data_6179 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the structured part of the 15th domain of LEKTI ; _BMRB_accession_number 6179 _BMRB_flat_file_name bmr6179.str _Entry_type original _Submission_date 2004-04-15 _Accession_date 2004-04-15 _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 Vitzithum Klaus . . 2 Roesch Paul . . 3 Marx Ute C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 312 "15N chemical shifts" 51 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-17 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 6180 'LEKTI Domain 15' stop_ _Original_release_date 2004-04-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Solution structure of a chimeric LEKTI domain reveals a chameleon sequence ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15366933 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tidow H. . . 2 Lauber T. . . 3 Vitzithum Klaus . . 4 Sommerhoff C. P. . 5 Roesch Paul . . 6 Marx Ute C. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 35 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11238 _Page_last 11247 _Year 2004 _Details . loop_ _Keyword Kazal LEKTI 'Serine Proteinase Inhibitor' 'Trypsin Inhibitor' stop_ save_ ################################## # Molecular system description # ################################## save_system_LEKTI_Domain_15_short _Saveframe_category molecular_system _Mol_system_name 'LEKTI Domain 15 short' _Abbreviation_common 'LEKTI Domain 15 short' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LEKTI Domain 15 short' $LEKTI_Domain_15_short stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function Kazal-type 'serine proteinase inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LEKTI_Domain_15_short _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LEKTI Domain 15 short' _Name_variant none _Abbreviation_common 'LEKTI Domain 15 short' _Molecular_mass 6922.9 _Mol_thiol_state 'all disulfide bound' _Details ; contains additional Gly and Pro residue at the N-terminus compared to the native sequence. ; ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; GPDSEMCKDYRVLPRIGYLC PKDLKPVCGDDGQTYNNPCM LCHENLIRQTNTHIRSTGKC E ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 PRO 3 1 ASP 4 2 SER 5 3 GLU 6 4 MET 7 5 CYS 8 6 LYS 9 7 ASP 10 8 TYR 11 9 ARG 12 10 VAL 13 11 LEU 14 12 PRO 15 13 ARG 16 14 ILE 17 15 GLY 18 16 TYR 19 17 LEU 20 18 CYS 21 19 PRO 22 20 LYS 23 21 ASP 24 22 LEU 25 23 LYS 26 24 PRO 27 25 VAL 28 26 CYS 29 27 GLY 30 28 ASP 31 29 ASP 32 30 GLY 33 31 GLN 34 32 THR 35 33 TYR 36 34 ASN 37 35 ASN 38 36 PRO 39 37 CYS 40 38 MET 41 39 LEU 42 40 CYS 43 41 HIS 44 42 GLU 45 43 ASN 46 44 LEU 47 45 ILE 48 46 ARG 49 47 GLN 50 48 THR 51 49 ASN 52 50 THR 53 51 HIS 54 52 ILE 55 53 ARG 56 54 SER 57 55 THR 58 56 GLY 59 57 