data_16690 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N chemical shift assignments for the prolyl isomerase Ess1 from Candida albicans ; _BMRB_accession_number 16690 _BMRB_flat_file_name bmr16690.str _Entry_type original _Submission_date 2010-01-22 _Accession_date 2010-01-22 _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 McNaughton Lynn . . 2 Li Zhong . . 3 'Van Roey' Patrick . . 4 Hanes Steven D. . 5 LeMaster David M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 165 "13C chemical shifts" 498 "15N chemical shifts" 165 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-25 update BMRB 'complete entry citation' 2010-05-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20304107 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McNaughton Lynn . . 2 Li Zhong . . 3 'Van Roey' Patrick . . 4 Hanes Steven D. . 5 Lemaster David M. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et biophysica acta' _Journal_volume 1804 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1537 _Page_last 1541 _Year 2010 _Details . loop_ _Keyword '15N relaxation' 'chemical shift' flexibility NMR 'prolyl isomerase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C. albicans Ess1 prolyl isomerase' _Enzyme_commission_number 'EC: 5.2.1.8' loop_ _Mol_system_component_name _Mol_label 'C. albicans Ess1 prolyl isomerase' $entity stop_ _System_molecular_weight 19855 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'C. albicans Ess1 prolyl isomerase' stop_ loop_ _Biological_function 'prolyl isomerase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C. albicans Ess1 prolyl isomerase' _Molecular_mass 19855 _Mol_thiol_state 'all free' loop_ _Biological_function 'prolyl isomerase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 180 _Mol_residue_sequence ; GSHMASTSTGLPPNWTIRVS RSHNKEYFLNQSTNESSWDP PYGTDKEVLNAYIAKFKNNG YKPLVNEDGQVRVSHLLIKN NQSRKPKSWKSPDGISRTRD ESIQILKKHLERILSGEVKL SELANTESDCSSHDRGGDLG FFSKGQMQPPFEEAAFNLHV GEVSNIIETNSGVHILQRTG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 ALA 6 3 SER 7 4 THR 8 5 SER 9 6 THR 10 7 GLY 11 8 LEU 12 9 PRO 13 10 PRO 14 11 ASN 15 12 TRP 16 13 THR 17 14 ILE 18 15 ARG 19 16 VAL 20 17 SER 21 18 ARG 22 19 SER 23 20 HIS 24 21 ASN 25 22 LYS 26 23 GLU 27 24 TYR 28 25 PHE 29 26 LEU 30 27 ASN 31 28 GLN 32 29 SER 33 30 THR 34 31 ASN 35 32 GLU 36 33 SER 37 34 SER 38 35 TRP 39 36 ASP 40 37 PRO 41 38 PRO 42 39 TYR 43 40 GLY 44 41 THR 45 42 ASP 46 43 LYS 47 44 GLU 48 45 VAL 49 46 LEU 50 47 ASN 51 48 ALA 52 49 TYR 53 50 ILE 54 51 ALA 55 52 LYS 56 53 PHE 57 54 LYS 58 55 ASN 59 56 ASN 60 57 GLY 61 58 TYR 62 59 LYS 63 60 PRO 64 61 LEU 65 62 VAL 66 63 ASN 67 64 GLU 68 65 ASP 69 66 GLY 70 67 GLN 71 68 VAL 72 69 ARG 73 70 VAL 74 71 SER 75 72 HIS 76 73 LEU 77 74 LEU 78 75 ILE 79 76 LYS 80 77 ASN 81 78 ASN 82 79 GLN 83 80 SER 84 81 ARG 85 82 LYS 86 83 PRO 87 84 LYS 88 85 SER 89 86 TRP 90 87 LYS 91 88 SER 92 89 PRO 93 90 ASP 94 91 GLY 95 92 ILE 96 93 SER 97 94 ARG 98 95 THR 99 96 ARG 100 97 ASP 101 98 GLU 102 99 SER 103 100 ILE 104 101 GLN 105 102 ILE 106 103 LEU 107 104 LYS 108 105 LYS 109 106 HIS 110 107 LEU 111 108 GLU 112 109 ARG 113 110 ILE 114 111 LEU 115 112 SER 116 113 GLY 117 114 GLU 118 115 VAL 119 116 LYS 120 117 LEU 121 118 SER 122 119 GLU 123 120 LEU 124 121 ALA 125 122 ASN 126 123 THR 127 124 GLU 128 125 SER 129 126 ASP 130 127 CYS 131 128 SER 132 129 SER 133 130 HIS 134 131 ASP 135 132 ARG 136 133 GLY 137 134 GLY 138 135 ASP 139 136 LEU 140 137 GLY 141 138 PHE 142 139 PHE 143 140 SER 144 141 LYS 145 142 GLY 146 143 GLN 147 144 MET 148 145 GLN 149 146 PRO 150 147 PRO 151 148 PHE 152 149 GLU 153 150 GLU 154 151 ALA 155 152 ALA 156 153 PHE 157 154 ASN 158 155 LEU 159 156 HIS 160 157 VAL 161 158 GLY 162 159 GLU 163 160 VAL 164 161 SER 165 162 ASN 166 163 ILE 167 164 ILE 168 165 GLU 169 166 THR 170 167 ASN 171 168 SER 172 169 GLY 173 170 VAL 174 171 HIS 175 172 ILE 176 173 LEU 177 174 GLN 178 175 ARG 179 176 THR 180 177 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 1YW5 "Peptidyl-Prolyl