data_6617 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H,15N assignment of the C-terminal haemopexin-like domain of matrix metalloproteinase MMP-13 (collagenase-3) ; _BMRB_accession_number 6617 _BMRB_flat_file_name bmr6617.str _Entry_type original _Submission_date 2005-05-03 _Accession_date 2005-05-03 _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 Jacobs Doris M. . 2 Grimme Susanne . . 3 Elshorst Bettina . . 4 Pescatore Barbara . . 5 Vogtherr Martin . . 6 Saxena Krishna . . 7 Betz Marco . . 8 Schieborr Ulrich . . 9 Langer Thomas . . 10 Schwalbe Harald . . 11 Fiebig Klaus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 137 "13C chemical shifts" 440 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-26 original author . stop_ _Original_release_date 2005-10-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone NMR Assignment of the C-terminal Haemopexin-like Domain (HPLD) of Human Matrix Metalloproteinase MMP-13 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16211490 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacobs Doris M. . 2 Grimme Susanne . . 3 Elshorst Bettina . . 4 Pescatore Barbara . . 5 Vogtherr Martin . . 6 Betz Marco . . 7 Schieborr Ulrich . . 8 Langer Thomas . . 9 Saxena Krishna . . 10 Schwalbe Harald . . 11 Fiebig Klaus . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 32 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 337 _Page_last 337 _Year 2005 _Details . loop_ _Keyword 'Haemopexin-like domain' 'Matrix metalloproteinase' 'NMR backbone assignment' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title ; The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8969305 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gomis-Ruth F.X. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full . _Journal_volume 264 _Journal_issue 3 _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 556 _Page_last 566 _Year 1996 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ; C-terminal haemopexin-like domain of matrix metalloproteinase MMP-13 (collagenase-3) ; _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'matrix metalloproteinase MMP-13' $MMP-13_HPLD 'CALCIUM (II) ION, 1' $CA 'CALCIUM (II) ION, 2' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MMP-13_HPLD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'c-terminal haemopexin-like domain of matrix metalloproteinase MMP-13' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 207 _Mol_residue_sequence ; LYGPGDEDPNPKHPKTPDKC DPSLSLDAITSLRGETMIFK DRFFWRLHPQQVDAELFLTK SFWPELPNRIDAAYEHPSHD LIFIFRGRKFWALNGYDILE GYPKKISELGLPKEVKKISA AVHFEDTGKTLLFSGNQVWR YDDTNHIMDKDYPRLIEEDF PGIGDKVDAVYEKNGYIYFF NGPIQFEYSIWSNRIVRVMP ANSILWC ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 TYR 3 GLY 4 PRO 5 GLY 6 ASP 7 GLU 8 ASP 9 PRO 10 ASN 11 PRO 12 LYS 13 HIS 14 PRO 15 LYS 16 THR 17 PRO 18 ASP 19 LYS 20 CYS 21 ASP 22 PRO 23 SER 24 LEU 25 SER 26 LEU 27 ASP 28 ALA 29 ILE 30 THR 31 SER 32 LEU 33 ARG 34 GLY 35 GLU 36 THR 37 MET 38 ILE 39 PHE 40 LYS 41 ASP 42 ARG 43 PHE 44 PHE 45 TRP 46 ARG 47 LEU 48 HIS 49 PRO 50 GLN 51 GLN 52 VAL 53 ASP 54 ALA 55 GLU 56 LEU 57 PHE 58 LEU 59 THR 60 LYS 61 SER 62 PHE 63 TRP 64 PRO 65 GLU 66 LEU 67 PRO 68 ASN 69 ARG 70 ILE 71 ASP 72 ALA 73 ALA 74 TYR 75 GLU 76 HIS 77 PRO 78 SER 79 HIS 80 ASP 81 LEU 82 ILE 83 PHE 84 ILE 85 PHE 86 ARG 87 GLY 88 ARG 89 LYS 90 PHE 91 TRP 92 ALA 93 LEU 94 ASN 95 GLY 96 TYR 97 ASP 98 ILE 99 LEU 100 GLU 101 GLY 102 TYR 103 PRO 104 LYS 105 LYS 106 ILE 107 SER 108 GLU 109 LEU 110 GLY 111 LEU 112 PRO 113 LYS 114 GLU 115 VAL 116 LYS 117 LYS 118 ILE 119 SER 120 ALA 121 ALA 122 VAL 123 HIS 124 PHE 125 GLU 126 ASP 127 THR 128 GLY 129 LYS 130 THR 131 LEU 132 LEU 133 PHE 134 SER 135 GLY 136 ASN 137 GLN 138 VAL 139 TRP 140 ARG 141 TYR 142 ASP 143 ASP 144 THR 145 ASN 146 HIS 147 ILE 148 MET 149 ASP 150 LYS 151 