data_16586 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of 3F5 heavy chain antibody fragment in its free form ; _BMRB_accession_number 16586 _BMRB_flat_file_name bmr16586.str _Entry_type original _Submission_date 2009-10-27 _Accession_date 2009-10-27 _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 Impagliazzo Antonietta . . 2 Ubbink Marcellus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 181 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-20 update BMRB 'complete entry citation' 2009-11-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 7434 '3F5 PABPN1 peptide complex' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for a PABPN1 aggregation-preventing antibody fragment in OPMD.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20226184 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Impagliazzo Antonietta . . 2 Tepper Armand W. . 3 Verrips Theo C. . 4 Ubbink Marcellus . . 5 'van der Maarel' Silvere M. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 584 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1558 _Page_last 1564 _Year 2010 _Details . loop_ _Keyword VHH stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 3F5_VHH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 3F5 $3F5_VHH stop_ _System_molecular_weight 22000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_3F5_VHH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 3F5_VHH _Molecular_mass . _Mol_thiol_state 'free and disulfide bound' loop_ _Biological_function 'Llama heavy chain antibody selected against PABPN1' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 136 _Mol_residue_sequence ; MAEVQLVESGGGLVQAGGSL RLSCAASGRTFSGYGMGWFR QAPGKEREFVAAISWRGGNT YYADSVKGRFTISRDNAKNT VWLQMNSLKPEDTAVYYCSG FVRTRDDPSRIRNYWGQGTQ VTVSTAAALEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 GLU 4 VAL 5 GLN 6 LEU 7 VAL 8 GLU 9 SER 10 GLY 11 GLY 12 GLY 13 LEU 14 VAL 15 GLN 16 ALA 17 GLY 18 GLY 19 SER 20 LEU 21 ARG 22 LEU 23 SER 24 CYS 25 ALA 26 ALA 27 SER 28 GLY 29 ARG 30 THR 31 PHE 32 SER 33 GLY 34 TYR 35 GLY 36 MET 37 GLY 38 TRP 39 PHE 40 ARG 41 GLN 42 ALA 43 PRO 44 GLY 45 LYS 46 GLU 47 ARG 48 GLU 49 PHE 50 VAL 51 ALA 52 ALA 53 ILE 54 SER 55 TRP 56 ARG 57 GLY 58 GLY 59 ASN 60 THR 61 TYR 62 TYR 63 ALA 64 ASP 65 SER 66 VAL 67 LYS 68 GLY 69 ARG 70 PHE 71 THR 72 ILE 73 SER 74 ARG 75 ASP 76 ASN 77 ALA 78 LYS 79 ASN 80 THR 81 VAL 82 TRP 83 LEU 84 GLN 85 MET 86 ASN 87 SER 88 LEU 89 LYS 90 PRO 91 GLU 92 ASP 93 THR 94 ALA 95 VAL 96 TYR 97 TYR 98 CYS 99 SER 100 GLY 101 PHE 102 VAL 103 ARG 104 THR 105 ARG 106 ASP 107 ASP 108 PRO 109 SER 