data_27180 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Coheson Domain 5 from Clostridium themocellum ; _BMRB_accession_number 27180 _BMRB_flat_file_name bmr27180.str _Entry_type original _Submission_date 2017-07-14 _Accession_date 2017-07-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Coheson Domain 5 from the Clostridium themocellum cellulosome' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Galera-Prat Albert . . 2 Laurents Douglas . . 3 'Carri n-V zquez' Mariano . . 4 Pantoja-Uceda David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 "13C chemical shifts" 480 "15N chemical shifts" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-28 original BMRB . stop_ _Original_release_date 2017-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution conformation of a cohesin module and its scaffoldin linker from a prototypical cellulosome ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29486159 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Galera-Prat Albert . . 2 Pantoja-Uceda David . . 3 Laurents Douglas V. . 4 'Carrion Vazquez' Mariano . . stop_ _Journal_abbreviation 'Arch. Biochem. Biophys.' _Journal_name_full 'Archives of biochemistry and biophysics' _Journal_volume 644 _Journal_issue . _Journal_ISSN 1096-0384 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1 _Page_last 7 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Cohesin Domain 5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Cohesin Domain 5' $Cohesin_Domain_5 stop_ _System_molecular_weight 15414 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Forms part of the structural core of the scaffoldin complex of the cellulosome.' stop_ _Database_query_date . _Details ; Cohesin domain 5 is part of a large protein called "Scaffolding" which in turn is connected by non-covalent interactions to dockerin proteins and attached hydrolytic enzymes, as well as to the cell wall. The linker sequence follows the folded cohesin domain in the WT protein except the linker has an extra Gly at the N-terminus and the peptide was acetylated at the N-terminus and amidated at the C-terminus (residues 146-169). ; save_ ######################## # Monomeric polymers # ######################## save_Cohesin_Domain_5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cohesin Domain 5' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 145 _Mol_residue_sequence ; GGAVRIKVDTVNAKPGDTVR IPVRFSGIPSKGIANCDFVY SYDPNVLEIIEIEPGDIIVD PNPDKSFDTAVYPDRKIIVF LFAEDSGTGAYAITKDGVFA TIVAKVKSGAPNGLSVIKFV EVGGFANNDLVEQKTQFFDG GVNVGGDTTEPATPTTPVTT PTTTDDLDA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 GLY 3 3 ALA 4 4 VAL 5 5 ARG 6 6 ILE 7 7 LYS 8 8 VAL 9 9 ASP 10 10 THR 11 11 VAL 12 12 ASN 13 13 ALA 14 14 LYS 15 15 PRO 16 16 GLY 17 17 ASP 18 18 THR 19 19 VAL 20 20 ARG 21 21 ILE 22 22 PRO 23 23 VAL 24 24 ARG 25 25 PHE 26 26 SER 27 27 GLY 28 28 ILE 29 29 PRO 30 30 SER 31 31 LYS 32 32 GLY 33 33 ILE 34 34 ALA 35 35 ASN 36 36 CYS 37 37 ASP 38 38 PHE 39 39 VAL 40 40 TYR 41 41 SER 42 42 TYR 43 43 ASP 44 44 PRO 45 45 ASN 46 46 VAL 47 47 LEU 48 48 GLU 49 49 ILE 50 50 ILE 51 51 GLU 52 52 ILE 53 53 GLU 54 54 PRO 55 55 GLY 56 56 ASP 57 57 ILE 58 58 ILE 59 59 VAL 60 60 ASP 61 61 PRO 62 62 ASN 63 63 PRO 64 64 ASP 65 65 LYS 66 66 SER 67 67 PHE 68 68 ASP 69 69 THR 70 70 ALA 71 71 VAL 72 72 TYR 73 73 PRO 74 74 ASP 75 75 ARG 76 76 LYS 77 77 ILE 78 78 ILE 79 79 VAL 80 80 PHE 81 81 LEU 82 82 PHE 83 83 ALA 84 84 GLU 85 85 ASP 86 86 SER 87 87 GLY 88 88 THR 89 89 GLY 90 90 ALA 91 91 TYR 92 92 ALA 93 93 ILE 94 94 THR 95 95 LYS 96 96 ASP 97 97 GLY 98 98 VAL 99 99 PHE 100 100 ALA 101 101 THR 102 102 ILE 103 103 VAL 104 104 ALA 105 105 LYS 106 106 VAL 107 107 LYS 108 108 SER 109 109 GLY 110 110 ALA 111 111 PRO 112 112 ASN 113 113 GLY 114 114 LEU 115 115 SER 116 116 VAL 117 117 ILE 118 118 LYS 119 119 PHE 120 120 VAL 121 121 GLU 122 122 VAL 123 123 GLY 124 124 GLY 125 125 PHE 126 126 ALA 127 127 ASN 128 128 ASN 129 129 ASP 130 130 LEU 131 131 VAL 132 132 GLU 133 133 GLN 134 134 LYS 135 135 THR 136 136 GLN 137 137 PHE 138 138 PHE 139 