data_15875 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignments and Relaxation Data for S. pombe Aps1d2-19 ; _BMRB_accession_number 15875 _BMRB_flat_file_name bmr15875.str _Entry_type original _Submission_date 2008-07-14 _Accession_date 2008-07-14 _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 Garza John A. . 2 Ilangovan Udayar . . 3 Hinck Andrew P. . 4 Barnes Larry D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 159 "13C chemical shifts" 503 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-07-01 update BMRB 'complete entry citation' 2009-05-29 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Kinetic, Dynamic, Ligand Binding Properties, and Structural Models of a Dual-Substrate Specific Nudix Hydrolase from Schizosaccharomyces pombe' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19462967 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Garza John A. . 2 Ilangovan Udayar . . 3 Hinck Andrew P. . 4 Barnes Larry D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 48 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6224 _Page_last 6239 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Nudix hydrolase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Nudix hydrolase' $Nudix_hydrolase stop_ _System_molecular_weight 24444 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Nudix_hydrolase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Nudix_hydrolase _Molecular_mass 24444 _Mol_thiol_state 'all free' loop_ _Biological_function 'diadenosine 5',5'''-P1,Pn-oligophosphate hydrolase' 'diphosphoinositol polyphosphate hydrolase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 216 _Mol_residue_sequence ; MGSSHHHHHHHHHHSSGLVP RGSHMVNRSMTSREGRTKNR FNPITGARLAAGVVALSADK RKVLLVSSAKKHPSWVVPKG GWEADESVQQAALREGWEEG GLVGHITRSLGSFKDKRPTD TIDRRKKYLKQLMSKSSGND VSTNTELGAEAEKLLLPPRA ECEFFEVIVERLEDNYPEMR KRRRKWMSYQEAKEALTSRK DILAALEKSSIIKEEN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -23 MET 2 -22 GLY 3 -21 SER 4 -20 SER 5 -19 HIS 6 -18 HIS 7 -17 HIS 8 -16 HIS 9 -15 HIS 10 -14 HIS 11 -13 HIS 12 -12 HIS 13 -11 HIS 14 -10 HIS 15 -9 SER 16 -8 SER 17 -7 GLY 18 -6 LEU 19 -5 VAL 20 -4 PRO 21 -3 ARG 22 -2 GLY 23 -1 SER 24 0 HIS 25 1 MET 26 20 VAL 27 21 ASN 28 22 ARG 29 23 SER 30 24 MET 31 25 THR 32 26 SER 33 27 ARG 34 28 GLU 35 29 GLY 36 30 ARG 37 31 THR 38 32 LYS 39 33 ASN 40 34 ARG 41 35 PHE 42 36 ASN 43 37 PRO 44 38 ILE 45 39 THR 46 40 GLY 47 41 ALA 48 42 ARG 49 43 LEU 50 44 ALA 51 45 ALA 52 46 GLY 53 47 VAL 54 48 VAL 55 49 ALA 56 50 LEU 57 51 SER 58 52 ALA 59 53 ASP 60 54 LYS 61 55 ARG 62 56 LYS 63 57 VAL 64 58 LEU 65 59 LEU 66 60 VAL 67 61 SER 68 62 SER 69 63 ALA 70 64 LYS 71 65 LYS 72 66 HIS 73 67 PRO 74 68 SER 75 69 TRP 76 70 VAL 77 71 VAL 78 72 PRO 79 73 LYS 80 74 GLY 81 75 GLY 82 76 TRP 83 77 GLU 84 78 ALA 85 79 ASP 86 80 GLU 87 81 SER 88 82 VAL 89 83 GLN 90 84 GLN 91 85 ALA 92 86 ALA 93 87 LEU 94 88 ARG 95 89 GLU 96 90 GLY 97 91 TRP 98 92 GLU 99 93 GLU 100 94 GLY 101 95 GLY 102 96 LEU 103 97 VAL 104 98 GLY 105 99 HIS 106 100 ILE 107 101 THR 108 102 ARG 109 103 SER 110 104 LEU 111 105 GLY 112 106 SER 113 107 PHE 114 108 LYS 115 109 ASP 116 110 LYS 117 111 ARG 118 112 PRO 119 113 THR 120 114 ASP 121 115 THR 122 116 ILE 123 117 ASP 124 118 ARG 125 119 ARG 126 120 LYS 127 121 LYS 128 122 TYR 129 123 LEU 130 124 LYS 131 125 GLN 132 126 LEU 133 127 MET 134 128 SER 135 129 LYS 136 130 SER 137 131 SER 138 132 GLY 139 133 ASN 140 134 ASP 141 135 VAL 142 136 SER 143 137 THR 144 138 ASN 145 139 THR 146 140 GLU 147 141 LEU 148 142 GLY 149 143 ALA 150 144 GLU 151 145 ALA 152 146 GLU 153 147 LYS 154 148 LEU 155 149 LEU 156 150 LEU 157 151 PRO 158 152 PRO 159 153 ARG 160 154 ALA 161 155 GLU 162 156 CYS 163 157 GLU 164 158 PHE 165 159 PHE 166 160 GLU 167 161 VAL 168 162 ILE 169 163 VAL 170 164 GLU 171 165 ARG 172 166 LEU 173 167 GLU 174 168 ASP 175 169 ASN 176 170 TYR 177 171 PRO 178 172 GLU 179 173 MET 180 174 ARG 181 175 LYS 182 176 ARG 183 177 ARG 184 178 ARG 185 179 LYS 186 180 TRP 187 181 MET 188 182 SER 189 183 TYR 190 184 GLN 191 185 GLU 192 186 ALA 193 187 LYS 194 188 GLU 195 189 ALA 196 190 LEU 197 191 THR 198 192 SER 199 193 ARG 200 194 LYS 201 195 ASP 202 196 ILE 203 197 LEU 204 198 ALA 205 199 ALA 206 200 LEU 207 201 GLU 208 202 LYS 209 203 SER 210 204 SER 211 205 ILE 212 206 ILE 213 207 LYS 214 208 GLU 215 209 GLU 216 