data_19563 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; chemical shift assignments for human dihdyrofolate reductase bound to folate ; _BMRB_accession_number 19563 _BMRB_flat_file_name bmr19563.str _Entry_type original _Submission_date 2013-10-18 _Accession_date 2013-10-18 _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 Wright Peter E. . 2 Bhabha Gira . . 3 Tuttle Lisa M. . 4 Kroon Gerard J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 180 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-04-04 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 19564 'DHFR bound to THF' 19565 'DHFR bound to NADP+ and THF' 19566 'DHFR bound to NADPH' 19567 'DHFR bound to NADP+ and folate' stop_ _Original_release_date 2016-04-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Side Chain Conformational Averaging in Human Dihydrofolate Reductase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24498949 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tuttle Lisa M. . 2 Dyson 'H. Jane' . . 3 Wright Peter E. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 53 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1134 _Page_last 1145 _Year 2014 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full . _Citation_title ; The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains ; _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 Tuttle Lisa M. . 2 Dyson H. Jane . 3 Wright Peter E. . stop_ _Journal_abbreviation 'Not known' _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DHFR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DHFR $DHFR Folate $entity_FOL 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_DHFR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DHFR _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 187 _Mol_residue_sequence ; MVGSLNCIVAVSQNMGIGKN GDLPWPPLRNEFRYFQRMTT TSSVEGKQNLVIMGKKTWFS IPEKNRPLKGRINLVLSREL KEPPQGAHFLSRSLDDALKL TEQPELANKVDMVWIVGGSS VYKEAMNHPGHLKLFVTRIM QDFESDTFFPEIDLEKYKLL PEYPGVLSDVQEEKGIKYKF EVYEKND ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 VAL 3 2 GLY 4 3 SER 5 4 LEU 6 5 ASN 7 6 CYS 8 7 ILE 9 8 VAL 10 9 ALA 11 10 VAL 12 11 SER 13 12 GLN 14 13 ASN 15 14 MET 16 15 GLY 17 16 ILE 18 17 GLY 19 18 LYS 20 19 ASN 21 20 GLY 22 21 ASP 23 22 LEU 24 23 PRO 25 24 TRP 26 25 PRO 27 26 PRO 28 27 LEU 29 28 ARG 30 29 ASN 31 30 GLU 32 31 PHE 33 32 ARG 34 33 TYR 35 34 PHE 36 35 GLN 37 36 ARG 38 37 MET 39 38 THR 40 39 THR 41 40 THR 42 41 SER 43 42 SER 44 43 VAL 45 44 GLU 46 45 GLY 47 46 LYS 48 47 GLN 49 48 ASN 50 49 LEU 51 50 VAL 52 51 ILE 53 52 MET 54 53 GLY 55 54 LYS 56 55 LYS 57 56 THR 58 57 TRP 59 58 PHE 60 59 SER 61 60 ILE 62 61 PRO 63 62 GLU 64 63 LYS 65 64 ASN 66 65 ARG 67 66 PRO 68 67 LEU 69 68 LYS 70 69 GLY 71 70 ARG 72 71 ILE 73 72 ASN 74 73 LEU 75 74 VAL 76 75 LEU 77 76 SER 78 77 ARG 79 78 GLU 80 79 LEU 81 80 LYS 82 81 GLU 83 82 PRO 84 83 PRO 85 84 GLN 86 85 GLY 87 86 ALA 88 87 HIS 89 88 PHE 90 89 LEU 91 