ASP 152 TYR 153 PRO 154 ARG 155 LEU 156 ILE 157 GLU 158 GLU 159 ASP 160 PHE 161 PRO 162 GLY 163 ILE 164 GLY 165 ASP 166 LYS 167 VAL 168 ASP 169 ALA 170 VAL 171 TYR 172 GLU 173 LYS 174 ASN 175 GLY 176 TYR 177 ILE 178 TYR 179 PHE 180 PHE 181 ASN 182 GLY 183 PRO 184 ILE 185 GLN 186 PHE 187 GLU 188 TYR 189 SER 190 ILE 191 TRP 192 SER 193 ASN 194 ARG 195 ILE 196 VAL 197 ARG 198 VAL 199 MET 200 PRO 201 ALA 202 ASN 203 SER 204 ILE 205 LEU 206 TRP 207 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 8 11:22:52 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MMP-13_HPLD human 9606 Eukaryota Metazoa Homo sapiens 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 $MMP-13_HPLD 'recombinant technology' E.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 $MMP-13_HPLD 0.7 mM '[U-13C; U-15N; U-50% 2H]' BisTris 20 mM . Na2SO4 200 mM . CaCl2 5 mM . Arginine 10 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _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_HNCOCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCACB _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _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 ; 20 mM BisTris 200 mM Na2SO4 5 mM CaCl2 10 mM Arginine ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 0.01 M pH 6.8 0.2 pH temperature 298 . 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H15N HSQC' HNCACB HNCOCACB HNCA HN(CA)CO HNCO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'matrix metalloproteinase MMP-13' _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 1 LEU C C 175.682 0.500 1 2 1 1 LEU CA C 54.646 0.500 1 3 1 1 LEU CB C 41.428 0.500 1 4 2 2 TYR H H 8.265 0.050 1 5 2 2 TYR C C 177.255 0.500 1 6 2 2 TYR CA C 56.948 0.500 1 7 2 2 TYR CB C 38.382 0.500 1 8 2 2 TYR N N 120.868 0.500 1 9 3 3 GLY H H 8.187 0.050 1 10 3 3 GLY CA C 43.916 0.500 1 11 3 3 GLY N N 110.224 0.500 1 12 4 4 PRO C C 176.121 0.500 1 13 4 4 PRO CA C 63.135 0.500 1 14 4 4 PRO CB C 30.995 0.500 1 15 5 5 GLY H H 8.527 0.050 1 16 5 5 GLY C C 179.9 0.500 1 17 5 5 GLY CA C 44.872 0.500 1 18 5 5 GLY N N 110.147 0.500 1 19 6 6 ASP H H 8.165 0.050 1 20 6 6 ASP C C 176.196 0.500 1 21 6 6 ASP CA C 54.885 0.500 1 22 6 6 ASP CB C 40.78 0.500 1 23 6 6 ASP N N 120.32 0.500 1 24 7 7 GLU H H 8.31 0.050 1 25 7 7 GLU C C 177.542 0.500 1 26 7 7 GLU CA C 55.904 0.500 1 27 7 7 GLU CB C 29.489 0.500 1 28 7 7 GLU N N 120.218 0.500 1 29 8 8 ASP H H 8.159 0.050 1 30 8 8 ASP CA C 51.636 0.500 1 31 8 8 ASP CB C 40.71 0.500 1 32 8 8 ASP N N 122.832 0.500 1 33 9 9 PRO C C 176.756 0.500 1 34 9 9 PRO CA C 62.851 0.500 1 35 9 9 PRO CB C 31.349 0.500 1 36 10 10 ASN H H 8.408 0.050 1 37 10 10 ASN CA C 52.018 0.500 1 38 10 10 ASN CB C 38.37 0.500 1 39 10 10 ASN N N 119.63 0.500 1 40 11 11 PRO C C 176.363 0.500 1 41 11 11 PRO CA C 63.031 0.500 1 42 11 11 PRO CB C 31.109 0.500 1 43 12 12 LYS H H 8.182 0.050 1 44 12 12 LYS C C 176.967 0.500 1 45 12 12 LYS CA C 55.792 0.500 1 46 12 12 LYS CB C 31.769 0.500 1 47 12 12 LYS N N 119.508 0.500 1 48 13 13 HIS H H 8.074 0.050 1 49 13 13 HIS CA C 53.203 0.500 1 50 13 13 HIS CB C 29.069 0.500 1 51 13 13 HIS N N 119.72 0.500 1 52 14 14 PRO C C 176.741 0.500 1 53 14 14 PRO CA C 62.611 0.500 1 54 14 14 PRO CB C 31.349 0.500 1 55 15 15 LYS H H 8.562 0.050 1 56 15 15 LYS C C 176.937 0.500 1 57 15 15 LYS CA C 55.725 0.500 1 58 15 15 LYS CB C 31.89 0.500 1 59 15 15 LYS N N 121.844 0.500 1 60 16 16 THR H H 8.023 0.050 1 61 16 16 THR CA C 59.012 0.500 1 62 16 16 THR CB C 68.371 0.500 1 63 16 16 THR N N 117.542 0.500 1 64 17 17 PRO CA C 62.611 0.500 1 65 17 17 PRO CB C 31.229 0.500 1 66 18 18 ASP H H 8.058 0.050 1 67 18 18 ASP CA C 50.681 0.500 1 68 18 18 ASP CB C 39.69 0.500 1 69 18 18 ASP N N 118.092 0.500 1 70 20 20 CYS CA C 59.012 0.500 1 71 20 20 CYS N N 114.117 0.500 1 72 22 22 PRO C C 175.259 0.500 1 73 22 22 PRO CA C 63.931 0.500 