data_16781 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for the microtubule binding domain of the Dictyostelium discoideum dynein heavy chain ; _BMRB_accession_number 16781 _BMRB_flat_file_name bmr16781.str _Entry_type original _Submission_date 2010-03-21 _Accession_date 2010-03-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'microtubule binding domain of the dynein heavy chain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McNaughton Lynn . . 2 Tikhonenko Irina . . 3 Banavali Nilesh K. . 4 LeMaster David M. . 5 Koonce Michael P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 116 "13C chemical shifts" 364 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-18 update BMRB 'complete entry citation' 2010-05-03 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'A low affinity ground state conformation for the Dynein microtubule binding domain.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20351100 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McNaughton Lynn . . 2 Tikhonenko Irina . . 3 Banavali Nilesh K. . 4 LeMaster David M. . 5 Koonce Michael P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 285 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 15994 _Page_last 16002 _Year 2010 _Details . loop_ _Keyword 'binding affinity' 'helical registry' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'dynein microtubule binding domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dynein headpiece' $dynein_microtubule_binding_domain stop_ _System_molecular_weight 15120 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'dynein headpiece' stop_ loop_ _Biological_function 'microtubule transport' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_dynein_microtubule_binding_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common dynein_microtubule_binding_domain _Molecular_mass 15120 _Mol_thiol_state 'all free' loop_ _Biological_function 'microtubule transport' 'molecular motor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; GSHMLEDPPAIIEAQEAVST IKKKHLDEIKSLPKPPTPVK LAMEAVCLMLGGKKLEWADI RKKIMEPNFITSIINYDTKK MMTPKIREAITKGYLEDPGF DYETVNRASKACGPLVKWAT AQTYYSEILDRIKP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -7 GLY 2 -6 SER 3 -5 HIS 4 -4 MET 5 -3 LEU 6 -2 GLU 7 -1 ASP 8 0 PRO 9 1 PRO 10 2 ALA 11 3 ILE 12 4 ILE 13 5 GLU 14 6 ALA 15 7 GLN 16 8 GLU 17 9 ALA 18 10 VAL 19 11 SER 20 12 THR 21 13 ILE 22 14 LYS 23 15 LYS 24 16 LYS 25 17 HIS 26 18 LEU 27 19 ASP 28 20 GLU 29 21 ILE 30 22 LYS 31 23 SER 32 24 LEU 33 25 PRO 34 26 LYS 35 27 PRO 36 28 PRO 37 29 THR 38 30 PRO 39 31 VAL 40 32 LYS 41 33 LEU 42 34 ALA 43 35 MET 44 36 GLU 45 37 ALA 46 38 VAL 47 39 CYS 48 40 LEU 49 41 MET 50 42 LEU 51 43 GLY 52 44 GLY 53 45 LYS 54 46 LYS 55 47 LEU 56 48 GLU 57 49 TRP 58 50 ALA 59 51 ASP 60 52 ILE 61 53 ARG 62 54 LYS 63 55 LYS 64 56 ILE 65 57 MET 66 58 GLU 67 59 PRO 68 60 ASN 69 61 PHE 70 62 ILE 71 63 THR 72 64 SER 73 65 ILE 74 66 ILE 75 67 ASN 76 68 TYR 77 69 ASP 78 70 THR 79 71 LYS 80 72 LYS 81 73 