data_26731 ####################### # 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 26731 _BMRB_flat_file_name bmr26731.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 in complex with 25bp dsDNA (CD19-2_Ains)' 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" 135 "13C chemical shifts" 424 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-14 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26730 'Paired domain of Pax5' 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 in complex with DNA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Paired domain of Pax5' $Paired_domain_of_Pax5 DNA_1 $DNA_1 DNA_2 $DNA_2 stop_ _System_molecular_weight . _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_ save_DNA_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common DNA_1 _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'CD19 promoter site' stop_ _Details . _Residue_count 25 _Mol_residue_sequence ; CGGTGGTCACGCCTCAGTGC CCCAT ; loop_ _Residue_seq_code _Residue_label 1 DC 2 DG 3 DG 4 DT 5 DG 6 DG 7 DT 8 DC 9 DA 10 DC 11 DG 12 DC 13 DC 14 DT 15 DC 16 DA 17 DG 18 DT 19 DG 20 DC 21 DC 22 DC 23 DC 24 DA 25 DT stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_DNA_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common DNA_2 _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'CD19 promoter site' stop_ _Details . _Residue_count 25 _Mol_residue_sequence ; GCCACCAGTGCGGAGTCACG GGGTA ; loop_ _Residue_seq_code _Residue_label 1 DG 2 DC 3 DC 4 DA 5 DC 6 DC 7 DA 8 DG 9 DT 10 DG 11 DC 12 DG 13 DG 14 DA 15 DG 16 DT 17 DC 18 DA 19 DC 20 DG 21 DG 22 DG 23 DG 24 DT 25 DA 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 $Paired_domain_of_Pax5 Human 9606 Eukaryota Metazoa . . $DNA_1 . . . . . . $DNA_2 . . . . . . 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' . . . 'BL21 (lambdaDE3)' pET28-MHL $DNA_1 'chemical synthesis' . . . . . $DNA_2 'chemical synthesis' . . . . . 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; U-80% 2H]' $DNA_1 0.35 mM 'natural abundance' $DNA_2 0.35 mM 'natural abundance' MES 20 mM 'natural abundance' NaCl 20 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 'cryoprobe equipped' 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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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, 20 mM NaCl, 2 mM DTT, 0.5 mM EDTA' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . 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 'The chemical shifts have not been corrected for the TROSY effect (850 MHz magnet) or deuteration.' loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '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 C C 175.7 . 1 2 1 3 MET CA C 55.1 . 1 3 1 3 MET CB C 31.75 . 1 4 2 4 ASP H H 8.309 . 1 5 2 4 ASP C C 176.2 . 1 6 2 4 ASP CA C 54.08 . 