data_26730 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural and dynamics studies of Pax5 reveal asymmetry in stability and DNA binding by the Paired domain ; _BMRB_accession_number 26730 _BMRB_flat_file_name bmr26730.str _Entry_type original _Submission_date 2016-01-14 _Accession_date 2016-01-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Paired domain (residues 1-149) of Pax5' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Perez-Borrajero Cecilia . . 2 McIntosh Lawrence P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 137 "13C chemical shifts" 431 "15N chemical shifts" 137 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-14 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26731 'Paired domain of Pax5 in complex with DNA' stop_ _Original_release_date 2016-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27067111 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Perez-Borrajero Cecilia . . 2 Okon Mark . . 3 McIntosh Lawrence P. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 428 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2372 _Page_last 2391 _Year 2016 _Details . loop_ _Keyword NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Paired domain of Pax5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Paired domain of Pax5' $Paired_domain_of_Pax5 stop_ _System_molecular_weight 16820 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Transcriptional regulation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Paired_domain_of_Pax5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Paired_domain_of_Pax5 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'DNA binding transcription factor' stop_ _Details 'Residues 1-149 of Pax5 and two non-native N-terminal residues (Gly-His).' ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; GHMDLEKNYPTPRTSRTGHG GVNQLGGVFVNGRPLPDVVR QRIVELAHQGVRPCDISRQL RVSHGCVSKILGRYYETGSI KPGVIGGSKPKVATPKVVEK IAEYKRQNPTMFAWEIRDRL LAERVCDNDTVPSVSSINRI IRTKVQQPPNQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 HIS 3 1 MET 4 2 ASP 5 3 LEU 6 4 GLU 7 5 LYS 8 6 ASN 9 7 TYR 10 8 PRO 11 9 THR 12 10 PRO 13 11 ARG 14 12 THR 15 13 SER 16 14 ARG 17 15 THR 18 16 GLY 19 17 HIS 20 18 GLY 21 19 GLY 22 20 VAL 23 21 ASN 24 22 GLN 25 23 LEU 26 24 GLY 27 25 GLY 28 26 VAL 29 27 PHE 30 28 VAL 31 29 ASN 32 30 GLY 33 31 ARG 34 32 PRO 35 33 LEU 36 34 PRO 37 35 ASP 38 36 VAL 39 37 VAL 40 38 ARG 41 39 GLN 42 40 ARG 43 41 ILE 44 42 VAL 45 43 GLU 46 44 LEU 47 45 ALA 48 46 HIS 49 47 GLN 50 48 GLY 51 49 VAL 52 50 ARG 53 51 PRO 54 52 CYS 55 53 ASP 56 54 ILE 57 55 SER 58 56 ARG 59 57 GLN 60 58 LEU 61 59 ARG 62 60 VAL 63 61 SER 64 62 HIS 65 63 GLY 66 64 CYS 67 65 VAL 68 66 SER 69 67 LYS 70 68 ILE 71 69 LEU 72 70 GLY 73 71 ARG 74 72 TYR 75 73 TYR 76 74 GLU 77 75 THR 78 76 GLY 79 77 SER 80 78 ILE 81 79 LYS 82 80 PRO 83 81 GLY 84 82 VAL 85 83 ILE 86 84 GLY 87 85 GLY 88 86 SER 89 87 LYS 90 88 PRO 91 89 LYS 92 90 VAL 93 91 ALA 94 92 THR 95 93 PRO 96 94 LYS 97 95 VAL 98 96 VAL 99 97 GLU 100 98 LYS 101 99 ILE 102 100 ALA 103 101 GLU 104 102 TYR 105 103 LYS 106 104 ARG 107 105 GLN 108 106 ASN 109 107 PRO 