data_7434 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of 3F5 heavy chain antibody fragment in its free form and in complex with PABPN1 ; _BMRB_accession_number 7434 _BMRB_flat_file_name bmr7434.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" 116 "13C chemical shifts" 228 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-24 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 16586 '3F5 VHH' stop_ _Original_release_date 2009-11-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural insight into the recognition of PABPN1 by the flexible loops of a heavy chain antibody fragment' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Impagliazzo Antonietta . . 2 Tepper Armand . . 3 Verrips Theo C. . 4 Ubbink Marcellus . . 5 'van der Maarel' Silvere M. . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword VHH stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 3F5_PABPN1pept_complex _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 3F5 $3F5_VHH PABPN1pept $PABPN1pept stop_ _System_molecular_weight 22000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Complex between llama heavy chain antibody and a fragment (Leu119-Gln147)of its antigene polyadenylate binding protein nuclear 1 (PABPN1)' 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 2014-12-20 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 16586 3F5_VHH 100.00 136 100.00 100.00 3.90e-96 stop_ save_ save_PABPN1pept _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PABPN1pept _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 32 _Mol_residue_sequence ; AIEDPELEAIKARVREMEEE AEKLKELQNEVK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ILE 3 GLU 4 ASP 5 PRO 6 GLU 7 LEU 8 GLU 9 ALA 10 ILE 11 LYS 12 ALA 13 ARG 14 VAL 15 ARG 16 GLU 17 MET 18 GLU 19 GLU 20 GLU 21 ALA 22 GLU 23 LYS 24 LEU 25 LYS 26 GLU 27 LEU 28 GLN 29 ASN 30 GLU 31 VAL 32 LYS 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 $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+PABPN1 pet' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3F5_VHH 1.6 mM '[U-98% 15N]' $PABPN1pept 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+PABPN1 pet' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3F5_VHH 1.6 mM '[U-98% 13C; U-98% 15N]' $PABPN1pept 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 bound to PABPN1 pept' 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 3 3 GLU CA C 57.22 0.07 1 2 3 3 GLU CB C 30.22 0.07 