data_16341 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The inactive form of the retroviral protease of the murine intracisternal particle, inMIA-14 PR ; _BMRB_accession_number 16341 _BMRB_flat_file_name bmr16341.str _Entry_type original _Submission_date 2009-06-09 _Accession_date 2009-06-09 _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 Motackova Veronika . . 2 Kubickova Monika . . 3 Kozisek Milan . . 4 Grantz-Saskova Klara . . 5 Svec Martin . . 6 Zidek Lukas . . 7 Sklenar Vladimir . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 135 "13C chemical shifts" 416 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-25 update BMRB 'complete entry citation' 2009-11-16 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone (1)H, (13)C, and (15)N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19856131 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Motakova Veronika . . 2 Kubikova Monika . . 3 Kozisek Milan . . 4 Sakova Klara . . 5 Svec Martin . . 6 Zidek Luka . . 7 Sklena Vladimir . . stop_ _Journal_abbreviation 'Biomol NMR Assign' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 3 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 261 _Page_last 264 _Year 2009 _Details . loop_ _Keyword Assignment 'C-terminal domain' Homodimer 'inMIA-14 PR' 'Murine intracisternal A-type particles' 'Retroviral protease' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name inMIA14-PR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label inMIA14-PR $inMIA14-PR stop_ _System_molecular_weight 34 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_inMIA14-PR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common inMIA14-PR _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; LVVSLNDRPKLRLKINGKEF EGILDTGADKSIISTHWWPK AWPTTESSHSLQGLGYQSCP TISSVALTWESSEGQQGKFI PYVLPLPVNLWGRDIMQHLG LILSNENAPSGGYSTKAKNI MAKMGYKEGKGLGHQEQGRI EPISPNGNQDRQGLGF ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 VAL 3 VAL 4 SER 5 LEU 6 ASN 7 ASP 8 ARG 9 PRO 10 LYS 11 LEU 12 ARG 13 LEU 14 LYS 15 ILE 16 ASN 17 GLY 18 LYS 19 GLU 20 PHE 21 GLU 22 GLY 23 ILE 24 LEU 25 ASP 26 THR 27 GLY 28 ALA 29 ASP 30 LYS 31 SER 32 ILE 33 ILE 34 SER 35 THR 36 HIS 37 TRP 38 TRP 39 PRO 40 LYS 41 ALA 42 TRP 43 PRO 44 THR 45 THR 46 GLU 47 SER 48 SER 49 HIS 50 SER 51 LEU 52 GLN 53 GLY 54 LEU 55 GLY 56 TYR 57 GLN 58 SER 59 CYS 60 PRO 61 THR 62 ILE 63 SER 64 SER 65 VAL 66 ALA 67 LEU 68 THR 69 TRP 70 GLU 71 SER 72 SER 73 GLU 74 GLY 75 GLN 76 GLN 77 GLY 78 LYS 79 PHE 80 ILE 81 PRO 82 TYR 83 VAL 84 LEU 85 PRO 86 LEU 87 PRO 88 VAL 89 ASN 90 LEU 91 TRP 92 GLY 93 ARG 94 ASP 95 ILE 96 MET 97 GLN 98 HIS 99 LEU 100 GLY 101 LEU 102 ILE 103 LEU 104 SER 105 ASN 106 GLU 107 ASN 108 ALA 109 PRO 110 SER 111 GLY 112 GLY 113 TYR 114 SER 115 THR 116 LYS 117 ALA 118 LYS 119 ASN 120 ILE 121 MET 122 ALA 123 LYS 124 MET 125 GLY 126 TYR 127 LYS 128 GLU 129 GLY 130 LYS 131 GLY 132 LEU 133 GLY 134 HIS 135 GLN 136 GLU 137 GLN 138 GLY 139 ARG 140 ILE 141 GLU 142 PRO 143 ILE 144 SER 145 PRO 146 ASN 147 GLY 148 ASN 149 GLN 150 ASP 151 ARG 152 GLN 153 GLY 154 LEU 155 GLY 156 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 DBJ BAC79171 "gag [Mus musculus]" 100.00 259 99.36 99.36 2.32e-107 EMBL CRH48730 "G-patch domain [Chlamydia trachomatis]" 57.69 91 98.89 100.00 1.52e-56 EMBL CRH55731 "Retroviral aspartyl protease [Chlamydia trachomatis]" 100.00 258 99.36 99.36 1.89e-107 EMBL CRH56783 "dUTP diphosphatase [Chlamydia trachomatis]" 100.00 269 99.36 99.36 1.74e-107 EMBL CRH57961 "Retroviral aspartyl protease [Chlamydia trachomatis]" 100.00 167 98.72 99.36 5.74e-108 