LYS 60 58 CYS 61 59 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 6180 'LEKTI Domain 15' 100.00 78 100.00 100.00 4.49e-29 PDB 1UVF 'Solution Structure Of The Structured Part Of The 15th Domain Of Lekti' 100.00 61 100.00 100.00 2.03e-28 PDB 1UVG 'Solution Structure Of The 15th Domain Of Lekti' 100.00 78 100.00 100.00 4.49e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $LEKTI_Domain_15_short Human 9606 Eukaryota Metazoa Homo sapiens 'vaginal epithelium and human skin epidermis' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $LEKTI_Domain_15_short 'recombinant technology' 'Escherichia coli' Escherichia coli Origami DE3 plasmid T7-Expressionsvector 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 $LEKTI_Domain_15_short 0.7 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LEKTI_Domain_15_short 1.6 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRview _Saveframe_category software _Name NMRview _Version 5.0.4 _Details . save_ save_NDEE _Saveframe_category software _Name NDEE _Version . loop_ _Vendor _Address _Electronic_address 'Spinup Inc.' 'Dortmund, Germany.' . stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D-TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _Sample_label . save_ save_2D-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-COSY _Sample_label . save_ save_2D-NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_1H,15N-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H,15N-HSQC _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_3D-1H,1H,15N-TOCSY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H,1H,15N-TOCSY-HSQC _Sample_label . save_ save_3D-1H,1H,15N-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H,1H,15N-NOESY-HSQC _Sample_label . save_ save_3D-1H,15N,15N-HMQC-NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H,15N,15N-HMQC-NOESY-HSQC _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 6.6 0.3 n/a pressure 1 . atm temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 2D-TOCSY 2D-COSY 2D-NOESY 1H,15N-HSQC HNHA 3D-1H,1H,15N-TOCSY-HSQC 3D-1H,1H,15N-NOESY-HSQC 3D-1H,15N,15N-HMQC-NOESY-HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'LEKTI Domain 15 short' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 3 ASP H H 8.600 0.02 1 2 1 3 ASP N N 120.80 0.2 1 3 1 3 ASP HA H 4.611 0.02 1 4 1 3 ASP HB2 H 2.730 0.02 1 5 2 4 SER H H 8.306 0.02 1 6 2 4 SER HA H 4.327 0.02 1 7 2 4 SER HB2 H 3.995 0.02 2 8 2 4 SER HB3 H 3.913 0.02 2 9 3 5 GLU H H 8.402 0.02 1 10 3 5 GLU N N 122.554 0.2 1 11 3 5 GLU HA H 4.310 0.02 1 12 3 5 GLU HB2 H 2.125 0.02 2 13 3 5 GLU HB3 H 2.021 0.02 2 14 3 5 GLU HG2 H 2.332 0.02 2 15 3 5 GLU HG3 H 2.288 0.02 2 16 4 6 MET H H 8.101 0.02 1 17 4 6 MET N N 118.829 0.2 1 18 4 6 MET HA H 4.154 0.02 1 19 4 6 MET HB2 