data_25032 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira ; _BMRB_accession_number 25032 _BMRB_flat_file_name bmr25032.str _Entry_type original _Submission_date 2014-06-19 _Accession_date 2014-06-19 _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 Mei Song . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 411 "13C chemical shifts" 193 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-07-14 original author . stop_ _Original_release_date 2014-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mei Song . . stop_ _Journal_abbreviation 'Not known' _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 'bacterial immunoglobulin-like domain form a surface protein of Leptospira' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'surface protein of Leptospira' $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 10426.439 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; ENIDITVSAATLSSISISPI NTNINTTVSKQFFAVGTYSD GTKADLTSSVTWSSSNQSQA KVSNASETKGLVTGIASGNP TIIATYGSVSGNTILTVNKT DT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLU 2 2 ASN 3 3 ILE 4 4 ASP 5 5 ILE 6 6 THR 7 7 VAL 8 8 SER 9 9 ALA 10 10 ALA 11 11 THR 12 12 LEU 13 13 SER 14 14 SER 15 15 ILE 16 16 SER 17 17 ILE 18 18 SER 19 19 PRO 20 20 ILE 21 21 ASN 22 22 THR 23 23 ASN 24 24 ILE 25 25 ASN 26 26 THR 27 27 THR 28 28 VAL 29 29 SER 30 30 LYS 31 31 GLN 32 32 PHE 33 33 PHE 34 34 ALA 35 35 VAL 36 36 GLY 37 37 THR 38 38 TYR 39 39 SER 40 40 ASP 41 41 GLY 42 42 THR 43 43 LYS 44 44 ALA 45 45 ASP 46 46 LEU 47 47 THR 48 48 SER 49 49 SER 50 50 VAL 51 51 THR 52 52 TRP 53 53 SER 54 54 SER 55 55 SER 56 56 ASN 57 57 GLN 58 58 SER 59 59 GLN 60 60 ALA 61 61 LYS 62 62 VAL 63 63 SER 64 64 ASN 65 65 ALA 66 66 SER 67 67 GLU 68 68 THR 69 69 LYS 70 70 GLY 71 71 LEU 72 72 VAL 73 73 THR 74 74 GLY 75 75 ILE 76 76 ALA 77 77 SER 78 78 GLY 79 79 ASN 80 80 PRO 81 81 THR 82 82 ILE 83 83 ILE 84 84 ALA 85 85 THR 86 86 TYR 87 87 GLY 88 88 SER 89 89 VAL 90 90 SER 91 91 GLY 92 92 ASN 93 93 THR 94 94 ILE 95 95 LEU 96 96 THR 97 97 VAL 98 98 ASN 99 99 LYS 100 100 THR 101 101 ASP 102 102 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19942 entity 93.14 95 100.00 100.00 1.83e-55 PDB 2MOG "Solution Structure Of The Terminal Ig-like Domain From Leptospira Interrogans Ligb" 93.14 95 100.00 100.00 1.83e-55 PDB 2MQG "Solution Structure Of A Bacterial Immunoglobulin-like Domain Form A Surface Protein Of Leptospira" 100.00 102 100.00 100.00 1.13e-60 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 $entity spirochetes 44276 Bacteria . Leptospira interrogans Pomona 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 $entity 'recombinant technology' . Escherichia coli . PQE30 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 H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 AMX _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 293 . K pH 6.5 . pH pressure 1 . atm 'ionic strength' 100 . mM 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 H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0 internal direct . . . 