GB AAC12789 "gag protein [Mus musculus domesticus]" 100.00 827 99.36 99.36 2.15e-102 GB AAC52922 "Gag [Mus musculus]" 100.00 827 99.36 99.36 1.17e-102 REF WP_057247684 "hypothetical protein [Chlamydia trachomatis]" 100.00 258 99.36 99.36 1.89e-107 REF WP_057256782 "hypothetical protein [Chlamydia trachomatis]" 100.00 269 99.36 99.36 1.74e-107 SP P11365 "RecName: Full=Retrovirus-related Gag polyprotein; Contains: RecName: Full=Protease; Flags: Precursor [Mouse intracisternal A-pa" 100.00 827 99.36 99.36 2.15e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $inMIA14-PR 'Murine endogenous retrovirus' 35275 Viruses . Betaretrovirus 'Murine endogenous retrovirus' NcoI 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 $inMIA14-PR 'recombinant technology' . Escherichia coli . pET22 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 $inMIA14-PR 0.3 mM '[U-100% 13C; U-100% 15N; U-75% 2H]' 'sodium chloride' 50 mM 'natural abundance' 'sodium azide' 50 uM 'natural abundance' 'phosphate buffer' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _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' 20 . mM pH 7.4 . pH pressure 1 . atm temperature 296 . 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 carbon' ppm 0 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal indirect . . . 1.0 'liquid anhydrous ammonia' N 15 nitrogen ppm 0 na direct . . . 1.0 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_ _Software_label $NMRPipe $NMRDraw $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HNCA' '3D HN(CO)CA' '3D HNCO' '3D HN(CO)CACB' 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 inMIA14-PR _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 3 3 VAL CA C 62.212 0.024 1 2 3 3 VAL CB C 32.632 0.024 1 3 4 4 SER H H 8.390 0.004 1 4 4 4 SER C C 174.928 0.024 1 5 4 4 SER CA C 58.097 0.024 1 6 4 4 SER CB C 63.708 0.024 1 7 4 4 SER N N 119.083 0.038 1 8 5 5 LEU H H 8.378 0.004 1 9 5 5 LEU C C 177.584 0.024 1 10 5 5 LEU CA C 55.773 0.024 1 11 5 5 LEU CB C 41.786 0.024 1 12 5 5 LEU N N 123.746 0.038 1 13 6 6 ASN H H 8.197 0.004 1 14 6 6 ASN C C 175.003 0.024 1 15 6 6 ASN CA C 54.234 0.024 1 16 6 6 ASN CB C 38.685 0.024 1 17 6 6 ASN N N 116.383 0.038 1 18 7 7 ASP H H 8.146 0.004 1 19 7 7 ASP C C 175.744 0.024 1 20 7 7 ASP CA C 54.272 0.024 1 21 7 7 ASP CB C 40.793 0.024 1 22 7 7 ASP N N 118.587 0.038 1 23 8 8 ARG H H 7.691 0.004 1 24 8 8 ARG CA C 53.811 0.024 1 25 8 8 ARG CB C 29.883 0.024 1 26 8 8 ARG N N 120.195 0.038 1 27 9 9 PRO C C 175.728 0.024 1 28 9 9 PRO CA C 63.261 0.024 1 29 9 9 PRO CB C 31.969 0.024 1 30 10 10 LYS H H 8.270 0.004 1 31 10 10 LYS C C 176.155 0.024 1 32 10 10 LYS CA C 55.149 0.024 1 33 10 10 LYS CB C 35.357 0.024 1 34 10 10 LYS N N 119.569 0.038 1 35 11 11 LEU H H 9.015 0.004 1 36 11 11 LEU C C 176.382 0.024 1 37 11 11 LEU CA C 54.575 0.024 1 38 11 11 LEU CB C 46.272 0.024 1 39 11 11 LEU N N 121.699 0.038 1 40 12 12 ARG H H 9.136 0.004 1 41 12 12 ARG C C 174.825 0.024 1 42 12 12 ARG CA C 55.511 0.024 1 43 12 12 ARG CB C 30.908 0.024 1 44 12 12 ARG N N 130.459 0.038 1 45 13 13 LEU H H 8.945 0.004 1 46 13 13 LEU C C 175.538 0.024 1 47 13 13 LEU CA C 53.420 0.024 1 48 13 13 LEU CB C 46.941 0.024 1 49 13 13 LEU N N 123.515 0.038 1 50 14 14 LYS H H 8.500 0.004 1 51 14 14 LYS C C 176.526 0.024 1 52 14 14 LYS CA C 55.572 0.024 1 53 14 14 LYS CB C 33.807 0.024 1 54 14 14 LYS N N 120.075 0.038 1 55 15 15 ILE H H 9.955 0.004 1 56 15 15 ILE C C 175.411 0.024 1 57 15 15 ILE CA C 59.376 0.024 1 58 15 15 ILE CB C 38.360 0.024 1 59 15 15 ILE N N 127.403 0.038 1 60 16 16 ASN H H 9.371 0.004 1 61 16 16 