data_5219 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase ; _BMRB_accession_number 5219 _BMRB_flat_file_name bmr5219.str _Entry_type original _Submission_date 2001-11-28 _Accession_date 2001-11-28 _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 Buchko Garry W . 2 Wallace Susan S . 3 Kennedy Michael A . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 "13C chemical shifts" 533 "15N chemical shifts" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21986775 _PubMed_ID 11991361 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Buchko Garry W . 2 Wallace Susan S . 3 Kennedy Michael A . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 301 _Page_last 302 _Year 2002 _Details . loop_ _Keyword 'chemical shift mapping' 7,8-dihydro-8-oxoguanine 'DNA repair' 'Fpg (Mut M) protein' 'oxidized DNA' stop_ save_ ################################## # Molecular system description # ################################## save_system_Fpg _Saveframe_category molecular_system _Mol_system_name 'Escherichia coli formamidopyrimidine-DNA glycosylase' _Abbreviation_common Fpg _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Fpg $Fpg 'Zinc ion(II)' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound, and free' loop_ _Biological_function 'DNA glycosylase' 'AP lyase' deoxyribophosphodiesterase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Fpg _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli formamidopyrimidine DNA glycosylase' _Abbreviation_common Fpg _Molecular_mass . _Mol_thiol_state 'other bound, and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 269 _Mol_residue_sequence ; MPELPEVETSRRGIEPHLVG ATILHAVVRNGRLRWPVSEE IYRLSDQPVLSVQRRAKYLL LELPEGWIIIHLGMSGSLRI LPEELPPEKHDHVDLVMSNG KVLRYTDPRRFGAWLWTKEL EGHNVLTHLGPEPLSDDFNG EYLHQKCAKKKTAIKPWLMD NKLVVGVGNIYASESLFAAG IHPDRLASSLSLAECELLAR VIKAVLLRSIEQGGTTLKDF LQSDGKPGYFAQELQVYGRK GEPCRVCGTPIVATKHAQRA TFYCRQCQK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 GLU 4 LEU 5 PRO 6 GLU 7 VAL 8 GLU 9 THR 10 SER 11 ARG 12 ARG 13 GLY 14 ILE 15 GLU 16 PRO 17 HIS 18 LEU 19 VAL 20 GLY 21 ALA 22 THR 23 ILE 24 LEU 25 HIS 26 ALA 27 VAL 28 VAL 29 ARG 30 ASN 31 GLY 32 ARG 33 LEU 34 ARG 35 TRP 36 PRO 37 VAL 38 SER 39 GLU 40 GLU 41 ILE 42 TYR 43 ARG 44 LEU 45 SER 46 ASP 47 GLN 48 PRO 49 VAL 50 LEU 51 SER 52 VAL 53 GLN 54 ARG 55 ARG 56 ALA 57 LYS 58 TYR 59 LEU 60 LEU 61 LEU 62 GLU 63 LEU 64 PRO 65 GLU 66 GLY 67 TRP 68 ILE 69 ILE 70 ILE 71 HIS 72 LEU 73 GLY 74 MET 75 SER 76 GLY 77 SER 78 LEU 79 ARG 80 ILE 81 LEU 82 PRO 83 GLU 84 GLU 85 LEU 86 PRO 87 PRO 88 GLU 89 LYS 90 HIS 91 ASP 92 HIS 93 VAL 94 ASP 95 LEU 96 VAL 97 MET 98 SER 99 ASN 100 GLY 101 LYS 102 VAL 103 LEU 104 ARG 105 TYR 106 THR 107 ASP 108 PRO 109 ARG 110 ARG 111 PHE 112 GLY 113 ALA 114 TRP 115 LEU 116 TRP 117 THR 118 LYS 119 GLU 120 LEU 121 GLU 122 GLY 123 HIS 124 ASN 125 VAL 126 LEU 127 THR 128 HIS 129 LEU 130 GLY 131 PRO 132 GLU 133 PRO 134 LEU 135 SER 136 ASP 137 ASP 138 PHE 139 ASN 140 GLY 141 GLU 142 TYR 143 LEU 144 HIS 145 GLN 146 LYS 147 CYS 148 ALA 149 LYS 150 LYS 151 LYS 152 THR 153 ALA 154 ILE 155 LYS 156 PRO 157 TRP 158 LEU 159 MET 160 ASP 161 ASN 162 LYS 163 LEU 164 VAL 165 VAL 166 GLY 167 VAL 168 GLY 169 ASN 170 ILE 171 TYR 172 ALA 173 SER 174 GLU 175 SER 176 LEU 177 PHE 178 ALA 179 ALA 180 GLY 181 ILE 182 HIS 183 PRO 184 ASP 185 ARG 186 LEU 187 ALA 188 SER 189 SER 190 LEU 191 SER 192 LEU 193 ALA 194 GLU 195 CYS 196 GLU 197 LEU 198 LEU 199 ALA 200 ARG 201 VAL 202 ILE 203 LYS 204 ALA 205 VAL 206 LEU 207 LEU 208 ARG 209 SER 210 ILE 211 GLU 212 GLN 213 GLY 214 GLY 215 THR 216 THR 217 LEU 218 LYS 219 ASP 220 PHE 221 LEU 222 GLN 223 SER 224 ASP 225 GLY 226 LYS 227 PRO 228 GLY 229 TYR 230 PHE 231 ALA 232 GLN 233 GLU 234 LEU 235 GLN 236 VAL 237 TYR 238 GLY 239 ARG 240 LYS 241 GLY 242 GLU 243 PRO 244 CYS 245 ARG 246 VAL 247 CYS 248 GLY 249 THR 250 PRO 251 ILE 252 VAL 253 ALA 254 THR 255 LYS 256 HIS 257 ALA 258 GLN 259 ARG 260 ALA 261 THR 262 PHE 263 TYR 264 CYS 265 ARG 266 GLN 267 CYS 268 GLN 269 LYS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P05523 'Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM)' 100.00 269 100.00 100.00 3.89e-156 SWISS-PROT B1IZF8 'Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM)' 100.00 269 99.63 99.63 1.26e-155 SWISS-PROT A8A697 'Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM)' 100.00 269 100.00 100.00 3.89e-156 SWISS-PROT A7ZTI6 'Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM)' 100.00 269 99.63 99.63 1.26e-155 SWISS-PROT A1AHG8 'Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM)' 100.00 269 99.63 99.63 1.26e-155 REF NP_709414 'formamidopyrimidine-DNA glycosylase [Shigella flexneri 2a str. 301]' 100.00 269 99.63 99.63 1.26e-155 REF NP_418092 'formamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]' 100.00 269 100.00 100.00 3.89e-156 REF NP_312537 'formamidopyrimidine-DNA glycosylase [Escherichia coli O157:H7 str. Sakai]' 100.00 269 99.63 99.63 1.26e-155 REF NP_290215 'formamidopyrimidine-DNA glycosylase [Escherichia coli O157:H7 EDL933]' 100.00 269 99.63 99.63 1.26e-155 REF AP_004156 'formamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase [Escherichia coli W3110]' 100.00 269 100.00 100.00 3.89e-156 GenBank AAN45121 'formamidopyrimidine DNA glycosylase [Shigella flexneri 2a str. 301]' 100.00 269 99.63 99.63 1.26e-155 GenBank AAG58779 'formamidopyrimidine DNA glycosylase [Escherichia coli O157:H7 EDL933]' 100.00 269 99.63 99.63 1.26e-155 GenBank AAC76659 'formamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]' 100.00 269 100.00 100.00 3.89e-156 GenBank AAB18612 'formamidopyrimidine-DNA glycosylase [Escherichia coli]' 100.00 269 100.00 100.00 3.89e-156 GenBank AAA61988 'formamidopyrimidine-DNA glycosylase' 67.29 181 100.00 100.00 1.93e-101 EMBL CAA29431 'unnamed protein product [Escherichia coli]' 100.00 269 100.00 100.00 3.89e-156 DBJ BAE77657 'formamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase [Escherichia coli W3110]' 100.00 269 100.00 100.00 3.89e-156 DBJ BAB37933 'formamidopyrimidine DNA glycosylase [Escherichia coli O157:H7 str. Sakai]' 100.00 269 99.63 99.63 1.26e-155 PDB 1K82 'Crystal Structure Of E.Coli Formamidopyrimidine-Dna Glycosylase (Fpg) Covalently Trapped With Dna' 99.63 268 100.00 100.00 2.08e-155 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 13 16:30:26 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Fpg '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_type _Vector_name $Fpg 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET-11d 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 $Fpg 0.8 mM '[U-2H; U-13C; U-15N]' 'phosphate buffer' 300 mM . DTT 3 mM . NaN3 50 uM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Nova _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Nova _Field_strength 800 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Nova _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $Sample_1 save_ save_HNCOCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label $Sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $Sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $Sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $Sample_1 save_ save_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label $Sample_1 save_ save_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $Sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.1 0.1 n/a temperature 298 1 K 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_cs_set_1 _Saveframe_category assigned_chemical_shifts _Details ; The carbon chemical shifts are for a perdeuterated sample. Hence, the 13Ca, 13Cb, and 15N chemical shifts reported here are shifted upfield approximately 0.4, 0.8, and 0.23 ppm, respectively, relative to the chemical shifts expected for a fully protonated sample. ; loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Fpg _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 . 8 GLU C C 178.2 0.1 1 2 . 8 GLU CA C 58.4 0.1 1 3 . 9 THR H H 7.45 0.02 1 4 . 9 THR C C 173.7 0.1 1 5 . 9 THR CA C 60.7 0.1 1 6 . 9 THR CB C 69.6 0.1 1 7 . 9 THR N N 113.6 0.1 1 8 . 10 SER H H 7.87 0.02 1 9 . 10 SER CA C 57.4 0.1 1 10 . 