data_6722 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR Assignment of low-molecular-weight Protein Tryosin Phosphatase (MPtpA) from Mycobacterium tuberculosis ; _BMRB_accession_number 6722 _BMRB_flat_file_name bmr6722.str _Entry_type original _Submission_date 2005-07-01 _Accession_date 2005-07-01 _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 Saxena Krishna . . 2 Elshorst Bettina . . 3 Berk Holger . . 4 Betz Marco . . 5 Grimme Susanne . . 6 Langer Thomas . . 7 Pescatore Barbara . . 8 Schieborr Ulrich . . 9 Vogtherr Martin . . 10 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 147 "13C chemical shifts" 444 "15N chemical shifts" 147 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-07 original author . stop_ _Original_release_date 2005-11-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone NMR Assignment of the Low-molecular-weight Protein Tyrosine Phosphatase (MPtpA) from Mycobacterium Tuberculosis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16258834 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saxena Krishna . . 2 Elshorst Bettina . . 3 Berk Holger . . 4 Betz Marco . . 5 Grimme Susanne . . 6 Langer Thomas . . 7 Pescatore Barbara . . 8 Schieborr Ulrich . . 9 Vogtherr Martin . . 10 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 33 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 136 _Page_last 136 _Year 2005 _Details . loop_ _Keyword 'Backbone NMR Assignment' 'Protein Tyrosin Phosphatase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Low-Molecular-Weight Protein Tyrosine Phosphatase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Low-Molecular-Weight Protein Tyrosin Phosphatase' $MPtpA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MPtpA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Low-Molecular-Weight Protein Tyrosine Phosphatase' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; GHMSDPLHVTFVCTGNICRS PMAEKMFAQQLRHRGLGDAV RVTSAGTGNWHVGSCADERA AGVLRAHGYPTDHRAAQVGT EHLAADLLVALDRNHARLLR QLGVEAARVRMLRSFDPRSG THALDVEDPYYGDHSDFEEV FAVIESALPGLHDWVDERLA RNGPS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 HIS 3 1 MET 4 2 SER 5 3 ASP 6 4 PRO 7 5 LEU 8 6 HIS 9 7 VAL 10 8 THR 11 9 PHE 12 10 VAL 13 11 CYS 14 12 THR 15 13 GLY 16 14 ASN 17 15 ILE 18 16 CYS 19 17 ARG 20 18 SER 21 19 PRO 22 20 MET 23 21 ALA 24 22 GLU 25 23 LYS 26 24 MET 27 25 PHE 28 26 ALA 29 27 GLN 30 28 GLN 31 29 LEU 32 30 ARG 33 31 HIS 34 32 ARG 35 33 GLY 36 34 LEU 37 35 GLY 38 36 ASP 39 37 ALA 40 38 VAL 41 39 ARG 42 40 VAL 43 41 THR 44 42 SER 45 43 ALA 46 44 GLY 47 45 THR 48 46 GLY 49 47 ASN 50 48 TRP 51 49 HIS 52 50 VAL 53 51 GLY 54 52 SER 55 53 CYS 56 54 ALA 57 55 ASP 58 56 GLU 59 57 ARG 60 58 ALA 61 59 ALA 62 60 GLY 63 61 VAL 64 62 LEU 65 63 ARG 66 64 ALA 67 65 HIS 68 66 GLY 69 67 TYR 70 68 PRO 71 69 THR 72 70 ASP 73 71 HIS 74 72 ARG 75 73 ALA 76 74 ALA 77 75 GLN 78 76 VAL 79 77 GLY 80 78 THR 81 79 GLU 82 80 HIS 83 81 LEU 84 82 ALA 85 83 ALA 86 84 ASP 87 85 LEU 88 86 LEU 89 87 VAL 90 88 ALA 91 89 LEU 92 90 ASP 93 91 ARG 94 92 ASN 95 93 HIS 96 94 ALA 97 95 ARG 98 96 LEU 99 97 LEU 100 98 ARG 101 99 GLN 102 100 LEU 103 101 GLY 104 102 VAL 105 103 GLU 106 104 ALA 107 105 ALA 108 106 ARG 109 107 VAL 110 108 ARG 111 109 MET 112 110 LEU 113 111 ARG 114 112 SER 115 113 PHE 116 114 ASP 117 115 PRO 118 116 ARG 119 117 SER 120 118 GLY 121 119 THR 122 120 HIS 123 121 ALA 124 122 LEU 125 123 ASP 126 124 VAL 127 125 GLU 128 126 ASP 129 127 PRO 130 128 TYR 131 129 TYR 132 130 GLY 133 131 ASP 134 132 HIS 135 133 SER 136 134 ASP 137 135 PHE 138 136 GLU 139 137 GLU 140 138 VAL 141 139 PHE 142 140 ALA 143 141 VAL 144 142 ILE 145 143 GLU 146 144 SER 147 145 ALA 148 146 LEU 149 147 PRO 150 148 GLY 151 149 LEU 152 150 HIS 153 151 ASP 154 152 TRP 155 153 VAL 156 154 ASP 157 155 GLU 158 156 ARG 159 157 LEU 160 158 ALA 161 159 ARG 162 160 ASN 163 161 GLY 164 162 PRO 165 163 SER 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 18533 mptpa 98.79 164 100.00 100.00 3.35e-114 BMRB 19361 MptpA 98.79 164 99.39 99.39 2.20e-113 