data_6180 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the 15th domain of LEKTI ; _BMRB_accession_number 6180 _BMRB_flat_file_name bmr6180.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" 365 "15N chemical shifts" 79 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-17 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6179 'LEKTI Domain 15 short' stop_ _Original_release_date 2005-05-17 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 'Serine Proteinase Inhibitor' 'Trypsin Inhibitor' Kazal LEKTI stop_ save_ ################################## # Molecular system description # ################################## save_system_LEKTI_Domain_15 _Saveframe_category molecular_system _Mol_system_name 'LEKTI Domain 15' _Abbreviation_common 'LEKTI Domain 15' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LEKTI Domain 15' $LEKTI_Domain_15 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'serine proteinase inhibitor' Kazal-type stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LEKTI_Domain_15 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LEKTI Domain 15' _Name_variant none _Abbreviation_common 'LEKTI Domain 15' _Molecular_mass 8569.6 _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 78 _Mol_residue_sequence ; GPDSEMCKDYRVLPRIGYLC PKDLKPVCGDDGQTYNNPCM LCHENLIRQTNTHIRSTGKC EESSTPGTTAASMPPSDE ; 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 62 60 GLU 63 61 SER 64 62 SER 65 63 THR 66 64 PRO 67 65 GLY 68 66 THR 69 67 THR 70 68 ALA 71 69 ALA 72 70 SER 73 71 MET 74 72 PRO 75 73 PRO 76 74 SER 77 75 ASP 78 76 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 PDB 1UVG 'Solution Structure Of The 15th Domain Of Lekti' 100.00 78 100.00 100.00 7.49e-39 PDB 1UVF 'Solution Structure Of The Structured Part Of The 15th Domain Of Lekti' 78.21 61 100.00 100.00 4.41e-29 BMRB 6179 'LEKTI Domain 15 short' 78.21 61 100.00 100.00 4.41e-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 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 '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 1.6 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 2.3 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-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_2D-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _Sample_label . save_ save_2D-COESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-COESY _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,15-NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H,1H,15-NOESY-HSQC _Sample_label . save_ save_3D-1H,1H,15N-TOCSY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H,1H,15N-TOCSY-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 pH 6.4 0.1 pH temperature 298 1 K 'ionic strength' 50 . mM pressure 1 . atm 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_ _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' _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 8.587 0.02 1 2 1 3 ASP HA H 4.604 0.02 1 3 1 3 ASP HB2 H 2.706 0.02 1 4 1 3 ASP N N 120.645 0.2 1 5 2 4 SER H H 8.275 0.02 1 6 2 4 SER HA H 4.382 0.02 1 7 2 4 SER HB3 H 3.888 0.02 1 8 2 4 SER N N 116.559 0.2 1 9 3 5 GLU H H 8.392 0.02 1 10 3 5 GLU HA H 4.200 0.02 1 11 3 5 GLU HB2 H 2.032 0.02 1 12 3 5 GLU HG2 H 2.286 0.02 1 13 3 5 GLU N N 122.418 0.2 1 14 4 6 MET H H 8.068 0.02 1 15 4 6 MET HA H 4.172 0.02 1 16 4 6 MET HB2 H 2.198 0.02 1 17 4 6 MET HG2 H 2.538 0.02 1 18 4 6 MET N N 118.770 0.2 1 19 5 7 CYS H H 8.023 0.02 1 20 5 7 CYS HA H 4.851 0.02 1 21 5 7 CYS HB2 H 3.571 0.02 2 22 5 7 CYS HB3 H 2.939 0.02 2 23 5 7 CYS N N 114.537 0.2 1 24 6 8 LYS H H 7.445 0.02 1 25 6 8 LYS HA H 4.201 0.02 1 26 6 8 LYS HB2 H 1.909 0.02 1 27 6 8 LYS HG2 H 1.459 0.02 2 28 6 8 LYS HG3 H 1.370 0.02 2 29 6 8 LYS HD2 H 1.682 0.02 1 30 6 8 LYS HE2 H 2.950 0.02 1 31 6 8 LYS N N 119.411 0.2 1 32 7 9 ASP H H 8.014 0.02 1 33 7 9 ASP HA H 4.505 0.02 1 34 7 9 ASP HB2 H 2.430 0.02 2 35 7 9 ASP HB3 H 1.864 0.02 2 36 7 9 ASP N N 117.597 0.2 1 37 8 10 TYR H H 7.396 0.02 1 38 8 10 TYR HA H 5.015 0.02 1 39 8 10 TYR HB2 H 3.504 0.02 2 40 8 10 TYR HB3 H 2.962 0.02 2 41 8 10 TYR HD1 H 7.170 0.02 1 42 8 10 TYR HD2 H 7.090 0.02 1 43 8 10 TYR HE1 H 6.790 0.02 1 44 8 10 TYR HE2 H 6.820 0.02 1 45 8 10 TYR N N 119.489 0.2 1 46 9 11 ARG H H 9.171 0.02 1 47 9 11 ARG HA H 4.354 0.02 1 48 9 11 ARG HB2 H 1.864 0.02 1 49 9 11 ARG HG2 H 1.636 0.02 1 50 9 11 ARG HD3 H 3.249 0.02 1 51 9 11 ARG HE H 7.224 0.02 1 52 9 11 ARG N N 123.480 0.2 1 53 9 11 ARG NE N 84.718 0.2 1 54 10 12 VAL H H 8.081 0.02 1 55 10 12 VAL HA H 4.176 0.02 1 56 10 12 VAL HB H 1.312 0.02 1 57 10 12 VAL HG1 H 0.551 0.02 2 58 10 12 VAL HG2 H 0.182 0.02 2 59 10 12 VAL N N 121.801 0.2 1 60 11 13 LEU H H 8.577 0.02 1 61 11 13 LEU HA H 4.900 0.02 1 62 11 13 LEU HB2 H 1.549 0.02 1 63 11 13 LEU HG H 1.549 0.02 1 64 11 13 LEU HD1 H 0.901 0.02 1 65 11 13 LEU HD2 H 0.901 0.02 1 66 11 13 LEU N N 128.850 0.2 1 67 12 14 PRO HA