90 SER 92 91 ARG 93 92 SER 94 93 LEU 95 94 ASP 96 95 ASP 97 96 ALA 98 97 LEU 99 98 LYS 100 99 LEU 101 100 THR 102 101 GLU 103 102 GLN 104 103 PRO 105 104 GLU 106 105 LEU 107 106 ALA 108 107 ASN 109 108 LYS 110 109 VAL 111 110 ASP 112 111 MET 113 112 VAL 114 113 TRP 115 114 ILE 116 115 VAL 117 116 GLY 118 117 GLY 119 118 SER 120 119 SER 121 120 VAL 122 121 TYR 123 122 LYS 124 123 GLU 125 124 ALA 126 125 MET 127 126 ASN 128 127 HIS 129 128 PRO 130 129 GLY 131 130 HIS 132 131 LEU 133 132 LYS 134 133 LEU 135 134 PHE 136 135 VAL 137 136 THR 138 137 ARG 139 138 ILE 140 139 MET 141 140 GLN 142 141 ASP 143 142 PHE 144 143 GLU 145 144 SER 146 145 ASP 147 146 THR 148 147 PHE 149 148 PHE 150 149 PRO 151 150 GLU 152 151 ILE 153 152 ASP 154 153 LEU 155 154 GLU 156 155 LYS 157 156 TYR 158 157 LYS 159 158 LEU 160 159 LEU 161 160 PRO 162 161 GLU 163 162 TYR 164 163 PRO 165 164 GLY 166 165 VAL 167 166 LEU 168 167 SER 169 168 ASP 170 169 VAL 171 170 GLN 172 171 GLU 173 172 GLU 174 173 LYS 175 174 GLY 176 175 ILE 177 176 LYS 178 177 TYR 179 178 LYS 180 179 PHE 181 180 GLU 182 181 VAL 183 182 TYR 184 183 GLU 185 184 LYS 186 185 ASN 187 186 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_FOL _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'FOLIC ACID' _BMRB_code FOL _PDB_code FOL _Molecular_mass 441.397 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? NA2 NA2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4A C4A C . 0 . ? N5 N5 N . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? N8 N8 N . 0 . ? C8A C8A C . 0 . ? C9 C9 C . 0 . ? N10 N10 N . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C C C . 0 . ? O O O . 0 . ? N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE1 OE1 O . 0 . ? OE2 OE2 O . 0 . ? CT CT C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? H7 H7 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? HN0 HN0 H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? H15 H15 H . 0 . ? H16 H16 H . 0 . ? HN HN H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HG1 HG1 H . 0 . ? HG2 HG2 H . 0 . ? HOE2 HOE2 H . 0 . ? HO2 HO2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? SING N1 C8A ? ? SING N1 HN1 ? ? SING C2 NA2 ? ? DOUB C2 N3 ? ? SING NA2 HN21 ? ? SING NA2 HN22 ? ? SING N3 C4 ? ? DOUB C4 O4 ? ? SING C4 C4A ? ? SING C4A N5 ? ? DOUB C4A C8A ? ? DOUB N5 C6 ? ? SING C6 C7 ? ? SING C6 C9 ? ? DOUB C7 N8 ? ? SING C7 H7 ? ? SING N8 C8A ? ? SING C9 N10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING N10 C14 ? ? SING N10 HN0 ? ? DOUB C11 C12 ? ? SING C11 C16 ? ? SING C11 C ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 H13 ? ? SING C14 C15 ? ? DOUB C15 C16 ? ? SING C15 H15 ? ? SING C16 H16 ? ? DOUB C O ? ? SING C N ? ? SING N CA ? ? SING N HN ? ? SING CA CB ? ? SING CA CT ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CG CD ? ? SING CG HG1 ? ? SING CG HG2 ? ? DOUB CD OE1 ? ? SING CD OE2 ? ? SING OE2 HOE2 ? ? DOUB CT O1 ? ? SING CT O2 ? ? SING O2 HO2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DHFR human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DHFR 'recombinant technology' . Escherichia coli . pET21a 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 $DHFR 1000 uM '[U-99% 15N]' 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . K 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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 '3D HN(CO)CA' '3D HNCA' '3D HNCO' 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 DHFR _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 0 1 MET CA C 55.054 0.25 1 2 1 2 VAL H H 8.543 0.03 1 3 1 2 VAL CA C 62.356 0.25 1 4 1 2 VAL N N 122.193 0.15 1 5 2 3 GLY H H 8.771 0.03 1 6 2 3 GLY CA C 45.730 0.25 1 7 2 3 GLY N N 112.630 0.15 1 8 3 4 SER H H 7.658 0.03 1 9 3 4 SER CA C 57.693 0.25 1 10 3 4 SER N N 112.771 0.15 1 11 4 5 LEU H H 8.403 0.03 1 12 4 5 LEU CA C 54.439 0.25 1 13 4 5 LEU N N 123.881 0.15 1 14 5 6 ASN H H 7.964 0.03 1 15 5 6 ASN CA C 51.536 0.25 1 16 5 6 ASN N N 121.350 0.15 1 17 6 7 CYS H H 9.463 0.03 1 18 6 7 CYS CA C 57.518 0.25 1 19 6 7 CYS N N 119.240 0.15 1 20 7 8 ILE H H 9.156 0.03 1 21 7 8 ILE CA C 59.629 0.25 1 22 7 8 ILE N N 125.147 0.15 1 23 8 9 VAL H H 8.946 0.03 1 24 8 9 VAL CA C 62.356 0.25 1 25 8 9 VAL N N 125.428 0.15 1 26 9 10 ALA H H 7.176 0.03 1 27 9 10 ALA CA C 51.096 0.25 1 28 9 10 ALA N N 127.538 0.15 1 29 10 11 VAL H H 8.797 0.03 1 30 10 11 VAL CA C 57.781 0.25 1 31 10 11 VAL N N 113.896 0.15 1 32 11 12 SER H H 8.806 0.03 1 33 11 12 SER CA C 58.485 0.25 1 34 11 12 SER N N 115.021 0.15 1 35 12 13 GLN H H 8.183 0.03 1 36 12 13 GLN CA C 59.629 0.25 1 37 12 13 GLN N N 123.178 0.15 1 38 13 14 ASN H H 9.130 0.03 1 39 13 14 ASN CA C 52.855 0.25 1 40 13 14 ASN N N 112.208 0.15 1 41 14 15 MET H H 8.219 0.03 1 42 14 15 MET CA C 55.934 0.25 1 43 14 15 MET N N 110.802 0.15 1 44 15 16 GLY H H 8.245 0.03 1 45 15 16 GLY CA C 45.730 0.25 1 46 15 16 GLY N N 108.130 0.15 1 47 16 17 ILE H H 8.385 0.03 1 48 16 17 ILE CA C 60.860 0.25 1 49 16 17 ILE N N 109.255 0.15 1 50 17 18 GLY H H 7.123 0.03 1 51 17 18 GLY CA C 45.202 0.25 1 52 17 18 GLY N N 107.286 0.15 1 53 18 19 LYS H H 8.920 0.03 1 54 18 19 LYS CA C 55.758 0.25 1 55 18 19 LYS N N 123.178 0.15 1 56 19 20 ASN H H 10.760 0.03 1 57 19 20 ASN CA C 54.351 0.25 1 58 19 20 ASN N N 130.350 0.15 1 59 20 21 GLY H H 9.279 0.03 1 60 20 21 GLY CA C 45.378 0.25 1 61 20 21 GLY N N 105.458 0.15 1 62 21 22 ASP H H 7.737 0.03 1 63 21 22 ASP CA C 51.711 0.25 1 64 21 22 ASP N N 120.787 0.15 1 65 22 23 LEU H H 8.744 0.03 1 66 22 23 LEU CA C 53.025 0.25 1 67 22 23 LEU N N 123.178 0.15 1 68 27 28 LEU CA C 52.415 0.25 1 69 28 29 ARG H H 8.534 0.03 1 70 28 29 ARG CA C 60.157 0.25 1 71 28 29 ARG N N 124.162 0.15 1 72 29 30 ASN H H 11.163 0.03 1 73 29 30 ASN CA C 55.758 0.25 1 74 29 30 ASN N N 121.068 0.15 1 75 30 31 GLU H H 7.526 0.03 1 76 30 31 GLU CA C 61.652 0.25 1 77 30 31 GLU N N 130.913 0.15 1 78 