data_5200 #Corrected using PDB structure: 1J1VA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 73 E CB 36.36 29.65 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.03 -0.33 0.06 0.09 -2.20 -0.02 # #bmr5200.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5200.str file): #HA CA CB CO N HN #N/A -0.14 -0.14 +0.09 -2.20 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.17 +/-0.18 +/-0.17 +/-0.37 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.787 0.962 0.995 0.718 0.843 0.572 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.131 0.828 0.838 0.775 1.739 0.237 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N chemical shift assignment of DnaA domain IV ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Imoto Taiji . . stop_ _BMRB_accession_number 5200 _BMRB_flat_file_name bmr5200.str _Entry_type new _Submission_date 2001-11-04 _Accession_date 2001-11-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 165 '15N chemical shifts' 89 '13C chemical shifts' 274 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Determination of the Secondary Structure in Solution of the Escherichia coli DnaA DNA-binding Domain ; _Citation_status published _Citation_type journal _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 _Page_first 42 _Page_last 48 _Year 2002 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_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' save_ ######################## # Monomeric polymers # ######################## save_DnaA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "chromosome replication initiator" _Name_variant . _Abbreviation_common "DnaA domain IV" _Mol_thiol_state 'all free' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 "A Chain A, Crystal Structure Of DnaaDomainiv Complexed With Dnaabox Dna" 101.06 94 98 98 3e-45 DBJ BAB38060.1 "replication initiation protein DnaA[Escherichia coli O157:H7]" 20.34 467 99 100 7e-47 EMBL CAC93547.1 "chromosomal replication initiatorprotein [Yersinia pestis CO92]" 20.56 462 99 100 7e-47 EMBL CAE12296.1 "Chromosomal replication initiatorprotein DnaA [Photorhabdus luminescens subsp. laumondiiTTO1]" 20.56 462 99 100 7e-47 EMBL CAG77337.1 "chromosomal replication initiatorprotein [Erwinia carotovora subsp. atroseptica SCRI1043]" 20.43 465 98 100 9e-47 EMBL CAD03157.1 "chromosomal replication initiatorprotein [Salmonella enterica subsp. enterica serovarTyphi]" 20.39 466 98 100 9e-47 GenBank AAS64144.1 "chromosomal replication initiatorprotein [Yersinia pestis biovar Medievalis str. 91001]" 20.56 462 99 100 7e-47 GenBank AAA83958.1 "dnaA gene product" 20.39 466 99 100 7e-47 GenBank AAM87655.1 "DNA biosynthesis protein [Yersiniapestis KIM]" 20.39 466 99 100 7e-47 GenBank AAG58899.1 "DNA biosynthesis; initiation ofchromosome replication; can be transcription regulator[Escherichia coli O157:H7 EDL933]" 20.34 467 99 100 7e-47 GenBank AAP18992.1 "replication initiation protein DnaA[Shigella flexneri 2a str. 2457T]" 20.34 467 99 100 7e-47 PIR AG0497 "chromosomal replication initiator protein[imported] - Yersinia pestis (strain CO92)" 20.56 462 99 100 7e-47 PIR IQEBV "replication initiation protein dnaA - Proteusmirabilis" 20.39 466 99 100 7e-47 PIR E91208 "replication initiation protein DnaA[imported] - Escherichia coli (strain O157:H7, substrainRIMD 0509952)" 20.34 467 99 100 7e-47 PIR G86054 "replication initiation protein DnaA[similarity] - Escherichia coli (strain O157:H7,substrain EDL933)" 20.34 467 99 100 7e-47 PIR IQECDA "replication initiation protein dnaA -Escherichia coli (strain K-12)" 20.34 467 99 100 7e-47 REF NP_407519.1 "chromosomal replication initiatorprotein [Yersinia pestis]" 20.56 462 99 100 