1 7 2 4 ASP CB C 40.42 . 1 8 2 4 ASP N N 122.1 . 1 9 3 5 LEU H H 8.144 . 1 10 3 5 LEU C C 177.6 . 1 11 3 5 LEU CA C 55.1 . 1 12 3 5 LEU CB C 41.13 . 1 13 3 5 LEU N N 122.7 . 1 14 4 6 GLU H H 8.272 . 1 15 4 6 GLU C C 176.5 . 1 16 4 6 GLU CA C 56.31 . 1 17 4 6 GLU CB C 29.1 . 1 18 4 6 GLU N N 120.8 . 1 19 5 7 LYS H H 8.024 . 1 20 5 7 LYS C C 175.9 . 1 21 5 7 LYS CA C 55.63 . 1 22 5 7 LYS CB C 31.82 . 1 23 5 7 LYS N N 121.5 . 1 24 6 8 ASN H H 8.207 . 1 25 6 8 ASN C C 174.2 . 1 26 6 8 ASN CA C 52.64 . 1 27 6 8 ASN CB C 38.52 . 1 28 6 8 ASN N N 119.4 . 1 29 7 9 TYR H H 8.015 . 1 30 7 9 TYR C C 173.9 . 1 31 7 9 TYR CA C 55.52 . 1 32 7 9 TYR CB C 37.39 . 1 33 7 9 TYR N N 121.8 . 1 34 8 10 PRO C C 176.7 . 1 35 8 10 PRO CA C 62.64 . 1 36 8 10 PRO CB C 31.09 . 1 37 9 11 THR H H 8.155 . 1 38 9 11 THR C C 172.9 . 1 39 9 11 THR CA C 59.39 . 1 40 9 11 THR CB C 69.2 . 1 41 9 11 THR N N 117.3 . 1 42 10 12 PRO C C 177 . 1 43 10 12 PRO CA C 62.81 . 1 44 10 12 PRO CB C 31.36 . 1 45 11 13 ARG H H 8.512 . 1 46 11 13 ARG C C 176.7 . 1 47 11 13 ARG CA C 55.84 . 1 48 11 13 ARG CB C 29.77 . 1 49 11 13 ARG N N 122.3 . 1 50 12 14 THR H H 8.166 . 1 51 12 14 THR C C 174.5 . 1 52 12 14 THR CA C 61.29 . 1 53 12 14 THR CB C 69.18 . 1 54 12 14 THR N N 115.5 . 1 55 13 15 SER H H 8.302 . 1 56 13 15 SER C C 174.5 . 1 57 13 15 SER CA C 57.84 . 1 58 13 15 SER CB C 63.16 . 1 59 13 15 SER N N 118.5 . 1 60 14 16 ARG H H 8.481 . 1 61 14 16 ARG C C 176.4 . 1 62 14 16 ARG CA C 55.78 . 1 63 14 16 ARG CB C 29.62 . 1 64 14 16 ARG N N 123.5 . 1 65 15 17 THR H H 8.079 . 1 66 15 17 THR C C 175.3 . 1 67 15 17 THR CA C 61.35 . 1 68 15 17 THR CB C 69.38 . 1 69 15 17 THR N N 114.6 . 1 70 16 18 GLY H H 8.506 . 1 71 16 18 GLY C C 173.9 . 1 72 16 18 GLY CA C 44.9 . 1 73 16 18 GLY N N 111.3 . 1 74 17 19 HIS H H 8.391 . 1 75 17 19 HIS C C 175.2 . 1 76 17 19 HIS CA C 55.19 . 1 77 17 19 HIS CB C 28.79 . 1 78 17 19 HIS N N 118.5 . 1 79 18 20 GLY H H 8.328 . 1 80 18 20 GLY C C 173.6 . 1 81 18 20 GLY CA C 44.81 . 1 82 18 20 GLY N N 110.4 . 1 83 19 21 GLY H H 7.82 . 1 84 19 21 GLY C C 172 . 1 85 19 21 GLY CA C 44.85 . 1 86 19 21 GLY N N 109.7 . 1 87 20 22 VAL H H 7.757 . 1 88 20 22 VAL C C 177 . 1 89 20 22 VAL CA C 60.07 . 1 90 20 22 VAL CB C 33.27 . 1 91 20 22 VAL N N 120 . 1 92 21 23 ASN H H 9.489 . 1 93 21 23 ASN C C 178.2 . 1 94 21 23 ASN CA C 51.9 . 1 95 21 23 ASN CB C 38.22 . 1 96 21 23 ASN N N 125.2 . 1 97 22 24 GLN H H 9.813 . 1 98 22 24 GLN C C 177.2 . 1 99 22 24 GLN CA C 58.22 . 1 100 22 24 GLN CB C 27.75 . 1 101 22 24 GLN N N 119 . 1 102 23 25 LEU H H 8.024 . 1 103 23 25 LEU C C 176.9 . 1 104 23 25 LEU CA C 54.37 . 1 105 23 25 LEU CB C 40.95 . 1 106 23 25 LEU N N 118.7 . 1 107 24 26 GLY H H 8.132 . 1 108 24 26 GLY C C 175 . 1 109 24 26 GLY CA C 44.8 . 1 110 24 26 GLY N N 108 . 1 111 25 27 GLY H H 8.67 . 1 112 25 27 GLY C C 172.3 . 