31 32 PHE H H 8.175 0.03 1 79 31 32 PHE CA C 58.309 0.25 1 80 31 32 PHE N N 117.131 0.15 1 81 32 33 ARG H H 8.096 0.03 1 82 32 33 ARG CA C 59.277 0.25 1 83 32 33 ARG N N 117.974 0.15 1 84 33 34 TYR H H 7.850 0.03 1 85 33 34 TYR CA C 61.916 0.25 1 86 33 34 TYR N N 124.303 0.15 1 87 34 35 PHE H H 8.350 0.03 1 88 34 35 PHE CA C 61.916 0.25 1 89 34 35 PHE N N 121.209 0.15 1 90 35 36 GLN H H 8.946 0.03 1 91 35 36 GLN CA C 59.805 0.25 1 92 35 36 GLN N N 122.615 0.15 1 93 36 37 ARG H H 8.744 0.03 1 94 36 37 ARG CA C 59.981 0.25 1 95 36 37 ARG N N 123.037 0.15 1 96 37 38 MET H H 8.464 0.03 1 97 37 38 MET CA C 56.286 0.25 1 98 37 38 MET N N 118.256 0.15 1 99 38 39 THR H H 6.808 0.03 1 100 38 39 THR CA C 63.148 0.25 1 101 38 39 THR N N 102.504 0.15 1 102 39 40 THR H H 7.439 0.03 1 103 39 40 THR CA C 65.259 0.25 1 104 39 40 THR N N 115.302 0.15 1 105 40 41 THR H H 7.211 0.03 1 106 40 41 THR CA C 65.963 0.25 1 107 40 41 THR N N 117.412 0.15 1 108 41 42 SER H H 8.718 0.03 1 109 41 42 SER CA C 56.726 0.25 1 110 41 42 SER N N 126.694 0.15 1 111 42 43 SER H H 9.717 0.03 1 112 42 43 SER CA C 59.456 0.25 1 113 42 43 SER N N 121.350 0.15 1 114 43 44 VAL H H 7.701 0.03 1 115 43 44 VAL CA C 61.300 0.25 1 116 43 44 VAL N N 121.631 0.15 1 117 44 45 GLU H H 8.744 0.03 1 118 44 45 GLU CA C 58.045 0.25 1 119 44 45 GLU N N 128.663 0.15 1 120 45 46 GLY H H 8.911 0.03 1 121 45 46 GLY CA C 45.202 0.25 1 122 45 46 GLY N N 112.771 0.15 1 123 46 47 LYS H H 7.579 0.03 1 124 46 47 LYS CA C 55.670 0.25 1 125 46 47 LYS N N 118.115 0.15 1 126 47 48 GLN H H 8.464 0.03 1 127 47 48 GLN CA C 54.087 0.25 1 128 47 48 GLN N N 117.974 0.15 1 129 48 49 ASN H H 9.998 0.03 1 130 48 49 ASN CA C 51.536 0.25 1 131 48 49 ASN N N 120.506 0.15 1 132 49 50 LEU H H 9.007 0.03 1 133 49 50 LEU CA C 53.440 0.25 1 134 49 50 LEU N N 123.740 0.15 1 135 50 51 VAL H H 9.594 0.03 1 136 50 51 VAL CA C 59.717 0.25 1 137 50 51 VAL N N 123.459 0.15 1 138 51 52 ILE H H 9.156 0.03 1 139 51 52 ILE CA C 60.772 0.25 1 140 51 52 ILE N N 125.147 0.15 1 141 52 53 MET H H 8.806 0.03 1 142 52 53 MET CA C 52.327 0.25 1 143 52 53 MET N N 123.881 0.15 1 144 53 54 GLY H H 9.349 0.03 1 145 53 54 GLY CA C 44.322 0.25 1 146 53 54 GLY N N 107.286 0.15 1 147 54 55 LYS H H 8.332 0.03 1 148 54 55 LYS CA C 60.684 0.25 1 149 54 55 LYS N N 120.928 0.15 1 150 55 56 LYS H H 9.051 0.03 1 151 55 56 LYS CA C 59.981 0.25 1 152 55 56 LYS N N 117.834 0.15 1 153 56 57 THR H H 7.964 0.03 1 154 56 57 THR CA C 67.810 0.25 1 155 56 57 THR N N 118.818 0.15 1 156 57 58 TRP H H 7.929 0.03 1 157 57 58 TRP CA C 61.036 0.25 1 158 57 58 TRP N N 123.459 0.15 1 159 58 59 PHE H H 7.561 0.03 1 160 58 59 PHE CA C 61.388 0.25 1 161 58 59 PHE N N 110.099 0.15 1 162 59 60 SER H H 7.815 0.03 1 163 59 60 SER CA C 59.717 0.25 1 164 59 60 SER N N 116.990 0.15 1 165 60 61 ILE H H 7.132 0.03 1 166 60 61 ILE CA C 59.629 0.25 1 167 60 61 ILE N N 128.803 0.15 1 168 61 62 PRO CA C 63.324 0.25 1 169 62 63 GLU H H 