7e-47 REF NP_927377.1 "Chromosomal replication initiatorprotein DnaA [Photorhabdus luminescens subsp. laumondiiTTO1]" 20.56 462 99 100 7e-47 REF NP_995267.1 "chromosomal replication initiatorprotein [Yersinia pestis biovar Medievalis str. 91001]" 20.56 462 99 100 7e-47 REF NP_290335.1 "DNA biosynthesis; initiation ofchromosome replication; can be transcription regulator[Escherichia coli O157:H7 EDL933]" 20.34 467 99 100 7e-47 REF NP_312664.1 "DnaA; replication initiation protein[Escherichia coli O157:H7]" 20.34 467 99 100 7e-47 SWISS-PROT Q8Z9U7 "DNAA_YERPE Chromosomal replication initiatorprotein dnaA" 20.56 462 99 100 7e-47 SWISS-PROT P29440 "DNAA_SERMA Chromosomal replication initiatorprotein dnaA" 20.47 464 99 100 7e-47 SWISS-PROT P22837 "DNAA_PROMI Chromosomal replication initiatorprotein dnaA" 20.39 466 99 100 7e-47 SWISS-PROT P03004 "DNAA_ECOLI Chromosomal replication initiatorprotein dnaA" 20.34 467 99 100 7e-47 SWISS-PROT Q8XBZ3 "DNAA_ECO57 Chromosomal replication initiatorprotein dnaA" 20.34 467 99 100 7e-47 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 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 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N NOESY ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions 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 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts 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" loop_ _Atom_shift_assign_ID _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 179.39 0.05 . 2 1 MET CA C 54.86 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 174.89 0.05 . 6 2 VAL CA C 61.66 0.05 . 7 2 VAL CB C 32.86 0.05 . 8 2 VAL N N 124.10 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 176.19 0.05 . 12 3 THR CA C 59.06 0.05 . 13 3 THR CB C 71.36 0.05 . 14 3 THR N N 113.60 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 177.79 0.05 . 18 4 ILE CA C 65.86 0.05 . 19 4 ILE CB C 36.36 0.05 . 20 4 ILE N N 121.30 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 177.99 0.05 . 24 5 ASP CA C 57.36 0.05 . 25 5 ASP CB C 40.66 0.05 . 26 5 ASP N N 118.90 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 179.09 0.05 . 30 6 ASN CA C 55.96 0.05 . 31 6 ASN CB C 38.56 0.05 . 32 6 ASN N N 117.30 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 177.39 0.05 . 36 7 ILE CA C 66.56 0.05 . 37 7 ILE CB C 38.16 0.05 . 38 7 ILE N N 122.10 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 177.19 0.05 . 42 8 GLN CA C 59.86 0.05 . 43 8 GLN CB C 27.16 0.05 . 44 8 GLN N N 116.70 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 178.89 0.05 . 48 9 LYS CA C 59.76 0.05 . 49 9 LYS CB C 32.56 0.05 . 50 9 LYS N N 117.30 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 176.99 0.05 . 54 10 THR CA C 66.96 0.05 . 55 10 THR CB C 67.56 0.05 . 56 10 THR N N 116.40 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 178.89 0.05 . 60 11 VAL CA C 66.96 0.05 . 61 11 VAL CB C 31.36 0.05 . 62 11 VAL N N 122.10 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 179.09 0.05 . 66 12 ALA CA C 55.86 0.05 . 67 12 ALA CB C 17.36 0.05 . 68 12 ALA N N 120.80 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 177.99 0.05 . 72 13 GLU CA C 59.16 0.05 . 73 13 GLU CB C 29.36 0.05 . 74 13 GLU N N 115.40 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 177.39 0.05 . 78 14 TYR CA C 61.76 0.05 . 79 14 TYR CB C 39.36 0.05 . 80 14 TYR N N 121.60 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 173.59 0.05 . 84 15 TYR CA C 59.16 0.05 . 85 15 TYR CB C 36.36 0.05 . 86 15 TYR N N 113.10 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 176.19 0.05 . 90 16 LYS CA C 57.06 0.05 . 91 16 LYS CB C 28.66 0.05 . 