139 ASP 140 140 GLY 141 141 GLY 142 142 VAL 143 143 ASN 144 144 VAL 145 145 GLY 146 146 GLY 147 147 ASP 148 148 THR 149 149 THR 150 150 GLU 151 151 PRO 152 152 ALA 153 153 THR 154 154 PRO 155 155 THR 156 156 THR 157 157 PRO 158 158 VAL 159 159 THR 160 160 THR 161 161 PRO 162 162 THR 163 163 THR 164 164 THR 165 165 ASP 166 166 ASP 167 167 LEU 168 168 ASP 169 169 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cohesin_Domain_5 'Clostridium thermocellum' 1515 Bacteria . Clostridium thermocellum 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 $Cohesin_Domain_5 'recombinant technology' . Escherichia coli BL12 ALBERT 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 $Cohesin_Domain_5 1.26 mM '[U-100% 13C; U-100% 15N]' KH2PO5 8.5 mM 'natural abundance' KH2PO4 1.5 mM 'natural abundance' 'sodium azide' 0.7 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Cohesin_Domain_5 2 mM '[U-100% 13C; U-100% 15N]' KH2PO5 8.5 mM 'natural abundance' KH2PO4 1.5 mM 'natural abundance' 'sodium azide' 0.7 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.13 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_2D_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_2 save_ save_2D_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 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' 0.02 0.001 M pH 6.02 0.02 pH pressure 1 . atm temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 0.001 M pH 6.02 0.02 pH pressure 1 . atm temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; 1H directly referenced to upfield tri-methyl group of DSS. 13C and 15N nuclei are indirectly referenced using their respective gyromagnetic ratios to 1H as recommended by Markley, Wuthrich, et al. ; 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 'The uncertainty for 13C alpha and beta is 0.05 ppm, but the uncertainty for 13CO is lower; it is equal to 0.01 ppm.' loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '3D HNCO' '2D 1H-13C HSQC aliphatic' '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HBHA(CO)NH' '3D HNCACB' '2D TOCSY' '2D NOESY' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Cohesin Domain 5' _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 1 GLY C C 173.18 0.01 1 2 2 2 GLY CA C 45.09 0.05 1 3 3 3 ALA H H 7.97 0.004 1 4 3 3 ALA C C 176.99 0.01 1 5 3 3 ALA CA C 51.43 0.05 1 6 3 3 ALA CB C 19.39 0.05 1 7 3 3 ALA N N 122.62 0.04 1 8 4 4 VAL H H 8.04 0.004 1 9 4 4 VAL C C 174.62 0.01 1 10 4 4 VAL CA C 62.25 0.05 1 11 4 4 VAL CB C 31.7 0.05 1 12 4 4 VAL N N 122.83 0.04 1 13 5 5 ARG H H 8.59 0.004 1 14 5 5 ARG C C 174.80 0.01 1 15 5 5 ARG CA C 54.73 0.05 1 16 5 5 ARG CB C 31.7 0.05 1 17 5 5 ARG N N 125.79 0.04 1 18 6 6 ILE H H 8.39 0.004 1 19 6 6 ILE C C 174.32 0.01 1 20 6 6 ILE CA C 61.26 0.05 1 21 6 6 ILE CB C 39.9 0.05 1 22 6 6 ILE N N 126.06 0.04 1 23 7 7 LYS H H 8.99 0.004 1 24 7 7 LYS C C 174.85 0.01 1 25 7 7 LYS CA C 55.3 0.05 1 26 7 7 LYS CB C 36.97 0.05 1 27 7 7 LYS N N 124.39 0.04 1 28 8 8 VAL H H 6.69 0.004 1 29 8 8 VAL C C 174.88 0.01 1 30 8 8 VAL CA C 61.39 0.05 1 31 8 8 VAL CB C 32.87 0.05 1 32 8 8 VAL N N 127.0 0.04 1 33 9 9 ASP H H 8.29 0.004 1 34 9 9 ASP C C 175.17 0.01 1 35 9 9 ASP CA C 55.75 0.05 1 36 9 9 ASP CB C 41.66 0.05 1 37 9 9 ASP N N 127.89 0.04 1 38 10 10 THR H H 8.09 0.004 1 39 10 10 THR C C 175.21 0.01 1 40 10 10 THR CA C 61.93 0.05 1 41 10 10 THR CB C 69.79 0.05 1 42 10 10 THR N N 113.50 0.04 1 43 11 11 VAL H H 8.28 0.004 1 44 11 11 VAL C C 173.96 0.01 1 45 11 11 VAL CA C 59.01 0.05 1 46 11 11 VAL CB C 35.22 0.05 1 47 11 11 VAL N N 121.75 0.04 1 48 12 12 ASN H H 8.69 0.004 1 49 12 12 ASN C C 174.66 0.01 1 50 12 12 ASN CA C 52.7 0.05 1 51 12 12 ASN CB C 39.9 0.05 1 52 12 12 ASN N N 122.18 0.04 1 53 13 13 ALA H H 8.38 0.004 1 54 13 13 ALA C C 174.43 0.01 1 55 13 13 ALA CA C 51.78 0.05 1 56 13 13 ALA CB C 24.67 0.05 1 57 13 13 ALA N N 122.25 0.04 1 58 14 14 LYS H H 8.52 0.004 1 59 14 14 LYS C C 174.14 0.01 1 60 14 14 LYS CA C 53.3 0.05 1 61 14 14 LYS CB C 32.28 0.05 1 62 14 14 LYS N N 118.95 0.04 1 63 15 15 PRO C C 177.29 0.01 1 64 15 15 