0.25144953 DSS N 15 'methyl protons' ppm 0 internal direct . . . 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 $chemical_shift_reference_1 _Mol_system_component_name 'surface protein of Leptospira' _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 GLU HA H 4.244 . . 2 1 1 GLU HB2 H 2.002 . . 3 1 1 GLU HB3 H 2.002 . . 4 1 1 GLU HG2 H 2.226 . . 5 1 1 GLU HG3 H 2.226 . . 6 1 1 GLU H H 8.652 . . 7 1 1 GLU CA C 56.895 . . 8 1 1 GLU CB C 30.022 . . 9 1 1 GLU N N 122.336 . . 10 2 2 ASN H H 8.473 . . 11 2 2 ASN HA H 4.660 . . 12 2 2 ASN HB2 H 2.739 . . 13 2 2 ASN HB3 H 2.686 . . 14 2 2 ASN CA C 53.375 . . 15 2 2 ASN CB C 38.819 . . 16 2 2 ASN N N 119.538 . . 17 3 3 ILE H H 8.075 . . 18 3 3 ILE HA H 4.134 . . 19 3 3 ILE HB H 1.815 . . 20 3 3 ILE HG2 H 1.097 . . 21 3 3 ILE HD1 H 0.823 . . 22 3 3 ILE CA C 61.242 . . 23 3 3 ILE CB C 38.795 . . 24 3 3 ILE N N 120.822 . . 25 4 4 ASP H H 8.438 . . 26 4 4 ASP HA H 4.621 . . 27 4 4 ASP HB2 H 2.701 . . 28 4 4 ASP HB3 H 2.549 . . 29 4 4 ASP CA C 54.259 . . 30 4 4 ASP CB C 41.158 . . 31 4 4 ASP N N 124.424 . . 32 5 5 ILE H H 8.142 . . 33 5 5 ILE HA H 4.223 . . 34 5 5 ILE HB H 1.898 . . 35 5 5 ILE HG12 H 1.366 . . 36 5 5 ILE HD1 H 0.853 . . 37 5 5 ILE CA C 61.492 . . 38 5 5 ILE CB C 38.607 . . 39 5 5 ILE N N 121.072 . . 40 6 6 THR H H 8.367 . . 41 6 6 THR HA H 4.278 . . 42 6 6 THR HB H 4.124 . . 43 6 6 THR HG2 H 1.149 . . 44 6 6 THR CA C 62.425 . . 45 6 6 THR CB C 69.891 . . 46 6 6 THR N N 118.243 . . 47 7 7 VAL H H 8.095 . . 48 7 7 VAL HA H 4.105 . . 49 7 7 VAL HB H 2.038 . . 50 7 7 VAL HG2 H 0.880 . . 51 7 7 VAL CA C 62.314 . . 52 7 7 VAL CB C 32.653 . . 53 7 7 VAL N N 122.730 . . 54 8 8 SER H H 8.352 . . 55 8 8 SER HA H 4.390 . . 56 8 8 SER HB2 H 3.771 . . 57 8 8 SER HB3 H 3.771 . . 58 8 8 SER CA C 58.148 . . 59 8 8 SER CB C 63.988 . . 60 8 8 SER N N 119.723 . . 61 9 9 ALA H H 8.365 . . 62 9 9 ALA HA H 4.264 . . 63 9 9 ALA HB H 1.342 . . 64 9 9 ALA CA C 52.201 . . 65 9 9 ALA CB C 19.233 . . 66 9 9 ALA N N 126.516 . . 67 10 10 ALA H H 8.342 . . 68 10 10 ALA HA H 4.212 . . 69 10 10 ALA HB H 1.340 . . 70 10 10 ALA CA C 52.361 . . 71 10 10 ALA CB C 19.534 . . 72 10 10 ALA N N 123.691 . . 73 11 11 THR H H 8.547 . . 74 11 11 THR HA H 4.609 . . 75 11 11 THR HB H 4.167 . . 76 11 11 THR HG2 H 1.193 . . 77 11 11 THR CA C 60.251 . . 78 11 11 THR CB C 71.167 . . 79 11 11 THR N N 112.866 . . 80 12 12 LEU H H 8.832 . . 81 12 12 LEU HA H 3.428 . . 82 12 12 LEU HB2 H 1.707 . . 83 12 12 LEU HB3 H 1.086 . . 84 12 12 LEU HG H 0.681 . . 85 12 12 LEU HD1 H 0.162 . . 86 12 12 LEU CA C 56.216 . . 87 12 12 LEU CB C 41.294 . . 88 12 12 LEU N N 125.987 . . 89 13 13 SER H H 9.143 . . 90 13 13 SER HA H 4.556 . . 91 13 13 SER HB2 H 3.694 . . 92 13 13 SER HB3 H 3.446 . . 93 13 13 SER CA C 59.802 . . 94 13 13 SER CB C 64.524 . . 95 13 13 SER N N 123.347 . . 96 14 14 SER H H 7.901 . . 97 14 14 SER HA H 4.485 . . 98 14 14 SER HB2 H 3.757 . . 99 14 14 SER HB3 H 3.757 . . 100 14 14 SER CA C 57.767 . . 101 14 14 SER CB C 64.988 . . 102 14 14 SER N N 112.067 . . 