BMRB 19388 MptpA 98.79 164 99.39 99.39 2.20e-113 PDB 1U2P "Crystal Structure Of Mycobacterium Tuberculosis Low Molecular Protein Tyrosine Phosphatase (Mptpa) At 1.9a Resolution" 98.79 163 100.00 100.00 2.78e-114 PDB 1U2Q "Crystal Structure Of Mycobacterium Tuberculosis Low Molecular Weight Protein Tyrosine Phosphatase (Mptpa) At 2.5a Resolution Wi" 98.79 163 100.00 100.00 2.78e-114 PDB 2LUO "Nmr Solution Structure Of Apo-Mptpa" 98.79 164 100.00 100.00 3.35e-114 DBJ BAH26529 "phosphotyrosine protein phosphatase [Mycobacterium bovis BCG str. Tokyo 172]" 98.79 163 100.00 100.00 2.78e-114 DBJ BAL66249 "phosphotyrosine protein phosphatase [Mycobacterium tuberculosis str. Erdman = ATCC 35801]" 98.79 163 100.00 100.00 2.78e-114 DBJ BAQ06307 "phosphotyrosine protein phosphatase [Mycobacterium tuberculosis str. Kurono]" 87.27 144 100.00 100.00 6.39e-98 DBJ GAA45923 "phosphotyrosine protein phosphatase [Mycobacterium tuberculosis NCGM2209]" 87.27 144 100.00 100.00 6.39e-98 EMBL CAD97111 "PHOSPHOTYROSINE PROTEIN PHOSPHATASE PTPA (PROTEIN-TYROSINE-PHOSPHATASE) (PTPase) (LMW PHOSPHATASE) [Mycobacterium bovis AF2122/" 98.79 163 100.00 100.00 2.78e-114 EMBL CAL72239 "Phosphotyrosine protein phosphatase ptpA [Mycobacterium bovis BCG str. Pasteur 1173P2]" 98.79 163 100.00 100.00 2.78e-114 EMBL CCC27315 "phosphotyrosine protein phosphatase PTPA (protein-tyrosine-phosphatase) [Mycobacterium africanum GM041182]" 98.79 163 100.00 100.00 2.78e-114 EMBL CCC44588 "phosphotyrosine protein phosphatase PTPA (protein-tyrosine-phosphatase) (PTPase) (LMW phosphatase) [Mycobacterium canettii CIPT" 98.79 163 100.00 100.00 2.78e-114 EMBL CCC64828 "Phosphotyrosine protein phosphatase ptpA [Mycobacterium bovis BCG str. Moreau RDJ]" 98.79 163 100.00 100.00 2.78e-114 GB AAK46577 "protein tyrosine phosphatase [Mycobacterium tuberculosis CDC1551]" 98.79 163 100.00 100.00 2.78e-114 GB ABQ74015 "protein tyrosine phosphatase [Mycobacterium tuberculosis H37Ra]" 98.79 163 100.00 100.00 2.78e-114 GB ABR06594 "phosphotyrosine protein phosphatase ptpA [Mycobacterium tuberculosis F11]" 98.79 163 100.00 100.00 2.78e-114 GB ACT24805 "phosphotyrosine protein phosphatase ptpA [Mycobacterium tuberculosis KZN 1435]" 98.79 163 100.00 100.00 2.78e-114 GB AEB03885 "phosphotyrosine protein phosphatase ptpA [Mycobacterium tuberculosis KZN 4207]" 98.79 163 100.00 100.00 2.78e-114 REF NP_216750 "protein-tyrosine-phosphatase [Mycobacterium tuberculosis H37Rv]" 98.79 163 100.00 100.00 2.78e-114 REF NP_336763 "protein tyrosine phosphatase [Mycobacterium tuberculosis CDC1551]" 98.79 163 100.00 100.00 2.78e-114 REF NP_855907 "phosphotyrosine protein phosphatase PtpA [Mycobacterium bovis AF2122/97]" 98.79 163 100.00 100.00 2.78e-114 REF WP_003411510 "MULTISPECIES: protein-tyrosine-phosphatase [Mycobacterium tuberculosis complex]" 98.79 163 100.00 100.00 2.78e-114 REF WP_003899227 "protein-tyrosine-phosphatase [Mycobacterium tuberculosis]" 98.79 163 99.39 99.39 1.73e-113 SP P65717 "RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase; Short=PTPase [Mycobacterium bovis AF2122/97]" 98.79 163 100.00 100.00 2.78e-114 SP P9WIA0 "RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase; Short=PTPase [Mycobacterium tuberculosis CDC1551]" 98.79 163 100.00 100.00 2.78e-114 SP P9WIA1 "RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase; Short=PTPase [Mycobacterium tuberculosis H37Rv]" 98.79 163 100.00 100.00 2.78e-114 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MPtpA 'Mycobacterium tuberculosis' 1773 Eubacteria 'Not applicable' Mycobacterium tuberculosis 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 $MPtpA 'recombinant technology' 'E. coli' Escherichia coli . . 