data_19343 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF OPA60 FROM N. GONORRHOEAE ; _BMRB_accession_number 19343 _BMRB_flat_file_name bmr19343.str _Entry_type original _Submission_date . _Accession_date . _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Old values: _Entry.Assigned_PDB_ID 2MAF _Entry.Assigned_PDB_deposition_code RCSB103410 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Columbus Linda . . 2 Fox Daniel A. . 3 Larsson Per . . 4 Lo Ryan H. . 5 Kroncke Brett M. . 6 Kasson Peter M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 "13C chemical shifts" 316 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-13 update author 'update assignments' 2014-08-05 update author 'update assignments' 2014-06-23 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the Neisserial Outer Membrane Protein Opa60: Loop Flexibility Essential to Receptor Recognition and Bacterial Engulfment' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24813921 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Columbus Linda . . 2 Fox Daniel A. . 3 Larsson Per . . 4 Lo Ryan H. . 5 Kroncke Brett M. . 6 Kasson Peter M. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'OPA60 FROM N. GONORRHOEAE' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'OPA60 FROM N. GONORRHOEAE' $OPA60 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OPA60 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common OPA60 _Molecular_mass 26655.883 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 238 _Mol_residue_sequence ; ASEDGGRGPYVQADLAYAYE HITHDYPEPTAPNKNKISTV SDYFRNIRTRSVHPRVSVGY DFGGWRIAADYARYRKWNNN KYSVNIENVRIRKENGIRID RKTENQENGTFHAVSSLGLS AIYDFQINDKFKPYIGARVA YGHVRHSIDSTKKTIEVTTV PSNAPNGAVTTYNTDPKTQN DYQSNSIRRVGLGVIAGVGF DITPKLTLDAGYRYHNWGRL ENTRFKTHEASLGVRYRF ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 GLU 4 ASP 5 GLY 6 GLY 7 ARG 8 GLY 9 PRO 10 TYR 11 VAL 12 GLN 13 ALA 14 ASP 15 LEU 16 ALA 17 TYR 18 ALA 19 TYR 20 GLU 21 HIS 22 ILE 23 THR 24 HIS 25 ASP 26 TYR 27 PRO 28 GLU 29 PRO 30 THR 31 ALA 32 PRO 33 ASN 34 LYS 35 ASN 36 LYS 37 ILE 38 SER 39 THR 40 VAL 41 SER 42 ASP 43 TYR 44 PHE 45 ARG 46 ASN 47 ILE 48 ARG 49 THR 50 ARG 51 SER 52 VAL 53 HIS 54 PRO 55 ARG 56 VAL 57 SER 58 VAL 59 GLY 60 TYR 61 ASP 62 PHE 63 GLY 64 GLY 65 TRP 66 ARG 67 ILE 68 ALA 69 ALA 70 ASP 71 TYR 72 ALA 73 ARG 74 TYR 75 ARG 76 LYS 77 TRP 78 ASN 79 ASN 80 ASN 81 LYS 82 TYR 83 SER 84 VAL 85 ASN 86 ILE 87 GLU 88 ASN 89 VAL 90 ARG 91 ILE 92 ARG 93 LYS 94 GLU 95 ASN 96 GLY 97 ILE 98 ARG 99 ILE 100 ASP 101 ARG 102 LYS 103 THR 104 GLU 105 ASN 106 GLN 107 GLU 108 ASN 109 GLY 110 THR 111 PHE 112 HIS 113 ALA 114 VAL 115 SER 116 SER 117 LEU 118 GLY 119 LEU 120 SER 121 ALA 122 ILE 123 TYR 124 ASP 125 PHE 126 GLN 127 ILE 128 ASN 129 ASP 130 LYS 131 PHE 132 LYS 133 PRO 134 TYR 135 ILE 136 GLY 137 ALA 138 ARG 139 VAL 140 ALA 141 TYR 142 GLY 143 HIS 144 