110 108 THR 111 109 MET 112 110 PHE 113 111 ALA 114 112 TRP 115 113 GLU 116 114 ILE 117 115 ARG 118 116 ASP 119 117 ARG 120 118 LEU 121 119 LEU 122 120 ALA 123 121 GLU 124 122 ARG 125 123 VAL 126 124 CYS 127 125 ASP 128 126 ASN 129 127 ASP 130 128 THR 131 129 VAL 132 130 PRO 133 131 SER 134 132 VAL 135 133 SER 136 134 SER 137 135 ILE 138 136 ASN 139 137 ARG 140 138 ILE 141 139 ILE 142 140 ARG 143 141 THR 144 142 LYS 145 143 VAL 146 144 GLN 147 145 GLN 148 146 PRO 149 147 PRO 150 148 ASN 151 149 GLN 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 _Gene_mnemonic $Paired_domain_of_Pax5 Human 9606 Eukaryota Metazoa Homo sapiens Pax5 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 $Paired_domain_of_Pax5 'recombinant technology' . Escherichia coli 'BL21 (lambdaDE3)' pET28-MHL 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 $Paired_domain_of_Pax5 0.35 mM '[U-100% 13C; U-100% 15N]' MES 20 mM 'natural abundance' NaCl 200 mM 'natural abundance' DTT 2 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _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_ save_3D_HN(CO)CA_5 _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 '20 mM MES, 200 mM NaCl, 2 mM DTT, 0.5 mM EDTA' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 . M pH 6.5 . pH pressure 1 . atm temperature 298.15 . 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 $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '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 'Paired domain of Pax5' _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 3 MET H H 8.576 . 1 2 1 3 MET C C 175.7 . 1 3 1 3 MET CA C 55.65 . 1 4 1 3 MET CB C 32.68 . 1 5 1 3 MET N N 121.8 . 1 6 2 4 ASP H H 8.382 . 1 7 2 4 ASP C C 176.2 . 1 8 2 4 ASP CA C 54.6 . 1 9 2 4 ASP CB C 41.04 . 1 10 2 4 ASP N N 121.8 . 1 11 3 5 LEU H H 8.21 . 1 12 3 5 LEU C C 177.6 . 1 13 3 5 LEU CA C 55.57 . 1 14 3 5 LEU CB C 42.29 . 1 15 3 5 LEU N N 122.3 . 1 16 4 6 GLU H H 8.335 . 1 17 4 6 GLU C C 176.6 . 1 18 4 6 GLU CA C 56.88 . 1 19 4 6 GLU CB C 29.98 . 1 20 4 6 GLU N N 120.7 . 1 21 5 7 LYS H H 8.118 . 1 22 5 7 LYS C C 175.9 . 1 23 5 7 LYS CA C 56.33 . 1 24 5 7 LYS CB C 32.88 . 1 25 5 7 LYS N N 121 . 1 26 6 8 ASN H H 8.233 . 1 27 6 8 ASN C C 174.2 . 1 28 6 8 ASN CA C 53.05 . 1 29 6 8 ASN CB C 39.19 . 1 30 6 8 ASN N N 118.8 . 1 31 7 9 TYR H H 8.053 . 1 32 7 9 TYR C C 173.8 . 1 33 7 9 TYR CA C 55.78 . 1 34 7 9 TYR CB C 38.23 . 1 35 7 9 TYR N N 121.5 . 1 36 8 10 PRO C C 176.7 . 1 37 8 10 PRO CA C 63.1 . 1 38 8 10 PRO CB C 31.96 . 1 39 9 11 THR H H 8.216 . 1 40 9 11 THR C C 173 . 1 41 9 11 THR CA C 59.92 . 1 42 9 11 THR CB C 69.84 . 1 43 9 11 THR N N 116.9 . 1 44 10 12 PRO C C 177 . 1 45 10 12 PRO CA C 63.38 . 1 46 10 12 PRO CB C 32.18 . 1 47 11 13 ARG H H 8.529 . 1 48 11 13 ARG C C 176.7 . 1 49 11 13 ARG CA C 56.39 . 1 50 11 13 ARG CB C 30.71 . 1 51 11 13 ARG N N 121.6 . 1 52 12 14 THR H H 8.139 . 1 53 12 14 THR C C 174.5 . 1 54 12 14 THR CA C 61.7 . 1 55 12 14 THR CB C 69.97 . 1 56 12 14 THR N N 114.5 . 1 57 13 15 SER H H 8.351 . 1 58 13 15 SER C C 174.6 . 1 59 13 15 SER CA C 58.37 . 1 60 13 15 SER CB C 63.96 . 1 61 13 15 SER N N 118 . 