data_5200 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N chemical shift assignment of DnaA domain IV ; _BMRB_accession_number 5200 _BMRB_flat_file_name bmr5200.str _Entry_type original _Submission_date 2001-11-04 _Accession_date 2001-11-05 _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 Imoto Taiji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 165 "13C chemical shifts" 274 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-10 original author . stop_ _Original_release_date 2003-06-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Determination of the Secondary Structure in Solution of the Escherichia coli DnaA DNA-binding Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22322782 _PubMed_ID 12435387 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Obita Takayuki . . 2 Iwura Takafumi . . 3 Su'etsugu Masayuki . . 4 Yoshida Yoichiro . . 5 Tanaka Yoshitsugu . . 6 Katayama Tsutomu . . 7 Ueda Tadashi . . 8 Imoto Taiji . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 299 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 42 _Page_last 48 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_DnaA _Saveframe_category molecular_system _Mol_system_name 'DnaA domain IV' _Abbreviation_common DnaA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DnaA domain IV' $DnaA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DnaA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'chromosome replication initiator' _Abbreviation_common 'DnaA domain IV' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; MVTIDNIQKTVAEYYKIKVA DLLSKRRSRSVARPRQMAMA LAKELTNHSLPEIGDAFGGR DHTTVLHACRKIEQLREESH DIKEDFSNLIRTLSS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 THR 4 ILE 5 ASP 6 ASN 7 ILE 8 GLN 9 LYS 10 THR 11 VAL 12 ALA 13 GLU 14 TYR 15 TYR 16 LYS 17 ILE 18 LYS 19 VAL 20 ALA 21 ASP 22 LEU 23 LEU 24 SER 25 LYS 26 ARG 27 ARG 28 SER 29 ARG 30 SER 31 VAL 32 ALA 33 ARG 34 PRO 35 ARG 36 GLN 37 MET 38 ALA 39 MET 40 ALA 41 LEU 42 ALA 43 LYS 44 GLU 45 LEU 46 THR 47 ASN 48 HIS 49 SER 50 LEU 51 PRO 52 GLU 53 ILE 54 GLY 55 ASP 56 ALA 57 PHE 58 GLY 59 GLY 60 ARG 61 ASP 62 HIS 63 THR 64 THR 65 VAL 66 LEU 67 HIS 68 ALA 69 CYS 70 ARG 71 LYS 72 ILE 73 GLU 74 GLN 75 LEU 76 ARG 77 GLU 78 GLU 79 SER 80 HIS 81 ASP 82 ILE 83 LYS 84 GLU 85 ASP 86 PHE 87 SER 88 ASN 89 LEU 90 ILE 91 ARG 92 THR 93 LEU 94 SER 95 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 PDB 1J1V "Crystal Structure Of Dnaa Domainiv Complexed With Dnaabox Dna" 98.95 94 97.87 97.87 1.76e-59 DBJ BAB38060 "replication initiation protein DnaA [Escherichia coli O157:H7 str. Sakai]" 100.00 467 98.95 100.00 3.87e-58 DBJ BAE73276 "chromosomal replication initiator protein DnaA [Sodalis glossinidius str. 