8.657 0.03 1 170 62 63 GLU CA C 61.036 0.25 1 171 62 63 GLU N N 125.147 0.15 1 172 63 64 LYS H H 8.350 0.03 1 173 63 64 LYS CA C 57.957 0.25 1 174 63 64 LYS N N 115.021 0.15 1 175 64 65 ASN H H 8.192 0.03 1 176 64 65 ASN CA C 51.272 0.25 1 177 64 65 ASN N N 117.693 0.15 1 178 65 66 ARG H H 7.062 0.03 1 179 65 66 ARG CA C 53.295 0.25 1 180 65 66 ARG N N 116.990 0.15 1 181 66 67 PRO CA C 62.444 0.25 1 182 67 68 LEU H H 9.253 0.03 1 183 67 68 LEU CA C 55.494 0.25 1 184 67 68 LEU N N 119.943 0.15 1 185 68 69 LYS H H 8.850 0.03 1 186 68 69 LYS CA C 57.957 0.25 1 187 68 69 LYS N N 127.256 0.15 1 188 69 70 GLY CA C 45.993 0.25 1 189 70 71 ARG H H 7.526 0.03 1 190 70 71 ARG CA C 54.263 0.25 1 191 70 71 ARG N N 118.256 0.15 1 192 71 72 ILE H H 9.139 0.03 1 193 71 72 ILE CA C 61.564 0.25 1 194 71 72 ILE N N 124.584 0.15 1 195 72 73 ASN H H 12.838 0.03 1 196 72 73 ASN CA C 53.647 0.25 1 197 72 73 ASN N N 131.287 0.15 1 198 73 74 LEU H H 9.410 0.03 1 199 73 74 LEU CA C 54.790 0.25 1 200 73 74 LEU N N 129.647 0.15 1 201 74 75 VAL H H 8.280 0.03 1 202 74 75 VAL CA C 60.069 0.25 1 203 74 75 VAL N N 126.131 0.15 1 204 75 76 LEU H H 8.981 0.03 1 205 75 76 LEU CA C 52.074 0.25 1 206 75 76 LEU N N 127.678 0.15 1 207 76 77 SER H H 8.420 0.03 1 208 76 77 SER CA C 58.336 0.25 1 209 76 77 SER N N 115.724 0.15 1 210 77 78 ARG H H 9.980 0.03 1 211 77 78 ARG CA C 57.518 0.25 1 212 77 78 ARG N N 127.959 0.15 1 213 78 79 GLU H H 8.376 0.03 1 214 78 79 GLU CA C 57.349 0.25 1 215 78 79 GLU N N 118.396 0.15 1 216 79 80 LEU H H 7.386 0.03 1 217 79 80 LEU CA C 55.054 0.25 1 218 79 80 LEU N N 118.256 0.15 1 219 80 81 LYS H H 8.744 0.03 1 220 80 81 LYS CA C 56.198 0.25 1 221 80 81 LYS N N 118.256 0.15 1 222 81 82 GLU H H 7.500 0.03 1 223 81 82 GLU CA C 53.207 0.25 1 224 81 82 GLU N N 116.849 0.15 1 225 83 84 PRO CA C 62.092 0.25 1 226 84 85 GLN H H 8.473 0.03 1 227 84 85 GLN CA C 58.573 0.25 1 228 84 85 GLN N N 121.490 0.15 1 229 85 86 GLY CA C 45.114 0.25 1 230 86 87 ALA H H 7.903 0.03 1 231 86 87 ALA CA C 52.063 0.25 1 232 86 87 ALA N N 123.037 0.15 1 233 87 88 HIS H H 7.588 0.03 1 234 87 88 HIS CA C 60.860 0.25 1 235 87 88 HIS N N 117.834 0.15 1 236 88 89 PHE H H 7.675 0.03 1 237 88 89 PHE CA C 57.254 0.25 1 238 88 89 PHE N N 111.646 0.15 1 239 89 90 LEU H H 8.823 0.03 1 240 89 90 LEU CA C 53.031 0.25 1 241 89 90 LEU N N 123.881 0.15 1 242 90 91 SER H H 8.727 0.03 1 243 90 91 SER CA C 57.781 0.25 1 244 90 91 SER N N 119.381 0.15 1 245 91 92 ARG H H 9.007 0.03 1 246 91 92 ARG CA C 57.078 0.25 1 247 91 92 ARG N N 120.365 0.15 1 248 92 93 SER H H 7.430 0.03 1 249 92 93 SER CA C 56.374 0.25 1 250 92 93 SER N N 108.552 0.15 1 251 93 94 LEU H H 9.708 0.03 1 252 93 94 LEU CA C 58.221 0.25 1 253 93 94 LEU N N 125.006 0.15 1 254 94 95 ASP H H 8.709 0.03 1 255 94 95 ASP CA C 58.088 0.25 1 256 94 95 ASP N N 117.552 0.15 1 257 95 96 ASP H H 7.877 0.03 1 258 95 96 ASP CA C 57.430 0.25 1 259 95 96 ASP N N 119.381 0.15 1 260 96 