1 62 14 16 ARG H H 8.482 . 1 63 14 16 ARG C C 176.5 . 1 64 14 16 ARG CA C 56.38 . 1 65 14 16 ARG CB C 30.69 . 1 66 14 16 ARG N N 123.2 . 1 67 15 17 THR H H 8.147 . 1 68 15 17 THR C C 175.1 . 1 69 15 17 THR CA C 61.93 . 1 70 15 17 THR CB C 69.96 . 1 71 15 17 THR N N 114.3 . 1 72 16 18 GLY H H 8.402 . 1 73 16 18 GLY C C 174 . 1 74 16 18 GLY CA C 45.35 . 1 75 16 18 GLY N N 111.1 . 1 76 17 19 HIS H H 8.413 . 1 77 17 19 HIS C C 175.2 . 1 78 17 19 HIS CA C 55.55 . 1 79 17 19 HIS CB C 29.47 . 1 80 17 19 HIS N N 118.4 . 1 81 18 20 GLY H H 8.552 . 1 82 18 20 GLY C C 174.5 . 1 83 18 20 GLY CA C 45.43 . 1 84 18 20 GLY N N 110.3 . 1 85 19 21 GLY H H 8.337 . 1 86 19 21 GLY C C 174.3 . 1 87 19 21 GLY CA C 45.25 . 1 88 19 21 GLY N N 109 . 1 89 20 22 VAL H H 8.091 . 1 90 20 22 VAL C C 176.1 . 1 91 20 22 VAL CA C 62.51 . 1 92 20 22 VAL CB C 32.67 . 1 93 20 22 VAL N N 118.9 . 1 94 21 23 ASN H H 8.565 . 1 95 21 23 ASN C C 175.1 . 1 96 21 23 ASN CA C 53.43 . 1 97 21 23 ASN CB C 38.78 . 1 98 21 23 ASN N N 121.9 . 1 99 22 24 GLN H H 8.339 . 1 100 22 24 GLN C C 175.9 . 1 101 22 24 GLN CA C 56.02 . 1 102 22 24 GLN CB C 29.31 . 1 103 22 24 GLN N N 120.8 . 1 104 23 25 LEU H H 8.305 . 1 105 23 25 LEU C C 177.8 . 1 106 23 25 LEU CA C 55.43 . 1 107 23 25 LEU CB C 42.27 . 1 108 23 25 LEU N N 122.8 . 1 109 24 26 GLY H H 8.392 . 1 110 24 26 GLY C C 174.4 . 1 111 24 26 GLY CA C 45.44 . 1 112 24 26 GLY N N 109.4 . 1 113 25 27 GLY H H 8.218 . 1 114 25 27 GLY C C 173.6 . 1 115 25 27 GLY CA C 45.25 . 1 116 25 27 GLY N N 108.4 . 1 117 26 28 VAL H H 7.931 . 1 118 26 28 VAL C C 175.4 . 1 119 26 28 VAL CA C 62.09 . 1 120 26 28 VAL CB C 32.9 . 1 121 26 28 VAL N N 119 . 1 122 27 29 PHE H H 8.492 . 1 123 27 29 PHE C C 175.7 . 1 124 27 29 PHE CA C 57.3 . 1 125 27 29 PHE CB C 40.34 . 1 126 27 29 PHE N N 124.6 . 1 127 28 30 VAL H H 8.432 . 1 128 28 30 VAL C C 175.8 . 1 129 28 30 VAL CA C 62.04 . 1 130 28 30 VAL CB C 33.47 . 1 131 28 30 VAL N N 121.5 . 1 132 29 31 ASN H H 8.875 . 1 133 29 31 ASN C C 175.6 . 1 134 29 31 ASN CA C 53.88 . 1 135 29 31 ASN CB C 38.37 . 1 136 29 31 ASN N N 123.6 . 1 137 30 32 GLY H H 8.501 . 1 138 30 32 GLY C C 173.6 . 1 139 30 32 GLY CA C 45.44 . 1 140 30 32 GLY N N 106.9 . 1 141 31 33 ARG H H 7.911 . 1 142 31 33 ARG C C 173.5 . 1 143 31 33 ARG CA C 53.49 . 1 144 31 33 ARG CB C 30.7 . 1 145 31 33 ARG N N 120.9 . 1 146 32 34 PRO C C 176.8 . 1 147 32 34 PRO CA C 62.72 . 1 148 32 34 PRO CB C 31.88 . 1 149 33 35 LEU H H 8.42 . 1 150 33 35 LEU C C 175.1 . 1 151 33 35 LEU CA C 52.96 . 1 152 33 35 LEU CB C 42.74 . 1 153 33 35 LEU N N 125 . 1 154 34 36 PRO C C 177.6 . 1 155 34 36 PRO CA C 63.12 . 1 156 34 36 PRO CB C 32.78 . 1 157 35 37 ASP H H 8.863 . 1 158 35 37 ASP C C 178.2 . 1 159 35 37 ASP CA C 57.94 . 1 160 35 37 ASP CB C 40.67 . 1 161 35 37 ASP N N 124.8 . 1 162 36 38 VAL H H 8.43 . 1 163 36 38 VAL C C 177.6 . 1 164 36 38 VAL CA C 65.1 . 1 165 36 38 VAL CB C 31.48 . 1 166 36 38 VAL N N 115.6 . 1 167 37 39 VAL H H 7.14 . 1 168 37 39 VAL C C 177.2 . 1 169 37 39 VAL CA C 65.97 . 1 170 37 39 VAL CB C 31.63 . 1 171 37 39 VAL N N 121.3 . 1 172 38 40 ARG H H 7.641 . 