VAL 145 ARG 146 HIS 147 SER 148 ILE 149 ASP 150 SER 151 THR 152 LYS 153 LYS 154 THR 155 ILE 156 GLU 157 VAL 158 THR 159 THR 160 VAL 161 PRO 162 SER 163 ASN 164 ALA 165 PRO 166 ASN 167 GLY 168 ALA 169 VAL 170 THR 171 THR 172 TYR 173 ASN 174 THR 175 ASP 176 PRO 177 LYS 178 THR 179 GLN 180 ASN 181 ASP 182 TYR 183 GLN 184 SER 185 ASN 186 SER 187 ILE 188 ARG 189 ARG 190 VAL 191 GLY 192 LEU 193 GLY 194 VAL 195 ILE 196 ALA 197 GLY 198 VAL 199 GLY 200 PHE 201 ASP 202 ILE 203 THR 204 PRO 205 LYS 206 LEU 207 THR 208 LEU 209 ASP 210 ALA 211 GLY 212 TYR 213 ARG 214 TYR 215 HIS 216 ASN 217 TRP 218 GLY 219 ARG 220 LEU 221 GLU 222 ASN 223 THR 224 ARG 225 PHE 226 LYS 227 THR 228 HIS 229 GLU 230 ALA 231 SER 232 LEU 233 GLY 234 VAL 235 ARG 236 TYR 237 ARG 238 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 PDB 2MAF "Solution Structure Of Opa60 From N. Gonorrhoeae" 100.00 238 100.00 100.00 1.29e-172 PDB 2MLH "Nmr Solution Structure Of Opa60 From N. Gonorrhoeae In Fc-12 Micelles" 100.00 238 100.00 100.00 1.29e-172 EMBL CAA43121 "opaH v18 [Neisseria gonorrhoeae]" 98.32 239 99.57 100.00 1.29e-169 EMBL CAA79372 "outer membrane protein [Neisseria gonorrhoeae]" 100.00 238 100.00 100.00 1.29e-172 GB AGU84980 "opacity protein [Neisseria gonorrhoeae MS11]" 95.80 228 99.12 100.00 4.09e-164 REF WP_017147145 "opacity-associated protein [Neisseria gonorrhoeae]" 95.80 228 99.12 100.00 4.09e-164 SP Q04884 "RecName: Full=Opacity protein opA60; Flags: Precursor, partial [Neisseria gonorrhoeae]" 100.00 238 100.00 100.00 1.29e-172 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $OPA60 'Neisseria gonorrhoeae' 485 Bacteria . Neisseria gonorrhoeae MS11 opaI 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 $OPA60 'recombinant technology' . Escherichia coli BL21(DE3) pET28b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $OPA60 800 uM '[U-100% 13C; U-100% 15N; U-80% 2H]' 'Dodecyl Phosphcholine' 150 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version 2.31 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4.2 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_GROMACS _Saveframe_category software _Name GROMACS _Version 4.5 loop_ _Vendor _Address _Electronic_address Lindahl . . stop_ loop_ _Task refinement stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 7.9 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600_MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details Cryoprobe save_ save_800_MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details Cryoprobe 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_HN(COCA)CB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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 temperature 313 . K pH 6.2 . pH pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'OPA60 FROM N. GONORRHOEAE' _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 ALA H H 8.45 0.02 1 2 