110 ARG 111 ILE 112 ARG 113 ASN 114 TYR 115 TRP 116 GLY 117 GLN 118 GLY 119 THR 120 GLN 121 VAL 122 THR 123 VAL 124 SER 125 THR 126 ALA 127 ALA 128 ALA 129 LEU 130 GLU 131 HIS 132 HIS 133 HIS 134 HIS 135 HIS 136 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 BMRB 7434 3F5_VHH 100.00 136 100.00 100.00 3.90e-96 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $3F5_VHH 'Lama glama' 9844 Eukaryota Metazoa Lama glama 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 $3F5_VHH 'recombinant technology' . Escherichia coli . pet28 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 3F5 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3F5_VHH 1.6 mM '[U-98% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' NaCl 150 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 3F5 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3F5_VHH 1.6 mM '[U-98% 13C; U-98% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' NaCl 150 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '3F5 free form' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 3F5 _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 2 2 ALA H H 9.051 0.005 1 2 2 2 ALA CA C 51.86 0.07 1 3 2 2 ALA CB C 23.39 0.07 1 4 2 2 ALA N N 119.67 0.05 1 5 3 3 GLU H H 9.06 0.005 1 6 3 3 GLU CA C 58.21 0.07 1 7 3 3 GLU N N 117.81 0.05 1 8 5 5 GLN CA C 54.98 0.07 1 9 5 5 GLN CB C 30.46 0.07 1 10 6 6 LEU H H 8.344 0.005 1 11 6 6 LEU CA C 53.57 0.07 1 12 6 6 LEU CB C 43.27 0.07 1 13 6 6 LEU N N 124.43 0.05 1 14 7 7 VAL H H 8.38 0.005 1 15 7 7 VAL CA C 62.21 0.07 1 16 7 7 VAL CB C 34.63 0.07 1 17 7 7 VAL N N 120.85 0.05 1 18 8 8 GLU H H 9.48 0.005 1 19 8 8 GLU CA C 56.28 0.07 1 20 8 8 GLU CB C 31.33 0.07 1 21 8 8 GLU N N 130.28 0.05 1 22 9 9 SER H H 9.182 0.005 1 23 9 9 SER CA C 57.92 0.07 1 24 9 9 SER CB C 65.56 0.07 1 25 9 9 SER N N 114.96 0.05 1 26 10 10 GLY H H 8.414 0.005 1 27 10 10 GLY CA C 44.74 0.07 1 28 10 10 GLY N N 108.35 0.05 1 29 11 11 GLY H H 7.75 0.005 1 30 11 11 GLY CA C 45.15 0.07 1 31 11 11 GLY N N 105.65 0.05 1 32 12 12 GLY H H 7.566 0.005 1 33 12 12 GLY CA C 44.81 0.07 1 34 12 12 GLY N N 107.13 0.05 1 35 13 13 LEU H H 7.99 0.005 1 36 13 13 LEU CA C 54.17 0.07 1 37 13 13 LEU CB C 43.49 0.07 1 38 13 13 LEU N N 122.89 0.05 1 39 14 14 VAL H H 8.923 0.005 1 40 14 14 VAL CA C 59.49 0.07 1 41 14 14 VAL CB C 35.42 0.07 1 42 14 14 VAL N N 124.27 0.05 1 43 15 15 GLN H H 8.203 0.005 1 44 15 15 GLN CA C 55.05 0.07 1 45 15 15 GLN CB C 29.65 0.07 1 46 15 15 GLN N N 123.45 0.05 1 47 16 16 ALA H H 8.041 0.005 1 48 16 16 ALA CA C 53.74 0.07 1 49 16 16 ALA CB C 17.73 0.07 1 50 