210 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 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 EMBL CAA91107 "diadenosine 5',5'''-p1,p6-hexaphosphate hydrolase Aps1 [Schizosaccharomyces pombe]" 88.43 210 100.00 100.00 2.79e-135 GB AAD20015 "diadenosine 5', 5'''-P1,P6-hexaphosphate hydrolase [Schizosaccharomyces pombe]" 88.43 210 100.00 100.00 2.79e-135 REF NP_592840 "diadenosine 5',5'''-p1,p6-hexaphosphate hydrolase Aps1 [Schizosaccharomyces pombe 972h-]" 88.43 210 100.00 100.00 2.79e-135 SP Q09790 "RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase aps1; AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydr" 88.43 210 100.00 100.00 2.79e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Nudix_hydrolase 'fission yeast' 4896 Eukaryota Fungi Schizosaccharomyces pombe 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 _Details $Nudix_hydrolase 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pet15b 'Vector was modified with an additional four histidine residues for a total of ten histidine residues.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_hydrolase 1.4 mM '[U-99% 15N]' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_sample_13C-15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_hydrolase 1.2 mM '[U-99% 13C; U-99% 15N]' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_sample_2H-13C-15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_hydrolase 0.35 mM '[U-100% 13C; U-100% 15N; 80% 2H]' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_sample_15N-Lys _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_hydrolase 1.4 mM [U-15N]-Lys H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_sample_15N-Leu _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Nudix_hydrolase 1 mM [U-15N]-Leu H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Equipped with cryoprobe.' save_ ############################# # NMR applied experiments # ############################# save_3D_C(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_13C-15N save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2H-13C-15N save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2H-13C-15N save_ save_3D_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_2H-13C-15N save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2H-13C-15N save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2H-13C-15N save_ save_1H-15N_heteronuclear_NOE_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N heteronuclear NOE' _Sample_label $sample_15N save_ save_15N_T1_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1' _Sample_label $sample_15N save_ save_15N_T2_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2' _Sample_label $sample_15N save_ save_2D_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2H-13C-15N save_ save_2D_1H-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_15N-Lys save_ save_2D_1H-15N_HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_15N-Leu 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' 25 . mM pH 6.4 . pH pressure 1 . atm temperature 300 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 C(CO)NH' '3D HNCA' '3D HNCACB' '3D HN(CO)CACB' '3D HNCO' '3D HN(CA)CO' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_13C-15N $sample_2H-13C-15N $sample_15N-Lys $sample_15N-Leu stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Nudix hydrolase' _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 -6 18 LEU H H 7.998 0.01 1 2 -6 18 LEU C C 177.115 0.1 1 3 -6 18 LEU CA C 54.694 0.1 1 4 -6 18 LEU CB C 41.377 0.1 1 5 -6 18 LEU N N 121.354 0.1 1 6 -5 19 VAL H H 8.050 0.01 1 7 -5 19 VAL C C 174.421 0.1 1 8 -5 19 VAL CA C 59.319 0.1 1 9 -5 19 VAL CB C 31.794 0.1 1 10 -5 19 VAL N N 122.260 0.1 1 11 -4 20 PRO C C 177.044 0.1 1 12 -4 20 PRO CA C 62.202 0.1 1 13 -4 20 PRO CB C 31.218 0.1 1 14 -3 21 ARG H H 8.499 0.01 1 15 -3 21 ARG C C 176.014 0.1 1 16 -3 21 ARG CA C 56.135 0.1 1 17 -3 21 ARG CB C 29.932 0.1 1 18 -3 21 ARG N N 120.399 0.1 1 19 -1 23 SER CA C 57.446 0.1 1 20 -1 23 SER CB C 63.354 0.1 1 21 0 24 HIS H H 8.594 0.01 1 22 0 24 HIS CA C 56.414 0.1 1 23 0 24 HIS CB C 28.696 0.1 1 24 0 24 HIS N N 116.688 0.1 1 25 1 25 MET C C 175.692 0.1 1 26 20 26 VAL H H 7.728 0.01 1 27 20 26 VAL C C 175.190 0.1 1 28 20 26 VAL CA C 61.409 0.1 1 29 20 26 VAL CB C 32.010 0.1 1 30 20 26 VAL N N 121.983 0.1 1 31 22 28 