1 1 ALA C C 178.366 0.3 1 3 1 1 ALA CA C 52.732 0.3 1 4 1 1 ALA CB C 18.62 0.3 1 5 1 1 ALA N N 125.12 0.3 1 6 2 2 SER H H 8.331 0.02 1 7 2 2 SER C C 175.434 0.3 1 8 2 2 SER CA C 58.61 0.3 1 9 2 2 SER CB C 63.837 0.3 1 10 2 2 SER N N 114.852 0.3 1 11 3 3 GLU H H 8.593 0.02 1 12 3 3 GLU C C 177.0 0.3 1 13 3 3 GLU CA C 56.833 0.3 1 14 3 3 GLU CB C 29.05 0.3 1 15 3 3 GLU N N 122.794 0.3 1 16 4 4 ASP H H 8.366 0.02 1 17 4 4 ASP C C 177.663 0.3 1 18 4 4 ASP CA C 56.351 0.3 1 19 4 4 ASP CB C 40.904 0.3 1 20 4 4 ASP N N 120.891 0.3 1 21 5 5 GLY H H 8.55 0.02 1 22 5 5 GLY C C 175.521 0.3 1 23 5 5 GLY CA C 45.33 0.3 1 24 5 5 GLY N N 110.851 0.3 1 25 6 6 GLY H H 8.449 0.02 1 26 6 6 GLY C C 173.807 0.3 1 27 6 6 GLY CA C 45.575 0.3 1 28 6 6 GLY N N 109.418 0.3 1 29 7 7 ARG H H 7.581 0.02 1 30 7 7 ARG C C 177.151 0.3 1 31 7 7 ARG CA C 55.066 0.3 1 32 7 7 ARG CB C 31.412 0.3 1 33 7 7 ARG N N 117.808 0.3 1 34 8 8 GLY H H 8.297 0.02 1 35 8 8 GLY CA C 44.677 0.3 1 36 8 8 GLY N N 109.915 0.3 1 37 9 9 PRO C C 175.944 0.3 1 38 9 9 PRO CA C 62.38 0.3 1 39 9 9 PRO CB C 32.521 0.3 1 40 10 10 TYR H H 8.847 0.02 1 41 10 10 TYR C C 173.151 0.3 1 42 10 10 TYR CA C 56.647 0.3 1 43 10 10 TYR CB C 41.002 0.3 1 44 10 10 TYR N N 115.969 0.3 1 45 11 11 VAL H H 8.882 0.02 1 46 11 11 VAL C C 174.053 0.3 1 47 11 11 VAL CA C 59.14 0.3 1 48 11 11 VAL CB C 34.77 0.3 1 49 11 11 VAL N N 114.755 0.3 1 50 12 12 GLN H H 9.252 0.02 1 51 12 12 GLN C C 174.087 0.3 1 52 12 12 GLN CA C 54.194 0.3 1 53 12 12 GLN CB C 31.644 0.3 1 54 12 12 GLN N N 126.391 0.3 1 55 13 13 ALA H H 8.692 0.02 1 56 13 13 ALA C C 174.387 0.3 1 57 13 13 ALA CA C 50.805 0.3 1 58 13 13 ALA CB C 20.76 0.3 1 59 13 13 ALA N N 127.788 0.3 1 60 14 14 ASP H H 9.041 0.02 1 61 14 14 ASP C C 176.1 0.3 1 62 14 14 ASP CA C 52.875 0.3 1 63 14 14 ASP CB C 45.821 0.3 1 64 14 14 ASP N N 118.37 0.3 1 65 29 29 PRO C C 177.686 0.3 1 66 29 29 PRO CA C 63.798 0.3 1 67 29 29 PRO CB C 28.501 0.02 1 68 30 30 THR H H 8.25 0.02 1 69 30 30 THR C C 174.747 0.3 1 70 30 30 THR CA C 61.999 0.3 1 71 30 30 THR CB C 69.429 0.3 1 72 30 30 THR N N 114.503 0.3 1 73 31 31 ALA H H 8.313 0.02 1 74 31 31 ALA C C 176.44 0.3 1 75 31 31 ALA CA C 50.66 0.3 1 76 31 31 ALA CB C 17.524 0.3 1 77 31 31 ALA N N 127.406 0.3 1 78 51 51 SER H H 8.2 0.02 1 79 51 51 SER C C 174.792 0.3 1 80 51 51 SER CA C 61.751 0.3 1 81 51 51 SER CB C 69.538 0.3 1 82 51 51 SER N N 113.737 0.3 1 83 52 52 VAL H H 8.226 0.02 1 84 52 52 VAL C C 175.153 0.3 1 85 52 52 VAL CA C 59.798 0.3 1 86 52 52 VAL CB C 31.878 0.3 1 87 52 52 VAL N N 123.687 0.3 1 88 57 57 SER H H 9.29 0.02 1 89 57 57 SER C C 173.257 0.3 1 90 57 57 SER CA C 57.391 0.3 1 91 57 57 SER CB C 66.123 0.3 1 92 57 57 SER N N 117.736 0.3 1 93 58 58 VAL H H 8.892 0.02 1 94 58 58 VAL C C 174.287 0.3 1 95 58 58 VAL CA C 60.05 0.3 1 96 58 58 VAL CB C 33.997 0.3 1 97 58 58 VAL N N 120.059 0.3 1 98 59 59 GLY H H 8.165 