data_15213 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of {lambda}-IntCB bound to a DNA half-site ; _BMRB_accession_number 15213 _BMRB_flat_file_name bmr15213.str _Entry_type original _Submission_date 2007-04-16 _Accession_date 2007-04-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Protein residues 62-176 of lambda-Int, plus DNA duplex: GCTCAAGTTAGTACG' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kamadurai Hari B. . 2 Foster Mark P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 220 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-14 update BMRB 'update DNA residue label to two-letter code' 2009-02-04 update BMRB 'Renumber residue codes in data table' 2008-02-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18001133 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kamadurai Hari B. . 2 Foster Mark P. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 49 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13939 _Page_last 13947 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'IntCB-DNA complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IntCB $Protein DNA $DNA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Protein _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; TLHSWLDRYEKIASRGIKQK TINYMSKIAIRRGLDATTKE IAANGYIDEGKAASKLIRST LSDAFRAEGHITTHVAATRA AKSEVR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 THR 2 3 LEU 3 4 HIS 4 5 SER 5 6 TRP 6 7 LEU 7 8 ASP 8 9 ARG 9 10 TYR 10 11 GLU 11 12 LYS 12 13 ILE 13 15 ALA 14 16 SER 15 17 ARG 16 18 GLY 17 19 ILE 18 20 LYS 19 21 GLN 20 22 LYS 21 23 THR 22 25 ILE 23 26 ASN 24 27 TYR 25 28 MET 26 29 SER 27 30 LYS 28 31 ILE 29 33 ALA 30 34 ILE 31 35 ARG 32 36 ARG 33 37 GLY 34 38 LEU 35 40 ASP 36 41 ALA 37 47 THR 38 48 THR 39 49 LYS 40 50 GLU 41 51 ILE 42 52 ALA 43 53 ALA 44 56 ASN 45 57 GLY 46 58 TYR 47 59 ILE 48 60 ASP 49 61 GLU 50 62 GLY 51 63 LYS 52 64 ALA 53 65 ALA 54 66 SER 55 68 LYS 56 69 LEU 57 70 ILE 58 71 ARG 59 72 SER 60 73 THR 61 74 LEU 62 75 SER 63 76 ASP 64 77 ALA 65 78 PHE 66 79 ARG 67 83 ALA 68 84 GLU 69 85 GLY 70 86 HIS 71 87 ILE 72 88 THR 73 89 THR 74 91 HIS 75 92 VAL 76 93 ALA 77 94 ALA 78 95 THR 79 96 ARG 80 97 ALA 81 98 ALA 82 99 LYS 83 100 SER 84 101 GLU 85 102 VAL 86 103 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_DNA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common DNA _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 15 _Mol_residue_sequence GCTCAAGGGAGTACG loop_ _Residue_seq_code _Residue_label 1 DG 2 DC 3 DT 