MET 82 74 MET 83 75 THR 84 76 PRO 85 77 LYS 86 78 ILE 87 79 ARG 88 80 GLU 89 81 ALA 90 82 ILE 91 83 THR 92 84 LYS 93 85 GLY 94 86 TYR 95 87 LEU 96 88 GLU 97 89 ASP 98 90 PRO 99 91 GLY 100 92 PHE 101 93 ASP 102 94 TYR 103 95 GLU 104 96 THR 105 97 VAL 106 98 ASN 107 99 ARG 108 100 ALA 109 101 SER 110 102 LYS 111 103 ALA 112 104 CYS 113 105 GLY 114 106 PRO 115 107 LEU 116 108 VAL 117 109 LYS 118 110 TRP 119 111 ALA 120 112 THR 121 113 ALA 122 114 GLN 123 115 THR 124 116 TYR 125 117 TYR 126 118 SER 127 119 GLU 128 120 ILE 129 121 LEU 130 122 ASP 131 123 ARG 132 124 ILE 133 125 LYS 134 126 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 3J6P "Pseudo-atomic Model Of Dynein Microtubule Binding Domain-tubulin Complex Based On A Cryoem Map" 80.60 108 100.00 100.00 6.87e-72 PDB 3VKH "X-Ray Structure Of A Functional Full-Length Dynein Motor Domain" 94.03 3367 100.00 100.00 1.88e-77 EMBL CAA78827 "cytoplasmic dynein heavy chain [Dictyostelium discoideum]" 94.03 4725 100.00 100.00 5.51e-77 GB EAL69258 "cytoplasmic dynein heavy chain [Dictyostelium discoideum AX4]" 94.03 4730 100.00 100.00 5.90e-77 REF XP_643185 "cytoplasmic dynein heavy chain [Dictyostelium discoideum AX4]" 94.03 4730 100.00 100.00 5.90e-77 SP P34036 "RecName: Full=Dynein heavy chain, cytoplasmic; AltName: Full=Dynein heavy chain, cytosolic; Short=DYHC" 94.03 4730 100.00 100.00 5.90e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dynein_microtubule_binding_domain 'Dictyostelium discoideum' 44689 Eukaryota . Dictyostelium discoideum 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_name $dynein_microtubule_binding_domain 'recombinant technology' . Escherichia coli K12 BL21(DE3)pLysS pET14b 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 $dynein_microtubule_binding_domain 0.5 mM '[U-99% 13C; U-99% 15N]' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' NaCl 150 mM 'natural abundance' PIPES-d18 20 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 2000 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 6.50 . pH pressure 1 . atm temperature 293 . 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_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '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 'dynein headpiece' _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 9 PRO C C 175.61 0.2 1 2 1 9 PRO CA C 62.72 0.2 1 3 1 9 PRO CB C 35.60 0.2 1 4 2 10 ALA H H 8.494 0.01 1 5 2 10 ALA C C 172.45 0.2 1 6 2 10 ALA CA C 54.77 0.2 1 7 2 10 ALA CB C 18.67 0.2 1 8 2 10 ALA N N 117.96 0.2 1 9 3 11 ILE H H 7.304 0.01 1 10 3 11 ILE C C 176.31 0.2 1 11 3 11 ILE CA C 62.12 0.2 1 12 3 11 ILE CB C 35.92 0.2 1 13 3 11 ILE N N 118.23 0.2 1 14 4 12 ILE H H 7.408 0.01 1 15 4 12 ILE C C 174.65 0.2 1 16 4 12 ILE CA C 64.17 0.2 1 17 4 12 ILE CB C 37.72 0.2 1 18 4 12 ILE N N 122.12 0.2 1 19 5 13 GLU H H 8.235 0.01 1 20 5 13 GLU C C 173.84 0.2 1 21 5 13 GLU CA C 59.30 0.2 1 22 5 13 GLU CB C 29.46 0.2 1 23 5 13 GLU N N 118.75 0.2 1 24 6 14 ALA H H 7.576 0.01 1 25 6 14 