0.02 1 99 59 59 GLY C C 171.019 0.3 1 100 59 59 GLY CA C 45.571 0.3 1 101 59 59 GLY N N 111.967 0.3 1 102 60 60 TYR H H 9.124 0.02 1 103 60 60 TYR C C 173.063 0.3 1 104 60 60 TYR CA C 58.122 0.3 1 105 60 60 TYR CB C 42.79 0.3 1 106 60 60 TYR N N 119.581 0.3 1 107 61 61 ASP H H 8.173 0.02 1 108 61 61 ASP C C 175.411 0.3 1 109 61 61 ASP CA C 52.492 0.3 1 110 61 61 ASP CB C 41.851 0.3 1 111 61 61 ASP N N 127.261 0.3 1 112 62 62 PHE H H 9.084 0.02 1 113 62 62 PHE C C 176.679 0.3 1 114 62 62 PHE CA C 59.644 0.3 1 115 62 62 PHE CB C 38.241 0.3 1 116 62 62 PHE N N 122.821 0.3 1 117 63 63 GLY H H 9.6 0.02 1 118 63 63 GLY C C 174.776 0.3 1 119 63 63 GLY CA C 46.663 0.3 1 120 63 63 GLY N N 113.407 0.3 1 121 64 64 GLY H H 8.986 0.02 1 122 64 64 GLY C C 172.481 0.3 1 123 64 64 GLY CA C 45.674 0.3 1 124 64 64 GLY N N 114.349 0.3 1 125 65 65 TRP H H 7.569 0.02 1 126 65 65 TRP C C 175.076 0.3 1 127 65 65 TRP CA C 55.987 0.3 1 128 65 65 TRP CB C 30.499 0.3 1 129 65 65 TRP N N 116.89 0.3 1 130 66 66 ARG H H 9.936 0.02 1 131 66 66 ARG C C 175.595 0.3 1 132 66 66 ARG CA C 55.166 0.3 1 133 66 66 ARG CB C 34.96 0.3 1 134 66 66 ARG N N 119.274 0.3 1 135 67 67 ILE H H 8.47 0.02 1 136 67 67 ILE C C 175.118 0.3 1 137 67 67 ILE CA C 58.77 0.3 1 138 67 67 ILE CB C 40.542 0.3 1 139 67 67 ILE N N 118.386 0.3 1 140 68 68 ALA H H 8.66 0.02 1 141 68 68 ALA C C 177.247 0.3 1 142 68 68 ALA CA C 51.727 0.3 1 143 68 68 ALA CB C 22.036 0.3 1 144 68 68 ALA N N 124.102 0.3 1 145 69 69 ALA H H 9.572 0.02 1 146 69 69 ALA C C 176.223 0.3 1 147 69 69 ALA CA C 49.95 0.3 1 148 69 69 ALA CB C 20.171 0.3 1 149 69 69 ALA N N 128.725 0.3 1 150 70 70 ASP H H 9.475 0.02 1 151 70 70 ASP C C 174.034 0.3 1 152 70 70 ASP CA C 52.369 0.3 1 153 70 70 ASP CB C 45.779 0.3 1 154 70 70 ASP N N 118.233 0.3 1 155 71 71 TYR H H 9.243 0.02 1 156 71 71 TYR C C 173.769 0.3 1 157 71 71 TYR CA C 57.126 0.3 1 158 71 71 TYR N N 118.228 0.3 1 159 95 95 ASN H H 8.393 0.02 1 160 95 95 ASN C C 177.514 0.3 1 161 95 95 ASN CA C 54.591 0.3 1 162 95 95 ASN CB C 40.573 0.3 1 163 95 95 ASN N N 119.591 0.3 1 164 96 96 GLY H H 8.34 0.02 1 165 96 96 GLY C C 174.697 0.3 1 166 96 96 GLY CA C 45.615 0.3 1 167 96 96 GLY N N 109.334 0.3 1 168 97 97 ILE H H 8.003 0.02 1 169 97 97 ILE CA C 61.288 0.3 1 170 97 97 ILE N N 119.953 0.3 1 171 109 109 GLY H H 8.315 0.02 1 172 109 109 GLY C C 174.875 0.3 1 173 109 109 GLY CA C 45.433 0.3 1 174 109 109 GLY N N 114.84 0.3 1 175 110 110 THR H H 8.282 0.02 1 176 110 110 THR C C 175.334 0.3 1 177 110 110 THR CA C 58.642 0.3 1 178 110 110 THR CB C 63.947 0.3 1 179 110 110 THR N N 115.92 0.3 1 180 118 118 GLY H H 9.424 0.02 1 181 118 118 GLY C C 171.826 0.3 1 182 118 118 GLY CA C 44.29 0.3 1 183 118 118 GLY N N 115.009 0.3 1 184 119 119 LEU H H 9.181 0.02 1 185 119 119 LEU C C 175.499 0.3 1 186 119 119 LEU CA C 54.018 0.3 1 187 119 119 LEU CB C 45.572 0.3 1 188 119 119 LEU