4 DC 5 DA 6 DA 7 DG 8 DG 9 DG 10 DA 11 DG 12 DT 13 DA 14 DC 15 DG 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 $Protein 'E. coli' 562 Bacteria . Escherichia coli 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 $Protein 'recombinant technology' . Escherichia coli . pT7 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 $Protein 1 mM '[U-99% 13C; U-99% 15N]' $DNA 1 mM 'natural abundance' TSP 0.02 % 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'chemical shift assignment' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_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_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'Referenced 1H to internal TSP, N and C indirectly' 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 '3D CBCA(CO)NH' '3D HNCACB' 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 IntCB _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 1 THR H H 8.47 0.02 1 2 2 1 THR C C 176.4 0.3 1 3 2 1 THR CA C 60.9 0.3 1 4 2 1 THR CB C 69.1 0.3 1 5 2 1 THR N N 118.6 0.3 1 6 3 2 LEU H H 9.06 0.02 1 7 3 2 LEU C C 179.0 0.3 1 8 3 2 LEU CA C 59.2 0.3 1 9 3 2 LEU CB C 41.1 0.3 1 10 3 2 LEU N N 120.3 0.3 1 11 4 3 HIS H H 9.49 0.02 1 12 4 3 HIS C C 178.9 0.3 1 13 4 3 HIS CA C 59.3 0.3 1 14 4 3 HIS CB C 29.5 0.3 1 15 4 3 HIS N N 117.8 0.3 1 16 5 4 SER H H 6.80 0.02 1 17 5 4 SER C C 177.4 0.3 1 18 5 4 SER CA C 61.9 0.3 1 19 5 4 SER CB C 63.0 0.3 1 20 5 4 SER N N 115.2 0.3 1 21 6 5 TRP H H 8.73 0.02 1 22 6 5 TRP C C 177.9 0.3 1 23 6 5 TRP CA C 58.8 0.3 1 24 6 5 TRP CB C 29.5 0.3 1 25 6 5 TRP N N 124.5 0.3 1 26 7 6 LEU H H 8.69 0.02 1 27 7 6 LEU C C 179.3 0.3 1 28 7 6 LEU CA C 58.0 0.3 1 29 7 6 LEU CB C 39.4 0.3 1 30 7 6 LEU N N 119.5 0.3 1 31 8 7 ASP H H 7.42 0.02 1 32 8 7 ASP C C 180.5 0.3 1 33 8 7 ASP CA C 57.6 0.3 1 34 8 7 ASP CB C 39.6 0.3 1 35 8 7 ASP N N 118.7 0.3 1 36 9 8 ARG H H 6.92 0.02 1 37 9 8 ARG C C 175.8 0.3 1 38 9 8 ARG CA C 58.1 0.3 1 39 9 8 ARG CB C 28.3 0.3 1 40 9 8 ARG N N 121.4 0.3 1 41 10 9 TYR H H 8.15 0.02 1 42 10 9 TYR C C 175.9 0.3 1 43 10 9 TYR CA C 54.2 0.3 1 44 10 9 TYR CB C 41.1 0.3 1 45 10 9 TYR N N 120.4 0.3 1 46 11 10 GLU H H 7.29 0.02 1 47 11 10 GLU C C 175.9 0.3 1 48 11 10 GLU CA C 60.1 0.3 1 49 11 10 GLU CB C 38.2 0.3 1 50 11 10 GLU N N 122.9 0.3 1 51 12 11 LYS H H 8.12 0.02 1 52 12 11 LYS C C 181.2 0.3 1 53 12 11 LYS CA C 60.3 0.3 1 54 12 11 LYS CB C 29.7 0.3 1 55 12 11 LYS N N 117.9 0.3 1 56 13 12 ILE H H 6.88 0.02 1 57 13 12 ILE CA C 65.2 0.3 1 58 13 12 ILE N N 118.2 0.3 1 59 15 