Isomerase Ess1 From Candida Albicans" 98.33 177 100.00 100.00 4.63e-127 EMBL CAX44676 "peptidyl prolyl cis/trans isomerase, putative [Candida dubliniensis CD36]" 98.33 177 97.18 98.31 7.84e-124 GB AAK00626 "peptidyl prolyl cis/trans isomerase [Candida albicans]" 98.33 177 100.00 100.00 4.63e-127 GB EAK91142 "hypothetical protein CaO19.5196 [Candida albicans SC5314]" 98.33 177 100.00 100.00 4.63e-127 GB EAK91153 "hypothetical protein CaO19.12663 [Candida albicans SC5314]" 98.33 177 100.00 100.00 4.63e-127 GB EEQ42732 "peptidyl-prolyl cis-trans isomerase 1 [Candida albicans WO-1]" 98.33 177 100.00 100.00 4.63e-127 GB KGQ91706 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Candida albicans P94015]" 98.33 177 100.00 100.00 4.63e-127 REF XP_002417086 "peptidyl prolyl cis/trans isomerase, putative [Candida dubliniensis CD36]" 98.33 177 97.18 98.31 7.84e-124 REF XP_710404 "hypothetical protein CaO19.5196 [Candida albicans SC5314]" 98.33 177 100.00 100.00 4.63e-127 REF XP_710415 "hypothetical protein CaO19.12663 [Candida albicans SC5314]" 98.33 177 100.00 100.00 4.63e-127 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $entity 'Candida albicans' 5476 Eukaryota Fungi Candida albicans ESS1 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 $entity 'recombinant technology' . Escherichia coli K-12 BL21(DE3) pET28a 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 $entity 0.5 mM '[U-13C; U-15N]' H2O 93 % 'natural abundance' D2O 7 % '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 processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '50 mM potassium phosphate + 5 mM dithiothreitol-d10' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 0.005 M pH 6.5 0.1 pH pressure 1 . atm temperature 298 0.1 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' '3D HNCACB' 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 'C. albicans Ess1 prolyl isomerase' _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 4 MET H H 8.299 0.01 1 2 1 4 MET C C 175.69 0.1 1 3 1 4 MET CA C 55.2 0.1 1 4 1 4 MET CB C 32.68 0.1 1 5 1 4 MET N N 121.79 0.2 1 6 2 5 ALA H H 8.425 0.01 1 7 2 5 ALA C C 178.31 0.1 1 8 2 5 ALA CA C 52.35 0.1 1 9 2 5 ALA CB C 19.11 0.1 1 10 2 5 ALA N N 125.49 0.2 1 11 3 6 SER H H 8.5 0.01 1 12 3 6 SER C C 175.24 0.1 1 13 3 6 SER CA C 59.34 0.1 1 14 3 6 SER CB C 63.9 0.1 1 15 3 6 SER N N 116.28 0.2 1 16 4 7 THR H H 7.739 0.01 1 17 4 7 THR C C 173.72 0.1 1 18 4 7 THR CA C 61.11 0.1 1 19 4 7 THR CB C 68.72 0.1 1 20 4 7 THR N N 109.27 0.2 1 21 5 8 SER H H 7.674 0.01 1 22 5 8 SER C C 173.7 0.1 1 23 5 8 SER CA C 59.22 0.1 1 24 5 8 SER CB C 63.62 0.1 1 25 5 8 SER N N 116.29 0.2 1 26 6 9 THR H H 8.339 0.01 1 27 6 9 THR C C 174.05 0.1 1 28 6 9 THR CA C 62.21 0.1 1 29 6 9 THR CB C 70.57 0.1 1 30 6 9 THR N N 113.34 0.2 1 31 7 10 GLY H H 7.401 0.01 1 32 7 10 GLY C C 175.25 0.1 1 33 7 10 GLY CA C 45.14 0.1 1 34 7 10 GLY N N 103.75 0.2 1 35 8 11 LEU H H 7.77 0.01 1 36 8 11 LEU C C 174.28 0.1 1 37 8 11 LEU CA C 53.64 0.1 1 38 8 11 LEU CB C 40.88 0.1 1 39 8 11 LEU N N 121.48 0.2 1 40 10 13 PRO C C 176.93 0.1 1 41 10 13 PRO CA C 64.35 0.1 1 42 10 13 PRO CB C 31.96 0.1 1 43 11 14 ASN H H 8.578 0.01 1 44 11 14 ASN C C 173.72 0.1 1 45 11 14 ASN CA C 56.07 0.1 1 46 11 14 ASN CB C 37.74 0.1 1 47 11 14 ASN N N 112.62 0.2 1 48 12 15 TRP H H 7.519 0.01 1 49 12 15 TRP C C 175.82 0.1 1 50 12 15 TRP CA C 56.9 0.1 1 51 12 15 TRP CB C 31.7 0.1 1 52 12 15 TRP N N 118.01 0.2 1 53 13 16 THR H H 9.368 0.01 1 54 13 16 THR C C 171.72 0.1 1 55 13 16 THR CA C 58.85 0.1 1 56 13 16 THR CB C 70.64 0.1 1 57 13 16 THR N N 116.27 0.2 1 58 14 17 ILE H H 7.479 0.01 1 59 14 17 ILE C C 174.4 0.1 1 60 14 17 ILE CA C 59.86 0.1 1 61 14 17 ILE CB C 41 0.1 1 62 14 17 ILE N N 122.4 0.2 1 63 15 18 ARG H H 8.238 0.01 1 64 15 18 ARG C C 173.44 0.1 1 65 15 18 ARG CA C 51.84 0.1 1 66 15 18 ARG CB C 34 0.1 1 67 15 18 ARG N N 126.63 0.2 1 68 16 19 VAL H H 8.159 0.01 1 69 16 19 VAL C C 176.12 0.1 1 70 16 19 VAL CA C 61.63 0.1 1 71 16 19 VAL CB C 34.4 0.1 1 72 16 19 VAL N N 116.2 0.2 1 73 17 