PRO CA C 64.51 0.05 1 65 15 15 PRO CB C 31.7 0.05 1 66 16 16 GLY H H 8.18 0.004 1 67 16 16 GLY C C 174.53 0.01 1 68 16 16 GLY CA C 45.29 0.05 1 69 16 16 GLY N N 114.32 0.04 1 70 17 17 ASP H H 8.03 0.004 1 71 17 17 ASP C C 176.11 0.01 1 72 17 17 ASP CA C 55.06 0.05 1 73 17 17 ASP CB C 41.66 0.05 1 74 17 17 ASP N N 121.62 0.04 1 75 18 18 THR H H 8.43 0.004 1 76 18 18 THR C C 174.48 0.01 1 77 18 18 THR CA C 62.76 0.05 1 78 18 18 THR CB C 69.79 0.04 1 79 18 18 THR N N 116.67 0.04 1 80 19 19 VAL H H 9.66 0.004 1 81 19 19 VAL C C 172.53 0.01 1 82 19 19 VAL CA C 58.9 0.05 1 83 19 19 VAL CB C 35.22 0.04 1 84 19 19 VAL N N 123.33 0.04 1 85 20 20 ARG H H 8.07 0.004 1 86 20 20 ARG C C 175.70 0.01 1 87 20 20 ARG CA C 54.77 0.05 1 88 20 20 ARG CB C 32.28 0.05 1 89 20 20 ARG N N 121.69 0.04 1 90 21 21 ILE H H 9.57 0.004 1 91 21 21 ILE C C 173.96 0.01 1 92 21 21 ILE CA C 59.09 0.05 1 93 21 21 ILE CB C 40.49 0.05 1 94 21 21 ILE N N 123.11 0.04 1 95 22 22 PRO C C 173.76 0.01 1 96 22 22 PRO CA C 63.54 0.05 1 97 22 22 PRO CB C 33.46 0.05 1 98 23 23 VAL H H 9.07 0.004 1 99 23 23 VAL C C 175.84 0.01 1 100 23 23 VAL CA C 61.81 0.05 1 101 23 23 VAL CB C 32.87 0.05 1 102 23 23 VAL N N 122.33 0.04 1 103 24 24 ARG H H 9.39 0.004 1 104 24 24 ARG C C 175.66 0.01 1 105 24 24 ARG CA C 55.49 0.05 1 106 24 24 ARG CB C 32.87 0.05 1 107 24 24 ARG N N 125.28 0.04 1 108 25 25 PHE H H 9.33 0.004 1 109 25 25 PHE C C 176.89 0.01 1 110 25 25 PHE CA C 52.67 0.05 1 111 25 25 PHE CB C 40.49 0.05 1 112 25 25 PHE N N 121.32 0.04 1 113 26 26 SER H H 9.25 0.004 1 114 26 26 SER C C 173.08 0.01 1 115 26 26 SER CA C 57.18 0.05 1 116 26 26 SER CB C 66.27 0.05 1 117 26 26 SER N N 117.15 0.04 1 118 27 27 GLY H H 9.13 0.004 1 119 27 27 GLY C C 174.99 0.01 1 120 27 27 GLY CA C 46.26 0.05 1 121 27 27 GLY N N 111.18 0.04 1 122 28 28 ILE H H 8.99 0.004 1 123 28 28 ILE C C 175.53 0.01 1 124 28 28 ILE CA C 56.66 0.05 1 125 28 28 ILE CB C 35.80 0.05 1 126 28 28 ILE N N 122.34 0.04 1 127 30 30 SER C C 176.10 0.01 1 128 30 30 SER CA C 61.36 0.05 1 129 30 30 SER CB C 62.17 0.05 1 130 31 31 LYS H H 7.68 0.004 1 131 31 31 LYS C C 176.92 0.01 1 132 31 31 LYS CA C 56.91 0.05 1 133 31 31 LYS CB C 32.87 0.05 1 134 31 31 LYS N N 117.84 0.04 1 135 32 32 GLY H H 7.69 0.004 1 136 32 32 GLY C C 171.97 0.01 1 137 32 32 GLY CA C 44.89 0.05 1 138 32 32 GLY N N 105.21 0.04 1 139 33 33 ILE H H 8.74 0.004 1 140 33 33 ILE C C 174.98 0.01 1 141 33 33 ILE CA C 57.64 0.05 1 142 33 33 ILE CB C 38.14 0.05 1 143 33 33 ILE N N 116.7 0.04 1 144 34 34 ALA H H 8.96 0.004 1 145 34 34 ALA C C 176.09 0.01 1 146 34 34 ALA CA C 53.38 0.05 1 147 34 34 ALA CB C 21.15 0.05 1 148 34 34 ALA N N 129.81 0.04 1 149 35 35 ASN H H 7.55 0.004 1 150 35 35 ASN C C 172.82 0.01 1 151 35 35 ASN CA C 53.35 0.05 1 152 35 35 ASN CB C 41.66 0.05 1 153 35 35 ASN N N 111.24 0.04 1 154 36 36 CYS H H 9.60 0.004 1 155 36 36 CYS C C 172.50 0.01 1 156 36 36 CYS CA C 56.13 0.05 1 157 36 36 CYS CB C 31.70 0.05 1 158 36 36 CYS N N 115.56 0.04 1 159 37 37 ASP H H 8.92 0.004 1 160 37 37 ASP C C 174.67 0.01 1 161 37 37 ASP CA C 54.02 0.05 1 162 37 37 ASP CB C 44.00 0.05 1 163 37 37 ASP N N 117.67 0.04 1 164 38 38 PHE H H 8.79 0.004 1 165 38 38 PHE C C 172.83 0.01 1 166 38 38 PHE CA C 57.01 0.05 1 167 38 38 PHE CB C 40.49 0.05 1 168 38 38 PHE N N 116.81 0.04 1 169 39 39 VAL H H 8.98 0.004 1 170 39 39 VAL C C 175.78 0.01 1 171 39 39 VAL CA C 61.67 0.05 1 172 39 39 VAL CB C 36.97 0.05 1 173 39 39 VAL N N 118.98 0.04 1 174 40 40 TYR C C 174.33 0.01 1 175 40 40 TYR CA C 57.1 0.05 1 176 40 40 TYR CB C 44.0 0.05 1 177 41 41 SER H H 10.40 0.004 1 178 41 41 SER CA C 55.92 0.05 1 179 41 41 SER CB C 66.86 0.05 1 180 41 41 SER N N 116.23 0.04 1 181 42 42 TYR H H 8.35 0.004 1 182 42 42 TYR C C 172.49 0.01 1 183 42 42 TYR CA C 55.17 0.05 1 184 42 42 TYR CB C 41.07 0.05 1 185 42 42 TYR N N 118.66 0.04 1 186 43 43 ASP H H 9.54 0.004 1 187 43 43 ASP C C 175.71 0.01 1 188 43 43 ASP CA C 49.82 0.05 1 189 43 43 ASP CB C 41.07 0.05 1 190 43 43 ASP N N 119.77 0.04 1 191 44 44 PRO C C 177.15 0.01 1 192 44 44 PRO CA C 62.85 0.05 1 