ALA C C 174.19 0.2 1 26 6 14 ALA CA C 55.17 0.2 1 27 6 14 ALA CB C 18.17 0.2 1 28 6 14 ALA N N 121.67 0.2 1 29 7 15 GLN H H 8.630 0.01 1 30 7 15 GLN C C 174.71 0.2 1 31 7 15 GLN CA C 59.78 0.2 1 32 7 15 GLN CB C 28.33 0.2 1 33 7 15 GLN N N 118.67 0.2 1 34 8 16 GLU H H 8.135 0.01 1 35 8 16 GLU C C 173.94 0.2 1 36 8 16 GLU CA C 59.28 0.2 1 37 8 16 GLU CB C 28.92 0.2 1 38 8 16 GLU N N 119.85 0.2 1 39 9 17 ALA H H 7.759 0.01 1 40 9 17 ALA C C 172.61 0.2 1 41 9 17 ALA CA C 55.10 0.2 1 42 9 17 ALA CB C 17.60 0.2 1 43 9 17 ALA N N 121.99 0.2 1 44 10 18 VAL H H 8.527 0.01 1 45 10 18 VAL C C 176.31 0.2 1 46 10 18 VAL CA C 66.00 0.2 1 47 10 18 VAL CB C 31.29 0.2 1 48 10 18 VAL N N 120.42 0.2 1 49 11 19 SER H H 7.829 0.01 1 50 11 19 SER C C 178.80 0.2 1 51 11 19 SER CA C 61.25 0.2 1 52 11 19 SER CB C 63.16 0.2 1 53 11 19 SER N N 114.04 0.2 1 54 12 20 THR H H 7.305 0.01 1 55 12 20 THR C C 178.79 0.2 1 56 12 20 THR CA C 62.31 0.2 1 57 12 20 THR CB C 70.24 0.2 1 58 12 20 THR N N 110.42 0.2 1 59 13 21 ILE H H 7.507 0.01 1 60 13 21 ILE C C 177.45 0.2 1 61 13 21 ILE CA C 63.22 0.2 1 62 13 21 ILE CB C 37.92 0.2 1 63 13 21 ILE N N 124.04 0.2 1 64 14 22 LYS H H 9.801 0.01 1 65 14 22 LYS C C 175.75 0.2 1 66 14 22 LYS CA C 54.10 0.2 1 67 14 22 LYS CB C 33.71 0.2 1 68 14 22 LYS N N 129.86 0.2 1 69 15 23 LYS H H 8.670 0.01 1 70 15 23 LYS C C 175.17 0.2 1 71 15 23 LYS CA C 60.32 0.2 1 72 15 23 LYS CB C 31.74 0.2 1 73 15 23 LYS N N 124.99 0.2 1 74 16 24 LYS H H 8.346 0.01 1 75 16 24 LYS C C 175.14 0.2 1 76 16 24 LYS CA C 58.83 0.2 1 77 16 24 LYS CB C 31.72 0.2 1 78 16 24 LYS N N 115.66 0.2 1 79 17 25 HIS H H 7.082 0.01 1 80 17 25 HIS C C 174.15 0.2 1 81 17 25 HIS CA C 58.45 0.2 1 82 17 25 HIS CB C 31.79 0.2 1 83 17 25 HIS N N 118.07 0.2 1 84 18 26 LEU H H 7.424 0.01 1 85 18 26 LEU C C 175.06 0.2 1 86 18 26 LEU CA C 57.51 0.2 1 87 18 26 LEU CB C 40.68 0.2 1 88 18 26 LEU N N 120.77 0.2 1 89 19 27 ASP H H 8.659 0.01 1 90 19 27 ASP C C 174.37 0.2 1 91 19 27 ASP CA C 57.15 0.2 1 92 19 27 ASP CB C 40.55 0.2 1 93 19 27 ASP N N 120.89 0.2 1 94 20 28 GLU H H 7.511 0.01 1 95 20 28 GLU C C 174.36 0.2 1 96 20 28 GLU CA C 59.02 0.2 1 97 20 28 GLU CB C 29.50 0.2 1 98 20 28 GLU N N 118.67 0.2 1 99 21 29 ILE H H 7.199 0.01 1 100 21 29 ILE C C 175.72 0.2 1 101 21 29 ILE CA C 64.17 0.2 1 102 21 29 ILE CB C 37.72 0.2 1 103 21 29 ILE N N 118.39 0.2 1 104 22 30 LYS H H 8.255 0.01 1 105 22 30 LYS C C 176.66 0.2 1 106 22 30 LYS CA C 58.95 0.2 1 107 22 30 LYS CB C 31.35 0.2 1 108 22 30 LYS N N 119.13 0.2 1 109 23 31 SER H H 7.515 0.01 1 110 23 31 SER C C 179.49 0.2 1 111 23 31 SER CA C 59.32 0.2 1 112 23 31 SER CB C 64.14 0.2 1 113 23 31 SER N N 112.64 0.2 1 114 24 32 LEU H H 7.396 0.01 1 115 24 32 LEU C C 177.31 0.2 1 116 24 32 LEU CA C 53.23 0.2 1 117 24 32 LEU CB C 42.41 0.2 1 118 24 32 LEU N N 123.76 0.2 1 119 25 33 PRO C C 176.31 0.2 1 120 25 33 PRO CA C 64.54 0.2 1 121 25 33 PRO CB C 31.96 0.2 1 122 26 34 LYS H H 7.154 0.01 1 123 26 34 LYS C C 180.80 0.2 1 124 26 34 LYS CA C 