13 ALA H H 7.28 0.02 1 60 15 13 ALA C C 181.3 0.3 1 61 15 13 ALA CA C 54.3 0.3 1 62 15 13 ALA CB C 17.8 0.3 1 63 15 13 ALA N N 118.2 0.3 1 64 16 14 SER H H 7.70 0.02 1 65 16 14 SER C C 172.7 0.3 1 66 16 14 SER CA C 59.4 0.3 1 67 16 14 SER CB C 63.9 0.3 1 68 16 14 SER N N 113.7 0.3 1 69 17 15 ARG H H 7.54 0.02 1 70 17 15 ARG C C 177.2 0.3 1 71 17 15 ARG CA C 57.7 0.3 1 72 17 15 ARG CB C 31.7 0.3 1 73 17 15 ARG N N 122.3 0.3 1 74 18 16 GLY H H 8.42 0.02 1 75 18 16 GLY C C 173.0 0.3 1 76 18 16 GLY CA C 46.2 0.3 1 77 18 16 GLY N N 109.1 0.3 1 78 19 17 ILE H H 7.22 0.02 1 79 19 17 ILE CA C 60.5 0.3 1 80 19 17 ILE N N 115.1 0.3 1 81 20 18 LYS H H 9.19 0.02 1 82 20 18 LYS C C 178.3 0.3 1 83 20 18 LYS CA C 56.5 0.3 1 84 20 18 LYS CB C 32.8 0.3 1 85 20 18 LYS N N 123.3 0.3 1 86 21 19 GLN H H 8.75 0.02 1 87 21 19 GLN CA C 59.6 0.3 1 88 21 19 GLN CB C 28.0 0.3 1 89 21 19 GLN N N 122.8 0.3 1 90 22 20 LYS H H 8.89 0.02 1 91 22 20 LYS C C 179.7 0.3 1 92 22 20 LYS CA C 59.4 0.3 1 93 22 20 LYS CB C 31.8 0.3 1 94 22 20 LYS N N 117.2 0.3 1 95 23 21 THR H H 6.89 0.02 1 96 23 21 THR CA C 58.3 0.3 1 97 23 21 THR N N 117.8 0.3 1 98 25 22 ILE H H 8.42 0.02 1 99 25 22 ILE C C 180.8 0.3 1 100 25 22 ILE CA C 64.9 0.3 1 101 25 22 ILE CB C 37.5 0.3 1 102 25 22 ILE N N 119.6 0.3 1 103 26 23 ASN H H 7.60 0.02 1 104 26 23 ASN C C 180.9 0.3 1 105 26 23 ASN CA C 56.2 0.3 1 106 26 23 ASN CB C 37.9 0.3 1 107 26 23 ASN N N 120.8 0.3 1 108 27 24 TYR H H 8.50 0.02 1 109 27 24 TYR CA C 60.8 0.3 1 110 27 24 TYR CB C 37.6 0.3 1 111 27 24 TYR N N 121.1 0.3 1 112 28 25 MET H H 9.05 0.02 1 113 28 25 MET C C 181.9 0.3 1 114 28 25 MET CA C 58.2 0.3 1 115 28 25 MET CB C 30.9 0.3 1 116 28 25 MET N N 119.1 0.3 1 117 29 26 SER H H 8.01 0.02 1 118 29 26 SER C C 178.5 0.3 1 119 29 26 SER CA C 61.4 0.3 1 120 29 26 SER CB C 62.8 0.3 1 121 29 26 SER N N 116.3 0.3 1 122 30 27 LYS H H 7.73 0.02 1 123 30 27 LYS C C 182.5 0.3 1 124 30 27 LYS CA C 58.4 0.3 1 125 30 27 LYS CB C 31.5 0.3 1 126 30 27 LYS N N 122.5 0.3 1 127 31 28 ILE H H 7.84 0.02 1 128 31 28 ILE CA C 65.4 0.3 1 129 31 28 ILE N N 124.4 0.3 1 130 33 29 ALA H H 7.37 0.02 1 131 33 29 ALA C C 185.0 0.3 1 132 33 29 ALA CA C 55.2 0.3 1 133 33 29 ALA CB C 17.5 0.3 1 134 33 29 ALA N N 121.5 0.3 1 135 34 30 ILE H H 8.05 0.02 1 136 34 30 ILE C C 176.0 0.3 1 137 34 30 ILE CA C 66.0 0.3 1 138 34 30 ILE CB C 37.3 0.3 1 139 34 30 ILE N N 122.1 0.3 1 140 35 31 ARG H H 8.21 0.02 1 141 35 31 ARG C C 177.8 0.3 1 142 35 31 ARG CA C 59.2 0.3 1 143 35 31 ARG CB C 30.5 0.3 