20 SER H H 8.86 0.01 1 74 17 20 SER CA C 56.58 0.1 1 75 17 20 SER CB C 63.19 0.1 1 76 17 20 SER N N 121.8 0.2 1 77 20 23 HIS C C 174.21 0.1 1 78 20 23 HIS CA C 56.52 0.1 1 79 20 23 HIS CB C 30.59 0.1 1 80 21 24 ASN H H 7.915 0.01 1 81 21 24 ASN C C 173.49 0.1 1 82 21 24 ASN CA C 53.77 0.1 1 83 21 24 ASN CB C 37.13 0.1 1 84 21 24 ASN N N 118.44 0.2 1 85 22 25 LYS H H 7.397 0.01 1 86 22 25 LYS C C 174 0.1 1 87 22 25 LYS CA C 56.12 0.1 1 88 22 25 LYS CB C 36.67 0.1 1 89 22 25 LYS N N 115.52 0.2 1 90 23 26 GLU H H 10.171 0.01 1 91 23 26 GLU C C 173.32 0.1 1 92 23 26 GLU CA C 56.13 0.1 1 93 23 26 GLU CB C 28.92 0.1 1 94 23 26 GLU N N 127.28 0.2 1 95 24 27 TYR H H 8.494 0.01 1 96 24 27 TYR C C 170.53 0.1 1 97 24 27 TYR CA C 55.19 0.1 1 98 24 27 TYR CB C 38.27 0.1 1 99 24 27 TYR N N 116.29 0.2 1 100 25 28 PHE H H 8.475 0.01 1 101 25 28 PHE C C 173.79 0.1 1 102 25 28 PHE CA C 56.56 0.1 1 103 25 28 PHE CB C 40.97 0.1 1 104 25 28 PHE N N 117.25 0.2 1 105 26 29 LEU H H 8.531 0.01 1 106 26 29 LEU C C 173.83 0.1 1 107 26 29 LEU CA C 53.07 0.1 1 108 26 29 LEU CB C 47.12 0.1 1 109 26 29 LEU N N 124.9 0.2 1 110 27 30 ASN H H 8.392 0.01 1 111 27 30 ASN C C 176.08 0.1 1 112 27 30 ASN CA C 50.9 0.1 1 113 27 30 ASN CB C 36.86 0.1 1 114 27 30 ASN N N 127.63 0.2 1 115 28 31 GLN H H 8.933 0.01 1 116 28 31 GLN C C 176.1 0.1 1 117 28 31 GLN CA C 59.25 0.1 1 118 28 31 GLN CB C 31.11 0.1 1 119 28 31 GLN N N 122.06 0.2 1 120 29 32 SER H H 8.246 0.01 1 121 29 32 SER C C 176.11 0.1 1 122 29 32 SER CA C 59.75 0.1 1 123 29 32 SER CB C 64.47 0.1 1 124 29 32 SER N N 111.48 0.2 1 125 30 33 THR H H 7.011 0.01 1 126 30 33 THR C C 176.1 0.1 1 127 30 33 THR CA C 60.75 0.1 1 128 30 33 THR CB C 70.58 0.1 1 129 30 33 THR N N 107.15 0.2 1 130 31 34 ASN H H 8.257 0.01 1 131 31 34 ASN C C 173.99 0.1 1 132 31 34 ASN CA C 55.15 0.1 1 133 31 34 ASN CB C 37.69 0.1 1 134 31 34 ASN N N 117.17 0.2 1 135 32 35 GLU H H 7.442 0.01 1 136 32 35 GLU C C 174.31 0.1 1 137 32 35 GLU CA C 56.6 0.1 1 138 32 35 GLU CB C 31.17 0.1 1 139 32 35 GLU N N 119.2 0.2 1 140 33 36 SER H H 8.353 0.01 1 141 33 36 SER C C 174.25 0.1 1 142 33 36 SER CA C 56.45 0.1 1 143 33 36 SER CB C 66.34 0.1 1 144 33 36 SER N N 116.57 0.2 1 145 34 37 SER H H 9.245 0.01 1 146 34 37 SER C C 174.62 0.1 1 147 34 37 SER CA C 56.61 0.1 1 148 34 37 SER CB C 65.82 0.1 1 149 34 37 SER N N 115.13 0.2 1 150 35 38 TRP H H 8.747 0.01 1 151 35 38 TRP C C 176.14 0.1 1 152 35 38 TRP CA C 58.87 0.1 1 153 35 38 TRP CB C 29.81 0.1 1 154 35 38 TRP N N 125.49 0.2 1 155 36 39 ASP H H 7.999 0.01 1 156 36 39 ASP C C 173.18 0.1 1 157 36 39 ASP CA C 51.23 0.1 1 158 36 39 ASP CB C 41.5 0.1 1 159 36 39 ASP N N 117.03 0.2 1 160 38 41 PRO C C 177.37 0.1 1 161 38 41 PRO CA C 60.76 0.1 1 162 38 41 PRO CB C 31.99 0.1 1 163 39 42 TYR H H 8.584 0.01 1 164 39 42 TYR C C 175.77 0.1 1 165 39 42 TYR CA C 60.35 0.1 1 166 39 42 TYR CB C 37.72 0.1 1 167 39 42 TYR N N 123.38 0.2 1 168 40 43 GLY H H 7.98 0.01 1 169 40 43 GLY C C 174.83 0.1 1 170 40 43 GLY CA C 43.84 0.1 1 171 40 43 GLY N N 114.24 0.2 1 172 41 44 THR H H 7.148 0.01 1 173 41 44 THR C C 173.82 0.1 1 174 41 44 THR CA C 64.51 0.1 1 175 41 44 THR CB C 69.58 0.1 1 176 41 44 THR N N 118.69 0.2 1 177 42 45 ASP H H 8.528 0.01 1 178 42 45 ASP C C 175.2 0.1 1 179 42 45 ASP CA C 53.19 0.1 1 180 42 45 ASP CB C 39.58 0.1 1 181 42 45 ASP N N 127.03 0.2 1 182 43 46 LYS H H 8.337 0.01 1 183 43 46 LYS C C 177.71 0.1 1 184 43 46 LYS CA C 59.75 0.1 1 185 43 46 LYS CB C 31.96 0.1 1 186 43 46 LYS N N 126.04 0.2 1 187 44 47 GLU H H 8.044 0.01 1 188 44 47 GLU C C 179.99 0.1 1 189 44 47 GLU CA C 59.39 0.1 1 190 44 47 GLU CB C 28.91 0.1 1 191 44 47 GLU N N 118.28 0.2 1 192 45 48 VAL H H 7.201 0.01 1 193 45 48 VAL C C 178.88 0.1 1 194 45 48 VAL CA C 66.29 0.1 1 195 45 48 VAL CB C 32.6 0.1 1 196 45 48 VAL N N 122.29 0.2 1 197 46 49 LEU H H 8.34 0.01 1 198 46 49 LEU C C 178.95 0.1 1 199 46 49 LEU CA C 58.01 0.1 1 200 46 49 LEU CB C 41.09 0.1 1 201 46 49 LEU N N 122.54 0.2 1 202 47 50 ASN H H 8.659 0.01 1 203 47 50 ASN C C 179.24 0.1 1 