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 $MPtpA 0.5 mM '[U-13C; U-15N]' Hepes 25 mM . NaCL 150 mM . DTT 10 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CARA _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Rochus Keller, Prof. Kurt Wuthrich' . www.nmr.ch stop_ loop_ _Task Assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCACONH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label $sample_1 save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ loop_ _Experiment_label 1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'Low-Molecular-Weight Protein Tyrosin Phosphatase' _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 1 3 MET H H 8.424 0.05 1 2 1 3 MET C C 175.161 0.5 1 3 1 3 MET CA C 55.132 0.5 1 4 1 3 MET CB C 32.199 0.5 1 5 1 3 MET N N 122.095 0.5 1 6 2 4 SER H H 8.325 0.05 1 7 2 4 SER C C 173.139 0.5 1 8 2 4 SER CA C 57.959 0.5 1 9 2 4 SER CB C 63.506 0.5 1 10 2 4 SER N N 116.586 0.5 1 11 3 5 ASP H H 8.268 0.05 1 12 3 5 ASP CA C 52.373 0.5 1 13 3 5 ASP CB C 39.944 0.5 1 14 3 5 ASP N N 122.988 0.5 1 15 4 6 PRO C C 176.593 0.5 1 16 4 6 PRO CA C 62.339 0.5 1 17 4 6 PRO CB C 31.065 0.5 1 18 5 7 LEU H H 7.644 0.05 1 19 5 7 LEU C C 174.508 0.5 1 20 5 7 LEU CA C 54.718 0.5 1 21 5 7 LEU CB C 43.817 0.5 1 22 5 7 LEU N N 123.005 0.5 1 23 6 8 HIS H H 10.071 0.05 1 24 6 8 HIS C C 173.708 0.5 1 25 6 8 HIS CA C 52.304 0.5 1 26 6 8 HIS CB C 31.349 0.5 1 27 6 8 HIS N N 126.927 0.5 1 28 7 9 VAL H H 8.907 0.05 1 29 7 9 VAL C C 171.602 0.5 1 30 7 9 VAL CA C 60.305 0.5 1 31 7 9 VAL CB C 34.038 0.5 1 32 7 9 VAL N N 128.347 0.5 1 33 8 10 THR H H 7.95 0.05 1 34 8 10 THR C C 171.244 0.5 1 35 8 10 THR CA C 57.959 0.5 1 36 8 10 THR CB C 70.36 0.5 1 37 8 10 THR N N 121.205 0.5 1 38 9 11 PHE H H 8.142 0.05 1 39 9 11 PHE C C 174.087 0.5 1 40 9 11 PHE CA C 55.787 0.5 1 41 9 11 PHE CB C 42.211 0.5 1 42 9 11 PHE N N 125.01 0.5 1 43 10 12 VAL H H 8.683 0.05 1 44 10 12 VAL CA C 59.994 0.5 1 45 10 12 VAL CB C 34.985 0.5 1 46 10 12 VAL N N 120.641 0.5 1 47 11 13 CYS H H 7.83 0.05 1 48 11 13 CYS CA C 57.063 0.5 1 49 11 13 CYS CB C 29.723 0.5 1 50 11 13 CYS N N 122.867 0.5 1 51 12 14 THR C C 180.762 0.5 1 52 13 15 GLY H H 7.487 0.05 1 53 13 15 GLY C C 172.761 0.5 1 54 13 15 GLY CA C 43.732 0.5 1 55 13 15 GLY N N 117.618 0.5 1 56 14 16 ASN H H 9.239 0.05 1 57 14 16 ASN C C 178.278 0.5 1 58 14 16 ASN CA C 53.809 0.5 1 59 14 16 ASN CB C 39.874 0.5 1 60 14 16 ASN N N 119.457 0.5 1 61 15 17 ILE H H 7.837 0.05 1 62 15 17 ILE C C 178.299 0.5 1 63 15 17 ILE CA C 62.408 0.5 1 64 15 17 ILE CB C 38.756 0.5 1 65 15 17 ILE N N 118.642 0.5 1 66 16 18 CYS H H 8.154 0.05 1 67 16 18 CYS C C 178.636 0.5 1 68 16 18 CYS CA C 59.032 0.5 1 69 16 18 CYS CB C 28.305 0.5 1 70 16 18 CYS N N 121.009 0.5 1 71 17 19 ARG H H 7.863 0.05 1 72 17 19 ARG C C 178.068 0.5 1 73 17 19 ARG CA C 58.891 0.5 1 74 17 19 ARG CB C 28.231 0.5 1 75 17 19 ARG N N 121.215 0.5 1 76 18 20 SER H H 7.759 0.05 1 77 18 20 SER CA C 66.616 0.5 1 78 18 20 SER CB C 66.084 0.5 1 79 18 20 SER N N 119.664 0.5 1 80 19 21 PRO C C 177.625 0.5 1 81 19 21 PRO CA C 64.477 0.5 1 82 19 21 PRO CB C 27.356 0.5 1 83 20 22 MET H H 6.328 0.05 1 84 20 22 MET C C 175.161 0.5 1 85 20 22 MET CA C 59.684 0.5 1 86 20 22 MET CB C 32.577 0.5 1 87 20 22 MET N N 112.253 0.5 1 88 21 23 ALA H H 6.579 0.05 1 89 21 23 ALA C C 176.193 0.5 1 90 21 23 ALA CA C 54.442 0.5 1 91 21 23 ALA CB C 15.952 0.5 1 92 21 23 ALA N N 117.422 0.5 1 93 22 24 GLU H H 7.745 0.05 1 94 22 24 GLU C C 177.141 0.5 1 95 22 24 GLU CA C 59.029 0.5 1 96 22 24 GLU CB C 29.306 0.5 1 97 22 24 GLU N N 115.182 0.5 1 98 23 25 LYS H H 8.071 0.05 1 99 23 25 LYS C C 180.532 0.5 1 100 23 25 LYS CA C 57.132 0.5 1 101 23 25 LYS CB C 29.554 0.5 1 102 23 25 LYS N N 113.765 0.5 1 103 24 26 MET H H 7.575 0.05 1 104 24 26 MET C C 179.837 0.5 1 105 24 26 MET CA C 57.373 0.5 1 106 24 26 MET CB C 34.844 0.5 1 107 24 26 MET N N 114.92 0.5 1 108 25 27 PHE H H 8.555 0.05 1 109 25 27 PHE C C 177.225 0.5 1 110 25 27 PHE CA C 59.58 0.5 1 111 25 27 PHE CB C 38.792 0.5 1 112 25 27 PHE N N 118.75 0.5 1 113 26 28 ALA H H 8.793 0.05 1 114 26 28 ALA C C 179.984 0.5 1 115 26 28 ALA CA C 55.545 0.5 1 116 26 28 ALA CB C 17.771 0.5 1 117 26 28 ALA N N 117.477 0.5 1 118 27 29 GLN H H 7.66 0.05 1 119 27 29 GLN C C 177.057 0.5 1 120 27 29 GLN CA C 59.132 0.5 1 121 27 29 GLN CB C 27.948 0.5 1 122 27 29 GLN N N 117.227 0.5 1 123 