1 144 35 31 ARG N N 118.1 0.3 1 145 36 32 ARG H H 7.48 0.02 1 146 36 32 ARG C C 179.3 0.3 1 147 36 32 ARG CA C 57.6 0.3 1 148 36 32 ARG CB C 30.7 0.3 1 149 36 32 ARG N N 113.3 0.3 1 150 37 33 GLY H H 7.91 0.02 1 151 37 33 GLY C C 168.9 0.3 1 152 37 33 GLY CA C 45.9 0.3 1 153 37 33 GLY N N 106.7 0.3 1 154 38 34 LEU H H 8.19 0.02 1 155 38 34 LEU CA C 51.2 0.3 1 156 38 34 LEU N N 122.2 0.3 1 157 40 35 ASP H H 8.23 0.02 1 158 40 35 ASP C C 173.2 0.3 1 159 40 35 ASP CA C 53.0 0.3 1 160 40 35 ASP CB C 37.9 0.3 1 161 40 35 ASP N N 119.6 0.3 1 162 41 36 ALA H H 7.63 0.02 1 163 41 36 ALA CA C 49.0 0.3 1 164 41 36 ALA N N 125.8 0.3 1 165 47 37 THR H H 8.58 0.02 1 166 47 37 THR C C 173.9 0.3 1 167 47 37 THR CA C 60.2 0.3 1 168 47 37 THR CB C 72.0 0.3 1 169 47 37 THR N N 119.3 0.3 1 170 48 38 THR H H 8.58 0.02 1 171 48 38 THR C C 175.8 0.3 1 172 48 38 THR CA C 66.2 0.3 1 173 48 38 THR CB C 68.4 0.3 1 174 48 38 THR N N 114.6 0.3 1 175 49 39 LYS H H 7.92 0.02 1 176 49 39 LYS C C 181.2 0.3 1 177 49 39 LYS CA C 59.8 0.3 1 178 49 39 LYS CB C 32.4 0.3 1 179 49 39 LYS N N 121.5 0.3 1 180 50 40 GLU H H 7.88 0.02 1 181 50 40 GLU C C 182.2 0.3 1 182 50 40 GLU CA C 59.8 0.3 1 183 50 40 GLU CB C 29.4 0.3 1 184 50 40 GLU N N 120.7 0.3 1 185 51 41 ILE H H 7.88 0.02 1 186 51 41 ILE C C 177.4 0.3 1 187 51 41 ILE CA C 66.0 0.3 1 188 51 41 ILE CB C 38.3 0.3 1 189 51 41 ILE N N 121.5 0.3 1 190 52 42 ALA H H 8.72 0.02 1 191 52 42 ALA C C 184.3 0.3 1 192 52 42 ALA CA C 55.2 0.3 1 193 52 42 ALA CB C 17.5 0.3 1 194 52 42 ALA N N 121.8 0.3 1 195 53 43 ALA H H 7.47 0.02 1 196 53 43 ALA CA C 58.7 0.3 1 197 53 43 ALA N N 119.4 0.3 1 198 56 44 ASN H H 9.22 0.02 1 199 56 44 ASN C C 177.9 0.3 1 200 56 44 ASN CA C 55.6 0.3 1 201 56 44 ASN CB C 37.4 0.3 1 202 56 44 ASN N N 118.7 0.3 1 203 57 45 GLY H H 7.70 0.02 1 204 57 45 GLY C C 175.0 0.3 1 205 57 45 GLY CA C 47.1 0.3 1 206 57 45 GLY N N 107.3 0.3 1 207 58 46 TYR H H 7.20 0.02 1 208 58 46 TYR C C 180.2 0.3 1 209 58 46 TYR CA C 62.0 0.3 1 210 58 46 TYR CB C 38.5 0.3 1 211 58 46 TYR N N 119.1 0.3 1 212 59 47 ILE H H 8.07 0.02 1 213 59 47 ILE C C 183.4 0.3 1 214 59 47 ILE CA C 66.0 0.3 1 215 59 47 ILE N N 122.0 0.3 1 216 60 48 ASP H H 8.94 0.02 1 217 60 48 ASP C C 178.3 0.3 1 218 60 48 ASP CA C 57.0 0.3 1 219 60 48 ASP CB C 40.0 0.3 1 220 60 48 ASP N N 122.5 0.3 1 221 61 49 GLU H H 7.22 0.02 1 222 61 49 GLU C C 175.7 0.3 1 223 61 49 GLU CA C 56.0 0.3 1 224 61 49 GLU CB C 30.1 0.3 1 225 61 49 GLU N N 117.4 0.3 1 226 62 50 GLY H H 8.07 0.02 1 227 62 50 