103 15 15 ILE H H 8.611 . . 104 15 15 ILE HA H 4.651 . . 105 15 15 ILE HB H 1.041 . . 106 15 15 ILE HD1 H 0.464 . . 107 15 15 ILE CA C 60.360 . . 108 15 15 ILE CB C 42.627 . . 109 15 15 ILE N N 120.108 . . 110 16 16 SER H H 8.776 . . 111 16 16 SER HA H 4.880 . . 112 16 16 SER HB2 H 3.747 . . 113 16 16 SER HB3 H 3.747 . . 114 16 16 SER CA C 56.389 . . 115 16 16 SER CB C 65.628 . . 116 16 16 SER N N 120.978 . . 117 17 17 ILE H H 8.838 . . 118 17 17 ILE HA H 5.439 . . 119 17 17 ILE HB H 1.654 . . 120 17 17 ILE HG12 H 1.276 . . 121 17 17 ILE HD1 H 0.752 . . 122 17 17 ILE CA C 59.300 . . 123 17 17 ILE CB C 39.536 . . 124 17 17 ILE N N 125.961 . . 125 18 18 SER H H 9.101 . . 126 18 18 SER CA C 55.479 . . 127 18 18 SER CB C 65.090 . . 128 18 18 SER N N 122.774 . . 129 19 19 PRO HA H 4.695 . . 130 19 19 PRO HB2 H 1.923 . . 131 19 19 PRO HB3 H 2.305 . . 132 19 19 PRO HG2 H 1.516 . . 133 19 19 PRO HG3 H 1.402 . . 134 19 19 PRO CA C 61.685 . . 135 19 19 PRO CB C 34.998 . . 136 20 20 ILE H H 8.214 . . 137 20 20 ILE CA C 61.535 . . 138 20 20 ILE CB C 39.132 . . 139 20 20 ILE N N 117.784 . . 140 21 21 ASN HA H 4.763 . . 141 21 21 ASN HB2 H 3.031 . . 142 21 21 ASN HB3 H 2.737 . . 143 21 21 ASN HD21 H 6.899 . . 144 21 21 ASN HD22 H 7.631 . . 145 21 21 ASN CA C 53.566 . . 146 21 21 ASN CB C 37.531 . . 147 21 21 ASN ND2 N 111.740 . . 148 22 22 THR H H 8.846 . . 149 22 22 THR HA H 4.572 . . 150 22 22 THR HB H 4.204 . . 151 22 22 THR HG2 H 1.176 . . 152 22 22 THR CA C 61.231 . . 153 22 22 THR CB C 69.883 . . 154 22 22 THR N N 114.787 . . 155 23 23 ASN H H 8.282 . . 156 23 23 ASN HA H 5.789 . . 157 23 23 ASN HB2 H 2.612 . . 158 23 23 ASN HB3 H 2.612 . . 159 23 23 ASN HD21 H 6.961 . . 160 23 23 ASN HD22 H 7.654 . . 161 23 23 ASN CA C 52.365 . . 162 23 23 ASN CB C 41.327 . . 163 23 23 ASN N N 119.957 . . 164 23 23 ASN ND2 N 114.252 . . 165 24 24 ILE H H 8.959 . . 166 24 24 ILE HA H 4.703 . . 167 24 24 ILE HB H 1.897 . . 168 24 24 ILE CA C 59.608 . . 169 24 24 ILE CB C 42.498 . . 170 24 24 ILE N N 118.302 . . 171 25 25 ASN H H 8.376 . . 172 25 25 ASN HA H 5.523 . . 173 25 25 ASN HB2 H 2.945 . . 174 25 25 ASN HB3 H 2.945 . . 175 25 25 ASN HD21 H 6.760 . . 176 25 25 ASN HD22 H 7.667 . . 177 25 25 ASN CA C 51.274 . . 178 25 25 ASN CB C 39.186 . . 179 25 25 ASN N N 122.659 . . 180 25 25 ASN ND2 N 111.931 . . 181 26 26 THR H H 8.169 . . 182 26 26 THR N N 108.598 . . 183 27 27 THR HA H 4.227 . . 184 27 27 THR HG2 H 1.171 . . 185 27 27 THR CA C 64.696 . . 186 27 27 THR CB C 69.914 . . 187 28 28 VAL H H 7.933 . . 188 28 28 VAL CA C 62.525 . . 189 28 28 VAL N N 124.010 . . 190 29 29 SER HB2 H 3.586 . . 191 29 29 SER HB3 H 3.586 . . 192 29 29 SER CA C 58.052 . . 193 29 29 SER CB C 65.012 . . 194 30 30 LYS H H 9.362 . . 195 30 30 LYS HA H 4.499 . . 196 30 30 LYS HB2 H 1.608 . . 197 30 30 LYS HB3 H 1.608 . . 198 30 30 LYS HG2 H 1.250 . . 199 30 30 LYS HG3 H 1.168 . . 200 30 30 LYS HE2 H 2.887 . . 201 30 30 LYS HE3 H 2.887 . . 202 30 30 LYS CA C 54.855 . . 203 30 30 LYS CB C 37.337 . . 