28 30 GLN H H 8.184 0.05 1 124 28 30 GLN C C 179.963 0.5 1 125 28 30 GLN CA C 58.58 0.5 1 126 28 30 GLN CB C 26.346 0.5 1 127 28 30 GLN N N 117.18 0.5 1 128 29 31 LEU H H 8.527 0.05 1 129 29 31 LEU C C 178.552 0.5 1 130 29 31 LEU CA C 57.615 0.5 1 131 29 31 LEU CB C 41.317 0.5 1 132 29 31 LEU N N 118.986 0.5 1 133 30 32 ARG H H 7.746 0.05 1 134 30 32 ARG CA C 57.89 0.5 1 135 30 32 ARG CB C 28.137 0.5 1 136 30 32 ARG N N 117.237 0.5 1 137 31 33 HIS C C 176.299 0.5 1 138 31 33 HIS CA C 57.511 0.5 1 139 31 33 HIS CB C 30.498 0.5 1 140 32 34 ARG H H 7.474 0.05 1 141 32 34 ARG C C 175.245 0.5 1 142 32 34 ARG CA C 55.339 0.5 1 143 32 34 ARG N N 115.14 0.5 1 144 33 35 GLY H H 7.734 0.05 1 145 33 35 GLY C C 175.161 0.5 1 146 33 35 GLY CA C 45.706 0.5 1 147 33 35 GLY N N 106.44 0.5 1 148 34 36 LEU H H 7.96 0.05 1 149 34 36 LEU C C 177.036 0.5 1 150 34 36 LEU CA C 53.545 0.5 1 151 34 36 LEU CB C 42.495 0.5 1 152 34 36 LEU N N 119.674 0.5 1 153 35 37 GLY H H 8.849 0.05 1 154 35 37 GLY C C 173.371 0.5 1 155 35 37 GLY CA C 46.544 0.5 1 156 35 37 GLY N N 108.425 0.5 1 157 36 38 ASP H H 8.29 0.05 1 158 36 38 ASP C C 175.835 0.5 1 159 36 38 ASP CA C 53.787 0.5 1 160 36 38 ASP CB C 40.638 0.5 1 161 36 38 ASP N N 114.937 0.5 1 162 37 39 ALA H H 7.361 0.05 1 163 37 39 ALA C C 175.688 0.5 1 164 37 39 ALA CA C 52.442 0.5 1 165 37 39 ALA CB C 20.108 0.5 1 166 37 39 ALA N N 121.176 0.5 1 167 38 40 VAL H H 7.087 0.05 1 168 38 40 VAL C C 173.203 0.5 1 169 38 40 VAL CA C 59.511 0.5 1 170 38 40 VAL CB C 34.56 0.5 1 171 38 40 VAL N N 115.382 0.5 1 172 39 41 ARG H H 9.726 0.05 1 173 39 41 ARG C C 173.308 0.5 1 174 39 41 ARG CA C 54.166 0.5 1 175 39 41 ARG CB C 31.632 0.5 1 176 39 41 ARG N N 129.004 0.5 1 177 40 42 VAL H H 8.634 0.05 1 178 40 42 VAL C C 175.561 0.5 1 179 40 42 VAL CA C 60.098 0.5 1 180 40 42 VAL CB C 33.11 0.5 1 181 40 42 VAL N N 126.023 0.5 1 182 41 43 THR H H 8.858 0.05 1 183 41 43 THR C C 172.971 0.5 1 184 41 43 THR CA C 59.856 0.5 1 185 41 43 THR CB C 73.428 0.5 1 186 41 43 THR N N 116.993 0.5 1 187 42 44 SER H H 8.026 0.05 1 188 42 44 SER C C 171.181 0.5 1 189 42 44 SER CA C 57.615 0.5 1 190 42 44 SER CB C 65.688 0.5 1 191 42 44 SER N N 109.585 0.5 1 192 43 45 ALA H H 8.689 0.05 1 193 43 45 ALA C C 174.003 0.5 1 194 43 45 ALA CA C 50.579 0.5 1 195 43 45 ALA CB C 20.108 0.5 1 196 43 45 ALA N N 118.785 0.5 1 197 44 46 GLY H H 8.652 0.05 1 198 44 46 GLY C C 173.877 0.5 1 199 44 46 GLY CA C 41.986 0.5 1 200 44 46 GLY N N 103.657 0.5 1 201 45 47 THR H H 9.156 0.05 1 202 45 47 THR C C 176.425 0.5 1 203 45 47 THR CA C 64.27 0.5 1 204 45 47 THR CB C 67.243 0.5 1 205 45 47 THR N N 113.945 0.5 1 206 46 48 GLY H H 8.932 0.05 1 207 46 48 GLY C C 173.16 0.5 1 208 46 48 GLY CA C 43.295 0.5 1 209 46 48 GLY N N 110.338 0.5 1 210 47 49 ASN H H 7.689 0.05 1 211 47 49 ASN CA C 51.097 0.5 1 212 47 49 ASN CB C 38.171 0.5 1 213 47 49 ASN N N 113.32 0.5 1 214 48 50 TRP C C 177.036 0.5 1 215 48 50 TRP CA C 60.236 0.5 1 216 49 51 HIS H H 8.648 0.05 1 217 49 51 HIS C C 174.529 0.5 1 218 49 51 HIS CA C 53.304 0.5 1 219 49 51 HIS CB C 29.89 0.5 1 220 49 51 HIS N N 111.977 0.5 1 221 50 52 VAL H H 6.864 0.05 1 222 50 52 VAL C C 176.762 0.5 1 223 50 52 VAL CA C 65.271 0.5 1 224 50 52 VAL CB C 30.687 0.5 1 225 50 52 VAL N N 118.729 0.5 1 226 51 53 GLY H H 9.095 0.05 1 227 51 53 GLY C C 173.898 0.5 1 228 51 53 GLY CA C 44.339 0.5 1 229 51 53 GLY N N 115.122 0.5 1 230 52 54 SER H H 8.387 0.05 1 231 52 54 SER C C 173.287 0.5 1 232 52 54 SER CA C 58.822 0.5 1 233 52 54 SER CB C 64.265 0.5 1 234 52 54 SER N N 116.269 0.5 1 235 53 55 CYS H H 8.171 0.05 1 236 53 55 CYS C C 178.826 0.5 1 237 53 55 CYS CA C 57.132 0.5 1 238 53 55 CYS CB C 27.639 0.5 1 239 53 55 CYS N N 118.491 0.5 1 240 54 56 ALA H H 8.446 0.05 1 241 54 56 ALA C C 176.172 0.5 1 242 54 56 ALA CA C 52.062 0.5 1 243 54 56 ALA CB C 16.046 0.5 1 244 54 56 ALA N N 118.268 0.5 1 245 55 57 ASP H H 8.496 0.05 1 246 55 57 ASP C C 176.846 0.5 1 247 55 57 ASP CA C 54.407 0.5 1 248 55 57 ASP CB C 45.517 0.5 1 249 55 57 ASP N N 121.341 0.5 1 