10 SER CB C 70 0.1 1 11 . 10 SER N N 121.1 0.1 1 12 . 16 PRO C C 177.6 0.1 1 13 . 16 PRO CA C 64.4 0.1 1 14 . 17 HIS H H 7.35 0.02 1 15 . 17 HIS C C 173.7 0.1 1 16 . 17 HIS CA C 56.2 0.1 1 17 . 17 HIS CB C 32.5 0.1 1 18 . 17 HIS N N 114.8 0.1 1 19 . 18 LEU H H 7.08 0.02 1 20 . 18 LEU C C 179.8 0.1 1 21 . 18 LEU CA C 54.8 0.1 1 22 . 18 LEU CB C 44.7 0.1 1 23 . 18 LEU N N 114.6 0.1 1 24 . 19 VAL H H 7.66 0.02 1 25 . 19 VAL C C 178.2 0.1 1 26 . 19 VAL CA C 65.2 0.1 1 27 . 19 VAL CB C 30.2 0.1 1 28 . 19 VAL N N 115.9 0.1 1 29 . 20 GLY H H 8.62 0.02 1 30 . 20 GLY C C 173.6 0.1 1 31 . 20 GLY CA C 44.7 0.1 1 32 . 20 GLY N N 116.1 0.1 1 33 . 21 ALA H H 8.21 0.02 1 34 . 21 ALA C C 174.9 0.1 1 35 . 21 ALA CA C 49.9 0.1 1 36 . 21 ALA CB C 19.9 0.1 1 37 . 21 ALA N N 124.4 0.1 1 38 . 22 THR H H 8.53 0.02 1 39 . 22 THR C C 174.2 0.1 1 40 . 22 THR CA C 61.2 0.1 1 41 . 22 THR CB C 70.5 0.1 1 42 . 22 THR N N 113.5 0.1 1 43 . 23 ILE H H 9.18 0.02 1 44 . 23 ILE C C 175.6 0.1 1 45 . 23 ILE CA C 60.9 0.1 1 46 . 23 ILE CB C 38.6 0.1 1 47 . 23 ILE N N 127.8 0.1 1 48 . 24 LEU H H 9.56 0.02 1 49 . 24 LEU C C 177.9 0.1 1 50 . 24 LEU CA C 57.4 0.1 1 51 . 24 LEU CB C 41 0.1 1 52 . 24 LEU N N 130.6 0.1 1 53 . 25 HIS H H 7.25 0.02 1 54 . 25 HIS C C 171.6 0.1 1 55 . 25 HIS CA C 54.6 0.1 1 56 . 25 HIS CB C 30.2 0.1 1 57 . 25 HIS N N 109.3 0.1 1 58 . 26 ALA H H 9.22 0.02 1 59 . 26 ALA C C 177 0.1 1 60 . 26 ALA CA C 49.7 0.1 1 61 . 26 ALA CB C 21.8 0.1 1 62 . 26 ALA N N 122.1 0.1 1 63 . 27 VAL H H 9.21 0.02 1 64 . 27 VAL C C 174.4 0.1 1 65 . 27 VAL CA C 61.4 0.1 1 66 . 27 VAL CB C 33 0.1 1 67 . 27 VAL N N 122.8 0.1 1 68 . 28 VAL H H 8.84 0.02 1 69 . 28 VAL C C 176.2 0.1 1 70 . 28 VAL CA C 60.5 0.1 1 71 . 28 VAL CB C 30.7 0.1 1 72 . 28 VAL N N 127.4 0.1 1 73 . 29 ARG H H 8.73 0.02 1 74 . 29 ARG C C 177.1 0.1 1 75 . 29 ARG CA C 57.4 0.1 1 76 . 29 ARG N N 127.3 0.1 1 77 . 30 ASN H H 7.28 0.02 1 78 . 30 ASN C C 173.1 0.1 1 79 . 30 ASN CA C 53.4 0.1 1 80 . 30 ASN CB C 40 0.1 1 81 . 30 ASN N N 115.9 0.1 1 82 . 31 GLY H H 8.42 0.02 1 83 . 31 GLY C C 175 0.1 1 84 . 31 GLY CA C 43.6 0.1 1 85 . 31 GLY N N 108.5 0.1 1 86 . 32 ARG H H 8.21 0.02 1 87 . 32 ARG C C 175.1 0.1 1 88 . 32 ARG CA C 54.4 0.1 1 89 . 32 ARG CB C 27.4 0.1 1 90 . 32 ARG N N 123.3 0.1 1 91 . 33 LEU H H 6.63 0.02 1 92 . 33 LEU C C 177.2 0.1 1 93 . 33 LEU CA C 53.2 0.1 1 94 . 33 LEU CB C 39.6 0.1 1 95 . 33 LEU N N 124 0.1 1 96 . 34 ARG H H 8.81 0.02 1 97 . 34 ARG C C 177.5 0.1 1 98 . 34 ARG CA C 59.8 0.1 1 99 . 34 ARG CB C 29.9 0.1 1 100 . 34 ARG N N 124.6 0.1 1 101 . 35 TRP H H 7.18 0.02 1 102 . 35 TRP CA C 55.1 0.1 1 103 . 35 TRP CB C 30.1 0.1 1 104 . 35 TRP N N 110.8 0.1 1 105 . 36 PRO C C 178.1 0.1 1 106 . 36 PRO CA C 62.8 0.1 1 107 . 37 VAL H H 8.96 0.02 1 108 . 37 VAL C C 178.1 0.1 1 109 . 37 VAL CA C 63.5 0.1 1 110 . 37 VAL CB C 31.1 0.1 1 111 . 37 VAL N N 126.6 0.1 1 112 . 38 SER H H 7.84 0.02 1 113 . 38 SER C C 175 0.1 1 114 . 38 SER CA C 60.5 0.1 1 115 . 38 SER CB C 63.9 0.1 1 116 . 38 SER N N 122.5 0.1 1 117 . 39 GLU H H 9.21 0.02 1 118 . 39 GLU C C 178.3 0.1 1 119 . 39 GLU CA C 59.3 0.1 1 120 . 39 GLU CB C 28.8 0.1 1 121 . 39 GLU N N 125.6 0.1 1 122 . 40 GLU H H 9.84 0.02 1 123 . 40 GLU CA C 60.2 0.1 1 124 . 40 GLU CB C 26.4 0.1 1 125 . 40 GLU N N 116.8 0.1 1 126 . 41 ILE H H 7.66 0.02 1 127 . 41 ILE C C 176.6 0.1 1 128 . 41 ILE CA C 62.3 0.1 1 129 . 41 ILE CB C 34.9 0.1 1 130 . 41 ILE N N 115.9 0.1 1 131 . 42 TYR H H 7.08 0.02 1 132 . 42 TYR C C 178.5 0.1 1 133 . 42 TYR CA C 60.9 0.1 1 134 . 42 TYR CB C 37.7 0.1 1 135 . 42 TYR N N 113.5 0.1 1 136 . 43 ARG H H 6.91 0.02 1 137 . 43 ARG C C 175.6 0.1 1 138 . 43 ARG CA C 54.6 0.1 1 139 . 43 ARG CB C 30.2 0.1 1 140 . 43 ARG N N 112.8 0.1 1 141 . 44 LEU H H 6.88 0.02 1 142 . 44 LEU C C 177.7 0.1 1 143 . 44 LEU CA C 55.8 0.1 1 144 . 44 LEU CB C 42.8 0.1 1 145 . 44 LEU N N 121.4 0.1 1 146 . 45 SER H H 8.31 0.02 1 147 . 45 SER C C 173.3 0.1 1 148 . 45 SER CA C 56.9 0.1 1 149 . 45 SER CB C 64.4 0.1 1 150 . 45 SER N N 115.4 0.1 1 151 . 46 ASP H H 8.41 0.02 1 152 . 46 ASP C C 175.2 0.1 1 153 . 46 ASP CA C 55.3 0.1 1 154 . 