ASN C C 175.675 0.024 1 62 16 16 ASN CA C 53.967 0.024 1 63 16 16 ASN CB C 37.450 0.024 1 64 16 16 ASN N N 127.888 0.038 1 65 17 17 GLY H H 8.723 0.004 1 66 17 17 GLY C C 173.608 0.024 1 67 17 17 GLY CA C 45.622 0.024 1 68 17 17 GLY N N 101.228 0.038 1 69 18 18 LYS H H 8.401 0.004 1 70 18 18 LYS C C 175.340 0.024 1 71 18 18 LYS CA C 54.944 0.024 1 72 18 18 LYS CB C 34.743 0.024 1 73 18 18 LYS N N 123.101 0.038 1 74 19 19 GLU H H 8.772 0.004 1 75 19 19 GLU C C 176.365 0.024 1 76 19 19 GLU CA C 57.570 0.024 1 77 19 19 GLU CB C 30.617 0.024 1 78 19 19 GLU N N 124.261 0.038 1 79 20 20 PHE H H 9.419 0.004 1 80 20 20 PHE CA C 57.111 0.024 1 81 20 20 PHE CB C 44.443 0.024 1 82 20 20 PHE N N 122.719 0.038 1 83 21 21 GLU C C 175.772 0.024 1 84 21 21 GLU CA C 55.101 0.024 1 85 21 21 GLU CB C 31.995 0.024 1 86 22 22 GLY H H 8.319 0.004 1 87 22 22 GLY C C 170.769 0.024 1 88 22 22 GLY CA C 44.373 0.024 1 89 22 22 GLY N N 113.554 0.038 1 90 23 23 ILE H H 7.987 0.004 1 91 23 23 ILE C C 176.031 0.024 1 92 23 23 ILE CA C 59.228 0.024 1 93 23 23 ILE CB C 39.699 0.024 1 94 23 23 ILE N N 116.674 0.038 1 95 24 24 LEU H H 8.422 0.004 1 96 24 24 LEU CA C 55.777 0.024 1 97 24 24 LEU CB C 41.212 0.024 1 98 24 24 LEU N N 125.157 0.038 1 99 25 25 ASP C C 174.179 0.024 1 100 26 26 THR H H 8.395 0.004 1 101 26 26 THR C C 175.417 0.024 1 102 26 26 THR CA C 63.932 0.024 1 103 26 26 THR CB C 68.770 0.024 1 104 26 26 THR N N 116.322 0.038 1 105 27 27 GLY H H 8.425 0.004 1 106 27 27 GLY C C 173.295 0.024 1 107 27 27 GLY CA C 45.129 0.024 1 108 27 27 GLY N N 108.152 0.038 1 109 28 28 ALA H H 7.372 0.004 1 110 28 28 ALA C C 176.336 0.024 1 111 28 28 ALA CA C 50.757 0.024 1 112 28 28 ALA CB C 19.280 0.024 1 113 28 28 ALA N N 123.912 0.038 1 114 29 29 ASP H H 8.800 0.004 1 115 29 29 ASP C C 175.669 0.024 1 116 29 29 ASP CA C 57.360 0.024 1 117 29 29 ASP CB C 41.123 0.024 1 118 29 29 ASP N N 123.650 0.038 1 119 30 30 LYS H H 7.689 0.004 1 120 30 30 LYS C C 175.610 0.024 1 121 30 30 LYS CA C 53.897 0.024 1 122 30 30 LYS CB C 34.428 0.024 1 123 30 30 LYS N N 117.180 0.038 1 124 31 31 SER H H 9.305 0.004 1 125 31 31 SER C C 171.636 0.024 1 126 31 31 SER CA C 60.882 0.024 1 127 31 31 SER CB C 65.482 0.024 1 128 31 31 SER N N 120.072 0.038 1 129 32 32 ILE H H 9.329 0.004 1 130 32 32 ILE C C 175.560 0.024 1 131 32 32 ILE CA C 60.254 0.024 1 132 32 32 ILE CB C 42.808 0.024 1 133 32 32 ILE N N 119.370 0.038 1 134 33 33 ILE H H 9.092 0.004 1 135 33 33 ILE C C 174.822 0.024 1 136 33 33 ILE CA C 59.086 0.024 1 137 33 33 ILE CB C 38.283 0.024 1 138 33 33 ILE N N 125.317 0.038 1 139 34 34 SER H H 9.299 0.004 1 140 34 34 SER C C 178.076 0.024 1 141 34 34 SER CA C 56.957 0.024 1 142 34 34 SER CB C 63.381 0.024 1 143 34 34 SER N N 118.923 0.038 1 144 35 35 THR H H 8.048 0.004 1 145 35 35 THR C C 176.202 0.024 1 146 35 35 THR CA C 65.318 0.024 1 147 35 35 THR CB C 68.052 0.024 1 148 35 35 THR N N 121.362 0.038 1 149 36 36 HIS H H 8.358 0.004 1 150 36 36 HIS C C 175.861 0.024 1 151 36 36 HIS CA C 57.900 0.024 1 152 36 36 HIS CB C 28.442 0.024 1 153 36 36 HIS N N 118.727 0.038 1 154 37 37 TRP H H 7.598 0.004 1 155 37 37 TRP C C 175.265 0.024 1 156 37 37 TRP CA C 57.770 0.024 1 157 37 37 TRP CB C 31.169 0.024 1 158 37 37 TRP N N 115.349 0.038 1 159 38 38 TRP H H 7.845 0.004 1 160 38 38 TRP CA C 55.258 0.024 1 161 38 38 TRP CB C 30.031 0.024 1 162 38 38 TRP N N 123.276 0.038 1 163 39 39 PRO C C 173.784 0.024 1 164 39 39 PRO CA C 62.431 0.024 1 165 39 39 PRO CB C 30.338 0.024 1 166 40 40 LYS H H 8.140 0.004 1 167 40 40 LYS C C 177.751 0.024 1 168 40 40 LYS CA C 58.735 0.024 1 