ARG H H 8.213 0.01 1 32 22 28 ARG C C 176.685 0.1 1 33 22 28 ARG CA C 57.158 0.1 1 34 22 28 ARG CB C 29.272 0.1 1 35 22 28 ARG N N 119.817 0.1 1 36 23 29 SER H H 8.358 0.01 1 37 23 29 SER C C 177.094 0.1 1 38 23 29 SER CA C 59.233 0.1 1 39 23 29 SER CB C 63.298 0.1 1 40 23 29 SER N N 116.471 0.1 1 41 27 33 ARG C C 176.620 0.1 1 42 27 33 ARG CA C 56.349 0.1 1 43 27 33 ARG CB C 29.705 0.1 1 44 28 34 GLU H H 8.379 0.01 1 45 28 34 GLU C C 177.086 0.1 1 46 28 34 GLU CA C 56.592 0.1 1 47 28 34 GLU CB C 29.304 0.1 1 48 28 34 GLU N N 120.969 0.1 1 49 29 35 GLY H H 8.374 0.01 1 50 29 35 GLY C C 174.315 0.1 1 51 29 35 GLY CA C 45.124 0.1 1 52 29 35 GLY N N 109.494 0.1 1 53 30 36 ARG H H 8.139 0.01 1 54 30 36 ARG C C 176.675 0.1 1 55 30 36 ARG CA C 55.861 0.1 1 56 30 36 ARG CB C 29.777 0.1 1 57 30 36 ARG N N 120.186 0.1 1 58 31 37 THR H H 8.148 0.01 1 59 31 37 THR C C 174.382 0.1 1 60 31 37 THR CA C 61.769 0.1 1 61 31 37 THR CB C 69.407 0.1 1 62 31 37 THR N N 114.863 0.1 1 63 32 38 LYS H H 8.491 0.01 1 64 32 38 LYS C C 175.750 0.1 1 65 32 38 LYS CA C 55.717 0.1 1 66 32 38 LYS CB C 32.155 0.1 1 67 32 38 LYS N N 123.296 0.1 1 68 33 39 ASN H H 8.154 0.01 1 69 33 39 ASN C C 174.275 0.1 1 70 33 39 ASN CA C 53.267 0.1 1 71 33 39 ASN CB C 39.864 0.1 1 72 33 39 ASN N N 118.904 0.1 1 73 34 40 ARG H H 8.253 0.01 1 74 34 40 ARG C C 175.243 0.1 1 75 34 40 ARG CA C 55.212 0.1 1 76 34 40 ARG CB C 31.506 0.1 1 77 34 40 ARG N N 120.061 0.1 1 78 35 41 PHE H H 8.230 0.01 1 79 35 41 PHE C C 175.243 0.1 1 80 35 41 PHE CA C 55.789 0.1 1 81 35 41 PHE CB C 41.738 0.1 1 82 35 41 PHE N N 117.375 0.1 1 83 36 42 ASN H H 9.218 0.01 1 84 36 42 ASN C C 175.429 0.1 1 85 36 42 ASN CA C 50.312 0.1 1 86 36 42 ASN CB C 38.640 0.1 1 87 36 42 ASN N N 123.147 0.1 1 88 37 43 PRO C C 177.402 0.1 1 89 37 43 PRO CA C 63.859 0.1 1 90 37 43 PRO CB C 31.506 0.1 1 91 38 44 ILE H H 8.445 0.01 1 92 38 44 ILE C C 177.656 0.1 1 93 38 44 ILE CA C 62.204 0.1 1 94 38 44 ILE CB C 36.898 0.1 1 95 38 44 ILE N N 118.093 0.1 1 96 39 45 THR H H 7.084 0.01 1 97 39 45 THR C C 176.342 0.1 1 98 39 45 THR CA C 61.200 0.1 1 99 39 45 THR CB C 70.233 0.1 1 100 39 45 THR N N 106.734 0.1 1 101 40 46 GLY H H 8.459 0.01 1 102 40 46 GLY C C 173.626 0.1 1 103 40 46 GLY CA C 44.927 0.1 1 104 40 46 GLY N N 110.131 0.1 1 105 41 47 ALA H H 7.658 0.01 1 106 41 47 ALA C C 176.953 0.1 1 107 41 47 ALA CA C 51.881 0.1 1 108 41 47 ALA CB C 19.334 0.1 1 109 41 47 ALA N N 121.686 0.1 1 110 42 48 ARG H H 8.616 0.01 1 111 42 48 ARG C C 175.018 0.1 1 112 42 48 ARG CA C 56.005 0.1 1 113 42 48 ARG CB C 30.425 0.1 1 114 42 48 ARG N N 122.233 0.1 1 115 43 49 LEU H H 7.787 0.01 1 116 43 49 LEU C C 176.766 0.1 1 117 43 49 LEU CA C 53.987 0.1 1 118 43 49 LEU CB C 41.666 0.1 1 119 43 49 LEU N N 121.504 0.1 1 120 44 50 ALA H H 8.728 0.01 1 121 44 50 ALA C C 174.859 0.1 1 122 44 50 ALA CA C 50.160 0.1 1 123 44 50 ALA CB C 22.201 0.1 1 124 44 50 ALA N N 124.826 0.1 1 125 45 51 ALA H H 9.045 0.01 1 126 45 51 ALA C C 176.065 0.1 1 127 45 51 ALA CA C 50.232 0.1 1 128 45 51 ALA CB C 22.130 0.1 1 129 45 51 ALA N N 123.074 0.1 1 130 46 52 GLY H H 8.395 0.01 1 131 46 52 GLY C C 172.976 0.1 1 132 46 52 GLY CA C 43.683 0.1 1 133 46 52 GLY N N 106.092 0.1 1 134 47 53 VAL H H 8.163 0.01 1 135 47 53 VAL C C 174.024 0.1 1 136 47 53 VAL CA C 59.536 0.1 1 137 47 53 VAL CB C 34.749 0.1 1 138 47 53 VAL N N 114.229 0.1 1 139 48 54 VAL H H 8.858 0.01 1 140 48 54 VAL C C 172.711 0.1 1 141 48 54 VAL CA C 61.631 0.1 1 142 48 54 VAL CB C 30.517 0.1 1 143 48 54 VAL N N 126.518 0.1 1 144 49 55 ALA H H 9.893 0.01 1 145 49 55 ALA C C 174.461 0.1 1 146 49 55 ALA CA C 49.658 0.1 1 147 49 55 ALA CB C 18.688 0.1 1 148 49 55 ALA N N 130.288 0.1 1 149 50 56 LEU H H 9.335 0.01 1 150 50 56 LEU C C 177.006 0.1 1 151 50 56 LEU CA C 51.809 0.1 1 152 50 56 LEU CB C 18.688 0.1 1 153 50 56 LEU N N 122.445 0.1 1 154 51 57 SER H H 8.501 0.01 1 155 51 57 SER C C 176.370 0.1 1 156 51 57 SER CA C 57.544 0.1 1 157 51 57 SER CB C 62.849 0.1 1 158 51 57 SER N N 114.456 0.1 1 159 52 58 ALA H H 8.600 0.01 1 160 52 58 ALA C C 178.955 0.1 1 161 52 58 ALA CA C 54.965 0.1 1 162 52 58 ALA CB C 17.167 0.1 1 163 52 58 ALA N N 122.224 0.1 1 164 53 59 ASP H H 7.694 0.01 1 165 53 59 ASP C C 175.773 0.1 1 166 53 59 ASP CA C 52.669 0.1 1 167 53 59 ASP CB C 39.262 0.1 1 168 53 59 ASP N N 113.114 0.1 1 169 54 60 LYS H H 8.412 0.01 