H 2.199 0.02 1 20 4 6 MET HG2 H 2.598 0.02 2 21 4 6 MET HG3 H 2.463 0.02 2 22 5 7 CYS H H 7.980 0.02 1 23 5 7 CYS N N 119.531 0.2 1 24 5 7 CYS HA H 4.903 0.02 1 25 5 7 CYS HB2 H 3.581 0.02 2 26 5 7 CYS HB3 H 2.941 0.02 2 27 6 8 LYS H H 7.446 0.02 1 28 6 8 LYS N N 119.531 0.2 1 29 6 8 LYS HA H 4.209 0.02 1 30 6 8 LYS HB2 H 1.895 0.02 1 31 6 8 LYS HG2 H 1.472 0.02 2 32 6 8 LYS HG3 H 1.350 0.02 2 33 6 8 LYS HD2 H 1.646 0.02 1 34 6 8 LYS HE2 H 2.935 0.02 1 35 7 9 ASP H H 8.047 0.02 1 36 7 9 ASP N N 117.794 0.2 1 37 7 9 ASP HA H 4.500 0.02 1 38 7 9 ASP HB2 H 2.416 0.02 2 39 7 9 ASP HB3 H 1.825 0.02 2 40 8 10 TYR H H 7.413 0.02 1 41 8 10 TYR N N 119.586 0.2 1 42 8 10 TYR HA H 5.036 0.02 1 43 8 10 TYR HB2 H 3.507 0.02 2 44 8 10 TYR HB3 H 2.976 0.02 2 45 8 10 TYR HD1 H 7.193 0.02 1 46 8 10 TYR HD2 H 7.090 0.02 1 47 8 10 TYR HE1 H 6.817 0.02 1 48 8 10 TYR HE2 H 6.863 0.02 1 49 9 11 ARG H H 9.200 0.02 1 50 9 11 ARG N N 123.555 0.2 1 51 9 11 ARG HA H 4.378 0.02 1 52 9 11 ARG HB2 H 1.877 0.02 1 53 9 11 ARG HG2 H 1.770 0.02 2 54 9 11 ARG HG3 H 1.613 0.02 2 55 9 11 ARG HD2 H 3.226 0.02 1 56 9 11 ARG HE H 7.238 0.02 1 57 10 12 VAL H H 8.102 0.02 1 58 10 12 VAL N N 122.151 0.2 1 59 10 12 VAL HA H 4.168 0.02 1 60 10 12 VAL HB H 1.268 0.02 1 61 10 12 VAL HG1 H 0.556 0.02 2 62 10 12 VAL HG2 H 0.157 0.02 2 63 11 13 LEU H H 8.651 0.02 1 64 11 13 LEU N N 129.086 0.2 1 65 11 13 LEU HA H 4.911 0.02 1 66 11 13 LEU HB2 H 1.554 0.02 1 67 11 13 LEU HG H 1.554 0.02 1 68 11 13 LEU HD1 H 0.910 0.02 1 69 11 13 LEU HD2 H 0.910 0.02 1 70 12 14 PRO HA H 4.236 0.02 1 71 12 14 PRO HB2 H 2.354 0.02 2 72 12 14 PRO HB3 H 2.013 0.02 2 73 12 14 PRO HG2 H 2.141 0.02 1 74 12 14 PRO HD2 H 3.908 0.02 2 75 12 14 PRO HD3 H 3.655 0.02 2 76 13 15 ARG H H 8.788 0.02 1 77 13 15 ARG HA H 3.815 0.02 1 78 13 15 ARG HB2 H 2.224 0.02 2 79 13 15 ARG HB3 H 2.030 0.02 2 80 13 15 ARG HG2 H 1.582 0.02 1 81 13 15 ARG HD2 H 3.230 0.02 1 82 13 15 ARG HE H 7.266 0.02 1 83 14 16 ILE H H 8.331 0.02 1 84 14 16 ILE N N 120.210 0.2 1 85 14 16 ILE HA H 4.124 0.02 1 86 14 16 ILE HB H 1.711 0.02 1 87 14 16 ILE HG12 H 1.447 0.02 2 88 14 16 ILE HG13 H 1.124 0.02 2 89 14 16 ILE HG2 H 0.866 0.02 1 90 14 16 ILE HD1 H 0.866 0.02 1 91 15 17 GLY H H 8.141 0.02 1 92 15 17 GLY N N 108.349 0.2 1 93 15 17 GLY HA2 H 4.606 0.02 2 94 15 17 GLY HA3 H 3.563 0.02 2 95 16 18 TYR H H 9.923 0.02 1 96 16 18 TYR N N 122.728 0.2 1 97 16 18 TYR HA H 4.816 0.02 1 98 16 18 TYR HB2 H 2.966 0.02 2 99 16 18 TYR HB3 H 2.678 0.02 2 100 16 18 TYR HD1 H 7.086 0.02 3 101 16 18 TYR HE1 H 6.814 0.02 3 102 17 19 LEU H H 8.600 0.02 1 103 17 19 LEU N N 124.487 0.2 1 104 17 19 LEU HA H 4.553 0.02 1 105 17 19 LEU HB2 H 1.577 0.02 1 106 17 19 LEU HG H 1.577 0.02 1 107 17 19 LEU HD1 H 0.848 0.02 1 108 17 19 LEU HD2 H 0.848 0.02 