204 30 30 LYS N N 124.031 . . 205 31 31 GLN H H 8.720 . . 206 31 31 GLN HA H 3.689 . . 207 31 31 GLN HB2 H 1.690 . . 208 31 31 GLN HB3 H 1.690 . . 209 31 31 GLN HG2 H 1.817 . . 210 31 31 GLN HG3 H 1.817 . . 211 31 31 GLN HE21 H 7.164 . . 212 31 31 GLN CA C 56.068 . . 213 31 31 GLN CB C 29.300 . . 214 31 31 GLN N N 128.579 . . 215 31 31 GLN NE2 N 116.969 . . 216 32 32 PHE H H 7.734 . . 217 32 32 PHE HA H 4.988 . . 218 32 32 PHE HB2 H 2.986 . . 219 32 32 PHE CA C 56.319 . . 220 32 32 PHE CB C 40.843 . . 221 32 32 PHE N N 128.404 . . 222 33 33 PHE H H 9.350 . . 223 33 33 PHE HA H 5.519 . . 224 33 33 PHE HB2 H 2.989 . . 225 33 33 PHE HB3 H 2.674 . . 226 33 33 PHE CA C 56.219 . . 227 33 33 PHE CB C 42.799 . . 228 33 33 PHE N N 114.574 . . 229 34 34 ALA H H 8.928 . . 230 34 34 ALA HA H 5.189 . . 231 34 34 ALA HB H 0.815 . . 232 34 34 ALA CA C 49.865 . . 233 34 34 ALA CB C 21.831 . . 234 34 34 ALA N N 123.237 . . 235 35 35 VAL H H 8.943 . . 236 35 35 VAL HA H 4.657 . . 237 35 35 VAL HB H 1.885 . . 238 35 35 VAL HG2 H 0.820 . . 239 35 35 VAL CA C 61.179 . . 240 35 35 VAL CB C 34.218 . . 241 35 35 VAL N N 122.872 . . 242 36 36 GLY H H 9.840 . . 243 36 36 GLY HA2 H 4.932 . . 244 36 36 GLY HA3 H 3.111 . . 245 36 36 GLY CA C 45.108 . . 246 36 36 GLY N N 118.442 . . 247 37 37 THR H H 8.624 . . 248 37 37 THR HA H 5.021 . . 249 37 37 THR HB H 3.879 . . 250 37 37 THR HG2 H 1.183 . . 251 37 37 THR CA C 62.439 . . 252 37 37 THR CB C 69.781 . . 253 37 37 THR N N 119.684 . . 254 38 38 TYR H H 9.401 . . 255 38 38 TYR HA H 4.995 . . 256 38 38 TYR HB2 H 3.175 . . 257 38 38 TYR HB3 H 2.745 . . 258 38 38 TYR CA C 58.011 . . 259 38 38 TYR CB C 40.909 . . 260 38 38 TYR N N 126.765 . . 261 39 39 SER H H 9.725 . . 262 39 39 SER HA H 4.083 . . 263 39 39 SER CA C 61.367 . . 264 39 39 SER CB C 62.722 . . 265 39 39 SER N N 118.044 . . 266 40 40 ASP H H 7.716 . . 267 40 40 ASP HA H 4.713 . . 268 40 40 ASP HB2 H 3.106 . . 269 40 40 ASP HB3 H 2.557 . . 270 40 40 ASP CA C 52.738 . . 271 40 40 ASP CB C 40.537 . . 272 40 40 ASP N N 119.583 . . 273 41 41 GLY H H 8.417 . . 274 41 41 GLY HA2 H 4.329 . . 275 41 41 GLY HA3 H 3.642 . . 276 41 41 GLY CA C 45.276 . . 277 41 41 GLY N N 108.650 . . 278 42 42 THR H H 7.892 . . 279 42 42 THR HG2 H 1.124 . . 280 42 42 THR CA C 62.967 . . 281 42 42 THR CB C 71.053 . . 282 42 42 THR N N 113.772 . . 283 43 43 LYS H H 8.356 . . 284 43 43 LYS HB2 H 1.566 . . 285 43 43 LYS HB3 H 1.566 . . 286 43 43 LYS HD2 H 1.399 . . 287 43 43 LYS HD3 H 1.399 . . 288 43 43 LYS HE2 H 2.910 . . 289 43 43 LYS HE3 H 2.910 . . 290 43 43 LYS CA C 54.610 . . 291 43 43 LYS CB C 36.729 . . 292 43 43 LYS N N 118.360 . . 293 44 44 ALA H H 8.890 . . 294 44 44 ALA HA H 4.639 . . 295 44 44 ALA HB H 1.384 . . 296 44 44 ALA CA C 51.411 . . 297 44 44 ALA CB C 23.598 . . 298 44 44 ALA N N 121.532 . . 299 45 45 ASP H H 8.961 . . 300 45 45 ASP HA H 4.805 . . 301 45 45 ASP HB2 H 2.950 . . 302 45 45 ASP HB3 H 2.662 . . 303 45 45 ASP CA C 55.272 . . 304 45 45 ASP CB C 40.881 . . 305 45 45 ASP N N 121.587 . . 