16 16 ALA N N 124.35 0.05 1 51 17 17 GLY H H 9.604 0.005 1 52 17 17 GLY CA C 45.01 0.07 1 53 17 17 GLY N N 113.18 0.05 1 54 18 18 GLY H H 8.397 0.005 1 55 18 18 GLY CA C 44.43 0.07 1 56 18 18 GLY N N 109.24 0.05 1 57 19 19 SER H H 7.772 0.005 1 58 19 19 SER CA C 56.33 0.07 1 59 19 19 SER CB C 67.21 0.07 1 60 19 19 SER N N 109.83 0.05 1 61 20 20 LEU H H 8.447 0.005 1 62 20 20 LEU CA C 54.16 0.07 1 63 20 20 LEU CB C 47.56 0.07 1 64 20 20 LEU N N 121.87 0.05 1 65 21 21 ARG H H 8.04 0.005 1 66 21 21 ARG CA C 54.44 0.07 1 67 21 21 ARG CB C 32.56 0.07 1 68 21 21 ARG N N 122.74 0.05 1 69 22 22 LEU H H 8.637 0.005 1 70 22 22 LEU CA C 52.96 0.07 1 71 22 22 LEU CB C 44.04 0.07 1 72 22 22 LEU N N 126.38 0.05 1 73 23 23 SER H H 8.784 0.005 1 74 23 23 SER CA C 56.52 0.07 1 75 23 23 SER CB C 66.43 0.07 1 76 23 23 SER N N 113.77 0.05 1 77 24 24 CYS H H 8.891 0.005 1 78 24 24 CYS CA C 53.6 0.07 1 79 24 24 CYS CB C 41.93 0.07 1 80 24 24 CYS N N 122.44 0.05 1 81 25 25 ALA H H 8.268 0.005 1 82 25 25 ALA CA C 50.2 0.07 1 83 25 25 ALA CB C 21.67 0.07 1 84 25 25 ALA N N 128.58 0.05 1 85 26 26 ALA H H 8.162 0.005 1 86 26 26 ALA CA C 50.28 0.07 1 87 26 26 ALA CB C 19.7 0.07 1 88 26 26 ALA N N 124.66 0.05 1 89 27 27 SER H H 8.441 0.005 1 90 27 27 SER CA C 58.26 0.07 1 91 27 27 SER CB C 64.08 0.07 1 92 27 27 SER N N 117.57 0.05 1 93 28 28 GLY H H 8.303 0.005 1 94 28 28 GLY CA C 44.97 0.07 1 95 28 28 GLY N N 109.62 0.05 1 96 29 29 ARG H H 8.11 0.005 1 97 29 29 ARG CA C 56.71 0.07 1 98 29 29 ARG CB C 30.97 0.07 1 99 29 29 ARG N N 119.02 0.05 1 100 30 30 THR H H 7.805 0.005 1 101 30 30 THR CA C 61.62 0.07 1 102 30 30 THR CB C 70.2 0.07 1 103 30 30 THR N N 112.5 0.05 1 104 37 37 GLY H H 8.911 0.005 1 105 37 37 GLY CA C 45.7 0.07 1 106 37 37 GLY N N 107.17 0.05 1 107 38 38 TRP H H 9.405 0.005 1 108 38 38 TRP CA C 55.55 0.07 1 109 38 38 TRP CB C 33.22 0.07 1 110 38 38 TRP N N 116.36 0.05 1 111 39 39 PHE H H 9.95 0.005 1 112 39 39 PHE CA C 56 0.07 1 113 39 39 PHE N N 122.22 0.05 1 114 40 40 ARG H H 9.834 0.005 1 115 40 40 ARG CA C 53.95 0.07 1 116 40 40 ARG CB C 32.05 0.07 1 117 40 40 ARG N N 117.08 0.05 1 118 41 41 GLN H H 9.39 0.005 1 119 41 41 GLN CA C 55.16 0.07 1 120 41 41 GLN N N 122.39 0.05 1 121 42 42 ALA H H 9.427 0.005 1 122 42 42 ALA CA C 49.84 0.07 1 123 42 42 ALA CB C 18.3 0.07 1 124 43 43 PRO CA C 64.19 0.07 1 125 43 43 PRO CB C 31.39 0.07 1 126 44 44 GLY H H 8.617 0.005 1 127 44 44 GLY CA C 45.68 0.07 1 128 44 44 GLY N N 112.49 0.05 1 129 45 45 LYS H H 7.889 0.005 1 130 45 45 LYS CA C 54.38 0.07 1 131 45 45 LYS CB C 35.38 0.07 1 132 45 45 LYS N N 120.05 