1 109 18 20 CYS H H 8.129 0.02 1 110 18 20 CYS N N 121.473 0.2 1 111 18 20 CYS HA H 5.399 0.02 1 112 18 20 CYS HB2 H 2.897 0.02 2 113 18 20 CYS HB3 H 2.565 0.02 2 114 19 21 PRO HA H 4.685 0.02 1 115 19 21 PRO HB2 H 2.495 0.02 2 116 19 21 PRO HB3 H 2.093 0.02 2 117 19 21 PRO HG2 H 2.285 0.02 1 118 19 21 PRO HD2 H 4.025 0.02 2 119 19 21 PRO HD3 H 3.389 0.02 2 120 20 22 LYS H H 8.693 0.02 1 121 20 22 LYS HA H 4.209 0.02 1 122 20 22 LYS HB2 H 2.096 0.02 1 123 20 22 LYS HG2 H 1.425 0.02 1 124 20 22 LYS HD2 H 1.693 0.02 1 125 20 22 LYS HE2 H 3.012 0.02 1 126 21 23 ASP H H 7.567 0.02 1 127 21 23 ASP N N 117.647 0.2 1 128 21 23 ASP HA H 4.256 0.02 1 129 21 23 ASP HB2 H 2.534 0.02 2 130 21 23 ASP HB3 H 2.417 0.02 2 131 22 24 LEU H H 8.651 0.02 1 132 22 24 LEU N N 125.168 0.2 1 133 22 24 LEU HA H 4.530 0.02 1 134 22 24 LEU HB2 H 1.655 0.02 1 135 22 24 LEU HG H 1.655 0.02 1 136 22 24 LEU HD1 H 0.947 0.02 1 137 22 24 LEU HD2 H 0.947 0.02 1 138 23 25 LYS H H 8.894 0.02 1 139 23 25 LYS N N 128.374 0.2 1 140 23 25 LYS HA H 4.615 0.02 1 141 23 25 LYS HB2 H 1.906 0.02 1 142 23 25 LYS HG2 H 1.400 0.02 1 143 23 25 LYS HD2 H 1.667 0.02 1 144 23 25 LYS HE2 H 3.042 0.02 1 145 24 26 PRO HA H 4.708 0.02 1 146 24 26 PRO HB2 H 2.084 0.02 2 147 24 26 PRO HB3 H 1.495 0.02 2 148 24 26 PRO HG2 H 1.931 0.02 1 149 24 26 PRO HD2 H 3.635 0.02 2 150 24 26 PRO HD3 H 3.388 0.02 2 151 25 27 VAL H H 8.526 0.02 1 152 25 27 VAL N N 111.763 0.2 1 153 25 27 VAL HA H 4.736 0.02 1 154 25 27 VAL HB H 2.185 0.02 1 155 25 27 VAL HG1 H 1.047 0.02 2 156 25 27 VAL HG2 H 0.673 0.02 2 157 26 28 CYS H H 8.859 0.02 1 158 26 28 CYS N N 121.822 0.2 1 159 26 28 CYS HA H 5.327 0.02 1 160 26 28 CYS HB2 H 3.115 0.02 2 161 26 28 CYS HB3 H 2.708 0.02 2 162 27 29 GLY H H 9.810 0.02 1 163 27 29 GLY N N 120.707 0.2 1 164 27 29 GLY HA2 H 4.756 0.02 2 165 27 29 GLY HA3 H 4.210 0.02 2 166 28 30 ASP H H 9.122 0.02 1 167 28 30 ASP HA H 4.401 0.02 1 168 28 30 ASP HB2 H 2.993 0.02 2 169 28 30 ASP HB3 H 2.442 0.02 2 170 29 31 ASP H H 8.339 0.02 1 171 29 31 ASP N N 117.256 0.2 1 172 29 31 ASP HA H 4.522 0.02 1 173 29 31 ASP HB2 H 3.047 0.02 2 174 29 31 ASP HB3 H 2.727 0.02 2 175 30 32 GLY H H 8.526 0.02 1 176 30 32 GLY N N 109.692 0.2 1 177 30 32 GLY HA2 H 4.112 0.02 2 178 30 32 GLY HA3 H 3.749 0.02 2 179 31 33 GLN H H 7.934 0.02 1 180 31 33 GLN N N 120.122 0.2 1 181 31 33 GLN HA H 4.453 0.02 1 182 31 33 GLN HB2 H 1.877 0.02 2 183 31 33 GLN HB3 H 1.723 0.02 2 184 31 33 GLN HG2 H 2.030 0.02 2 185 31 33 GLN HG3 H 1.953 0.02 2 186 31 33 GLN HE21 H 7.237 0.02 2 187 31 33 GLN HE22 H 6.778 0.02 2 188 31 33 GLN NE2 N 112.749 0.2 1 189 32 34 THR H H 8.393 0.02 1 190 32 34 THR HA H 4.939 0.02 1 191 32 34 THR HB H 3.930 0.02 1 192 32 34 THR HG2 H 1.160 0.02 1 193 33 35 TYR H H 9.415 0.02 1 194 