97 ALA H H 8.201 0.03 1 261 96 97 ALA CA C 54.790 0.25 1 262 96 97 ALA N N 125.428 0.15 1 263 97 98 LEU H H 8.280 0.03 1 264 97 98 LEU CA C 57.254 0.25 1 265 97 98 LEU N N 114.458 0.15 1 266 98 99 LYS H H 7.964 0.03 1 267 98 99 LYS CA C 59.277 0.25 1 268 98 99 LYS N N 122.193 0.15 1 269 99 100 LEU H H 7.780 0.03 1 270 99 100 LEU CA C 58.045 0.25 1 271 99 100 LEU N N 122.193 0.15 1 272 100 101 THR H H 7.237 0.03 1 273 100 101 THR CA C 64.643 0.25 1 274 100 101 THR N N 105.177 0.15 1 275 101 102 GLU H H 7.316 0.03 1 276 101 102 GLU CA C 55.670 0.25 1 277 101 102 GLU N N 116.568 0.15 1 278 102 103 GLN H H 7.701 0.03 1 279 102 103 GLN CA C 54.346 0.25 1 280 102 103 GLN N N 121.068 0.15 1 281 103 104 PRO CA C 66.314 0.25 1 282 104 105 GLU H H 9.261 0.03 1 283 104 105 GLU CA C 59.893 0.25 1 284 104 105 GLU N N 115.865 0.15 1 285 105 106 LEU H H 7.517 0.03 1 286 105 106 LEU CA C 55.054 0.25 1 287 105 106 LEU N N 116.427 0.15 1 288 106 107 ALA H H 8.464 0.03 1 289 106 107 ALA CA C 55.406 0.25 1 290 106 107 ALA N N 123.881 0.15 1 291 107 108 ASN H H 8.473 0.03 1 292 107 108 ASN CA C 54.087 0.25 1 293 107 108 ASN N N 112.771 0.15 1 294 108 109 LYS H H 7.956 0.03 1 295 108 109 LYS CA C 56.902 0.25 1 296 108 109 LYS N N 117.552 0.15 1 297 109 110 VAL H H 7.579 0.03 1 298 109 110 VAL CA C 61.388 0.25 1 299 109 110 VAL N N 118.115 0.15 1 300 110 111 ASP H H 8.595 0.03 1 301 110 111 ASP CA C 54.175 0.25 1 302 110 111 ASP N N 125.850 0.15 1 303 111 112 MET H H 7.982 0.03 1 304 111 112 MET CA C 55.406 0.25 1 305 111 112 MET N N 115.724 0.15 1 306 112 113 VAL H H 8.385 0.03 1 307 112 113 VAL CA C 61.476 0.25 1 308 112 113 VAL N N 120.225 0.15 1 309 113 114 TRP H H 9.656 0.03 1 310 113 114 TRP CA C 55.406 0.25 1 311 113 114 TRP N N 128.100 0.15 1 312 114 115 ILE H H 9.761 0.03 1 313 114 115 ILE CA C 60.680 0.25 1 314 114 115 ILE N N 125.428 0.15 1 315 115 116 VAL H H 8.771 0.03 1 316 115 116 VAL CA C 60.157 0.25 1 317 115 116 VAL N N 117.552 0.15 1 318 116 117 GLY H H 6.133 0.03 1 319 116 117 GLY CA C 42.123 0.25 1 320 116 117 GLY N N 103.489 0.15 1 321 117 118 GLY H H 7.526 0.03 1 322 117 118 GLY CA C 46.081 0.25 1 323 117 118 GLY N N 108.833 0.15 1 324 120 121 VAL H H 7.377 0.03 1 325 120 121 VAL CA C 65.875 0.25 1 326 120 121 VAL N N 125.569 0.15 1 327 121 122 TYR H H 8.762 0.03 1 328 121 122 TYR CA C 60.508 0.25 1 329 121 122 TYR N N 118.818 0.15 1 330 122 123 LYS H H 8.192 0.03 1 331 122 123 LYS CA C 60.307 0.25 1 332 122 123 LYS N N 117.693 0.15 1 333 123 124 GLU H H 7.640 0.03 1 334 123 124 GLU CA C 59.453 0.25 1 335 123 124 GLU N N 118.537 0.15 1 336 124 125 ALA H H 8.508 0.03 1 337 124 125 ALA CA C 55.406 0.25 1 338 124 125 ALA N N 121.068 0.15 1 339 125 126 MET H H 8.481 0.03 1 340 125 126 MET CA C 58.397 0.25 1 341 125 126 MET N N 113.474 0.15 1 342 126 127 ASN H H 7.465 0.03 1 343 126 127 ASN CA C 52.767 0.25 1 344 126 127 ASN N N 115.584 0.15 1 345 127 128 HIS H H 7.798 0.03 1 346 127 128 