46 ASP CB C 39.6 0.1 1 155 . 46 ASP N N 127.3 0.1 1 156 . 47 GLN H H 7.7 0.02 1 157 . 47 GLN CA C 51.1 0.1 1 158 . 47 GLN CB C 31.6 0.1 1 159 . 47 GLN N N 115.7 0.1 1 160 . 48 PRO C C 174 0.1 1 161 . 48 PRO CA C 61.6 0.1 1 162 . 49 VAL H H 7.8 0.02 1 163 . 49 VAL C C 177.3 0.1 1 164 . 49 VAL CA C 61.4 0.1 1 165 . 49 VAL CB C 29.7 0.1 1 166 . 49 VAL N N 117.3 0.1 1 167 . 50 LEU H H 9.49 0.02 1 168 . 50 LEU C C 177.8 0.1 1 169 . 50 LEU CA C 55.8 0.1 1 170 . 50 LEU CB C 41 0.1 1 171 . 50 LEU N N 128.5 0.1 1 172 . 51 SER H H 7.53 0.02 1 173 . 51 SER C C 171.3 0.1 1 174 . 51 SER CA C 58.8 0.1 1 175 . 51 SER CB C 64.4 0.1 1 176 . 51 SER N N 110 0.1 1 177 . 52 VAL H H 8.86 0.02 1 178 . 52 VAL CA C 61.2 0.1 1 179 . 52 VAL N N 119.5 0.1 1 180 . 60 LEU C C 175.9 0.1 1 181 . 60 LEU CA C 53.2 0.1 1 182 . 61 LEU H H 9.59 0.02 1 183 . 61 LEU C C 174.4 0.1 1 184 . 61 LEU CA C 53.2 0.1 1 185 . 61 LEU CB C 42 0.1 1 186 . 61 LEU N N 123.3 0.1 1 187 . 62 GLU H H 8.05 0.02 1 188 . 62 GLU CA C 55.5 0.1 1 189 . 62 GLU CB C 30.3 0.1 1 190 . 62 GLU N N 125.3 0.1 1 191 . 64 PRO C C 178.4 0.1 1 192 . 64 PRO CA C 65.9 0.1 1 193 . 65 GLU H H 8.04 0.02 1 194 . 65 GLU C C 175.5 0.1 1 195 . 65 GLU CA C 55.1 0.1 1 196 . 65 GLU CB C 29.7 0.1 1 197 . 65 GLU N N 109.9 0.1 1 198 . 66 GLY H H 7.01 0.02 1 199 . 66 GLY C C 169.1 0.1 1 200 . 66 GLY CA C 45.5 0.1 1 201 . 66 GLY N N 106.4 0.1 1 202 . 67 TRP H H 8 0.02 1 203 . 67 TRP C C 177.8 0.1 1 204 . 67 TRP CA C 54.8 0.1 1 205 . 67 TRP CB C 28.8 0.1 1 206 . 67 TRP N N 117.7 0.1 1 207 . 68 ILE H H 8.69 0.02 1 208 . 68 ILE CA C 59.8 0.1 1 209 . 68 ILE CB C 41.4 0.1 1 210 . 68 ILE N N 118.8 0.1 1 211 . 69 ILE H H 9.25 0.02 1 212 . 69 ILE CA C 59.5 0.1 1 213 . 69 ILE N N 127.6 0.1 1 214 . 75 SER C C 173.8 0.1 1 215 . 75 SER CA C 57.2 0.1 1 216 . 76 GLY H H 7.84 0.02 1 217 . 76 GLY C C 172.8 0.1 1 218 . 76 GLY CA C 44.7 0.1 1 219 . 76 GLY N N 111.7 0.1 1 220 . 77 SER H H 9.04 0.02 1 221 . 77 SER CA C 57.2 0.1 1 222 . 77 SER N N 114 0.1 1 223 . 78 LEU CA C 52.7 0.1 1 224 . 78 LEU CB C 45.7 0.1 1 225 . 79 ARG H H 8.57 0.02 1 226 . 79 ARG C C 174.4 0.1 1 227 . 79 ARG CA C 54.1 0.1 1 228 . 79 ARG CB C 34.9 0.1 1 229 . 79 ARG N N 119.1 0.1 1 230 . 80 ILE H H 8.46 0.02 1 231 . 80 ILE CA C 56.7 0.1 1 232 . 80 ILE CB C 41 0.1 1 233 . 80 ILE N N 121.7 0.1 1 234 . 90 HIS C C 173.9 0.1 1 235 . 90 HIS CA C 53.2 0.1 1 236 . 91 ASP H H 6.99 0.02 1 237 . 91 ASP C C 176.4 0.1 1 238 . 91 ASP CA C 52.3 0.1 1 239 . 91 ASP CB C 39.1 0.1 1 240 . 91 ASP N N 121 0.1 1 241 . 92 HIS H H 7.12 0.02 1 242 . 92 HIS C C 176.2 0.1 1 243 . 92 HIS CA C 58.6 0.1 1 244 . 92 HIS N N 122.4 0.1 1 245 . 93 VAL H H 7.43 0.02 1 246 . 93 VAL C C 173.4 0.1 1 247 . 93 VAL CA C 61.2 0.1 1 248 . 93 VAL CB C 37.2 0.1 1 249 . 93 VAL N N 115 0.1 1 250 . 94 ASP H H 8.7 0.02 1 251 . 94 ASP C C 176.5 0.1 1 252 . 94 ASP CA C 51.8 0.1 1 253 . 94 ASP CB C 44.2 0.1 1 254 . 94 ASP N N 123.4 0.1 1 255 . 95 LEU H H 9.31 0.02 1 256 . 95 LEU C C 174.9 0.1 1 257 . 95 LEU CA C 53.9 0.1 1 258 . 95 LEU CB C 42.8 0.1 1 259 . 95 LEU N N 118.2 0.1 1 260 . 96 VAL H H 8.26 0.02 1 261 . 96 VAL C C 174.8 0.1 1 262 . 96 VAL CA C 63 0.1 1 263 . 96 VAL CB C 30.7 0.1 1 264 . 96 VAL N N 125 0.1 1 265 . 97 MET H H 8.39 0.02 1 266 . 97 MET CA C 52.3 0.1 1 267 . 97 MET CB C 36.3 0.1 1 268 . 97 MET N N 122.7 0.1 1 269 . 98 SER H H 9.51 0.02 1 270 . 98 SER C C 174.3 0.1 1 271 . 98 SER CA C 60.2 0.1 1 272 . 98 SER N N 115.9 0.1 1 273 . 99 ASN H H 7.25 0.02 1 274 . 99 ASN C C 176 0.1 1 275 . 99 ASN CA C 51.5 0.1 1 276 . 99 ASN CB C 37.2 0.1 1 277 . 99 ASN N N 117.5 0.1 1 278 . 100 GLY H H 7.87 0.02 1 279 . 100 GLY C C 173.3 0.1 1 280 . 100 GLY CA C 45 0.1 1 281 . 100 GLY N N 107.4 0.1 1 282 . 101 LYS H H 7.3 0.02 1 283 . 101 LYS CA C 54.1 0.1 1 284 . 101 LYS CB C 33 0.1 1 285 . 101 LYS N N 116.9 0.1 1 286 . 102 VAL C C 175.3 0.1 1 287 . 102 VAL CA C 59.3 0.1 1 288 . 103 LEU H H 8.94 0.02 1 289 . 103 LEU C C 173.7 0.1 1 290 . 103 LEU CA C 53.2 0.1 1 291 . 103 LEU CB C 42.4 0.1 1 292 . 103 LEU N N 126.8 0.1 1 293 . 104 ARG H H 9.35 0.02 1 294 . 104 ARG C C 174.9 0.1 1 295 . 