N N 119.633 0.3 1 189 120 120 SER H H 9.152 0.02 1 190 120 120 SER C C 173.046 0.3 1 191 120 120 SER CA C 57.454 0.3 1 192 120 120 SER CB C 65.655 0.3 1 193 120 120 SER N N 118.198 0.3 1 194 121 121 ALA H H 8.726 0.02 1 195 121 121 ALA C C 176.277 0.3 1 196 121 121 ALA CA C 50.935 0.3 1 197 121 121 ALA CB C 20.3 0.3 1 198 121 121 ALA N N 125.527 0.3 1 199 122 122 ILE H H 9.499 0.02 1 200 122 122 ILE C C 173.875 0.3 1 201 122 122 ILE CA C 61.257 0.3 1 202 122 122 ILE CB C 41.973 0.3 1 203 122 122 ILE N N 121.964 0.3 1 204 123 123 TYR H H 9.576 0.02 1 205 123 123 TYR C C 174.052 0.3 1 206 123 123 TYR CA C 57.492 0.3 1 207 123 123 TYR CB C 41.416 0.3 1 208 123 123 TYR N N 128.727 0.3 1 209 124 124 ASP H H 7.767 0.02 1 210 124 124 ASP C C 175.217 0.3 1 211 124 124 ASP CA C 53.534 0.3 1 212 124 124 ASP CB C 43.131 0.3 1 213 124 124 ASP N N 125.662 0.3 1 214 125 125 PHE H H 9.213 0.02 1 215 125 125 PHE C C 176.347 0.3 1 216 125 125 PHE CA C 57.665 0.3 1 217 125 125 PHE CB C 39.719 0.3 1 218 125 125 PHE N N 121.435 0.3 1 219 126 126 GLN H H 8.929 0.02 1 220 126 126 GLN C C 176.717 0.3 1 221 126 126 GLN CA C 55.054 0.3 1 222 126 126 GLN CB C 27.334 0.3 1 223 126 126 GLN N N 122.72 0.3 1 224 127 127 ILE H H 8.267 0.02 1 225 127 127 ILE C C 175.87 0.3 1 226 127 127 ILE CA C 61.837 0.3 1 227 127 127 ILE CB C 37.631 0.3 1 228 127 127 ILE N N 120.01 0.3 1 229 128 128 ASN H H 8.342 0.02 1 230 128 128 ASN C C 174.334 0.3 1 231 128 128 ASN CA C 53.316 0.3 1 232 128 128 ASN CB C 39.409 0.3 1 233 128 128 ASN N N 118.359 0.3 1 234 129 129 ASP H H 8.632 0.02 1 235 129 129 ASP C C 176.841 0.3 1 236 129 129 ASP CA C 56.154 0.3 1 237 129 129 ASP CB C 40.406 0.3 1 238 129 129 ASP N N 117.685 0.3 1 239 130 130 LYS H H 8.571 0.02 1 240 130 130 LYS C C 176.011 0.3 1 241 130 130 LYS CA C 56.924 0.3 1 242 130 130 LYS CB C 33.895 0.3 1 243 130 130 LYS N N 116.361 0.3 1 244 131 131 PHE H H 8.112 0.02 1 245 131 131 PHE C C 174.776 0.3 1 246 131 131 PHE CA C 56.891 0.3 1 247 131 131 PHE CB C 40.466 0.3 1 248 131 131 PHE N N 118.309 0.3 1 249 132 132 LYS H H 8.974 0.02 1 250 132 132 LYS C C 176.029 0.3 1 251 132 132 LYS CA C 53.437 0.3 1 252 132 132 LYS CB C 33.453 0.3 1 253 132 132 LYS N N 121.819 0.3 1 254 133 133 PRO C C 173.716 0.3 1 255 133 133 PRO CA C 62.78 0.3 1 256 133 133 PRO CB C 32.095 0.3 1 257 134 134 TYR H H 8.905 0.02 1 258 134 134 TYR C C 174.016 0.3 1 259 134 134 TYR CA C 56.37 0.3 1 260 134 134 TYR CB C 41.993 0.3 1 261 134 134 TYR N N 117.842 0.3 1 262 135 135 ILE H H 8.79 0.02 1 263 135 135 ILE C C 174.246 0.3 1 264 135 135 ILE CA C 58.982 0.3 1 265 135 135 ILE CB C 42.685 0.3 1 266 135 135 ILE N N 114.98 0.3 1 267 136 136 GLY H H 9.48 0.02 1 268 136 136 GLY C C 171.642 0.3 1 269 136 136 GLY CA C 46.934 0.3 1 270 136 136 GLY N N 111.712 0.3 1 271 137 137 ALA H H 8.796 0.02 1 272 137 137 ALA C C 175.323 0.3 1 273 137 137 ALA CA C 