52.91 0.2 1 125 26 34 LYS CB C 33.72 0.2 1 126 26 34 LYS N N 115.21 0.2 1 127 28 36 PRO C C 176.24 0.2 1 128 28 36 PRO CA C 62.05 0.2 1 129 28 36 PRO CB C 32.72 0.2 1 130 29 37 THR H H 9.047 0.01 1 131 29 37 THR CA C 68.90 0.2 1 132 29 37 THR CB C 67.06 0.2 1 133 29 37 THR N N 121.47 0.2 1 134 30 38 PRO C C 175.47 0.2 1 135 30 38 PRO CA C 66.52 0.2 1 136 30 38 PRO CB C 32.60 0.2 1 137 31 39 VAL H H 6.313 0.01 1 138 31 39 VAL C C 176.81 0.2 1 139 31 39 VAL CA C 64.94 0.2 1 140 31 39 VAL CB C 32.22 0.2 1 141 31 39 VAL N N 113.27 0.2 1 142 32 40 LYS H H 7.572 0.01 1 143 32 40 LYS C C 175.26 0.2 1 144 32 40 LYS CA C 60.23 0.2 1 145 32 40 LYS CB C 32.59 0.2 1 146 32 40 LYS N N 119.71 0.2 1 147 33 41 LEU H H 8.516 0.01 1 148 33 41 LEU C C 174.79 0.2 1 149 33 41 LEU CA C 58.37 0.2 1 150 33 41 LEU CB C 43.41 0.2 1 151 33 41 LEU N N 115.53 0.2 1 152 34 42 ALA H H 7.722 0.01 1 153 34 42 ALA C C 174.26 0.2 1 154 34 42 ALA CA C 56.01 0.2 1 155 34 42 ALA CB C 18.62 0.2 1 156 34 42 ALA N N 118.54 0.2 1 157 35 43 MET H H 8.106 0.01 1 158 35 43 MET C C 174.21 0.2 1 159 35 43 MET CA C 56.69 0.2 1 160 35 43 MET CB C 32.29 0.2 1 161 35 43 MET N N 111.74 0.2 1 162 36 44 GLU H H 9.189 0.01 1 163 36 44 GLU C C 173.45 0.2 1 164 36 44 GLU CA C 59.91 0.2 1 165 36 44 GLU CB C 31.16 0.2 1 166 36 44 GLU N N 121.87 0.2 1 167 37 45 ALA H H 8.052 0.01 1 168 37 45 ALA C C 174.29 0.2 1 169 37 45 ALA CA C 55.51 0.2 1 170 37 45 ALA CB C 17.55 0.2 1 171 37 45 ALA N N 121.11 0.2 1 172 38 46 VAL H H 7.664 0.01 1 173 38 46 VAL C C 175.17 0.2 1 174 38 46 VAL CA C 66.85 0.2 1 175 38 46 VAL CB C 31.74 0.2 1 176 38 46 VAL N N 115.04 0.2 1 177 39 47 CYS H H 8.360 0.01 1 178 39 47 CYS C C 175.32 0.2 1 179 39 47 CYS CA C 65.55 0.2 1 180 39 47 CYS CB C 26.56 0.2 1 181 39 47 CYS N N 115.87 0.2 1 182 40 48 LEU H H 8.110 0.01 1 183 40 48 LEU C C 174.88 0.2 1 184 40 48 LEU CA C 58.57 0.2 1 185 40 48 LEU CB C 42.08 0.2 1 186 40 48 LEU N N 126.09 0.2 1 187 41 49 MET H H 7.878 0.01 1 188 41 49 MET C C 174.16 0.2 1 189 41 49 MET CA C 59.89 0.2 1 190 41 49 MET CB C 32.99 0.2 1 191 41 49 MET N N 118.73 0.2 1 192 42 50 LEU H H 8.102 0.01 1 193 42 50 LEU C C 175.17 0.2 1 194 42 50 LEU CA C 57.09 0.2 1 195 42 50 LEU CB C 43.41 0.2 1 196 42 50 LEU N N 117.54 0.2 1 197 43 51 GLY H H 7.802 0.01 1 198 43 51 GLY C C 178.02 0.2 1 199 43 51 GLY CA C 45.42 0.2 1 200 43 51 GLY N N 102.94 0.2 1 201 44 52 GLY H H 8.558 0.01 1 202 44 52 GLY C C 180.22 0.2 1 203 44 52 GLY CA C 46.16 0.2 1 204 44 52 GLY N N 109.64 0.2 1 205 45 53 LYS H H 7.674 0.01 1 206 45 53 LYS C C 177.80 0.2 1 207 45 53 LYS CA C 54.62 0.2 1 208 45 53 LYS CB C 35.94 0.2 1 209 45 53 LYS N N 117.44 0.2 1 210 46 54 LYS H H 8.834 0.01 1 211 46 54 LYS C C 178.41 0.2 1 212 46 54 LYS CA C 56.93 0.2 1 213 46 54 LYS CB C 31.85 0.2 1 214 46 54 LYS N N 126.38 0.2 1 215 47 55 LEU H H 8.213 0.01 1 216 47 55 LEU C C 176.42 0.2 1 217 47 55 LEU CA C 53.32 0.2 1 218 47 55 LEU CB C 44.41 0.2 1 219 47 55 LEU N N 128.75 0.2 1 220 48 56 GLU H H 8.864 0.01 1 221 