.787 0.004 1 468 110 110 VAL C C 175.940 0.012 1 469 110 110 VAL CA C 62.676 0.046 1 470 110 110 VAL CB C 31.612 0.023 1 471 110 110 VAL N N 119.272 0.055 1 472 111 111 TYR H H 7.858 0.004 1 473 111 111 TYR C C 176.313 0.012 1 474 111 111 TYR CA C 57.776 0.046 1 475 111 111 TYR CB C 37.877 0.023 1 476 111 111 TYR N N 121.392 0.055 1 477 112 112 GLY H H 7.931 0.004 1 478 112 112 GLY C C 173.587 0.012 1 479 112 112 GLY CA C 45.224 0.046 1 480 112 112 GLY N N 110.361 0.055 1 481 113 113 LYS H H 7.851 0.004 1 482 113 113 LYS C C 175.332 0.012 1 483 113 113 LYS CA C 55.630 0.046 1 484 113 113 LYS CB C 32.453 0.023 1 485 113 113 LYS N N 121.020 0.055 1 486 114 114 ASN H H 7.913 0.004 1 487 114 114 ASN C C 169.890 0.012 1 488 114 114 ASN CA C 54.517 0.046 1 489 114 114 ASN CB C 40.278 0.023 1 490 114 114 ASN N N 126.096 0.055 1 491 116 116 ASP C C 175.784 0.012 1 492 116 116 ASP CA C 54.022 0.046 1 493 116 116 ASP CB C 41.630 0.023 1 494 117 117 THR H H 8.057 0.004 1 495 117 117 THR C C 174.258 0.012 1 496 117 117 THR CA C 61.299 0.046 1 497 117 117 THR CB C 70.118 0.023 1 498 117 117 THR N N 116.032 0.055 1 499 118 118 GLY H H 7.983 0.004 1 500 118 118 GLY C C 171.764 0.012 1 501 118 118 GLY CA C 44.806 0.046 1 502 118 118 GLY N N 111.314 0.055 1 503 119 119 VAL H H 8.046 0.004 1 504 119 119 VAL C C 175.261 0.012 1 505 119 119 VAL CA C 59.971 0.046 1 506 119 119 VAL CB C 33.650 0.023 1 507 119 119 VAL N N 118.896 0.055 1 508 121 121 PRO C C 174.765 0.012 1 509 121 121 PRO CA C 62.797 0.046 1 510 121 121 PRO CB C 31.881 0.023 1 511 122 122 VAL H H 7.892 0.004 1 512 122 122 VAL C C 172.221 0.012 1 513 122 122 VAL CA C 60.314 0.046 1 514 122 122 VAL CB C 34.408 0.023 1 515 122 122 VAL N N 122.746 0.055 1 516 123 123 PHE C C 173.942 0.012 1 517 123 123 PHE CA C 54.781 0.046 1 518 123 123 PHE CB C 42.867 0.023 1 519 124 124 ALA H H 9.022 0.004 1 520 124 124 ALA C C 176.315 0.012 1 521 124 124 ALA CA C 49.894 0.046 1 522 124 124 ALA CB C 22.383 0.023 1 523 124 124 ALA N N 125.477 0.055 1 524 125 125 GLY H H 8.358 0.004 1 525 125 125 GLY C C 170.882 0.012 1 526 125 125 GLY CA C 44.394 0.046 1 527 125 125 GLY N N 107.000 0.055 1 528 126 126 GLY H H 8.051 0.004 1 529 126 126 GLY C C 170.170 0.012 1 530 126 126 GLY CA C 45.879 0.046 1 531 126 126 GLY N N 109.824 0.055 1 532 127 127 VAL H H 8.296 0.004 1 533 127 127 VAL C C 174.592 0.012 1 534 127 127 VAL CA C 57.983 0.046 1 535 127 127 VAL CB C 34.636 0.023 1 536 127 127 VAL N N 111.822 0.055 1 537 128 128 GLU H H 8.916 0.004 1 538 128 128 