50.366 0.3 1 274 137 137 ALA CB C 22.064 0.3 1 275 137 137 ALA N N 120.962 0.3 1 276 138 138 ARG H H 8.433 0.02 1 277 138 138 ARG C C 174.44 0.3 1 278 138 138 ARG CA C 55.088 0.3 1 279 138 138 ARG CB C 32.787 0.3 1 280 138 138 ARG N N 121.465 0.3 1 281 139 139 VAL H H 9.163 0.02 1 282 139 139 VAL C C 173.787 0.3 1 283 139 139 VAL CA C 58.665 0.3 1 284 139 139 VAL CB C 34.261 0.3 1 285 139 139 VAL N N 125.073 0.3 1 286 140 140 ALA H H 8.821 0.02 1 287 140 140 ALA C C 176.929 0.3 1 288 140 140 ALA CA C 50.949 0.3 1 289 140 140 ALA CB C 22.578 0.3 1 290 140 140 ALA N N 123.524 0.3 1 291 157 157 VAL H H 8.27 0.02 1 292 157 157 VAL C C 175.063 0.3 1 293 157 157 VAL CA C 62.019 0.3 1 294 157 157 VAL N N 116.065 0.3 1 295 159 159 THR H H 8.243 0.02 1 296 159 159 THR C C 176.622 0.3 1 297 159 159 THR CA C 61.897 0.3 1 298 159 159 THR CB C 69.477 0.3 1 299 159 159 THR N N 117.027 0.3 1 300 160 160 VAL H H 8.527 0.02 1 301 160 160 VAL C C 177.14 0.3 1 302 160 160 VAL CA C 56.845 0.3 1 303 160 160 VAL CB C 29.394 0.3 1 304 160 160 VAL N N 123.139 0.3 1 305 161 161 PRO C C 177.568 0.3 1 306 161 161 PRO CA C 63.531 0.3 1 307 161 161 PRO CB C 31.329 0.3 1 308 162 162 SER H H 8.436 0.02 1 309 162 162 SER C C 175.042 0.3 1 310 162 162 SER CA C 58.554 0.3 1 311 162 162 SER CB C 63.934 0.3 1 312 162 162 SER N N 115.87 0.3 1 313 163 163 ASN H H 8.466 0.02 1 314 163 163 ASN C C 175.683 0.3 1 315 163 163 ASN CA C 53.351 0.3 1 316 163 163 ASN CB C 38.656 0.3 1 317 163 163 ASN N N 120.667 0.3 1 318 164 164 ALA H H 8.227 0.02 1 319 164 164 ALA C C 176.372 0.3 1 320 164 164 ALA CA C 50.619 0.3 1 321 164 164 ALA CB C 17.815 0.3 1 322 164 164 ALA N N 124.946 0.3 1 323 165 165 PRO C C 176.557 0.3 1 324 165 165 PRO CA C 63.666 0.3 1 325 165 165 PRO CB C 31.072 0.3 1 326 166 166 ASN H H 8.051 0.02 1 327 166 166 ASN C C 177.248 0.3 1 328 166 166 ASN CA C 55.152 0.3 1 329 166 166 ASN CB C 40.764 0.3 1 330 166 166 ASN N N 124.475 0.3 1 331 167 167 GLY H H 8.402 0.02 1 332 167 167 GLY C C 174.773 0.3 1 333 167 167 GLY CA C 45.662 0.3 1 334 167 167 GLY N N 110.212 0.3 1 335 168 168 ALA H H 8.365 0.02 1 336 168 168 ALA C C 178.532 0.3 1 337 168 168 ALA CA C 52.44 0.3 1 338 168 168 ALA CB C 18.569 0.3 1 339 168 168 ALA N N 123.653 0.3 1 340 169 169 VAL H H 8.213 0.02 1 341 169 169 VAL C C 177.117 0.3 1 342 169 169 VAL CA C 62.438 0.3 1 343 169 169 VAL CB C 31.959 0.3 1 344 169 169 VAL N N 119.182 0.3 1 345 170 170 THR H H 8.314 0.02 1 346 170 170 THR C C 175.078 0.3 1 347 170 170 THR CA C 61.635 0.3 1 348 170 170 THR CB C 69.477 0.3 1 349 170 170 THR N N 118.011 0.3 1 350 171 171 THR H H 8.146 0.02 1 351 171 171 THR C C 176.816 0.3 1 352 171 171 THR CA C 62.259 0.3 1 353 171 171 THR CB C 69.477 0.3 1 354 171 171 THR N N 116.394 0.3 1 355 172 172 TYR H H 8.312 0.02 1 356 172 172 TYR C C 176.286 0.3 1 357 172 172 TYR CA C 56.261 0.3 1 358 172 172 TYR N N 121.464 