48 56 GLU C C 175.01 0.2 1 222 48 56 GLU CA C 55.29 0.2 1 223 48 56 GLU CB C 30.24 0.2 1 224 48 56 GLU N N 119.22 0.2 1 225 49 57 TRP H H 9.071 0.01 1 226 49 57 TRP C C 176.83 0.2 1 227 49 57 TRP CA C 60.45 0.2 1 228 49 57 TRP CB C 29.39 0.2 1 229 49 57 TRP N N 124.34 0.2 1 230 50 58 ALA H H 8.878 0.01 1 231 50 58 ALA C C 173.35 0.2 1 232 50 58 ALA CA C 55.50 0.2 1 233 50 58 ALA CB C 18.46 0.2 1 234 50 58 ALA N N 117.68 0.2 1 235 51 59 ASP H H 6.962 0.01 1 236 51 59 ASP C C 174.51 0.2 1 237 51 59 ASP CA C 56.52 0.2 1 238 51 59 ASP CB C 41.91 0.2 1 239 51 59 ASP N N 114.49 0.2 1 240 52 60 ILE H H 7.803 0.01 1 241 52 60 ILE C C 176.55 0.2 1 242 52 60 ILE CA C 66.05 0.2 1 243 52 60 ILE CB C 36.80 0.2 1 244 52 60 ILE N N 126.38 0.2 1 245 53 61 ARG H H 7.724 0.01 1 246 53 61 ARG C C 176.54 0.2 1 247 53 61 ARG CA C 59.98 0.2 1 248 53 61 ARG CB C 30.79 0.2 1 249 53 61 ARG N N 115.72 0.2 1 250 54 62 LYS H H 6.247 0.01 1 251 54 62 LYS C C 174.70 0.2 1 252 54 62 LYS CA C 58.53 0.2 1 253 54 62 LYS CB C 32.75 0.2 1 254 54 62 LYS N N 113.31 0.2 1 255 55 63 LYS H H 7.516 0.01 1 256 55 63 LYS C C 174.68 0.2 1 257 55 63 LYS CA C 58.36 0.2 1 258 55 63 LYS CB C 31.17 0.2 1 259 55 63 LYS N N 121.64 0.2 1 260 56 64 ILE H H 7.521 0.01 1 261 56 64 ILE C C 178.55 0.2 1 262 56 64 ILE CA C 62.75 0.2 1 263 56 64 ILE CB C 36.90 0.2 1 264 56 64 ILE N N 109.59 0.2 1 265 57 65 MET H H 6.468 0.01 1 266 57 65 MET C C 176.06 0.2 1 267 57 65 MET CA C 53.40 0.2 1 268 57 65 MET CB C 32.79 0.2 1 269 57 65 MET N N 113.73 0.2 1 270 58 66 GLU H H 7.469 0.01 1 271 58 66 GLU CA C 55.65 0.2 1 272 58 66 GLU CB C 28.36 0.2 1 273 58 66 GLU N N 123.92 0.2 1 274 59 67 PRO C C 176.24 0.2 1 275 59 67 PRO CA C 65.07 0.2 1 276 59 67 PRO CB C 31.74 0.2 1 277 60 68 ASN H H 8.065 0.01 1 278 60 68 ASN C C 177.93 0.2 1 279 60 68 ASN CA C 52.41 0.2 1 280 60 68 ASN CB C 37.86 0.2 1 281 60 68 ASN N N 113.39 0.2 1 282 61 69 PHE H H 7.638 0.01 1 283 61 69 PHE C C 176.66 0.2 1 284 61 69 PHE CA C 62.76 0.2 1 285 61 69 PHE CB C 39.30 0.2 1 286 61 69 PHE N N 122.67 0.2 1 287 62 70 ILE H H 8.381 0.01 1 288 62 70 ILE C C 174.79 0.2 1 289 62 70 ILE CA C 62.66 0.2 1 290 62 70 ILE CB C 35.04 0.2 1 291 62 70 ILE N N 118.61 0.2 1 292 63 71 THR H H 7.861 0.01 1 293 63 71 THR C C 177.44 0.2 1 294 63 71 THR CA C 66.48 0.2 1 295 63 71 THR CB C 68.66 0.2 1 296 63 71 THR N N 115.14 0.2 1 297 64 72 SER H H 8.177 0.01 1 298 64 72 SER C C 178.79 0.2 1 299 64 72 SER CA C 61.35 0.2 1 300 64 72 SER CB C 62.65 0.2 1 301 64 72 SER N N 117.90 0.2 1 302 65 73 ILE H H 6.741 0.01 1 303 65 73 ILE C C 175.76 0.2 1 304 65 73 ILE CA C 63.97 0.2 1 305 65 73 ILE CB C 37.40 0.2 1 306 65 73 ILE N N 123.22 0.2 1 307 66 74 ILE H H 7.749 0.01 1 308 66 74 ILE C C 176.26 0.2 1 309 66 74 ILE CA C 65.00 0.2 1 310 66 74 ILE CB C 37.31 0.2 1 311 66 74 ILE N N 119.33 0.2 1 312 67 75 ASN H H 7.982 0.01 1 313 67 75 ASN C C 179.58 0.2 1 314 67 75 ASN CA C 52.83 0.2 1 315 67 75 ASN CB C 38.17 0.2 1 316 67 75 ASN N N 114.82 0.2 1 317 68 76 TYR H