204 47 50 ASN CA C 56.11 0.1 1 205 47 50 ASN CB C 37.36 0.1 1 206 47 50 ASN N N 116.88 0.2 1 207 48 51 ALA H H 7.232 0.01 1 208 48 51 ALA C C 179.25 0.1 1 209 48 51 ALA CA C 54.97 0.1 1 210 48 51 ALA CB C 17.99 0.1 1 211 48 51 ALA N N 121.84 0.2 1 212 49 52 TYR H H 8.211 0.01 1 213 49 52 TYR C C 178.2 0.1 1 214 49 52 TYR CA C 62.17 0.1 1 215 49 52 TYR CB C 38.74 0.1 1 216 49 52 TYR N N 121.37 0.2 1 217 50 53 ILE H H 9.437 0.01 1 218 50 53 ILE C C 177.66 0.1 1 219 50 53 ILE CA C 63.51 0.1 1 220 50 53 ILE CB C 36.41 0.1 1 221 50 53 ILE N N 118.19 0.2 1 222 51 54 ALA H H 7.558 0.01 1 223 51 54 ALA C C 180.61 0.1 1 224 51 54 ALA CA C 55.49 0.1 1 225 51 54 ALA CB C 17.94 0.1 1 226 51 54 ALA N N 120.78 0.2 1 227 52 55 LYS H H 7.183 0.01 1 228 52 55 LYS C C 178.9 0.1 1 229 52 55 LYS CA C 59.36 0.1 1 230 52 55 LYS CB C 33.11 0.1 1 231 52 55 LYS N N 116.88 0.2 1 232 53 56 PHE H H 9.141 0.01 1 233 53 56 PHE C C 177.65 0.1 1 234 53 56 PHE CA C 59.67 0.1 1 235 53 56 PHE CB C 40.08 0.1 1 236 53 56 PHE N N 124.18 0.2 1 237 54 57 LYS H H 8.439 0.01 1 238 54 57 LYS C C 178.69 0.1 1 239 54 57 LYS CA C 59.37 0.1 1 240 54 57 LYS CB C 32 0.1 1 241 54 57 LYS N N 119.15 0.2 1 242 55 58 ASN H H 7.138 0.01 1 243 55 58 ASN C C 174.84 0.1 1 244 55 58 ASN CA C 54.61 0.1 1 245 55 58 ASN CB C 38.73 0.1 1 246 55 58 ASN N N 116.84 0.2 1 247 56 59 ASN H H 7.516 0.01 1 248 56 59 ASN C C 176.42 0.1 1 249 56 59 ASN CA C 52.19 0.1 1 250 56 59 ASN CB C 39.96 0.1 1 251 56 59 ASN N N 118.65 0.2 1 252 57 60 GLY H H 7.693 0.01 1 253 57 60 GLY C C 174.46 0.1 1 254 57 60 GLY CA C 46.29 0.1 1 255 57 60 GLY N N 107.48 0.2 1 256 58 61 TYR H H 7.474 0.01 1 257 58 61 TYR C C 174.36 0.1 1 258 58 61 TYR CA C 58.26 0.1 1 259 58 61 TYR CB C 33.39 0.1 1 260 58 61 TYR N N 111.49 0.2 1 261 59 62 LYS H H 6.854 0.01 1 262 59 62 LYS CA C 52.33 0.1 1 263 59 62 LYS CB C 32.55 0.1 1 264 59 62 LYS N N 118.15 0.2 1 265 60 63 PRO C C 175.33 0.1 1 266 60 63 PRO CA C 63.47 0.1 1 267 60 63 PRO CB C 32.99 0.1 1 268 61 64 LEU H H 7.05 0.01 1 269 61 64 LEU C C 176.65 0.1 1 270 61 64 LEU CA C 55.1 0.1 1 271 61 64 LEU CB C 41.43 0.1 1 272 61 64 LEU N N 119.54 0.2 1 273 62 65 VAL H H 8.139 0.01 1 274 62 65 VAL C C 174.91 0.1 1 275 62 65 VAL CA C 60.26 0.1 1 276 62 65 VAL CB C 34.56 0.1 1 277 62 65 VAL N N 115.41 0.2 1 278 63 66 ASN H H 8.279 0.01 1 279 63 66 ASN C C 176.82 0.1 1 280 63 66 ASN CA C 52.32 0.1 1 281 63 66 ASN CB C 37.82 0.1 1 282 63 66 ASN N N 119.61 0.2 1 283 64 67 GLU H H 9.057 0.01 1 284 64 67 GLU C C 176.78 0.1 1 285 64 67 GLU CA C 59.39 0.1 1 286 64 67 GLU CB C 28.79 0.1 1 287 64 67 GLU N N 118.29 0.2 1 288 65 68 ASP H H 7.448 0.01 1 289 65 68 ASP C C 176.49 0.1 1 290 65 68 ASP CA C 53.77 0.1 1 291 65 68 ASP CB C 40.97 0.1 1 292 65 68 ASP N N 116.74 0.2 1 293 66 69 GLY H H 8.343 0.01 1 294 66 69 GLY C C 174.18 0.1 1 295 66 69 GLY CA C 46.09 0.1 1 296 66 69 GLY N N 109.36 0.2 1 297 67 70 GLN H H 7.524 0.01 1 298 67 70 GLN C C 175.06 0.1 1 299 67 70 GLN CA C 55 0.1 1 300 67 70 GLN CB C 32.89 0.1 1 301 67 70 GLN N N 116.3 0.2 1 302 68 71 VAL H H 7.421 0.01 1 303 68 71 VAL C C 171.35 0.1 1 304 68 71 VAL CA C 59.25 0.1 1 305 68 71 VAL CB C 35.25 0.1 1 306 68 71 VAL N N 110.49 0.2 1 307 69 72 ARG H H 7.701 0.01 1 308 69 72 ARG C C 176.25 0.1 1 309 69 72 ARG CA C 53.68 0.1 1 310 69 72 ARG CB C 31.72 0.1 1 311 69 72 ARG N N 121.65 0.2 1 312 70 73 VAL H H 6.812 0.01 1 313 70 73 VAL C C 174.32 0.1 1 314 70 73 VAL CA C 58.27 0.1 1 315 70 73 VAL CB C 35.88 0.1 1 316 70 73 VAL N N 115.5 0.2 1 317 71 74 SER H H 8.594 0.01 1 318 71 74 SER C C 173.04 0.1 1 319 71 74 SER CA C 56.58 0.1 1 320 71 74 SER CB C 65.83 0.1 1 321 71 74 SER N N 116.42 0.2 1 322 72 75 HIS H H 9.322 0.01 1 323 72 75 HIS C C 171.55 0.1 1 324 72 75 HIS CA C 53.59 0.1 1 325 72 75 HIS CB C 37.81 0.1 1 326 72 75 HIS N N 120.78 0.2 1 327 73 76 LEU H H 8.616 0.01 1 328 73 76 LEU C C 172.68 0.1 1 329 73 76 LEU CA C 55.04 0.1 1 330 73 76 LEU CB C 45.74 0.1 1 331 73 76 LEU N N 124.55 0.2 1 332 74 77 LEU H H 7.447 0.01 1 333 74 77 LEU C C 173.96 0.1 