'morsitans']" 100.00 464 97.89 100.00 1.57e-57 DBJ BAE77592 "chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator [Escherichia coli str. K-12 substr. " 100.00 467 98.95 100.00 4.04e-58 DBJ BAG79512 "DNA replication initiator protein DnaA [Escherichia coli SE11]" 100.00 467 98.95 100.00 4.04e-58 DBJ BAH65893 "chromosomal replication initiation protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 467 98.95 100.00 4.12e-58 EMBL CAD03157 "chromosomal replication initiator protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 466 97.89 100.00 9.62e-58 EMBL CAE12296 "Chromosomal replication initiator protein DnaA [Photorhabdus luminescens subsp. laumondii TTO1]" 100.00 462 98.95 100.00 4.51e-58 EMBL CAG77337 "chromosomal replication initiator protein [Pectobacterium atrosepticum SCRI1043]" 100.00 465 97.89 100.00 1.24e-57 EMBL CAH23181 "chromosomal replication initiator protein [Yersinia pseudotuberculosis IP 32953]" 100.00 462 98.95 100.00 5.01e-58 EMBL CAL14189 "chromosomal replication initiator protein [Yersinia enterocolitica subsp. enterocolitica 8081]" 100.00 462 98.95 100.00 5.94e-58 GB AAA02815 "dnaA protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 466 97.89 100.00 9.62e-58 GB AAA02924 "DnaA [Serratia marcescens]" 100.00 464 98.95 100.00 4.22e-58 GB AAA83958 "dnaA [Proteus mirabilis]" 100.00 466 98.95 100.00 5.61e-58 GB AAB59149 "DnaA protein (gtg start codon) [Escherichia coli]" 100.00 467 98.95 100.00 4.04e-58 GB AAC76725 "chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator [Escherichia coli str. K-12 substr. " 100.00 467 98.95 100.00 4.04e-58 PIR AI0957 "chromosomal replication initiator protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 466 97.89 100.00 9.62e-58 REF NP_290335 "chromosome replication initiator DnaA [Escherichia coli O157:H7 str. EDL933]" 100.00 467 98.95 100.00 3.87e-58 REF NP_312664 "chromosomal replication initiation protein [Escherichia coli O157:H7 str. Sakai]" 100.00 467 98.95 100.00 3.87e-58 REF NP_418157 "chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator [Escherichia coli str. K-12 substr. " 100.00 467 98.95 100.00 4.04e-58 REF NP_458104 "chromosomal replication initiator protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 466 97.89 100.00 9.62e-58 REF NP_462738 "chromosomal replication initiation protein DnaA [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 466 97.89 100.00 9.03e-58 SP A1JT80 "RecName: Full=Chromosomal replication initiator protein DnaA [Yersinia enterocolitica subsp. enterocolitica 8081]" 100.00 462 98.95 100.00 5.94e-58 SP A4TGL5 "RecName: Full=Chromosomal replication initiator protein DnaA [Yersinia pestis Pestoides F]" 100.00 462 98.95 100.00 5.01e-58 SP A7FPB7 "RecName: Full=Chromosomal replication initiator protein DnaA [Yersinia pseudotuberculosis IP 31758]" 100.00 462 98.95 100.00 5.01e-58 SP A7ZTQ8 "RecName: Full=Chromosomal replication initiator protein DnaA [Escherichia coli E24377A]" 100.00 467 98.95 100.00 4.04e-58 SP A8A6G3 "RecName: Full=Chromosomal replication initiator protein DnaA [Escherichia coli HS]" 100.00 467 98.95 100.00 4.04e-58 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DnaA 'E. coli' 562 Eubacteria . 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 $DnaA 'recombinant technology' . . . . . 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 $DnaA 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 303 0.1 K 'ionic strength' 0.1 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'DnaA domain IV' _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 MET C C 179.3 0.05 . 2 . 1 MET CA C 55 0.05 . 3 . 2 VAL H H 8.62 0.02 . 4 . 2 VAL HA H 4.44 0.02 . 5 . 2 VAL C C 174.8 0.05 . 6 . 2 VAL CA C 61.8 0.05 . 7 . 2 VAL CB C 33.0 0.05 . 8 . 2 VAL N N 126.3 0.05 . 9 . 3 THR H H 8.10 0.02 . 10 . 3 THR HA H 4.82 0.02 . 11 . 3 THR C C 176.1 0.05 . 12 . 3 THR CA C 59.2 0.05 . 13 . 3 THR CB C 71.5 0.05 . 14 . 3 THR N N 115.8 0.05 . 15 . 4 ILE H H 9.29 0.02 . 16 . 4 ILE HA H 3.52 0.02 . 17 . 4 ILE C C 177.7 0.05 . 18 . 4 ILE CA C 66.0 0.05 . 19 . 4 ILE CB C 36.5 0.05 . 20 . 4 ILE N N 123.5 0.05 . 21 . 5 ASP H H 8.48 0.02 . 22 . 5 ASP HA H 4.18 0.02 . 23 . 5 ASP C C 177.9 0.05 . 24 . 5 ASP CA C 57.5 0.05 . 25 . 5 ASP CB C 40.8 0.05 . 26 . 5 ASP N N 121.1 0.05 . 27 . 6 ASN H H 7.80 0.02 . 28 . 6 ASN HA H 4.54 0.02 . 29 . 6 ASN C C 179 0.05 . 30 . 6 ASN CA C 56.1 0.05 . 31 . 6 ASN CB C 38.7 0.05 . 32 . 6 ASN N N 119.5 0.05 . 33 . 7 ILE H H 8.11 0.02 . 34 . 7 ILE HA H 3.54 0.02 . 35 . 7 ILE C C 177.3 0.05 . 36 . 7 ILE CA C 66.7 0.05 . 37 . 7 ILE CB C 38.3 0.05 . 38 . 7 ILE N N 124.3 0.05 . 39 . 8 GLN H H 8.64 0.02 . 40 . 8 GLN HA H 3.54 0.02 . 41 . 8 GLN C C 177.1 0.05 . 42 . 8 GLN CA C 60 0.05 . 43 . 8 GLN CB C 27.3 0.05 . 44 . 8 GLN N N 118.9 0.05 . 45 . 9 LYS H H 8.11 0.02 . 46 . 9 LYS HA H 3.80 0.02 . 47 . 9 LYS C C 178.8 0.05 . 48 . 9 LYS CA C 59.9 0.05 . 49 . 9 LYS CB C 32.7 0.05 . 50 . 9 LYS N N 119.5 0.05 . 51 . 10 THR H H 8.27 0.02 . 52 . 10 THR HA H 4.13 0.02 . 53 . 10 THR C C 176.9 0.05 . 54 . 10 THR CA C 67.1 0.05 . 55 . 10 THR CB C 67.7 0.05 . 56 . 10 THR N N 118.6 0.05 . 57 . 11 VAL H H 8.74 0.02 . 58 . 11 VAL HA H 3.56 0.02 . 59 . 11 VAL C C 178.8 0.05 . 60 . 11 VAL CA C 67.1 0.05 . 61 . 11 VAL CB C 31.5 0.05 . 62 . 11 VAL N N 124.3 0.05 . 63 . 12 ALA H H 8.34 0.02 . 64 . 12 ALA HA H 3.79 0.02 . 65 . 12 ALA C C 179 0.05 . 66 . 12 ALA CA C 56 0.05 . 67 . 12 ALA CB C 17.5 0.05 . 68 . 12 ALA N N 123.0 0.05 . 