1 3 4 4 VAL H H 8.003 0.005 1 4 4 4 VAL CA C 62.13 0.07 1 5 4 4 VAL CB C 32.65 0.07 1 6 4 4 VAL N N 129.1 0.05 1 7 5 5 GLN H H 8.401 0.005 1 8 5 5 GLN CA C 54.65 0.07 1 9 5 5 GLN CB C 29.44 0.07 1 10 5 5 GLN N N 125.47 0.05 1 11 6 6 LEU H H 8.508 0.005 1 12 6 6 LEU CA C 53.27 0.07 1 13 6 6 LEU CB C 43.03 0.07 1 14 6 6 LEU N N 124.89 0.05 1 15 7 7 VAL H H 8.391 0.005 1 16 7 7 VAL CA C 62.31 0.07 1 17 7 7 VAL CB C 34.77 0.07 1 18 7 7 VAL N N 120.92 0.05 1 19 8 8 GLU H H 9.498 0.005 1 20 8 8 GLU CA C 56.04 0.07 1 21 8 8 GLU CB C 31.38 0.07 1 22 8 8 GLU N N 130.12 0.05 1 23 9 9 SER H H 9.202 0.005 1 24 9 9 SER CA C 57.91 0.07 1 25 9 9 SER CB C 65.53 0.07 1 26 9 9 SER N N 114.81 0.05 1 27 10 10 GLY H H 8.455 0.005 1 28 10 10 GLY CA C 44.56 0.07 1 29 10 10 GLY N N 108.09 0.05 1 30 11 11 GLY H H 7.817 0.005 1 31 11 11 GLY CA C 45.01 0.07 1 32 11 11 GLY N N 105.66 0.05 1 33 12 12 GLY H H 7.582 0.005 1 34 12 12 GLY CA C 44.69 0.07 1 35 12 12 GLY N N 107.17 0.05 1 36 13 13 LEU H H 8.035 0.005 1 37 13 13 LEU CA C 54.07 0.07 1 38 13 13 LEU CB C 46.27 0.07 1 39 13 13 LEU N N 122.84 0.05 1 40 14 14 VAL H H 8.928 0.005 1 41 14 14 VAL CA C 59.43 0.07 1 42 14 14 VAL CB C 35.38 0.07 1 43 14 14 VAL N N 124.42 0.05 1 44 15 15 GLN H H 8.205 0.005 1 45 15 15 GLN CA C 54.96 0.07 1 46 15 15 GLN CB C 29.61 0.07 1 47 15 15 GLN N N 123.4 0.05 1 48 16 16 ALA H H 8.084 0.005 1 49 16 16 ALA CA C 53.68 0.07 1 50 16 16 ALA CB C 17.66 0.07 1 51 16 16 ALA N N 124.23 0.05 1 52 17 17 GLY H H 9.583 0.005 1 53 17 17 GLY CA C 44.71 0.07 1 54 17 17 GLY N N 113.11 0.05 1 55 18 18 GLY H H 8.419 0.005 1 56 18 18 GLY CA C 44.33 0.07 1 57 18 18 GLY N N 109.37 0.05 1 58 19 19 SER H H 7.811 0.005 1 59 19 19 SER CA C 56.3 0.07 1 60 19 19 SER CB C 67.21 0.07 1 61 19 19 SER N N 109.83 0.05 1 62 20 20 LEU H H 8.435 0.005 1 63 20 20 LEU CA C 54.47 0.07 1 64 20 20 LEU CB C 47.45 0.07 1 65 20 20 LEU N N 121.84 0.05 1 66 21 21 ARG H H 8.095 0.005 1 67 21 21 ARG CA C 54.36 0.07 1 68 21 21 ARG CB C 32.52 0.07 1 69 21 21 ARG N N 123.25 0.05 1 70 22 22 LEU H H 8.661 0.005 1 71 22 22 LEU CA C 52.9 0.07 1 72 22 22 LEU CB C 44.13 0.07 1 73 22 22 LEU N N 126.78 0.05 1 74 23 23 SER H H 8.807 0.005 1 75 23 23 SER CA C 56.52 0.07 1 76 23 23 SER CB C 66.66 0.07 1 77 23 23 SER N N 113.91 0.05 1 78 24 24 CYS H H 8.963 0.005 1 79 24 24 CYS CA C 53.36 0.07 1 80 24 24 CYS CB C 41.93 0.07 1 81 24 24 CYS N N 122.37 0.05 1 82 25 25 ALA H H 8.255 0.005 1 83 25 25 ALA CA