1 170 54 60 LYS C C 174.624 0.1 1 171 54 60 LYS CA C 57.759 0.1 1 172 54 60 LYS CB C 27.865 0.1 1 173 54 60 LYS N N 113.444 0.1 1 174 55 61 ARG H H 7.719 0.01 1 175 55 61 ARG C C 176.807 0.1 1 176 55 61 ARG CA C 57.831 0.1 1 177 55 61 ARG CB C 30.517 0.1 1 178 55 61 ARG N N 114.511 0.1 1 179 56 62 LYS H H 7.750 0.01 1 180 56 62 LYS C C 173.215 0.1 1 181 56 62 LYS CA C 53.171 0.1 1 182 56 62 LYS CB C 37.113 0.1 1 183 56 62 LYS N N 116.217 0.1 1 184 57 63 VAL H H 9.418 0.01 1 185 57 63 VAL C C 172.940 0.1 1 186 57 63 VAL CA C 56.756 0.1 1 187 57 63 VAL CB C 34.245 0.1 1 188 57 63 VAL N N 117.727 0.1 1 189 58 64 LEU H H 8.619 0.01 1 190 58 64 LEU C C 174.918 0.1 1 191 58 64 LEU CA C 53.556 0.1 1 192 58 64 LEU CB C 41.166 0.1 1 193 58 64 LEU N N 130.347 0.1 1 194 59 65 LEU H H 8.447 0.01 1 195 59 65 LEU C C 176.211 0.1 1 196 59 65 LEU CA C 53.084 0.1 1 197 59 65 LEU CB C 42.594 0.1 1 198 59 65 LEU N N 126.231 0.1 1 199 60 66 VAL H H 8.675 0.01 1 200 60 66 VAL C C 175.202 0.1 1 201 60 66 VAL CA C 57.626 0.1 1 202 60 66 VAL CB C 35.064 0.1 1 203 60 66 VAL N N 109.161 0.1 1 204 61 67 SER H H 8.507 0.01 1 205 61 67 SER C C 175.123 0.1 1 206 61 67 SER CA C 57.023 0.1 1 207 61 67 SER CB C 64.070 0.1 1 208 61 67 SER N N 115.108 0.1 1 209 64 70 LYS H H 7.973 0.01 1 210 64 70 LYS C C 178.252 0.1 1 211 64 70 LYS CA C 58.599 0.1 1 212 64 70 LYS CB C 31.650 0.1 1 213 64 70 LYS N N 118.058 0.1 1 214 65 71 LYS H H 7.770 0.01 1 215 65 71 LYS C C 178.158 0.1 1 216 65 71 LYS CA C 58.383 0.1 1 217 65 71 LYS CB C 31.722 0.1 1 218 65 71 LYS N N 119.429 0.1 1 219 67 73 PRO C C 176.209 0.1 1 220 67 73 PRO CA C 62.922 0.1 1 221 67 73 PRO CB C 31.218 0.1 1 222 68 74 SER H H 7.832 0.01 1 223 68 74 SER C C 173.125 0.1 1 224 68 74 SER CA C 56.797 0.1 1 225 68 74 SER CB C 64.003 0.1 1 226 68 74 SER N N 116.193 0.1 1 227 69 75 TRP H H 9.511 0.01 1 228 69 75 TRP C C 175.051 0.1 1 229 69 75 TRP CA C 59.576 0.1 1 230 69 75 TRP CB C 35.325 0.1 1 231 69 75 TRP N N 114.852 0.1 1 232 70 76 VAL H H 6.545 0.01 1 233 70 76 VAL C C 173.702 0.1 1 234 70 76 VAL CA C 57.874 0.1 1 235 70 76 VAL CB C 29.782 0.1 1 236 70 76 VAL N N 106.839 0.1 1 237 71 77 VAL H H 9.223 0.01 1 238 71 77 VAL C C 177.866 0.1 1 239 71 77 VAL CA C 60.328 0.1 1 240 71 77 VAL CB C 29.488 0.1 1 241 71 77 VAL N N 116.773 0.1 1 242 73 79 LYS H H 7.890 0.01 1 243 73 79 LYS C C 174.103 0.1 1 244 73 79 LYS CA C 55.012 0.1 1 245 73 79 LYS CB C 33.695 0.1 1 246 73 79 LYS N N 122.424 0.1 1 247 74 80 GLY H H 8.645 0.01 1 248 74 80 GLY C C 172.207 0.1 1 249 74 80 GLY CA C 44.603 0.1 1 250 74 80 GLY N N 108.498 0.1 1 251 75 81 GLY H H 8.433 0.01 1 252 75 81 GLY C C 172.119 0.1 1 253 75 81 GLY CA C 45.454 0.1 1 254 75 81 GLY N N 105.354 0.1 1 255 77 83 GLU C C 178.291 0.1 1 256 77 83 GLU CA C 55.789 0.1 1 257 77 83 GLU CB C 30.065 0.1 1 258 78 84 ALA H H 8.428 0.01 1 259 78 84 ALA C C 177.654 0.1 1 260 78 84 ALA CA C 53.843 0.1 1 261 78 84 ALA CB C 17.960 0.1 1 262 78 84 ALA N N 120.887 0.1 1 263 79 85 ASP H H 8.210 0.01 1 264 79 85 ASP C C 174.607 0.1 1 265 79 85 ASP CA C 53.915 0.1 1 266 79 85 ASP CB C 39.648 0.1 1 267 79 85 ASP N N 114.429 0.1 1 268 80 86 GLU H H 7.669 0.01 1 269 80 86 GLU C C 175.946 0.1 1 270 80 86 GLU CA C 53.652 0.1 1 271 80 86 GLU CB C 31.578 0.1 1 272 80 86 GLU N N 117.142 0.1 1 273 82 88 VAL C C 175.745 0.1 1 274 82 88 VAL CA C 64.363 0.1 1 275 82 88 VAL CB C 29.128 0.1 1 276 83 89 GLN H H 7.497 0.01 1 277 83 89 GLN C C 178.027 0.1 1 278 83 89 GLN CA C 59.552 0.1 1 279 83 89 GLN CB C 25.857 0.1 1 280 83 89 GLN N N 119.022 0.1 1 281 84 90 GLN H H 7.377 0.01 1 282 84 90 GLN C C 179.180 0.1 1 283 84 90 GLN CA C 58.261 0.1 1 284 84 90 GLN CB C 27.650 0.1 1 285 84 90 GLN N N 117.321 0.1 1 286 85 91 ALA H H 8.019 0.01 1 287 85 91 ALA C C 178.902 0.1 1 288 85 91 ALA CA C 54.892 0.1 1 289 85 91 ALA CB C 18.043 0.1 1 290 85 91 ALA N N 122.957 0.1 1 291 86 92 ALA H H 7.577 0.01 1 292 86 92 ALA C C 179.141 0.1 1 293 86 92 ALA CA C 54.820 0.1 1 294 86 92 ALA CB C 17.111 0.1 1 295 86 92 ALA N N 119.202 0.1 1 296 87 93 LEU H H 7.649 0.01 1 297 87 93 LEU C C 180.506 0.1 1 298 87 93 LEU CA C 57.257 0.1 1 299 87 93 LEU CB C 40.482 0.1 1 300 87 93 LEU N N 115.057 0.1 1 301 88 94 ARG H H 8.653 0.01 1 302 88 94 ARG C C 178.517 0.1 1 303 88 94 ARG CA C 59.480 0.1 1 304 88 94 ARG CB C 27.936 0.1 1 305 88 94 ARG N N 123.523 0.1 1 306 89 95 GLU