92 16 LYS N N 117.30 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 174.69 0.05 . 96 17 ILE CA C 59.36 0.05 . 97 17 ILE CB C 39.56 0.05 . 98 17 ILE N N 113.20 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 179.09 0.05 . 102 18 LYS CA C 54.46 0.05 . 103 18 LYS CB C 33.26 0.05 . 104 18 LYS N N 117.80 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 178.39 0.05 . 108 19 VAL CA C 67.56 0.05 . 109 19 VAL CB C 31.06 0.05 . 110 19 VAL N N 125.00 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 180.79 0.05 . 114 20 ALA CA C 54.96 0.05 . 115 20 ALA CB C 18.16 0.05 . 116 20 ALA N N 118.60 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 178.99 0.05 . 120 21 ASP CA C 57.36 0.05 . 121 21 ASP CB C 40.76 0.05 . 122 21 ASP N N 125.00 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 177.79 0.05 . 126 22 LEU CA C 57.56 0.05 . 127 22 LEU CB C 42.06 0.05 . 128 22 LEU N N 118.70 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 177.39 0.05 . 132 23 LEU CA C 55.96 0.05 . 133 23 LEU CB C 41.86 0.05 . 134 23 LEU N N 115.30 0.05 . 135 24 SER H H 7.21 0.02 . 136 24 SER CA C 58.66 0.05 . 137 24 SER CB C 64.26 0.05 . 138 24 SER N N 113.50 0.05 . 139 25 LYS C C 176.99 0.05 . 140 25 LYS CA C 56.06 0.05 . 141 25 LYS CB C 32.36 0.05 . 142 26 ARG H H 8.00 0.02 . 143 26 ARG C C 177.09 0.05 . 144 26 ARG CA C 57.66 0.05 . 145 26 ARG CB C 30.86 0.05 . 146 26 ARG N N 120.40 0.05 . 147 27 ARG C C 176.09 0.05 . 148 27 ARG CA C 56.16 0.05 . 149 27 ARG CB C 30.56 0.05 . 150 27 ARG N N 122.60 0.05 . 151 28 SER C C 175.29 0.05 . 152 28 SER CA C 56.06 0.05 . 153 28 SER CB C 63.86 0.05 . 154 28 SER N N 115.80 0.05 . 155 29 ARG C C 177.99 0.05 . 156 29 ARG CA C 59.46 0.05 . 157 29 ARG N N 128.30 0.05 . 158 30 SER C C 174.49 0.05 . 159 30 SER CA C 60.46 0.05 . 160 30 SER CB C 62.86 0.05 . 161 30 SER N N 112.30 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 175.79 0.05 . 165 31 VAL CA C 61.86 0.05 . 166 31 VAL CB C 32.86 0.05 . 167 31 VAL N N 113.40 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 179.49 0.05 . 171 32 ALA CA C 55.76 0.05 . 172 32 ALA CB C 17.86 0.05 . 173 32 ALA N N 124.40 0.05 . 174 33 ARG H H 8.36 0.02 . 175 33 ARG CA C 59.86 0.05 . 176 33 ARG CB C 26.36 0.05 . 177 33 ARG N N 116.10 0.05 . 178 34 PRO C C 177.39 0.05 . 179 34 PRO CA C 65.56 0.05 . 180 34 PRO CB C 29.86 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 177.89 0.05 . 184 35 ARG CA C 60.86 0.05 . 185 35 ARG CB C 31.46 0.05 . 186 35 ARG N N 116.10 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 178.19 0.05 . 190 36 GLN CA C 59.46 0.05 . 191 36 GLN CB C 26.86 0.05 . 192 36 GLN N N 118.20 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 177.69 0.05 . 196 37 MET CA C 57.56 0.05 . 197 37 MET CB C 32.16 0.05 . 198 37 MET N N 117.50 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 178.69 0.05 . 202 38 ALA CA C 55.26 0.05 . 203 38 ALA CB C 18.16 0.05 . 204 38 ALA N N 119.10 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 176.79 0.05 . 208 39 MET CA C 60.46 0.05 . 209 39 MET CB C 32.96 0.05 . 210 39 MET N N 117.60 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 177.59 0.05 . 214 40 ALA CA C 54.86 0.05 . 215 40 ALA CB C 17.86 0.05 . 216 40 ALA N N 120.60 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 178.39 0.05 . 220 41 LEU CA C 57.86 0.05 . 221 41 LEU CB C 42.26 0.05 . 222 41 LEU N N 119.30 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 179.39 0.05 . 226 42 ALA CA C 55.06 0.05 . 227 42 ALA CB C 17.66 0.05 . 228 42 ALA N N 120.80 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 176.99 0.05 . 232 43 LYS CA C 58.06 0.05 . 233 43 LYS CB C 32.36 0.05 . 