193 44 44 PRO CB C 31.70 0.05 1 194 45 45 ASN H H 8.38 0.004 1 195 45 45 ASN C C 175.16 0.01 1 196 45 45 ASN CA C 54.53 0.05 1 197 45 45 ASN CB C 38.14 0.05 1 198 45 45 ASN N N 115.07 0.04 1 199 46 46 VAL H H 7.71 0.004 1 200 46 46 VAL C C 173.77 0.01 1 201 46 46 VAL CA C 64.39 0.05 1 202 46 46 VAL CB C 34.63 0.05 1 203 46 46 VAL N N 118.99 0.04 1 204 47 47 LEU H H 8.14 0.004 1 205 47 47 LEU C C 175.07 0.01 1 206 47 47 LEU CA C 52.98 0.05 1 207 47 47 LEU CB C 45.18 0.05 1 208 47 47 LEU N N 117.35 0.04 1 209 48 48 GLU H H 8.96 0.004 1 210 48 48 GLU C C 175.97 0.01 1 211 48 48 GLU CA C 53.99 0.05 1 212 48 48 GLU CB C 31.70 0.05 1 213 48 48 GLU N N 121.36 0.04 1 214 49 49 ILE H H 8.40 0.004 1 215 49 49 ILE C C 175.94 0.01 1 216 49 49 ILE CA C 61.26 0.05 1 217 49 49 ILE CB C 34.63 0.05 1 218 49 49 ILE N N 125.81 0.04 1 219 50 50 ILE H H 9.15 0.004 1 220 50 50 ILE C C 175.95 0.01 1 221 50 50 ILE CA C 62.35 0.05 1 222 50 50 ILE CB C 38.73 0.05 1 223 50 50 ILE N N 129.98 0.04 1 224 51 51 GLU H H 7.80 0.004 1 225 51 51 GLU C C 172.98 0.01 1 226 51 51 GLU CA C 55.14 0.05 1 227 51 51 GLU CB C 32.28 0.05 1 228 51 51 GLU N N 115.31 0.04 1 229 52 52 ILE H H 8.61 0.004 1 230 52 52 ILE C C 175.41 0.01 1 231 52 52 ILE CA C 60.66 0.05 1 232 52 52 ILE CB C 37.56 0.05 1 233 52 52 ILE N N 120.60 0.04 1 234 53 53 GLU H H 8.87 0.004 1 235 53 53 GLU C C 174.77 0.01 1 236 53 53 GLU CA C 53.01 0.05 1 237 53 53 GLU CB C 31.70 0.05 1 238 53 53 GLU N N 128.22 0.04 1 239 54 54 PRO C C 177.03 0.01 1 240 54 54 PRO CA C 62.51 0.05 1 241 54 54 PRO CB C 31.10 0.05 1 242 55 55 GLY H H 7.33 0.004 1 243 55 55 GLY C C 174.41 0.01 1 244 55 55 GLY CA C 43.060 0.05 1 245 55 55 GLY N N 110.36 0.04 1 246 56 56 ASP H H 7.57 0.004 1 247 56 56 ASP C C 177.55 0.01 1 248 56 56 ASP CA C 55.65 0.05 1 249 56 56 ASP CB C 40.49 0.05 1 250 56 56 ASP N N 116.13 0.04 1 251 57 57 ILE H H 7.03 0.004 1 252 57 57 ILE C C 175.25 0.01 1 253 57 57 ILE CA C 61.76 0.05 1 254 57 57 ILE CB C 35.22 0.05 1 255 57 57 ILE N N 109.29 0.04 1 256 58 58 ILE H H 7.14 0.004 1 257 58 58 ILE C C 176.29 0.01 1 258 58 58 ILE CA C 59.73 0.05 1 259 58 58 ILE CB C 35.22 0.05 1 260 58 58 ILE N N 122.81 0.04 1 261 59 59 VAL H H 8.87 0.004 1 262 59 59 VAL C C 176.08 0.01 1 263 59 59 VAL CA C 61.44 0.05 1 264 59 59 VAL CB C 31.70 0.05 1 265 59 59 VAL N N 120.75 0.04 1 266 60 60 ASP H H 6.71 0.004 1 267 60 60 ASP C C 174.99 0.01 1 268 60 60 ASP CA C 51.66 0.05 1 269 60 60 ASP CB C 42.25 0.05 1 270 60 60 ASP N N 124.38 0.04 1 271 61 61 PRO C C 176.77 0.01 1 272 61 61 PRO CA C 63.78 0.05 1 273 61 61 PRO CB C 32.28 0.05 1 274 62 62 ASN H H 8.83 0.004 1 275 62 62 ASN C C 171.97 0.01 1 276 62 62 ASN CA C 50.52 0.05 1 277 62 62 ASN CB C 39.32 0.05 1 278 62 62 ASN N N 118.00 0.04 1 279 63 63 PRO C C 176.75 0.01 1 280 63 63 PRO CA C 66.32 0.05 1 281 63 63 PRO CB C 31.70 0.05 1 282 64 64 ASP H H 8.36 0.004 1 283 64 64 ASP C C 177.01 0.01 1 284 64 64 ASP CA C 55.29 0.05 1 285 64 64 ASP CB C 39.90 0.05 1 286 64 64 ASP N N 113.8 0.04 1 287 65 65 LYS H H 8.35 0.004 1 288 65 65 LYS C C 178.09 0.01 1 289 65 65 LYS CA C 57.12 0.05 1 290 65 65 LYS CB C 31.11 0.05 1 291 65 65 LYS N N 118.41 0.04 1 292 66 66 SER H H 7.18 0.004 1 293 66 66 SER C C 171.81 0.01 1 294 66 66 SER CA C 60.56 0.05 1 295 66 66 SER CB C 66.27 0.05 1 296 66 66 SER N N 112.8 0.01 1 297 67 67 PHE H H 8.40 0.004 1 298 67 67 PHE C C 172.09 0.01 1 299 67 67 PHE CA C 56.89 0.05 1 300 67 67 PHE CB C 43.42 0.05 1 301 67 67 PHE N N 123.91 0.04 1 302 68 68 ASP H H 8.70 0.004 1 303 68 68 ASP C C 173.09 0.01 1 304 68 68 ASP CA C 52.42 0.05 1 305 68 68 ASP CB C 44.59 0.05 1 306 68 68 ASP N N 127.07 0.04 1 307 69 69 THR H H 7.82 0.004 1 308 69 69 THR C C 173.39 0.01 1 309 69 69 THR CA C 58.97 0.05 1 310 69 69 THR CB C 74.47 0.05 1 311 69 69 THR N N 108.33 0.04 1 312 70 70 ALA H H 8.39 0.004 1 313 70 70 ALA C C 174.23 0.01 1 314 70 70 ALA CA C 51.48 0.05 1 315 70 70 ALA CB C 22.32 0.05 1 316 70 70 ALA N N 122.00 0.04 1 317 71 71 VAL H H 7.99 0.004 1 318 71 71 VAL C C 175.27 0.01 1 319 71 71 VAL CA C 61.26 0.05 1 320 71 71 VAL