0.3 1 359 173 173 ASN H H 8.471 0.02 1 360 173 173 ASN C C 175.672 0.3 1 361 173 173 ASN CA C 53.617 0.3 1 362 173 173 ASN CB C 38.681 0.3 1 363 173 173 ASN N N 119.854 0.3 1 364 174 174 THR H H 8.156 0.02 1 365 174 174 THR C C 174.634 0.3 1 366 174 174 THR CA C 61.908 0.3 1 367 174 174 THR CB C 69.397 0.3 1 368 174 174 THR N N 114.27 0.3 1 369 175 175 ASP H H 8.382 0.02 1 370 175 175 ASP C C 175.537 0.3 1 371 175 175 ASP CA C 52.364 0.3 1 372 175 175 ASP CB C 40.674 0.3 1 373 175 175 ASP N N 124.265 0.3 1 374 176 176 PRO C C 178.033 0.3 1 375 176 176 PRO CA C 64.103 0.3 1 376 176 176 PRO CB C 31.347 0.3 1 377 177 177 LYS H H 8.524 0.02 1 378 177 177 LYS C C 177.982 0.3 1 379 177 177 LYS CA C 57.038 0.3 1 380 177 177 LYS CB C 31.397 0.3 1 381 177 177 LYS N N 119.424 0.3 1 382 178 178 THR H H 8.06 0.02 1 383 178 178 THR C C 175.486 0.3 1 384 178 178 THR CA C 62.259 0.3 1 385 178 178 THR CB C 69.557 0.3 1 386 178 178 THR N N 113.513 0.3 1 387 190 190 VAL H H 9.585 0.02 1 388 190 190 VAL C C 174.758 0.3 1 389 190 190 VAL CA C 62.426 0.3 1 390 190 190 VAL CB C 31.878 0.3 1 391 190 190 VAL N N 127.004 0.3 1 392 191 191 GLY H H 8.71 0.02 1 393 191 191 GLY C C 172.392 0.3 1 394 191 191 GLY CA C 44.631 0.3 1 395 191 191 GLY N N 114.195 0.3 1 396 192 192 LEU H H 7.814 0.02 1 397 192 192 LEU C C 175.446 0.3 1 398 192 192 LEU CA C 53.632 0.3 1 399 192 192 LEU CB C 46.647 0.3 1 400 192 192 LEU N N 120.017 0.3 1 401 193 193 GLY H H 9.258 0.02 1 402 193 193 GLY C C 172.428 0.3 1 403 193 193 GLY CA C 46.071 0.3 1 404 193 193 GLY N N 109.61 0.3 1 405 194 194 VAL H H 8.769 0.02 1 406 194 194 VAL C C 174.37 0.3 1 407 194 194 VAL CA C 59.907 0.3 1 408 194 194 VAL CB C 35.673 0.3 1 409 194 194 VAL N N 114.126 0.3 1 410 195 195 ILE H H 8.698 0.02 1 411 195 195 ILE C C 174.087 0.3 1 412 195 195 ILE CA C 58.698 0.3 1 413 195 195 ILE CB C 40.126 0.3 1 414 195 195 ILE N N 118.306 0.3 1 415 196 196 ALA H H 9.311 0.02 1 416 196 196 ALA C C 175.775 0.3 1 417 196 196 ALA CA C 51.657 0.3 1 418 196 196 ALA CB C 22.347 0.3 1 419 196 196 ALA N N 123.076 0.3 1 420 197 197 GLY H H 7.573 0.02 1 421 197 197 GLY C C 171.97 0.3 1 422 197 197 GLY CA C 46.636 0.3 1 423 197 197 GLY N N 106.713 0.3 1 424 198 198 VAL H H 9.444 0.02 1 425 198 198 VAL C C 173.452 0.3 1 426 198 198 VAL CA C 60.905 0.3 1 427 198 198 VAL CB C 35.299 0.3 1 428 198 198 VAL N N 115.826 0.3 1 429 199 199 GLY H H 8.007 0.02 1 430 199 199 GLY C C 173.36 0.3 1 431 199 199 GLY CA C 43.667 0.3 1 432 199 199 GLY N N 111.96 0.3 1 433 200 200 PHE H H 9.479 0.02 1 434 200 200 PHE C C 175.233 0.3 1 435 200 200 PHE CA C 55.778 0.3 1 436 200 200 PHE CB C 41.971 0.3 1 437 200 200 PHE N N 123.684 0.3 1 438 201 201 ASP H H 8.849 0.02 1 439 201 201 ASP C C 174.97 0.3 1 440 201 201 ASP CA C 55.157 0.3 1 441 201 201 ASP CB C 38.632 0.3 1 442 201 201 ASP N N 130.386 0.3 1 443 202 202 ILE H H 8.646 0.02 1 444 