104 ARG CA C 54.8 0.1 1 296 . 104 ARG CB C 33 0.1 1 297 . 104 ARG N N 129.2 0.1 1 298 . 105 TYR H H 9.43 0.02 1 299 . 105 TYR C C 173.1 0.1 1 300 . 105 TYR CA C 55.3 0.1 1 301 . 105 TYR CB C 41.4 0.1 1 302 . 105 TYR N N 130.9 0.1 1 303 . 106 THR H H 8.33 0.02 1 304 . 106 THR C C 174 0.1 1 305 . 106 THR CA C 60.5 0.1 1 306 . 106 THR CB C 70.5 0.1 1 307 . 106 THR N N 126.4 0.1 1 308 . 107 ASP H H 7.98 0.02 1 309 . 107 ASP CA C 51.3 0.1 1 310 . 107 ASP CB C 42.4 0.1 1 311 . 107 ASP N N 117 0.1 1 312 . 108 PRO C C 177.7 0.1 1 313 . 108 PRO CA C 64 0.1 1 314 . 109 ARG H H 7.49 0.02 1 315 . 109 ARG C C 174.8 0.1 1 316 . 109 ARG CA C 54.6 0.1 1 317 . 109 ARG CB C 29.2 0.1 1 318 . 109 ARG N N 113.1 0.1 1 319 . 110 ARG H H 7.4 0.02 1 320 . 110 ARG C C 177.8 0.1 1 321 . 110 ARG CA C 58.1 0.1 1 322 . 110 ARG CB C 26.4 0.1 1 323 . 110 ARG N N 113.1 0.1 1 324 . 111 PHE H H 7.49 0.02 1 325 . 111 PHE C C 176.5 0.1 1 326 . 111 PHE CA C 56.2 0.1 1 327 . 111 PHE CB C 40.5 0.1 1 328 . 111 PHE N N 115.9 0.1 1 329 . 112 GLY H H 8.14 0.02 1 330 . 112 GLY C C 170.7 0.1 1 331 . 112 GLY CA C 43.8 0.1 1 332 . 112 GLY N N 108.9 0.1 1 333 . 113 ALA H H 9.15 0.02 1 334 . 113 ALA C C 174.8 0.1 1 335 . 113 ALA CA C 52.5 0.1 1 336 . 113 ALA CB C 22.7 0.1 1 337 . 113 ALA N N 116.7 0.1 1 338 . 114 TRP H H 9.05 0.02 1 339 . 114 TRP C C 174.7 0.1 1 340 . 114 TRP CA C 57.4 0.1 1 341 . 114 TRP CB C 31.1 0.1 1 342 . 114 TRP N N 121.7 0.1 1 343 . 115 LEU H H 9.31 0.02 1 344 . 115 LEU CA C 51.5 0.1 1 345 . 115 LEU CB C 45.7 0.1 1 346 . 115 LEU N N 122.1 0.1 1 347 . 116 TRP H H 8.52 0.02 1 348 . 116 TRP C C 176.3 0.1 1 349 . 116 TRP CA C 54.8 0.1 1 350 . 116 TRP CB C 34.9 0.1 1 351 . 116 TRP N N 119.4 0.1 1 352 . 117 THR H H 7.88 0.02 1 353 . 117 THR C C 173.8 0.1 1 354 . 117 THR CA C 59.1 0.1 1 355 . 117 THR CB C 69.6 0.1 1 356 . 117 THR N N 120.4 0.1 1 357 . 118 LYS H H 8.52 0.02 1 358 . 118 LYS C C 176.3 0.1 1 359 . 118 LYS CA C 58.6 0.1 1 360 . 118 LYS N N 127.8 0.1 1 361 . 119 GLU H H 7.71 0.02 1 362 . 119 GLU CA C 53.7 0.1 1 363 . 119 GLU N N 113.9 0.1 1 364 . 124 ASN C C 169.1 0.1 1 365 . 124 ASN CA C 54.8 0.1 1 366 . 125 VAL H H 8.83 0.02 1 367 . 125 VAL C C 178.9 0.1 1 368 . 125 VAL CA C 65.4 0.1 1 369 . 125 VAL CB C 31.1 0.1 1 370 . 125 VAL N N 118.4 0.1 1 371 . 126 LEU H H 7.87 0.02 1 372 . 126 LEU C C 177.8 0.1 1 373 . 126 LEU CA C 57.4 0.1 1 374 . 126 LEU CB C 41 0.1 1 375 . 126 LEU N N 121.1 0.1 1 376 . 127 THR H H 8.38 0.02 1 377 . 127 THR CA C 66.6 0.1 1 378 . 127 THR N N 116.5 0.1 1 379 . 133 PRO C C 176.9 0.1 1 380 . 133 PRO CA C 63 0.1 1 381 . 134 LEU H H 7.71 0.02 1 382 . 134 LEU C C 176.9 0.1 1 383 . 134 LEU CA C 53.7 0.1 1 384 . 134 LEU CB C 38.6 0.1 1 385 . 134 LEU N N 113.9 0.1 1 386 . 135 SER H H 7.56 0.02 1 387 . 135 SER CA C 57.2 0.1 1 388 . 135 SER CB C 65.8 0.1 1 389 . 135 SER N N 115.4 0.1 1 390 . 136 ASP H H 8.31 0.02 1 391 . 136 ASP C C 176.7 0.1 1 392 . 136 ASP CA C 55.5 0.1 1 393 . 136 ASP CB C 40.5 0.1 1 394 . 136 ASP N N 118.2 0.1 1 395 . 137 ASP H H 7.76 0.02 1 396 . 137 ASP C C 175.5 0.1 1 397 . 137 ASP CA C 55.1 0.1 1 398 . 137 ASP CB C 40.5 0.1 1 399 . 137 ASP N N 116.5 0.1 1 400 . 138 PHE H H 7.25 0.02 1 401 . 138 PHE C C 172 0.1 1 402 . 138 PHE CA C 57.2 0.1 1 403 . 138 PHE CB C 38.2 0.1 1 404 . 138 PHE N N 117.5 0.1 1 405 . 139 ASN H H 6.41 0.02 1 406 . 139 ASN C C 174.1 0.1 1 407 . 139 ASN CA C 50.8 0.1 1 408 . 139 ASN CB C 39.6 0.1 1 409 . 139 ASN N N 119.6 0.1 1 410 . 140 GLY H H 8.86 0.02 1 411 . 140 GLY C C 173.9 0.1 1 412 . 140 GLY CA C 47.3 0.1 1 413 . 140 GLY N N 106.9 0.1 1 414 . 141 GLU H H 8.31 0.02 1 415 . 141 GLU C C 178.6 0.1 1 416 . 141 GLU CA C 59.5 0.1 1 417 . 141 GLU CB C 28.8 0.1 1 418 . 141 GLU N N 122.8 0.1 1 419 . 142 TYR H H 8.38 0.02 1 420 . 142 TYR C C 176.6 0.1 1 421 . 142 TYR CA C 60.5 0.1 1 422 . 142 TYR CB C 38.2 0.1 1 423 . 142 TYR N N 121.1 0.1 1 424 . 143 LEU H H 8.13 0.02 1 425 . 143 LEU C C 178 0.1 1 426 . 143 LEU CA C 57.4 0.1 1 427 . 143 LEU CB C 41.9 0.1 1 428 . 143 LEU N N 118.3 0.1 1 429 . 144 HIS H H 8.76 0.02 1 430 . 144 HIS CA C 60.9 0.1 1 431 . 