250 56 58 GLU H H 9.23 0.05 1 251 56 58 GLU C C 178.552 0.5 1 252 56 58 GLU CA C 59.132 0.5 1 253 56 58 GLU CB C 28.798 0.5 1 254 56 58 GLU N N 127.388 0.5 1 255 57 59 ARG H H 9.184 0.05 1 256 57 59 ARG C C 178.236 0.5 1 257 57 59 ARG CA C 57.615 0.5 1 258 57 59 ARG CB C 26.626 0.5 1 259 57 59 ARG N N 120.501 0.5 1 260 58 60 ALA H H 6.642 0.05 1 261 58 60 ALA C C 177.836 0.5 1 262 58 60 ALA CA C 54.2 0.5 1 263 58 60 ALA CB C 17.841 0.5 1 264 58 60 ALA N N 121.393 0.5 1 265 59 61 ALA H H 8.542 0.05 1 266 59 61 ALA C C 178.552 0.5 1 267 59 61 ALA CA C 54.732 0.5 1 268 59 61 ALA CB C 17.558 0.5 1 269 59 61 ALA N N 118.592 0.5 1 270 60 62 GLY H H 8.188 0.05 1 271 60 62 GLY C C 176.13 0.5 1 272 60 62 GLY CA C 46.745 0.5 1 273 60 62 GLY N N 103.8 0.5 1 274 61 63 VAL H H 7.293 0.05 1 275 61 63 VAL C C 177.352 0.5 1 276 61 63 VAL CA C 65.822 0.5 1 277 61 63 VAL CB C 31.254 0.5 1 278 61 63 VAL N N 122.549 0.5 1 279 62 64 LEU H H 8.092 0.05 1 280 62 64 LEU C C 179.142 0.5 1 281 62 64 LEU CA C 58.442 0.5 1 282 62 64 LEU CB C 40.823 0.5 1 283 62 64 LEU N N 120.002 0.5 1 284 63 65 ARG H H 8.734 0.05 1 285 63 65 ARG C C 180.342 0.5 1 286 63 65 ARG CA C 58.925 0.5 1 287 63 65 ARG CB C 29.648 0.5 1 288 63 65 ARG N N 119.126 0.5 1 289 64 66 ALA H H 7.907 0.05 1 290 64 66 ALA C C 178.32 0.5 1 291 64 66 ALA CA C 53.994 0.5 1 292 64 66 ALA CB C 17.369 0.5 1 293 64 66 ALA N N 122.272 0.5 1 294 65 67 HIS H H 7.399 0.05 1 295 65 67 HIS C C 173.224 0.5 1 296 65 67 HIS CA C 54.794 0.5 1 297 65 67 HIS CB C 29.459 0.5 1 298 65 67 HIS N N 112.303 0.5 1 299 66 68 GLY H H 7.847 0.05 1 300 66 68 GLY C C 173.518 0.5 1 301 66 68 GLY CA C 45.801 0.5 1 302 66 68 GLY N N 107.154 0.5 1 303 67 69 TYR H H 8.373 0.05 1 304 67 69 TYR CA C 56.58 0.5 1 305 67 69 TYR CB C 39.283 0.5 1 306 67 69 TYR N N 119.617 0.5 1 307 68 70 PRO C C 174.382 0.5 1 308 68 70 PRO CA C 62.204 0.5 1 309 68 70 PRO CB C 32.102 0.5 1 310 69 71 THR H H 7.847 0.05 1 311 69 71 THR C C 174.34 0.5 1 312 69 71 THR CA C 60.878 0.5 1 313 69 71 THR CB C 70.36 0.5 1 314 69 71 THR N N 100.304 0.5 1 315 70 72 ASP H H 7.931 0.05 1 316 70 72 ASP C C 175.814 0.5 1 317 70 72 ASP CA C 55.573 0.5 1 318 70 72 ASP CB C 40.318 0.5 1 319 70 72 ASP N N 122.622 0.5 1 320 71 73 HIS H H 7.991 0.05 1 321 71 73 HIS C C 172.171 0.5 1 322 71 73 HIS CA C 56.89 0.5 1 323 71 73 HIS CB C 34.655 0.5 1 324 71 73 HIS N N 121.414 0.5 1 325 72 74 ARG H H 7.239 0.05 1 326 72 74 ARG C C 174.087 0.5 1 327 72 74 ARG CA C 53.856 0.5 1 328 72 74 ARG CB C 31.632 0.5 1 329 72 74 ARG N N 125.45 0.5 1 330 73 75 ALA H H 9.077 0.05 1 331 73 75 ALA C C 177.31 0.5 1 332 73 75 ALA CA C 51.648 0.5 1 333 73 75 ALA CB C 18.219 0.5 1 334 73 75 ALA N N 127.743 0.5 1 335 74 76 ALA H H 9.391 0.05 1 336 74 76 ALA C C 175.372 0.5 1 337 74 76 ALA CA C 50.372 0.5 1 338 74 76 ALA CB C 22.942 0.5 1 339 74 76 ALA N N 125.891 0.5 1 340 75 77 GLN H H 8.814 0.05 1 341 75 77 GLN C C 174.024 0.5 1 342 75 77 GLN CA C 52.993 0.5 1 343 75 77 GLN CB C 29.356 0.5 1 344 75 77 GLN N N 123.101 0.5 1 345 76 78 VAL H H 8.535 0.05 1 346 76 78 VAL C C 174.972 0.5 1 347 76 78 VAL CA C 63.167 0.5 1 348 76 78 VAL CB C 32.01 0.5 1 349 76 78 VAL N N 125.226 0.5 1 350 77 79 GLY H H 10.944 0.05 1 351 77 79 GLY C C 173.94 0.5 1 352 77 79 GLY CA C 43.25 0.5 1 353 77 79 GLY N N 121.792 0.5 1 354 78 80 THR H H 8.545 0.05 1 355 78 80 THR C C 176.362 0.5 1 356 78 80 THR CA C 66.098 0.5 1 357 78 80 THR CB C 68.377 0.5 1 358 78 80 THR N N 114.92 0.5 1 359 79 81 GLU H H 9.09 0.05 1 360 79 81 GLU C C 177.604 0.5 1 361 79 81 GLU CA C 58.546 0.5 1 362 79 81 GLU CB C 28.359 0.5 1 363 79 81 GLU N N 118.986 0.5 1 364 80 82 HIS H H 7.007 0.05 1 365 80 82 HIS C C 176.804 0.5 1 366 80 82 HIS CA C 59.96 0.5 1 367 80 82 HIS CB C 30.215 0.5 1 368 80 82 HIS N N 118.115 0.5 1 369 81 83 LEU H H 7.862 0.05 1 370 81 83 LEU C C 176.172 0.5 1 371 81 83 LEU CA C 56.166 0.5 1 372 81 83 LEU CB C 40.164 0.5 1 373 81 83 LEU N N 113.677 0.5 1 374 82 84 ALA H H 6.934 0.05 1 375 82 84 ALA C C 176.32 0.5 1 376 82 84 ALA CA C 50.614 0.5 1 377 