33 35 TYR N N 127.649 0.2 1 195 33 35 TYR HA H 4.550 0.02 1 196 33 35 TYR HB2 H 2.732 0.02 1 197 33 35 TYR HB3 H 2.537 0.02 1 198 33 35 TYR HD1 H 8.527 0.02 3 199 33 35 TYR HE1 H 6.882 0.02 3 200 34 36 ASN H H 9.167 0.02 1 201 34 36 ASN N N 120.982 0.2 1 202 34 36 ASN HA H 4.218 0.02 1 203 34 36 ASN HB2 H 2.802 0.02 1 204 34 36 ASN HD21 H 7.453 0.02 2 205 34 36 ASN HD22 H 6.845 0.02 2 206 35 37 ASN H H 7.433 0.02 1 207 35 37 ASN N N 107.197 0.2 1 208 35 37 ASN HA H 5.130 0.02 1 209 35 37 ASN HB2 H 3.355 0.02 2 210 35 37 ASN HB3 H 3.044 0.02 2 211 35 37 ASN HD21 H 7.901 0.02 2 212 35 37 ASN HD22 H 6.371 0.02 2 213 35 37 ASN ND2 N 113.901 0.2 1 214 36 38 PRO HA H 4.022 0.02 1 215 36 38 PRO HB2 H 2.489 0.02 2 216 36 38 PRO HB3 H 2.236 0.02 2 217 36 38 PRO HG2 H 2.342 0.02 1 218 36 38 PRO HD2 H 4.184 0.02 2 219 36 38 PRO HD3 H 3.922 0.02 2 220 37 39 CYS H H 7.562 0.02 1 221 37 39 CYS HA H 3.155 0.02 1 222 37 39 CYS N N 115.583 0.2 1 223 37 39 CYS HB2 H 2.719 0.02 2 224 37 39 CYS HB3 H 0.780 0.02 2 225 38 40 MET H H 7.843 0.02 1 226 38 40 MET N N 118.115 0.2 1 227 38 40 MET HA H 4.271 0.02 1 228 38 40 MET HB2 H 2.440 0.02 2 229 38 40 MET HB3 H 2.199 0.02 2 230 38 40 MET HG2 H 2.805 0.02 2 231 38 40 MET HG3 H 2.679 0.02 2 232 39 41 LEU H H 6.885 0.02 1 233 39 41 LEU N N 122.017 0.2 1 234 39 41 LEU HA H 3.619 0.02 1 235 39 41 LEU HB2 H 1.775 0.02 2 236 39 41 LEU HB3 H 0.455 0.02 2 237 39 41 LEU HG H 0.920 0.02 1 238 39 41 LEU HD1 H 0.422 0.02 2 239 39 41 LEU HD2 H -0.022 0.02 2 240 40 42 CYS H H 7.749 0.02 1 241 40 42 CYS N N 119.018 0.2 1 242 40 42 CYS HA H 3.910 0.02 1 243 40 42 CYS HB2 H 3.147 0.02 2 244 40 42 CYS HB3 H 2.033 0.02 2 245 41 43 HIS H H 8.570 0.02 1 246 41 43 HIS N N 120.107 0.2 1 247 41 43 HIS HA H 4.436 0.02 1 248 41 43 HIS HB2 H 3.363 0.02 2 249 41 43 HIS HB3 H 3.110 0.02 2 250 41 43 HIS HD2 H 8.363 0.02 1 251 41 43 HIS HE1 H 7.247 0.02 1 252 42 44 GLU H H 8.238 0.02 1 253 42 44 GLU N N 119.454 0.2 1 254 42 44 GLU HA H 4.083 0.02 1 255 42 44 GLU HB2 H 2.122 0.02 1 256 42 44 GLU HG2 H 2.760 0.02 2 257 42 44 GLU HG3 H 2.421 0.02 2 258 43 45 ASN H H 8.448 0.02 1 259 43 45 ASN N N 115.856 0.2 1 260 43 45 ASN HA H 4.561 0.02 1 261 43 45 ASN HB2 H 2.855 0.02 2 262 43 45 ASN HB3 H 2.768 0.02 2 263 43 45 ASN HD21 H 7.747 0.02 2 264 43 45 ASN HD22 H 7.397 0.02 2 265 43 45 ASN ND2 N 111.690 0.2 1 266 44 46 LEU H H 7.702 0.02 1 267 44 46 LEU N N 121.043 0.2 1 268 44 46 LEU HA H 4.265 0.02 1 269 44 46 LEU HB2 H 2.296 0.02 2 270 44 46 LEU HB3 H 1.841 0.02 2 271 44 46 LEU HG H 1.555 0.02 1 272 44 46 LEU HD1 H 0.931 0.02 2 273 45 47 ILE H H 8.311 0.02 1 274 45 47 ILE N N 117.238 0.2 1 275 45 47 ILE HA H 3.896 0.02 1 276 45 47 ILE HB H 1.937 0.02 1 277 45 47 ILE HG12 H 1.261 0.02 1 278 45 47 ILE HG2 H 0.794 0.02 1 