0.05 1 133 46 46 GLU H H 8.261 0.005 1 134 46 46 GLU CA C 55.65 0.07 1 135 46 46 GLU CB C 30.44 0.07 1 136 46 46 GLU N N 118.63 0.05 1 137 47 47 ARG H H 8.666 0.005 1 138 47 47 ARG CA C 57.35 0.07 1 139 47 47 ARG CB C 30.22 0.07 1 140 47 47 ARG N N 122.71 0.05 1 141 48 48 GLU H H 9.586 0.005 1 142 48 48 GLU CA C 54.15 0.07 1 143 48 48 GLU CB C 33.54 0.07 1 144 48 48 GLU N N 125.01 0.05 1 145 49 49 PHE H H 8.99 0.005 1 146 49 49 PHE CA C 59.35 0.07 1 147 49 49 PHE N N 125.36 0.05 1 148 50 50 VAL H H 7.416 0.005 1 149 50 50 VAL CA C 63.95 0.07 1 150 50 50 VAL N N 124.85 0.05 1 151 57 57 GLY CA C 45.68 0.07 1 152 58 58 GLY H H 7.58 0.005 1 153 58 58 GLY CA C 46.1 0.07 1 154 58 58 GLY N N 108.2 0.05 1 155 59 59 ASN H H 8.025 0.005 1 156 59 59 ASN CA C 54.08 0.07 1 157 59 59 ASN CB C 38.89 0.07 1 158 59 59 ASN N N 117.55 0.05 1 159 60 60 THR H H 8.096 0.005 1 160 60 60 THR CA C 59.75 0.07 1 161 60 60 THR N N 111.49 0.05 1 162 63 63 ALA CA C 52.13 0.07 1 163 63 63 ALA CB C 19.59 0.07 1 164 64 64 ASP H H 8.978 0.005 1 165 64 64 ASP CA C 58.02 0.07 1 166 64 64 ASP CB C 40.48 0.07 1 167 64 64 ASP N N 123.08 0.05 1 168 65 65 SER H H 8.111 0.005 1 169 65 65 SER CA C 59.9 0.07 1 170 65 65 SER CB C 62.74 0.07 1 171 65 65 SER N N 110.3 0.05 1 172 66 66 VAL H H 7.2 0.005 1 173 66 66 VAL CA C 60.28 0.07 1 174 66 66 VAL CB C 31.62 0.07 1 175 66 66 VAL N N 111.55 0.05 1 176 67 67 LYS H H 7.252 0.005 1 177 67 67 LYS CA C 58.29 0.07 1 178 67 67 LYS CB C 32.21 0.07 1 179 67 67 LYS N N 125.36 0.05 1 180 68 68 GLY H H 9.07 0.005 1 181 68 68 GLY CA C 45.35 0.07 1 182 68 68 GLY N N 115.86 0.05 1 183 69 69 ARG H H 7.659 0.005 1 184 69 69 ARG CA C 57.32 0.07 1 185 69 69 ARG CB C 30.95 0.07 1 186 69 69 ARG N N 117.25 0.05 1 187 70 70 PHE H H 7.575 0.005 1 188 70 70 PHE CA C 52.45 0.07 1 189 70 70 PHE CB C 39.19 0.07 1 190 70 70 PHE N N 119.44 0.05 1 191 71 71 THR H H 8.857 0.005 1 192 71 71 THR CA C 61.12 0.07 1 193 71 71 THR CB C 72.2 0.07 1 194 71 71 THR N N 112.63 0.05 1 195 72 72 ILE H H 9.204 0.005 1 196 72 72 ILE CA C 58.08 0.07 1 197 72 72 ILE CB C 42.25 0.07 1 198 72 72 ILE N N 130.42 0.05 1 199 73 73 SER H H 8.612 0.005 1 200 73 73 SER CA C 57.56 0.07 1 201 73 73 SER CB C 65.71 0.07 1 202 73 73 SER N N 118.82 0.05 1 203 74 74 ARG H H 9.063 0.005 1 204 74 74 ARG CA C 54.43 0.07 1 205 74 74 ARG CB C 33.69 0.07 1 206 74 74 ARG N N 117.45 0.05 1 207 75 75 ASP H H 8.62 0.005 1 208 75 75 ASP CA C 52.98 0.07 1 209 75 75 ASP CB C 43.08 0.07 1 210 75 75 ASP N N 122.81 0.05 1 211 76 76 ASN H H 8.815 0.005 1 212 76 76 ASN CA C 56.11 0.07 1 213 76 76 ASN CB C 38.1 