C 49.79 0.07 1 84 25 25 ALA CB C 21.74 0.07 1 85 25 25 ALA N N 128.22 0.05 1 86 26 26 ALA H H 8.116 0.005 1 87 26 26 ALA CA C 50 0.07 1 88 26 26 ALA CB C 19.21 0.07 1 89 26 26 ALA N N 124.26 0.05 1 90 27 27 SER H H 8.527 0.005 1 91 27 27 SER CA C 58.1 0.07 1 92 27 27 SER CB C 64.14 0.07 1 93 27 27 SER N N 118.63 0.05 1 94 28 28 GLY H H 8.423 0.005 1 95 28 28 GLY CA C 44.93 0.07 1 96 28 28 GLY N N 109.52 0.05 1 97 29 29 ARG H H 8.049 0.005 1 98 29 29 ARG CA C 56.4 0.07 1 99 29 29 ARG CB C 31.21 0.07 1 100 29 29 ARG N N 119.06 0.05 1 101 30 30 THR H H 7.993 0.005 1 102 30 30 THR CA C 62.04 0.07 1 103 30 30 THR CB C 70.32 0.07 1 104 30 30 THR N N 114 0.05 1 105 31 31 PHE H H 8.704 0.005 1 106 31 31 PHE CA C 58.44 0.07 1 107 31 31 PHE CB C 39.19 0.07 1 108 31 31 PHE N N 126.8 0.05 1 109 32 32 SER H H 8.021 0.005 1 110 32 32 SER CA C 56.46 0.07 1 111 32 32 SER CB C 63.51 0.07 1 112 32 32 SER N N 121.17 0.05 1 113 33 33 GLY CA C 44.81 0.07 1 114 34 34 TYR H H 8.114 0.005 1 115 34 34 TYR CA C 59.27 0.07 1 116 34 34 TYR CB C 39.37 0.07 1 117 34 34 TYR N N 115.66 0.05 1 118 35 35 GLY CA C 45.66 0.07 1 119 36 36 MET H H 8.327 0.005 1 120 36 36 MET CA C 54.34 0.07 1 121 36 36 MET CB C 39.02 0.07 1 122 36 36 MET N N 115.98 0.05 1 123 37 37 GLY H H 9.261 0.005 1 124 37 37 GLY CA C 45.56 0.07 1 125 37 37 GLY N N 106.05 0.07 1 126 38 38 TRP H H 9.544 0.005 1 127 38 38 TRP CA C 55.32 0.07 1 128 38 38 TRP CB C 32.95 0.07 1 129 38 38 TRP N N 116.67 0.05 1 130 39 39 PHE H H 9.909 0.005 1 131 39 39 PHE CA C 55.77 0.07 1 132 39 39 PHE CB C 43.99 0.07 1 133 39 39 PHE N N 122 0.05 1 134 40 40 ARG H H 9.962 0.005 1 135 40 40 ARG CA C 53.89 0.07 1 136 40 40 ARG CB C 31.92 0.07 1 137 40 40 ARG N N 117.69 0.05 1 138 41 41 GLN H H 9.352 0.005 1 139 41 41 GLN CA C 55.1 0.07 1 140 41 41 GLN CB C 32.21 0.07 1 141 41 41 GLN N N 122.13 0.05 1 142 42 42 ALA H H 9.522 0.005 1 143 42 42 ALA CA C 49.7 0.07 1 144 42 42 ALA CB C 18.18 0.07 1 145 43 43 PRO CA C 64.11 0.07 1 146 43 43 PRO CB C 31.32 0.07 1 147 44 44 GLY H H 8.655 0.005 1 148 44 44 GLY CA C 45.61 0.07 1 149 44 44 GLY N N 112.59 0.05 1 150 45 45 LYS H H 7.885 0.005 1 151 45 45 LYS CA C 54.23 0.07 1 152 45 45 LYS CB C 35.22 0.07 1 153 45 45 LYS N N 119.88 0.05 1 154 46 46 GLU H H 8.361 0.005 1 155 46 46 GLU CA C 55.3 0.07 1 156 46 46 GLU CB C 29.86 0.07 1 157 46 46 GLU N N 118.52 0.05 1 158 47 47 ARG H H 8.706 0.005 1 159 47 47 ARG CA C 57.19 0.07 1 160 47 47 ARG CB C 29.96 