169 40 40 LYS CB C 32.352 0.024 1 170 40 40 LYS N N 123.532 0.038 1 171 41 41 ALA H H 8.018 0.004 1 172 41 41 ALA C C 178.453 0.024 1 173 41 41 ALA CA C 52.786 0.024 1 174 41 41 ALA CB C 18.701 0.024 1 175 41 41 ALA N N 116.912 0.038 1 176 42 42 TRP H H 8.053 0.004 1 177 42 42 TRP CA C 53.238 0.024 1 178 42 42 TRP CB C 28.252 0.024 1 179 42 42 TRP N N 122.977 0.038 1 180 43 43 PRO C C 177.748 0.024 1 181 43 43 PRO CA C 63.710 0.024 1 182 43 43 PRO CB C 31.924 0.024 1 183 44 44 THR H H 8.339 0.004 1 184 44 44 THR C C 173.857 0.024 1 185 44 44 THR CA C 59.893 0.024 1 186 44 44 THR CB C 72.838 0.024 1 187 44 44 THR N N 111.495 0.038 1 188 45 45 THR H H 8.966 0.004 1 189 45 45 THR C C 172.932 0.024 1 190 45 45 THR CA C 60.376 0.024 1 191 45 45 THR CB C 70.716 0.024 1 192 45 45 THR N N 114.022 0.038 1 193 46 46 GLU H H 8.287 0.004 1 194 46 46 GLU C C 176.565 0.024 1 195 46 46 GLU CA C 56.720 0.024 1 196 46 46 GLU CB C 30.231 0.024 1 197 46 46 GLU N N 123.625 0.038 1 198 47 47 SER H H 8.288 0.004 1 199 47 47 SER CA C 58.125 0.024 1 200 47 47 SER CB C 64.260 0.024 1 201 47 47 SER N N 117.676 0.038 1 202 49 49 HIS C C 175.518 0.024 1 203 49 49 HIS CA C 55.927 0.024 1 204 49 49 HIS CB C 29.212 0.024 1 205 50 50 SER H H 7.843 0.004 1 206 50 50 SER C C 174.360 0.024 1 207 50 50 SER CA C 58.242 0.024 1 208 50 50 SER CB C 64.068 0.024 1 209 50 50 SER N N 115.624 0.038 1 210 51 51 LEU H H 8.460 0.004 1 211 51 51 LEU C C 175.603 0.024 1 212 51 51 LEU CA C 53.552 0.024 1 213 51 51 LEU CB C 38.760 0.024 1 214 51 51 LEU N N 120.604 0.038 1 215 52 52 GLN H H 8.408 0.004 1 216 52 52 GLN C C 176.501 0.024 1 217 52 52 GLN CA C 56.282 0.024 1 218 52 52 GLN CB C 29.094 0.024 1 219 52 52 GLN N N 120.484 0.038 1 220 53 53 GLY H H 8.453 0.004 1 221 53 53 GLY C C 174.128 0.024 1 222 53 53 GLY CA C 45.265 0.024 1 223 53 53 GLY N N 109.991 0.038 1 224 54 54 LEU H H 8.109 0.004 1 225 54 54 LEU C C 177.117 0.024 1 226 54 54 LEU CA C 55.354 0.024 1 227 54 54 LEU CB C 41.962 0.024 1 228 54 54 LEU N N 121.164 0.038 1 229 55 55 GLY H H 8.381 0.004 1 230 55 55 GLY C C 173.916 0.024 1 231 55 55 GLY CA C 45.314 0.024 1 232 55 55 GLY N N 109.468 0.038 1 233 56 56 TYR H H 7.702 0.004 1 234 56 56 TYR CA C 57.843 0.024 1 235 56 56 TYR CB C 38.838 0.024 1 236 56 56 TYR N N 119.441 0.038 1 237 57 57 GLN C C 174.399 0.024 1 238 57 57 GLN CA C 55.545 0.024 1 239 57 57 GLN CB C 30.247 0.024 1 240 58 58 SER H H 8.322 0.004 1 241 58 58 SER C C 173.711 0.024 1 242 58 58 SER CA C 58.388 0.024 1 243 58 58 SER CB C 63.698 0.024 1 244 58 58 SER N N 116.393 0.038 1 245 59 59 CYS H H 8.542 0.004 1 246 59 59 CYS CA C 53.787 0.024 1 247 59 59 CYS CB C 40.864 0.024 1 248 59 59 CYS N N 121.379 0.038 1 249 60 60 PRO C C 176.021 0.024 1 250 60 60 PRO CA C 63.168 0.024 1 251 60 60 PRO CB C 32.007 0.024 1 252 61 61 THR H H 7.507 0.004 1 253 61 61 THR C C 172.923 0.024 1 254 61 61 THR CA C 62.766 0.024 1 255 61 61 THR CB C 70.002 0.024 1 256 61 61 THR N N 116.116 0.038 1 257 62 62 ILE H H 8.842 0.004 1 258 62 62 ILE C C 174.092 0.024 1 259 62 62 ILE CA C 59.165 0.024 1 260 62 62 ILE CB C 43.417 0.024 1 261 62 62 ILE N N 121.890 0.038 1 262 63 63 SER H H 7.659 0.004 1 263 63 63 SER C C 175.703 0.024 1 264 63 63 SER CA C 59.326 0.024 1 265 63 63 SER CB C 63.856 0.024 1 266 63 63 SER N N 115.380 0.038 1 267 64 64 SER H H 8.378 0.004 1 268 64 64 SER C C 173.408 0.024 1 269 64 64 SER CA C 61.469 0.024 1 270 64 64 SER CB C 63.326 0.024 1 271 64 64 SER N N 122.318 0.038 1 272 65 65 VAL H H 7.182 0.004 1 273 65 65 VAL C C 174.990 0.024 1 274 65 65 VAL CA C 58.548 0.024 1 275 65 65 VAL CB C 