82 84 ALA CB C 18.502 0.5 1 378 82 84 ALA N N 118.687 0.5 1 379 83 85 ALA H H 7.28 0.05 1 380 83 85 ALA C C 174.424 0.5 1 381 83 85 ALA CA C 52.821 0.5 1 382 83 85 ALA CB C 16.613 0.5 1 383 83 85 ALA N N 122.321 0.5 1 384 84 86 ASP H H 8.415 0.05 1 385 84 86 ASP C C 174.74 0.5 1 386 84 86 ASP CA C 57.17 0.5 1 387 84 86 ASP CB C 42.202 0.5 1 388 84 86 ASP N N 118.347 0.5 1 389 85 87 LEU H H 7.258 0.05 1 390 85 87 LEU C C 171.918 0.5 1 391 85 87 LEU CA C 54.545 0.5 1 392 85 87 LEU CB C 44.573 0.5 1 393 85 87 LEU N N 114.832 0.5 1 394 86 88 LEU H H 8.772 0.05 1 395 86 88 LEU C C 173.097 0.5 1 396 86 88 LEU CA C 54.718 0.5 1 397 86 88 LEU CB C 41.55 0.5 1 398 86 88 LEU N N 127.861 0.5 1 399 87 89 VAL H H 8.999 0.05 1 400 87 89 VAL C C 174.74 0.5 1 401 87 89 VAL CA C 59.477 0.5 1 402 87 89 VAL CB C 30.215 0.5 1 403 87 89 VAL N N 122.23 0.5 1 404 88 90 ALA H H 8.577 0.05 1 405 88 90 ALA C C 176.383 0.5 1 406 88 90 ALA CA C 50.166 0.5 1 407 88 90 ALA CB C 20.108 0.5 1 408 88 90 ALA N N 129.516 0.5 1 409 89 91 LEU H H 8.51 0.05 1 410 89 91 LEU CA C 54.862 0.5 1 411 89 91 LEU N N 128.912 0.5 1 412 90 92 ASP C C 175.604 0.5 1 413 90 92 ASP CA C 52.671 0.5 1 414 90 92 ASP CB C 42.949 0.5 1 415 91 93 ARG H H 8.616 0.05 1 416 91 93 ARG C C 178.7 0.5 1 417 91 93 ARG CA C 58.479 0.5 1 418 91 93 ARG CB C 29.64 0.5 1 419 91 93 ARG N N 116.801 0.5 1 420 92 94 ASN H H 8.547 0.05 1 421 92 94 ASN C C 177.499 0.5 1 422 92 94 ASN CA C 55.614 0.5 1 423 92 94 ASN CB C 36.922 0.5 1 424 92 94 ASN N N 120.265 0.5 1 425 93 95 HIS H H 7.41 0.05 1 426 93 95 HIS C C 176.825 0.5 1 427 93 95 HIS CA C 59.132 0.5 1 428 93 95 HIS CB C 30.782 0.5 1 429 93 95 HIS N N 120.632 0.5 1 430 94 96 ALA H H 7.185 0.05 1 431 94 96 ALA C C 177.625 0.5 1 432 94 96 ALA CA C 54.994 0.5 1 433 94 96 ALA CB C 17.369 0.5 1 434 94 96 ALA N N 118.063 0.5 1 435 95 97 ARG H H 7.596 0.05 1 436 95 97 ARG C C 178.615 0.5 1 437 95 97 ARG CA C 59.029 0.5 1 438 95 97 ARG CB C 29.459 0.5 1 439 95 97 ARG N N 116.886 0.5 1 440 96 98 LEU H H 8.004 0.05 1 441 96 98 LEU CA C 57.408 0.5 1 442 96 98 LEU CB C 40.795 0.5 1 443 96 98 LEU N N 120.367 0.5 1 444 98 100 ARG C C 180.995 0.5 1 445 98 100 ARG CA C 58.035 0.5 1 446 98 100 ARG CB C 29.806 0.5 1 447 99 101 GLN H H 8.023 0.05 1 448 99 101 GLN C C 177.499 0.5 1 449 99 101 GLN CA C 58.132 0.5 1 450 99 101 GLN CB C 27.665 0.5 1 451 99 101 GLN N N 121.048 0.5 1 452 100 102 LEU H H 7.754 0.05 1 453 100 102 LEU C C 176.551 0.5 1 454 100 102 LEU CA C 54.959 0.5 1 455 100 102 LEU CB C 41.834 0.5 1 456 100 102 LEU N N 118.714 0.5 1 457 101 103 GLY H H 7.702 0.05 1 458 101 103 GLY C C 173.666 0.5 1 459 101 103 GLY CA C 44.478 0.5 1 460 101 103 GLY N N 105.501 0.5 1 461 102 104 VAL H H 7.494 0.05 1 462 102 104 VAL C C 174.719 0.5 1 463 102 104 VAL CA C 63.167 0.5 1 464 102 104 VAL CB C 30.876 0.5 1 465 102 104 VAL N N 122.074 0.5 1 466 103 105 GLU H H 9.215 0.05 1 467 103 105 GLU C C 176.067 0.5 1 468 103 105 GLU CA C 56.339 0.5 1 469 103 105 GLU CB C 28.231 0.5 1 470 103 105 GLU N N 128.767 0.5 1 471 104 106 ALA H H 8.488 0.05 1 472 104 106 ALA C C 179.331 0.5 1 473 104 106 ALA CA C 55.132 0.5 1 474 104 106 ALA CB C 17.558 0.5 1 475 104 106 ALA N N 124.098 0.5 1 476 105 107 ALA H H 8.266 0.05 1 477 105 107 ALA C C 178.026 0.5 1 478 105 107 ALA CA C 53.511 0.5 1 479 105 107 ALA CB C 18.53 0.5 1 480 105 107 ALA N N 114.763 0.5 1 481 106 108 ARG H H 7.739 0.05 1 482 106 108 ARG C C 172.297 0.5 1 483 106 108 ARG CA C 55.994 0.5 1 484 106 108 ARG CB C 31.726 0.5 1 485 106 108 ARG N N 114.852 0.5 1 486 107 109 VAL H H 7.279 0.05 1 487 107 109 VAL C C 174.909 0.5 1 488 107 109 VAL CA C 60.201 0.5 1 489 107 109 VAL CB C 32.954 0.5 1 490 107 109 VAL N N 117.929 0.5 1 491 108 110 ARG H H 8.387 0.05 1 492 108 110 ARG C C 175.14 0.5 1 493 108 110 ARG CA C 51.2 0.5 1 494 108 110 ARG CB C 34.371 0.5 1 495 108 110 ARG N N 123.864 0.5 1 496 109 111 MET H H 8.926 0.05 1 497 109 111 MET C C 179.1 0.5 1 498 109 111 MET CA C 53.438 0.5 1 499 109 111 MET CB C 30.121 0.5 1 500 109 111 MET N N 119.669 