0.07 1 214 76 76 ASN N N 123.14 0.05 1 215 77 77 ALA H H 8.453 0.005 1 216 77 77 ALA CA C 54.12 0.07 1 217 77 77 ALA CB C 18.73 0.07 1 218 77 77 ALA N N 121.98 0.05 1 219 78 78 LYS H H 7.631 0.005 1 220 78 78 LYS CA C 55.28 0.07 1 221 78 78 LYS CB C 33.01 0.07 1 222 78 78 LYS N N 114.62 0.05 1 223 79 79 ASN H H 8.302 0.005 1 224 79 79 ASN CA C 54.17 0.07 1 225 79 79 ASN CB C 38.28 0.07 1 226 79 79 ASN N N 120.94 0.05 1 227 80 80 THR H H 7.466 0.005 1 228 80 80 THR CA C 61.46 0.07 1 229 80 80 THR CB C 73.06 0.07 1 230 80 80 THR N N 110.4 0.05 1 231 81 81 VAL H H 8.818 0.005 1 232 81 81 VAL CA C 59.2 0.07 1 233 81 81 VAL CB C 35.27 0.07 1 234 81 81 VAL N N 123 0.05 1 235 82 82 TRP H H 9.045 0.005 1 236 82 82 TRP CA C 56.67 0.07 1 237 82 82 TRP CB C 32.36 0.07 1 238 82 82 TRP N N 125.12 0.05 1 239 83 83 LEU H H 8.886 0.005 1 240 83 83 LEU CA C 52.9 0.07 1 241 83 83 LEU CB C 43.29 0.07 1 242 83 83 LEU N N 122.62 0.05 1 243 84 84 GLN H H 9.114 0.005 1 244 84 84 GLN CA C 54.9 0.07 1 245 84 84 GLN CB C 28.92 0.07 1 246 84 84 GLN N N 128.39 0.05 1 247 85 85 MET H H 8.775 0.005 1 248 85 85 MET CA C 54.73 0.07 1 249 85 85 MET CB C 34.77 0.07 1 250 85 85 MET N N 127.33 0.05 1 251 86 86 ASN H H 7.516 0.005 1 252 86 86 ASN CA C 51.24 0.07 1 253 86 86 ASN CB C 40.98 0.07 1 254 86 86 ASN N N 119.62 0.05 1 255 87 87 SER H H 8.497 0.005 1 256 87 87 SER CA C 57.61 0.07 1 257 87 87 SER CB C 61.89 0.07 1 258 87 87 SER N N 111.18 0.05 1 259 88 88 LEU H H 8.047 0.005 1 260 88 88 LEU CA C 56.52 0.07 1 261 88 88 LEU CB C 42.69 0.07 1 262 88 88 LEU N N 118.92 0.05 1 263 89 89 LYS H H 9.625 0.005 1 264 89 89 LYS CA C 53.3 0.07 1 265 89 89 LYS CB C 33.94 0.07 1 266 89 89 LYS N N 122.48 0.05 1 267 90 90 PRO CA C 66.28 0.07 1 268 91 91 GLU H H 9.331 0.005 1 269 91 91 GLU CA C 58.77 0.07 1 270 91 91 GLU CB C 28.35 0.07 1 271 91 91 GLU N N 115.41 0.05 1 272 92 92 ASP H H 8.657 0.005 1 273 92 92 ASP CA C 55.08 0.07 1 274 92 92 ASP CB C 41.99 0.07 1 275 92 92 ASP N N 118.35 0.05 1 276 93 93 THR H H 7.86 0.005 1 277 93 93 THR CA C 65.02 0.07 1 278 93 93 THR CB C 69.89 0.07 1 279 93 93 THR N N 120.58 0.05 1 280 94 94 ALA H H 9.111 0.005 1 281 94 94 ALA CA C 52.58 0.07 1 282 94 94 ALA CB C 21.39 0.07 1 283 94 94 ALA N N 128.29 0.05 1 284 95 95 VAL H H 7.599 0.005 1 285 95 95 VAL CA C 63.02 0.07 1 286 95 95 VAL CB C 31.75 0.07 1 287 95 95 VAL N N 118.29 0.05 1 288 96 96 TYR H H 9.238 0.005 1 289 96 96 TYR CA C 57.96 0.07 1 290 96 96 TYR CB C 40.23 0.07 1 291 96 96 TYR N N 128.29 0.05 1 292 97 97 TYR H H 9.574 0.005 1 293 97 97 TYR CA C 56.64 0.07 1 294 97 97 TYR CB C 42.92 