1 173 38 40 ARG C C 177.6 . 1 174 38 40 ARG CA C 60.6 . 1 175 38 40 ARG CB C 29.77 . 1 176 38 40 ARG N N 119.8 . 1 177 39 41 GLN H H 8.289 . 1 178 39 41 GLN C C 178.3 . 1 179 39 41 GLN CA C 58.65 . 1 180 39 41 GLN CB C 28.12 . 1 181 39 41 GLN N N 115.1 . 1 182 40 42 ARG H H 7.722 . 1 183 40 42 ARG C C 177.9 . 1 184 40 42 ARG CA C 58.29 . 1 185 40 42 ARG CB C 30.03 . 1 186 40 42 ARG N N 120.3 . 1 187 41 43 ILE H H 8.119 . 1 188 41 43 ILE C C 176.7 . 1 189 41 43 ILE CA C 66.38 . 1 190 41 43 ILE CB C 38.04 . 1 191 41 43 ILE N N 119.7 . 1 192 42 44 VAL H H 7.369 . 1 193 42 44 VAL C C 178.1 . 1 194 42 44 VAL CA C 66.7 . 1 195 42 44 VAL CB C 31.69 . 1 196 42 44 VAL N N 117.5 . 1 197 43 45 GLU H H 8.318 . 1 198 43 45 GLU C C 179.7 . 1 199 43 45 GLU CA C 59.53 . 1 200 43 45 GLU CB C 29.87 . 1 201 43 45 GLU N N 121.1 . 1 202 44 46 LEU H H 8.531 . 1 203 44 46 LEU C C 179.7 . 1 204 44 46 LEU CA C 57.79 . 1 205 44 46 LEU CB C 41.77 . 1 206 44 46 LEU N N 119.2 . 1 207 45 47 ALA H H 8.209 . 1 208 45 47 ALA C C 182.5 . 1 209 45 47 ALA CA C 55.2 . 1 210 45 47 ALA CB C 18.63 . 1 211 45 47 ALA N N 122.9 . 1 212 46 48 HIS H H 8.463 . 1 213 46 48 HIS C C 176.4 . 1 214 46 48 HIS CA C 58.3 . 1 215 46 48 HIS CB C 28.41 . 1 216 46 48 HIS N N 118.6 . 1 217 47 49 GLN H H 7.793 . 1 218 47 49 GLN C C 176.1 . 1 219 47 49 GLN CA C 56.11 . 1 220 47 49 GLN CB C 28.78 . 1 221 47 49 GLN N N 117.6 . 1 222 48 50 GLY H H 7.913 . 1 223 48 50 GLY C C 174.3 . 1 224 48 50 GLY CA C 45.31 . 1 225 48 50 GLY N N 107.2 . 1 226 49 51 VAL H H 7.777 . 1 227 49 51 VAL C C 176.1 . 1 228 49 51 VAL CA C 63 . 1 229 49 51 VAL CB C 31.15 . 1 230 49 51 VAL N N 123.2 . 1 231 50 52 ARG H H 9.094 . 1 232 50 52 ARG C C 176.8 . 1 233 50 52 ARG CA C 55.36 . 1 234 50 52 ARG CB C 30 . 1 235 50 52 ARG N N 128 . 1 236 51 53 PRO C C 177.9 . 1 237 51 53 PRO CA C 66.9 . 1 238 51 53 PRO CB C 32.04 . 1 239 52 54 CYS H H 8.725 . 1 240 52 54 CYS C C 176 . 1 241 52 54 CYS CA C 60.25 . 1 242 52 54 CYS CB C 26.52 . 1 243 52 54 CYS N N 114.6 . 1 244 53 55 ASP H H 7.445 . 1 245 53 55 ASP C C 178 . 1 246 53 55 ASP CA C 57.01 . 1 247 53 55 ASP CB C 41 . 1 248 53 55 ASP N N 124.6 . 1 249 54 56 ILE H H 8.218 . 1 250 54 56 ILE C C 177.4 . 1 251 54 56 ILE CA C 66.67 . 1 252 54 56 ILE CB C 38.03 . 1 253 54 56 ILE N N 123.5 . 1 254 55 57 SER H H 7.971 . 1 255 55 57 SER C C 176.7 . 1 256 55 57 SER CA C 61.48 . 1 257 55 57 SER CB C 63.14 . 1 258 55 57 SER N N 112 . 1 259 56 58 ARG H H 7.293 . 1 260 56 58 ARG C C 178.8 . 1 261 56 58 ARG CA C 59.06 . 1 262 56 58 ARG CB C 30.62 . 1 263 56 58 ARG N N 118.8 . 1 264 57 59 GLN H H 8.321 . 1 265 57 59 GLN C C 177.9 . 1 266 57 59 GLN CA C 59 . 1 267 57 59 GLN CB C 29.08 . 1 268 57 59 GLN N N 117.6 . 1 269 58 60 LEU H H 8.066 . 1 270 58 60 LEU C C 175.6 . 1 271 58 60 LEU CA C 54.35 . 1 272 58 60 LEU CB C 42.09 . 1 273 58 60 LEU N N 115.2 . 1 274 59 61 ARG H H 7.783 . 1 275 59 61 ARG C C 175.4 . 1 276 59 61 ARG CA C 57.2 . 1 277 59 61 ARG CB C 26.52 . 1 278 59 61 ARG N N 116.6 . 1 279 60 62 VAL H H 7.676 . 1 280 60 62 VAL C C 175.5 . 1 281 60 62 VAL CA C 59.39 . 1 282 60 62 VAL CB C 35.22 . 1 283 60 62 VAL N N 112.1 . 