1 74 22 22 PRO CB C 31.229 0.500 1 75 23 23 SER H H 8.683 0.050 1 76 23 23 SER C C 179.749 0.500 1 77 23 23 SER CA C 57.355 0.500 1 78 23 23 SER CB C 63.151 0.500 1 79 23 23 SER N N 114.107 0.500 1 80 24 24 LEU H H 7.534 0.050 1 81 24 24 LEU C C 178.751 0.500 1 82 24 24 LEU CA C 56.719 0.500 1 83 24 24 LEU CB C 41.97 0.500 1 84 24 24 LEU N N 124.735 0.500 1 85 25 25 SER H H 7.67 0.050 1 86 25 25 SER C C 179.492 0.500 1 87 25 25 SER CA C 55.114 0.500 1 88 25 25 SER CB C 65.671 0.500 1 89 25 25 SER N N 118.321 0.500 1 90 26 26 LEU H H 9.568 0.050 1 91 26 26 LEU C C 176.831 0.500 1 92 26 26 LEU CA C 53.891 0.500 1 93 26 26 LEU CB C 44.01 0.500 1 94 26 26 LEU N N 121.865 0.500 1 95 27 27 ASP H H 7.736 0.050 1 96 27 27 ASP C C 177.451 0.500 1 97 27 27 ASP CA C 55.42 0.500 1 98 27 27 ASP CB C 40.53 0.500 1 99 27 27 ASP N N 117.37 0.500 1 100 28 28 ALA H H 7.543 0.050 1 101 28 28 ALA C C 178.162 0.500 1 102 28 28 ALA CA C 51.598 0.500 1 103 28 28 ALA CB C 21.329 0.500 1 104 28 28 ALA N N 118.294 0.500 1 105 29 29 ILE H H 8.807 0.050 1 106 29 29 ILE C C 180.157 0.500 1 107 29 29 ILE CA C 60.006 0.500 1 108 29 29 ILE CB C 42.15 0.500 1 109 29 29 ILE N N 122.016 0.500 1 110 30 30 THR H H 8.775 0.050 1 111 30 30 THR CA C 59.7 0.500 1 112 30 30 THR CB C 68.731 0.500 1 113 30 30 THR N N 118.439 0.500 1 114 33 33 ARG CA C 54.273 0.500 1 115 33 33 ARG N N 122.963 0.500 1 116 34 34 GLY CA C 45.177 0.500 1 117 34 34 GLY N N 105.289 0.500 1 118 35 35 GLU CA C 54.732 0.500 1 119 35 35 GLU N N 120.274 0.500 1 120 37 37 MET C C 179.749 0.500 1 121 37 37 MET CA C 53.5 0.500 1 122 37 37 MET CB C 34.47 0.500 1 123 37 37 MET N N 125.587 0.500 1 124 38 38 ILE H H 8.92 0.050 1 125 38 38 ILE C C 178.555 0.500 1 126 38 38 ILE CA C 59.551 0.500 1 127 38 38 ILE CB C 40.29 0.500 1 128 38 38 ILE N N 122.861 0.500 1 129 39 39 PHE H H 9.104 0.050 1 130 39 39 PHE C C 177.451 0.500 1 131 39 39 PHE CA C 58.344 0.500 1 132 39 39 PHE CB C 39.93 0.500 1 133 39 39 PHE N N 124.526 0.500 1 134 40 40 LYS H H 8.925 0.050 1 135 40 40 LYS C C 180.309 0.500 1 136 40 40 LYS CA C 55.19 0.500 1 137 40 40 LYS CB C 34.53 0.500 1 138 40 40 LYS N N 122.095 0.500 1 139 41 41 ASP H H 9.689 0.050 1 140 41 41 ASP C C 177.527 0.500 1 141 41 41 ASP CA C 55.878 0.500 1 142 41 41 ASP CB C 39.63 0.500 1 143 41 41 ASP N N 128.547 0.500 1 144 42 42 ARG H H 7.453 0.050 1 145 42 42 ARG C C 179.719 0.500 1 146 42 42 ARG CA C 56.108 0.500 1 147 42 42 ARG CB C 29.069 0.500 1 148 42 42 ARG N N 121.015 0.500 1 149 43 43 PHE H H 8.362 0.050 1 150 43 43 PHE C C 178.494 0.500 1 151 43 43 PHE CA C 56.566 0.500 1 152 43 43 PHE CB C 43.11 0.500 1 153 43 43 PHE N N 120.247 0.500 1 154 44 44 PHE H H 8.756 0.050 1 155 44 44 PHE C C 179.885 0.500 1 156 44 44 PHE CA C 56.337 0.500 1 157 44 44 PHE CB C 40.77 0.500 1 158 44 44 PHE N N 113.524 0.500 1 159 45 45 TRP H H 9.334 0.050 1 160 45 45 TRP CA C 56.872 0.500 1 161 45 45 TRP CB C 31.109 0.500 1 162 45 45 TRP N N 118.149 0.500 1 163 50 50 GLN CA C 56.827 0.500 1 164 50 50 GLN N N 121.015 0.500 1 165 51 51 GLN H H 7.633 0.050 1 166 51 51 GLN C C 178.162 0.500 1 167 51 51 GLN CA C 54.732 0.500 1 168 51 51 GLN CB C 27.25 0.500 1 169 51 51 GLN N N 117.727 0.500 1 170 52 52 VAL H H 7.81 0.050 1 171 52 52 VAL C C 178.872 0.500 1 172 52 52 VAL CA C 61.535 0.500 1 173 52 52 VAL CB C 29.849 0.500 1 174 52 52 VAL N N 117.295 0.500 1 175 53 53 ASP H H 7.367 0.050 1 176 53 53 ASP C C 178.797 0.500 1 177 53 53 ASP CA C 52.744 0.500 1 178 53 53 ASP CB C 42.39 0.500 1 179 53 53 ASP N N 118.756 0.500 1 180 54 54 ALA H H 8.478 0.050 1 181 54 54 ALA C C 177.497 0.500 1 182 54 54 ALA CA C 51.216 0.500 1 183 54 54 ALA CB C 19.829 0.500 1 184 54 54 ALA N N 125.625 0.500 1 185 55 55 GLU H H 8.204 0.050 1 186 55 55 GLU C C 179.961 0.500 1 187 55 55 GLU CA C 55.443 0.500 1 188 55 55 GLU CB C 31.95 0.500 1 189 55 55 