144 HIS CB C 30.7 0.1 1 432 . 144 HIS N N 119 0.1 1 433 . 145 GLN H H 8.31 0.02 1 434 . 145 GLN C C 179.7 0.1 1 435 . 145 GLN CA C 58.6 0.1 1 436 . 145 GLN CB C 27.4 0.1 1 437 . 145 GLN N N 118.2 0.1 1 438 . 146 LYS H H 7.86 0.02 1 439 . 146 LYS C C 178.7 0.1 1 440 . 146 LYS CA C 55.5 0.1 1 441 . 146 LYS CB C 32.1 0.1 1 442 . 146 LYS N N 116.1 0.1 1 443 . 147 CYS H H 7.98 0.02 1 444 . 147 CYS C C 175 0.1 1 445 . 147 CYS CA C 62.1 0.1 1 446 . 147 CYS CB C 27.8 0.1 1 447 . 147 CYS N N 116.6 0.1 1 448 . 148 ALA H H 7.15 0.02 1 449 . 148 ALA CA C 54.6 0.1 1 450 . 148 ALA N N 121.7 0.1 1 451 . 151 LYS C C 175.7 0.1 1 452 . 151 LYS CA C 54.6 0.1 1 453 . 151 LYS CB C 29.7 0.1 1 454 . 152 THR H H 7.26 0.02 1 455 . 152 THR C C 172.5 0.1 1 456 . 152 THR CA C 60.2 0.1 1 457 . 152 THR CB C 70 0.1 1 458 . 152 THR N N 114 0.1 1 459 . 153 ALA H H 8.65 0.02 1 460 . 153 ALA C C 178.8 0.1 1 461 . 153 ALA CA C 52.5 0.1 1 462 . 153 ALA CB C 17.5 0.1 1 463 . 153 ALA N N 128 0.1 1 464 . 154 ILE H H 8.98 0.02 1 465 . 154 ILE C C 174.9 0.1 1 466 . 154 ILE CA C 60 0.1 1 467 . 154 ILE CB C 38.6 0.1 1 468 . 154 ILE N N 119.6 0.1 1 469 . 155 LYS H H 7.23 0.02 1 470 . 155 LYS CA C 63 0.1 1 471 . 155 LYS CB C 28.8 0.1 1 472 . 155 LYS N N 120.2 0.1 1 473 . 156 PRO C C 179.3 0.1 1 474 . 156 PRO CA C 64.4 0.1 1 475 . 157 TRP H H 7.22 0.02 1 476 . 157 TRP C C 176.3 0.1 1 477 . 157 TRP CA C 57.9 0.1 1 478 . 157 TRP CB C 31.6 0.1 1 479 . 157 TRP N N 122.7 0.1 1 480 . 158 LEU H H 7.8 0.02 1 481 . 158 LEU C C 175.9 0.1 1 482 . 158 LEU CA C 56.2 0.1 1 483 . 158 LEU CB C 42.4 0.1 1 484 . 158 LEU N N 113.8 0.1 1 485 . 159 MET H H 6.68 0.02 1 486 . 159 MET C C 174.8 0.1 1 487 . 159 MET CA C 54.8 0.1 1 488 . 159 MET CB C 33.5 0.1 1 489 . 159 MET N N 110.3 0.1 1 490 . 160 ASP H H 7.71 0.02 1 491 . 160 ASP C C 176.5 0.1 1 492 . 160 ASP CA C 53.2 0.1 1 493 . 160 ASP CB C 42.8 0.1 1 494 . 160 ASP N N 123.4 0.1 1 495 . 161 ASN H H 8.65 0.02 1 496 . 161 ASN C C 176.3 0.1 1 497 . 161 ASN CA C 54.4 0.1 1 498 . 161 ASN CB C 38.6 0.1 1 499 . 161 ASN N N 124.7 0.1 1 500 . 162 LYS H H 8.98 0.02 1 501 . 162 LYS C C 178.1 0.1 1 502 . 162 LYS CA C 58.1 0.1 1 503 . 162 LYS CB C 32 0.1 1 504 . 162 LYS N N 118.1 0.1 1 505 . 163 LEU H H 7.88 0.02 1 506 . 163 LEU CA C 56 0.1 1 507 . 163 LEU CB C 38.6 0.1 1 508 . 163 LEU N N 120.4 0.1 1 509 . 172 ALA C C 179.9 0.1 1 510 . 172 ALA CA C 56.7 0.1 1 511 . 173 SER H H 8.42 0.02 1 512 . 173 SER C C 174 0.1 1 513 . 173 SER CA C 64.9 0.1 1 514 . 173 SER N N 119.5 0.1 1 515 . 174 GLU H H 7.43 0.02 1 516 . 174 GLU C C 179.7 0.1 1 517 . 174 GLU CA C 59.3 0.1 1 518 . 174 GLU CB C 31.6 0.1 1 519 . 174 GLU N N 116.1 0.1 1 520 . 175 SER H H 8.77 0.02 1 521 . 175 SER C C 175.2 0.1 1 522 . 175 SER CA C 62.3 0.1 1 523 . 175 SER N N 117 0.1 1 524 . 176 LEU H H 7.49 0.02 1 525 . 176 LEU C C 178.5 0.1 1 526 . 176 LEU CA C 58.4 0.1 1 527 . 176 LEU CB C 38.2 0.1 1 528 . 176 LEU N N 121.7 0.1 1 529 . 177 PHE H H 7.69 0.02 1 530 . 177 PHE CA C 61.9 0.1 1 531 . 177 PHE CB C 38.2 0.1 1 532 . 177 PHE N N 118.2 0.1 1 533 . 178 ALA H H 7.84 0.02 1 534 . 178 ALA C C 178.5 0.1 1 535 . 178 ALA CA C 53.9 0.1 1 536 . 178 ALA CB C 17.5 0.1 1 537 . 178 ALA N N 122.5 0.1 1 538 . 179 ALA H H 7.98 0.02 1 539 . 179 ALA C C 175.7 0.1 1 540 . 179 ALA CA C 51.1 0.1 1 541 . 179 ALA CB C 19.9 0.1 1 542 . 179 ALA N N 116.6 0.1 1 543 . 180 GLY H H 7.77 0.02 1 544 . 180 GLY C C 175.6 0.1 1 545 . 180 GLY CA C 46.4 0.1 1 546 . 180 GLY N N 108.3 0.1 1 547 . 181 ILE H H 8.31 0.02 1 548 . 181 ILE C C 173.9 0.1 1 549 . 181 ILE CA C 59.5 0.1 1 550 . 181 ILE CB C 41 0.1 1 551 . 181 ILE N N 122.8 0.1 1 552 . 182 HIS H H 8.12 0.02 1 553 . 182 HIS CA C 52.3 0.1 1 554 . 182 HIS N N 121.5 0.1 1 555 . 183 PRO C C 175.3 0.1 1 556 . 183 PRO CA C 64.2 0.1 1 557 . 183 PRO CB C 32.5 0.1 1 558 . 184 ASP H H 9.97 0.02 1 559 . 184 ASP C C 178.1 0.1 1 560 . 184 ASP CA C 54.4 0.1 1 561 . 184 ASP CB C 41 0.1 1 562 . 184 ASP N N 115.4 0.1 1 563 . 185 ARG H H 7.78 0.02 1 564 . 185 ARG C C 176.3 0.1 1 565 . 185 ARG CA C 55.3 0.1 1 566 . 185 ARG CB C 27.8 0.1 1 567 . 185 ARG N N 121.3 0.1 1 568 . 