H H 8.561 0.01 1 307 89 95 GLU C C 179.934 0.1 1 308 89 95 GLU CA C 58.439 0.1 1 309 89 95 GLU CB C 26.895 0.1 1 310 89 95 GLU N N 119.097 0.1 1 311 90 96 GLY H H 8.453 0.01 1 312 90 96 GLY C C 175.469 0.1 1 313 90 96 GLY CA C 47.358 0.1 1 314 90 96 GLY N N 104.392 0.1 1 315 91 97 TRP H H 8.091 0.01 1 316 91 97 TRP C C 177.218 0.1 1 317 91 97 TRP CA C 60.102 0.1 1 318 91 97 TRP CB C 28.696 0.1 1 319 91 97 TRP N N 124.066 0.1 1 320 92 98 GLU H H 9.223 0.01 1 321 92 98 GLU C C 177.876 0.1 1 322 92 98 GLU CA C 60.314 0.1 1 323 92 98 GLU CB C 29.526 0.1 1 324 92 98 GLU N N 116.772 0.1 1 325 93 99 GLU H H 8.094 0.01 1 326 93 99 GLU C C 176.662 0.1 1 327 93 99 GLU CA C 57.783 0.1 1 328 93 99 GLU CB C 30.116 0.1 1 329 93 99 GLU N N 107.719 0.1 1 330 94 100 GLY H H 6.992 0.01 1 331 94 100 GLY C C 183.344 0.1 1 332 94 100 GLY CA C 43.887 0.1 1 333 94 100 GLY N N 128.233 0.1 1 334 95 101 GLY H H 7.533 0.01 1 335 95 101 GLY C C 172.473 0.1 1 336 95 101 GLY CA C 46.323 0.1 1 337 95 101 GLY N N 112.132 0.1 1 338 96 102 LEU H H 6.832 0.01 1 339 96 102 LEU C C 174.130 0.1 1 340 96 102 LEU CA C 53.458 0.1 1 341 96 102 LEU CB C 43.421 0.1 1 342 96 102 LEU N N 116.055 0.1 1 343 97 103 VAL H H 8.448 0.01 1 344 97 103 VAL C C 176.489 0.1 1 345 97 103 VAL CA C 60.555 0.1 1 346 97 103 VAL CB C 33.385 0.1 1 347 97 103 VAL N N 122.142 0.1 1 348 98 104 GLY H H 8.737 0.01 1 349 98 104 GLY C C 181.368 0.1 1 350 98 104 GLY CA C 46.146 0.1 1 351 98 104 GLY N N 113.604 0.1 1 352 99 105 HIS H H 7.762 0.01 1 353 99 105 HIS C C 173.440 0.1 1 354 99 105 HIS CA C 53.315 0.1 1 355 99 105 HIS CB C 31.162 0.1 1 356 99 105 HIS N N 114.108 0.1 1 357 100 106 ILE H H 8.939 0.01 1 358 100 106 ILE C C 177.722 0.1 1 359 100 106 ILE CA C 60.585 0.1 1 360 100 106 ILE CB C 38.843 0.1 1 361 100 106 ILE N N 123.190 0.1 1 362 101 107 THR H H 9.093 0.01 1 363 101 107 THR C C 175.905 0.1 1 364 101 107 THR CA C 61.846 0.1 1 365 101 107 THR CB C 67.366 0.1 1 366 101 107 THR N N 119.160 0.1 1 367 102 108 ARG H H 7.504 0.01 1 368 102 108 ARG C C 174.859 0.1 1 369 102 108 ARG CA C 54.892 0.1 1 370 102 108 ARG CB C 30.446 0.1 1 371 102 108 ARG N N 115.976 0.1 1 372 103 109 SER H H 8.715 0.01 1 373 103 109 SER C C 175.959 0.1 1 374 103 109 SER CA C 57.401 0.1 1 375 103 109 SER CB C 62.276 0.1 1 376 103 109 SER N N 114.092 0.1 1 377 104 110 LEU H H 9.301 0.01 1 378 104 110 LEU C C 175.773 0.1 1 379 104 110 LEU CA C 53.960 0.1 1 380 104 110 LEU CB C 40.984 0.1 1 381 104 110 LEU N N 127.205 0.1 1 382 105 111 GLY H H 8.044 0.01 1 383 105 111 GLY C C 171.969 0.1 1 384 105 111 GLY CA C 43.063 0.1 1 385 105 111 GLY N N 106.759 0.1 1 386 106 112 SER H H 7.730 0.01 1 387 106 112 SER C C 174.236 0.1 1 388 106 112 SER CA C 56.469 0.1 1 389 106 112 SER CB C 63.925 0.1 1 390 106 112 SER N N 112.517 0.1 1 391 108 114 LYS H H 8.036 0.01 1 392 108 114 LYS CA C 57.734 0.1 1 393 108 114 LYS CB C 29.921 0.1 1 394 108 114 LYS N N 120.301 0.1 1 395 109 115 ASP H H 8.771 0.01 1 396 109 115 ASP C C 174.130 0.1 1 397 109 115 ASP CA C 56.509 0.1 1 398 109 115 ASP CB C 40.945 0.1 1 399 109 115 ASP N N 118.319 0.1 1 400 110 116 LYS H H 8.817 0.01 1 401 110 116 LYS C C 178.093 0.1 1 402 110 116 LYS CA C 57.806 0.1 1 403 110 116 LYS CB C 31.434 0.1 1 404 110 116 LYS N N 124.983 0.1 1 405 112 118 PRO C C 176.514 0.1 1 406 112 118 PRO CA C 64.579 0.1 1 407 112 118 PRO CB C 31.794 0.1 1 408 113 119 THR H H 8.090 0.01 1 409 113 119 THR CA C 61.625 0.1 1 410 113 119 THR CB C 69.479 0.1 1 411 113 119 THR N N 113.932 0.1 1 412 114 120 ASP H H 8.277 0.01 1 413 114 120 ASP C C 176.184 0.1 1 414 114 120 ASP CA C 53.339 0.1 1 415 114 120 ASP CB C 40.369 0.1 1 416 114 120 ASP N N 120.672 0.1 1 417 117 123 ASP H H 8.048 0.01 1 418 117 123 ASP CA C 54.420 0.1 1 419 117 123 ASP CB C 40.225 0.1 1 420 117 123 ASP N N 124.844 0.1 1 421 119 125 ARG H H 8.737 0.01 1 422 119 125 ARG C C 174.882 0.1 1 423 119 125 ARG CA C 56.869 0.1 1 424 119 125 ARG CB C 31.218 0.1 1 425 119 125 ARG N N 117.389 0.1 1 426 120 126 LYS H H 8.871 0.01 1 427 120 126 LYS C C 174.539 0.1 1 428 120 126 LYS CA C 56.009 0.1 1 429 120 126 LYS CB C 36.550 0.1 1 430 120 126 LYS N N 123.132 0.1 1 431 121 127 LYS H H 7.594 0.01 1 432 121 127 LYS C C 171.743 0.1 1 433 121 127 LYS CA C 55.162 0.1 1 434 121 127 LYS CB C 33.091 0.1 1 435 121 127 LYS N N 118.698 0.1 1 436 123 129 LEU H H 8.247 0.01 1 437 