306 46 46 LEU H H 9.214 . . 307 46 46 LEU HA H 4.838 . . 308 46 46 LEU HB2 H 1.596 . . 309 46 46 LEU HB3 H 0.992 . . 310 46 46 LEU HD2 H 0.598 . . 311 46 46 LEU CA C 53.603 . . 312 46 46 LEU CB C 43.920 . . 313 46 46 LEU N N 128.252 . . 314 47 47 THR H H 8.986 . . 315 47 47 THR HA H 4.498 . . 316 47 47 THR HB H 3.989 . . 317 47 47 THR HG2 H 1.509 . . 318 47 47 THR CB C 69.413 . . 319 47 47 THR N N 122.416 . . 320 48 48 SER H H 8.735 . . 321 48 48 SER HA H 4.477 . . 322 48 48 SER HB2 H 4.012 . . 323 48 48 SER HB3 H 4.012 . . 324 48 48 SER CA C 60.134 . . 325 48 48 SER CB C 63.846 . . 326 48 48 SER N N 109.841 . . 327 49 49 SER H H 8.066 . . 328 49 49 SER HA H 4.694 . . 329 49 49 SER HB2 H 3.719 . . 330 49 49 SER HB3 H 3.547 . . 331 49 49 SER CA C 59.965 . . 332 49 49 SER CB C 64.972 . . 333 49 49 SER N N 116.988 . . 334 50 50 VAL H H 7.481 . . 335 50 50 VAL HA H 4.299 . . 336 50 50 VAL HB H 1.551 . . 337 50 50 VAL HG2 H 0.572 . . 338 50 50 VAL CA C 61.079 . . 339 50 50 VAL CB C 32.172 . . 340 50 50 VAL N N 113.701 . . 341 51 51 THR H H 8.998 . . 342 51 51 THR HA H 4.510 . . 343 51 51 THR HB H 3.887 . . 344 51 51 THR HG2 H 1.148 . . 345 51 51 THR CA C 62.575 . . 346 51 51 THR CB C 70.008 . . 347 51 51 THR N N 116.116 . . 348 52 52 TRP H H 9.640 . . 349 52 52 TRP HA H 5.366 . . 350 52 52 TRP HB2 H 3.125 . . 351 52 52 TRP HB3 H 2.822 . . 352 52 52 TRP HE1 H 10.005 . . 353 52 52 TRP CA C 56.750 . . 354 52 52 TRP CB C 31.469 . . 355 52 52 TRP N N 133.471 . . 356 52 52 TRP NE1 N 127.953 . . 357 53 53 SER H H 9.980 . . 358 53 53 SER HA H 4.593 . . 359 53 53 SER HB2 H 3.793 . . 360 53 53 SER HB3 H 3.793 . . 361 53 53 SER CA C 58.025 . . 362 53 53 SER CB C 65.888 . . 363 53 53 SER N N 116.986 . . 364 54 54 SER H H 8.566 . . 365 54 54 SER HA H 5.508 . . 366 54 54 SER HB2 H 3.603 . . 367 54 54 SER HB3 H 3.467 . . 368 54 54 SER CA C 53.568 . . 369 54 54 SER CB C 66.245 . . 370 54 54 SER N N 112.794 . . 371 55 55 SER H H 9.679 . . 372 55 55 SER HA H 4.235 . . 373 55 55 SER HB2 H 3.834 . . 374 55 55 SER HB3 H 3.834 . . 375 55 55 SER CA C 60.526 . . 376 55 55 SER CB C 62.670 . . 377 55 55 SER N N 122.420 . . 378 56 56 ASN H H 7.992 . . 379 56 56 ASN HA H 4.724 . . 380 56 56 ASN HB2 H 2.910 . . 381 56 56 ASN HB3 H 2.705 . . 382 56 56 ASN HD21 H 7.247 . . 383 56 56 ASN HD22 H 7.389 . . 384 56 56 ASN CA C 53.583 . . 385 56 56 ASN CB C 37.883 . . 386 56 56 ASN N N 118.092 . . 387 56 56 ASN ND2 N 112.177 . . 388 57 57 GLN H H 9.367 . . 389 57 57 GLN HA H 4.517 . . 390 57 57 GLN HB2 H 2.179 . . 391 57 57 GLN HB3 H 2.053 . . 392 57 57 GLN HG2 H 2.507 . . 393 57 57 GLN HG3 H 2.507 . . 394 57 57 GLN HE21 H 7.076 . . 395 57 57 GLN CA C 57.680 . . 396 57 57 GLN CB C 28.794 . . 397 57 57 GLN N N 126.746 . . 398 57 57 GLN NE2 N 112.674 . . 399 58 58 SER H H 8.203 . . 400 58 58 SER HA H 4.302 . . 401 58 58 SER HB2 H 3.927 . . 402 58 58 SER HB3 H 3.927 . . 403 58 58 SER CA C 60.091 . . 404 58 58 SER CB C 63.026 . . 405 58 58 SER N N 113.148 . . 406 59 59 GLN H H 7.278 . . 407 59 59 GLN HA H 4.542 . . 