GLU N N 123.937 0.500 1 190 56 56 LEU H H 7.925 0.050 1 191 56 56 LEU C C 178.192 0.500 1 192 56 56 LEU CA C 54.35 0.500 1 193 56 56 LEU CB C 42.87 0.500 1 194 56 56 LEU N N 125.885 0.500 1 195 57 57 PHE H H 8.921 0.050 1 196 57 57 PHE C C 179.099 0.500 1 197 57 57 PHE CA C 56.108 0.500 1 198 57 57 PHE CB C 42.93 0.500 1 199 57 57 PHE N N 125.036 0.500 1 200 58 58 LEU H H 8.438 0.050 1 201 58 58 LEU CA C 53.662 0.500 1 202 58 58 LEU CB C 42.57 0.500 1 203 58 58 LEU N N 120.218 0.500 1 204 60 60 LYS CA C 57.483 0.500 1 205 60 60 LYS N N 118.835 0.500 1 206 61 61 SER CA C 60.082 0.500 1 207 61 61 SER N N 112.902 0.500 1 208 64 64 PRO C C 176.03 0.500 1 209 65 65 GLU H H 8.524 0.050 1 210 65 65 GLU C C 176.151 0.500 1 211 65 65 GLU CA C 56.108 0.500 1 212 65 65 GLU CB C 28.769 0.500 1 213 65 65 GLU N N 113.842 0.500 1 214 66 66 LEU H H 7.108 0.050 1 215 66 66 LEU CA C 52.439 0.500 1 216 66 66 LEU CB C 38.79 0.500 1 217 66 66 LEU N N 119.175 0.500 1 218 67 67 PRO C C 179.099 0.500 1 219 67 67 PRO CA C 61.411 0.500 1 220 67 67 PRO CB C 31.349 0.500 1 221 68 68 ASN H H 8.177 0.050 1 222 68 68 ASN C C 179.356 0.500 1 223 68 68 ASN CA C 54.388 0.500 1 224 68 68 ASN CB C 38.07 0.500 1 225 68 68 ASN N N 113.353 0.500 1 226 69 69 ARG H H 7.143 0.050 1 227 69 69 ARG C C 180.777 0.500 1 228 69 69 ARG CA C 54.579 0.500 1 229 69 69 ARG CB C 31.95 0.500 1 230 69 69 ARG N N 116.856 0.500 1 231 70 70 ILE H H 9.566 0.050 1 232 70 70 ILE C C 176.846 0.500 1 233 70 70 ILE CA C 58.63 0.500 1 234 70 70 ILE CB C 38.01 0.500 1 235 70 70 ILE N N 122.077 0.500 1 236 71 71 ASP H H 8.831 0.050 1 237 71 71 ASP C C 177.497 0.500 1 238 71 71 ASP CA C 55.573 0.500 1 239 71 71 ASP CB C 41.07 0.500 1 240 71 71 ASP N N 123.968 0.500 1 241 72 72 ALA H H 7.538 0.050 1 242 72 72 ALA C C 178.797 0.500 1 243 72 72 ALA CA C 51.75 0.500 1 244 72 72 ALA CB C 21.689 0.500 1 245 72 72 ALA N N 118.358 0.500 1 246 73 73 ALA H H 8.528 0.050 1 247 73 73 ALA C C 179.054 0.500 1 248 73 73 ALA CA C 51.552 0.500 1 249 73 73 ALA CB C 22.589 0.500 1 250 73 73 ALA N N 121.811 0.500 1 251 74 74 TYR H H 8.889 0.050 1 252 74 74 TYR CA C 57.355 0.500 1 253 74 74 TYR CB C 39.27 0.500 1 254 74 74 TYR N N 113.576 0.500 1 255 80 80 ASP CA C 54.19 0.500 1 256 80 80 ASP N N 126.574 0.500 1 257 81 81 LEU CA C 53.585 0.500 1 258 81 81 LEU N N 128.565 0.500 1 259 83 83 PHE C C 179.129 0.500 1 260 83 83 PHE CA C 57.157 0.500 1 261 83 83 PHE N N 120.218 0.500 1 262 84 84 ILE H H 8.884 0.050 1 263 84 84 ILE C C 178.903 0.500 1 264 84 84 ILE CA C 57.355 0.500 1 265 84 84 ILE CB C 39.63 0.500 1 266 84 84 ILE N N 113.82 0.500 1 267 85 85 PHE H H 8.587 0.050 1 268 85 85 PHE CA C 57.025 0.500 1 269 85 85 PHE CB C 41.25 0.500 1 270 85 85 PHE N N 124.136 0.500 1 271 86 86 ARG H H 9.077 0.050 1 272 86 86 ARG CA C 56.031 0.500 1 273 86 86 ARG CB C 31.349 0.500 1 274 86 86 ARG N N 120.097 0.500 1 275 87 87 GLY H H 9.792 0.050 1 276 87 87 GLY C C 178.706 0.500 1 277 87 87 GLY CA C 46.477 0.500 1 278 87 87 GLY N N 121.082 0.500 1 279 88 88 ARG H H 8.803 0.050 1 280 88 88 ARG C C 178.132 0.500 1 281 88 88 ARG CA C 55.772 0.500 1 282 88 88 ARG CB C 28.469 0.500 1 283 88 88 ARG N N 122.848 0.500 1 284 89 89 LYS H H 7.961 0.050 1 285 89 89 LYS C C 179.402 0.500 1 286 89 89 LYS CA C 54.52 0.500 1 287 89 89 LYS CB C 36.33 0.500 1 288 89 89 LYS N N 120.483 0.500 1 289 90 90 PHE H H 8.496 0.050 1 290 90 90 PHE C C 181.08 0.500 1 291 90 90 PHE CA C 54.732 0.500 1 292 90 90 PHE CB C 41.43 0.500 1 293 90 90 PHE N N 113.82 0.500 1 294 91 91 TRP H H 9.419 0.050 1 295 91 91 TRP CA C 58.095 0.500 1 296 91 91 TRP N N 120.218 0.500 1 297 93 93 LEU CA C 53.432 0.500 1 298 93 93 LEU N N 121.488 0.500 1 299 96 96 TYR C C 178.358 0.500 1 300 97 97 ASP H H 7.968 0.050 1 301 97 97 ASP C C 178.585 0.500 1 302 97 97 ASP CA C 53.597 0.500 1 303 97 97 ASP CB C 42.45 