1 284 61 63 SER H H 8.7 . 1 285 61 63 SER C C 175.2 . 1 286 61 63 SER CA C 57.77 . 1 287 61 63 SER CB C 64.81 . 1 288 61 63 SER N N 119.5 . 1 289 62 64 HIS H H 9.145 . 1 290 62 64 HIS C C 178.3 . 1 291 62 64 HIS CA C 59.58 . 1 292 62 64 HIS CB C 30.39 . 1 293 62 64 HIS N N 121.8 . 1 294 63 65 GLY H H 8.816 . 1 295 63 65 GLY C C 175.8 . 1 296 63 65 GLY CA C 47.01 . 1 297 63 65 GLY N N 107.8 . 1 298 64 66 CYS H H 7.829 . 1 299 64 66 CYS C C 176.3 . 1 300 64 66 CYS CA C 62.21 . 1 301 64 66 CYS CB C 26.59 . 1 302 64 66 CYS N N 121.9 . 1 303 65 67 VAL H H 7.647 . 1 304 65 67 VAL C C 177.4 . 1 305 65 67 VAL CA C 67.54 . 1 306 65 67 VAL CB C 31.61 . 1 307 65 67 VAL N N 118.5 . 1 308 66 68 SER H H 8.551 . 1 309 66 68 SER C C 177.2 . 1 310 66 68 SER CA C 62.84 . 1 311 66 68 SER CB C 62.84 . 1 312 66 68 SER N N 113.9 . 1 313 67 69 LYS H H 7.922 . 1 314 67 69 LYS C C 179.1 . 1 315 67 69 LYS CA C 59.16 . 1 316 67 69 LYS CB C 32.46 . 1 317 67 69 LYS N N 122.3 . 1 318 68 70 ILE H H 7.903 . 1 319 68 70 ILE C C 178.3 . 1 320 68 70 ILE CA C 63.19 . 1 321 68 70 ILE CB C 37.21 . 1 322 68 70 ILE N N 119.9 . 1 323 69 71 LEU H H 8.474 . 1 324 69 71 LEU C C 178.7 . 1 325 69 71 LEU CA C 56.78 . 1 326 69 71 LEU CB C 41.08 . 1 327 69 71 LEU N N 118.2 . 1 328 70 72 GLY H H 8.093 . 1 329 70 72 GLY C C 175.2 . 1 330 70 72 GLY CA C 46.78 . 1 331 70 72 GLY N N 106.7 . 1 332 71 73 ARG H H 7.819 . 1 333 71 73 ARG C C 177.2 . 1 334 71 73 ARG CA C 57.13 . 1 335 71 73 ARG CB C 30.15 . 1 336 71 73 ARG N N 119.5 . 1 337 72 74 TYR H H 8.119 . 1 338 72 74 TYR C C 176.4 . 1 339 72 74 TYR CA C 59.63 . 1 340 72 74 TYR CB C 38.88 . 1 341 72 74 TYR N N 119.7 . 1 342 73 75 TYR H H 8.195 . 1 343 73 75 TYR C C 176.3 . 1 344 73 75 TYR CA C 58.87 . 1 345 73 75 TYR CB C 38.68 . 1 346 73 75 TYR N N 119.9 . 1 347 74 76 GLU H H 8.129 . 1 348 74 76 GLU C C 177 . 1 349 74 76 GLU CA C 57.25 . 1 350 74 76 GLU CB C 30.28 . 1 351 74 76 GLU N N 120.8 . 1 352 75 77 THR H H 8.09 . 1 353 75 77 THR C C 175.5 . 1 354 75 77 THR CA C 62.46 . 1 355 75 77 THR CB C 70.31 . 1 356 75 77 THR N N 112.4 . 1 357 76 78 GLY H H 8.396 . 1 358 76 78 GLY C C 174 . 1 359 76 78 GLY CA C 45.52 . 1 360 76 78 GLY N N 111.2 . 1 361 77 79 SER H H 8.108 . 1 362 77 79 SER C C 174.3 . 1 363 77 79 SER CA C 58.25 . 1 364 77 79 SER CB C 64.12 . 1 365 77 79 SER N N 115.2 . 1 366 78 80 ILE H H 8.128 . 1 367 78 80 ILE C C 175.8 . 1 368 78 80 ILE CA C 61.06 . 1 369 78 80 ILE CB C 38.72 . 1 370 78 80 ILE N N 121.7 . 1 371 79 81 LYS H H 8.368 . 1 372 79 81 LYS C C 174.3 . 1 373 79 81 LYS CA C 54.07 . 1 374 79 81 LYS CB C 32.54 . 1 375 79 81 LYS N N 126.6 . 1 376 80 82 PRO C C 177.4 . 1 377 80 82 PRO CA C 63.37 . 1 378 80 82 PRO CB C 32.11 . 1 379 81 83 GLY H H 8.461 . 1 380 81 83 GLY C C 174 . 1 381 81 83 GLY CA C 45.27 . 1 382 81 83 GLY N N 109.3 . 1 383 82 84 VAL H H 7.955 . 1 384 82 84 VAL C C 176.4 . 1 385 82 84 VAL CA C 62.36 . 1 386 82 84 VAL CB C 32.79 . 1 387 82 84 VAL N N 119.7 . 1 388 83 85 ILE H H 8.345 . 1 389 83 85 ILE C C 176.8 . 1 390 83 85 ILE CA C 61.3 . 1 391 83 85 ILE CB C 38.47 . 1 392 83 85 ILE N N 125.3 . 1 393 84 86 GLY H H 8.565 . 