0.07 1 161 47 47 ARG N N 122.9 0.05 1 162 48 48 GLU H H 9.611 0.005 1 163 48 48 GLU CA C 54.01 0.07 1 164 48 48 GLU CB C 33.45 0.07 1 165 48 48 GLU N N 125.51 0.05 1 166 49 49 PHE H H 9.157 0.005 1 167 49 49 PHE CA C 53.34 0.07 1 168 49 49 PHE CB C 39.45 0.07 1 169 49 49 PHE N N 125.11 0.05 1 170 50 50 VAL H H 7.181 0.005 1 171 50 50 VAL CA C 63.86 0.07 1 172 50 50 VAL CB C 32.21 0.07 1 173 50 50 VAL N N 124.6 0.05 1 174 51 51 ALA H H 6.931 0.005 1 175 51 51 ALA CA C 51.52 0.07 1 176 51 51 ALA CB C 23.4 0.07 1 177 51 51 ALA N N 115.37 0.05 1 178 52 52 ALA H H 9.249 0.005 1 179 52 52 ALA CA C 51.49 0.07 1 180 52 52 ALA CB C 23.65 0.07 1 181 52 52 ALA N N 119.85 0.05 1 182 53 53 ILE H H 8.878 0.005 1 183 53 53 ILE CA C 57.69 0.07 1 184 53 53 ILE CB C 42.85 0.07 1 185 53 53 ILE N N 117.42 0.05 1 186 54 54 SER H H 9.076 0.005 1 187 54 54 SER CA C 58.09 0.07 1 188 54 54 SER CB C 64.66 0.07 1 189 54 54 SER N N 121.56 0.05 1 190 55 55 TRP H H 9.003 0.005 1 191 55 55 TRP CA C 61.04 0.07 1 192 55 55 TRP CB C 31.43 0.07 1 193 55 55 TRP N N 126.17 0.05 1 194 56 56 ARG H H 10.207 0.005 1 195 56 56 ARG CA C 59.4 0.07 1 196 56 56 ARG CB C 28.84 0.07 1 197 56 56 ARG N N 122.24 0.05 1 198 57 57 GLY H H 9.233 0.005 1 199 57 57 GLY CA C 46.04 0.07 1 200 57 57 GLY N N 106.66 0.05 1 201 58 58 GLY H H 7.377 0.005 1 202 58 58 GLY CA C 45.89 0.07 1 203 58 58 GLY N N 109.18 0.05 1 204 59 59 ASN H H 7.748 0.005 1 205 59 59 ASN CA C 53.19 0.07 1 206 59 59 ASN CB C 40.11 0.07 1 207 59 59 ASN N N 116.47 0.05 1 208 60 60 THR H H 8.195 0.005 1 209 60 60 THR CA C 60.76 0.07 1 210 60 60 THR CB C 72.49 0.07 1 211 60 60 THR N N 108.48 0.05 1 212 61 61 TYR H H 7.983 0.005 1 213 61 61 TYR CA C 56.14 0.07 1 214 61 61 TYR CB C 42.47 0.07 1 215 61 61 TYR N N 120.24 0.05 1 216 62 62 TYR H H 8.584 0.005 1 217 62 62 TYR CA C 57.09 0.07 1 218 62 62 TYR CB C 42.49 0.07 1 219 62 62 TYR N N 124.15 0.05 1 220 63 63 ALA H H 7.819 0.005 1 221 63 63 ALA CA C 51.89 0.07 1 222 63 63 ALA CB C 19.57 0.07 1 223 63 63 ALA N N 122.97 0.05 1 224 64 64 ASP H H 8.916 0.005 1 225 64 64 ASP CA C 57.77 0.07 1 226 64 64 ASP CB C 40.22 0.07 1 227 64 64 ASP N N 122.78 0.05 1 228 65 65 SER H H 8.096 0.005 1 229 65 65 SER CA C 59.79 0.07 1 230 65 65 SER CB C 62.64 0.07 1 231 65 65 SER N N 110.59 0.05 1 232 66 66 VAL H H 7.079 0.005 1 233 66 66 VAL CA C 60.28 0.07 1 234 66 66 VAL CB C 31.56 0.07 1 235 66 66 VAL N N 111.3 0.05 1 236 67 67 LYS H H 7.188 0.005 1 237 