1 334 74 77 LEU CA C 52.28 0.1 1 335 74 77 LEU CB C 45.33 0.1 1 336 74 77 LEU N N 126.56 0.2 1 337 75 78 ILE H H 9.192 0.01 1 338 75 78 ILE C C 175.94 0.1 1 339 75 78 ILE CA C 58.31 0.1 1 340 75 78 ILE CB C 36.37 0.1 1 341 75 78 ILE N N 127.34 0.2 1 342 76 79 LYS H H 8.922 0.01 1 343 76 79 LYS C C 175.17 0.1 1 344 76 79 LYS CA C 56.91 0.1 1 345 76 79 LYS CB C 36.39 0.1 1 346 76 79 LYS N N 124.01 0.2 1 347 77 80 ASN H H 9.027 0.01 1 348 77 80 ASN C C 174.71 0.1 1 349 77 80 ASN CA C 52.65 0.1 1 350 77 80 ASN CB C 41.08 0.1 1 351 77 80 ASN N N 113.95 0.2 1 352 78 81 ASN H H 8.963 0.01 1 353 78 81 ASN C C 176.31 0.1 1 354 78 81 ASN CA C 55.04 0.1 1 355 78 81 ASN CB C 36.88 0.1 1 356 78 81 ASN N N 114.96 0.2 1 357 79 82 GLN H H 8.837 0.01 1 358 79 82 GLN C C 176.3 0.1 1 359 79 82 GLN CA C 55.08 0.1 1 360 79 82 GLN CB C 29.17 0.1 1 361 79 82 GLN N N 118.66 0.2 1 362 80 83 SER H H 7.846 0.01 1 363 80 83 SER C C 173.63 0.1 1 364 80 83 SER CA C 61.68 0.1 1 365 80 83 SER CB C 64.05 0.1 1 366 80 83 SER N N 120.82 0.2 1 367 81 84 ARG H H 8.426 0.01 1 368 81 84 ARG C C 176.56 0.1 1 369 81 84 ARG CA C 58.49 0.1 1 370 81 84 ARG CB C 28.88 0.1 1 371 81 84 ARG N N 121.59 0.2 1 372 82 85 LYS H H 8.231 0.01 1 373 82 85 LYS C C 174.3 0.1 1 374 82 85 LYS CA C 53.17 0.1 1 375 82 85 LYS CB C 33.15 0.1 1 376 82 85 LYS N N 119.41 0.2 1 377 83 86 PRO C C 173.44 0.1 1 378 83 86 PRO CA C 63.11 0.1 1 379 83 86 PRO CB C 27.42 0.1 1 380 84 87 LYS H H 8.982 0.01 1 381 84 87 LYS C C 173.26 0.1 1 382 84 87 LYS CA C 56.56 0.1 1 383 84 87 LYS CB C 35.02 0.1 1 384 84 87 LYS N N 122.17 0.2 1 385 85 88 SER H H 7.46 0.01 1 386 85 88 SER C C 174.74 0.1 1 387 85 88 SER CA C 57.4 0.1 1 388 85 88 SER CB C 68.6 0.1 1 389 85 88 SER N N 113.8 0.2 1 390 86 89 TRP H H 8.76 0.01 1 391 86 89 TRP C C 175.65 0.1 1 392 86 89 TRP CA C 58.38 0.1 1 393 86 89 TRP CB C 26.92 0.1 1 394 86 89 TRP N N 119.43 0.2 1 395 87 90 LYS H H 5.635 0.01 1 396 87 90 LYS C C 175.65 0.1 1 397 87 90 LYS CA C 55.16 0.1 1 398 87 90 LYS CB C 29.73 0.1 1 399 87 90 LYS N N 116.93 0.2 1 400 88 91 SER H H 6.818 0.01 1 401 88 91 SER C C 173.68 0.1 1 402 88 91 SER CB C 64.56 0.1 1 403 88 91 SER N N 118.6 0.2 1 404 89 92 PRO C C 177.38 0.1 1 405 89 92 PRO CA C 64.89 0.1 1 406 89 92 PRO CB C 31.66 0.1 1 407 90 93 ASP H H 8.375 0.01 1 408 90 93 ASP C C 176 0.1 1 409 90 93 ASP CA C 53.78 0.1 1 410 90 93 ASP CB C 40.87 0.1 1 411 90 93 ASP N N 116.03 0.2 1 412 91 94 GLY H H 7.128 0.01 1 413 91 94 GLY C C 172.85 0.1 1 414 91 94 GLY CA C 43.86 0.1 1 415 91 94 GLY N N 106.96 0.2 1 416 92 95 ILE H H 7.576 0.01 1 417 92 95 ILE C C 174.5 0.1 1 418 92 95 ILE CA C 60.65 0.1 1 419 92 95 ILE CB C 39.99 0.1 1 420 92 95 ILE N N 122.28 0.2 1 421 93 96 SER H H 8.412 0.01 1 422 93 96 SER C C 174.65 0.1 1 423 93 96 SER CA C 57.47 0.1 1 424 93 96 SER CB C 64.53 0.1 1 425 93 96 SER N N 121.07 0.2 1 426 94 97 ARG H H 7.145 0.01 1 427 94 97 ARG C C 174.23 0.1 1 428 94 97 ARG CA C 55.69 0.1 1 429 94 97 ARG CB C 31.1 0.1 1 430 94 97 ARG N N 123.69 0.2 1 431 95 98 THR H H 8.878 0.01 1 432 95 98 THR C C 176.04 0.1 1 433 95 98 THR CA C 60.75 0.1 1 434 95 98 THR CB C 71.39 0.1 1 435 95 98 THR N N 114.45 0.2 1 436 96 99 ARG H H 9.441 0.01 1 437 96 99 ARG C C 180.07 0.1 1 438 96 99 ARG CA C 59.41 0.1 1 439 96 99 ARG CB C 29.32 0.1 1 440 96 99 ARG N N 122.75 0.2 1 441 97 100 ASP H H 8.933 0.01 1 442 97 100 ASP C C 178.77 0.1 1 443 97 100 ASP CA C 58 0.1 1 444 97 100 ASP CB C 40.03 0.1 1 445 97 100 ASP N N 120.43 0.2 1 446 98 101 GLU H H 7.862 0.01 1 447 98 101 GLU C C 179.38 0.1 1 448 98 101 GLU CA C 59.65 0.1 1 449 98 101 GLU CB C 29.65 0.1 1 450 98 101 GLU N N 120.28 0.2 1 451 99 102 SER H H 8.534 0.01 1 452 99 102 SER C C 174.54 0.1 1 453 99 102 SER CA C 61.88 0.1 1 454 99 102 SER CB C 63.05 0.1 1 455 99 102 SER N N 114.28 0.2 1 456 100 103 ILE H H 7.517 0.01 1 457 100 103 ILE C C 176.78 0.1 1 458 100 103 ILE CA C 66.28 0.1 1 459 100 103 ILE CB C 38.16 0.1 1 460 100 103 ILE N N 123.6 0.2 1 461 101 104 GLN H H 7.752 0.01 1 462 101 104 GLN C C 179.49 0.1 1 