1 113 25 27 GLY CA C 44.38 . 1 114 25 27 GLY N N 112.7 . 1 115 26 28 VAL H H 8.289 . 1 116 26 28 VAL C C 176.4 . 1 117 26 28 VAL CA C 61.23 . 1 118 26 28 VAL CB C 31.65 . 1 119 26 28 VAL N N 123.1 . 1 120 27 29 PHE H H 8.6 . 1 121 27 29 PHE C C 173 . 1 122 27 29 PHE CA C 54.87 . 1 123 27 29 PHE CB C 41.94 . 1 124 27 29 PHE N N 125.3 . 1 125 28 30 VAL H H 8.254 . 1 126 28 30 VAL C C 176 . 1 127 28 30 VAL CA C 60.83 . 1 128 28 30 VAL CB C 31.53 . 1 129 28 30 VAL N N 122.5 . 1 130 29 31 ASN H H 8.373 . 1 131 29 31 ASN C C 175.9 . 1 132 29 31 ASN CA C 54.28 . 1 133 29 31 ASN CB C 37.42 . 1 134 29 31 ASN N N 127.6 . 1 135 30 32 GLY H H 9.612 . 1 136 30 32 GLY C C 174.7 . 1 137 30 32 GLY CA C 44.59 . 1 138 30 32 GLY N N 115.8 . 1 139 31 33 ARG H H 7.485 . 1 140 31 33 ARG C C 173.2 . 1 141 31 33 ARG CA C 51.44 . 1 142 31 33 ARG CB C 29.16 . 1 143 31 33 ARG N N 117.7 . 1 144 34 36 PRO C C 177.1 . 1 145 34 36 PRO CA C 62.35 . 1 146 34 36 PRO CB C 32.31 . 1 147 35 37 ASP H H 8.811 . 1 148 35 37 ASP C C 177.8 . 1 149 35 37 ASP CA C 57.9 . 1 150 35 37 ASP CB C 39.5 . 1 151 35 37 ASP N N 125.1 . 1 152 36 38 VAL H H 8.454 . 1 153 36 38 VAL C C 177.8 . 1 154 36 38 VAL CA C 64.64 . 1 155 36 38 VAL CB C 30.44 . 1 156 36 38 VAL N N 114.9 . 1 157 37 39 VAL H H 7.067 . 1 158 37 39 VAL C C 177.6 . 1 159 37 39 VAL CA C 65.14 . 1 160 37 39 VAL CB C 30.96 . 1 161 37 39 VAL N N 122 . 1 162 38 40 ARG H H 7.666 . 1 163 38 40 ARG C C 177.6 . 1 164 38 40 ARG CA C 59.88 . 1 165 38 40 ARG N N 119.6 . 1 166 39 41 GLN H H 8.415 . 1 167 39 41 GLN C C 178.2 . 1 168 39 41 GLN CA C 57.85 . 1 169 39 41 GLN CB C 27.34 . 1 170 39 41 GLN N N 115 . 1 171 40 42 ARG H H 7.324 . 1 172 40 42 ARG C C 177.8 . 1 173 40 42 ARG CA C 57.67 . 1 174 40 42 ARG CB C 28.48 . 1 175 40 42 ARG N N 120.7 . 1 176 41 43 ILE H H 7.952 . 1 177 41 43 ILE C C 176.7 . 1 178 41 43 ILE CA C 65.69 . 1 179 41 43 ILE CB C 36.71 . 1 180 41 43 ILE N N 119.9 . 1 181 42 44 VAL H H 6.834 . 1 182 42 44 VAL C C 177.9 . 1 183 42 44 VAL CA C 65.54 . 1 184 42 44 VAL CB C 30.28 . 1 185 42 44 VAL N N 116.3 . 1 186 43 45 GLU H H 8.269 . 1 187 43 45 GLU C C 179.9 . 1 188 43 45 GLU CA C 58.91 . 1 189 43 45 GLU CB C 30.4 . 1 190 43 45 GLU N N 122 . 1 191 44 46 LEU H H 8.469 . 1 192 44 46 LEU C C 179.7 . 1 193 44 46 LEU CA C 57.28 . 1 194 44 46 LEU CB C 40.75 . 1 195 44 46 LEU N N 119.3 . 1 196 45 47 ALA H H 8.062 . 1 197 45 47 ALA C C 182.8 . 1 198 45 47 ALA CA C 54.93 . 1 199 45 47 ALA CB C 17.5 . 1 200 45 47 ALA N N 123.8 . 1 201 46 48 HIS H H 8.502 . 1 202 46 48 HIS C C 176.8 . 1 203 46 48 HIS CA C 57.83 . 1 204 46 48 HIS CB C 28.09 . 1 205 46 48 HIS N N 119.3 . 1 206 47 49 GLN H H 7.69 . 1 207 47 49 GLN C C 176.1 . 1 208 47 49 GLN CA C 55.49 . 1 209 47 49 GLN CB C 27.91 . 1 210 47 49 GLN N N 117.9 . 1 211 48 50 GLY H H 7.913 . 1 212 48 50 GLY C C 174.2 . 