123 129 LEU C C 178.226 0.1 1 438 123 129 LEU CA C 56.509 0.1 1 439 123 129 LEU CB C 40.945 0.1 1 440 123 129 LEU N N 121.406 0.1 1 441 124 130 LYS H H 7.939 0.01 1 442 124 130 LYS C C 178.080 0.1 1 443 124 130 LYS CA C 57.806 0.1 1 444 124 130 LYS CB C 31.434 0.1 1 445 124 130 LYS N N 119.310 0.1 1 446 125 131 GLN H H 7.965 0.01 1 447 125 131 GLN C C 177.152 0.1 1 448 125 131 GLN CA C 56.869 0.1 1 449 125 131 GLN CB C 28.119 0.1 1 450 125 131 GLN N N 118.777 0.1 1 451 126 132 LEU H H 8.008 0.01 1 452 126 132 LEU C C 178.211 0.1 1 453 126 132 LEU CA C 55.789 0.1 1 454 126 132 LEU CB C 41.233 0.1 1 455 126 132 LEU N N 121.257 0.1 1 456 127 133 MET H H 8.103 0.01 1 457 127 133 MET C C 176.778 0.1 1 458 127 133 MET CA C 55.691 0.1 1 459 127 133 MET CB C 31.873 0.1 1 460 127 133 MET N N 118.498 0.1 1 461 129 135 LYS H H 7.943 0.01 1 462 129 135 LYS C C 176.899 0.1 1 463 129 135 LYS CA C 56.487 0.1 1 464 129 135 LYS CB C 31.794 0.1 1 465 129 135 LYS N N 120.120 0.1 1 466 131 137 SER C C 175.003 0.1 1 467 131 137 SER CA C 56.487 0.1 1 468 131 137 SER CB C 64.579 0.1 1 469 132 138 GLY H H 8.366 0.01 1 470 132 138 GLY C C 173.957 0.1 1 471 132 138 GLY CA C 45.052 0.1 1 472 132 138 GLY N N 110.322 0.1 1 473 133 139 ASN H H 8.258 0.01 1 474 133 139 ASN C C 174.859 0.1 1 475 133 139 ASN CA C 52.906 0.1 1 476 133 139 ASN CB C 38.712 0.1 1 477 133 139 ASN N N 118.325 0.1 1 478 134 140 ASP H H 8.333 0.01 1 479 134 140 ASP C C 176.237 0.1 1 480 134 140 ASP CA C 54.131 0.1 1 481 134 140 ASP CB C 40.585 0.1 1 482 134 140 ASP N N 120.270 0.1 1 483 135 141 VAL H H 8.049 0.01 1 484 135 141 VAL C C 176.489 0.1 1 485 135 141 VAL CA C 61.985 0.1 1 486 135 141 VAL CB C 31.722 0.1 1 487 135 141 VAL N N 119.378 0.1 1 488 136 142 SER H H 8.392 0.01 1 489 136 142 SER C C 174.978 0.1 1 490 136 142 SER CA C 58.424 0.1 1 491 136 142 SER CB C 63.499 0.1 1 492 136 142 SER N N 118.751 0.1 1 493 137 143 THR H H 8.105 0.01 1 494 137 143 THR C C 174.435 0.1 1 495 137 143 THR CA C 61.697 0.1 1 496 137 143 THR CB C 69.191 0.1 1 497 137 143 THR N N 115.060 0.1 1 498 138 144 ASN H H 8.357 0.01 1 499 138 144 ASN C C 175.601 0.1 1 500 138 144 ASN CA C 53.627 0.1 1 501 138 144 ASN CB C 38.279 0.1 1 502 138 144 ASN N N 120.738 0.1 1 503 139 145 THR H H 8.128 0.01 1 504 139 145 THR C C 174.806 0.1 1 505 139 145 THR CA C 62.057 0.1 1 506 139 145 THR CB C 69.191 0.1 1 507 139 145 THR N N 114.519 0.1 1 508 140 146 GLU H H 8.375 0.01 1 509 140 146 GLU C C 176.715 0.1 1 510 140 146 GLU CA C 56.437 0.1 1 511 140 146 GLU CB C 29.128 0.1 1 512 140 146 GLU N N 122.790 0.1 1 513 141 147 LEU H H 8.194 0.01 1 514 141 147 LEU C C 178.160 0.1 1 515 141 147 LEU CA C 55.181 0.1 1 516 141 147 LEU CB C 41.738 0.1 1 517 141 147 LEU N N 122.261 0.1 1 518 142 148 GLY H H 8.343 0.01 1 519 142 148 GLY C C 174.474 0.1 1 520 142 148 GLY CA C 45.052 0.1 1 521 142 148 GLY N N 109.064 0.1 1 522 143 149 ALA H H 8.166 0.01 1 523 143 149 ALA C C 178.769 0.1 1 524 143 149 ALA CA C 52.979 0.1 1 525 143 149 ALA CB C 18.104 0.1 1 526 143 149 ALA N N 123.512 0.1 1 527 144 150 GLU H H 8.437 0.01 1 528 144 150 GLU C C 177.364 0.1 1 529 144 150 GLU CA C 52.906 0.1 1 530 144 150 GLU CB C 28.696 0.1 1 531 144 150 GLU N N 118.731 0.1 1 532 145 151 ALA H H 8.067 0.01 1 533 145 151 ALA C C 178.690 0.1 1 534 145 151 ALA CA C 53.195 0.1 1 535 145 151 ALA CB C 17.960 0.1 1 536 145 151 ALA N N 122.822 0.1 1 537 146 152 GLU H H 8.138 0.01 1 538 146 152 GLU C C 177.073 0.1 1 539 146 152 GLU CA C 57.230 0.1 1 540 146 152 GLU CB C 29.056 0.1 1 541 146 152 GLU N N 117.814 0.1 1 542 147 153 LYS H H 7.864 0.01 1 543 147 153 LYS C C 176.648 0.1 1 544 147 153 LYS CA C 56.365 0.1 1 545 147 153 LYS CB C 31.794 0.1 1 546 147 153 LYS N N 119.377 0.1 1 547 148 154 LEU H H 7.728 0.01 1 548 148 154 LEU C C 176.622 0.1 1 549 148 154 LEU CA C 54.924 0.1 1 550 148 154 LEU CB C 41.522 0.1 1 551 148 154 LEU N N 121.120 0.1 1 552 149 155 LEU C C 176.423 0.1 1 553 149 155 LEU CA C 54.276 0.1 1 554 149 155 LEU CB C 41.330 0.1 1 555 150 156 LEU H H 8.031 0.01 1 556 150 156 LEU C C 174.408 0.1 1 557 150 156 LEU CA C 51.826 0.1 1 558 150 156 LEU CB C 41.161 0.1 1 559 150 156 LEU N N 123.528 0.1 1 560 152 158 PRO C C 176.912 0.1 1 561 152 158 PRO CA C 62.706 0.1 1 562 152 158 PRO CB C 31.218 0.1 1 563 153 159 ARG H H 8.440 0.01 1 564 153 159 ARG C C 176.025 0.1 1 565 153 159 ARG