463 101 104 GLN CA C 59.28 0.1 1 464 101 104 GLN CB C 27.93 0.1 1 465 101 104 GLN N N 119.04 0.2 1 466 102 105 ILE H H 7.974 0.01 1 467 102 105 ILE C C 177.72 0.1 1 468 102 105 ILE CA C 64.8 0.1 1 469 102 105 ILE CB C 39.2 0.1 1 470 102 105 ILE N N 119.2 0.2 1 471 103 106 LEU H H 7.849 0.01 1 472 103 106 LEU C C 178.25 0.1 1 473 103 106 LEU CA C 57.41 0.1 1 474 103 106 LEU CB C 41.93 0.1 1 475 103 106 LEU N N 119.92 0.2 1 476 104 107 LYS H H 8.79 0.01 1 477 104 107 LYS C C 179.31 0.1 1 478 104 107 LYS CA C 60.34 0.1 1 479 104 107 LYS CB C 32.51 0.1 1 480 104 107 LYS N N 119.09 0.2 1 481 105 108 LYS H H 6.993 0.01 1 482 105 108 LYS C C 179.33 0.1 1 483 105 108 LYS CA C 58.39 0.1 1 484 105 108 LYS CB C 30.76 0.1 1 485 105 108 LYS N N 118.75 0.2 1 486 106 109 HIS H H 7.373 0.01 1 487 106 109 HIS C C 177.97 0.1 1 488 106 109 HIS CA C 58.16 0.1 1 489 106 109 HIS CB C 30.45 0.1 1 490 106 109 HIS N N 118.61 0.2 1 491 107 110 LEU H H 8.76 0.01 1 492 107 110 LEU C C 177.74 0.1 1 493 107 110 LEU CA C 58.27 0.1 1 494 107 110 LEU CB C 41.44 0.1 1 495 107 110 LEU N N 119.43 0.2 1 496 108 111 GLU H H 7.728 0.01 1 497 108 111 GLU C C 179.71 0.1 1 498 108 111 GLU CA C 59.63 0.1 1 499 108 111 GLU CB C 29.65 0.1 1 500 108 111 GLU N N 116.89 0.2 1 501 109 112 ARG H H 7.571 0.01 1 502 109 112 ARG C C 178.68 0.1 1 503 109 112 ARG CA C 59.63 0.1 1 504 109 112 ARG CB C 30.66 0.1 1 505 109 112 ARG N N 118.92 0.2 1 506 110 113 ILE H H 8.181 0.01 1 507 110 113 ILE C C 180.77 0.1 1 508 110 113 ILE CA C 63.57 0.1 1 509 110 113 ILE CB C 39.09 0.1 1 510 110 113 ILE N N 121.13 0.2 1 511 111 114 LEU H H 8.88 0.01 1 512 111 114 LEU C C 178.7 0.1 1 513 111 114 LEU CA C 57.78 0.1 1 514 111 114 LEU CB C 40.96 0.1 1 515 111 114 LEU N N 120.46 0.2 1 516 112 115 SER H H 7.768 0.01 1 517 112 115 SER C C 175.69 0.1 1 518 112 115 SER CA C 59.72 0.1 1 519 112 115 SER CB C 63.96 0.1 1 520 112 115 SER N N 111.06 0.2 1 521 113 116 GLY H H 7.668 0.01 1 522 113 116 GLY C C 174.79 0.1 1 523 113 116 GLY CA C 45.14 0.1 1 524 113 116 GLY N N 109.06 0.2 1 525 114 117 GLU H H 8.008 0.01 1 526 114 117 GLU C C 175.93 0.1 1 527 114 117 GLU CA C 58.89 0.1 1 528 114 117 GLU CB C 30.32 0.1 1 529 114 117 GLU N N 121.03 0.2 1 530 115 118 VAL H H 7.145 0.01 1 531 115 118 VAL C C 173.55 0.1 1 532 115 118 VAL CA C 58.89 0.1 1 533 115 118 VAL CB C 35.32 0.1 1 534 115 118 VAL N N 111.51 0.2 1 535 116 119 LYS H H 8.33 0.01 1 536 116 119 LYS C C 177.56 0.1 1 537 116 119 LYS CA C 55.05 0.1 1 538 116 119 LYS CB C 33.6 0.1 1 539 116 119 LYS N N 122.13 0.2 1 540 117 120 LEU H H 9.315 0.01 1 541 117 120 LEU C C 178.62 0.1 1 542 117 120 LEU CA C 60.75 0.1 1 543 117 120 LEU CB C 41.09 0.1 1 544 117 120 LEU N N 125.44 0.2 1 545 118 121 SER H H 8.602 0.01 1 546 118 121 SER C C 175.9 0.1 1 547 118 121 SER CA C 60.7 0.1 1 548 118 121 SER CB C 62.52 0.1 1 549 118 121 SER N N 112.33 0.2 1 550 119 122 GLU H H 6.524 0.01 1 551 119 122 GLU C C 179.29 0.1 1 552 119 122 GLU CA C 58.28 0.1 1 553 119 122 GLU CB C 29.76 0.1 1 554 119 122 GLU N N 120.48 0.2 1 555 120 123 LEU H H 7.542 0.01 1 556 120 123 LEU C C 178.6 0.1 1 557 120 123 LEU CA C 56.55 0.1 1 558 120 123 LEU CB C 42.86 0.1 1 559 120 123 LEU N N 119.4 0.2 1 560 121 124 ALA H H 9.017 0.01 1 561 121 124 ALA C C 178.44 0.1 1 562 121 124 ALA CA C 55.11 0.1 1 563 121 124 ALA CB C 17.03 0.1 1 564 121 124 ALA N N 120.23 0.2 1 565 122 125 ASN H H 7.118 0.01 1 566 122 125 ASN C C 177.12 0.1 1 567 122 125 ASN CA C 56.41 0.1 1 568 122 125 ASN CB C 39.71 0.1 1 569 122 125 ASN N N 110.88 0.2 1 570 123 126 THR H H 6.951 0.01 1 571 123 126 THR C C 176.09 0.1 1 572 123 126 THR CA C 62.18 0.1 1 573 123 126 THR CB C 69.54 0.1 1 574 123 126 THR N N 102.49 0.2 1 575 124 127 GLU H H 8.298 0.01 1 576 124 127 GLU C C 176.17 0.1 1 577 124 127 GLU CA C 55.54 0.1 1 578 124 127 GLU CB C 30.64 0.1 1 579 124 127 GLU N N 115.54 0.2 1 580 125 128 SER H H 7.644 0.01 1 581 125 128 SER C C 175.82 0.1 1 582 125 128 SER CA C 56.52 0.1 1 583 125 128 SER CB C 66.23 0.1 1 584 125 128 SER N N 108.44 0.2 1 