H 4.225 0.02 1 68 12 14 PRO HB2 H 2.343 0.02 2 69 12 14 PRO HB3 H 2.000 0.02 2 70 12 14 PRO HG2 H 2.110 0.02 1 71 12 14 PRO HD2 H 3.880 0.02 2 72 12 14 PRO HD3 H 3.655 0.02 2 73 13 15 ARG H H 8.759 0.02 1 74 13 15 ARG HA H 3.828 0.02 1 75 13 15 ARG HB2 H 2.217 0.02 2 76 13 15 ARG HB3 H 2.017 0.02 2 77 13 15 ARG HG2 H 1.566 0.02 1 78 13 15 ARG HD3 H 3.210 0.02 1 79 13 15 ARG HE H 7.249 0.02 1 80 13 15 ARG N N 117.347 0.2 1 81 13 15 ARG NE N 84.259 0.2 1 82 14 16 ILE H H 8.295 0.02 1 83 14 16 ILE HA H 4.124 0.02 1 84 14 16 ILE HB H 1.709 0.02 1 85 14 16 ILE HG12 H 1.471 0.02 2 86 14 16 ILE HG13 H 1.119 0.02 2 87 14 16 ILE HG2 H 0.856 0.02 1 88 14 16 ILE HD1 H 0.856 0.02 1 89 14 16 ILE N N 119.747 0.2 1 90 15 17 GLY H H 8.164 0.02 1 91 15 17 GLY HA2 H 4.550 0.02 2 92 15 17 GLY HA3 H 3.532 0.02 2 93 15 17 GLY N N 108.362 0.2 1 94 16 18 TYR H H 9.545 0.02 1 95 16 18 TYR HA H 4.810 0.02 1 96 16 18 TYR HB2 H 2.930 0.02 2 97 16 18 TYR HB3 H 2.660 0.02 2 98 16 18 TYR HD1 H 7.080 0.02 3 99 16 18 TYR HE1 H 6.840 0.02 3 100 16 18 TYR N N 122.355 0.2 1 101 17 19 LEU H H 8.607 0.02 1 102 17 19 LEU HA H 4.535 0.02 1 103 17 19 LEU HB2 H 1.559 0.02 1 104 17 19 LEU HG H 1.559 0.02 1 105 17 19 LEU HD1 H 0.842 0.02 1 106 17 19 LEU HD2 H 0.842 0.02 1 107 17 19 LEU N N 124.619 0.2 1 108 18 20 CYS H H 8.138 0.02 1 109 18 20 CYS HA H 5.430 0.02 1 110 18 20 CYS HB2 H 2.911 0.02 2 111 18 20 CYS HB3 H 2.560 0.02 2 112 18 20 CYS N N 121.348 0.2 1 113 19 21 PRO HA H 4.660 0.02 1 114 19 21 PRO HB2 H 2.481 0.02 2 115 19 21 PRO HB3 H 2.084 0.02 2 116 19 21 PRO HG2 H 2.280 0.02 1 117 19 21 PRO HD2 H 4.000 0.02 2 118 19 21 PRO HD3 H 3.340 0.02 2 119 20 22 LYS H H 8.684 0.02 1 120 20 22 LYS HA H 4.192 0.02 1 121 20 22 LYS HB2 H 1.929 0.02 1 122 20 22 LYS HG2 H 1.452 0.02 1 123 20 22 LYS HD2 H 1.704 0.02 1 124 20 22 LYS HE2 H 2.997 0.02 1 125 20 22 LYS N N 119.009 0.2 1 126 21 23 ASP H H 7.602 0.02 1 127 21 23 ASP HA H 4.268 0.02 1 128 21 23 ASP HB2 H 2.445 0.02 1 129 21 23 ASP N N 117.644 0.2 1 130 22 24 LEU H H 8.607 0.02 1 131 22 24 LEU HA H 4.538 0.02 1 132 22 24 LEU HB2 H 1.647 0.02 1 133 22 24 LEU HG H 1.650 0.02 1 134 22 24 LEU HD1 H 0.920 0.02 1 135 22 24 LEU HD2 H 0.920 0.02 1 136 22 24 LEU N N 124.792 0.2 1 137 23 25 LYS H H 8.877 0.02 1 138 23 25 LYS HA H 4.618 0.02 1 139 23 25 LYS HB2 H 1.897 0.02 1 140 23 25 LYS HG2 H 1.406 0.02 1 141 23 25 LYS HD2 H 1.690 0.02 1 142 23 25 LYS HE2 H 3.030 0.02 1 143 23 25 LYS N N 128.318 