CA C 55.925 0.1 1 566 153 159 ARG CB C 29.921 0.1 1 567 153 159 ARG N N 121.713 0.1 1 568 154 160 ALA H H 8.641 0.01 1 569 154 160 ALA C C 178.252 0.1 1 570 154 160 ALA CA C 52.114 0.1 1 571 154 160 ALA CB C 18.536 0.1 1 572 154 160 ALA N N 122.694 0.1 1 573 155 161 GLU H H 8.568 0.01 1 574 155 161 GLU C C 174.315 0.1 1 575 155 161 GLU CA C 54.708 0.1 1 576 155 161 GLU CB C 30.137 0.1 1 577 155 161 GLU N N 122.372 0.1 1 578 156 162 CYS H H 8.356 0.01 1 579 156 162 CYS C C 172.486 0.1 1 580 156 162 CYS CA C 56.509 0.1 1 581 156 162 CYS CB C 29.344 0.1 1 582 156 162 CYS N N 123.744 0.1 1 583 157 163 GLU H H 8.008 0.01 1 584 157 163 GLU C C 174.753 0.1 1 585 157 163 GLU CA C 54.636 0.1 1 586 157 163 GLU CB C 29.488 0.1 1 587 157 163 GLU N N 130.499 0.1 1 588 161 167 VAL H H 8.817 0.01 1 589 161 167 VAL C C 174.501 0.1 1 590 161 167 VAL CA C 58.959 0.1 1 591 161 167 VAL CB C 35.973 0.1 1 592 161 167 VAL N N 128.355 0.1 1 593 162 168 ILE H H 8.277 0.01 1 594 162 168 ILE C C 176.410 0.1 1 595 162 168 ILE CA C 57.590 0.1 1 596 162 168 ILE CB C 35.397 0.1 1 597 162 168 ILE N N 124.963 0.1 1 598 163 169 VAL H H 9.061 0.01 1 599 163 169 VAL C C 175.734 0.1 1 600 163 169 VAL CA C 64.291 0.1 1 601 163 169 VAL CB C 31.938 0.1 1 602 163 169 VAL N N 128.597 0.1 1 603 164 170 GLU H H 9.704 0.01 1 604 164 170 GLU C C 176.927 0.1 1 605 164 170 GLU CA C 57.086 0.1 1 606 164 170 GLU CB C 30.353 0.1 1 607 164 170 GLU N N 129.476 0.1 1 608 165 171 ARG H H 7.998 0.01 1 609 165 171 ARG C C 172.698 0.1 1 610 165 171 ARG CA C 54.996 0.1 1 611 165 171 ARG CB C 31.794 0.1 1 612 165 171 ARG N N 114.371 0.1 1 613 166 172 LEU H H 8.450 0.01 1 614 166 172 LEU C C 177.722 0.1 1 615 166 172 LEU CA C 52.762 0.1 1 616 166 172 LEU CB C 41.810 0.1 1 617 166 172 LEU N N 119.081 0.1 1 618 167 173 GLU H H 8.992 0.01 1 619 167 173 GLU C C 177.656 0.1 1 620 167 173 GLU CA C 54.708 0.1 1 621 167 173 GLU CB C 30.497 0.1 1 622 167 173 GLU N N 122.006 0.1 1 623 168 174 ASP H H 8.855 0.01 1 624 168 174 ASP C C 175.601 0.1 1 625 168 174 ASP CA C 55.789 0.1 1 626 168 174 ASP CB C 41.017 0.1 1 627 168 174 ASP N N 120.410 0.1 1 628 169 175 ASN H H 7.965 0.01 1 629 169 175 ASN C C 172.990 0.1 1 630 169 175 ASN CA C 52.042 0.1 1 631 169 175 ASN CB C 39.144 0.1 1 632 169 175 ASN N N 116.345 0.1 1 633 170 176 TYR H H 7.348 0.01 1 634 170 176 TYR C C 175.336 0.1 1 635 170 176 TYR CA C 55.356 0.1 1 636 170 176 TYR CB C 34.028 0.1 1 637 170 176 TYR N N 119.546 0.1 1 638 171 177 PRO C C 178.715 0.1 1 639 171 177 PRO CA C 67.094 0.1 1 640 171 177 PRO CB C 27.255 0.1 1 641 172 178 GLU H H 7.506 0.01 1 642 172 178 GLU C C 176.383 0.1 1 643 172 178 GLU CA C 55.572 0.1 1 644 172 178 GLU CB C 27.183 0.1 1 645 172 178 GLU N N 112.582 0.1 1 646 173 179 MET H H 6.574 0.01 1 647 173 179 MET C C 175.957 0.1 1 648 173 179 MET CA C 58.671 0.1 1 649 173 179 MET CB C 31.074 0.1 1 650 173 179 MET N N 118.256 0.1 1 651 174 180 ARG C C 176.806 0.1 1 652 174 180 ARG CA C 58.992 0.1 1 653 174 180 ARG CB C 28.696 0.1 1 654 175 181 LYS H H 7.632 0.01 1 655 175 181 LYS C C 175.931 0.1 1 656 175 181 LYS CA C 56.221 0.1 1 657 175 181 LYS CB C 34.172 0.1 1 658 175 181 LYS N N 117.864 0.1 1 659 176 182 ARG H H 7.808 0.01 1 660 176 182 ARG C C 175.825 0.1 1 661 176 182 ARG CA C 54.203 0.1 1 662 176 182 ARG CB C 33.091 0.1 1 663 176 182 ARG N N 118.091 0.1 1 664 179 185 LYS H H 8.445 0.01 1 665 179 185 LYS C C 177.074 0.1 1 666 179 185 LYS CA C 55.789 0.1 1 667 179 185 LYS CB C 30.930 0.1 1 668 179 185 LYS N N 124.939 0.1 1 669 180 186 TRP C C 177.097 0.1 1 670 180 186 TRP CA C 55.717 0.1 1 671 180 186 TRP CB C 30.569 0.1 1 672 181 187 MET H H 9.628 0.01 1 673 181 187 MET C C 175.230 0.1 1 674 181 187 MET CA C 54.852 0.1 1 675 181 187 MET CB C 35.973 0.1 1 676 181 187 MET N N 122.899 0.1 1 677 182 188 SER H H 8.952 0.01 1 678 182 188 SER C C 173.732 0.1 1 679 182 188 SER CA C 57.230 0.1 1 680 182 188 SER CB C 64.579 0.1 1 681 182 188 SER N N 116.827 0.1 1 682 183 189 TYR H H 9.155 0.01 1 683 183 189 TYR C C 176.039 0.1 1 684 183 189 TYR CA C 61.985 0.1 1 685 183 189 TYR CB C 37.775 0.1 1 686 183 189 TYR N N 120.121 0.1 1 687 184 190 GLN H H 8.708 0.01 1 688 184 190 GLN C C 179.127 0.1 1 689 184 190 GLN CA C 58.959 0.1 1 690 184 190 GLN CB C 26.967 0.1 1 691 184 190 GLN N N 115.974 0.1 1 692 185 191 GLU H H 7.432 0.01 1 693 185 191 GLU C C 179.326 0.1 