585 126 129 ASP H H 9.474 0.01 1 586 126 129 ASP C C 174.44 0.1 1 587 126 129 ASP CA C 56.86 0.1 1 588 126 129 ASP CB C 44.18 0.1 1 589 126 129 ASP N N 124.13 0.2 1 590 127 130 CYS H H 7.931 0.01 1 591 127 130 CYS C C 176.64 0.1 1 592 127 130 CYS CA C 60.55 0.1 1 593 127 130 CYS CB C 28.82 0.1 1 594 127 130 CYS N N 122.34 0.2 1 595 128 131 SER H H 8.793 0.01 1 596 128 131 SER C C 175.11 0.1 1 597 128 131 SER CA C 62.58 0.1 1 598 128 131 SER N N 127.62 0.2 1 599 129 132 SER H H 9.714 0.01 1 600 129 132 SER C C 177.58 0.1 1 601 129 132 SER CA C 60.7 0.1 1 602 129 132 SER CB C 63.55 0.1 1 603 129 132 SER N N 120.09 0.2 1 604 130 133 HIS H H 8.246 0.01 1 605 130 133 HIS C C 174.06 0.1 1 606 130 133 HIS CA C 59.34 0.1 1 607 130 133 HIS CB C 26 0.1 1 608 130 133 HIS N N 125.7 0.2 1 609 131 134 ASP H H 6.388 0.01 1 610 131 134 ASP C C 176.21 0.1 1 611 131 134 ASP CA C 54.53 0.1 1 612 131 134 ASP CB C 39.1 0.1 1 613 131 134 ASP N N 116.82 0.2 1 614 132 135 ARG H H 7.511 0.01 1 615 132 135 ARG C C 177.97 0.1 1 616 132 135 ARG CA C 54.03 0.1 1 617 132 135 ARG CB C 29.36 0.1 1 618 132 135 ARG N N 119.3 0.2 1 619 133 136 GLY H H 8 0.01 1 620 133 136 GLY C C 174.32 0.1 1 621 133 136 GLY CA C 47.24 0.1 1 622 133 136 GLY N N 111.16 0.2 1 623 134 137 GLY H H 7.708 0.01 1 624 134 137 GLY C C 173.92 0.1 1 625 134 137 GLY CA C 44.74 0.1 1 626 134 137 GLY N N 102.95 0.2 1 627 135 138 ASP H H 6.882 0.01 1 628 135 138 ASP C C 175.5 0.1 1 629 135 138 ASP CB C 42 0.1 1 630 135 138 ASP N N 117.56 0.2 1 631 136 139 LEU H H 8.428 0.01 1 632 136 139 LEU C C 178.44 0.1 1 633 136 139 LEU CA C 53.75 0.1 1 634 136 139 LEU CB C 42.99 0.1 1 635 136 139 LEU N N 125.89 0.2 1 636 137 140 GLY H H 8.153 0.01 1 637 137 140 GLY C C 171.47 0.1 1 638 137 140 GLY CA C 44.41 0.1 1 639 137 140 GLY N N 108.05 0.2 1 640 138 141 PHE H H 8.145 0.01 1 641 138 141 PHE C C 178.28 0.1 1 642 138 141 PHE CA C 58.33 0.1 1 643 138 141 PHE CB C 40.08 0.1 1 644 138 141 PHE N N 114.89 0.2 1 645 139 142 PHE H H 8.828 0.01 1 646 139 142 PHE C C 172.92 0.1 1 647 139 142 PHE CA C 56.14 0.1 1 648 139 142 PHE CB C 41.38 0.1 1 649 139 142 PHE N N 117.96 0.2 1 650 140 143 SER H H 8.465 0.01 1 651 140 143 SER C C 175.54 0.1 1 652 140 143 SER CA C 56.95 0.1 1 653 140 143 SER CB C 66.28 0.1 1 654 140 143 SER N N 113.53 0.2 1 655 141 144 LYS H H 8.891 0.01 1 656 141 144 LYS C C 177.67 0.1 1 657 141 144 LYS CA C 58.9 0.1 1 658 141 144 LYS CB C 32.06 0.1 1 659 141 144 LYS N N 122.49 0.2 1 660 142 145 GLY H H 10.292 0.01 1 661 142 145 GLY C C 174.43 0.1 1 662 142 145 GLY CA C 45.2 0.1 1 663 142 145 GLY N N 113.53 0.2 1 664 143 146 GLN H H 7.592 0.01 1 665 143 146 GLN C C 176.45 0.1 1 666 143 146 GLN CA C 57.97 0.1 1 667 143 146 GLN CB C 31.53 0.1 1 668 143 146 GLN N N 118.21 0.2 1 669 144 147 MET H H 9.04 0.01 1 670 144 147 MET C C 175.46 0.1 1 671 144 147 MET CA C 52.24 0.1 1 672 144 147 MET CB C 32.97 0.1 1 673 144 147 MET N N 117.51 0.2 1 674 145 148 GLN H H 8.463 0.01 1 675 145 148 GLN C C 178.67 0.1 1 676 145 148 GLN CA C 55.21 0.1 1 677 145 148 GLN CB C 28.73 0.1 1 678 145 148 GLN N N 118.96 0.2 1 679 147 150 PRO C C 179.56 0.1 1 680 147 150 PRO CA C 65.78 0.1 1 681 147 150 PRO CB C 31.13 0.1 1 682 148 151 PHE H H 7.091 0.01 1 683 148 151 PHE C C 175.98 0.1 1 684 148 151 PHE CA C 60.73 0.1 1 685 148 151 PHE CB C 40.58 0.1 1 686 148 151 PHE N N 117.14 0.2 1 687 149 152 GLU H H 8.211 0.01 1 688 149 152 GLU C C 177.21 0.1 1 689 149 152 GLU CA C 60.35 0.1 1 690 149 152 GLU CB C 30.7 0.1 1 691 149 152 GLU N N 118.67 0.2 1 692 150 153 GLU H H 8.443 0.01 1 693 150 153 GLU C C 178.39 0.1 1 694 150 153 GLU CA C 58.9 0.1 1 695 150 153 GLU CB C 29.34 0.1 1 696 150 153 GLU N N 116.99 0.2 1 697 151 154 ALA H H 6.884 0.01 1 698 151 154 ALA C C 179.95 0.1 1 699 151 154 ALA CA C 54.27 0.1 1 700 151 154 ALA CB C 19.01 0.1 1 701 151 154 ALA N N 117.26 0.2 1 702 152 155 ALA H H 8.203 0.01 1 703 152 155 ALA C C 177.9 0.1 1 704 152 155 ALA CA C 55.55 0.1 1 705 152 155 ALA CB C 19.46 0.1 1 706 152 155 ALA N N 118.67 0.2 1 707 153 