1 213 48 50 GLY CA C 44.73 . 1 214 48 50 GLY N N 108 . 1 215 49 51 VAL H H 7.733 . 1 216 49 51 VAL C C 175.8 . 1 217 49 51 VAL CA C 62.39 . 1 218 49 51 VAL CB C 30.15 . 1 219 49 51 VAL N N 124.1 . 1 220 50 52 ARG H H 9.042 . 1 221 50 52 ARG C C 176.4 . 1 222 50 52 ARG CA C 55.03 . 1 223 50 52 ARG CB C 30.14 . 1 224 50 52 ARG N N 128.8 . 1 225 51 53 PRO C C 177.9 . 1 226 51 53 PRO CA C 66.56 . 1 227 51 53 PRO CB C 30.87 . 1 228 52 54 CYS H H 8.988 . 1 229 52 54 CYS C C 175.9 . 1 230 52 54 CYS CA C 58.92 . 1 231 52 54 CYS CB C 27.08 . 1 232 52 54 CYS N N 117 . 1 233 53 55 ASP H H 7.345 . 1 234 53 55 ASP C C 178.4 . 1 235 53 55 ASP CA C 56.65 . 1 236 53 55 ASP CB C 40.47 . 1 237 53 55 ASP N N 125.3 . 1 238 54 56 ILE H H 8.316 . 1 239 54 56 ILE C C 177.5 . 1 240 54 56 ILE CA C 66.37 . 1 241 54 56 ILE CB C 37.02 . 1 242 54 56 ILE N N 124.8 . 1 243 55 57 SER H H 8.374 . 1 244 55 57 SER C C 176.9 . 1 245 55 57 SER CA C 60.48 . 1 246 55 57 SER CB C 62.44 . 1 247 55 57 SER N N 112.4 . 1 248 56 58 ARG H H 7.576 . 1 249 56 58 ARG C C 179.1 . 1 250 56 58 ARG CA C 60 . 1 251 56 58 ARG CB C 30.76 . 1 252 56 58 ARG N N 116.2 . 1 253 57 59 GLN H H 8.436 . 1 254 57 59 GLN C C 178.3 . 1 255 57 59 GLN CA C 58.61 . 1 256 57 59 GLN CB C 28.26 . 1 257 57 59 GLN N N 118.1 . 1 258 58 60 LEU H H 8.198 . 1 259 58 60 LEU C C 175.9 . 1 260 58 60 LEU CA C 53.86 . 1 261 58 60 LEU CB C 40.33 . 1 262 58 60 LEU N N 115.8 . 1 263 59 61 ARG H H 7.855 . 1 264 59 61 ARG C C 174.3 . 1 265 59 61 ARG CA C 56.36 . 1 266 59 61 ARG CB C 24.95 . 1 267 59 61 ARG N N 117.9 . 1 268 60 62 VAL H H 7.896 . 1 269 60 62 VAL C C 174.7 . 1 270 60 62 VAL CA C 59.93 . 1 271 60 62 VAL CB C 35.15 . 1 272 60 62 VAL N N 119.8 . 1 273 61 63 SER H H 9.456 . 1 274 61 63 SER C C 176.8 . 1 275 61 63 SER CA C 59.92 . 1 276 61 63 SER CB C 62.72 . 1 277 61 63 SER N N 124.3 . 1 278 62 64 HIS H H 9.224 . 1 279 62 64 HIS C C 178 . 1 280 62 64 HIS CA C 59.19 . 1 281 62 64 HIS CB C 25.55 . 1 282 62 64 HIS N N 122.6 . 1 283 63 65 GLY H H 9.437 . 1 284 63 65 GLY C C 176.1 . 1 285 63 65 GLY CA C 46.38 . 1 286 63 65 GLY N N 113.7 . 1 287 64 66 CYS H H 7.314 . 1 288 64 66 CYS C C 175.9 . 1 289 64 66 CYS CA C 60.73 . 1 290 64 66 CYS CB C 26.61 . 1 291 64 66 CYS N N 126.2 . 1 292 65 67 VAL H H 7.635 . 1 293 65 67 VAL C C 177.1 . 1 294 65 67 VAL CA C 67.72 . 1 295 65 67 VAL CB C 30.71 . 1 296 65 67 VAL N N 119.4 . 1 297 66 68 SER H H 8.269 . 1 298 66 68 SER C C 177.7 . 1 299 66 68 SER CA C 61.62 . 1 300 66 68 SER CB C 62.84 . 1 301 66 68 SER N N 111.4 . 1 302 67 69 LYS H H 7.303 . 1 303 67 69 LYS C C 179 . 1 304 67 69 LYS CA C 58.82 . 1 305 67 69 LYS CB C 31.39 . 1 306 67 69 LYS N N 122.2 . 1 307 68 70 ILE H H 8.57 . 1 308 68 70 ILE C C 179.8 . 1 309 68 70 ILE CA C 64.75 . 1 310 68 70 ILE CB C 36.68 . 1 311 68 70 ILE N N 120.2 . 1 312 69 71 LEU H H 8.734 . 