0.2 1 144 24 26 PRO HA H 4.680 0.02 1 145 24 26 PRO HB2 H 2.074 0.02 2 146 24 26 PRO HB3 H 1.481 0.02 2 147 24 26 PRO HG2 H 1.904 0.02 1 148 24 26 PRO HD2 H 3.624 0.02 2 149 24 26 PRO HD3 H 3.369 0.02 2 150 25 27 VAL H H 8.511 0.02 1 151 25 27 VAL HA H 4.759 0.02 1 152 25 27 VAL HB H 2.179 0.02 1 153 25 27 VAL HG1 H 1.044 0.02 2 154 25 27 VAL HG2 H 0.675 0.02 2 155 25 27 VAL N N 111.573 0.2 1 156 26 28 CYS H H 8.869 0.02 1 157 26 28 CYS HA H 5.328 0.02 1 158 26 28 CYS HB2 H 3.118 0.02 2 159 26 28 CYS HB3 H 2.682 0.02 2 160 26 28 CYS N N 121.561 0.2 1 161 27 29 GLY H H 9.822 0.02 1 162 27 29 GLY HA2 H 4.777 0.02 2 163 27 29 GLY HA3 H 4.215 0.02 2 164 27 29 GLY N N 116.035 0.2 1 165 28 30 ASP H H 9.138 0.02 1 166 28 30 ASP HA H 4.407 0.02 1 167 28 30 ASP HB2 H 3.124 0.02 2 168 28 30 ASP HB3 H 2.504 0.02 2 169 28 30 ASP N N 120.715 0.2 1 170 29 31 ASP H H 8.384 0.02 1 171 29 31 ASP HA H 4.539 0.02 1 172 29 31 ASP HB2 H 3.084 0.02 2 173 29 31 ASP HB3 H 2.730 0.02 2 174 29 31 ASP N N 117.211 0.2 1 175 30 32 GLY H H 8.515 0.02 1 176 30 32 GLY HA2 H 4.100 0.02 2 177 30 32 GLY HA3 H 3.744 0.02 2 178 30 32 GLY N N 109.346 0.2 1 179 31 33 GLN H H 7.933 0.02 1 180 31 33 GLN HA H 4.466 0.02 1 181 31 33 GLN HB2 H 1.733 0.02 1 182 31 33 GLN HG3 H 1.969 0.02 1 183 31 33 GLN HE21 H 7.221 0.02 2 184 31 33 GLN HE22 H 6.764 0.02 2 185 31 33 GLN N N 120.025 0.2 1 186 31 33 GLN NE2 N 112.507 0.2 1 187 32 34 THR H H 8.420 0.02 1 188 32 34 THR HA H 4.955 0.02 1 189 32 34 THR HB H 3.961 0.02 1 190 32 34 THR HG2 H 1.165 0.02 1 191 32 34 THR N N 121.586 0.2 1 192 33 35 TYR H H 9.423 0.02 1 193 33 35 TYR HA H 4.542 0.02 1 194 33 35 TYR HB2 H 2.729 0.02 2 195 33 35 TYR HB3 H 2.542 0.02 2 196 33 35 TYR HD1 H 8.500 0.02 3 197 33 35 TYR HE1 H 6.850 0.02 3 198 33 35 TYR N N 127.474 0.2 1 199 34 36 ASN H H 9.151 0.02 1 200 34 36 ASN HA H 4.210 0.02 1 201 34 36 ASN HB2 H 2.772 0.02 1 202 34 36 ASN HD21 H 7.445 0.02 2 203 34 36 ASN HD22 H 6.832 0.02 2 204 34 36 ASN N N 120.715 0.2 1 205 34 36 ASN ND2 N 110.319 0.2 1 206 35 37 ASN H H 7.456 0.02 1 207 35 37 ASN HA H 5.157 0.02 1 208 35 37 ASN HB2 H 3.360 0.02 2 209 35 37 ASN HB3 H 3.036 0.02 2 210 35 37 ASN HD21 H 7.934 0.02 2 211 35 37 ASN HD22 H 6.370 0.02 2 212 35 37 ASN N N 107.038 0.2 1 213 35 37 ASN ND2 N 113.850 0.2 1 214 36 38 PRO HA H 4.008 0.02 1 215 36 38 PRO HB2 H 2.497 0.02 2 216 36 38 PRO HB3 H 2.222 0.02 2 217 36 38 PRO HG2 H 2.300 0.02 1 218 36 38 PRO HD2 H 4.179 