69 . 13 GLU H H 7.95 0.02 . 70 . 13 GLU HA H 3.95 0.02 . 71 . 13 GLU C C 177.9 0.05 . 72 . 13 GLU CA C 59.3 0.05 . 73 . 13 GLU CB C 29.5 0.05 . 74 . 13 GLU N N 117.6 0.05 . 75 . 14 TYR H H 8.25 0.02 . 76 . 14 TYR HA H 3.93 0.02 . 77 . 14 TYR C C 177.3 0.05 . 78 . 14 TYR CA C 61.9 0.05 . 79 . 14 TYR CB C 39.5 0.05 . 80 . 14 TYR N N 123.8 0.05 . 81 . 15 TYR H H 7.84 0.02 . 82 . 15 TYR HA H 4.49 0.02 . 83 . 15 TYR C C 173.5 0.05 . 84 . 15 TYR CA C 59.3 0.05 . 85 . 15 TYR CB C 36.5 0.05 . 86 . 15 TYR N N 115.3 0.05 . 87 . 16 LYS H H 7.90 0.02 . 88 . 16 LYS HA H 4.00 0.02 . 89 . 16 LYS C C 176.1 0.05 . 90 . 16 LYS CA C 57.2 0.05 . 91 . 16 LYS CB C 28.8 0.05 . 92 . 16 LYS N N 119.5 0.05 . 93 . 17 ILE H H 8.45 0.02 . 94 . 17 ILE HA H 4.79 0.02 . 95 . 17 ILE C C 174.6 0.05 . 96 . 17 ILE CA C 59.5 0.05 . 97 . 17 ILE CB C 39.7 0.05 . 98 . 17 ILE N N 115.4 0.05 . 99 . 18 LYS H H 8.63 0.02 . 100 . 18 LYS HA H 4.71 0.02 . 101 . 18 LYS C C 179 0.05 . 102 . 18 LYS CA C 54.6 0.05 . 103 . 18 LYS CB C 33.4 0.05 . 104 . 18 LYS N N 120.0 0.05 . 105 . 19 VAL H H 9.03 0.02 . 106 . 19 VAL HA H 3.34 0.02 . 107 . 19 VAL C C 178.3 0.05 . 108 . 19 VAL CA C 67.7 0.05 . 109 . 19 VAL CB C 31.2 0.05 . 110 . 19 VAL N N 127.2 0.05 . 111 . 20 ALA H H 8.50 0.02 . 112 . 20 ALA HA H 3.94 0.02 . 113 . 20 ALA C C 180.7 0.05 . 114 . 20 ALA CA C 55.1 0.05 . 115 . 20 ALA CB C 18.3 0.05 . 116 . 20 ALA N N 120.8 0.05 . 117 . 21 ASP H H 7.23 0.02 . 118 . 21 ASP HA H 4.44 0.02 . 119 . 21 ASP C C 178.9 0.05 . 120 . 21 ASP CA C 57.5 0.05 . 121 . 21 ASP CB C 40.9 0.05 . 122 . 21 ASP N N 127.2 0.05 . 123 . 22 LEU H H 7.69 0.02 . 124 . 22 LEU HA H 3.93 0.02 . 125 . 22 LEU C C 177.7 0.05 . 126 . 22 LEU CA C 57.7 0.05 . 127 . 22 LEU CB C 42.2 0.05 . 128 . 22 LEU N N 120.9 0.05 . 129 . 23 LEU H H 7.37 0.02 . 130 . 23 LEU HA H 3.96 0.02 . 131 . 23 LEU C C 177.3 0.05 . 132 . 23 LEU CA C 56.1 0.05 . 133 . 23 LEU CB C 42 0.05 . 134 . 23 LEU N N 117.5 0.05 . 135 . 24 SER H H 7.21 0.02 . 136 . 24 SER CA C 58.8 0.05 . 137 . 24 SER CB C 64.4 0.05 . 138 . 24 SER N N 115.7 0.05 . 139 . 25 LYS C C 176.9 0.05 . 140 . 25 LYS CA C 56.2 0.05 . 141 . 25 LYS CB C 32.5 0.05 . 142 . 26 ARG H H 8.00 0.02 . 143 . 26 ARG C C 177 0.05 . 144 . 26 ARG CA C 57.8 0.05 . 145 . 26 ARG CB C 31 0.05 . 146 . 26 ARG N N 122.6 0.05 . 147 . 27 ARG C C 176 0.05 . 148 . 27 ARG CA C 56.3 0.05 . 149 . 27 ARG CB C 30.7 0.05 . 150 . 27 ARG N N 124.8 0.05 . 151 . 28 SER C C 175.2 0.05 . 152 . 28 SER CA C 56.2 0.05 . 153 . 28 SER CB C 64 0.05 . 154 . 28 SER N N 118.0 0.05 . 155 . 29 ARG C C 177.9 0.05 . 156 . 29 ARG CA C 59.6 0.05 . 157 . 29 ARG N N 130.5 0.05 . 158 . 30 SER C C 174.4 0.05 . 159 . 30 SER CA C 60.6 0.05 . 160 . 30 SER CB C 63 0.05 . 161 . 