0.500 1 304 97 97 ASP N N 119.421 0.500 1 305 98 98 ILE H H 8.683 0.050 1 306 98 98 ILE C C 176.332 0.500 1 307 98 98 ILE CA C 60.847 0.500 1 308 98 98 ILE CB C 37.11 0.500 1 309 98 98 ILE N N 123.41 0.500 1 310 99 99 LEU H H 8.092 0.050 1 311 99 99 LEU C C 176.181 0.500 1 312 99 99 LEU CA C 55.725 0.500 1 313 99 99 LEU CB C 41.97 0.500 1 314 99 99 LEU N N 130.334 0.500 1 315 100 100 GLU H H 8.319 0.050 1 316 100 100 GLU C C 176.045 0.500 1 317 100 100 GLU CA C 56.948 0.500 1 318 100 100 GLU CB C 28.889 0.500 1 319 100 100 GLU N N 120.564 0.500 1 320 101 101 GLY H H 8.681 0.050 1 321 101 101 GLY C C 180.596 0.500 1 322 101 101 GLY CA C 44.336 0.500 1 323 101 101 GLY N N 111.065 0.500 1 324 102 102 TYR H H 7.354 0.050 1 325 102 102 TYR CA C 56.26 0.500 1 326 102 102 TYR CB C 37.53 0.500 1 327 102 102 TYR N N 116.693 0.500 1 328 103 103 PRO C C 178.086 0.500 1 329 103 103 PRO CA C 61.051 0.500 1 330 103 103 PRO CB C 32.97 0.500 1 331 104 104 LYS H H 7.905 0.050 1 332 104 104 LYS C C 178.933 0.500 1 333 104 104 LYS CA C 53.86 0.500 1 334 104 104 LYS CB C 35.79 0.500 1 335 104 104 LYS N N 120.261 0.500 1 336 105 105 LYS H H 8.382 0.050 1 337 105 105 LYS C C 172.87 0.500 1 338 105 105 LYS CA C 54.12 0.500 1 339 105 105 LYS CB C 32.79 0.500 1 340 105 105 LYS N N 117.489 0.500 1 341 106 106 ILE H H 8.682 0.050 1 342 106 106 ILE C C 176.166 0.500 1 343 106 106 ILE CA C 64.674 0.500 1 344 106 106 ILE CB C 36.45 0.500 1 345 106 106 ILE N N 114.904 0.500 1 346 107 107 SER H H 7.572 0.050 1 347 107 107 SER C C 174.896 0.500 1 348 107 107 SER CA C 59.624 0.500 1 349 107 107 SER CB C 62.011 0.500 1 350 107 107 SER N N 116.141 0.500 1 351 108 108 GLU H H 8.466 0.050 1 352 108 108 GLU C C 175.471 0.500 1 353 108 108 GLU CA C 58.706 0.500 1 354 108 108 GLU CB C 28.529 0.500 1 355 108 108 GLU N N 123.415 0.500 1 356 109 109 LEU H H 7.28 0.050 1 357 109 109 LEU C C 178.328 0.500 1 358 109 109 LEU CA C 54.044 0.500 1 359 109 109 LEU CB C 40.29 0.500 1 360 109 109 LEU N N 117.099 0.500 1 361 110 110 GLY H H 7.429 0.050 1 362 110 110 GLY C C 178.555 0.500 1 363 110 110 GLY CA C 44.183 0.500 1 364 110 110 GLY N N 101.156 0.500 1 365 111 111 LEU H H 6.199 0.050 1 366 111 111 LEU CA C 51.216 0.500 1 367 111 111 LEU CB C 39.75 0.500 1 368 111 111 LEU N N 120.251 0.500 1 369 112 112 PRO C C 175.622 0.500 1 370 112 112 PRO CA C 62.011 0.500 1 371 112 112 PRO CB C 32.01 0.500 1 372 113 113 LYS H H 8.626 0.050 1 373 113 113 LYS C C 176.453 0.500 1 374 113 113 LYS CA C 58.324 0.500 1 375 113 113 LYS CB C 31.409 0.500 1 376 113 113 LYS N N 120.696 0.500 1 377 114 114 GLU H H 8.673 0.050 1 378 114 114 GLU C C 176.347 0.500 1 379 114 114 GLU CA C 58.019 0.500 1 380 114 114 GLU CB C 27.929 0.500 1 381 114 114 GLU N N 114.91 0.500 1 382 115 115 VAL H H 7.289 0.050 1 383 115 115 VAL C C 178.51 0.500 1 384 115 115 VAL CA C 62.987 0.500 1 385 115 115 VAL CB C 29.969 0.500 1 386 115 115 VAL N N 121.082 0.500 1 387 116 116 LYS H H 8.6 0.050 1 388 116 116 LYS C C 178.268 0.500 1 389 116 116 LYS CA C 55.955 0.500 1 390 116 116 LYS CB C 32.43 0.500 1 391 116 116 LYS N N 126.071 0.500 1 392 117 117 LYS H H 7.068 0.050 1 393 117 117 LYS CA C 54.426 0.500 1 394 117 117 LYS CB C 33.27 0.500 1 395 117 117 LYS N N 112.317 0.500 1 396 119 119 SER H H 9.302 0.050 1 397 119 119 SER C C 178.963 0.500 1 398 119 119 SER CA C 58.859 0.500 1 399 119 119 SER CB C 65.671 0.500 1 400 119 119 SER N N 118.848 0.500 1 401 120 120 ALA H H 7.614 0.050 1 402 120 120 ALA C C 178.887 0.500 1 403 120 120 ALA CA C 52.133 0.500 1 404 120 120 ALA CB C 21.569 0.500 1 405 120 120 ALA N N 122.716 0.500 1 406 121 121 ALA H H 8.805 0.050 1 407 121 121 ALA C C 179.795 0.500 1 408 121 121 ALA CA C 51.674 0.500 1 409 121 121 ALA CB C 23.789 0.500 1 410 121 121 ALA N N 123.937 0.500 1 411 122 122 VAL H H 8.259 0.050 1 412 122 122 VAL CA C 