GLY C C 173.6 0.3 1 228 62 50 GLY CA C 45.7 0.3 1 229 62 50 GLY N N 108.5 0.3 1 230 63 51 LYS H H 8.13 0.02 1 231 63 51 LYS C C 176.8 0.3 1 232 63 51 LYS CA C 54.1 0.3 1 233 63 51 LYS N N 122.7 0.3 1 234 64 52 ALA H H 7.92 0.02 1 235 64 52 ALA C C 183.4 0.3 1 236 64 52 ALA CA C 55.5 0.3 1 237 64 52 ALA CB C 18.5 0.3 1 238 64 52 ALA N N 124.4 0.3 1 239 65 53 ALA H H 8.99 0.02 1 240 65 53 ALA C C 184.6 0.3 1 241 65 53 ALA CA C 55.5 0.3 1 242 65 53 ALA CB C 17.6 0.3 1 243 65 53 ALA N N 122.3 0.3 1 244 66 54 SER H H 7.99 0.02 1 245 66 54 SER CA C 62.5 0.3 1 246 66 54 SER N N 115.9 0.3 1 247 68 55 LYS H H 7.77 0.02 1 248 68 55 LYS C C 180.9 0.3 1 249 68 55 LYS CA C 60.0 0.3 1 250 68 55 LYS CB C 32.4 0.3 1 251 68 55 LYS N N 118.0 0.3 1 252 69 56 LEU H H 7.41 0.02 1 253 69 56 LEU C C 184.2 0.3 1 254 69 56 LEU CA C 57.0 0.3 1 255 69 56 LEU CB C 41.8 0.3 1 256 69 56 LEU N N 119.8 0.3 1 257 70 57 ILE H H 8.66 0.02 1 258 70 57 ILE C C 177.1 0.3 1 259 70 57 ILE CA C 66.1 0.3 1 260 70 57 ILE N N 123.8 0.3 1 261 71 58 ARG H H 8.28 0.02 1 262 71 58 ARG C C 178.9 0.3 1 263 71 58 ARG CA C 60.6 0.3 1 264 71 58 ARG CB C 29.3 0.3 1 265 71 58 ARG N N 120.4 0.3 1 266 72 59 SER H H 8.14 0.02 1 267 72 59 SER C C 178.1 0.3 1 268 72 59 SER CA C 62.1 0.3 1 269 72 59 SER N N 114.6 0.3 1 270 73 60 THR H H 8.03 0.02 1 271 73 60 THR C C 173.4 0.3 1 272 73 60 THR CA C 67.4 0.3 1 273 73 60 THR N N 121.8 0.3 1 274 74 61 LEU H H 8.52 0.02 1 275 74 61 LEU C C 178.6 0.3 1 276 74 61 LEU CA C 57.6 0.3 1 277 74 61 LEU CB C 41.5 0.3 1 278 74 61 LEU N N 122.2 0.3 1 279 75 62 SER H H 8.54 0.02 1 280 75 62 SER C C 177.4 0.3 1 281 75 62 SER CA C 61.7 0.3 1 282 75 62 SER CB C 63.0 0.3 1 283 75 62 SER N N 112.7 0.3 1 284 76 63 ASP H H 8.01 0.02 1 285 76 63 ASP C C 178.2 0.3 1 286 76 63 ASP CA C 58.1 0.3 1 287 76 63 ASP N N 121.3 0.3 1 288 77 64 ALA H H 8.49 0.02 1 289 77 64 ALA C C 187.2 0.3 1 290 77 64 ALA CA C 55.6 0.3 1 291 77 64 ALA CB C 16.1 0.3 1 292 77 64 ALA N N 121.3 0.3 1 293 78 65 PHE H H 8.67 0.02 1 294 78 65 PHE C C 180.2 0.3 1 295 78 65 PHE CA C 60.8 0.3 1 296 78 65 PHE N N 120.9 0.3 1 297 79 66 ARG H H 8.79 0.02 1 298 79 66 ARG CA C 60.0 0.3 1 299 79 66 ARG N N 123.3 0.3 1 300 83 67 ALA H H 7.76 0.02 1 301 83 67 ALA C C 182.2 0.3 1 302 83 67 ALA CA C 55.0 0.3 1 303 83 67 ALA CB C 17.5 0.3 1 304 83 67 ALA N N 124.8 0.3 1 305 84 68 GLU H H 7.40 0.02 1 306 84 68 GLU C C 175.1 0.3 1 307 84 68 GLU CA C 56.8 0.3 1 308 84 68 GLU CB C 30.2 0.3 1 309 84 68 GLU N N 115.1 0.3 1 310 85 69 GLY H H 