1 394 84 86 GLY C C 174.6 . 1 395 84 86 GLY CA C 45.39 . 1 396 84 86 GLY N N 113.8 . 1 397 85 87 GLY H H 8.287 . 1 398 85 87 GLY C C 174.1 . 1 399 85 87 GLY CA C 45.26 . 1 400 85 87 GLY N N 108.9 . 1 401 86 88 SER H H 8.248 . 1 402 86 88 SER C C 174.2 . 1 403 86 88 SER CA C 58.25 . 1 404 86 88 SER CB C 64.06 . 1 405 86 88 SER N N 115.6 . 1 406 87 89 LYS H H 8.378 . 1 407 87 89 LYS C C 174.4 . 1 408 87 89 LYS CA C 54.38 . 1 409 87 89 LYS CB C 32.49 . 1 410 87 89 LYS N N 124.3 . 1 411 88 90 PRO C C 176.7 . 1 412 88 90 PRO CA C 63.1 . 1 413 88 90 PRO CB C 32.17 . 1 414 89 91 LYS H H 8.484 . 1 415 89 91 LYS C C 176.6 . 1 416 89 91 LYS CA C 56.25 . 1 417 89 91 LYS CB C 32.89 . 1 418 89 91 LYS N N 122.4 . 1 419 90 92 VAL H H 8.125 . 1 420 90 92 VAL C C 175.7 . 1 421 90 92 VAL CA C 61.79 . 1 422 90 92 VAL CB C 33.19 . 1 423 90 92 VAL N N 121.2 . 1 424 91 93 ALA H H 8.447 . 1 425 91 93 ALA C C 176.8 . 1 426 91 93 ALA CA C 51.76 . 1 427 91 93 ALA CB C 19.01 . 1 428 91 93 ALA N N 127.9 . 1 429 92 94 THR H H 7.934 . 1 430 92 94 THR C C 173.4 . 1 431 92 94 THR CA C 60.37 . 1 432 92 94 THR CB C 68.51 . 1 433 92 94 THR N N 114.6 . 1 434 93 95 PRO C C 178.5 . 1 435 93 95 PRO CA C 65.73 . 1 436 93 95 PRO CB C 31.86 . 1 437 94 96 LYS H H 8.166 . 1 438 94 96 LYS C C 178.4 . 1 439 94 96 LYS CA C 58.61 . 1 440 94 96 LYS CB C 32.03 . 1 441 94 96 LYS N N 117 . 1 442 95 97 VAL H H 7.5 . 1 443 95 97 VAL C C 177.3 . 1 444 95 97 VAL CA C 66.76 . 1 445 95 97 VAL CB C 31.63 . 1 446 95 97 VAL N N 120.3 . 1 447 96 98 VAL H H 8.036 . 1 448 96 98 VAL C C 177.6 . 1 449 96 98 VAL CA C 67.61 . 1 450 96 98 VAL CB C 31.48 . 1 451 96 98 VAL N N 119.7 . 1 452 97 99 GLU H H 8.015 . 1 453 97 99 GLU C C 179.4 . 1 454 97 99 GLU CA C 58.96 . 1 455 97 99 GLU CB C 29.37 . 1 456 97 99 GLU N N 117.7 . 1 457 98 100 LYS H H 7.662 . 1 458 98 100 LYS C C 176.8 . 1 459 98 100 LYS CA C 57.26 . 1 460 98 100 LYS CB C 30.53 . 1 461 98 100 LYS N N 120.4 . 1 462 99 101 ILE H H 8.135 . 1 463 99 101 ILE C C 177 . 1 464 99 101 ILE CA C 66.66 . 1 465 99 101 ILE CB C 37.62 . 1 466 99 101 ILE N N 118.3 . 1 467 100 102 ALA H H 7.826 . 1 468 100 102 ALA C C 180 . 1 469 100 102 ALA CA C 55.03 . 1 470 100 102 ALA CB C 17.85 . 1 471 100 102 ALA N N 118.9 . 1 472 101 103 GLU H H 7.944 . 1 473 101 103 GLU C C 179.3 . 1 474 101 103 GLU CA C 59.41 . 1 475 101 103 GLU CB C 29.63 . 1 476 101 103 GLU N N 120.3 . 1 477 102 104 TYR H H 8.705 . 1 478 102 104 TYR C C 179.2 . 1 479 102 104 TYR CA C 57.73 . 1 480 102 104 TYR CB C 36.46 . 1 481 102 104 TYR N N 119.5 . 1 482 103 105 LYS H H 8.023 . 1 483 103 105 LYS C C 178 . 1 484 103 105 LYS CA C 56.47 . 1 485 103 105 LYS CB C 32.27 . 1 486 103 105 LYS N N 117.4 . 1 487 104 106 ARG H H 8.064 . 1 488 104 106 ARG C C 178.6 . 1 489 104 106 ARG CA C 59.02 . 1 490 104 106 ARG CB C 30.29 . 1 491 104 106 ARG N N 119.1 . 1 492 105 107 GLN H H 7.719 . 1 493 105 107 GLN C C 176.6 . 1 494 105 107 GLN CA C 57.61 . 1 495 105 107 GLN CB C 29.09 . 1 496 105 107 GLN N N 116.3 . 1 497 106 108 ASN H H 7.962 . 1 498 106 108 ASN C C 172.2 . 1 499 106 108 ASN CA C 50.45 . 1 500 106 108 ASN CB C 39.24 . 