35.613 0.024 1 276 65 65 VAL N N 110.329 0.038 1 277 66 66 ALA H H 8.521 0.004 1 278 66 66 ALA C C 176.798 0.024 1 279 66 66 ALA CA C 52.454 0.024 1 280 66 66 ALA CB C 18.032 0.024 1 281 66 66 ALA N N 124.330 0.038 1 282 67 67 LEU H H 9.067 0.004 1 283 67 67 LEU C C 176.542 0.024 1 284 67 67 LEU CA C 52.742 0.024 1 285 67 67 LEU CB C 43.659 0.024 1 286 67 67 LEU N N 124.095 0.038 1 287 68 68 THR H H 8.569 0.004 1 288 68 68 THR C C 174.003 0.024 1 289 68 68 THR CA C 61.941 0.024 1 290 68 68 THR CB C 70.089 0.024 1 291 68 68 THR N N 117.247 0.038 1 292 69 69 TRP H H 8.497 0.004 1 293 69 69 TRP C C 174.472 0.024 1 294 69 69 TRP CA C 53.728 0.024 1 295 69 69 TRP CB C 32.964 0.024 1 296 69 69 TRP N N 124.307 0.038 1 297 70 70 GLU H H 8.758 0.004 1 298 70 70 GLU C C 176.509 0.024 1 299 70 70 GLU CA C 55.019 0.024 1 300 70 70 GLU CB C 33.851 0.024 1 301 70 70 GLU N N 117.732 0.038 1 302 71 71 SER H H 9.356 0.004 1 303 71 71 SER C C 176.678 0.024 1 304 71 71 SER CA C 56.316 0.024 1 305 71 71 SER CB C 66.332 0.024 1 306 71 71 SER N N 121.571 0.038 1 307 72 72 SER H H 9.626 0.004 1 308 72 72 SER C C 175.384 0.024 1 309 72 72 SER CA C 61.325 0.024 1 310 72 72 SER CB C 62.856 0.024 1 311 72 72 SER N N 119.121 0.038 1 312 73 73 GLU H H 8.042 0.004 1 313 73 73 GLU C C 176.830 0.024 1 314 73 73 GLU CA C 56.665 0.024 1 315 73 73 GLU CB C 28.818 0.024 1 316 73 73 GLU N N 118.106 0.038 1 317 74 74 GLY H H 7.907 0.004 1 318 74 74 GLY C C 175.167 0.024 1 319 74 74 GLY CA C 45.449 0.024 1 320 74 74 GLY N N 106.908 0.038 1 321 75 75 GLN H H 7.390 0.004 1 322 75 75 GLN C C 174.003 0.024 1 323 75 75 GLN CA C 56.144 0.024 1 324 75 75 GLN CB C 28.333 0.024 1 325 75 75 GLN N N 119.645 0.038 1 326 76 76 GLN H H 7.955 0.004 1 327 76 76 GLN C C 174.149 0.024 1 328 76 76 GLN CA C 53.504 0.024 1 329 76 76 GLN CB C 32.749 0.024 1 330 76 76 GLN N N 118.833 0.038 1 331 77 77 GLY H H 6.504 0.004 1 332 77 77 GLY C C 170.773 0.024 1 333 77 77 GLY CA C 44.712 0.024 1 334 77 77 GLY N N 106.764 0.038 1 335 78 78 LYS H H 8.138 0.004 1 336 78 78 LYS C C 176.895 0.024 1 337 78 78 LYS CA C 54.043 0.024 1 338 78 78 LYS CB C 35.897 0.024 1 339 78 78 LYS N N 116.736 0.038 1 340 79 79 PHE H H 9.609 0.004 1 341 79 79 PHE C C 172.151 0.024 1 342 79 79 PHE CA C 55.745 0.024 1 343 79 79 PHE CB C 39.473 0.024 1 344 79 79 PHE N N 121.877 0.038 1 345 80 80 ILE H H 9.063 0.004 1 346 80 80 ILE CA C 58.942 0.024 1 347 80 80 ILE CB C 39.525 0.024 1 348 80 80 ILE N N 120.194 0.038 1 349 81 81 PRO C C 176.947 0.024 1 350 81 81 PRO CA C 62.562 0.024 1 351 81 81 PRO CB C 31.766 0.024 1 352 82 82 TYR H H 8.183 0.004 1 353 82 82 TYR C C 174.955 0.024 1 354 82 82 TYR CA C 58.015 0.024 1 355 82 82 TYR CB C 40.192 0.024 1 356 82 82 TYR N N 115.480 0.038 1 357 83 83 VAL H H 7.873 0.004 1 358 83 83 VAL C C 176.291 0.024 1 359 83 83 VAL CA C 61.362 0.024 1 360 83 83 VAL CB C 32.222 0.024 1 361 83 83 VAL N N 121.450 0.038 1 362 84 84 LEU H H 7.650 0.004 1 363 84 84 LEU CA C 51.933 0.024 1 364 84 84 LEU CB C 46.061 0.024 1 365 84 84 LEU N N 123.215 0.038 1 366 85 85 PRO C C 175.856 0.024 1 367 85 85 PRO CA C 63.473 0.024 1 368 85 85 PRO CB C 31.697 0.024 1 369 86 86 LEU H H 7.944 0.004 1 370 86 86 LEU CA C 54.977 0.024 1 371 86 86 LEU CB C 40.795 0.024 1 372 86 86 LEU N N 123.733 0.038 1 373 87 87 PRO C C 175.571 0.024 1 374 87 87 PRO CA C 64.533 0.024 1 375 87 87 PRO CB C 32.094 0.024 1 376 88 88 VAL H H 6.852 0.004 1 377 88 88 VAL C C 172.995 0.024 1 378 88 88 VAL CA C 58.483 0.024 1 379 88 88 VAL CB C 35.384 0.024 1 380 88 88 VAL N N 108.601 0.038 1 381 89 89 ASN H H 7.780 0.004 1 382 89 89 