186 LEU H H 8.67 0.02 1 569 . 186 LEU C C 169.4 0.1 1 570 . 186 LEU CA C 54.1 0.1 1 571 . 186 LEU CB C 40.5 0.1 1 572 . 186 LEU N N 120.9 0.1 1 573 . 187 ALA H H 9.35 0.02 1 574 . 187 ALA C C 178.2 0.1 1 575 . 187 ALA CA C 55.5 0.1 1 576 . 187 ALA CB C 17.1 0.1 1 577 . 187 ALA N N 129.6 0.1 1 578 . 188 SER H H 7.73 0.02 1 579 . 188 SER C C 175 0.1 1 580 . 188 SER CA C 59.5 0.1 1 581 . 188 SER CB C 62.5 0.1 1 582 . 188 SER N N 110.3 0.1 1 583 . 189 SER H H 8.09 0.02 1 584 . 189 SER C C 175.3 0.1 1 585 . 189 SER CA C 58.6 0.1 1 586 . 189 SER CB C 65.8 0.1 1 587 . 189 SER N N 117.7 0.1 1 588 . 190 LEU H H 7.3 0.02 1 589 . 190 LEU C C 177.9 0.1 1 590 . 190 LEU CA C 54.8 0.1 1 591 . 190 LEU CB C 41.4 0.1 1 592 . 190 LEU N N 124.8 0.1 1 593 . 191 SER H H 9.67 0.02 1 594 . 191 SER C C 175.5 0.1 1 595 . 191 SER CA C 56.2 0.1 1 596 . 191 SER CB C 65.3 0.1 1 597 . 191 SER N N 120.9 0.1 1 598 . 192 LEU H H 8.87 0.02 1 599 . 192 LEU C C 178.1 0.1 1 600 . 192 LEU CA C 58.6 0.1 1 601 . 192 LEU CB C 39.6 0.1 1 602 . 192 LEU N N 123.6 0.1 1 603 . 193 ALA H H 8.26 0.02 1 604 . 193 ALA CA C 54.8 0.1 1 605 . 193 ALA CB C 17.5 0.1 1 606 . 193 ALA N N 119.8 0.1 1 607 . 194 GLU H H 8.04 0.02 1 608 . 194 GLU C C 178.5 0.1 1 609 . 194 GLU CA C 59.3 0.1 1 610 . 194 GLU CB C 28.8 0.1 1 611 . 194 GLU N N 119.4 0.1 1 612 . 195 CYS H H 8.26 0.02 1 613 . 195 CYS C C 176.8 0.1 1 614 . 195 CYS CA C 64.7 0.1 1 615 . 195 CYS CB C 28.8 0.1 1 616 . 195 CYS N N 117.5 0.1 1 617 . 196 GLU H H 8.94 0.02 1 618 . 196 GLU C C 178.8 0.1 1 619 . 196 GLU CA C 59.1 0.1 1 620 . 196 GLU CB C 28.8 0.1 1 621 . 196 GLU N N 120.4 0.1 1 622 . 197 LEU H H 7.74 0.02 1 623 . 197 LEU C C 173 0.1 1 624 . 197 LEU CA C 57.2 0.1 1 625 . 197 LEU CB C 41 0.1 1 626 . 197 LEU N N 120.5 0.1 1 627 . 208 ARG C C 179 0.1 1 628 . 208 ARG CA C 56.2 0.1 1 629 . 209 SER H H 7.07 0.02 1 630 . 209 SER CA C 64.2 0.1 1 631 . 209 SER CB C 66.3 0.1 1 632 . 209 SER N N 111.4 0.1 1 633 . 210 ILE H H 8.5 0.02 1 634 . 210 ILE CA C 59.1 0.1 1 635 . 210 ILE CB C 45.7 0.1 1 636 . 210 ILE N N 119.5 0.1 1 637 . 212 GLN C C 177.2 0.1 1 638 . 212 GLN CA C 56.2 0.1 1 639 . 212 GLN CB C 28.3 0.1 1 640 . 213 GLY H H 8.07 0.02 1 641 . 213 GLY C C 174.9 0.1 1 642 . 213 GLY CA C 45.4 0.1 1 643 . 213 GLY N N 108 0.1 1 644 . 214 GLY H H 8.19 0.02 1 645 . 214 GLY C C 174.6 0.1 1 646 . 214 GLY CA C 45.2 0.1 1 647 . 214 GLY N N 108.4 0.1 1 648 . 215 THR H H 8.02 0.02 1 649 . 215 THR C C 174.8 0.1 1 650 . 215 THR CA C 61.9 0.1 1 651 . 215 THR N N 113.1 0.1 1 652 . 216 THR H H 8.15 0.02 1 653 . 216 THR C C 174.9 0.1 1 654 . 216 THR CA C 61.6 0.1 1 655 . 216 THR CB C 70 0.1 1 656 . 216 THR N N 115.4 0.1 1 657 . 217 LEU H H 8.15 0.02 1 658 . 217 LEU C C 177.7 0.1 1 659 . 217 LEU CA C 55.5 0.1 1 660 . 217 LEU CB C 41 0.1 1 661 . 217 LEU N N 123.3 0.1 1 662 . 218 LYS H H 8.12 0.02 1 663 . 218 LYS C C 176.7 0.1 1 664 . 218 LYS CA C 56.9 0.1 1 665 . 218 LYS CB C 32.1 0.1 1 666 . 218 LYS N N 120.3 0.1 1 667 . 219 ASP H H 8.08 0.02 1 668 . 219 ASP C C 176.5 0.1 1 669 . 219 ASP CA C 54.6 0.1 1 670 . 219 ASP CB C 40.5 0.1 1 671 . 219 ASP N N 119.2 0.1 1 672 . 220 PHE H H 7.98 0.02 1 673 . 220 PHE C C 176.1 0.1 1 674 . 220 PHE CA C 58.4 0.1 1 675 . 220 PHE CB C 39.1 0.1 1 676 . 220 PHE N N 119.7 0.1 1 677 . 221 LEU H H 8.09 0.02 1 678 . 221 LEU C C 177.5 0.1 1 679 . 221 LEU CA C 55.1 0.1 1 680 . 221 LEU CB C 41.4 0.1 1 681 . 221 LEU N N 121.1 0.1 1 682 . 222 GLN H H 8.08 0.02 1 683 . 222 GLN C C 176.4 0.1 1 684 . 222 GLN CA C 55.3 0.1 1 685 . 222 GLN CB C 28.8 0.1 1 686 . 222 GLN N N 119.2 0.1 1 687 . 223 SER H H 8.24 0.02 1 688 . 223 SER C C 174.4 0.1 1 689 . 223 SER CA C 58.6 0.1 1 690 . 223 SER CB C 63.5 0.1 1 691 . 223 SER N N 116.2 0.1 1 692 . 224 ASP H H 8.24 0.02 1 693 . 224 ASP C C 176.7 0.1 1 694 . 224 ASP CA C 53.9 0.1 1 695 . 224 ASP CB C 40.5 0.1 1 696 . 224 ASP N N 121.1 0.1 1 697 . 225 GLY H H 8.21 0.02 1 698 . 225 GLY C C 173.8 0.1 1 699 . 225 GLY CA C 45 0.1 1 700 . 225 GLY N N 108 0.1 1 701 . 226 LYS H H 7.94 0.02 1 702 . 226 LYS CA C 53.9 0.1 1 703 . 226 LYS CB C 31.6 0.1 1 704 . 