1 313 69 71 LEU C C 178 . 1 314 69 71 LEU CA C 57.5 . 1 315 69 71 LEU CB C 39.57 . 1 316 69 71 LEU N N 120.7 . 1 317 70 72 GLY H H 8.348 . 1 318 70 72 GLY C C 177.2 . 1 319 70 72 GLY CA C 47.08 . 1 320 70 72 GLY N N 106.9 . 1 321 71 73 ARG H H 8.068 . 1 322 71 73 ARG C C 180.2 . 1 323 71 73 ARG CA C 58.43 . 1 324 71 73 ARG CB C 29.01 . 1 325 71 73 ARG N N 121.1 . 1 326 72 74 TYR H H 8.272 . 1 327 72 74 TYR C C 179.1 . 1 328 72 74 TYR CA C 61.02 . 1 329 72 74 TYR CB C 37.11 . 1 330 72 74 TYR N N 124.8 . 1 331 73 75 TYR H H 8.949 . 1 332 73 75 TYR C C 177.9 . 1 333 73 75 TYR CA C 59.62 . 1 334 73 75 TYR CB C 35.96 . 1 335 73 75 TYR N N 121.4 . 1 336 74 76 GLU H H 7.704 . 1 337 74 76 GLU C C 178.2 . 1 338 74 76 GLU CA C 58.4 . 1 339 74 76 GLU CB C 30.21 . 1 340 74 76 GLU N N 117.1 . 1 341 75 77 THR H H 8.162 . 1 342 75 77 THR C C 176.3 . 1 343 75 77 THR CA C 61.83 . 1 344 75 77 THR CB C 72.58 . 1 345 75 77 THR N N 105.9 . 1 346 76 78 GLY H H 8.68 . 1 347 76 78 GLY C C 173.1 . 1 348 76 78 GLY CA C 45.06 . 1 349 76 78 GLY N N 113.5 . 1 350 77 79 SER H H 7.816 . 1 351 77 79 SER C C 175.6 . 1 352 77 79 SER CA C 55.44 . 1 353 77 79 SER CB C 64.03 . 1 354 77 79 SER N N 113.7 . 1 355 78 80 ILE H H 8.497 . 1 356 78 80 ILE C C 176.1 . 1 357 78 80 ILE CA C 60.17 . 1 358 78 80 ILE CB C 37.94 . 1 359 78 80 ILE N N 119.8 . 1 360 79 81 LYS H H 8.232 . 1 361 79 81 LYS C C 175.7 . 1 362 79 81 LYS CA C 54.65 . 1 363 79 81 LYS CB C 30.73 . 1 364 79 81 LYS N N 124.6 . 1 365 80 82 PRO C C 176 . 1 366 80 82 PRO CA C 61.96 . 1 367 80 82 PRO CB C 31.44 . 1 368 81 83 GLY H H 9.16 . 1 369 81 83 GLY C C 171.5 . 1 370 81 83 GLY CA C 43.9 . 1 371 81 83 GLY N N 108.1 . 1 372 82 84 VAL H H 8.036 . 1 373 82 84 VAL C C 175.9 . 1 374 82 84 VAL CA C 63.54 . 1 375 82 84 VAL CB C 30.39 . 1 376 82 84 VAL N N 119.9 . 1 377 83 85 ILE H H 7.645 . 1 378 83 85 ILE C C 176.7 . 1 379 83 85 ILE CA C 59.72 . 1 380 83 85 ILE CB C 38.87 . 1 381 83 85 ILE N N 129.4 . 1 382 84 86 GLY H H 8.719 . 1 383 84 86 GLY C C 174.3 . 1 384 84 86 GLY CA C 44.51 . 1 385 84 86 GLY N N 114.9 . 1 386 85 87 GLY H H 7.578 . 1 387 85 87 GLY C C 172 . 1 388 85 87 GLY CA C 43.3 . 1 389 85 87 GLY N N 106 . 1 390 86 88 SER H H 7.713 . 1 391 86 88 SER C C 173.3 . 1 392 86 88 SER CA C 56.85 . 1 393 86 88 SER CB C 65.85 . 1 394 86 88 SER N N 110.6 . 1 395 87 89 LYS H H 8.223 . 1 396 87 89 LYS C C 176.7 . 1 397 87 89 LYS CA C 56.89 . 1 398 87 89 LYS CB C 31.29 . 1 399 87 89 LYS N N 119 . 1 400 88 90 PRO C C 176 . 1 401 88 90 PRO CA C 62.92 . 1 402 88 90 PRO CB C 31.54 . 1 403 89 91 LYS H H 8.628 . 1 404 89 91 LYS C C 176.4 . 1 405 89 91 LYS CA C 57.08 . 1 406 89 91 LYS CB C 34.84 . 1 407 89 91 LYS N N 123.5 . 1 408 90 92 VAL H H 8.661 . 1 409 90 92 VAL C C 177.3 . 1 410 90 92 VAL CA C 60.13 . 1 411 90 92 VAL CB C 31.98 . 1 412 90 92 VAL N N 111.7 . 