0.5 1 501 110 112 LEU H H 9.175 0.05 1 502 110 112 LEU C C 177.394 0.5 1 503 110 112 LEU CA C 59.003 0.5 1 504 110 112 LEU CB C 40.133 0.5 1 505 110 112 LEU N N 128.19 0.5 1 506 111 113 ARG H H 8.92 0.05 1 507 111 113 ARG C C 177.078 0.5 1 508 111 113 ARG CA C 59.442 0.5 1 509 111 113 ARG CB C 27.854 0.5 1 510 111 113 ARG N N 111.506 0.5 1 511 112 114 SER H H 7.651 0.05 1 512 112 114 SER C C 174.15 0.5 1 513 112 114 SER CA C 60.537 0.5 1 514 112 114 SER CB C 62.898 0.5 1 515 112 114 SER N N 114.579 0.5 1 516 113 115 PHE H H 7.583 0.05 1 517 113 115 PHE C C 174.656 0.5 1 518 113 115 PHE CA C 59.373 0.5 1 519 113 115 PHE CB C 39.189 0.5 1 520 113 115 PHE N N 118.962 0.5 1 521 114 116 ASP H H 7.403 0.05 1 522 114 116 ASP CA C 50.579 0.5 1 523 114 116 ASP CB C 41.928 0.5 1 524 114 116 ASP N N 120.909 0.5 1 525 115 117 PRO C C 177.331 0.5 1 526 115 117 PRO CA C 63.926 0.5 1 527 115 117 PRO CB C 31.529 0.5 1 528 116 118 ARG H H 8.594 0.05 1 529 116 118 ARG C C 176.783 0.5 1 530 116 118 ARG CA C 55.856 0.5 1 531 116 118 ARG CB C 29.347 0.5 1 532 116 118 ARG N N 117.61 0.5 1 533 117 119 SER H H 7.96 0.05 1 534 117 119 SER CA C 59.408 0.5 1 535 117 119 SER CB C 63.276 0.5 1 536 117 119 SER N N 115.864 0.5 1 537 118 120 GLY H H 8.203 0.05 1 538 118 120 GLY CA C 44.718 0.5 1 539 118 120 GLY N N 110.142 0.5 1 540 119 121 THR H H 8.248 0.05 1 541 119 121 THR C C 173.898 0.5 1 542 119 121 THR CA C 62.925 0.5 1 543 119 121 THR N N 113.042 0.5 1 544 120 122 HIS H H 7.945 0.05 1 545 120 122 HIS C C 174.298 0.5 1 546 120 122 HIS CA C 55.27 0.5 1 547 120 122 HIS CB C 30.215 0.5 1 548 120 122 HIS N N 119.086 0.5 1 549 121 123 ALA H H 8.005 0.05 1 550 121 123 ALA C C 175.519 0.5 1 551 121 123 ALA CA C 50.993 0.5 1 552 121 123 ALA N N 125.653 0.5 1 553 122 124 LEU H H 7.85 0.05 1 554 122 124 LEU C C 175.772 0.5 1 555 122 124 LEU CA C 53.856 0.5 1 556 122 124 LEU CB C 43.062 0.5 1 557 122 124 LEU N N 119.644 0.5 1 558 123 125 ASP H H 8.307 0.05 1 559 123 125 ASP C C 176.699 0.5 1 560 123 125 ASP CA C 54.787 0.5 1 561 123 125 ASP CB C 41.928 0.5 1 562 123 125 ASP N N 118.837 0.5 1 563 124 126 VAL H H 7.861 0.05 1 564 124 126 VAL C C 174.593 0.5 1 565 124 126 VAL CA C 61.886 0.5 1 566 124 126 VAL CB C 30.233 0.5 1 567 124 126 VAL N N 121.62 0.5 1 568 125 127 GLU H H 9.199 0.05 1 569 125 127 GLU C C 175.435 0.5 1 570 125 127 GLU CA C 56.477 0.5 1 571 125 127 GLU CB C 29.15 0.5 1 572 125 127 GLU N N 129.477 0.5 1 573 126 128 ASP H H 8.689 0.05 1 574 126 128 ASP CA C 51.166 0.5 1 575 126 128 ASP CB C 41.847 0.5 1 576 126 128 ASP N N 121.849 0.5 1 577 127 129 PRO C C 176.383 0.5 1 578 127 129 PRO CA C 66.581 0.5 1 579 127 129 PRO CB C 30.408 0.5 1 580 128 130 TYR H H 8.046 0.05 1 581 128 130 TYR C C 176.572 0.5 1 582 128 130 TYR CA C 62.201 0.5 1 583 128 130 TYR CB C 38.594 0.5 1 584 128 130 TYR N N 118.907 0.5 1 585 129 131 TYR H H 8.66 0.05 1 586 129 131 TYR C C 174.951 0.5 1 587 129 131 TYR CA C 57.925 0.5 1 588 129 131 TYR CB C 35.989 0.5 1 589 129 131 TYR N N 115.992 0.5 1 590 130 132 GLY H H 8.053 0.05 1 591 130 132 GLY C C 172.381 0.5 1 592 130 132 GLY CA C 43.574 0.5 1 593 130 132 GLY N N 110.646 0.5 1 594 131 133 ASP H H 9.305 0.05 1 595 131 133 ASP CA C 51.442 0.5 1 596 131 133 ASP CB C 42.967 0.5 1 597 131 133 ASP N N 121.411 0.5 1 598 132 134 HIS C C 177.331 0.5 1 599 132 134 HIS CA C 60.994 0.5 1 600 132 134 HIS CB C 29.566 0.5 1 601 133 135 SER H H 8.398 0.05 1 602 133 135 SER C C 176.72 0.5 1 603 133 135 SER CA C 61.667 0.5 1 604 133 135 SER CB C 66.672 0.5 1 605 133 135 SER N N 115.163 0.5 1 606 134 136 ASP H H 7.967 0.05 1 607 134 136 ASP C C 179.079 0.5 1 608 134 136 ASP CA C 57.442 0.5 1 609 134 136 ASP CB C 40.228 0.5 1 610 134 136 ASP N N 123.074 0.5 1 611 135 137 PHE H H 8.203 0.05 1 612 135 137 PHE C C 179.037 0.5 1 613 135 137 PHE CA C 57.511 0.5 1 614 135 137 PHE CB C 41.267 0.5 1 615 135 137 PHE N N 118.198 0.5 1 616 136 138 GLU H H 8.042 0.05 1 617 136 138 GLU C C 180.574 0.5 1 618 136 138 GLU CA C 59.339 0.5 1 619 136 138 GLU CB C 28.893 0.5 1 