30 SER N N 114.5 0.05 . 162 . 31 VAL H H 7.21 0.02 . 163 . 31 VAL HA H 4.16 0.02 . 164 . 31 VAL C C 175.7 0.05 . 165 . 31 VAL CA C 62 0.05 . 166 . 31 VAL CB C 33 0.05 . 167 . 31 VAL N N 115.6 0.05 . 168 . 32 ALA H H 8.16 0.02 . 169 . 32 ALA HA H 3.97 0.02 . 170 . 32 ALA C C 179.4 0.05 . 171 . 32 ALA CA C 55.9 0.05 . 172 . 32 ALA CB C 18 0.05 . 173 . 32 ALA N N 126.6 0.05 . 174 . 33 ARG H H 8.36 0.02 . 175 . 33 ARG CA C 60 0.05 . 176 . 33 ARG CB C 26.5 0.05 . 177 . 33 ARG N N 118.3 0.05 . 178 . 34 PRO C C 177.3 0.05 . 179 . 34 PRO CA C 65.7 0.05 . 180 . 34 PRO CB C 30 0.05 . 181 . 35 ARG H H 7.88 0.02 . 182 . 35 ARG HA H 3.76 0.02 . 183 . 35 ARG C C 177.8 0.05 . 184 . 35 ARG CA C 61 0.05 . 185 . 35 ARG CB C 31.6 0.05 . 186 . 35 ARG N N 118.3 0.05 . 187 . 36 GLN H H 8.16 0.02 . 188 . 36 GLN HA H 3.80 0.02 . 189 . 36 GLN C C 178.1 0.05 . 190 . 36 GLN CA C 59.6 0.05 . 191 . 36 GLN CB C 27 0.05 . 192 . 36 GLN N N 120.4 0.05 . 193 . 37 MET H H 8.66 0.02 . 194 . 37 MET HA H 4.26 0.02 . 195 . 37 MET C C 177.6 0.05 . 196 . 37 MET CA C 57.7 0.05 . 197 . 37 MET CB C 32.3 0.05 . 198 . 37 MET N N 119.7 0.05 . 199 . 38 ALA H H 8.54 0.02 . 200 . 38 ALA HA H 4.00 0.02 . 201 . 38 ALA C C 178.6 0.05 . 202 . 38 ALA CA C 55.4 0.05 . 203 . 38 ALA CB C 18.3 0.05 . 204 . 38 ALA N N 121.3 0.05 . 205 . 39 MET H H 7.95 0.02 . 206 . 39 MET HA H 3.35 0.02 . 207 . 39 MET C C 176.7 0.05 . 208 . 39 MET CA C 60.6 0.05 . 209 . 39 MET CB C 33.1 0.05 . 210 . 39 MET N N 119.8 0.05 . 211 . 40 ALA H H 8.43 0.02 . 212 . 40 ALA HA H 4.54 0.02 . 213 . 40 ALA C C 177.5 0.05 . 214 . 40 ALA CA C 55 0.05 . 215 . 40 ALA CB C 18 0.05 . 216 . 40 ALA N N 122.8 0.05 . 217 . 41 LEU H H 8.75 0.02 . 218 . 41 LEU HA H 3.91 0.02 . 219 . 41 LEU C C 178.3 0.05 . 220 . 41 LEU CA C 58 0.05 . 221 . 41 LEU CB C 42.4 0.05 . 222 . 41 LEU N N 121.5 0.05 . 223 . 42 ALA H H 8.22 0.02 . 224 . 42 ALA HA H 3.99 0.02 . 225 . 42 ALA C C 179.3 0.05 . 226 . 42 ALA CA C 55.2 0.05 . 227 . 42 ALA CB C 17.8 0.05 . 228 . 42 ALA N N 123.0 0.05 . 229 . 43 LYS H H 7.91 0.02 . 230 . 43 LYS HA H 4.17 0.02 . 231 . 43 LYS C C 176.9 0.05 . 232 . 43 LYS CA C 58.2 0.05 . 233 . 43 LYS CB C 32.5 0.05 . 234 . 43 LYS N N 122.9 0.05 . 235 . 44 GLU H H 7.71 0.02 . 236 . 44 GLU HA H 4.19 0.02 . 237 . 44 GLU C C 179 0.05 . 238 . 44 GLU CA C 58.5 0.05 . 239 . 44 GLU CB C 30 0.05 . 240 . 44 GLU N N 117.9 0.05 . 241 . 45 LEU H H 8.34 0.02 . 242 . 45 LEU HA H 4.48 0.02 . 243 . 45 LEU C C 176.9 0.05 . 244 . 45 LEU CA C 55.3 0.05 . 245 . 45 LEU CB C 44.5 0.05 . 246 . 45 LEU N N 114.7 0.05 . 247 . 46 THR H H 7.53 0.02 . 248 . 46 THR HA H 4.46 0.02 . 249 . 46 THR C C 173.3 0.05 . 250 . 46 THR CA C 60 0.05 . 251 . 46 THR CB C 71.7 0.05 . 252 . 46 THR N N 110.2 0.05 . 253 . 