CB C 33.46 0.05 1 321 71 71 VAL N N 121.74 0.04 1 322 72 72 TYR H H 8.77 0.004 1 323 72 72 TYR C C 174.72 0.01 1 324 72 72 TYR CA C 53.40 0.05 1 325 72 72 TYR CB C 39.32 0.05 1 326 72 72 TYR N N 125.53 0.04 1 327 73 73 PRO C C 178.68 0.01 1 328 73 73 PRO CA C 65.48 0.05 1 329 73 73 PRO CB C 32.28 0.05 1 330 74 74 ASP H H 8.87 0.004 1 331 74 74 ASP C C 177.43 0.01 1 332 74 74 ASP CA C 56.09 0.05 1 333 74 74 ASP CB C 39.32 0.05 1 334 74 74 ASP N N 113.78 0.04 1 335 75 75 ARG H H 7.24 0.004 1 336 75 75 ARG C C 174.19 0.01 1 337 75 75 ARG CA C 55.89 0.05 1 338 75 75 ARG CB C 32.28 0.05 1 339 75 75 ARG N N 117.94 0.04 1 340 76 76 LYS H H 7.99 0.004 1 341 76 76 LYS C C 175.21 0.01 1 342 76 76 LYS CA C 57.59 0.05 1 343 76 76 LYS CB C 28.18 0.05 1 344 76 76 LYS N N 115.82 0.04 1 345 77 77 ILE H H 7.38 0.004 1 346 77 77 ILE C C 173.87 0.01 1 347 77 77 ILE CA C 59.82 0.05 1 348 77 77 ILE CB C 44.00 0.05 1 349 77 77 ILE N N 106.90 0.04 1 350 78 78 ILE H H 9.32 0.004 1 351 78 78 ILE C C 173.84 0.01 1 352 78 78 ILE CA C 60.89 0.05 1 353 78 78 ILE CB C 41.70 0.05 1 354 78 78 ILE N N 120.99 0.04 1 355 79 79 VAL H H 9.02 0.004 1 356 79 79 VAL C C 174.72 0.01 1 357 79 79 VAL CA C 61.35 0.05 1 358 79 79 VAL CB C 34.04 0.05 1 359 79 79 VAL N N 125.7 0.04 1 360 80 80 PHE H H 9.01 0.004 1 361 80 80 PHE C C 174.29 0.01 1 362 80 80 PHE CA C 56.84 0.05 1 363 80 80 PHE CB C 41.07 0.05 1 364 80 80 PHE N N 124.01 0.04 1 365 81 81 LEU H H 8.25 0.004 1 366 81 81 LEU C C 174.26 0.01 1 367 81 81 LEU CA C 54.70 0.05 1 368 81 81 LEU CB C 44.59 0.05 1 369 81 81 LEU N N 120.87 0.04 1 370 82 82 PHE H H 9.32 0.004 1 371 82 82 PHE C C 174.96 0.01 1 372 82 82 PHE CA C 56.07 0.05 1 373 82 82 PHE CB C 43.42 0.05 1 374 82 82 PHE N N 123.51 0.04 1 375 83 83 ALA H H 8.63 0.004 1 376 83 83 ALA C C 175.80 0.01 1 377 83 83 ALA CA C 51.60 0.05 1 378 83 83 ALA CB C 19.39 0.05 1 379 83 83 ALA N N 132.98 0.04 1 380 84 84 GLU H H 8.21 0.004 1 381 84 84 GLU C C 178.89 0.01 1 382 84 84 GLU CA C 55.93 0.05 1 383 84 84 GLU CB C 28.77 0.05 1 384 84 84 GLU N N 126.38 0.04 1 385 85 85 ASP H H 8.64 0.004 1 386 85 85 ASP C C 176.82 0.01 1 387 85 85 ASP CA C 56.38 0.05 1 388 85 85 ASP CB C 44.00 0.05 1 389 85 85 ASP N N 122.08 0.04 1 390 86 86 SER H H 7.61 0.004 1 391 86 86 SER C C 176.60 0.01 1 392 86 86 SER CA C 61.33 0.05 1 393 86 86 SER CB C 63.34 0.05 1 394 86 86 SER N N 113.48 0.04 1 395 87 87 GLY H H 7.55 0.004 1 396 87 87 GLY C C 174.42 0.01 1 397 87 87 GLY CA C 45.89 0.05 1 398 87 87 GLY N N 110.56 0.04 1 399 88 88 THR H H 8.53 0.004 1 400 88 88 THR C C 175.52 0.01 1 401 88 88 THR CA C 60.88 0.05 1 402 88 88 THR CB C 70.96 0.05 1 403 88 88 THR N N 110.16 0.04 1 404 89 89 GLY H H 8.70 0.004 1 405 89 89 GLY C C 175.37 0.01 1 406 89 89 GLY CA C 44.90 0.05 1 407 89 89 GLY N N 112.21 0.04 1 408 90 90 ALA H H 7.71 0.004 1 409 90 90 ALA C C 179.30 0.01 1 410 90 90 ALA CA C 54.82 0.05 1 411 90 90 ALA CB C 17.64 0.05 1 412 90 90 ALA N N 124.18 0.04 1 413 91 91 TYR H H 7.42 0.004 1 414 91 91 TYR C C 175.67 0.01 1 415 91 91 TYR CA C 52.37 0.05 1 416 91 91 TYR CB C 36.39 0.05 1 417 91 91 TYR N N 112.93 0.04 1 418 92 92 ALA H H 7.17 0.004 1 419 92 92 ALA C C 176.90 0.01 1 420 92 92 ALA CA C 53.10 0.05 1 421 92 92 ALA CB C 18.81 0.05 1 422 92 92 ALA N N 121.36 0.04 1 423 93 93 ILE H H 8.78 0.004 1 424 93 93 ILE C C 177.00 0.01 1 425 93 93 ILE CA C 62.38 0.05 1 426 93 93 ILE CB C 39.90 0.05 1 427 93 93 ILE N N 121.86 0.04 1 428 94 94 THR H H 9.03 0.004 1 429 94 94 THR C C 173.47 0.01 1 430 94 94 THR CA C 61.26 0.05 1 431 94 94 THR CB C 70.96 0.05 1 432 94 94 THR N N 115.91 0.04 1 433 95 95 LYS H H 7.50 0.004 1 434 95 95 LYS C C 172.44 0.01 1 435 95 95 LYS CA C 54.28 0.05 1 436 95 95 LYS CB C 35.80 0.05 1 437 95 95 LYS N N 122.86 0.04 1 438 96 96 ASP H H 7.71 0.004 1 439 96 96 ASP C C 177.03 0.01 1 440 96 96 ASP CA C 53.81 0.05 1 441 96 96 ASP CB C 41.07 0.05 1 442 96 96 ASP N N 117.81 0.04 1 443 97 97 GLY H H 8.25 0.004 1 444 97 97 GLY C C 171.75 0.01 1 445 97 97 GLY CA C 45.47 0.05 1 446 97 97 GLY N N 107.11 0.04 1 447 98 98 VAL H H 9.06 0.004 