408 59 59 GLN HB2 H 1.720 . . 409 59 59 GLN HB3 H 1.720 . . 410 59 59 GLN HG2 H 2.102 . . 411 59 59 GLN HG3 H 1.952 . . 412 59 59 GLN HE21 H 7.055 . . 413 59 59 GLN HE22 H 7.055 . . 414 59 59 GLN CA C 56.180 . . 415 59 59 GLN CB C 29.623 . . 416 59 59 GLN N N 116.425 . . 417 59 59 GLN NE2 N 107.720 . . 418 60 60 ALA H H 8.139 . . 419 60 60 ALA HA H 4.904 . . 420 60 60 ALA HB H 0.978 . . 421 60 60 ALA CA C 52.361 . . 422 60 60 ALA CB C 22.074 . . 423 60 60 ALA N N 119.214 . . 424 61 61 LYS H H 8.392 . . 425 61 61 LYS HA H 4.875 . . 426 61 61 LYS HB2 H 1.761 . . 427 61 61 LYS HB3 H 1.617 . . 428 61 61 LYS HD2 H 1.328 . . 429 61 61 LYS HD3 H 1.328 . . 430 61 61 LYS HE2 H 2.859 . . 431 61 61 LYS HE3 H 2.859 . . 432 61 61 LYS CA C 53.804 . . 433 61 61 LYS CB C 36.105 . . 434 61 61 LYS N N 120.692 . . 435 62 62 VAL H H 8.724 . . 436 62 62 VAL HA H 4.934 . . 437 62 62 VAL HB H 1.555 . . 438 62 62 VAL HG1 H 0.746 . . 439 62 62 VAL HG2 H 0.376 . . 440 62 62 VAL CA C 58.065 . . 441 62 62 VAL CB C 34.564 . . 442 62 62 VAL N N 118.353 . . 443 63 63 SER H H 7.860 . . 444 63 63 SER HA H 4.346 . . 445 63 63 SER HB2 H 3.728 . . 446 63 63 SER HB3 H 3.728 . . 447 63 63 SER CA C 57.530 . . 448 63 63 SER CB C 63.859 . . 449 63 63 SER N N 119.944 . . 450 64 64 ASN H H 9.151 . . 451 64 64 ASN HA H 5.246 . . 452 64 64 ASN HB2 H 3.130 . . 453 64 64 ASN HB3 H 2.626 . . 454 64 64 ASN HD21 H 7.054 . . 455 64 64 ASN HD22 H 8.061 . . 456 64 64 ASN CA C 53.380 . . 457 64 64 ASN CB C 41.513 . . 458 64 64 ASN N N 124.532 . . 459 64 64 ASN ND2 N 115.866 . . 460 65 65 ALA H H 8.115 . . 461 65 65 ALA HA H 4.309 . . 462 65 65 ALA HB H 1.365 . . 463 65 65 ALA CA C 52.330 . . 464 65 65 ALA CB C 18.544 . . 465 65 65 ALA N N 126.870 . . 466 66 66 SER H H 8.743 . . 467 66 66 SER HB2 H 3.941 . . 468 66 66 SER HB3 H 3.941 . . 469 66 66 SER CA C 62.570 . . 470 66 66 SER CB C 63.073 . . 471 66 66 SER N N 116.292 . . 472 67 67 GLU H H 9.186 . . 473 67 67 GLU HA H 4.216 . . 474 67 67 GLU HB2 H 2.074 . . 475 67 67 GLU HB3 H 2.074 . . 476 67 67 GLU HG2 H 2.350 . . 477 67 67 GLU HG3 H 2.350 . . 478 67 67 GLU CA C 58.873 . . 479 67 67 GLU CB C 29.559 . . 480 67 67 GLU N N 117.021 . . 481 68 68 THR H H 7.369 . . 482 68 68 THR HA H 4.796 . . 483 68 68 THR HB H 4.731 . . 484 68 68 THR HG2 H 1.012 . . 485 68 68 THR CA C 59.162 . . 486 68 68 THR CB C 69.331 . . 487 68 68 THR N N 107.110 . . 488 69 69 LYS H H 6.924 . . 489 69 69 LYS HA H 3.669 . . 490 69 69 LYS HB2 H 1.877 . . 491 69 69 LYS HB3 H 1.877 . . 492 69 69 LYS HD2 H 1.674 . . 493 69 69 LYS HD3 H 1.674 . . 494 69 69 LYS HE2 H 3.322 . . 495 69 69 LYS HE3 H 3.242 . . 496 69 69 LYS CA C 58.248 . . 497 69 69 LYS CB C 33.057 . . 498 69 69 LYS N N 122.826 . . 499 70 70 GLY H H 7.947 . . 500 70 70 GLY HA2 H 2.847 . . 501 70 70 GLY CA C 44.445 . . 502 70 70 GLY N N 111.617 . . 503 71 71 LEU H H 7.782 . . 504 71 71 LEU HA H 4.052 . . 505 71 71 LEU HB2 H 1.821 . . 506 71 71 LEU HB3 H 1.265 . . 507 71 71 LEU CA C 55.592 . . 508 71 71 LEU CB C 43.108 . . 509 71 71 LEU N N 120.786 . . 