1 501 106 108 ASN N N 114.7 . 1 502 107 109 PRO C C 178.6 . 1 503 107 109 PRO CA C 64.99 . 1 504 107 109 PRO CB C 32.62 . 1 505 108 110 THR H H 7.671 . 1 506 108 110 THR C C 175 . 1 507 108 110 THR CA C 60.96 . 1 508 108 110 THR CB C 68.65 . 1 509 108 110 THR N N 107 . 1 510 109 111 MET H H 7.445 . 1 511 109 111 MET C C 175.9 . 1 512 109 111 MET CA C 57.45 . 1 513 109 111 MET CB C 34.19 . 1 514 109 111 MET N N 122.8 . 1 515 110 112 PHE H H 8.944 . 1 516 110 112 PHE C C 178.1 . 1 517 110 112 PHE CA C 57.18 . 1 518 110 112 PHE CB C 40.72 . 1 519 110 112 PHE N N 123 . 1 520 111 113 ALA H H 9.448 . 1 521 111 113 ALA C C 179.8 . 1 522 111 113 ALA CA C 56.3 . 1 523 111 113 ALA CB C 18.94 . 1 524 111 113 ALA N N 124 . 1 525 112 114 TRP H H 8.13 . 1 526 112 114 TRP C C 177.2 . 1 527 112 114 TRP CA C 59.65 . 1 528 112 114 TRP CB C 26.98 . 1 529 112 114 TRP N N 114.2 . 1 530 113 115 GLU H H 6.19 . 1 531 113 115 GLU C C 179.9 . 1 532 113 115 GLU CA C 58.69 . 1 533 113 115 GLU CB C 30.13 . 1 534 113 115 GLU N N 122.2 . 1 535 114 116 ILE H H 7.803 . 1 536 114 116 ILE C C 176.4 . 1 537 114 116 ILE CA C 65.76 . 1 538 114 116 ILE CB C 37.58 . 1 539 114 116 ILE N N 122.3 . 1 540 115 117 ARG H H 8.189 . 1 541 115 117 ARG C C 177.2 . 1 542 115 117 ARG CA C 60.75 . 1 543 115 117 ARG CB C 29.45 . 1 544 115 117 ARG N N 121 . 1 545 116 118 ASP H H 7.767 . 1 546 116 118 ASP C C 179.1 . 1 547 116 118 ASP CA C 57.49 . 1 548 116 118 ASP CB C 40.05 . 1 549 116 118 ASP N N 116.3 . 1 550 117 119 ARG H H 8.064 . 1 551 117 119 ARG C C 177.4 . 1 552 117 119 ARG CA C 59.73 . 1 553 117 119 ARG CB C 29.52 . 1 554 117 119 ARG N N 123.3 . 1 555 118 120 LEU H H 8.545 . 1 556 118 120 LEU C C 180.4 . 1 557 118 120 LEU CA C 58.05 . 1 558 118 120 LEU CB C 42.94 . 1 559 118 120 LEU N N 119.3 . 1 560 119 121 LEU H H 7.387 . 1 561 119 121 LEU C C 181.1 . 1 562 119 121 LEU CA C 57.02 . 1 563 119 121 LEU CB C 42.36 . 1 564 119 121 LEU N N 116.9 . 1 565 120 122 ALA H H 8.733 . 1 566 120 122 ALA C C 180.4 . 1 567 120 122 ALA CA C 55.45 . 1 568 120 122 ALA CB C 18.58 . 1 569 120 122 ALA N N 125.9 . 1 570 121 123 GLU H H 8.544 . 1 571 121 123 GLU C C 175.6 . 1 572 121 123 GLU CA C 56.56 . 1 573 121 123 GLU CB C 29.5 . 1 574 121 123 GLU N N 114 . 1 575 122 124 ARG H H 7.959 . 1 576 122 124 ARG C C 176 . 1 577 122 124 ARG CA C 57.47 . 1 578 122 124 ARG CB C 26.14 . 1 579 122 124 ARG N N 113.9 . 1 580 123 125 VAL H H 8.397 . 1 581 123 125 VAL C C 176.7 . 1 582 123 125 VAL CA C 64.97 . 1 583 123 125 VAL CB C 32.63 . 1 584 123 125 VAL N N 120.2 . 1 585 124 126 CYS H H 7.301 . 1 586 124 126 CYS C C 171.9 . 1 587 124 126 CYS CA C 55.98 . 1 588 124 126 CYS CB C 32.64 . 1 589 124 126 CYS N N 112 . 1 590 125 127 ASP H H 7.69 . 1 591 125 127 ASP C C 176.3 . 1 592 125 127 ASP CA C 52.38 . 1 593 125 127 ASP CB C 42.51 . 1 594 125 127 ASP N N 119.8 . 1 595 126 128 ASN H H 8.656 . 1 596 126 128 ASN C C 176.3 . 1 597 126 128 ASN CA C 56.85 . 1 598 126 128 ASN CB C 38.57 . 1 599 126 128 ASN N N 115.9 . 1 600 127 129 ASP H H 8.468 . 1 601 127 129 ASP C C 177.6 . 1 602 127 129 ASP CA C 55.97 . 1 603 127 129 ASP CB C 41.5 . 