ASN C C 173.705 0.024 1 383 89 89 ASN CA C 52.189 0.024 1 384 89 89 ASN CB C 38.211 0.024 1 385 89 89 ASN N N 114.666 0.038 1 386 90 90 LEU H H 9.150 0.004 1 387 90 90 LEU C C 174.637 0.024 1 388 90 90 LEU CA C 53.605 0.024 1 389 90 90 LEU CB C 45.125 0.024 1 390 90 90 LEU N N 122.726 0.038 1 391 91 91 TRP H H 8.702 0.004 1 392 91 91 TRP C C 175.588 0.024 1 393 91 91 TRP CA C 52.885 0.024 1 394 91 91 TRP CB C 30.444 0.024 1 395 91 91 TRP N N 123.939 0.038 1 396 92 92 GLY H H 9.281 0.004 1 397 92 92 GLY C C 175.267 0.024 1 398 92 92 GLY CA C 43.032 0.024 1 399 92 92 GLY N N 112.000 0.038 1 400 93 93 ARG H H 8.990 0.004 1 401 93 93 ARG C C 176.729 0.024 1 402 93 93 ARG CA C 60.133 0.024 1 403 93 93 ARG CB C 30.600 0.024 1 404 93 93 ARG N N 118.785 0.038 1 405 94 94 ASP H H 7.994 0.004 1 406 94 94 ASP C C 177.855 0.024 1 407 94 94 ASP CA C 56.464 0.024 1 408 94 94 ASP CB C 37.787 0.024 1 409 94 94 ASP N N 118.628 0.038 1 410 95 95 ILE H H 7.881 0.004 1 411 95 95 ILE C C 177.957 0.024 1 412 95 95 ILE CA C 63.219 0.024 1 413 95 95 ILE CB C 39.251 0.024 1 414 95 95 ILE N N 122.590 0.038 1 415 96 96 MET H H 8.563 0.004 1 416 96 96 MET C C 178.509 0.024 1 417 96 96 MET CA C 59.718 0.024 1 418 96 96 MET CB C 33.025 0.024 1 419 96 96 MET N N 115.073 0.038 1 420 97 97 GLN H H 8.483 0.004 1 421 97 97 GLN C C 176.563 0.024 1 422 97 97 GLN CA C 58.097 0.024 1 423 97 97 GLN CB C 27.794 0.024 1 424 97 97 GLN N N 115.893 0.038 1 425 98 98 HIS H H 7.631 0.004 1 426 98 98 HIS C C 175.519 0.024 1 427 98 98 HIS CA C 56.468 0.024 1 428 98 98 HIS CB C 30.932 0.024 1 429 98 98 HIS N N 117.085 0.038 1 430 99 99 LEU H H 7.325 0.004 1 431 99 99 LEU C C 177.072 0.024 1 432 99 99 LEU CA C 54.627 0.024 1 433 99 99 LEU CB C 42.455 0.024 1 434 99 99 LEU N N 118.220 0.038 1 435 100 100 GLY H H 8.046 0.004 1 436 100 100 GLY C C 174.558 0.024 1 437 100 100 GLY CA C 46.003 0.024 1 438 100 100 GLY N N 107.739 0.038 1 439 101 101 LEU H H 7.619 0.004 1 440 101 101 LEU C C 174.743 0.024 1 441 101 101 LEU CA C 55.039 0.024 1 442 101 101 LEU CB C 42.481 0.024 1 443 101 101 LEU N N 119.145 0.038 1 444 102 102 ILE H H 8.011 0.004 1 445 102 102 ILE C C 176.116 0.024 1 446 102 102 ILE CA C 60.732 0.024 1 447 102 102 ILE CB C 37.956 0.024 1 448 102 102 ILE N N 120.554 0.038 1 449 103 103 LEU H H 8.354 0.004 1 450 103 103 LEU C C 177.151 0.024 1 451 103 103 LEU CA C 54.889 0.024 1 452 103 103 LEU CB C 41.858 0.024 1 453 103 103 LEU N N 126.280 0.038 1 454 104 104 SER H H 8.257 0.004 1 455 104 104 SER C C 174.738 0.024 1 456 104 104 SER CA C 58.234 0.024 1 457 104 104 SER CB C 64.022 0.024 1 458 104 104 SER N N 116.114 0.038 1 459 105 105 ASN H H 8.441 0.004 1 460 105 105 ASN C C 175.606 0.024 1 461 105 105 ASN CA C 54.848 0.024 1 462 105 105 ASN CB C 42.030 0.024 1 463 105 105 ASN N N 124.356 0.038 1 464 106 106 GLU H H 8.362 0.004 1 465 106 106 GLU C C 174.052 0.024 1 466 106 106 GLU CA C 57.114 0.024 1 467 106 106 GLU CB C 29.744 0.024 1 468 106 106 GLU N N 121.504 0.038 1 469 107 107 ASN H H 8.345 0.004 1 470 107 107 ASN C C 175.078 0.024 1 471 107 107 ASN CA C 53.488 0.024 1 472 107 107 ASN CB C 38.811 0.024 1 473 107 107 ASN N N 118.548 0.038 1 474 108 108 ALA H H 8.043 0.004 1 475 108 108 ALA CA C 50.723 0.024 1 476 108 108 ALA CB C 17.987 0.024 1 477 108 108 ALA N N 124.773 0.038 1 478 109 109 PRO C C 177.338 0.024 1 479 109 109 PRO CA C 63.306 0.024 1 480 109 109 PRO CB C 31.599 0.024 1 481 110 110 SER H H 8.415 0.004 1 482 110 110 SER C C 175.346 0.024 1 483 110 110 SER CA C 58.775 0.024 1 484 110 110 SER CB C 63.994 0.024 1 485 110 110 SER N N 115.816 0.038 