279 45 47 ILE HD1 H 0.794 0.02 1 280 46 48 ARG H H 8.640 0.02 1 281 46 48 ARG N N 117.975 0.2 1 282 46 48 ARG HA H 4.329 0.02 1 283 46 48 ARG HB2 H 2.024 0.02 2 284 46 48 ARG HB3 H 1.981 0.02 2 285 46 48 ARG HG2 H 1.730 0.02 1 286 46 48 ARG HD2 H 3.323 0.02 1 287 46 48 ARG HD3 H 3.192 0.02 1 288 46 48 ARG HE H 7.368 0.02 1 289 47 49 GLN H H 7.760 0.02 1 290 47 49 GLN N N 115.468 0.2 1 291 47 49 GLN HA H 4.123 0.02 1 292 47 49 GLN HB2 H 2.329 0.02 1 293 47 49 GLN HG2 H 2.330 0.02 1 294 47 49 GLN HE21 H 7.731 0.02 2 295 47 49 GLN HE22 H 6.900 0.02 2 296 48 50 THR H H 8.115 0.02 1 297 48 50 THR N N 108.986 0.2 1 298 48 50 THR HA H 4.565 0.02 1 299 48 50 THR HB H 4.379 0.02 1 300 48 50 THR HG2 H 1.127 0.02 1 301 49 51 ASN H H 8.645 0.02 1 302 49 51 ASN N N 119.741 0.2 1 303 49 51 ASN HA H 4.847 0.02 1 304 49 51 ASN HB2 H 2.762 0.02 2 305 49 51 ASN HB3 H 2.463 0.02 2 306 49 51 ASN HD21 H 7.561 0.02 2 307 49 51 ASN HD22 H 6.874 0.02 2 308 50 52 THR H H 7.815 0.02 1 309 50 52 THR HA H 4.108 0.02 1 310 50 52 THR HB H 4.085 0.02 1 311 50 52 THR HG2 H 1.355 0.02 1 312 51 53 HIS H H 8.704 0.02 1 313 51 53 HIS HA H 4.814 0.02 1 314 51 53 HIS HB2 H 3.163 0.02 2 315 51 53 HIS HB3 H 3.115 0.02 2 316 51 53 HIS HD2 H 8.515 0.02 1 317 51 53 HIS HE1 H 7.285 0.02 1 318 52 54 ILE H H 8.690 0.02 1 319 52 54 ILE N N 120.273 0.2 1 320 52 54 ILE HA H 3.700 0.02 1 321 52 54 ILE HB H 1.726 0.02 1 322 52 54 ILE HG12 H 0.924 0.02 1 323 52 54 ILE HG2 H 0.741 0.02 1 324 52 54 ILE HD1 H 0.565 0.02 1 325 53 55 ARG H H 9.692 0.02 1 326 53 55 ARG N N 131.890 0.2 1 327 53 55 ARG HA H 4.441 0.02 1 328 53 55 ARG HB2 H 1.661 0.02 1 329 53 55 ARG HG2 H 1.661 0.02 1 330 53 55 ARG HD2 H 3.237 0.02 1 331 53 55 ARG HE H 7.317 0.02 1 332 54 56 SER H H 7.958 0.02 1 333 54 56 SER N N 111.080 0.2 1 334 54 56 SER HA H 4.670 0.02 1 335 54 56 SER HB2 H 3.970 0.02 2 336 54 56 SER HB3 H 3.847 0.02 2 337 55 57 THR H H 8.550 0.02 1 338 55 57 THR N N 114.265 0.2 1 339 55 57 THR HA H 4.396 0.02 1 340 55 57 THR HB H 4.386 0.02 1 341 55 57 THR HG2 H 1.291 0.02 1 342 56 58 GLY H H 8.158 0.02 1 343 56 58 GLY N N 113.495 0.2 1 344 56 58 GLY HA2 H 4.349 0.02 2 345 56 58 GLY HA3 H 3.519 0.02 2 346 57 59 LYS H H 7.844 0.02 1 347 57 59 LYS N N 113.240 0.2 1 348 57 59 LYS HA H 4.130 0.02 1 349 57 59 LYS HB2 H 1.732 0.02 1 350 57 59 LYS HG2 H 1.367 0.02 1 351 57 59 LYS HD2 H 1.732 0.02 1 352 57 59 LYS HE2 H 2.975 0.02 1 353 58 60 CYS H H 8.262 0.02 1 354 58 60 CYS N N 120.376 0.2 1 355 58 60 CYS HA H 4.477 0.02 1 356 58 60 CYS HB2 H 3.148 0.02 2 357 58 60 CYS HB3 H 2.584 0.02 2 358 59 61 GLU H H 8.149 0.02 1 359 59 61 GLU N N 126.966 0.2 1 360 59 61 GLU HA H 4.095 0.02 1 361 59 61 GLU HB2 H 2.034 0.02 2 362 59 61 GLU HB3 H 1.855 0.02 2 363 59 61 GLU HG2 H 2.176 0.02 1 stop_ save_