620 136 138 GLU N N 120.642 0.5 1 621 137 139 GLU H H 8.453 0.05 1 622 137 139 GLU CA C 57.511 0.5 1 623 137 139 GLU CB C 29.932 0.5 1 624 137 139 GLU N N 119.319 0.5 1 625 139 141 PHE C C 175.182 0.5 1 626 139 141 PHE CA C 62.236 0.5 1 627 139 141 PHE CB C 38.456 0.5 1 628 140 142 ALA H H 7.968 0.05 1 629 140 142 ALA C C 180.742 0.5 1 630 140 142 ALA CA C 54.58 0.5 1 631 140 142 ALA CB C 17.651 0.5 1 632 140 142 ALA N N 120.659 0.5 1 633 141 143 VAL H H 8.264 0.05 1 634 141 143 VAL C C 177.752 0.5 1 635 141 143 VAL CA C 65.236 0.5 1 636 141 143 VAL CB C 30.844 0.5 1 637 141 143 VAL N N 118.45 0.5 1 638 142 144 ILE H H 8.168 0.05 1 639 142 144 ILE C C 177.541 0.5 1 640 142 144 ILE CA C 65.629 0.5 1 641 142 144 ILE CB C 36.733 0.5 1 642 142 144 ILE N N 121.11 0.5 1 643 143 145 GLU H H 8.61 0.05 1 644 143 145 GLU C C 178.721 0.5 1 645 143 145 GLU CA C 59.27 0.5 1 646 143 145 GLU CB C 29.082 0.5 1 647 143 145 GLU N N 119.231 0.5 1 648 144 146 SER H H 7.636 0.05 1 649 144 146 SER C C 174.129 0.5 1 650 144 146 SER CA C 60.339 0.5 1 651 144 146 SER CB C 63.221 0.5 1 652 144 146 SER N N 110.65 0.5 1 653 145 147 ALA H H 7.476 0.05 1 654 145 147 ALA C C 176.278 0.5 1 655 145 147 ALA CA C 52.89 0.5 1 656 145 147 ALA CB C 20.202 0.5 1 657 145 147 ALA N N 122.815 0.5 1 658 146 148 LEU H H 7.386 0.05 1 659 146 148 LEU CA C 58.546 0.5 1 660 146 148 LEU CB C 38.835 0.5 1 661 146 148 LEU N N 113.765 0.5 1 662 147 149 PRO C C 178.531 0.5 1 663 147 149 PRO CA C 67.409 0.5 1 664 147 149 PRO CB C 30.228 0.5 1 665 148 150 GLY H H 7.929 0.05 1 666 148 150 GLY C C 176.404 0.5 1 667 148 150 GLY CA C 46.745 0.5 1 668 148 150 GLY N N 102.149 0.5 1 669 149 151 LEU H H 7.616 0.05 1 670 149 151 LEU C C 178.847 0.5 1 671 149 151 LEU CA C 56.787 0.5 1 672 149 151 LEU CB C 40.606 0.5 1 673 149 151 LEU N N 127.887 0.5 1 674 150 152 HIS H H 8.413 0.05 1 675 150 152 HIS C C 177.457 0.5 1 676 150 152 HIS CA C 61.925 0.5 1 677 150 152 HIS CB C 29.837 0.5 1 678 150 152 HIS N N 120.422 0.5 1 679 151 153 ASP H H 7.795 0.05 1 680 151 153 ASP C C 177.646 0.5 1 681 151 153 ASP CA C 57.304 0.5 1 682 151 153 ASP CB C 39.472 0.5 1 683 151 153 ASP N N 117.815 0.5 1 684 152 154 TRP H H 7.907 0.05 1 685 152 154 TRP C C 178.236 0.5 1 686 152 154 TRP CA C 62.183 0.5 1 687 152 154 TRP CB C 29.20 0.5 1 688 152 154 TRP N N 122.548 0.5 1 689 153 155 VAL H H 8.587 0.05 1 690 153 155 VAL C C 176.488 0.5 1 691 153 155 VAL CA C 66.512 0.5 1 692 153 155 VAL CB C 29.069 0.5 1 693 153 155 VAL N N 119.24 0.5 1 694 154 156 ASP H H 8.534 0.05 1 695 154 156 ASP C C 179.015 0.5 1 696 154 156 ASP CA C 57.028 0.5 1 697 154 156 ASP CB C 39.378 0.5 1 698 154 156 ASP N N 120.124 0.5 1 699 155 157 GLU H H 7.861 0.05 1 700 155 157 GLU C C 178.026 0.5 1 701 155 157 GLU CA C 58.684 0.5 1 702 155 157 GLU CB C 28.609 0.5 1 703 155 157 GLU N N 119.862 0.5 1 704 156 158 ARG H H 7.641 0.05 1 705 156 158 ARG C C 178.952 0.5 1 706 156 158 ARG CA C 56.477 0.5 1 707 156 158 ARG CB C 28.326 0.5 1 708 156 158 ARG N N 118.951 0.5 1 709 157 159 LEU H H 8.51 0.05 1 710 157 159 LEU C C 178.005 0.5 1 711 157 159 LEU CA C 56.273 0.5 1 712 157 159 LEU CB C 41.073 0.5 1 713 157 159 LEU N N 118.555 0.5 1 714 158 160 ALA H H 7.467 0.05 1 715 158 160 ALA C C 177.689 0.5 1 716 158 160 ALA CA C 52.752 0.5 1 717 158 160 ALA CB C 17.652 0.5 1 718 158 160 ALA N N 120.336 0.5 1 719 159 161 ARG H H 7.598 0.05 1 720 159 161 ARG C C 175.625 0.5 1 721 159 161 ARG CA C 56.408 0.5 1 722 159 161 ARG CB C 29.743 0.5 1 723 159 161 ARG N N 117.599 0.5 1 724 160 162 ASN H H 8.083 0.05 1 725 160 162 ASN C C 174.635 0.5 1 726 160 162 ASN CA C 52.718 0.5 1 727 160 162 ASN CB C 38.456 0.5 1 728 160 162 ASN N N 118.235 0.5 1 729 161 163 GLY H H 7.979 0.05 1 730 161 163 GLY CA C 44.187 0.5 1 731 161 163 GLY N N 108.552 0.5 1 732 162 164 PRO C C 175.814 0.5 1 733 162 164 PRO CA C 62.908 0.5 1 734 162 164 PRO CB C 31.494 0.5 1 735 163 165 SER H H 8.01 0.05 1 736 163 165 SER CA C 59.615 0.5 1 737 163 165 SER CB C 64.504 0.5 1 738 163 165 SER N N 121.598 0.5 1 stop_ save_