1 448 98 98 VAL C C 174.31 0.01 1 449 98 98 VAL CA C 64.23 0.05 1 450 98 98 VAL CB C 32.28 0.05 1 451 98 98 VAL N N 124.23 0.04 1 452 99 99 PHE H H 8.94 0.004 1 453 99 99 PHE C C 173.53 0.01 1 454 99 99 PHE CA C 57.90 0.05 1 455 99 99 PHE CB C 40.49 0.05 1 456 99 99 PHE N N 129.32 0.04 1 457 100 100 ALA H H 7.66 0.004 1 458 100 100 ALA C C 174.86 0.01 1 459 100 100 ALA CA C 50.34 0.05 1 460 100 100 ALA CB C 24.08 0.05 1 461 100 100 ALA N N 116.32 0.04 1 462 101 101 THR H H 8.82 0.004 1 463 101 101 THR C C 173.63 0.01 1 464 101 101 THR CA C 62.27 0.05 1 465 101 101 THR CB C 70.37 0.05 1 466 101 101 THR N N 114.59 0.04 1 467 102 102 ILE H H 8.62 0.004 1 468 102 102 ILE C C 173.77 0.01 1 469 102 102 ILE CA C 62.04 0.05 1 470 102 102 ILE CB C 39.32 0.05 1 471 102 102 ILE N N 128.41 0.04 1 472 103 103 VAL H H 9.03 0.004 1 473 103 103 VAL C C 175.01 0.01 1 474 103 103 VAL CA C 62.03 0.05 1 475 103 103 VAL CB C 31.11 0.05 1 476 103 103 VAL N N 130.58 0.04 1 477 104 104 ALA H H 9.03 0.004 1 478 104 104 ALA C C 174.05 0.01 1 479 104 104 ALA CA C 49.92 0.05 1 480 104 104 ALA CB C 23.5 0.05 1 481 104 104 ALA N N 129.13 0.04 1 482 105 105 LYS H H 9.10 0.004 1 483 105 105 LYS C C 176.06 0.01 1 484 105 105 LYS CA C 54.28 0.05 1 485 105 105 LYS CB C 35.22 0.05 1 486 105 105 LYS N N 121.44 0.04 1 487 106 106 VAL H H 8.77 0.004 1 488 106 106 VAL C C 177.35 0.01 1 489 106 106 VAL CA C 61.44 0.05 1 490 106 106 VAL CB C 30.53 0.05 1 491 106 106 VAL N N 125.89 0.04 1 492 107 107 LYS H H 9.00 0.004 1 493 107 107 LYS C C 177.47 0.01 1 494 107 107 LYS CA C 58.33 0.05 1 495 107 107 LYS CB C 32.28 0.05 1 496 107 107 LYS N N 130.84 0.04 1 497 108 108 SER H H 8.47 0.004 1 498 108 108 SER C C 177.56 0.01 1 499 108 108 SER CA C 61.18 0.05 1 500 108 108 SER CB C 63.34 0.05 1 501 108 108 SER N N 115.81 0.04 1 502 109 109 GLY H H 8.43 0.004 1 503 109 109 GLY C C 174.13 0.01 1 504 109 109 GLY CA C 44.89 0.05 1 505 109 109 GLY N N 110.44 0.04 1 506 110 110 ALA H H 7.43 0.004 1 507 110 110 ALA C C 174.36 0.01 1 508 110 110 ALA CA C 50.77 0.05 1 509 110 110 ALA CB C 19.39 0.05 1 510 110 110 ALA N N 123.77 0.04 1 511 111 111 PRO C C 175.78 0.01 1 512 111 111 PRO CA C 61.58 0.05 1 513 111 111 PRO CB C 32.28 0.05 1 514 112 112 ASN H H 8.18 0.05 1 515 112 112 ASN C C 176.10 0.01 1 516 112 112 ASN CA C 53.37 0.05 1 517 112 112 ASN CB C 38.73 0.05 1 518 112 112 ASN N N 117.26 0.04 1 519 113 113 GLY H H 9.12 0.004 1 520 113 113 GLY C C 175.06 0.01 1 521 113 113 GLY CA C 43.62 0.05 1 522 113 113 GLY N N 109.68 0.04 1 523 114 114 LEU H H 8.59 0.004 1 524 114 114 LEU C C 175.79 0.01 1 525 114 114 LEU CA C 55.99 0.05 1 526 114 114 LEU CB C 41.66 0.05 1 527 114 114 LEU N N 123.98 0.04 1 528 115 115 SER H H 9.37 0.004 1 529 115 115 SER C C 175.87 0.01 1 530 115 115 SER CA C 56.34 0.05 1 531 115 115 SER CB C 64.51 0.05 1 532 115 115 SER N N 125.73 0.04 1 533 116 116 VAL H H 8.64 0.004 1 534 116 116 VAL C C 177.09 0.01 1 535 116 116 VAL CA C 63.8 0.05 1 536 116 116 VAL CB C 33.46 0.05 1 537 116 116 VAL N N 126.86 0.04 1 538 117 117 ILE H H 8.41 0.004 1 539 117 117 ILE C C 174.98 0.01 1 540 117 117 ILE CA C 61.38 0.05 1 541 117 117 ILE CB C 39.90 0.05 1 542 117 117 ILE N N 132.04 0.04 1 543 118 118 LYS H H 8.41 0.004 1 544 118 118 LYS C C 175.18 0.01 1 545 118 118 LYS CA C 54.70 0.05 1 546 118 118 LYS CB C 36.39 0.05 1 547 118 118 LYS N N 127.54 0.04 1 548 119 119 PHE H H 9.10 0.004 1 549 119 119 PHE C C 175.10 0.01 1 550 119 119 PHE CA C 59.43 0.05 1 551 119 119 PHE CB C 38.73 0.05 1 552 119 119 PHE N N 129.83 0.04 1 553 120 120 VAL H H 7.90 0.004 1 554 120 120 VAL C C 174.37 0.01 1 555 120 120 VAL CA C 63.74 0.05 1 556 120 120 VAL CB C 33.46 0.05 1 557 120 120 VAL N N 127.98 0.04 1 558 121 121 GLU H H 6.52 0.004 1 559 121 121 GLU C C 172.02 0.01 1 560 121 121 GLU CA C 55.48 0.05 1 561 121 121 GLU CB C 31.70 0.05 1 562 121 121 GLU N N 112.67 0.04 1 563 122 122 VAL H H 8.51 0.004 1 564 122 122 VAL C C 173.60 0.01 1 565 122 122 VAL CA C 58.43 0.05 1 566 122 122 VAL CB C 35.22 0.05 1 567 122 122 VAL N N 119.63 0.04 1 568 123 123 