1 486 111 111 GLY H H 8.405 0.004 1 487 111 111 GLY C C 174.640 0.024 1 488 111 111 GLY CA C 45.347 0.024 1 489 111 111 GLY N N 110.690 0.038 1 490 112 112 GLY H H 8.150 0.004 1 491 112 112 GLY CA C 44.997 0.024 1 492 112 112 GLY N N 108.257 0.038 1 493 113 113 TYR H H 8.097 0.004 1 494 113 113 TYR CA C 58.235 0.024 1 495 113 113 TYR CB C 38.877 0.024 1 496 113 113 TYR N N 119.701 0.038 1 497 114 114 SER H H 8.297 0.004 1 498 114 114 SER C C 176.189 0.024 1 499 114 114 SER CA C 58.241 0.024 1 500 114 114 SER CB C 64.092 0.024 1 501 114 114 SER N N 117.088 0.038 1 502 115 115 THR H H 8.205 0.004 1 503 115 115 THR C C 176.952 0.024 1 504 115 115 THR CA C 62.784 0.024 1 505 115 115 THR CB C 69.443 0.024 1 506 115 115 THR N N 116.114 0.038 1 507 116 116 LYS H H 8.154 0.004 1 508 116 116 LYS C C 176.724 0.024 1 509 116 116 LYS CA C 56.857 0.024 1 510 116 116 LYS CB C 32.461 0.024 1 511 116 116 LYS N N 122.761 0.038 1 512 117 117 ALA H H 8.142 0.004 1 513 117 117 ALA C C 177.601 0.024 1 514 117 117 ALA CA C 52.964 0.024 1 515 117 117 ALA CB C 18.907 0.024 1 516 117 117 ALA N N 124.243 0.038 1 517 118 118 LYS H H 8.235 0.004 1 518 118 118 LYS C C 176.793 0.024 1 519 118 118 LYS CA C 56.923 0.024 1 520 118 118 LYS CB C 32.592 0.024 1 521 118 118 LYS N N 119.809 0.038 1 522 119 119 ASN H H 8.309 0.004 1 523 119 119 ASN C C 174.229 0.024 1 524 119 119 ASN CA C 53.702 0.024 1 525 119 119 ASN CB C 38.467 0.024 1 526 119 119 ASN N N 119.056 0.038 1 527 120 120 ILE H H 8.040 0.004 1 528 120 120 ILE C C 176.644 0.024 1 529 120 120 ILE CA C 61.972 0.024 1 530 120 120 ILE CB C 38.134 0.024 1 531 120 120 ILE N N 121.029 0.038 1 532 121 121 MET H H 8.261 0.004 1 533 121 121 MET C C 176.483 0.024 1 534 121 121 MET CA C 55.995 0.024 1 535 121 121 MET CB C 32.400 0.024 1 536 121 121 MET N N 122.608 0.038 1 537 122 122 ALA H H 8.102 0.004 1 538 122 122 ALA CA C 53.019 0.024 1 539 122 122 ALA CB C 18.873 0.024 1 540 122 122 ALA N N 124.254 0.038 1 541 123 123 LYS H H 8.108 0.004 1 542 123 123 LYS C C 174.128 0.024 1 543 123 123 LYS CA C 56.589 0.024 1 544 123 123 LYS CB C 32.403 0.024 1 545 123 123 LYS N N 119.739 0.038 1 546 124 124 MET H H 8.214 0.004 1 547 124 124 MET C C 176.665 0.024 1 548 124 124 MET CA C 55.812 0.024 1 549 124 124 MET CB C 32.542 0.024 1 550 124 124 MET N N 120.630 0.038 1 551 125 125 GLY H H 8.307 0.004 1 552 125 125 GLY C C 173.797 0.024 1 553 125 125 GLY CA C 45.293 0.024 1 554 125 125 GLY N N 109.480 0.038 1 555 126 126 TYR H H 7.993 0.004 1 556 126 126 TYR C C 175.050 0.024 1 557 126 126 TYR CA C 58.190 0.024 1 558 126 126 TYR CB C 38.781 0.024 1 559 126 126 TYR N N 120.318 0.038 1 560 127 127 LYS H H 8.191 0.004 1 561 127 127 LYS C C 175.946 0.024 1 562 127 127 LYS CA C 56.091 0.024 1 563 127 127 LYS CB C 32.862 0.024 1 564 127 127 LYS N N 123.683 0.038 1 565 128 128 GLU H H 8.303 0.004 1 566 128 128 GLU C C 176.992 0.024 1 567 128 128 GLU CA C 56.724 0.024 1 568 128 128 GLU CB C 29.857 0.024 1 569 128 128 GLU N N 121.826 0.038 1 570 129 129 GLY H H 8.487 0.004 1 571 129 129 GLY C C 174.411 0.024 1 572 129 129 GLY CA C 45.347 0.024 1 573 129 129 GLY N N 109.522 0.038 1 574 130 130 LYS H H 8.228 0.004 1 575 130 130 LYS CA C 56.134 0.024 1 576 130 130 LYS CB C 32.736 0.024 1 577 130 130 LYS N N 125.507 0.038 1 578 131 131 GLY C C 174.223 0.024 1 579 131 131 GLY CA C 45.362 0.024 1 580 132 132 LEU H H 8.030 0.004 1 581 132 132 LEU C C 178.103 0.024 1 582 132 132 LEU CA C 55.369 0.024 1 583 132 132 LEU CB C 41.978 0.024 1 584 132 132 LEU N N 120.956 0.038 1 585 133 133 GLY H H 8.454 0.004 1 586 133 133 GLY C C 174.050 