47 ASN H H 8.30 0.02 . 254 . 47 ASN HA H 5.02 0.02 . 255 . 47 ASN C C 176 0.05 . 256 . 47 ASN CA C 51.7 0.05 . 257 . 47 ASN CB C 38.3 0.05 . 258 . 47 ASN N N 118.1 0.05 . 259 . 48 HIS H H 7.65 0.02 . 260 . 48 HIS HA H 4.56 0.02 . 261 . 48 HIS C C 175 0.05 . 262 . 48 HIS CA C 57.2 0.05 . 263 . 48 HIS CB C 30 0.05 . 264 . 48 HIS N N 119.2 0.05 . 265 . 49 SER H H 8.48 0.02 . 266 . 49 SER HA H 4.06 0.02 . 267 . 49 SER C C 174.7 0.05 . 268 . 49 SER CA C 57.2 0.05 . 269 . 49 SER CB C 66 0.05 . 270 . 49 SER N N 118.7 0.05 . 271 . 50 LEU H H 9.08 0.02 . 272 . 50 LEU CA C 60.5 0.05 . 273 . 50 LEU CB C 39 0.05 . 274 . 50 LEU N N 120.7 0.05 . 275 . 51 PRO C C 179.3 0.05 . 276 . 51 PRO CA C 66.2 0.05 . 277 . 51 PRO CB C 31.4 0.05 . 278 . 52 GLU H H 7.23 0.02 . 279 . 52 GLU HA H 4.03 0.02 . 280 . 52 GLU C C 180.4 0.05 . 281 . 52 GLU CA C 59 0.05 . 282 . 52 GLU CB C 30 0.05 . 283 . 52 GLU N N 118.9 0.05 . 284 . 53 ILE H H 8.39 0.02 . 285 . 53 ILE HA H 3.5 0.02 . 286 . 53 ILE C C 177.8 0.05 . 287 . 53 ILE CA C 66.4 0.05 . 288 . 53 ILE CB C 38 0.05 . 289 . 53 ILE N N 122.4 0.05 . 290 . 54 GLY H H 8.55 0.02 . 291 . 54 GLY HA2 H 3.22 0.02 . 292 . 54 GLY HA3 H 3.65 0.02 . 293 . 54 GLY C C 177.9 0.05 . 294 . 54 GLY CA C 48.8 0.05 . 295 . 54 GLY N N 108.5 0.05 . 296 . 55 ASP H H 8.4 0.02 . 297 . 55 ASP HA H 4.26 0.02 . 298 . 55 ASP C C 178.4 0.05 . 299 . 55 ASP CA C 58 0.05 . 300 . 55 ASP CB C 41.3 0.05 . 301 . 55 ASP N N 124.5 0.05 . 302 . 56 ALA H H 7.47 0.02 . 303 . 56 ALA HA H 4.23 0.02 . 304 . 56 ALA C C 177.8 0.05 . 305 . 56 ALA CA C 53.4 0.05 . 306 . 56 ALA CB C 19 0.05 . 307 . 56 ALA N N 121.0 0.05 . 308 . 57 PHE H H 7.77 0.02 . 309 . 57 PHE HA H 4.40 0.02 . 310 . 57 PHE C C 174.8 0.05 . 311 . 57 PHE CA C 56.6 0.05 . 312 . 57 PHE CB C 38 0.05 . 313 . 57 PHE N N 120.3 0.05 . 314 . 58 GLY H H 7.96 0.02 . 315 . 58 GLY HA2 H 3.87 0.02 . 316 . 58 GLY HA3 H 4.23 0.02 . 317 . 58 GLY C C 175.6 0.05 . 318 . 58 GLY CA C 46.6 0.05 . 319 . 58 GLY N N 109.5 0.05 . 320 . 59 GLY H H 7.99 0.02 . 321 . 59 GLY HA2 H 4.02 0.02 . 322 . 59 GLY C C 175.6 0.05 . 323 . 59 GLY CA C 46.8 0.05 . 324 . 59 GLY N N 109.1 0.05 . 325 . 60 ARG H H 7.11 0.02 . 326 . 60 ARG HA H 4.27 0.02 . 327 . 60 ARG C C 175.2 0.05 . 328 . 60 ARG CA C 55.8 0.05 . 329 . 60 ARG CB C 31.6 0.05 . 330 . 60 ARG N N 122.4 0.05 . 331 . 61 ASP H H 8.26 0.02 . 332 . 61 ASP HA H 4.29 0.02 . 333 . 61 ASP CA C 53.1 0.05 . 334 . 61 ASP CB C 42.8 0.05 . 335 . 61 ASP N N 121.1 0.05 . 336 . 62 HIS C C 176.9 0.05 . 337 . 62 HIS CA C 59 0.05 . 338 . 62 HIS CB C 30.7 0.05 . 339 . 63 THR H H 7.40 0.02 . 340 . 63 THR HA H 3.96 0.02 . 341 . 63 THR C C 176.6 0.05 . 342 . 63 THR CA C 65.9 0.05 . 343 . 63 THR CB C 68 0.05 . 344 . 63 THR N N 118.5 0.05 . 345 . 