156 PHE H H 7.967 0.01 1 708 153 156 PHE C C 175.36 0.1 1 709 153 156 PHE CA C 60.62 0.1 1 710 153 156 PHE CB C 38.26 0.1 1 711 153 156 PHE N N 109.5 0.2 1 712 154 157 ASN H H 7.114 0.01 1 713 154 157 ASN C C 174.56 0.1 1 714 154 157 ASN CA C 52.75 0.1 1 715 154 157 ASN CB C 39.66 0.1 1 716 154 157 ASN N N 115.18 0.2 1 717 155 158 LEU H H 6.904 0.01 1 718 155 158 LEU C C 176.3 0.1 1 719 155 158 LEU CA C 53.71 0.1 1 720 155 158 LEU CB C 44.13 0.1 1 721 155 158 LEU N N 121.13 0.2 1 722 156 159 HIS H H 7.872 0.01 1 723 156 159 HIS C C 176.32 0.1 1 724 156 159 HIS CA C 55.89 0.1 1 725 156 159 HIS CB C 31.25 0.1 1 726 156 159 HIS N N 118.91 0.2 1 727 157 160 VAL H H 9.882 0.01 1 728 157 160 VAL C C 176.85 0.1 1 729 157 160 VAL CA C 67.79 0.1 1 730 157 160 VAL CB C 30.25 0.1 1 731 157 160 VAL N N 123.61 0.2 1 732 158 161 GLY H H 8.761 0.01 1 733 158 161 GLY C C 174.28 0.1 1 734 158 161 GLY CA C 44.64 0.1 1 735 158 161 GLY N N 117.26 0.2 1 736 159 162 GLU H H 8.457 0.01 1 737 159 162 GLU C C 174.28 0.1 1 738 159 162 GLU CA C 56.61 0.1 1 739 159 162 GLU CB C 32.08 0.1 1 740 159 162 GLU N N 125.17 0.2 1 741 160 163 VAL H H 8.669 0.01 1 742 160 163 VAL C C 177.18 0.1 1 743 160 163 VAL CA C 60.75 0.1 1 744 160 163 VAL CB C 33.49 0.1 1 745 160 163 VAL N N 126.33 0.2 1 746 161 164 SER H H 9.458 0.01 1 747 161 164 SER C C 172.41 0.1 1 748 161 164 SER CA C 59.31 0.1 1 749 161 164 SER CB C 65.35 0.1 1 750 161 164 SER N N 124.85 0.2 1 751 162 165 ASN H H 7.719 0.01 1 752 162 165 ASN C C 175.46 0.1 1 753 162 165 ASN CA C 52.2 0.1 1 754 162 165 ASN CB C 39.16 0.1 1 755 162 165 ASN N N 112.95 0.2 1 756 163 166 ILE H H 8.472 0.01 1 757 163 166 ILE C C 176.37 0.1 1 758 163 166 ILE CA C 63.52 0.1 1 759 163 166 ILE CB C 37.59 0.1 1 760 163 166 ILE N N 119.61 0.2 1 761 164 167 ILE H H 9.092 0.01 1 762 164 167 ILE C C 174.24 0.1 1 763 164 167 ILE CA C 57.98 0.1 1 764 164 167 ILE CB C 40.49 0.1 1 765 164 167 ILE N N 127.56 0.2 1 766 165 168 GLU H H 8.654 0.01 1 767 165 168 GLU C C 175.54 0.1 1 768 165 168 GLU CA C 55.1 0.1 1 769 165 168 GLU CB C 32.48 0.1 1 770 165 168 GLU N N 126.29 0.2 1 771 166 169 THR H H 9.152 0.01 1 772 166 169 THR C C 175.45 0.1 1 773 166 169 THR CA C 60.6 0.1 1 774 166 169 THR CB C 72.31 0.1 1 775 166 169 THR N N 115.1 0.2 1 776 167 170 ASN H H 9.032 0.01 1 777 167 170 ASN C C 176.9 0.1 1 778 167 170 ASN CA C 55.1 0.1 1 779 167 170 ASN CB C 37.64 0.1 1 780 167 170 ASN N N 116.04 0.2 1 781 168 171 SER H H 9.137 0.01 1 782 168 171 SER C C 174.78 0.1 1 783 168 171 SER CA C 61.53 0.1 1 784 168 171 SER CB C 63.57 0.1 1 785 168 171 SER N N 115.29 0.2 1 786 169 172 GLY H H 7.523 0.01 1 787 169 172 GLY C C 169.69 0.1 1 788 169 172 GLY CA C 44.82 0.1 1 789 169 172 GLY N N 111.79 0.2 1 790 170 173 VAL H H 7.746 0.01 1 791 170 173 VAL C C 174.49 0.1 1 792 170 173 VAL CA C 59.25 0.1 1 793 170 173 VAL CB C 33.13 0.1 1 794 170 173 VAL N N 112.41 0.2 1 795 171 174 HIS H H 9.409 0.01 1 796 171 174 HIS C C 177.22 0.1 1 797 171 174 HIS CA C 53.76 0.1 1 798 171 174 HIS CB C 33.55 0.1 1 799 171 174 HIS N N 117.89 0.2 1 800 172 175 ILE H H 8.051 0.01 1 801 172 175 ILE C C 174.18 0.1 1 802 172 175 ILE CA C 62.03 0.1 1 803 172 175 ILE CB C 41.9 0.1 1 804 172 175 ILE N N 113.55 0.2 1 805 173 176 LEU H H 8.818 0.01 1 806 173 176 LEU C C 175 0.1 1 807 173 176 LEU CA C 54.64 0.1 1 808 173 176 LEU CB C 46.16 0.1 1 809 173 176 LEU N N 123.97 0.2 1 810 174 177 GLN H H 8.888 0.01 1 811 174 177 GLN C C 175.55 0.1 1 812 174 177 GLN CA C 54.16 0.1 1 813 174 177 GLN CB C 32.13 0.1 1 814 174 177 GLN N N 117.83 0.2 1 815 175 178 ARG H H 7.944 0.01 1 816 175 178 ARG C C 176.32 0.1 1 817 175 178 ARG CA C 57.1 0.1 1 818 175 178 ARG CB C 29.51 0.1 1 819 175 178 ARG N N 126.31 0.2 1 820 176 179 THR H H 8.854 0.01 1 821 176 179 THR C C 174.94 0.1 1 822 176 179 THR CA C 61.15 0.1 1 823 176 179 THR CB C 69.57 0.1 1 824 176 179 THR N N 120.06 0.2 1 825 177 180 GLY H H 7.689 0.01 1 826 177 180 GLY C C 177.03 0.1 1 827 177 180 GLY CA C 47.62 0.1 1 828 177 180 GLY N N 117.77 0.2 1 stop_ save_