GLU C C 173.601 0.012 1 539 128 128 GLU CA C 55.141 0.046 1 540 128 128 GLU CB C 32.977 0.023 1 541 128 128 GLU N N 123.089 0.055 1 542 129 129 TYR H H 9.406 0.004 1 543 129 129 TYR C C 173.722 0.012 1 544 129 129 TYR CA C 54.921 0.046 1 545 129 129 TYR CB C 42.282 0.023 1 546 129 129 TYR N N 130.126 0.055 1 547 130 130 ALA H H 8.316 0.004 1 548 130 130 ALA C C 174.325 0.012 1 549 130 130 ALA CA C 51.149 0.046 1 550 130 130 ALA CB C 17.004 0.023 1 551 130 130 ALA N N 133.123 0.055 1 552 131 131 ILE H H 8.058 0.004 1 553 131 131 ILE C C 176.700 0.012 1 554 131 131 ILE CA C 63.501 0.046 1 555 131 131 ILE CB C 38.176 0.023 1 556 131 131 ILE N N 126.543 0.055 1 557 132 132 THR H H 8.154 0.004 1 558 132 132 THR C C 172.180 0.012 1 559 132 132 THR CA C 58.288 0.046 1 560 132 132 THR CB C 68.782 0.023 1 561 132 132 THR N N 111.002 0.055 1 562 133 133 PRO C C 177.276 0.012 1 563 133 133 PRO CA C 64.823 0.046 1 564 133 133 PRO CB C 30.654 0.023 1 565 134 134 GLU H H 7.320 0.004 1 566 134 134 GLU C C 174.366 0.012 1 567 134 134 GLU CA C 57.368 0.046 1 568 134 134 GLU CB C 30.456 0.023 1 569 134 134 GLU N N 110.590 0.055 1 570 135 135 ILE H H 7.172 0.004 1 571 135 135 ILE C C 173.792 0.012 1 572 135 135 ILE CA C 59.399 0.046 1 573 135 135 ILE CB C 38.543 0.023 1 574 135 135 ILE N N 118.706 0.055 1 575 136 136 ALA H H 8.580 0.004 1 576 136 136 ALA C C 176.607 0.012 1 577 136 136 ALA CA C 49.106 0.046 1 578 136 136 ALA CB C 21.586 0.023 1 579 136 136 ALA N N 127.496 0.055 1 580 137 137 THR H H 9.107 0.004 1 581 137 137 THR C C 172.493 0.012 1 582 137 137 THR CA C 58.921 0.046 1 583 137 137 THR CB C 70.916 0.023 1 584 137 137 THR N N 114.862 0.055 1 585 138 138 ARG H H 9.146 0.004 1 586 138 138 ARG C C 173.605 0.012 1 587 138 138 ARG CA C 53.051 0.046 1 588 138 138 ARG CB C 33.062 0.023 1 589 138 138 ARG N N 123.234 0.055 1 590 139 139 LEU H H 8.419 0.004 1 591 139 139 LEU C C 174.532 0.012 1 592 139 139 LEU CA C 53.586 0.046 1 593 139 139 LEU CB C 44.764 0.023 1 594 139 139 LEU N N 124.515 0.055 1 595 140 140 GLU H H 8.710 0.004 1 596 140 140 GLU C C 173.420 0.012 1 597 140 140 GLU CA C 54.139 0.046 1 598 140 140 GLU CB C 33.832 0.023 1 599 140 140 GLU N N 121.948 0.055 1 600 141 141 TYR H H 8.809 0.004 1 601 141 141 TYR C C 173.731 0.012 1 602 141 141 TYR CA C 56.127 0.046 1 603 141 141 TYR CB C 41.334 0.023 1 604 141 141 TYR N N 124.800 0.055 1 605 142 142 GLN H H 8.493 0.004 1 606 142 142 GLN C C 173.732 0.012 1 607 142 142 GLN CA C 53.754 0.046 1 608 142 142 GLN CB C 34.040 0.023 