64 THR H H 7.81 0.02 . 346 . 64 THR HA H 4.27 0.02 . 347 . 64 THR C C 176.8 0.05 . 348 . 64 THR CA C 66.5 0.05 . 349 . 64 THR CB C 67.3 0.05 . 350 . 64 THR N N 122.2 0.05 . 351 . 65 VAL H H 7.41 0.02 . 352 . 65 VAL HA H 3.89 0.02 . 353 . 65 VAL C C 179.8 0.05 . 354 . 65 VAL CA C 65.8 0.05 . 355 . 65 VAL CB C 32 0.05 . 356 . 65 VAL N N 124.5 0.05 . 357 . 66 LEU H H 8.25 0.02 . 358 . 66 LEU HA H 3.93 0.02 . 359 . 66 LEU C C 179 0.05 . 360 . 66 LEU CA C 58.6 0.05 . 361 . 66 LEU CB C 41.8 0.05 . 362 . 66 LEU N N 123.7 0.05 . 363 . 67 HIS H H 8.28 0.02 . 364 . 67 HIS HA H 4.25 0.02 . 365 . 67 HIS C C 177.7 0.05 . 366 . 67 HIS CA C 59.3 0.05 . 367 . 67 HIS CB C 30 0.05 . 368 . 67 HIS N N 118.5 0.05 . 369 . 68 ALA H H 7.95 0.02 . 370 . 68 ALA HA H 3.92 0.02 . 371 . 68 ALA C C 178.9 0.05 . 372 . 68 ALA CA C 55.8 0.05 . 373 . 68 ALA CB C 19.6 0.05 . 374 . 68 ALA N N 124.1 0.05 . 375 . 69 CYS H H 8.19 0.02 . 376 . 69 CYS HA H 3.88 0.02 . 377 . 69 CYS C C 177.7 0.05 . 378 . 69 CYS CA C 64.5 0.05 . 379 . 69 CYS CB C 26.5 0.05 . 380 . 69 CYS N N 116.8 0.05 . 381 . 70 ARG H H 8.20 0.02 . 382 . 70 ARG HA H 4.02 0.02 . 383 . 70 ARG C C 177 0.05 . 384 . 70 ARG CA C 58.7 0.05 . 385 . 70 ARG CB C 30.1 0.05 . 386 . 70 ARG N N 121.6 0.05 . 387 . 71 LYS H H 8.34 0.02 . 388 . 71 LYS HA H 4.05 0.02 . 389 . 71 LYS C C 178.8 0.05 . 390 . 71 LYS CA C 58 0.05 . 391 . 71 LYS CB C 31 0.05 . 392 . 71 LYS N N 122.9 0.05 . 393 . 72 ILE H H 8.10 0.02 . 394 . 72 ILE HA H 3.89 0.02 . 395 . 72 ILE C C 177.5 0.05 . 396 . 72 ILE CA C 61 0.05 . 397 . 72 ILE CB C 34.3 0.05 . 398 . 72 ILE N N 120.2 0.05 . 399 . 73 GLU H H 7.91 0.02 . 400 . 73 GLU HA H 3.65 0.02 . 401 . 73 GLU C C 178.7 0.05 . 402 . 73 GLU CA C 60 0.05 . 403 . 73 GLU CB C 36.3 0.05 . 404 . 73 GLU N N 122.5 0.05 . 405 . 74 GLN H H 7.65 0.02 . 406 . 74 GLN HA H 4.04 0.02 . 407 . 74 GLN C C 179.3 0.05 . 408 . 74 GLN CA C 58.6 0.05 . 409 . 74 GLN CB C 33.3 0.05 . 410 . 74 GLN N N 119.9 0.05 . 411 . 75 LEU H H 8.73 0.02 . 412 . 75 LEU HA H 4.04 0.02 . 413 . 75 LEU C C 179 0.05 . 414 . 75 LEU CA C 58 0.05 . 415 . 75 LEU CB C 42.8 0.05 . 416 . 75 LEU N N 122.0 0.05 . 417 . 76 ARG H H 8.49 0.02 . 418 . 76 ARG HA H 3.72 0.02 . 419 . 76 ARG C C 176.9 0.05 . 420 . 76 ARG CA C 59.6 0.05 . 421 . 76 ARG CB C 30.5 0.05 . 422 . 76 ARG N N 119.8 0.05 . 423 . 77 GLU H H 7.04 0.02 . 424 . 77 GLU HA H 4.24 0.02 . 425 . 77 GLU C C 177.8 0.05 . 426 . 77 GLU CA C 57.2 0.05 . 427 . 77 GLU CB C 30 0.05 . 428 . 77 GLU N N 116.3 0.05 . 429 . 78 GLU H H 7.56 0.02 . 430 . 78 GLU HA H 4.33 0.02 . 431 . 78 GLU C C 176.4 0.05 . 432 . 78 GLU CA C 57.5 0.05 . 433 . 78 GLU CB C 32.1 0.05 . 434 . 78 GLU N N 118.3 0.05 . 435 . 79 SER H H 8.74 0.02 . 436 . 79 SER CA C 56 0.05 . 437 . 