510 72 72 VAL H H 8.972 . . 511 72 72 VAL HA H 4.631 . . 512 72 72 VAL HB H 1.960 . . 513 72 72 VAL HG1 H 0.440 . . 514 72 72 VAL HG2 H 0.199 . . 515 72 72 VAL CA C 61.518 . . 516 72 72 VAL CB C 32.751 . . 517 72 72 VAL N N 107.012 . . 518 73 73 THR H H 8.939 . . 519 73 73 THR HA H 4.764 . . 520 73 73 THR HB H 3.536 . . 521 73 73 THR HG2 H 0.966 . . 522 73 73 THR CA C 61.299 . . 523 73 73 THR CB C 71.624 . . 524 73 73 THR N N 121.860 . . 525 74 74 GLY H H 9.194 . . 526 74 74 GLY HA2 H 3.922 . . 527 74 74 GLY HA3 H 3.396 . . 528 74 74 GLY CA C 46.346 . . 529 74 74 GLY N N 114.171 . . 530 75 75 ILE H H 8.910 . . 531 75 75 ILE HA H 4.117 . . 532 75 75 ILE HB H 1.426 . . 533 75 75 ILE CA C 61.735 . . 534 75 75 ILE CB C 38.859 . . 535 75 75 ILE N N 126.338 . . 536 76 76 ALA H H 8.410 . . 537 76 76 ALA HA H 4.391 . . 538 76 76 ALA HB H 1.455 . . 539 76 76 ALA CA C 51.898 . . 540 76 76 ALA CB C 21.985 . . 541 76 76 ALA N N 122.268 . . 542 77 77 SER H H 8.086 . . 543 77 77 SER HA H 3.998 . . 544 77 77 SER HB2 H 3.791 . . 545 77 77 SER HB3 H 3.791 . . 546 77 77 SER CA C 58.637 . . 547 77 77 SER CB C 64.148 . . 548 77 77 SER N N 110.536 . . 549 78 78 GLY H H 8.051 . . 550 78 78 GLY HA2 H 4.283 . . 551 78 78 GLY HA3 H 3.772 . . 552 78 78 GLY CA C 44.544 . . 553 78 78 GLY N N 108.428 . . 554 79 79 ASN H H 8.222 . . 555 79 79 ASN CA C 51.395 . . 556 79 79 ASN CB C 39.858 . . 557 79 79 ASN N N 116.152 . . 558 80 80 PRO HA H 4.433 . . 559 80 80 PRO HB2 H 1.904 . . 560 80 80 PRO HB3 H 2.345 . . 561 80 80 PRO CA C 63.499 . . 562 80 80 PRO CB C 32.002 . . 563 81 81 THR H H 8.754 . . 564 81 81 THR HA H 4.838 . . 565 81 81 THR HB H 3.866 . . 566 81 81 THR HG2 H 1.098 . . 567 81 81 THR CA C 61.792 . . 568 81 81 THR CB C 70.635 . . 569 81 81 THR N N 115.077 . . 570 82 82 ILE H H 8.986 . . 571 82 82 ILE HB H 1.817 . . 572 82 82 ILE CA C 57.728 . . 573 82 82 ILE CB C 36.731 . . 574 82 82 ILE N N 126.538 . . 575 83 83 ILE H H 8.973 . . 576 83 83 ILE HA H 4.642 . . 577 83 83 ILE HB H 1.641 . . 578 83 83 ILE HD1 H 0.720 . . 579 83 83 ILE CA C 60.636 . . 580 83 83 ILE CB C 40.952 . . 581 83 83 ILE N N 126.649 . . 582 84 84 ALA H H 8.423 . . 583 84 84 ALA HA H 4.495 . . 584 84 84 ALA CA C 49.741 . . 585 84 84 ALA CB C 21.444 . . 586 84 84 ALA N N 126.429 . . 587 85 85 THR H H 8.147 . . 588 85 85 THR HA H 4.819 . . 589 85 85 THR HB H 3.641 . . 590 85 85 THR CA C 61.556 . . 591 85 85 THR CB C 71.694 . . 592 85 85 THR N N 116.628 . . 593 86 86 TYR H H 9.123 . . 594 86 86 TYR HA H 4.601 . . 595 86 86 TYR HB2 H 2.796 . . 596 86 86 TYR HB3 H 2.456 . . 597 86 86 TYR CA C 57.703 . . 598 86 86 TYR CB C 40.488 . . 599 86 86 TYR N N 127.831 . . 600 87 87 GLY H H 8.760 . . 601 87 87 GLY HA2 H 3.811 . . 602 87 87 GLY HA3 H 3.440 . . 603 87 87 GLY CA C 47.004 . . 604 87 87 GLY N N 118.193 . . 605 88 88 SER H H 8.768 . . 606 88 88 SER HA H 4.339 . . 607 88 88 SER HB2 H 4.023 . . 608 88 88 SER HB3 H 3.838 . . 609 88 88 SER CA C 58.673 . . 610 88 88 SER CB C 63.569 . . 611 88 88 SER N N 121.951 . . 612 89 89 VAL H H 7.860 . . 