1 609 142 142 GLN N N 127.171 0.055 1 610 145 145 ASN C C 174.438 0.012 1 611 145 145 ASN CA C 52.555 0.046 1 612 145 145 ASN CB C 40.793 0.023 1 613 146 146 ASN H H 8.664 0.004 1 614 146 146 ASN C C 174.813 0.012 1 615 146 146 ASN CA C 53.315 0.046 1 616 146 146 ASN CB C 38.023 0.023 1 617 146 146 ASN N N 119.917 0.055 1 618 147 147 ILE H H 8.112 0.004 1 619 147 147 ILE C C 175.779 0.012 1 620 147 147 ILE CA C 61.194 0.046 1 621 147 147 ILE CB C 37.674 0.023 1 622 147 147 ILE N N 121.423 0.055 1 623 148 148 GLY C C 173.203 0.012 1 624 148 148 GLY CA C 44.781 0.046 1 625 149 149 ASP H H 7.830 0.004 1 626 149 149 ASP C C 176.276 0.012 1 627 149 149 ASP CA C 53.703 0.046 1 628 149 149 ASP CB C 41.404 0.023 1 629 149 149 ASP N N 120.392 0.055 1 630 150 150 ALA H H 8.206 0.004 1 631 150 150 ALA C C 177.853 0.012 1 632 150 150 ALA CA C 52.996 0.046 1 633 150 150 ALA CB C 18.090 0.023 1 634 150 150 ALA N N 124.319 0.055 1 635 151 151 HIS C C 175.034 0.012 1 636 151 151 HIS CA C 56.013 0.046 1 637 151 151 HIS CB C 29.992 0.023 1 638 152 152 THR H H 7.746 0.004 1 639 152 152 THR C C 174.495 0.012 1 640 152 152 THR CA C 61.879 0.046 1 641 152 152 THR CB C 69.242 0.023 1 642 152 152 THR N N 114.749 0.055 1 643 153 153 ILE H H 7.991 0.004 1 644 153 153 ILE C C 176.240 0.012 1 645 153 153 ILE CA C 61.286 0.046 1 646 153 153 ILE CB C 37.764 0.023 1 647 153 153 ILE N N 122.796 0.055 1 648 154 154 GLY H H 8.155 0.004 1 649 154 154 GLY C C 173.815 0.012 1 650 154 154 GLY CA C 45.136 0.046 1 651 154 154 GLY N N 112.193 0.055 1 652 155 155 THR H H 7.708 0.004 1 653 155 155 THR C C 173.858 0.012 1 654 155 155 THR CA C 61.317 0.046 1 655 155 155 THR CB C 69.301 0.023 1 656 155 155 THR N N 113.729 0.055 1 657 156 156 ARG H H 8.092 0.004 1 658 156 156 ARG C C 173.935 0.012 1 659 156 156 ARG CA C 53.468 0.046 1 660 156 156 ARG CB C 29.730 0.023 1 661 156 156 ARG N N 123.536 0.055 1 662 157 157 PRO C C 175.562 0.012 1 663 157 157 PRO CA C 62.646 0.046 1 664 157 157 PRO CB C 31.273 0.023 1 665 158 158 ASP H H 8.177 0.004 1 666 158 158 ASP C C 175.545 0.012 1 667 158 158 ASP CA C 53.451 0.046 1 668 158 158 ASP CB C 42.217 0.023 1 669 158 158 ASP N N 119.090 0.055 1 670 159 159 ASN H H 8.350 0.004 1 671 159 159 ASN C C 173.662 0.012 1 672 159 159 ASN CA C 52.893 0.046 1 673 159 159 ASN CB C 41.111 0.023 1 674 159 159 ASN N N 118.163 0.055 1 675 161 161 MET C C 173.844 0.012 1 676 161 161 MET CA C 54.117 0.046 1 677 161 161 MET CB C 35.691 0.023 1 678 162 162 LEU H H 8.290 0.004 1 679 162 162 LEU C C 