59.929 0.500 1 413 122 122 VAL CB C 32.61 0.500 1 414 122 122 VAL N N 114.396 0.500 1 415 123 123 HIS C C 180.868 0.500 1 416 124 124 PHE H H 8.195 0.050 1 417 124 124 PHE C C 177.905 0.500 1 418 124 124 PHE CA C 54.732 0.500 1 419 124 124 PHE CB C 38.61 0.500 1 420 124 124 PHE N N 124.735 0.500 1 421 125 125 GLU H H 8.96 0.050 1 422 125 125 GLU C C 175.153 0.500 1 423 125 125 GLU CA C 57.942 0.500 1 424 125 125 GLU CB C 29.369 0.500 1 425 125 125 GLU N N 124.694 0.500 1 426 126 126 ASP H H 8.929 0.050 1 427 126 126 ASP C C 175.697 0.500 1 428 126 126 ASP CA C 56.108 0.500 1 429 126 126 ASP CB C 39.21 0.500 1 430 126 126 ASP N N 115.967 0.500 1 431 127 127 THR H H 7.204 0.050 1 432 127 127 THR C C 176.756 0.500 1 433 127 127 THR CA C 60.464 0.500 1 434 127 127 THR CB C 69.511 0.500 1 435 127 127 THR N N 106.013 0.500 1 436 128 128 GLY H H 8.039 0.050 1 437 128 128 GLY C C 176.363 0.500 1 438 128 128 GLY CA C 46.4 0.500 1 439 128 128 GLY N N 111.952 0.500 1 440 129 129 LYS H H 7.112 0.050 1 441 129 129 LYS C C 178.343 0.500 1 442 129 129 LYS CA C 52.476 0.500 1 443 129 129 LYS CB C 34.05 0.500 1 444 129 129 LYS N N 115.701 0.500 1 445 130 130 THR H H 9.406 0.050 1 446 130 130 THR C C 179.598 0.500 1 447 130 130 THR CA C 60.541 0.500 1 448 130 130 THR CB C 70.531 0.500 1 449 130 130 THR N N 118.98 0.500 1 450 131 131 LEU H H 9.119 0.050 1 451 131 131 LEU C C 178.857 0.500 1 452 131 131 LEU CA C 53.05 0.500 1 453 131 131 LEU CB C 41.97 0.500 1 454 131 131 LEU N N 125.364 0.500 1 455 132 132 LEU H H 8.446 0.050 1 456 132 132 LEU CA C 52.974 0.500 1 457 132 132 LEU N N 121.015 0.500 1 458 134 134 SER C C 177.814 0.500 1 459 135 135 GLY H H 9.684 0.050 1 460 135 135 GLY C C 179.598 0.500 1 461 135 135 GLY CA C 46.935 0.500 1 462 135 135 GLY N N 121.809 0.500 1 463 136 136 ASN H H 8.356 0.050 1 464 136 136 ASN CA C 51.75 0.500 1 465 136 136 ASN CB C 37.71 0.500 1 466 136 136 ASN N N 123.689 0.500 1 467 137 137 GLN CA C 54.885 0.500 1 468 137 137 GLN N N 118.862 0.500 1 469 139 139 TRP CA C 56.184 0.500 1 470 139 139 TRP N N 121.811 0.500 1 471 141 141 TYR CA C 56.49 0.500 1 472 141 141 TYR N N 129.608 0.500 1 473 142 142 ASP CA C 52.592 0.500 1 474 142 142 ASP N N 126.853 0.500 1 475 143 143 ASP N N 125.643 0.500 1 476 144 144 THR CA C 65.433 0.500 1 477 144 144 THR N N 109.591 0.500 1 478 145 145 ASN CA C 52.974 0.500 1 479 145 145 ASN N N 116.498 0.500 1 480 146 146 HIS CA C 55.97 0.500 1 481 146 146 HIS N N 117.827 0.500 1 482 147 147 ILE CA C 59.089 0.500 1 483 147 147 ILE N N 119.984 0.500 1 484 148 148 MET N N 115.783 0.500 1 485 153 153 PRO C C 178.207 0.500 1 486 153 153 PRO CA C 60.691 0.500 1 487 153 153 PRO CB C 33.99 0.500 1 488 154 154 ARG H H 8.089 0.050 1 489 154 154 ARG C C 178.147 0.500 1 490 154 154 ARG CA C 53.509 0.500 1 491 154 154 ARG CB C 33.03 0.500 1 492 154 154 ARG N N 118.043 0.500 1 493 155 155 LEU H H 8.703 0.050 1 494 155 155 LEU C C 174.367 0.500 1 495 155 155 LEU CA C 54.502 0.500 1 496 155 155 LEU CB C 40.29 0.500 1 497 155 155 LEU N N 119.984 0.500 1 498 156 156 ILE H H 8.552 0.050 1 499 156 156 ILE C C 175.959 0.500 1 500 156 156 ILE CA C 66.656 0.500 1 501 156 156 ILE CB C 38.19 0.500 1 502 156 156 ILE N N 125.904 0.500 1 503 157 157 GLU H H 8.67 0.050 1 504 157 157 GLU C C 180.396 0.500 1 505 157 157 GLU CA C 57.289 0.500 1 506 157 157 GLU CB C 29.309 0.500 1 507 157 157 GLU N N 113.576 0.500 1 508 158 158 GLU H H 7.11 0.050 1 509 158 158 GLU C C 176.353 0.500 1 510 158 158 GLU CA C 57.289 0.500 1 511 158 158 GLU CB C 28.949 0.500 1 512 158 158 GLU N N 115.735 0.500 1 513 159 159 ASP H H 6.892 0.050 1 514 159 159 ASP C C 177.198 0.500 1 515 159 159 ASP CA C 55.037 0.500 1 516 159 159 ASP CB C 41.43 0.500 1 517 159 159 ASP N N 118.48 0.500 1 518 160 160 PHE H H 8.307 0.050 1 519 160 160 PHE CA C 53.509 0.500 1 520 160 160 PHE CB C 