7.62 0.02 1 311 85 69 GLY CA C 45.4 0.3 1 312 85 69 GLY N N 106.7 0.3 1 313 86 70 HIS H H 7.59 0.02 1 314 86 70 HIS C C 172.9 0.3 1 315 86 70 HIS CA C 58.0 0.3 1 316 86 70 HIS CB C 32.4 0.3 1 317 86 70 HIS N N 117.9 0.3 1 318 87 71 ILE H H 7.03 0.02 1 319 87 71 ILE C C 173.3 0.3 1 320 87 71 ILE CA C 59.2 0.3 1 321 87 71 ILE N N 110.6 0.3 1 322 88 72 THR H H 8.56 0.02 1 323 88 72 THR C C 172.2 0.3 1 324 88 72 THR CA C 62.2 0.3 1 325 88 72 THR CB C 70.3 0.3 1 326 88 72 THR N N 110.4 0.3 1 327 89 73 THR H H 7.49 0.02 1 328 89 73 THR CA C 61.6 0.3 1 329 89 73 THR N N 116.6 0.3 1 330 91 74 HIS H H 8.10 0.02 1 331 91 74 HIS C C 175.5 0.3 1 332 91 74 HIS CA C 57.7 0.3 1 333 91 74 HIS CB C 30.7 0.3 1 334 91 74 HIS N N 123.4 0.3 1 335 92 75 VAL H H 7.98 0.02 1 336 92 75 VAL C C 176.7 0.3 1 337 92 75 VAL CA C 63.8 0.3 1 338 92 75 VAL CB C 31.0 0.3 1 339 92 75 VAL N N 118.5 0.3 1 340 93 76 ALA H H 7.39 0.02 1 341 93 76 ALA C C 178.2 0.3 1 342 93 76 ALA CA C 53.3 0.3 1 343 93 76 ALA CB C 18.4 0.3 1 344 93 76 ALA N N 124.4 0.3 1 345 94 77 ALA H H 7.70 0.02 1 346 94 77 ALA C C 179.0 0.3 1 347 94 77 ALA CA C 52.4 0.3 1 348 94 77 ALA CB C 19.1 0.3 1 349 94 77 ALA N N 120.8 0.3 1 350 95 78 THR H H 7.88 0.02 1 351 95 78 THR C C 172.2 0.3 1 352 95 78 THR CA C 62.2 0.3 1 353 95 78 THR CB C 70.0 0.3 1 354 95 78 THR N N 113.0 0.3 1 355 96 79 ARG H H 8.28 0.02 1 356 96 79 ARG C C 174.4 0.3 1 357 96 79 ARG CA C 55.8 0.3 1 358 96 79 ARG CB C 31.1 0.3 1 359 96 79 ARG N N 123.7 0.3 1 360 97 80 ALA H H 8.38 0.02 1 361 97 80 ALA C C 176.7 0.3 1 362 97 80 ALA CA C 52.1 0.3 1 363 97 80 ALA CB C 18.9 0.3 1 364 97 80 ALA N N 126.1 0.3 1 365 98 81 ALA H H 8.16 0.02 1 366 98 81 ALA C C 178.0 0.3 1 367 98 81 ALA CA C 52.2 0.3 1 368 98 81 ALA CB C 19.5 0.3 1 369 98 81 ALA N N 124.0 0.3 1 370 99 82 LYS H H 8.33 0.02 1 371 99 82 LYS C C 176.2 0.3 1 372 99 82 LYS CA C 56.3 0.3 1 373 99 82 LYS CB C 33.0 0.3 1 374 99 82 LYS N N 121.3 0.3 1 375 100 83 SER H H 8.33 0.02 1 376 100 83 SER C C 171.8 0.3 1 377 100 83 SER CA C 58.2 0.3 1 378 100 83 SER CB C 63.7 0.3 1 379 100 83 SER N N 117.8 0.3 1 380 101 84 GLU H H 8.45 0.02 1 381 101 84 GLU C C 175.2 0.3 1 382 101 84 GLU CA C 56.3 0.3 1 383 101 84 GLU CB C 30.3 0.3 1 384 101 84 GLU N N 123.8 0.3 1 385 102 85 VAL H H 8.18 0.02 1 386 102 85 VAL C C 173.4 0.3 1 387 102 85 VAL CA C 62.5 0.3 1 388 102 85 VAL CB C 32.4 0.3 1 389 102 85 VAL N N 122.7 0.3 1 390 103 86 ARG H H 7.96 0.02 1 391 103 86 ARG CA C 57.3 0.3 1 392 103 86 ARG N N 109.2 0.3 1 stop_ save_