1 604 127 129 ASP N N 116.2 . 1 605 128 130 THR H H 7.942 . 1 606 128 130 THR C C 175.1 . 1 607 128 130 THR CA C 61.25 . 1 608 128 130 THR CB C 71.04 . 1 609 128 130 THR N N 109 . 1 610 129 131 VAL H H 7.91 . 1 611 129 131 VAL C C 172.5 . 1 612 129 131 VAL CA C 58.75 . 1 613 129 131 VAL CB C 32.75 . 1 614 129 131 VAL N N 125.1 . 1 615 130 132 PRO C C 175.5 . 1 616 130 132 PRO CA C 62.17 . 1 617 130 132 PRO CB C 31.9 . 1 618 131 133 SER H H 8.467 . 1 619 131 133 SER C C 175.4 . 1 620 131 133 SER CA C 56.98 . 1 621 131 133 SER CB C 65.26 . 1 622 131 133 SER N N 114.5 . 1 623 132 134 VAL H H 9.043 . 1 624 132 134 VAL C C 177.9 . 1 625 132 134 VAL CA C 67.89 . 1 626 132 134 VAL CB C 31.57 . 1 627 132 134 VAL N N 120.7 . 1 628 133 135 SER H H 8.465 . 1 629 133 135 SER C C 177.8 . 1 630 133 135 SER CA C 61.52 . 1 631 133 135 SER CB C 62.44 . 1 632 133 135 SER N N 114.1 . 1 633 134 136 SER H H 8.192 . 1 634 134 136 SER C C 176.6 . 1 635 134 136 SER CA C 61.81 . 1 636 134 136 SER CB C 62.68 . 1 637 134 136 SER N N 120.6 . 1 638 135 137 ILE H H 8.531 . 1 639 135 137 ILE C C 177.5 . 1 640 135 137 ILE CA C 66.38 . 1 641 135 137 ILE CB C 37.99 . 1 642 135 137 ILE N N 122.6 . 1 643 136 138 ASN H H 8.617 . 1 644 136 138 ASN C C 177.4 . 1 645 136 138 ASN CA C 56.34 . 1 646 136 138 ASN CB C 38.26 . 1 647 136 138 ASN N N 118.1 . 1 648 137 139 ARG H H 7.811 . 1 649 137 139 ARG C C 179.1 . 1 650 137 139 ARG CA C 59.73 . 1 651 137 139 ARG CB C 29.84 . 1 652 137 139 ARG N N 119.8 . 1 653 138 140 ILE H H 8.209 . 1 654 138 140 ILE C C 178.5 . 1 655 138 140 ILE CA C 65.17 . 1 656 138 140 ILE CB C 38.32 . 1 657 138 140 ILE N N 122 . 1 658 139 141 ILE H H 8.404 . 1 659 139 141 ILE C C 177.2 . 1 660 139 141 ILE CA C 64.76 . 1 661 139 141 ILE CB C 38.01 . 1 662 139 141 ILE N N 117.3 . 1 663 140 142 ARG H H 7.849 . 1 664 140 142 ARG C C 177.2 . 1 665 140 142 ARG CA C 57.98 . 1 666 140 142 ARG CB C 30.45 . 1 667 140 142 ARG N N 118.6 . 1 668 141 143 THR H H 7.885 . 1 669 141 143 THR C C 175.2 . 1 670 141 143 THR CA C 63.12 . 1 671 141 143 THR CB C 70.48 . 1 672 141 143 THR N N 111.1 . 1 673 142 144 LYS H H 8.363 . 1 674 142 144 LYS C C 176.5 . 1 675 142 144 LYS CA C 56.15 . 1 676 142 144 LYS CB C 33.26 . 1 677 142 144 LYS N N 121.9 . 1 678 143 145 VAL H H 7.875 . 1 679 143 145 VAL C C 175.8 . 1 680 143 145 VAL CA C 62.71 . 1 681 143 145 VAL CB C 32.51 . 1 682 143 145 VAL N N 120.3 . 1 683 144 146 GLN H H 8.412 . 1 684 144 146 GLN C C 175.4 . 1 685 144 146 GLN CA C 55.78 . 1 686 144 146 GLN CB C 29.33 . 1 687 144 146 GLN N N 123.4 . 1 688 145 147 GLN H H 8.381 . 1 689 145 147 GLN C C 173.5 . 1 690 145 147 GLN CA C 53.63 . 1 691 145 147 GLN CB C 29.01 . 1 692 145 147 GLN N N 123.1 . 1 693 147 149 PRO C C 176.7 . 1 694 147 149 PRO CA C 63.03 . 1 695 147 149 PRO CB C 32.05 . 1 696 148 150 ASN H H 8.489 . 1 697 148 150 ASN C C 174.2 . 1 698 148 150 ASN CA C 53.5 . 1 699 148 150 ASN CB C 38.8 . 1 700 148 150 ASN N N 118.4 . 1 701 149 151 GLN H H 7.898 . 1 702 149 151 GLN C C 180.3 . 1 703 149 151 GLN CA C 57.35 . 1 704 149 151 GLN CB C 30.55 . 1 705 149 151 GLN N N 124.9 . 1 stop_ save_