1 694 185 191 GLU CA C 58.239 0.1 1 695 185 191 GLU CB C 29.705 0.1 1 696 185 191 GLU N N 118.637 0.1 1 697 186 192 ALA H H 8.953 0.01 1 698 186 192 ALA C C 178.624 0.1 1 699 186 192 ALA CA C 53.987 0.1 1 700 186 192 ALA CB C 17.599 0.1 1 701 186 192 ALA N N 123.191 0.1 1 702 187 193 LYS H H 8.327 0.01 1 703 187 193 LYS C C 178.955 0.1 1 704 187 193 LYS CA C 59.319 0.1 1 705 187 193 LYS CB C 30.497 0.1 1 706 187 193 LYS N N 117.239 0.1 1 707 188 194 GLU H H 7.007 0.01 1 708 188 194 GLU C C 179.472 0.1 1 709 188 194 GLU CA C 58.239 0.1 1 710 188 194 GLU CB C 28.480 0.1 1 711 188 194 GLU N N 116.502 0.1 1 712 189 195 ALA H H 7.909 0.01 1 713 189 195 ALA C C 179.512 0.1 1 714 189 195 ALA CA C 54.131 0.1 1 715 189 195 ALA CB C 17.816 0.1 1 716 189 195 ALA N N 122.167 0.1 1 717 190 196 LEU H H 7.962 0.01 1 718 190 196 LEU C C 176.569 0.1 1 719 190 196 LEU CA C 53.987 0.1 1 720 190 196 LEU CB C 41.594 0.1 1 721 190 196 LEU N N 115.968 0.1 1 722 191 197 THR H H 7.042 0.01 1 723 191 197 THR C C 174.620 0.1 1 724 191 197 THR CA C 65.732 0.1 1 725 191 197 THR CB C 69.047 0.1 1 726 191 197 THR N N 113.810 0.1 1 727 192 198 SER H H 8.459 0.01 1 728 192 198 SER C C 174.633 0.1 1 729 192 198 SER CA C 59.103 0.1 1 730 192 198 SER CB C 62.994 0.1 1 731 192 198 SER N N 113.495 0.1 1 732 193 199 ARG H H 8.418 0.01 1 733 193 199 ARG C C 174.965 0.1 1 734 193 199 ARG CA C 50.889 0.1 1 735 193 199 ARG CB C 27.615 0.1 1 736 193 199 ARG N N 124.665 0.1 1 737 194 200 LYS H H 8.653 0.01 1 738 194 200 LYS C C 178.597 0.1 1 739 194 200 LYS CA C 58.887 0.1 1 740 194 200 LYS CB C 31.218 0.1 1 741 194 200 LYS N N 121.495 0.1 1 742 195 201 ASP H H 9.695 0.01 1 743 195 201 ASP C C 175.415 0.1 1 744 195 201 ASP CA C 55.717 0.1 1 745 195 201 ASP CB C 37.775 0.1 1 746 195 201 ASP N N 117.079 0.1 1 747 196 202 ILE H H 7.152 0.01 1 748 196 202 ILE C C 178.133 0.1 1 749 196 202 ILE CA C 63.859 0.1 1 750 196 202 ILE CB C 36.622 0.1 1 751 196 202 ILE N N 117.976 0.1 1 752 197 203 LEU H H 8.335 0.01 1 753 197 203 LEU C C 178.305 0.1 1 754 197 203 LEU CA C 57.374 0.1 1 755 197 203 LEU CB C 40.945 0.1 1 756 197 203 LEU N N 118.332 0.1 1 757 198 204 ALA H H 7.290 0.01 1 758 198 204 ALA C C 179.883 0.1 1 759 198 204 ALA CA C 54.348 0.1 1 760 198 204 ALA CB C 16.879 0.1 1 761 198 204 ALA N N 120.181 0.1 1 762 199 205 ALA H H 6.555 0.01 1 763 199 205 ALA C C 178.809 0.1 1 764 199 205 ALA CA C 54.348 0.1 1 765 199 205 ALA CB C 15.870 0.1 1 766 199 205 ALA N N 120.785 0.1 1 767 200 206 LEU H H 8.224 0.01 1 768 200 206 LEU C C 178.822 0.1 1 769 200 206 LEU CA C 57.662 0.1 1 770 200 206 LEU CB C 41.522 0.1 1 771 200 206 LEU N N 117.634 0.1 1 772 201 207 GLU H H 8.382 0.01 1 773 201 207 GLU C C 178.120 0.1 1 774 201 207 GLU CA C 58.166 0.1 1 775 201 207 GLU CB C 28.624 0.1 1 776 201 207 GLU N N 117.920 0.1 1 777 202 208 LYS H H 7.231 0.01 1 778 202 208 LYS C C 176.807 0.1 1 779 202 208 LYS CA C 55.789 0.1 1 780 202 208 LYS CB C 32.371 0.1 1 781 202 208 LYS N N 116.106 0.1 1 782 203 209 SER H H 7.615 0.01 1 783 203 209 SER C C 173.109 0.1 1 784 203 209 SER CA C 59.103 0.1 1 785 203 209 SER CB C 64.796 0.1 1 786 203 209 SER N N 116.333 0.1 1 787 204 210 SER H H 9.295 0.01 1 788 204 210 SER C C 172.791 0.1 1 789 204 210 SER CA C 57.662 0.1 1 790 204 210 SER CB C 62.346 0.1 1 791 204 210 SER N N 114.379 0.1 1 792 205 211 ILE H H 7.272 0.01 1 793 205 211 ILE C C 173.931 0.1 1 794 205 211 ILE CA C 60.616 0.1 1 795 205 211 ILE CB C 37.270 0.1 1 796 205 211 ILE N N 120.838 0.1 1 797 206 212 ILE H H 8.311 0.01 1 798 206 212 ILE C C 176.728 0.1 1 799 206 212 ILE CA C 61.841 0.1 1 800 206 212 ILE CB C 37.126 0.1 1 801 206 212 ILE N N 127.503 0.1 1 802 207 213 LYS H H 8.410 0.01 1 803 207 213 LYS C C 176.410 0.1 1 804 207 213 LYS CA C 55.861 0.1 1 805 207 213 LYS CB C 31.866 0.1 1 806 207 213 LYS N N 128.040 0.1 1 807 208 214 GLU H H 7.397 0.01 1 808 208 214 GLU C C 175.800 0.1 1 809 208 214 GLU CA C 55.686 0.1 1 810 208 214 GLU CB C 30.209 0.1 1 811 208 214 GLU N N 119.315 0.1 1 812 209 215 GLU H H 8.567 0.01 1 813 209 215 GLU C C 175.283 0.1 1 814 209 215 GLU CA C 56.149 0.1 1 815 209 215 GLU CB C 29.921 0.1 1 816 209 215 GLU N N 122.176 0.1 1 817 210 216 ASN H H 8.028 0.01 1 818 210 216 ASN C C 179.353 0.1 1 819 210 216 ASN CA C 54.420 0.1 1 820 210 216 ASN CB C 40.153 0.1 1 821 210 216 ASN N N 124.308 0.1 1 stop_ save_