67 67 LYS CA C 51.22 0.07 1 238 67 67 LYS CB C 32.27 0.05 1 239 67 67 LYS N N 125.17 0.005 1 240 68 68 GLY H H 9.055 0.07 1 241 68 68 GLY CA C 45.23 0.07 1 242 68 68 GLY N N 115.62 0.05 1 243 69 69 ARG H H 7.626 0.005 1 244 69 69 ARG CA C 57.27 0.07 1 245 69 69 ARG CB C 30.99 0.07 1 246 69 69 ARG N N 117.3 0.05 1 247 70 70 PHE H H 7.512 0.005 1 248 70 70 PHE CA C 52.19 0.07 1 249 70 70 PHE CB C 39.12 0.07 1 250 70 70 PHE N N 118.98 0.05 1 251 71 71 THR H H 8.913 0.005 1 252 71 71 THR CA C 60.92 0.07 1 253 71 71 THR CB C 71.97 0.07 1 254 71 71 THR N N 112.68 0.05 1 255 72 72 ILE H H 9.258 0.005 1 256 72 72 ILE CA C 57.9 0.07 1 257 72 72 ILE CB C 42.35 0.07 1 258 72 72 ILE N N 130.83 0.05 1 259 73 73 SER H H 8.593 0.005 1 260 73 73 SER CA C 57.54 0.07 1 261 73 73 SER CB C 65.84 0.07 1 262 73 73 SER N N 118.99 0.05 1 263 74 74 ARG H H 9.534 0.005 1 264 74 74 ARG CA C 54.13 0.07 1 265 74 74 ARG CB C 33.11 0.07 1 266 74 74 ARG N N 116.04 0.05 1 267 75 75 ASP H H 8.715 0.005 1 268 75 75 ASP CA C 52.56 0.07 1 269 75 75 ASP CB C 43.63 0.07 1 270 75 75 ASP N N 122.7 0.05 1 271 76 76 ASN H H 8.75 0.005 1 272 76 76 ASN CA C 56.04 0.07 1 273 76 76 ASN CB C 37.7 0.07 1 274 76 76 ASN N N 122.89 0.05 1 275 77 77 ALA H H 8.533 0.005 1 276 77 77 ALA CA C 54.22 0.07 1 277 77 77 ALA CB C 18.51 0.07 1 278 77 77 ALA N N 122.22 0.05 1 279 78 78 LYS H H 7.632 0.005 1 280 78 78 LYS CA C 55.15 0.07 1 281 78 78 LYS CB C 33.16 0.07 1 282 78 78 LYS N N 114.17 0.05 1 283 79 79 ASN H H 8.343 0.005 1 284 79 79 ASN CA C 54.27 0.07 1 285 79 79 ASN CB C 38.54 0.07 1 286 79 79 ASN N N 121.62 0.05 1 287 80 80 THR H H 7.421 0.005 1 288 80 80 THR CA C 61.61 0.07 1 289 80 80 THR CB C 73.45 0.07 1 290 80 80 THR N N 108.82 0.05 1 291 81 81 VAL H H 8.934 0.005 1 292 81 81 VAL CA C 58.55 0.07 1 293 81 81 VAL CB C 35.66 0.07 1 294 81 81 VAL N N 123.62 0.05 1 295 82 82 TRP H H 9.095 0.005 1 296 82 82 TRP CA C 57.18 0.07 1 297 82 82 TRP CB C 32.37 0.07 1 298 82 82 TRP N N 124.95 0.05 1 299 83 83 LEU H H 8.791 0.005 1 300 83 83 LEU CA C 52.76 0.07 1 301 83 83 LEU CB C 43.16 0.07 1 302 83 83 LEU N N 122.26 0.05 1 303 84 84 GLN H H 9.119 0.005 1 304 84 84 GLN CA C 54.69 0.07 1 305 84 84 GLN CB C 28.83 0.07 1 306 84 84 GLN N N 128.59 0.05 1 307 85 85 MET H H 8.799 0.005 1 308 85 85 MET CA C 54.59 0.07 1 309 85 85 MET CB C 34.62 0.07 1 310 85 85 MET N N 127.58 0.05 1 311 86 86 ASN H H 7.449 0.005 1 312 86 86 ASN CA C 51.09 0.07 1 313 86 86 ASN