1 413 91 93 ALA H H 8.594 . 1 414 91 93 ALA C C 176.1 . 1 415 91 93 ALA CA C 49.62 . 1 416 91 93 ALA CB C 16.96 . 1 417 91 93 ALA N N 130.4 . 1 418 92 94 THR H H 7.258 . 1 419 92 94 THR C C 173.1 . 1 420 92 94 THR CA C 59.64 . 1 421 92 94 THR CB C 66.74 . 1 422 92 94 THR N N 111.5 . 1 423 93 95 PRO C C 179.1 . 1 424 93 95 PRO CA C 66.2 . 1 425 93 95 PRO CB C 30.89 . 1 426 94 96 LYS H H 8.142 . 1 427 94 96 LYS C C 178.3 . 1 428 94 96 LYS CA C 58.07 . 1 429 94 96 LYS CB C 31.04 . 1 430 94 96 LYS N N 115.9 . 1 431 95 97 VAL H H 7.151 . 1 432 95 97 VAL C C 177.6 . 1 433 95 97 VAL CA C 66.37 . 1 434 95 97 VAL CB C 31.08 . 1 435 95 97 VAL N N 121.1 . 1 436 96 98 VAL H H 8.443 . 1 437 96 98 VAL C C 177.2 . 1 438 96 98 VAL CA C 67.07 . 1 439 96 98 VAL CB C 30.54 . 1 440 96 98 VAL N N 120 . 1 441 97 99 GLU H H 7.888 . 1 442 97 99 GLU C C 179.5 . 1 443 97 99 GLU CA C 58.58 . 1 444 97 99 GLU CB C 28.79 . 1 445 97 99 GLU N N 117.3 . 1 446 98 100 LYS H H 7.553 . 1 447 98 100 LYS C C 176.7 . 1 448 98 100 LYS CA C 56.66 . 1 449 98 100 LYS CB C 29.58 . 1 450 98 100 LYS N N 120.3 . 1 451 99 101 ILE H H 8.238 . 1 452 99 101 ILE C C 177.2 . 1 453 99 101 ILE CA C 66.34 . 1 454 99 101 ILE CB C 36.51 . 1 455 99 101 ILE N N 118.8 . 1 456 100 102 ALA H H 7.967 . 1 457 100 102 ALA C C 179.8 . 1 458 100 102 ALA CA C 54.68 . 1 459 100 102 ALA CB C 17.41 . 1 460 100 102 ALA N N 119.1 . 1 461 101 103 GLU H H 7.817 . 1 462 101 103 GLU C C 179.5 . 1 463 101 103 GLU CA C 58.89 . 1 464 101 103 GLU CB C 28.82 . 1 465 101 103 GLU N N 120.3 . 1 466 102 104 TYR H H 8.741 . 1 467 102 104 TYR C C 179.2 . 1 468 102 104 TYR CA C 56.99 . 1 469 102 104 TYR CB C 35.53 . 1 470 102 104 TYR N N 120 . 1 471 103 105 LYS H H 8.132 . 1 472 103 105 LYS C C 178.3 . 1 473 103 105 LYS CA C 55.94 . 1 474 103 105 LYS CB C 30.96 . 1 475 103 105 LYS N N 117.6 . 1 476 104 106 ARG H H 7.954 . 1 477 104 106 ARG C C 178.6 . 1 478 104 106 ARG CA C 58.39 . 1 479 104 106 ARG CB C 29.17 . 1 480 104 106 ARG N N 118.7 . 1 481 105 107 GLN H H 7.588 . 1 482 105 107 GLN C C 176.7 . 1 483 105 107 GLN CA C 57.16 . 1 484 105 107 GLN CB C 28.2 . 1 485 105 107 GLN N N 117 . 1 486 106 108 ASN H H 7.959 . 1 487 106 108 ASN C C 172 . 1 488 106 108 ASN CA C 50.05 . 1 489 106 108 ASN CB C 38.45 . 1 490 106 108 ASN N N 115 . 1 491 107 109 PRO C C 178.3 . 1 492 107 109 PRO CA C 64.55 . 1 493 107 109 PRO CB C 31.73 . 1 494 108 110 THR H H 7.442 . 1 495 108 110 THR C C 174.8 . 1 496 108 110 THR CA C 60.25 . 1 497 108 110 THR CB C 67.95 . 1 498 108 110 THR N N 105.9 . 1 499 109 111 MET H H 7.225 . 1 500 109 111 MET C C 175.3 . 1 501 109 111 MET CA C 56.25 . 1 502 109 111 MET CB C 32.98 . 1 503 109 111 MET N N 123.2 . 1 504 110 112 PHE H H 8.771 . 1 505 110 112 PHE C C 178.4 . 1 506 110 112 PHE CA C 55.79 . 1 507 110 112 PHE CB C 40.02 . 1 508 110 112 PHE N N 123.5 . 