613 89 89 VAL HA H 4.235 . . 614 89 89 VAL HB H 1.982 . . 615 89 89 VAL HG2 H 0.688 . . 616 89 89 VAL CA C 61.891 . . 617 89 89 VAL CB C 33.106 . . 618 89 89 VAL N N 124.193 . . 619 90 90 SER H H 8.523 . . 620 90 90 SER HA H 5.503 . . 621 90 90 SER HB2 H 3.562 . . 622 90 90 SER HB3 H 3.562 . . 623 90 90 SER CA C 56.541 . . 624 90 90 SER CB C 66.805 . . 625 90 90 SER N N 118.986 . . 626 91 91 GLY H H 8.961 . . 627 91 91 GLY HA2 H 4.677 . . 628 91 91 GLY HA3 H 3.554 . . 629 91 91 GLY CA C 44.248 . . 630 91 91 GLY N N 111.324 . . 631 92 92 ASN H H 8.730 . . 632 92 92 ASN HB2 H 2.603 . . 633 92 92 ASN HB3 H 2.603 . . 634 92 92 ASN HD21 H 6.777 . . 635 92 92 ASN HD22 H 7.410 . . 636 92 92 ASN CA C 52.858 . . 637 92 92 ASN CB C 43.278 . . 638 92 92 ASN N N 114.845 . . 639 92 92 ASN ND2 N 113.195 . . 640 93 93 THR H H 8.917 . . 641 93 93 THR HA H 4.659 . . 642 93 93 THR HB H 4.164 . . 643 93 93 THR HG2 H 1.163 . . 644 93 93 THR CA C 61.877 . . 645 93 93 THR CB C 70.809 . . 646 93 93 THR N N 114.421 . . 647 94 94 ILE H H 8.012 . . 648 94 94 ILE HA H 4.539 . . 649 94 94 ILE HB H 1.721 . . 650 94 94 ILE HG12 H 1.572 . . 651 94 94 ILE HG13 H 1.137 . . 652 94 94 ILE HD1 H 0.810 . . 653 94 94 ILE CA C 61.434 . . 654 94 94 ILE CB C 39.229 . . 655 94 94 ILE N N 125.766 . . 656 95 95 LEU H H 8.780 . . 657 95 95 LEU HA H 4.679 . . 658 95 95 LEU HB2 H 1.563 . . 659 95 95 LEU HB3 H 1.375 . . 660 95 95 LEU HD2 H 0.521 . . 661 95 95 LEU CA C 53.767 . . 662 95 95 LEU CB C 45.660 . . 663 95 95 LEU N N 129.200 . . 664 96 96 THR H H 7.889 . . 665 96 96 THR HA H 4.729 . . 666 96 96 THR HB H 3.967 . . 667 96 96 THR CA C 62.806 . . 668 96 96 THR CB C 70.447 . . 669 96 96 THR N N 117.640 . . 670 97 97 VAL H H 9.125 . . 671 97 97 VAL HB H 2.188 . . 672 97 97 VAL CA C 60.599 . . 673 97 97 VAL CB C 31.387 . . 674 97 97 VAL N N 127.422 . . 675 98 98 ASN H H 8.990 . . 676 98 98 ASN HA H 4.820 . . 677 98 98 ASN HB2 H 2.718 . . 678 98 98 ASN HB3 H 2.718 . . 679 98 98 ASN HD21 H 7.176 . . 680 98 98 ASN CA C 52.751 . . 681 98 98 ASN CB C 40.805 . . 682 98 98 ASN N N 126.554 . . 683 98 98 ASN ND2 N 113.831 . . 684 99 99 LYS H H 8.543 . . 685 99 99 LYS HA H 4.411 . . 686 99 99 LYS HB2 H 1.692 . . 687 99 99 LYS HB3 H 1.692 . . 688 99 99 LYS HG2 H 1.425 . . 689 99 99 LYS HG3 H 1.425 . . 690 99 99 LYS HE2 H 2.976 . . 691 99 99 LYS HE3 H 2.976 . . 692 99 99 LYS CA C 56.554 . . 693 99 99 LYS CB C 33.122 . . 694 99 99 LYS N N 122.429 . . 695 100 100 THR H H 8.407 . . 696 100 100 THR HA H 4.308 . . 697 100 100 THR HB H 4.160 . . 698 100 100 THR HG2 H 1.176 . . 699 100 100 THR CA C 62.162 . . 700 100 100 THR CB C 69.881 . . 701 100 100 THR N N 119.080 . . 702 101 101 ASP H H 8.561 . . 703 101 101 ASP HA H 4.655 . . 704 101 101 ASP HB2 H 2.657 . . 705 101 101 ASP HB3 H 2.657 . . 706 101 101 ASP CA C 54.559 . . 707 101 101 ASP CB C 41.111 . . 708 101 101 ASP N N 123.942 . . 709 102 102 THR H H 7.799 . . 710 102 102 THR CA C 63.393 . . 711 102 102 THR CB C 70.968 . . 712 102 102 THR N N 118.961 . . stop_ save_