0.02 2 219 36 38 PRO HD3 H 3.900 0.02 2 220 37 39 CYS H H 7.563 0.02 1 221 37 39 CYS HA H 3.189 0.02 1 222 37 39 CYS HB2 H 2.726 0.02 2 223 37 39 CYS HB3 H 0.873 0.02 2 224 37 39 CYS N N 115.586 0.2 1 225 38 40 MET H H 7.913 0.02 1 226 38 40 MET HA H 4.293 0.02 1 227 38 40 MET HB2 H 2.432 0.02 2 228 38 40 MET HB3 H 2.205 0.02 2 229 38 40 MET HG2 H 2.718 0.02 1 230 38 40 MET N N 118.351 0.2 1 231 39 41 LEU H H 6.907 0.02 1 232 39 41 LEU HA H 3.605 0.02 1 233 39 41 LEU HB2 H 1.776 0.02 2 234 39 41 LEU HB3 H 0.450 0.02 2 235 39 41 LEU HG H 0.912 0.02 1 236 39 41 LEU HD1 H 0.445 0.02 2 237 39 41 LEU N N 121.877 0.2 1 238 39 41 LEU HD2 H -0.025 0.2 2 239 40 42 CYS H H 7.706 0.02 1 240 40 42 CYS HA H 3.909 0.02 1 241 40 42 CYS HB2 H 3.137 0.02 2 242 40 42 CYS HB3 H 2.034 0.02 2 243 40 42 CYS N N 118.988 0.2 1 244 41 43 HIS H H 8.645 0.02 1 245 41 43 HIS HA H 4.385 0.02 1 246 41 43 HIS HB2 H 3.420 0.02 2 247 41 43 HIS HB3 H 3.127 0.02 2 248 41 43 HIS HD2 H 8.306 0.02 1 249 41 43 HIS HE1 H 7.101 0.02 1 250 41 43 HIS N N 119.632 0.2 1 251 42 44 GLU H H 8.300 0.02 1 252 42 44 GLU HA H 4.084 0.02 1 253 42 44 GLU HB2 H 2.130 0.02 1 254 42 44 GLU HG2 H 2.782 0.02 2 255 42 44 GLU HG3 H 2.458 0.02 2 256 42 44 GLU N N 119.286 0.2 1 257 43 45 ASN H H 8.464 0.02 1 258 43 45 ASN HA H 4.549 0.02 1 259 43 45 ASN HB2 H 2.799 0.02 1 260 43 45 ASN HD21 H 7.672 0.02 2 261 43 45 ASN HD22 H 7.391 0.02 2 262 43 45 ASN N N 116.223 0.2 1 263 43 45 ASN ND2 N 111.298 0.2 1 264 44 46 LEU H H 7.675 0.02 1 265 44 46 LEU HA H 4.265 0.02 1 266 44 46 LEU HB2 H 2.252 0.02 2 267 44 46 LEU HB3 H 1.847 0.02 2 268 44 46 LEU HG H 1.559 0.02 1 269 44 46 LEU HD1 H 0.939 0.02 1 270 44 46 LEU HD2 H 0.939 0.02 1 271 44 46 LEU N N 120.645 0.2 1 272 45 47 ILE H H 8.161 0.02 1 273 45 47 ILE HA H 3.907 0.02 1 274 45 47 ILE HB H 1.906 0.02 1 275 45 47 ILE HG12 H 1.266 0.02 1 276 45 47 ILE HG2 H 0.815 0.02 1 277 45 47 ILE HD1 H 0.815 0.02 1 278 45 47 ILE N N 116.799 0.2 1 279 46 48 ARG H H 8.593 0.02 1 280 46 48 ARG HA H 4.326 0.02 1 281 46 48 ARG HB2 H 1.968 0.02 1 282 46 48 ARG HG2 H 1.719 0.02 1 283 46 48 ARG HD2 H 3.190 0.02 2 284 46 48 ARG HD3 H 3.320 0.02 2 285 46 48 ARG HE H 7.296 0.02 1 286 46 48 ARG N N 117.616 0.2 1 287 46 48 ARG NE N 85.297 0.2 1 288 47 49 GLN H H 7.767 0.02 1 289 47 49 GLN HA H 4.113 0.02 1 290 47 49 GLN HB2 H 2.335 0.02 1 291 47 49 GLN HG2 H 2.335 0.02 1 292 47 49 GLN HE21 H 7.710 0.02 2 293 47 49 GLN HE22 H 6.883 0.02 2 