H 6.887 0.01 1 318 68 76 TYR C C 179.00 0.2 1 319 68 76 TYR CA C 59.76 0.2 1 320 68 76 TYR CB C 41.54 0.2 1 321 68 76 TYR N N 122.67 0.2 1 322 69 77 ASP H H 8.048 0.01 1 323 69 77 ASP C C 179.06 0.2 1 324 69 77 ASP CA C 51.93 0.2 1 325 69 77 ASP CB C 40.23 0.2 1 326 69 77 ASP N N 129.80 0.2 1 327 70 78 THR H H 7.776 0.01 1 328 70 78 THR C C 177.92 0.2 1 329 70 78 THR CA C 67.88 0.2 1 330 70 78 THR CB C 70.05 0.2 1 331 70 78 THR N N 121.84 0.2 1 332 71 79 LYS H H 8.291 0.01 1 333 71 79 LYS C C 175.90 0.2 1 334 71 79 LYS CA C 58.54 0.2 1 335 71 79 LYS CB C 32.18 0.2 1 336 71 79 LYS N N 118.02 0.2 1 337 72 80 LYS H H 7.044 0.01 1 338 72 80 LYS C C 175.78 0.2 1 339 72 80 LYS CA C 57.47 0.2 1 340 72 80 LYS CB C 34.14 0.2 1 341 72 80 LYS N N 115.64 0.2 1 342 73 81 MET H H 7.909 0.01 1 343 73 81 MET C C 175.77 0.2 1 344 73 81 MET CA C 55.70 0.2 1 345 73 81 MET CB C 33.20 0.2 1 346 73 81 MET N N 113.68 0.2 1 347 74 82 MET H H 8.006 0.01 1 348 74 82 MET C C 178.22 0.2 1 349 74 82 MET CA C 54.79 0.2 1 350 74 82 MET CB C 30.43 0.2 1 351 74 82 MET N N 120.77 0.2 1 352 75 83 THR H H 6.781 0.01 1 353 75 83 THR C C 180.33 0.2 1 354 75 83 THR CA C 59.34 0.2 1 355 75 83 THR CB C 68.78 0.2 1 356 75 83 THR N N 114.56 0.2 1 357 76 84 PRO C C 174.53 0.2 1 358 76 84 PRO CA C 66.37 0.2 1 359 76 84 PRO CB C 31.74 0.2 1 360 77 85 LYS H H 7.828 0.01 1 361 77 85 LYS C C 173.64 0.2 1 362 77 85 LYS CA C 59.04 0.2 1 363 77 85 LYS CB C 32.52 0.2 1 364 77 85 LYS N N 115.89 0.2 1 365 78 86 ILE H H 7.530 0.01 1 366 78 86 ILE C C 176.26 0.2 1 367 78 86 ILE CA C 64.54 0.2 1 368 78 86 ILE CB C 37.72 0.2 1 369 78 86 ILE N N 122.46 0.2 1 370 79 87 ARG H H 8.622 0.01 1 371 79 87 ARG C C 174.15 0.2 1 372 79 87 ARG CA C 60.74 0.2 1 373 79 87 ARG CB C 30.38 0.2 1 374 79 87 ARG N N 120.60 0.2 1 375 80 88 GLU H H 8.243 0.01 1 376 80 88 GLU C C 176.07 0.2 1 377 80 88 GLU CA C 59.30 0.2 1 378 80 88 GLU CB C 29.46 0.2 1 379 80 88 GLU N N 120.91 0.2 1 380 81 89 ALA H H 7.575 0.01 1 381 81 89 ALA C C 171.30 0.2 1 382 81 89 ALA CA C 55.17 0.2 1 383 81 89 ALA CB C 18.17 0.2 1 384 81 89 ALA N N 121.60 0.2 1 385 82 90 ILE H H 8.640 0.01 1 386 82 90 ILE C C 174.70 0.2 1 387 82 90 ILE CA C 61.66 0.2 1 388 82 90 ILE CB C 35.60 0.2 1 389 82 90 ILE N N 118.87 0.2 1 390 83 91 THR H H 8.496 0.01 1 391 83 91 THR C C 178.64 0.2 1 392 83 91 THR CA C 67.60 0.2 1 393 83 91 THR CB C 68.94 0.2 1 394 83 91 THR N N 118.18 0.2 1 395 84 92 LYS H H 8.242 0.01 1 396 84 92 LYS C C 174.82 0.2 1 397 84 92 LYS CA C 57.52 0.2 1 398 84 92 LYS CB C 32.14 0.2 1 399 84 92 LYS N N 116.32 0.2 1 400 85 93 GLY H H 7.536 0.01 1 401 85 93 GLY C C 180.18 0.2 1 402 85 93 GLY CA C 45.71 0.2 1 403 85 93 GLY N N 103.15 0.2 1 404 86 94 TYR H H 7.027 0.01 1 405 86 94 TYR C C 177.85 0.2 1 406 86 94 TYR CA C 60.47 0.2 1 407 86 94 TYR CB C 37.83 0.2 1 408 86 94 TYR N N 115.27 0.2 1 409 87 95 LEU H H 8.078 0.01 1 410 87 95 LEU C C 173.97 0.2 1 411 87 95 LEU CA C 58.55 0.2 1 412 87 95 LEU CB C 40.27 0.2 1 413 87 95 LEU N N 114.99 0.2 