GLY H H 8.86 0.004 1 569 123 123 GLY C C 174.41 0.01 1 570 123 123 GLY CA C 45.61 0.05 1 571 123 123 GLY N N 118.34 0.04 1 572 124 124 GLY H H 8.99 0.004 1 573 124 124 GLY C C 172.45 0.01 1 574 124 124 GLY CA C 45.26 0.05 1 575 124 124 GLY N N 116.00 0.04 1 576 125 125 PHE H H 9.82 0.004 1 577 125 125 PHE C C 173.95 0.01 1 578 125 125 PHE CA C 58.84 0.05 1 579 125 125 PHE CB C 39.9 0.05 1 580 125 125 PHE N N 127.35 0.04 1 581 126 126 ALA H H 8.57 0.004 1 582 126 126 ALA C C 177.82 0.01 1 583 126 126 ALA CA C 51.44 0.05 1 584 126 126 ALA CB C 22.32 0.05 1 585 126 126 ALA N N 126.61 0.04 1 586 127 127 ASN H H 8.01 0.004 1 587 127 127 ASN C C 177.11 0.01 1 588 127 127 ASN CA C 51.70 0.05 1 589 127 127 ASN CB C 39.90 0.05 1 590 127 127 ASN N N 117.68 0.04 1 591 128 128 ASN H H 7.82 0.004 1 592 128 128 ASN C C 176.05 0.01 1 593 128 128 ASN CA C 55.59 0.05 1 594 128 128 ASN CB C 38.73 0.05 1 595 128 128 ASN N N 114.88 0.04 1 596 129 129 ASP H H 7.45 0.004 1 597 129 129 ASP C C 174.86 0.01 1 598 129 129 ASP CA C 54.45 0.05 1 599 129 129 ASP CB C 41.07 0.05 1 600 129 129 ASP N N 118.06 0.04 1 601 130 130 LEU H H 8.40 0.004 1 602 130 130 LEU C C 176.09 0.01 1 603 130 130 LEU CA C 56.07 0.05 1 604 130 130 LEU CB C 37.54 0.05 1 605 130 130 LEU N N 114.86 0.04 1 606 131 131 VAL H H 7.67 0.004 1 607 131 131 VAL C C 177.92 0.01 1 608 131 131 VAL CA C 61.970 0.05 1 609 131 131 VAL CB C 32.28 0.05 1 610 131 131 VAL N N 120.25 0.04 1 611 132 132 GLU H H 9.00 0.004 1 612 132 132 GLU C C 176.68 0.01 1 613 132 132 GLU CA C 57.33 0.05 1 614 132 132 GLU CB C 29.99 0.05 1 615 132 132 GLU N N 131.07 0.04 1 616 133 133 GLN H H 9.18 0.004 1 617 133 133 GLN C C 175.26 0.01 1 618 133 133 GLN CA C 52.88 0.05 1 619 133 133 GLN CB C 30.53 0.05 1 620 133 133 GLN N N 122.47 0.04 1 621 134 134 LYS H H 8.450 0.004 1 622 134 134 LYS C C 176.02 0.01 1 623 134 134 LYS CA C 56.53 0.05 1 624 134 134 LYS CB C 32.28 0.05 1 625 134 134 LYS N N 123.30 0.04 1 626 135 135 THR H H 7.87 0.004 1 627 135 135 THR C C 174.64 0.01 1 628 135 135 THR CA C 58.72 0.05 1 629 135 135 THR CB C 73.89 0.05 1 630 135 135 THR N N 111.9 0.04 1 631 136 136 GLN H H 8.06 0.004 1 632 136 136 GLN C C 172.54 0.01 1 633 136 136 GLN CA C 55.27 0.05 1 634 136 136 GLN CB C 31.70 0.05 1 635 136 136 GLN N N 120.44 0.04 1 636 137 137 PHE H H 8.11 0.004 1 637 137 137 PHE C C 176.50 0.01 1 638 137 137 PHE CA C 56.50 0.05 1 639 137 137 PHE CB C 40.49 0.05 1 640 137 137 PHE N N 123.07 0.04 1 641 138 138 PHE H H 9.14 0.004 1 642 138 138 PHE C C 176.20 0.01 1 643 138 138 PHE CA C 56.70 0.05 1 644 138 138 PHE CB C 42.25 0.05 1 645 138 138 PHE N N 119.14 0.04 1 646 139 139 ASP H H 9.05 0.004 1 647 139 139 ASP C C 176.32 0.01 1 648 139 139 ASP CA C 55.07 0.05 1 649 139 139 ASP CB C 42.83 0.05 1 650 139 139 ASP N N 125.06 0.04 1 651 140 140 GLY H H 8.60 0.004 1 652 140 140 GLY C C 175.57 0.01 1 653 140 140 GLY CA C 45.62 0.05 1 654 140 140 GLY N N 108.54 0.04 1 655 141 141 GLY H H 8.89 0.004 1 656 141 141 GLY C C 170.34 0.01 1 657 141 141 GLY CA C 46.23 0.05 1 658 141 141 GLY N N 112.31 0.04 1 659 142 142 VAL H H 8.79 0.004 1 660 142 142 VAL C C 174.45 0.01 1 661 142 142 VAL CA C 59.68 0.05 1 662 142 142 VAL CB C 35.22 0.05 1 663 142 142 VAL N N 117.37 0.04 1 664 143 143 ASN H H 9.53 0.004 1 665 143 143 ASN C C 174.26 0.01 1 666 143 143 ASN CA C 52.42 0.05 1 667 143 143 ASN CB C 38.14 0.05 1 668 143 143 ASN N N 127.81 0.04 1 669 144 144 VAL H H 8.31 0.004 1 670 144 144 VAL C C 176.57 0.01 1 671 144 144 VAL CA C 62.49 0.05 1 672 144 144 VAL CB C 31.70 0.05 1 673 144 144 VAL N N 130.35 0.04 1 674 145 145 GLY H H 8.76 0.004 1 675 145 145 GLY C C 178.16 0.01 1 676 145 145 GLY CA C 46.37 0.05 1 677 145 145 GLY N N 123.56 0.04 1 678 146 146 GLY H H 8.46 0.005 1 679 146 146 GLY HA2 H 3.95 0.005 2 680 146 146 GLY HA3 H 3.95 0.005 2 681 146 146 GLY CA C 45.1 0.05 1 682 147 147 ASP H H 8.58 0.005 1 683 147 147 ASP HA H 4.74 0.005 1 684 147 147 ASP CA C 54.3 0.05 1 685 147 147 ASP CB C 39.2 0.10 1 686 147 147 ASP N N 120.1 0.1 1 687 148 148 THR H H 8.38 0.005 1 688 148 148 