294 47 49 GLN N N 115.331 0.2 1 295 47 49 GLN NE2 N 113.034 0.2 1 296 48 50 THR H H 8.094 0.02 1 297 48 50 THR HA H 4.562 0.02 1 298 48 50 THR HB H 4.361 0.02 1 299 48 50 THR HG2 H 1.126 0.02 1 300 48 50 THR N N 108.863 0.2 1 301 49 51 ASN H H 8.573 0.02 1 302 49 51 ASN HA H 4.815 0.02 1 303 49 51 ASN HB2 H 2.728 0.02 2 304 49 51 ASN HB3 H 2.441 0.02 2 305 49 51 ASN HD21 H 7.544 0.02 2 306 49 51 ASN HD22 H 6.890 0.02 2 307 49 51 ASN N N 119.772 0.2 1 308 49 51 ASN ND2 N 112.062 0.2 1 309 50 52 THR H H 7.773 0.02 1 310 50 52 THR HA H 4.071 0.02 1 311 50 52 THR HB H 4.063 0.02 1 312 50 52 THR HG2 H 1.360 0.02 1 313 50 52 THR N N 118.457 0.2 1 314 51 53 HIS H H 8.794 0.02 1 315 51 53 HIS HA H 4.824 0.02 1 316 51 53 HIS HB2 H 3.330 0.02 2 317 51 53 HIS HB3 H 3.111 0.02 2 318 51 53 HIS HD2 H 8.410 0.02 1 319 51 53 HIS HE1 H 7.270 0.02 1 320 51 53 HIS N N 125.159 0.2 1 321 52 54 ILE H H 8.803 0.02 1 322 52 54 ILE HA H 3.684 0.02 1 323 52 54 ILE HB H 1.720 0.02 1 324 52 54 ILE HG12 H 0.918 0.02 1 325 52 54 ILE HG2 H 0.736 0.02 1 326 52 54 ILE HD1 H 0.577 0.02 1 327 52 54 ILE N N 120.553 0.2 1 328 53 55 ARG H H 9.704 0.02 1 329 53 55 ARG HA H 4.451 0.02 1 330 53 55 ARG HB2 H 1.678 0.02 1 331 53 55 ARG HG2 H 1.678 0.02 1 332 53 55 ARG HD2 H 3.233 0.02 1 333 53 55 ARG HE H 7.313 0.02 1 334 53 55 ARG N N 131.659 0.2 1 335 53 55 ARG NE N 84.775 0.2 1 336 54 56 SER H H 7.950 0.02 1 337 54 56 SER HA H 4.685 0.02 1 338 54 56 SER HB2 H 3.977 0.02 2 339 54 56 SER HB3 H 3.842 0.02 2 340 54 56 SER N N 110.902 0.2 1 341 55 57 THR H H 8.537 0.02 1 342 55 57 THR HA H 4.401 0.02 1 343 55 57 THR HB H 4.357 0.02 1 344 55 57 THR HG2 H 1.279 0.02 1 345 55 57 THR N N 114.030 0.2 1 346 56 58 GLY H H 8.168 0.02 1 347 56 58 GLY HA2 H 4.367 0.02 2 348 56 58 GLY HA3 H 3.522 0.02 2 349 56 58 GLY N N 113.218 0.2 1 350 57 59 LYS H H 7.917 0.02 1 351 57 59 LYS HA H 4.125 0.02 1 352 57 59 LYS HB2 H 1.812 0.02 1 353 57 59 LYS HG2 H 1.402 0.02 1 354 57 59 LYS HD2 H 1.668 0.02 1 355 57 59 LYS HE2 H 2.953 0.02 1 356 57 59 LYS N N 113.221 0.2 1 357 58 60 CYS H H 8.382 0.02 1 358 58 60 CYS HA H 4.450 0.02 1 359 58 60 CYS HB2 H 3.086 0.02 2 360 58 60 CYS HB3 H 2.588 0.02 2 361 58 60 CYS N N 120.746 0.2 1 362 59 61 GLU H H 8.859 0.02 1 363 59 61 GLU HA H 4.230 0.02 1 364 59 61 GLU HB2 H 1.937 0.02 1 365 59 61 GLU HG2 H 2.277 0.02 1 366 59 61 GLU N N 121.157 0.2 1 367 60 62 GLU H H 8.297 0.02 1 368 60 62 GLU HA H 4.310 0.02 1 369 60 62 GLU HB2 