234 43 LYS N N 120.70 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 179.09 0.05 . 238 44 GLU CA C 58.36 0.05 . 239 44 GLU CB C 29.86 0.05 . 240 44 GLU N N 115.70 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 176.99 0.05 . 244 45 LEU CA C 55.16 0.05 . 245 45 LEU CB C 44.36 0.05 . 246 45 LEU N N 112.50 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 173.39 0.05 . 250 46 THR CA C 59.86 0.05 . 251 46 THR CB C 71.56 0.05 . 252 46 THR N N 108.00 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 176.09 0.05 . 256 47 ASN CA C 51.56 0.05 . 257 47 ASN CB C 38.16 0.05 . 258 47 ASN N N 115.90 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 175.09 0.05 . 262 48 HIS CA C 57.06 0.05 . 263 48 HIS CB C 29.86 0.05 . 264 48 HIS N N 117.00 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 174.79 0.05 . 268 49 SER CA C 57.06 0.05 . 269 49 SER CB C 65.86 0.05 . 270 49 SER N N 116.50 0.05 . 271 50 LEU H H 9.08 0.02 . 272 50 LEU CA C 60.36 0.05 . 273 50 LEU CB C 38.86 0.05 . 274 50 LEU N N 118.50 0.05 . 275 51 PRO C C 179.39 0.05 . 276 51 PRO CA C 66.06 0.05 . 277 51 PRO CB C 31.26 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 180.49 0.05 . 281 52 GLU CA C 58.86 0.05 . 282 52 GLU CB C 29.86 0.05 . 283 52 GLU N N 116.70 0.05 . 284 53 ILE H H 8.39 0.02 . 285 53 ILE HA H 3.50 0.02 . 286 53 ILE C C 177.89 0.05 . 287 53 ILE CA C 66.26 0.05 . 288 53 ILE CB C 37.86 0.05 . 289 53 ILE N N 120.20 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 177.99 0.05 . 294 54 GLY CA C 48.66 0.05 . 295 54 GLY N N 106.30 0.05 . 296 55 ASP H H 8.40 0.02 . 297 55 ASP HA H 4.26 0.02 . 298 55 ASP C C 178.49 0.05 . 299 55 ASP CA C 57.86 0.05 . 300 55 ASP CB C 41.16 0.05 . 301 55 ASP N N 122.30 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 177.89 0.05 . 305 56 ALA CA C 53.26 0.05 . 306 56 ALA CB C 18.86 0.05 . 307 56 ALA N N 118.80 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 174.89 0.05 . 311 57 PHE CA C 56.46 0.05 . 312 57 PHE CB C 37.86 0.05 . 313 57 PHE N N 118.10 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 175.69 0.05 . 318 58 GLY CA C 46.46 0.05 . 319 58 GLY N N 107.30 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 175.69 0.05 . 323 59 GLY CA C 46.66 0.05 . 324 59 GLY N N 106.90 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 175.29 0.05 . 328 60 ARG CA C 55.66 0.05 . 329 60 ARG CB C 31.46 0.05 . 330 60 ARG N N 120.20 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 52.96 0.05 . 334 61 ASP CB C 42.66 0.05 . 335 61 ASP N N 118.90 0.05 . 336 62 HIS C C 176.99 0.05 . 337 62 HIS CA C 58.86 0.05 . 338 62 HIS CB C 30.56 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 176.69 0.05 . 342 63 THR CA C 65.76 0.05 . 343 63 THR CB C 67.86 0.05 . 344 63 THR N N 116.30 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 176.89 0.05 . 348 64 THR CA C 66.36 0.05 . 349 64 THR CB C 67.16 0.05 . 350 64 THR N N 120.00 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 179.89 0.05 . 354 65 VAL CA C 65.66 0.05 . 355 65 VAL CB C 31.86 0.05 . 356 65 VAL N N 122.30 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 179.09 0.05 . 360 66 LEU CA C 58.46 0.05 . 361 66 LEU CB C 41.66 0.05 . 362 66 LEU N N 121.50 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 177.79 0.05 . 366 67 HIS CA C 59.16 0.05 . 367 67 HIS CB C 29.86 0.05 . 368 67 HIS N N 116.30 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 178.99 0.05 . 372 68 ALA CA C 55.66 0.05 . 373 68 ALA CB C 19.46 0.05 . 374 68 ALA N N 121.90 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 177.79 0.05 . 378 69 CYS CA C 64.36 0.05 . 379 69 CYS CB C 26.36 0.05 . 380 69 CYS N N 114.60 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 177.09 0.05 . 