CB C 40.85 0.07 1 314 86 86 ASN N N 119.56 0.05 1 315 87 87 SER H H 8.544 0.005 1 316 87 87 SER CA C 57.47 0.07 1 317 87 87 SER CB C 61.79 0.07 1 318 87 87 SER N N 111.05 0.05 1 319 88 88 LEU H H 8.017 0.005 1 320 88 88 LEU CA C 56.41 0.07 1 321 88 88 LEU CB C 42.61 0.07 1 322 88 88 LEU N N 118.81 0.05 1 323 89 89 LYS H H 9.621 0.005 1 324 89 89 LYS CA C 53.17 0.07 1 325 89 89 LYS CB C 33.97 0.07 1 326 89 89 LYS N N 122.47 0.05 1 327 90 90 PRO CA C 66.15 0.07 1 328 90 90 PRO CB C 31.53 0.07 1 329 91 91 GLU H H 9.297 0.005 1 330 91 91 GLU CA C 58.61 0.07 1 331 91 91 GLU CB C 28.06 0.07 1 332 91 91 GLU N N 115.28 0.05 1 333 92 92 ASP H H 8.652 0.005 1 334 92 92 ASP CA C 54.96 0.07 1 335 92 92 ASP CB C 41.95 0.07 1 336 92 92 ASP N N 118.28 0.05 1 337 93 93 THR H H 7.851 0.005 1 338 93 93 THR CA C 64.9 0.07 1 339 93 93 THR CB C 69.84 0.07 1 340 93 93 THR N N 120.62 0.05 1 341 94 94 ALA H H 9.114 0.005 1 342 94 94 ALA CA C 52.53 0.07 1 343 94 94 ALA CB C 21.4 0.07 1 344 94 94 ALA N N 128.37 0.05 1 345 95 95 VAL H H 7.585 0.005 1 346 95 95 VAL CA C 62.92 0.07 1 347 95 95 VAL CB C 31.7 0.07 1 348 95 95 VAL N N 118.17 0.05 1 349 96 96 TYR H H 9.253 0.005 1 350 96 96 TYR CA C 57.92 0.07 1 351 96 96 TYR CB C 40.03 0.07 1 352 96 96 TYR N N 128.01 0.05 1 353 97 97 TYR H H 9.662 0.005 1 354 97 97 TYR CA C 56.72 0.07 1 355 97 97 TYR CB C 42.78 0.07 1 356 97 97 TYR N N 120.16 0.05 1 357 98 98 CYS CA C 53.24 0.07 1 358 98 98 CYS CB C 41.96 0.07 1 359 99 99 SER H H 8.58 0.005 1 360 99 99 SER CA C 54.75 0.07 1 361 99 99 SER CB C 67.06 0.07 1 362 99 99 SER N N 116.92 0.05 1 363 100 100 GLY H H 7.773 0.005 1 364 100 100 GLY CA C 43.99 0.07 1 365 100 100 GLY N N 111.91 0.05 1 366 101 101 PHE H H 8.367 0.005 1 367 101 101 PHE CA C 56.56 0.07 1 368 101 101 PHE CB C 39.49 0.07 1 369 101 101 PHE N N 122.76 0.05 1 370 102 102 VAL H H 8.872 0.005 1 371 102 102 VAL CA C 60.03 0.07 1 372 102 102 VAL CB C 35.62 0.07 1 373 102 102 VAL N N 121.26 0.05 1 374 103 103 ARG H H 8.582 0.005 1 375 103 103 ARG CA C 55.93 0.07 1 376 103 103 ARG CB C 30.91 0.07 1 377 103 103 ARG N N 123.17 0.05 1 378 104 104 THR H H 7.912 0.005 1 379 104 104 THR CA C 61.56 0.07 1 380 104 104 THR CB C 70.22 0.07 1 381 104 104 THR N N 112.86 0.05 1 382 105 105 ARG H H 8.672 0.005 1 383 105 105 ARG CA C 58.29 0.07 1 384 105 105 ARG CB C 29.9 0.07 1 385 105 105 ARG N N 122.86 0.05 1 386 106 106 ASP H H 8.257 0.005 1 387 106 106 ASP CA C 54.63 0.07 1 388 106 