202 202 ILE C C 176.841 0.3 1 445 202 202 ILE CA C 63.05 0.3 1 446 202 202 ILE CB C 38.361 0.3 1 447 202 202 ILE N N 124.928 0.3 1 448 203 203 THR H H 8.472 0.02 1 449 203 203 THR C C 173.505 0.3 1 450 203 203 THR CA C 59.322 0.3 1 451 203 203 THR CB C 68.634 0.3 1 452 203 203 THR N N 112.006 0.3 1 453 204 204 PRO C C 177.459 0.3 1 454 204 204 PRO CA C 65.387 0.3 1 455 204 204 PRO CB C 31.55 0.3 1 456 205 205 LYS H H 7.801 0.02 1 457 205 205 LYS C C 175.235 0.3 1 458 205 205 LYS CA C 56.124 0.3 1 459 205 205 LYS CB C 33.189 0.3 1 460 205 205 LYS N N 111.965 0.3 1 461 206 206 LEU H H 7.584 0.02 1 462 206 206 LEU C C 175.976 0.3 1 463 206 206 LEU CA C 54.109 0.3 1 464 206 206 LEU CB C 45.105 0.3 1 465 206 206 LEU N N 121.328 0.3 1 466 207 207 THR H H 9.192 0.02 1 467 207 207 THR C C 174.158 0.3 1 468 207 207 THR CA C 62.017 0.3 1 469 207 207 THR CB C 72.182 0.3 1 470 207 207 THR N N 123.091 0.3 1 471 208 208 LEU H H 9.418 0.02 1 472 208 208 LEU C C 174.828 0.3 1 473 208 208 LEU CA C 54.127 0.3 1 474 208 208 LEU CB C 43.177 0.3 1 475 208 208 LEU N N 128.382 0.3 1 476 209 209 ASP H H 9.155 0.02 1 477 209 209 ASP C C 175.876 0.3 1 478 209 209 ASP CA C 53.112 0.3 1 479 209 209 ASP CB C 45.149 0.3 1 480 209 209 ASP N N 127.139 0.3 1 481 210 210 ALA H H 9.03 0.02 1 482 210 210 ALA C C 175.876 0.3 1 483 210 210 ALA CA C 50.451 0.3 1 484 210 210 ALA CB C 19.968 0.3 1 485 210 210 ALA N N 131.933 0.3 1 486 211 211 GLY H H 8.963 0.02 1 487 211 211 GLY C C 171.654 0.3 1 488 211 211 GLY CA C 45.896 0.3 1 489 211 211 GLY N N 107.876 0.3 1 490 212 212 TYR H H 9.675 0.02 1 491 212 212 TYR C C 175.287 0.3 1 492 212 212 TYR CA C 55.861 0.3 1 493 212 212 TYR CB C 42.69 0.3 1 494 212 212 TYR N N 120.649 0.3 1 495 231 231 SER H H 9.663 0.02 1 496 231 231 SER C C 172.475 0.3 1 497 231 231 SER CA C 57.333 0.3 1 498 231 231 SER CB C 63.387 0.3 1 499 231 231 SER N N 113.24 0.3 1 500 233 233 GLY H H 9.209 0.02 1 501 233 233 GLY C C 173.063 0.3 1 502 233 233 GLY CA C 46.307 0.3 1 503 233 233 GLY N N 112.364 0.3 1 504 234 234 VAL H H 8.647 0.02 1 505 234 234 VAL C C 174.052 0.3 1 506 234 234 VAL CA C 59.15 0.3 1 507 234 234 VAL CB C 34.744 0.3 1 508 234 234 VAL N N 114.067 0.3 1 509 235 235 ARG H H 9.454 0.02 1 510 235 235 ARG C C 174.723 0.3 1 511 235 235 ARG CA C 53.493 0.3 1 512 235 235 ARG CB C 32.045 0.3 1 513 235 235 ARG N N 124.171 0.3 1 514 236 236 TYR H H 9.462 0.02 1 515 236 236 TYR C C 174.26 0.3 1 516 236 236 TYR CA C 56.355 0.3 1 517 236 236 TYR CB C 41.543 0.3 1 518 236 236 TYR N N 125.851 0.3 1 519 237 237 ARG H H 8.227 0.02 1 520 237 237 ARG C C 174.405 0.3 1 521 237 237 ARG CA C 54.973 0.3 1 522 237 237 ARG CB C 30.2 0.3 1 523 237 237 ARG N N 128.757 0.3 1 524 238 238 PHE H H 7.537 0.02 1 525 238 238 PHE C C 181.184 0.3 1 526 238 238 PHE CA C 59.949 0.3 1 527 238 238 PHE CB C 39.934 0.3 1 528 238 238 PHE N N 125.181 0.3 1 stop_ save_