1 414 88 96 GLU H H 7.453 0.01 1 415 88 96 GLU C C 177.38 0.2 1 416 88 96 GLU CA C 56.13 0.2 1 417 88 96 GLU CB C 29.47 0.2 1 418 88 96 GLU N N 113.46 0.2 1 419 89 97 ASP H H 7.591 0.01 1 420 89 97 ASP C C 175.00 0.2 1 421 89 97 ASP CA C 51.86 0.2 1 422 89 97 ASP CB C 43.02 0.2 1 423 89 97 ASP N N 124.47 0.2 1 424 90 98 PRO C C 175.24 0.2 1 425 90 98 PRO CA C 64.67 0.2 1 426 90 98 PRO CB C 31.83 0.2 1 427 91 99 GLY H H 9.437 0.01 1 428 91 99 GLY C C 181.52 0.2 1 429 91 99 GLY CA C 45.77 0.2 1 430 91 99 GLY N N 107.74 0.2 1 431 92 100 PHE H H 7.905 0.01 1 432 92 100 PHE C C 179.39 0.2 1 433 92 100 PHE CA C 56.63 0.2 1 434 92 100 PHE CB C 41.93 0.2 1 435 92 100 PHE N N 121.20 0.2 1 436 93 101 ASP H H 6.860 0.01 1 437 93 101 ASP C C 178.10 0.2 1 438 93 101 ASP CA C 53.74 0.2 1 439 93 101 ASP CB C 43.84 0.2 1 440 93 101 ASP N N 119.24 0.2 1 441 94 102 TYR H H 8.833 0.01 1 442 94 102 TYR C C 177.80 0.2 1 443 94 102 TYR CA C 62.79 0.2 1 444 94 102 TYR CB C 38.28 0.2 1 445 94 102 TYR N N 126.07 0.2 1 446 95 103 GLU H H 8.504 0.01 1 447 95 103 GLU C C 174.25 0.2 1 448 95 103 GLU CA C 59.50 0.2 1 449 95 103 GLU CB C 28.81 0.2 1 450 95 103 GLU N N 117.64 0.2 1 451 96 104 THR H H 7.677 0.01 1 452 96 104 THR C C 176.63 0.2 1 453 96 104 THR CA C 66.84 0.2 1 454 96 104 THR CB C 68.78 0.2 1 455 96 104 THR N N 116.60 0.2 1 456 97 105 VAL H H 8.277 0.01 1 457 97 105 VAL C C 176.61 0.2 1 458 97 105 VAL CA C 66.51 0.2 1 459 97 105 VAL CB C 31.69 0.2 1 460 97 105 VAL N N 122.35 0.2 1 461 98 106 ASN H H 8.629 0.01 1 462 98 106 ASN C C 176.61 0.2 1 463 98 106 ASN CA C 55.26 0.2 1 464 98 106 ASN CB C 38.79 0.2 1 465 98 106 ASN N N 117.50 0.2 1 466 99 107 ARG H H 7.221 0.01 1 467 99 107 ARG C C 175.90 0.2 1 468 99 107 ARG CA C 58.50 0.2 1 469 99 107 ARG CB C 30.23 0.2 1 470 99 107 ARG N N 114.75 0.2 1 471 100 108 ALA H H 7.015 0.01 1 472 100 108 ALA C C 174.76 0.2 1 473 100 108 ALA CA C 53.74 0.2 1 474 100 108 ALA CB C 18.94 0.2 1 475 100 108 ALA N N 121.01 0.2 1 476 101 109 SER H H 8.239 0.01 1 477 101 109 SER C C 179.07 0.2 1 478 101 109 SER CA C 57.38 0.2 1 479 101 109 SER CB C 64.47 0.2 1 480 101 109 SER N N 111.92 0.2 1 481 102 110 LYS H H 8.819 0.01 1 482 102 110 LYS C C 175.20 0.2 1 483 102 110 LYS CA C 57.52 0.2 1 484 102 110 LYS CB C 31.35 0.2 1 485 102 110 LYS N N 130.21 0.2 1 486 103 111 ALA H H 7.704 0.01 1 487 103 111 ALA C C 176.56 0.2 1 488 103 111 ALA CA C 53.37 0.2 1 489 103 111 ALA CB C 19.15 0.2 1 490 103 111 ALA N N 118.22 0.2 1 491 104 112 CYS H H 7.141 0.01 1 492 104 112 CYS C C 176.57 0.2 1 493 104 112 CYS CA C 61.78 0.2 1 494 104 112 CYS CB C 28.81 0.2 1 495 104 112 CYS N N 109.29 0.2 1 496 105 113 GLY H H 7.647 0.01 1 497 105 113 GLY C C 179.53 0.2 1 498 105 113 GLY CA C 49.07 0.2 1 499 105 113 GLY N N 108.10 0.2 1 500 106 114 PRO C C 175.89 0.2 1 501 106 114 PRO CA C 65.47 0.2 1 502 106 114 PRO CB C 33.14 0.2 1 503 107 115 LEU H H 6.631 0.01 1 504 107 115 LEU C C 174.64 0.2 1 505 107 115 LEU CA C 57.43 0.2 1 506 107 115 LEU CB C 39.79 