1 509 111 113 ALA H H 9.208 . 1 510 111 113 ALA C C 181.3 . 1 511 111 113 ALA CA C 56.34 . 1 512 111 113 ALA CB C 17.66 . 1 513 111 113 ALA N N 126.2 . 1 514 112 114 TRP H H 9.575 . 1 515 112 114 TRP C C 178.1 . 1 516 112 114 TRP CA C 59.53 . 1 517 112 114 TRP CB C 26.46 . 1 518 112 114 TRP N N 117.1 . 1 519 113 115 GLU H H 6.322 . 1 520 113 115 GLU C C 180.2 . 1 521 113 115 GLU CA C 58.29 . 1 522 113 115 GLU CB C 29.16 . 1 523 113 115 GLU N N 122.7 . 1 524 114 116 ILE H H 7.784 . 1 525 114 116 ILE C C 176.6 . 1 526 114 116 ILE CA C 65.44 . 1 527 114 116 ILE CB C 36.23 . 1 528 114 116 ILE N N 123.7 . 1 529 115 117 ARG H H 8.408 . 1 530 115 117 ARG C C 177.3 . 1 531 115 117 ARG CA C 60.11 . 1 532 115 117 ARG CB C 28.61 . 1 533 115 117 ARG N N 121.8 . 1 534 116 118 ASP H H 7.855 . 1 535 116 118 ASP C C 179.2 . 1 536 116 118 ASP CA C 57 . 1 537 116 118 ASP CB C 39.46 . 1 538 116 118 ASP N N 116.6 . 1 539 117 119 ARG H H 7.996 . 1 540 117 119 ARG C C 177.5 . 1 541 117 119 ARG CA C 59.27 . 1 542 117 119 ARG CB C 28.57 . 1 543 117 119 ARG N N 123.8 . 1 544 118 120 LEU H H 8.589 . 1 545 118 120 LEU C C 180.6 . 1 546 118 120 LEU CA C 57.58 . 1 547 118 120 LEU CB C 41.7 . 1 548 118 120 LEU N N 119.8 . 1 549 119 121 LEU H H 7.358 . 1 550 119 121 LEU C C 181.1 . 1 551 119 121 LEU CA C 56.54 . 1 552 119 121 LEU CB C 41.34 . 1 553 119 121 LEU N N 117.4 . 1 554 120 122 ALA H H 8.721 . 1 555 120 122 ALA C C 180.5 . 1 556 120 122 ALA CA C 54.9 . 1 557 120 122 ALA CB C 17.66 . 1 558 120 122 ALA N N 126.2 . 1 559 121 123 GLU H H 8.521 . 1 560 121 123 GLU C C 175.7 . 1 561 121 123 GLU CA C 56.1 . 1 562 121 123 GLU CB C 28.6 . 1 563 121 123 GLU N N 114.3 . 1 564 122 124 ARG H H 7.909 . 1 565 122 124 ARG C C 176.1 . 1 566 122 124 ARG CA C 56.77 . 1 567 122 124 ARG CB C 25.06 . 1 568 122 124 ARG N N 114.6 . 1 569 123 125 VAL H H 8.327 . 1 570 123 125 VAL C C 176.7 . 1 571 123 125 VAL CA C 64.41 . 1 572 123 125 VAL CB C 31.7 . 1 573 123 125 VAL N N 120.8 . 1 574 124 126 CYS H H 7.256 . 1 575 124 126 CYS C C 172.1 . 1 576 124 126 CYS CA C 55.47 . 1 577 124 126 CYS CB C 31.77 . 1 578 124 126 CYS N N 112.7 . 1 579 125 127 ASP H H 7.692 . 1 580 125 127 ASP C C 176.4 . 1 581 125 127 ASP CA C 52.19 . 1 582 125 127 ASP CB C 41.88 . 1 583 125 127 ASP N N 120.4 . 1 584 126 128 ASN H H 8.634 . 1 585 126 128 ASN C C 176 . 1 586 126 128 ASN CA C 56.39 . 1 587 126 128 ASN CB C 37.85 . 1 588 126 128 ASN N N 116.5 . 1 589 127 129 ASP H H 8.421 . 1 590 127 129 ASP C C 177.1 . 1 591 127 129 ASP CA C 55.03 . 1 592 127 129 ASP CB C 40.54 . 1 593 127 129 ASP N N 115.5 . 1 594 128 130 THR H H 7.699 . 1 595 128 130 THR C C 174.2 . 1 596 128 130 THR CA C 60.28 . 1 597 128 130 THR CB C 70.2 . 1 598 128 130 THR N N 109.3 . 1 599 129 131 VAL H H 7.62 . 1 600 129 131 VAL C C 172.7 . 1 601 129 131 VAL CA C 57.82 . 