384 70 ARG CA C 58.56 0.05 . 385 70 ARG CB C 29.96 0.05 . 386 70 ARG N N 119.40 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 178.89 0.05 . 390 71 LYS CA C 57.86 0.05 . 391 71 LYS CB C 30.86 0.05 . 392 71 LYS N N 120.70 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 177.59 0.05 . 396 72 ILE CA C 60.86 0.05 . 397 72 ILE CB C 34.16 0.05 . 398 72 ILE N N 118.00 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 178.79 0.05 . 402 73 GLU CA C 59.86 0.05 . 403 73 GLU CB C 36.16 0.05 . 404 73 GLU N N 120.30 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 179.39 0.05 . 408 74 GLN CA C 58.46 0.05 . 409 74 GLN CB C 33.16 0.05 . 410 74 GLN N N 117.70 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 179.09 0.05 . 414 75 LEU CA C 57.86 0.05 . 415 75 LEU CB C 42.66 0.05 . 416 75 LEU N N 119.80 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 176.99 0.05 . 420 76 ARG CA C 59.46 0.05 . 421 76 ARG CB C 30.36 0.05 . 422 76 ARG N N 117.60 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 177.89 0.05 . 426 77 GLU CA C 57.06 0.05 . 427 77 GLU CB C 29.86 0.05 . 428 77 GLU N N 114.10 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 176.49 0.05 . 432 78 GLU CA C 57.36 0.05 . 433 78 GLU CB C 31.96 0.05 . 434 78 GLU N N 116.10 0.05 . 435 79 SER H H 8.74 0.02 . 436 79 SER CA C 55.86 0.05 . 437 79 SER CB C 63.36 0.05 . 438 79 SER N N 114.80 0.05 . 439 80 HIS C C 176.49 0.05 . 440 80 HIS CA C 59.46 0.05 . 441 80 HIS CB C 28.86 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 177.49 0.05 . 445 81 ASP CA C 56.86 0.05 . 446 81 ASP CB C 39.86 0.05 . 447 81 ASP N N 117.50 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 177.89 0.05 . 451 82 ILE CA C 61.86 0.05 . 452 82 ILE CB C 35.16 0.05 . 453 82 ILE N N 119.40 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 179.59 0.05 . 457 83 LYS CA C 60.86 0.05 . 458 83 LYS CB C 31.86 0.05 . 459 83 LYS N N 120.90 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 178.39 0.05 . 463 84 GLU CA C 59.06 0.05 . 464 84 GLU CB C 28.16 0.05 . 465 84 GLU N N 118.80 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 181.89 0.05 . 469 85 ASP CA C 57.76 0.05 . 470 85 ASP CB C 40.86 0.05 . 471 85 ASP N N 120.40 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 176.79 0.05 . 475 86 PHE CA C 62.36 0.05 . 476 86 PHE CB C 39.36 0.05 . 477 86 PHE N N 119.20 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 177.29 0.05 . 481 87 SER CA C 61.36 0.05 . 482 87 SER CB C 62.86 0.05 . 483 87 SER N N 111.90 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 178.39 0.05 . 487 88 ASN CA C 55.56 0.05 . 488 88 ASN CB C 37.56 0.05 . 489 88 ASN N N 121.20 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 178.69 0.05 . 493 89 LEU CA C 58.26 0.05 . 494 89 LEU CB C 41.86 0.05 . 495 89 LEU N N 122.40 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 179.09 0.05 . 499 90 ILE CA C 64.66 0.05 . 500 90 ILE CB C 36.36 0.05 . 501 90 ILE N N 119.40 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 179.39 0.05 . 505 91 ARG CA C 59.66 0.05 . 506 91 ARG CB C 29.86 0.05 . 507 91 ARG N N 120.90 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 176.39 0.05 . 511 92 THR CA C 66.06 0.05 . 512 92 THR CB C 68.56 0.05 . 513 92 THR N N 115.80 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 176.89 0.05 . 517 93 LEU CA C 56.66 0.05 . 518 93 LEU CB C 42.66 0.05 . 519 93 LEU N N 119.70 0.05 . 520 94 SER H H 7.63 0.02 . 521 94 SER C C 173.39 0.05 . 522 94 SER CA C 58.86 0.05 . 523 94 SER CB C 63.86 0.05 . 524 94 SER N N 113.20 0.05 . 525 95 SER H H 7.46 0.02 . 526 95 SER CA C 60.36 0.05 . 527 95 SER CB C 64.86 0.05 . 528 95 SER N N 122.30 0.05 . stop_ save_