H 1.959 0.02 1 370 60 62 GLU HG2 H 2.267 0.02 1 371 60 62 GLU N N 121.704 0.2 1 372 61 63 SER H H 8.275 0.02 1 373 61 63 SER HA H 4.308 0.02 1 374 61 63 SER HB2 H 3.900 0.02 1 375 61 63 SER N N 116.511 0.2 1 376 62 64 SER H H 8.355 0.02 1 377 62 64 SER HA H 4.537 0.02 1 378 62 64 SER HB2 H 3.883 0.02 1 379 62 64 SER N N 117.921 0.2 1 380 63 65 THR H H 8.244 0.02 1 381 63 65 THR HA H 4.635 0.02 1 382 63 65 THR HB H 4.158 0.02 1 383 63 65 THR HG2 H 1.239 0.02 1 384 63 65 THR N N 118.133 0.2 1 385 64 66 PRO HA H 4.410 0.02 1 386 64 66 PRO HB2 H 1.950 0.02 1 387 64 66 PRO HG2 H 1.950 0.02 1 388 64 66 PRO HD2 H 3.850 0.02 1 389 65 67 GLY H H 8.517 0.02 1 390 65 67 GLY HA2 H 4.030 0.02 1 391 65 67 GLY N N 109.382 0.2 1 392 66 68 THR H H 8.045 0.02 1 393 66 68 THR HA H 4.449 0.02 1 394 66 68 THR HB H 4.271 0.02 1 395 66 68 THR HG2 H 1.212 0.02 1 396 66 68 THR N N 113.421 0.2 1 397 67 69 THR H H 8.225 0.02 1 398 67 69 THR HA H 4.380 0.02 1 399 67 69 THR HB H 4.380 0.02 1 400 67 69 THR HG2 H 1.220 0.02 1 401 67 69 THR N N 116.723 0.2 1 402 68 70 ALA H H 8.357 0.02 1 403 68 70 ALA HA H 4.321 0.02 1 404 68 70 ALA HB H 1.403 0.02 1 405 68 70 ALA N N 126.732 0.2 1 406 69 71 ALA H H 8.335 0.02 1 407 69 71 ALA HA H 4.353 0.02 1 408 69 71 ALA HB H 1.395 0.02 1 409 69 71 ALA N N 127.607 0.2 1 410 70 72 SER H H 8.185 0.02 1 411 70 72 SER HA H 4.442 0.02 1 412 70 72 SER HB2 H 3.859 0.02 1 413 70 72 SER N N 114.871 0.2 1 414 71 73 MET H H 8.245 0.02 1 415 71 73 MET HA H 4.832 0.02 1 416 71 73 MET HB2 H 1.975 0.02 1 417 71 73 MET HG2 H 2.611 0.02 1 418 71 73 MET N N 123.167 0.2 1 419 72 74 PRO HA H 4.670 0.02 1 420 72 74 PRO HB2 H 2.030 0.02 2 421 72 74 PRO HB3 H 1.810 0.02 2 422 72 74 PRO HG2 H 2.060 0.02 1 423 72 74 PRO HD2 H 3.990 0.02 2 424 72 74 PRO HD3 H 3.480 0.02 2 425 73 75 PRO HA H 4.450 0.02 1 426 73 75 PRO HB2 H 2.320 0.02 2 427 73 75 PRO HB3 H 1.880 0.02 2 428 73 75 PRO HG2 H 1.990 0.02 1 429 73 75 PRO HD2 H 3.850 0.02 2 430 73 75 PRO HD3 H 3.640 0.02 2 431 74 76 SER H H 8.274 0.02 1 432 74 76 SER HA H 4.420 0.02 1 433 74 76 SER HB2 H 3.875 0.02 1 434 74 76 SER N N 115.375 0.2 1 435 75 77 ASP H H 8.463 0.02 1 436 75 77 ASP HA H 4.589 0.02 1 437 75 77 ASP HB2 H 2.694 0.02 1 438 75 77 ASP N N 120.891 0.2 1 439 76 78 GLU H H 7.862 0.02 1 440 76 78 GLU HA H 4.122 0.02 1 441 76 78 GLU HB2 H 2.074 0.02 2 442 76 78 GLU HB3 H 1.876 0.02 2 443 76 78 GLU HG2 H 2.211 0.02 1 444 76 78 GLU N N 125.337 0.2 1 stop_ save_