175.274 0.012 1 680 162 162 LEU CA C 53.526 0.046 1 681 162 162 LEU CB C 43.337 0.023 1 682 162 162 LEU N N 131.252 0.055 1 683 163 163 SER H H 9.419 0.004 1 684 163 163 SER C C 171.202 0.012 1 685 163 163 SER CA C 56.711 0.046 1 686 163 163 SER CB C 66.655 0.023 1 687 163 163 SER N N 119.502 0.055 1 688 164 164 LEU H H 8.578 0.004 1 689 164 164 LEU C C 175.483 0.012 1 690 164 164 LEU CA C 52.904 0.046 1 691 164 164 LEU CB C 45.305 0.023 1 692 164 164 LEU N N 123.743 0.055 1 693 165 165 GLY H H 9.255 0.004 1 694 165 165 GLY C C 172.607 0.012 1 695 165 165 GLY CA C 43.634 0.046 1 696 165 165 GLY N N 110.163 0.055 1 697 166 166 VAL H H 8.995 0.004 1 698 166 166 VAL C C 173.051 0.012 1 699 166 166 VAL CA C 59.739 0.046 1 700 166 166 VAL CB C 34.340 0.023 1 701 166 166 VAL N N 120.767 0.055 1 702 167 167 SER H H 9.043 0.004 1 703 167 167 SER C C 171.112 0.012 1 704 167 167 SER CA C 55.814 0.046 1 705 167 167 SER CB C 66.736 0.023 1 706 167 167 SER N N 117.577 0.055 1 707 168 168 TYR H H 8.865 0.004 1 708 168 168 TYR C C 174.406 0.012 1 709 168 168 TYR CA C 55.657 0.046 1 710 168 168 TYR CB C 41.767 0.023 1 711 168 168 TYR N N 122.853 0.055 1 712 169 169 ARG H H 8.556 0.004 1 713 169 169 ARG C C 174.421 0.012 1 714 169 169 ARG CA C 54.110 0.046 1 715 169 169 ARG CB C 30.303 0.023 1 716 169 169 ARG N N 126.607 0.055 1 717 170 170 PHE H H 8.501 0.004 1 718 170 170 PHE C C 179.329 0.012 1 719 170 170 PHE CA C 58.247 0.046 1 720 170 170 PHE CB C 39.774 0.023 1 721 170 170 PHE N N 121.617 0.055 1 722 171 171 GLY H H 9.259 0.004 1 723 171 171 GLY C C 175.501 0.012 1 724 171 171 GLY CA C 47.334 0.046 1 725 171 171 GLY N N 112.601 0.055 1 726 172 172 GLN H H 8.832 0.004 1 727 172 172 GLN C C 176.629 0.012 1 728 172 172 GLN CA C 55.344 0.046 1 729 172 172 GLN CB C 27.955 0.023 1 730 172 172 GLN N N 116.181 0.055 1 731 173 173 GLY H H 8.132 0.004 1 732 173 173 GLY C C 173.845 0.012 1 733 173 173 GLY CA C 44.828 0.046 1 734 173 173 GLY N N 108.123 0.055 1 735 174 174 GLU H H 8.016 0.004 1 736 174 174 GLU C C 176.100 0.012 1 737 174 174 GLU CA C 55.882 0.046 1 738 174 174 GLU CB C 29.816 0.023 1 739 174 174 GLU N N 120.946 0.055 1 740 175 175 ALA H H 8.092 0.004 1 741 175 175 ALA C C 176.205 0.012 1 742 175 175 ALA CA C 52.029 0.046 1 743 175 175 ALA CB C 18.660 0.023 1 744 175 175 ALA N N 126.058 0.055 1 745 176 176 ALA H H 7.673 0.004 1 746 176 176 ALA C C 173.075 0.012 1 747 176 176 ALA CA C 53.321 0.046 1 748 176 176 ALA CB C 19.532 0.023 1 749 176 176 ALA N N 129.706 0.055 1 stop_ save_