0.2 1 507 107 115 LEU N N 112.64 0.2 1 508 108 116 VAL H H 7.749 0.01 1 509 108 116 VAL C C 173.87 0.2 1 510 108 116 VAL CA C 66.45 0.2 1 511 108 116 VAL CB C 31.65 0.2 1 512 108 116 VAL N N 119.69 0.2 1 513 109 117 LYS H H 7.681 0.01 1 514 109 117 LYS C C 174.62 0.2 1 515 109 117 LYS CA C 59.91 0.2 1 516 109 117 LYS CB C 32.17 0.2 1 517 109 117 LYS N N 122.31 0.2 1 518 110 118 TRP H H 8.474 0.01 1 519 110 118 TRP C C 177.35 0.2 1 520 110 118 TRP CA C 63.02 0.2 1 521 110 118 TRP CB C 28.50 0.2 1 522 110 118 TRP N N 120.22 0.2 1 523 111 119 ALA H H 8.825 0.01 1 524 111 119 ALA C C 173.15 0.2 1 525 111 119 ALA CA C 55.50 0.2 1 526 111 119 ALA CB C 17.80 0.2 1 527 111 119 ALA N N 121.48 0.2 1 528 112 120 THR H H 8.057 0.01 1 529 112 120 THR C C 178.29 0.2 1 530 112 120 THR CA C 66.94 0.2 1 531 112 120 THR CB C 69.16 0.2 1 532 112 120 THR N N 113.58 0.2 1 533 113 121 ALA H H 7.907 0.01 1 534 113 121 ALA C C 172.80 0.2 1 535 113 121 ALA CA C 55.19 0.2 1 536 113 121 ALA CB C 18.14 0.2 1 537 113 121 ALA N N 123.41 0.2 1 538 114 122 GLN H H 8.164 0.01 1 539 114 122 GLN C C 175.41 0.2 1 540 114 122 GLN CA C 58.49 0.2 1 541 114 122 GLN CB C 28.00 0.2 1 542 114 122 GLN N N 115.92 0.2 1 543 115 123 THR H H 7.353 0.01 1 544 115 123 THR C C 176.71 0.2 1 545 115 123 THR CA C 67.98 0.2 1 546 115 123 THR N N 115.36 0.2 1 547 116 124 TYR H H 7.594 0.01 1 548 116 124 TYR C C 175.49 0.2 1 549 116 124 TYR CA C 60.27 0.2 1 550 116 124 TYR CB C 37.37 0.2 1 551 116 124 TYR N N 121.16 0.2 1 552 117 125 TYR H H 8.274 0.01 1 553 117 125 TYR C C 176.55 0.2 1 554 117 125 TYR CA C 58.33 0.2 1 555 117 125 TYR CB C 38.41 0.2 1 556 117 125 TYR N N 120.07 0.2 1 557 118 126 SER H H 8.259 0.01 1 558 118 126 SER C C 177.62 0.2 1 559 118 126 SER CA C 60.81 0.2 1 560 118 126 SER CB C 63.53 0.2 1 561 118 126 SER N N 112.90 0.2 1 562 119 127 GLU H H 7.281 0.01 1 563 119 127 GLU C C 174.88 0.2 1 564 119 127 GLU CA C 59.49 0.2 1 565 119 127 GLU CB C 29.45 0.2 1 566 119 127 GLU N N 119.18 0.2 1 567 120 128 ILE H H 7.281 0.01 1 568 120 128 ILE C C 174.41 0.2 1 569 120 128 ILE CA C 64.16 0.2 1 570 120 128 ILE CB C 37.68 0.2 1 571 120 128 ILE N N 119.18 0.2 1 572 121 129 LEU H H 8.087 0.01 1 573 121 129 LEU C C 174.40 0.2 1 574 121 129 LEU CA C 57.03 0.2 1 575 121 129 LEU CB C 41.71 0.2 1 576 121 129 LEU N N 120.93 0.2 1 577 122 130 ASP H H 7.556 0.01 1 578 122 130 ASP C C 176.79 0.2 1 579 122 130 ASP CA C 55.29 0.2 1 580 122 130 ASP CB C 41.08 0.2 1 581 122 130 ASP N N 118.09 0.2 1 582 123 131 ARG H H 7.427 0.01 1 583 123 131 ARG C C 176.78 0.2 1 584 123 131 ARG CA C 56.98 0.2 1 585 123 131 ARG CB C 30.68 0.2 1 586 123 131 ARG N N 118.20 0.2 1 587 124 132 ILE H H 7.655 0.01 1 588 124 132 ILE C C 177.69 0.2 1 589 124 132 ILE CA C 61.67 0.2 1 590 124 132 ILE CB C 38.25 0.2 1 591 124 132 ILE N N 120.02 0.2 1 592 125 133 LYS H H 8.059 0.01 1 593 125 133 LYS C C 180.13 0.2 1 594 125 133 LYS CA C 53.87 0.2 1 595 125 133 LYS CB C 32.42 0.2 1 596 125 133 LYS N N 127.04 0.2 1 stop_ save_