0.024 1 587 133 133 GLY CA C 45.265 0.024 1 588 133 133 GLY N N 109.135 0.038 1 589 134 134 HIS H H 8.267 0.004 1 590 134 134 HIS C C 174.896 0.024 1 591 134 134 HIS CA C 56.002 0.024 1 592 134 134 HIS CB C 29.611 0.024 1 593 134 134 HIS N N 118.644 0.038 1 594 135 135 GLN H H 8.431 0.004 1 595 135 135 GLN C C 176.542 0.024 1 596 135 135 GLN CA C 56.643 0.024 1 597 135 135 GLN CB C 29.833 0.024 1 598 135 135 GLN N N 121.761 0.038 1 599 136 136 GLU H H 8.468 0.004 1 600 136 136 GLU C C 175.854 0.024 1 601 136 136 GLU CA C 56.012 0.024 1 602 136 136 GLU CB C 29.140 0.024 1 603 136 136 GLU N N 121.484 0.038 1 604 137 137 GLN H H 8.563 0.004 1 605 137 137 GLN C C 176.898 0.024 1 606 137 137 GLN CA C 56.556 0.024 1 607 137 137 GLN CB C 29.696 0.024 1 608 137 137 GLN N N 122.422 0.038 1 609 138 138 GLY H H 8.372 0.004 1 610 138 138 GLY C C 173.709 0.024 1 611 138 138 GLY CA C 45.375 0.024 1 612 138 138 GLY N N 109.949 0.038 1 613 139 139 ARG H H 8.071 0.004 1 614 139 139 ARG C C 176.026 0.024 1 615 139 139 ARG CA C 55.937 0.024 1 616 139 139 ARG CB C 30.588 0.024 1 617 139 139 ARG N N 120.683 0.038 1 618 140 140 ILE H H 8.279 0.004 1 619 140 140 ILE C C 176.047 0.024 1 620 140 140 ILE CA C 60.897 0.024 1 621 140 140 ILE CB C 38.373 0.024 1 622 140 140 ILE N N 123.323 0.038 1 623 141 141 GLU H H 8.449 0.004 1 624 141 141 GLU CA C 54.144 0.024 1 625 141 141 GLU CB C 29.480 0.024 1 626 141 141 GLU N N 126.940 0.038 1 627 142 142 PRO C C 176.734 0.024 1 628 142 142 PRO CA C 62.952 0.024 1 629 142 142 PRO CB C 31.791 0.024 1 630 143 143 ILE H H 8.200 0.004 1 631 143 143 ILE C C 176.277 0.024 1 632 143 143 ILE CA C 61.122 0.024 1 633 143 143 ILE CB C 38.600 0.024 1 634 143 143 ILE N N 121.011 0.038 1 635 144 144 SER H H 8.418 0.004 1 636 144 144 SER CA C 56.276 0.024 1 637 144 144 SER CB C 63.616 0.024 1 638 144 144 SER N N 121.029 0.038 1 639 145 145 PRO C C 176.879 0.024 1 640 145 145 PRO CA C 63.630 0.024 1 641 145 145 PRO CB C 31.670 0.024 1 642 146 146 ASN H H 8.360 0.004 1 643 146 146 ASN C C 175.762 0.024 1 644 146 146 ASN CA C 53.347 0.024 1 645 146 146 ASN CB C 38.877 0.024 1 646 146 146 ASN N N 117.630 0.038 1 647 147 147 GLY H H 8.232 0.004 1 648 147 147 GLY C C 174.486 0.024 1 649 147 147 GLY CA C 45.511 0.024 1 650 147 147 GLY N N 109.002 0.038 1 651 148 148 ASN H H 8.463 0.004 1 652 148 148 ASN CA C 53.683 0.024 1 653 148 148 ASN CB C 38.800 0.024 1 654 148 148 ASN N N 118.406 0.038 1 655 149 149 GLN C C 175.857 0.024 1 656 149 149 GLN CA C 56.206 0.024 1 657 149 149 GLN CB C 28.923 0.024 1 658 150 150 ASP H H 8.339 0.004 1 659 150 150 ASP C C 176.415 0.024 1 660 150 150 ASP CA C 54.553 0.024 1 661 150 150 ASP CB C 40.831 0.024 1 662 150 150 ASP N N 120.875 0.038 1 663 151 151 ARG H H 8.202 0.004 1 664 151 151 ARG CA C 56.140 0.024 1 665 151 151 ARG CB C 30.022 0.024 1 666 151 151 ARG N N 120.890 0.038 1 667 152 152 GLN C C 177.151 0.024 1 668 152 152 GLN CA C 56.241 0.024 1 669 152 152 GLN CB C 32.632 0.024 1 670 153 153 GLY H H 8.436 0.004 1 671 153 153 GLY C C 174.143 0.024 1 672 153 153 GLY CA C 45.265 0.024 1 673 153 153 GLY N N 109.700 0.038 1 674 154 154 LEU H H 8.144 0.004 1 675 154 154 LEU C C 177.789 0.024 1 676 154 154 LEU CA C 55.381 0.024 1 677 154 154 LEU CB C 41.976 0.024 1 678 154 154 LEU N N 121.358 0.038 1 679 155 155 GLY H H 8.280 0.004 1 680 155 155 GLY C C 173.361 0.024 1 681 155 155 GLY CA C 45.074 0.024 1 682 155 155 GLY N N 108.534 0.038 1 683 156 156 PHE H H 7.927 0.004 1 684 156 156 PHE CA C 55.650 0.024 1 685 156 156 PHE CB C 38.736 0.024 1 686 156 156 PHE N N 120.658 0.038 1 stop_ save_