106 ASP CB C 40.61 0.07 1 389 106 106 ASP N N 115.09 0.05 1 390 107 107 ASP H H 7.16 0.005 1 391 107 107 ASP CA C 51.24 0.07 1 392 107 107 ASP CB C 41.64 0.07 1 393 107 107 ASP N N 116.33 0.05 1 394 108 108 PRO CA C 64.14 0.07 1 395 109 109 SER H H 8.377 0.005 1 396 109 109 SER CA C 63.9 0.07 1 397 109 109 SER N N 113.86 0.05 1 398 110 110 ARG CA C 54.17 0.07 1 399 111 111 ILE H H 8.466 0.005 1 400 111 111 ILE CA C 60.16 0.07 1 401 111 111 ILE N N 120.66 0.05 1 402 112 112 ARG H H 8.877 0.005 1 403 112 112 ARG CA C 53.77 0.07 1 404 112 112 ARG CB C 32.57 0.07 1 405 112 112 ARG N N 124.42 0.05 1 406 113 113 ASN H H 8.283 0.005 1 407 113 113 ASN CA C 52.46 0.07 1 408 113 113 ASN CB C 40.32 0.07 1 409 113 113 ASN N N 117.72 0.05 1 410 114 114 TYR H H 7.752 0.005 1 411 114 114 TYR CA C 56.17 0.07 1 412 114 114 TYR CB C 40.91 0.07 1 413 114 114 TYR N N 118.85 0.05 1 414 115 115 TRP H H 9.183 0.005 1 415 115 115 TRP CA C 57.06 0.07 1 416 115 115 TRP CB C 33.66 0.05 1 417 115 115 TRP N N 123.09 0.005 1 418 116 116 GLY H H 8.74 0.07 1 419 116 116 GLY CA C 44.58 0.07 1 420 116 116 GLY N N 110.06 0.05 1 421 117 117 GLN H H 8.899 0.005 1 422 117 117 GLN CA C 56.88 0.07 1 423 117 117 GLN CB C 29.95 0.05 1 424 117 117 GLN N N 117.58 0.005 1 425 118 118 GLY H H 9.11 0.07 1 426 118 118 GLY CA C 44.36 0.07 1 427 118 118 GLY N N 111.5 0.05 1 428 119 119 THR H H 8.733 0.005 1 429 119 119 THR CA C 60.16 0.07 1 430 119 119 THR CB C 70.84 0.07 1 431 119 119 THR N N 117.94 0.05 1 432 120 120 GLN H H 8.69 0.005 1 433 120 120 GLN CA C 56.8 0.07 1 434 120 120 GLN CB C 29.2 0.07 1 435 120 120 GLN N N 130.78 0.05 1 436 121 121 VAL H H 8.789 0.005 1 437 121 121 VAL CA C 62.03 0.07 1 438 121 121 VAL CB C 33.96 0.07 1 439 121 121 VAL N N 128.65 0.05 1 440 122 122 THR H H 8.513 0.005 1 441 122 122 THR CA C 61.87 0.07 1 442 122 122 THR CB C 70.42 0.07 1 443 122 122 THR N N 125.09 0.05 1 444 123 123 VAL H H 8.39 0.005 1 445 123 123 VAL CA C 59.82 0.07 1 446 123 123 VAL CB C 31.65 0.07 1 447 123 123 VAL N N 127.92 0.05 1 448 124 124 SER H H 8.644 0.005 1 449 124 124 SER CA C 56.73 0.07 1 450 124 124 SER CB C 65.02 0.07 1 451 124 124 SER N N 121.59 0.05 1 452 125 125 THR H H 8.342 0.005 1 453 125 125 THR CA C 61.89 0.07 1 454 125 125 THR CB C 69.46 0.07 1 455 125 125 THR N N 115.09 0.05 1 456 126 126 ALA H H 8.322 0.005 1 457 126 126 ALA CA C 52.21 0.07 1 458 126 126 ALA CB C 19.3 0.07 1 459 126 126 ALA N N 126.24 0.05 1 stop_ save_