79 SER CB C 63.5 0.05 . 438 . 79 SER N N 117.0 0.05 . 439 . 80 HIS C C 176.4 0.05 . 440 . 80 HIS CA C 59.6 0.05 . 441 . 80 HIS CB C 29 0.05 . 442 . 81 ASP H H 8.27 0.02 . 443 . 81 ASP HA H 4.33 0.02 . 444 . 81 ASP C C 177.4 0.05 . 445 . 81 ASP CA C 57 0.05 . 446 . 81 ASP CB C 40 0.05 . 447 . 81 ASP N N 119.7 0.05 . 448 . 82 ILE H H 7.49 0.02 . 449 . 82 ILE HA H 3.98 0.02 . 450 . 82 ILE C C 177.8 0.05 . 451 . 82 ILE CA C 62 0.05 . 452 . 82 ILE CB C 35.3 0.05 . 453 . 82 ILE N N 121.6 0.05 . 454 . 83 LYS H H 8.03 0.02 . 455 . 83 LYS HA H 3.82 0.02 . 456 . 83 LYS C C 179.5 0.05 . 457 . 83 LYS CA C 61 0.05 . 458 . 83 LYS CB C 32 0.05 . 459 . 83 LYS N N 123.1 0.05 . 460 . 84 GLU H H 8.13 0.02 . 461 . 84 GLU HA H 4.06 0.02 . 462 . 84 GLU C C 178.3 0.05 . 463 . 84 GLU CA C 59.2 0.05 . 464 . 84 GLU CB C 28.3 0.05 . 465 . 84 GLU N N 121.0 0.05 . 466 . 85 ASP H H 8.63 0.02 . 467 . 85 ASP HA H 4.34 0.02 . 468 . 85 ASP C C 181.8 0.05 . 469 . 85 ASP CA C 57.9 0.05 . 470 . 85 ASP CB C 41 0.05 . 471 . 85 ASP N N 122.6 0.05 . 472 . 86 PHE H H 8.72 0.02 . 473 . 86 PHE HA H 3.91 0.02 . 474 . 86 PHE C C 176.7 0.05 . 475 . 86 PHE CA C 62.5 0.05 . 476 . 86 PHE CB C 39.5 0.05 . 477 . 86 PHE N N 121.4 0.05 . 478 . 87 SER H H 7.89 0.02 . 479 . 87 SER HA H 4.04 0.02 . 480 . 87 SER C C 177.2 0.05 . 481 . 87 SER CA C 61.5 0.05 . 482 . 87 SER CB C 63 0.05 . 483 . 87 SER N N 114.1 0.05 . 484 . 88 ASN H H 8.83 0.02 . 485 . 88 ASN HA H 4.35 0.02 . 486 . 88 ASN C C 178.3 0.05 . 487 . 88 ASN CA C 55.7 0.05 . 488 . 88 ASN CB C 37.7 0.05 . 489 . 88 ASN N N 123.4 0.05 . 490 . 89 LEU H H 8.31 0.02 . 491 . 89 LEU HA H 3.68 0.02 . 492 . 89 LEU C C 178.6 0.05 . 493 . 89 LEU CA C 58.4 0.05 . 494 . 89 LEU CB C 42 0.05 . 495 . 89 LEU N N 124.6 0.05 . 496 . 90 ILE H H 8.32 0.02 . 497 . 90 ILE HA H 3.45 0.02 . 498 . 90 ILE C C 179 0.05 . 499 . 90 ILE CA C 64.8 0.05 . 500 . 90 ILE CB C 36.5 0.05 . 501 . 90 ILE N N 121.6 0.05 . 502 . 91 ARG H H 7.79 0.02 . 503 . 91 ARG HA H 3.96 0.02 . 504 . 91 ARG C C 179.3 0.05 . 505 . 91 ARG CA C 59.8 0.05 . 506 . 91 ARG CB C 30 0.05 . 507 . 91 ARG N N 123.1 0.05 . 508 . 92 THR H H 7.97 0.02 . 509 . 92 THR HA H 4.11 0.02 . 510 . 92 THR C C 176.3 0.05 . 511 . 92 THR CA C 66.2 0.05 . 512 . 92 THR CB C 68.7 0.05 . 513 . 92 THR N N 118.0 0.05 . 514 . 93 LEU H H 7.99 0.02 . 515 . 93 LEU HA H 4.16 0.02 . 516 . 93 LEU C C 176.8 0.05 . 517 . 93 LEU CA C 56.8 0.05 . 518 . 93 LEU CB C 42.8 0.05 . 519 . 93 LEU N N 121.9 0.05 . 520 . 94 SER H H 7.63 0.02 . 521 . 94 SER C C 173.3 0.05 . 522 . 94 SER CA C 59 0.05 . 523 . 94 SER CB C 64 0.05 . 524 . 94 SER N N 115.4 0.05 . 525 . 95 SER H H 7.46 0.02 . 526 . 95 SER CA C 60.5 0.05 . 527 . 95 SER CB C 65 0.05 . 528 . 95 SER N N 124.5 0.05 . stop_ save_