HIS CA C 54.966 0.25 1 347 127 128 HIS N N 124.725 0.15 1 348 128 129 PRO CA C 63.411 0.25 1 349 129 130 GLY H H 8.525 0.03 1 350 129 130 GLY CA C 44.322 0.25 1 351 129 130 GLY N N 110.239 0.15 1 352 130 131 HIS H H 8.595 0.03 1 353 130 131 HIS CA C 55.582 0.25 1 354 130 131 HIS N N 119.803 0.15 1 355 131 132 LEU H H 8.148 0.03 1 356 131 132 LEU CA C 55.142 0.25 1 357 131 132 LEU N N 130.210 0.15 1 358 132 133 LYS H H 7.815 0.03 1 359 132 133 LYS CA C 55.318 0.25 1 360 132 133 LYS N N 121.350 0.15 1 361 133 134 LEU H H 9.261 0.03 1 362 133 134 LEU CA C 52.855 0.25 1 363 133 134 LEU N N 120.787 0.15 1 364 134 135 PHE H H 9.822 0.03 1 365 134 135 PHE CA C 57.869 0.25 1 366 134 135 PHE N N 127.538 0.15 1 367 135 136 VAL H H 8.981 0.03 1 368 135 136 VAL CA C 60.772 0.25 1 369 135 136 VAL N N 126.694 0.15 1 370 136 137 THR H H 9.235 0.03 1 371 136 137 THR CA C 61.300 0.25 1 372 136 137 THR N N 126.975 0.15 1 373 137 138 ARG H H 9.261 0.03 1 374 137 138 ARG CA C 53.295 0.25 1 375 137 138 ARG N N 128.100 0.15 1 376 138 139 ILE H H 8.981 0.03 1 377 138 139 ILE CA C 61.124 0.25 1 378 138 139 ILE N N 126.694 0.15 1 379 139 140 MET H H 8.867 0.03 1 380 139 140 MET CA C 56.726 0.25 1 381 139 140 MET N N 132.319 0.15 1 382 140 141 GLN H H 8.438 0.03 1 383 140 141 GLN CA C 55.670 0.25 1 384 140 141 GLN N N 119.521 0.15 1 385 141 142 ASP H H 8.736 0.03 1 386 141 142 ASP CA C 54.790 0.25 1 387 141 142 ASP N N 125.569 0.15 1 388 142 143 PHE H H 8.087 0.03 1 389 142 143 PHE CA C 58.218 0.25 1 390 142 143 PHE N N 117.974 0.15 1 391 143 144 GLU H H 9.218 0.03 1 392 143 144 GLU CA C 58.221 0.25 1 393 143 144 GLU N N 127.256 0.15 1 394 144 145 SER H H 8.762 0.03 1 395 144 145 SER CA C 58.749 0.25 1 396 144 145 SER N N 120.506 0.15 1 397 145 146 ASP H H 9.130 0.03 1 398 145 146 ASP CA C 53.119 0.25 1 399 145 146 ASP N N 118.256 0.15 1 400 146 147 THR H H 7.211 0.03 1 401 146 147 THR CA C 62.004 0.25 1 402 146 147 THR N N 117.131 0.15 1 403 147 148 PHE H H 9.051 0.03 1 404 147 148 PHE CA C 57.869 0.25 1 405 147 148 PHE N N 125.147 0.15 1 406 148 149 PHE H H 9.332 0.03 1 407 148 149 PHE CA C 55.846 0.25 1 408 148 149 PHE N N 126.553 0.15 1 409 149 150 PRO CA C 62.180 0.25 1 410 150 151 GLU H H 7.596 0.03 1 411 150 151 GLU CA C 57.078 0.25 1 412 150 151 GLU N N 115.865 0.15 1 413 151 152 ILE H H 8.201 0.03 1 414 151 152 ILE CA C 61.564 0.25 1 415 151 152 ILE N N 125.147 0.15 1 416 152 153 ASP H H 8.464 0.03 1 417 152 153 ASP CA C 53.735 0.25 1 418 152 153 ASP N N 127.538 0.15 1 419 153 154 LEU H H 8.797 0.03 1 420 153 154 LEU CA C 56.374 0.25 1 421 153 154 LEU N N 129.366 0.15 1 422 154 155 GLU H H 8.709 0.03 1 423 154 155 GLU CA C 58.088 0.25 1 424 154 155 GLU N N 117.552 0.15 1 425 155 156 LYS H H 7.561 0.03 1 426 155 156 LYS CA C 56.990 0.25 1 427 155 156 LYS N N 118.115 0.15 1 428 156 157 TYR H H 8.403 0.03 1 429 156 157 TYR CA C 58.397 0.25 1 430 156 157 TYR N N 117.693 0.15 1 431 157 158 LYS H H 8.595 0.03 