THR HA H 4.44 0.005 1 689 148 148 THR CA C 61.5 0.050 1 690 148 148 THR CB C 69.55 0.15 5 691 148 148 THR CG2 C 21.30 0.3 5 692 148 148 THR N N 114.5 0.1 1 693 149 149 THR H H 8.36 0.005 1 694 149 149 THR HA H 4.34 0.005 1 695 149 149 THR CA C 61.8 0.05 1 696 149 149 THR CB C 69.7 0.05 1 697 149 149 THR CG2 C 21.4 0.05 1 698 149 149 THR N N 116.9 0.1 1 699 150 150 GLU H H 8.50 0.005 1 700 150 150 GLU HA H 4.64 0.005 1 701 150 150 GLU CA C 53.5 0.05 1 702 150 150 GLU CB C 28.4 0.05 1 703 150 150 GLU CG C 34.5 0.05 1 704 150 150 GLU N N 125.3 0.1 1 705 151 151 PRO HA H 4.41 0.005 1 706 151 151 PRO CA C 62.9 0.05 1 707 151 151 PRO CG C 27.4 0.05 1 708 151 151 PRO CD C 50.6 0.05 1 709 152 152 ALA H H 8.62 0.005 1 710 152 152 ALA HA H 4.33 0.005 1 711 152 152 ALA CA C 52.2 0.05 1 712 152 152 ALA CB C 19.1 0.05 1 713 152 152 ALA N N 124.8 0.1 1 714 153 153 THR H H 8.41 0.005 1 715 153 153 THR HA H 4.59 0.005 1 716 153 153 THR CA C 59.2 0.2 1 717 153 153 THR CB C 69.6 0.2 5 718 153 153 THR CG2 C 21.4 0.2 5 719 153 153 THR N N 115.8 0.1 1 720 154 154 PRO HA H 4.50 0.005 1 721 154 154 PRO CA C 63.0 0.05 1 722 154 154 PRO CB C 32.2 0.05 1 723 154 154 PRO CG C 27.4 0.05 1 724 155 155 THR H H 8.59 0.005 1 725 155 155 THR HA H 4.40 0.08 5 726 155 155 THR CB C 69.6 0.2 5 727 155 155 THR CG2 C 21.4 0.2 5 728 155 155 THR N N 115.6 0.1 1 729 156 156 THR H H 8.38 0.005 1 730 156 156 THR HA H 4.60 0.02 5 731 156 156 THR CA C 59.9 0.2 5 732 156 156 THR CB C 69.6 0.2 5 733 156 156 THR CG2 C 21.4 0.2 5 734 156 156 THR N N 120.1 0.1 1 735 157 157 PRO HA H 4.45 0.005 1 736 157 157 PRO C C 32.2 0.05 1 737 157 157 PRO CA C 63.0 0.05 1 738 157 157 PRO CG C 27.4 0.05 1 739 157 157 PRO CD C 51.2 0.05 1 740 158 158 VAL H H 8.55 0.005 1 741 158 158 VAL HA H 4.15 0.005 1 742 158 158 VAL CA C 62.3 0.05 1 743 158 158 VAL CB C 32.7 0.05 1 744 158 158 VAL CG1 C 20.6 0.05 2 745 158 158 VAL CG2 C 21.1 0.05 2 746 158 158 VAL N N 121.4 0.1 1 747 159 159 THR H H 8.49 0.005 1 748 159 159 THR HA H 4.42 0.005 1 749 159 159 THR CA C 61.7 0.05 1 750 159 159 THR CB C 69.6 0.05 1 751 159 159 THR CG2 C 21.3 0.05 1 752 159 159 THR N N 119.2 0.1 1 753 160 160 THR H H 8.45 0.005 1 754 160 160 THR HA H 4.60 0.005 1 755 160 160 THR CA C 59.9 0.2 1 756 160 160 THR CB C 69.6 0.2 5 757 160 160 THR CG2 C 21.3 0.2 5 758 160 160 THR N N 114.5 0.1 1 759 161 161 PRO HA H 4.50 0.01 5 760 161 161 PRO CA C 63.2 0.1 5 761 161 161 PRO CB C 32.2 0.1 5 762 161 161 PRO CG C 27.4 0.1 5 763 162 162 THR H H 8.54 0.005 1 764 162 162 THR HA H 4.40 0.08 5 765 162 162 THR HG2 H 1.22 0.05 5 766 162 162 THR CA C 61.7 0.25 5 767 162 162 THR CB C 69.6 0.2 5 768 162 162 THR CG2 C 21.3 0.3 5 769 162 162 THR N N 115.4 0.1 1 770 163 163 THR H H 8.41 0.005 1 771 163 163 THR HA H 4.40 0.08 5 772 163 163 THR HG2 H 1.22 0.05 5 773 163 163 THR CA C 61.7 0.25 5 774 163 163 THR CB C 69.6 0.2 5 775 163 163 THR CG2 C 21.3 0.3 5 776 163 163 THR N N 116.8 0.1 1 777 164 164 THR H H 8.58 0.005 1 778 164 164 THR HA H 4.41 0.005 1 779 164 164 THR CA C 61.7 0.05 1 780 164 164 THR CB C 69.6 0.05 1 781 164 164 THR CG2 C 21.3 0.05 1 782 165 165 ASP H H 8.50 0.005 1 783 165 165 ASP HA H 4.63 0.005 1 784 165 165 ASP CA C 53.5 0.1 1 785 165 165 ASP CB C 39.3 0.1 5 786 165 165 ASP N N 122.7 0.1 1 787 166 166 ASP H H 8.47 0.005 1 788 166 166 ASP HA H 4.61 0.005 1 789 166 166 ASP CA C 53.5 0.1 1 790 166 166 ASP CB C 39.3 0.1 1 791 166 166 ASP N N 120.1 0.1 1 792 167 167 LEU H H 8.40 0.005 1 793 167 167 LEU HA H 4.29 0.005 1 794 167 167 LEU CA C 55.6 0.05 1 795 167 167 LEU CB C 41.8 0.05 1 796 167 167 LEU CG C 26.9 0.05 1 797 167 167 LEU CD1 C 24.8 0.05 2 798 167 167 LEU CD2 C 23.1 0.05 2 799 167 167 LEU N N 122.5 0.1 1 800 168 168 ASP H H 8.40 0.005 1 801 168 168 ASP HA H 4.60 0.005 1 802 168 168 ASP CA C 53.5 0.05 1 803 168 168 ASP CB C 38.8 0.05 1 804 168 168 ASP N N 120.6 0.1 1 805 169 169 ALA H H 8.23 0.005 1 806 169 169 ALA HA H 4.24 0.005 1 807 169 169 ALA HB H 1.41 0.005 1 808 169 169 ALA CA C 52.4 0.05 1 809 169 169 ALA CB C 18.3 0.05 1 810 169 169 ALA N N 125.5 0.1 1 stop_ save_