39.09 0.500 1 521 160 160 PHE N N 117.08 0.500 1 522 161 161 PRO C C 175.621 0.500 1 523 161 161 PRO CA C 63.331 0.500 1 524 161 161 PRO CB C 30.629 0.500 1 525 162 162 GLY H H 8.067 0.050 1 526 162 162 GLY C C 178.227 0.500 1 527 162 162 GLY CA C 44.871 0.500 1 528 162 162 GLY N N 109.002 0.500 1 529 163 163 ILE H H 7.003 0.050 1 530 163 163 ILE C C 178.41 0.500 1 531 163 163 ILE CA C 60.235 0.500 1 532 163 163 ILE CB C 36.87 0.500 1 533 163 163 ILE N N 113.04 0.500 1 534 164 164 GLY H H 7.588 0.050 1 535 164 164 GLY C C 180.452 0.500 1 536 164 164 GLY CA C 43.343 0.500 1 537 164 164 GLY N N 108.138 0.500 1 538 165 165 ASP H H 7.798 0.050 1 539 165 165 ASP C C 179.424 0.500 1 540 165 165 ASP CA C 52.41 0.500 1 541 165 165 ASP CB C 40.35 0.500 1 542 165 165 ASP N N 115.329 0.500 1 543 166 166 LYS H H 7.192 0.050 1 544 166 166 LYS C C 180.184 0.500 1 545 166 166 LYS CA C 54.502 0.500 1 546 166 166 LYS CB C 34.05 0.500 1 547 166 166 LYS N N 112.74 0.500 1 548 167 167 VAL H H 8.591 0.050 1 549 167 167 VAL C C 178.551 0.500 1 550 167 167 VAL CA C 61.305 0.500 1 551 167 167 VAL CB C 34.71 0.500 1 552 167 167 VAL N N 117.455 0.500 1 553 168 168 ASP H H 9.342 0.050 1 554 168 168 ASP C C 178.227 0.500 1 555 168 168 ASP CA C 55.955 0.500 1 556 168 168 ASP CB C 41.55 0.500 1 557 168 168 ASP N N 126.89 0.500 1 558 169 169 ALA H H 7.764 0.050 1 559 169 169 ALA C C 179.001 0.500 1 560 169 169 ALA CA C 51.292 0.500 1 561 169 169 ALA CB C 19.289 0.500 1 562 169 169 ALA N N 118.057 0.500 1 563 170 170 VAL H H 8.808 0.050 1 564 170 170 VAL C C 180.494 0.500 1 565 170 170 VAL CA C 59.471 0.500 1 566 170 170 VAL CB C 32.49 0.500 1 567 170 170 VAL N N 120.472 0.500 1 568 171 171 TYR H H 8.149 0.050 1 569 171 171 TYR C C 182.917 0.500 1 570 171 171 TYR CA C 55.904 0.500 1 571 171 171 TYR N N 121.897 0.500 1 572 172 172 GLU H H 8.775 0.050 1 573 172 172 GLU C C 182.889 0.500 1 574 172 172 GLU CA C 53.399 0.500 1 575 172 172 GLU CB C 31.83 0.500 1 576 172 172 GLU N N 120.749 0.500 1 577 173 173 LYS H H 8.773 0.050 1 578 173 173 LYS C C 176.691 0.500 1 579 173 173 LYS CA C 57.025 0.500 1 580 173 173 LYS CB C 31.589 0.500 1 581 173 173 LYS N N 120.551 0.500 1 582 174 174 ASN H H 8.835 0.050 1 583 174 174 ASN CA C 54.652 0.500 1 584 174 174 ASN CB C 38.43 0.500 1 585 174 174 ASN N N 116.031 0.500 1 586 175 175 GLY C C 180.241 0.500 1 587 176 176 TYR H H 8.1 0.050 1 588 176 176 TYR C C 179.128 0.500 1 589 176 176 TYR CA C 55.649 0.500 1 590 176 176 TYR CB C 40.52 0.500 1 591 176 176 TYR N N 120.3 0.500 1 592 177 177 ILE H H 9.266 0.050 1 593 177 177 ILE C C 180.269 0.500 1 594 177 177 ILE CA C 59.853 0.500 1 595 177 177 ILE CB C 39.51 0.500 1 596 177 177 ILE N N 121.195 0.500 1 597 178 178 TYR H H 8.538 0.050 1 598 178 178 TYR C C 179.255 0.500 1 599 178 178 TYR CA C 56.566 0.500 1 600 178 178 TYR CB C 38.91 0.500 1 601 178 178 TYR N N 126.328 0.500 1 602 179 179 PHE H H 8.522 0.050 1 603 179 179 PHE C C 179.452 0.500 1 604 179 179 PHE CA C 56.49 0.500 1 605 179 179 PHE CB C 41.97 0.500 1 606 179 179 PHE N N 120.419 0.500 1 607 180 180 PHE H H 8.748 0.050 1 608 180 180 PHE C C 178.367 0.500 1 609 180 180 PHE CA C 57.101 0.500 1 610 180 180 PHE CB C 38.73 0.500 1 611 180 180 PHE N N 120.483 0.500 1 612 181 181 ASN H H 9.132 0.050 1 613 181 181 ASN C C 178.1 0.500 1 614 181 181 ASN CA C 51.684 0.500 1 615 181 181 ASN CB C 38.49 0.500 1 616 181 181 ASN N N 121.846 0.500 1 617 182 182 GLY H H 9.625 0.050 1 618 182 182 GLY CA C 44.413 0.500 1 619 182 182 GLY N N 117.619 0.500 1 620 183 183 PRO C C 176.917 0.500 1 621 183 183 PRO CA C 63.211 0.500 1 622 183 183 PRO CB C 30.449 0.500 1 623 184 184 ILE H H 7.635 0.050 1 624 184 184 ILE C C 181.367 0.500 1 625 184 184 ILE CA C 59.471 0.500 1 626 184 184 ILE CB C 40.17 0.500 1 627 184 184 ILE N N 124.202 0.500 1 628 185 185 GLN H H 8.705 0.050 1 629 