1 432 157 158 LYS CA C 53.999 0.25 1 433 157 158 LYS N N 119.803 0.15 1 434 158 159 LEU H H 8.639 0.03 1 435 158 159 LEU CA C 54.790 0.25 1 436 158 159 LEU N N 126.272 0.15 1 437 159 160 LEU H H 9.191 0.03 1 438 159 160 LEU CA C 52.327 0.25 1 439 159 160 LEU N N 131.194 0.15 1 440 160 161 PRO CA C 64.291 0.25 1 441 161 162 GLU H H 7.535 0.03 1 442 161 162 GLU CA C 54.790 0.25 1 443 161 162 GLU N N 112.771 0.15 1 444 162 163 TYR H H 8.850 0.03 1 445 162 163 TYR CA C 57.078 0.25 1 446 162 163 TYR N N 124.584 0.15 1 447 163 164 PRO CA C 64.027 0.25 1 448 164 165 GLY H H 8.674 0.03 1 449 164 165 GLY CA C 45.378 0.25 1 450 164 165 GLY N N 110.661 0.15 1 451 165 166 VAL H H 7.999 0.03 1 452 165 166 VAL CA C 61.706 0.25 1 453 165 166 VAL N N 122.334 0.15 1 454 166 167 LEU H H 8.902 0.03 1 455 166 167 LEU CA C 55.883 0.25 1 456 166 167 LEU N N 130.069 0.15 1 457 167 168 SER H H 8.753 0.03 1 458 167 168 SER CA C 59.365 0.25 1 459 167 168 SER N N 116.568 0.15 1 460 168 169 ASP H H 8.026 0.03 1 461 168 169 ASP CA C 53.471 0.25 1 462 168 169 ASP N N 119.943 0.15 1 463 169 170 VAL H H 8.736 0.03 1 464 169 170 VAL CA C 65.171 0.25 1 465 169 170 VAL N N 124.865 0.15 1 466 170 171 GLN H H 8.963 0.03 1 467 170 171 GLN CA C 52.415 0.25 1 468 170 171 GLN N N 127.959 0.15 1 469 171 172 GLU H H 7.956 0.03 1 470 171 172 GLU CA C 55.566 0.25 1 471 171 172 GLU N N 117.552 0.15 1 472 172 173 GLU H H 8.736 0.03 1 473 172 173 GLU CA C 56.550 0.25 1 474 172 173 GLU N N 125.569 0.15 1 475 173 174 LYS H H 9.261 0.03 1 476 173 174 LYS CA C 56.814 0.25 1 477 173 174 LYS N N 119.521 0.15 1 478 174 175 GLY H H 8.744 0.03 1 479 174 175 GLY CA C 45.466 0.25 1 480 174 175 GLY N N 103.911 0.15 1 481 175 176 ILE H H 8.376 0.03 1 482 175 176 ILE CA C 60.860 0.25 1 483 175 176 ILE N N 125.147 0.15 1 484 176 177 LYS H H 8.280 0.03 1 485 176 177 LYS CA C 54.772 0.25 1 486 176 177 LYS N N 126.131 0.15 1 487 177 178 TYR H H 8.490 0.03 1 488 177 178 TYR CA C 55.758 0.25 1 489 177 178 TYR N N 115.865 0.15 1 490 178 179 LYS H H 8.254 0.03 1 491 178 179 LYS CA C 53.999 0.25 1 492 178 179 LYS N N 116.990 0.15 1 493 179 180 PHE H H 9.218 0.03 1 494 179 180 PHE CA C 57.078 0.25 1 495 179 180 PHE N N 123.740 0.15 1 496 180 181 GLU H H 9.367 0.03 1 497 180 181 GLU CA C 54.790 0.25 1 498 180 181 GLU N N 123.178 0.15 1 499 181 182 VAL H H 8.552 0.03 1 500 181 182 VAL CA C 61.388 0.25 1 501 181 182 VAL N N 123.178 0.15 1 502 182 183 TYR H H 9.296 0.03 1 503 182 183 TYR CA C 55.494 0.25 1 504 182 183 TYR N N 123.178 0.15 1 505 183 184 GLU H H 9.332 0.03 1 506 183 184 GLU CA C 55.406 0.25 1 507 183 184 GLU N N 119.943 0.15 1 508 184 185 LYS H H 8.920 0.03 1 509 184 185 LYS CA C 55.237 0.25 1 510 184 185 LYS N N 126.272 0.15 1 511 185 186 ASN H H 8.814 0.03 1 512 185 186 ASN CA C 53.647 0.25 1 513 185 186 ASN N N 122.193 0.15 1 514 186 187 ASP H H 7.745 0.03 1 515 186 187 ASP CA C 55.494 0.25 1 516 186 187 ASP N N 126.272 0.15 1 stop_ save_