0.07 1 295 97 97 TYR N N 119.96 0.05 1 296 98 98 CYS H H 8.447 0.005 1 297 98 98 CYS CA C 58.1 0.07 1 298 98 98 CYS N N 121.85 0.05 1 299 102 102 VAL H H 8.065 0.005 1 300 102 102 VAL CA C 62.08 0.07 1 301 102 102 VAL CB C 32.62 0.07 1 302 102 102 VAL N N 121.76 0.05 1 303 103 103 ARG H H 8.297 0.005 1 304 103 103 ARG CA C 56.5 0.07 1 305 103 103 ARG N N 123.44 0.05 1 306 104 104 THR CA C 61.87 0.07 1 307 104 104 THR CB C 70.07 0.07 1 308 108 108 PRO CA C 64.16 0.07 1 309 109 109 SER H H 8.26 0.005 1 310 109 109 SER CA C 59.52 0.07 1 311 109 109 SER CB C 63.76 0.07 1 312 109 109 SER N N 113.77 0.05 1 313 116 116 GLY H H 8.794 0.005 1 314 116 116 GLY CA C 44.73 0.07 1 315 116 116 GLY N N 110.05 0.05 1 316 117 117 GLN H H 8.925 0.005 1 317 117 117 GLN CA C 56.99 0.07 1 318 117 117 GLN CB C 30.44 0.07 1 319 117 117 GLN N N 117.79 0.05 1 320 118 118 GLY H H 9.215 0.005 1 321 118 118 GLY CA C 44.32 0.07 1 322 118 118 GLY N N 111.35 0.05 1 323 119 119 THR H H 8.787 0.005 1 324 119 119 THR CA C 60.11 0.07 1 325 119 119 THR CB C 70.81 0.07 1 326 119 119 THR N N 117.55 0.05 1 327 120 120 GLN H H 8.623 0.005 1 328 120 120 GLN CA C 56.92 0.07 1 329 120 120 GLN CB C 29.33 0.07 1 330 120 120 GLN N N 130.74 0.05 1 331 121 121 VAL H H 8.794 0.005 1 332 121 121 VAL CA C 62.14 0.07 1 333 121 121 VAL CB C 33.96 0.07 1 334 121 121 VAL N N 128.5 0.05 1 335 122 122 THR H H 8.506 0.005 1 336 122 122 THR CA C 62 0.07 1 337 122 122 THR CB C 70.4 0.07 1 338 122 122 THR N N 125.12 0.05 1 339 123 123 VAL H H 8.382 0.005 1 340 123 123 VAL CA C 59.96 0.07 1 341 123 123 VAL CB C 31.77 0.07 1 342 123 123 VAL N N 127.89 0.05 1 343 124 124 SER H H 8.579 0.005 1 344 124 124 SER CA C 56.56 0.07 1 345 124 124 SER CB C 65.08 0.07 1 346 124 124 SER N N 121.15 0.05 1 347 125 125 THR H H 8.412 0.005 1 348 125 125 THR CA C 62.14 0.07 1 349 125 125 THR CB C 69.57 0.07 1 350 125 125 THR N N 115.86 0.05 1 351 126 126 ALA H H 8.39 0.005 1 352 126 126 ALA CA C 52.98 0.07 1 353 126 126 ALA CB C 18.99 0.07 1 354 126 126 ALA N N 125.63 0.05 1 355 127 127 ALA H H 8.122 0.005 1 356 127 127 ALA CA C 52.96 0.07 1 357 127 127 ALA CB C 18.89 0.07 1 358 127 127 ALA N N 122.47 0.05 1 359 128 128 ALA H H 8.002 0.005 1 360 128 128 ALA CA C 52.72 0.07 1 361 128 128 ALA CB C 18.9 0.07 1 362 128 128 ALA N N 121.9 0.05 1 363 129 129 LEU H H 7.897 0.005 1 364 129 129 LEU CA C 55.35 0.07 1 365 129 129 LEU CB C 42.14 0.07 1 366 129 129 LEU N N 120.19 0.05 1 367 130 130 GLU H H 8.018 0.005 1 368 130 130 GLU CA C 56.62 0.07 1 369 130 130 GLU CB C 30.11 0.07 1 370 130 130 GLU N N 120.47 0.05 1 stop_ save_