185 185 GLN C C 180.706 0.500 1 630 185 185 GLN CA C 51.751 0.500 1 631 185 185 GLN CB C 30.749 0.500 1 632 185 185 GLN N N 120.775 0.500 1 633 186 186 PHE H H 9.278 0.050 1 634 186 186 PHE C C 178.621 0.500 1 635 186 186 PHE CA C 55.641 0.500 1 636 186 186 PHE CB C 41.25 0.500 1 637 186 186 PHE N N 121.015 0.500 1 638 187 187 GLU H H 8.786 0.050 1 639 187 187 GLU C C 180.086 0.500 1 640 187 187 GLU CA C 55.343 0.500 1 641 187 187 GLU CB C 31.109 0.500 1 642 187 187 GLU N N 123.186 0.500 1 643 188 188 TYR H H 9.756 0.050 1 644 188 188 TYR C C 178.212 0.500 1 645 188 188 TYR CA C 56.893 0.500 1 646 188 188 TYR N N 132.567 0.500 1 647 189 189 SER H H 8.504 0.050 1 648 189 189 SER C C 178.325 0.500 1 649 189 189 SER CA C 56.498 0.500 1 650 189 189 SER CB C 63.571 0.500 1 651 189 189 SER N N 121.28 0.500 1 652 190 190 ILE H H 8.084 0.050 1 653 190 190 ILE C C 175.48 0.500 1 654 190 190 ILE CA C 64.286 0.500 1 655 190 190 ILE CB C 37.35 0.500 1 656 190 190 ILE N N 128.77 0.500 1 657 191 191 TRP H H 7.888 0.050 1 658 191 191 TRP C C 175.536 0.500 1 659 191 191 TRP CA C 58.554 0.500 1 660 191 191 TRP CB C 28.589 0.500 1 661 191 191 TRP N N 118.769 0.500 1 662 192 192 SER H H 7.67 0.050 1 663 192 192 SER C C 179.762 0.500 1 664 192 192 SER CA C 56.893 0.500 1 665 192 192 SER CB C 63.631 0.500 1 666 192 192 SER N N 109.912 0.500 1 667 193 193 ASN H H 7.78 0.050 1 668 193 193 ASN C C 180.269 0.500 1 669 193 193 ASN CA C 53.585 0.500 1 670 193 193 ASN CB C 36.69 0.500 1 671 193 193 ASN N N 121.053 0.500 1 672 194 194 ARG H H 6.691 0.050 1 673 194 194 ARG C C 179.184 0.500 1 674 194 194 ARG CA C 53.662 0.500 1 675 194 194 ARG CB C 32.31 0.500 1 676 194 194 ARG N N 111.664 0.500 1 677 195 195 ILE H H 8.491 0.050 1 678 195 195 ILE C C 176.945 0.500 1 679 195 195 ILE CA C 61.764 0.500 1 680 195 195 ILE CB C 38.31 0.500 1 681 195 195 ILE N N 121.515 0.500 1 682 196 196 VAL H H 9.337 0.050 1 683 196 196 VAL C C 177.142 0.500 1 684 196 196 VAL CA C 62.146 0.500 1 685 196 196 VAL CB C 32.07 0.500 1 686 196 196 VAL N N 124.992 0.500 1 687 197 197 ARG H H 7.501 0.050 1 688 197 197 ARG C C 180.522 0.500 1 689 197 197 ARG CA C 55.802 0.500 1 690 197 197 ARG CB C 34.05 0.500 1 691 197 197 ARG N N 117.375 0.500 1 692 198 198 VAL H H 8.15 0.050 1 693 198 198 VAL C C 178.072 0.500 1 694 198 198 VAL CA C 60.464 0.500 1 695 198 198 VAL CB C 33.45 0.500 1 696 198 198 VAL N N 121.581 0.500 1 697 199 199 MET H H 8.85 0.050 1 698 199 199 MET CA C 53.135 0.500 1 699 199 199 MET CB C 33.81 0.500 1 700 199 199 MET N N 124.731 0.500 1 701 200 200 PRO C C 174.114 0.500 1 702 200 200 PRO CA C 62.311 0.500 1 703 200 200 PRO CB C 30.809 0.500 1 704 201 201 ALA H H 8.808 0.050 1 705 201 201 ALA C C 174.804 0.500 1 706 201 201 ALA CA C 55.343 0.500 1 707 201 201 ALA CB C 16.649 0.500 1 708 201 201 ALA N N 130.632 0.500 1 709 202 202 ASN H H 8.323 0.050 1 710 202 202 ASN C C 176.156 0.500 1 711 202 202 ASN CA C 54.256 0.500 1 712 202 202 ASN CB C 37.29 0.500 1 713 202 202 ASN N N 109.982 0.500 1 714 203 203 SER H H 7.458 0.050 1 715 203 203 SER C C 176.114 0.500 1 716 203 203 SER CA C 60.77 0.500 1 717 203 203 SER CB C 62.611 0.500 1 718 203 203 SER N N 116.628 0.500 1 719 204 204 ILE H H 7.161 0.050 1 720 204 204 ILE C C 179.987 0.500 1 721 204 204 ILE CA C 61.458 0.500 1 722 204 204 ILE CB C 37.95 0.500 1 723 204 204 ILE N N 120.23 0.500 1 724 205 205 LEU H H 6.806 0.050 1 725 205 205 LEU C C 178.367 0.500 1 726 205 205 LEU CA C 53.662 0.500 1 727 205 205 LEU CB C 39.81 0.500 1 728 205 205 LEU N N 119.438 0.500 1 729 206 206 TRP H H 7.154 0.050 1 730 206 206 TRP CA C 58.095 0.500 1 731 206 206 TRP CB C 24.209 0.500 1 732 206 206 TRP N N 111.5 0.500 1 733 207 207 CYS H H 6.699 0.050 1 734 207 207 CYS CA C 57.789 0.500 1 735 207 207 CYS CB C 41.55 0.500 1 736 207 207 CYS N N 122.395 0.500 1 stop_ save_