1 602 129 131 VAL CB C 32.01 . 1 603 129 131 VAL N N 124.3 . 1 604 130 132 PRO C C 175.5 . 1 605 130 132 PRO CA C 61.55 . 1 606 130 132 PRO CB C 31.03 . 1 607 131 133 SER H H 8.047 . 1 608 131 133 SER C C 175.4 . 1 609 131 133 SER CA C 57.84 . 1 610 131 133 SER CB C 65.18 . 1 611 131 133 SER N N 113.8 . 1 612 132 134 VAL H H 9.195 . 1 613 132 134 VAL C C 177.6 . 1 614 132 134 VAL CA C 67.54 . 1 615 132 134 VAL CB C 30.68 . 1 616 132 134 VAL N N 121.8 . 1 617 133 135 SER H H 8.451 . 1 618 133 135 SER C C 178.8 . 1 619 133 135 SER CA C 60.95 . 1 620 133 135 SER CB C 62.42 . 1 621 133 135 SER N N 112.2 . 1 622 134 136 SER H H 8.098 . 1 623 134 136 SER C C 175.4 . 1 624 134 136 SER CA C 61.91 . 1 625 134 136 SER CB C 61.87 . 1 626 134 136 SER N N 118.7 . 1 627 135 137 ILE H H 8.7 . 1 628 135 137 ILE C C 177.2 . 1 629 135 137 ILE CA C 66.21 . 1 630 135 137 ILE CB C 36.53 . 1 631 135 137 ILE N N 124.3 . 1 632 136 138 ASN H H 8.154 . 1 633 136 138 ASN C C 177.7 . 1 634 136 138 ASN CA C 56.57 . 1 635 136 138 ASN CB C 36.81 . 1 636 136 138 ASN N N 117.2 . 1 637 137 139 ARG H H 8.276 . 1 638 137 139 ARG C C 179.4 . 1 639 137 139 ARG CA C 59.67 . 1 640 137 139 ARG CB C 29.38 . 1 641 137 139 ARG N N 123.4 . 1 642 138 140 ILE H H 9.048 . 1 643 138 140 ILE C C 178.4 . 1 644 138 140 ILE CA C 64.56 . 1 645 138 140 ILE CB C 36.94 . 1 646 138 140 ILE N N 124.3 . 1 647 139 141 ILE H H 8.399 . 1 648 139 141 ILE C C 177.7 . 1 649 139 141 ILE CA C 65.57 . 1 650 139 141 ILE CB C 36.89 . 1 651 139 141 ILE N N 122.3 . 1 652 140 142 ARG H H 8.081 . 1 653 140 142 ARG C C 178.2 . 1 654 140 142 ARG CA C 58.77 . 1 655 140 142 ARG CB C 30.22 . 1 656 140 142 ARG N N 115.9 . 1 657 141 143 THR H H 7.884 . 1 658 141 143 THR C C 176.1 . 1 659 141 143 THR CA C 62.64 . 1 660 141 143 THR CB C 70.95 . 1 661 141 143 THR N N 106.8 . 1 662 142 144 LYS H H 8.484 . 1 663 142 144 LYS C C 176.8 . 1 664 142 144 LYS CA C 55.54 . 1 665 142 144 LYS CB C 33.44 . 1 666 142 144 LYS N N 120.1 . 1 667 143 145 VAL H H 7.462 . 1 668 143 145 VAL C C 175.9 . 1 669 143 145 VAL CA C 63.01 . 1 670 143 145 VAL CB C 31.23 . 1 671 143 145 VAL N N 119.8 . 1 672 144 146 GLN H H 8.326 . 1 673 144 146 GLN C C 175.5 . 1 674 144 146 GLN CA C 55.08 . 1 675 144 146 GLN CB C 28.33 . 1 676 144 146 GLN N N 122.3 . 1 677 145 147 GLN H H 8.256 . 1 678 145 147 GLN C C 173.7 . 1 679 145 147 GLN CA C 53.09 . 1 680 145 147 GLN CB C 28.09 . 1 681 145 147 GLN N N 123 . 1 682 147 149 PRO C C 176.7 . 1 683 147 149 PRO CA C 62.5 . 1 684 147 149 PRO CB C 31.18 . 1 685 148 150 ASN H H 8.437 . 1 686 148 150 ASN C C 174.2 . 1 687 148 150 ASN CA C 53.05 . 1 688 148 150 ASN CB C 38.21 . 1 689 148 150 ASN N N 119 . 1 690 149 151 GLN H H 7.861 . 1 691 149 151 GLN C C 180.3 . 1 692 149 151 GLN CA C 56.84 . 1 693 149 151 GLN CB C 29.7 . 1 694 149 151 GLN N N 125.4 . 1 stop_ save_