226 LYS N N 121.4 0.1 1 705 . 227 PRO C C 177.4 0.1 1 706 . 227 PRO CA C 62.8 0.1 1 707 . 228 GLY H H 8.39 0.02 1 708 . 228 GLY C C 173.6 0.1 1 709 . 228 GLY CA C 45 0.1 1 710 . 228 GLY N N 108.8 0.1 1 711 . 229 TYR H H 7.88 0.02 1 712 . 229 TYR C C 175.4 0.1 1 713 . 229 TYR CA C 57.6 0.1 1 714 . 229 TYR CB C 38.6 0.1 1 715 . 229 TYR N N 119.7 0.1 1 716 . 230 PHE H H 7.88 0.02 1 717 . 230 PHE C C 175.1 0.1 1 718 . 230 PHE CA C 57.2 0.1 1 719 . 230 PHE CB C 39.1 0.1 1 720 . 230 PHE N N 120.4 0.1 1 721 . 231 ALA H H 7.95 0.02 1 722 . 231 ALA C C 177.4 0.1 1 723 . 231 ALA CA C 52.3 0.1 1 724 . 231 ALA CB C 18.9 0.1 1 725 . 231 ALA N N 124.6 0.1 1 726 . 232 GLN H H 8 0.02 1 727 . 232 GLN CA C 55.3 0.1 1 728 . 232 GLN CB C 28.8 0.1 1 729 . 232 GLN N N 117.7 0.1 1 730 . 233 GLU C C 176.3 0.1 1 731 . 233 GLU CA C 55.5 0.1 1 732 . 233 GLU CB C 30.6 0.1 1 733 . 234 LEU H H 8.12 0.02 1 734 . 234 LEU C C 177.1 0.1 1 735 . 234 LEU CA C 54.1 0.1 1 736 . 234 LEU CB C 40.5 0.1 1 737 . 234 LEU N N 123.9 0.1 1 738 . 235 GLN H H 10.94 0.02 1 739 . 235 GLN C C 179.1 0.1 1 740 . 235 GLN CA C 56.9 0.1 1 741 . 235 GLN CB C 30.7 0.1 1 742 . 235 GLN N N 123.1 0.1 1 743 . 236 VAL H H 10.11 0.02 1 744 . 236 VAL C C 173.5 0.1 1 745 . 236 VAL CA C 61.6 0.1 1 746 . 236 VAL CB C 34.4 0.1 1 747 . 236 VAL N N 115.3 0.1 1 748 . 237 TYR H H 8.98 0.02 1 749 . 237 TYR CA C 60.2 0.1 1 750 . 237 TYR CB C 38.2 0.1 1 751 . 237 TYR N N 123.6 0.1 1 752 . 238 GLY C C 174.4 0.1 1 753 . 238 GLY CA C 45 0.1 1 754 . 238 GLY N N 108.8 0.1 1 755 . 238 GLY H H 3.03 0.02 1 756 . 239 ARG H H 6.63 0.02 1 757 . 239 ARG C C 175.3 0.1 1 758 . 239 ARG CA C 54.4 0.1 1 759 . 239 ARG CB C 28.3 0.1 1 760 . 239 ARG N N 116.7 0.1 1 761 . 240 LYS H H 7.25 0.02 1 762 . 240 LYS C C 177.9 0.1 1 763 . 240 LYS CA C 58.6 0.1 1 764 . 240 LYS CB C 32.1 0.1 1 765 . 240 LYS N N 118.2 0.1 1 766 . 241 GLY H H 9.22 0.02 1 767 . 241 GLY C C 173.3 0.1 1 768 . 241 GLY CA C 45.2 0.1 1 769 . 241 GLY N N 115.2 0.1 1 770 . 242 GLU H H 8.18 0.02 1 771 . 242 GLU CA C 53.4 0.1 1 772 . 242 GLU CB C 32.1 0.1 1 773 . 242 GLU N N 121.7 0.1 1 774 . 243 PRO C C 177.8 0.1 1 775 . 243 PRO CA C 62.8 0.1 1 776 . 243 PRO CB C 31.1 0.1 1 777 . 244 CYS H H 8.46 0.02 1 778 . 244 CYS C C 178.5 0.1 1 779 . 244 CYS CA C 59.5 0.1 1 780 . 244 CYS CB C 31.1 0.1 1 781 . 244 CYS N N 128 0.1 1 782 . 245 ARG H H 9.82 0.02 1 783 . 245 ARG C C 176.6 0.1 1 784 . 245 ARG CA C 58.1 0.1 1 785 . 245 ARG CB C 29.3 0.1 1 786 . 245 ARG N N 130.1 0.1 1 787 . 246 VAL H H 9.75 0.02 1 788 . 246 VAL C C 177.6 0.1 1 789 . 246 VAL CA C 64.7 0.1 1 790 . 246 VAL CB C 32.1 0.1 1 791 . 246 VAL N N 122.5 0.1 1 792 . 247 CYS H H 8.6 0.02 1 793 . 247 CYS C C 177.2 0.1 1 794 . 247 CYS CA C 58.6 0.1 1 795 . 247 CYS CB C 33 0.1 1 796 . 247 CYS N N 118.2 0.1 1 797 . 248 GLY H H 7.86 0.02 1 798 . 248 GLY C C 173 0.1 1 799 . 248 GLY CA C 45.7 0.1 1 800 . 248 GLY N N 113 0.1 1 801 . 249 THR H H 9.01 0.02 1 802 . 249 THR CA C 62.3 0.1 1 803 . 249 THR CB C 67.7 0.1 1 804 . 249 THR N N 124.9 0.1 1 805 . 250 PRO C C 178.2 0.1 1 806 . 250 PRO CA C 63 0.1 1 807 . 250 PRO CB C 30.7 0.1 1 808 . 251 ILE H H 9.03 0.02 1 809 . 251 ILE C C 174.8 0.1 1 810 . 251 ILE CA C 59.5 0.1 1 811 . 251 ILE CB C 34.4 0.1 1 812 . 251 ILE N N 128.7 0.1 1 813 . 252 VAL H H 8.57 0.02 1 814 . 252 VAL C C 173.3 0.1 1 815 . 252 VAL CA C 61.2 0.1 1 816 . 252 VAL CB C 32.5 0.1 1 817 . 252 VAL N N 129.9 0.1 1 818 . 253 ALA H H 8.28 0.02 1 819 . 253 ALA C C 176.7 0.1 1 820 . 253 ALA CA C 49.2 0.1 1 821 . 253 ALA CB C 22.2 0.1 1 822 . 253 ALA N N 124.3 0.1 1 823 . 254 THR H H 8.7 0.02 1 824 . 254 THR C C 173.3 0.1 1 825 . 254 THR CA C 57.9 0.1 1 826 . 254 THR CB C 69.1 0.1 1 827 . 254 THR N N 117 0.1 1 828 . 255 LYS H H 8.42 0.02 1 829 . 255 LYS C C 174.7 0.1 1 830 . 255 LYS CA C 55.3 0.1 1 831 . 255 LYS CB C 35.8 0.1 1 832 . 255 LYS N N 122.8 0.1 1 833 . 256 HIS H H 8.63 0.02 1 834 . 256 HIS CA C 55.1 0.1 1 835 . 256 HIS CB C 33 0.1 1 836 . 256 HIS N N 118.2 0.1 1 837 . 258 GLN C C 175.1 0.1 1 838 . 258 GLN CA C 57 0.1 1 839 . 258 GLN CB C 26.5 0.1 1 840 . 259 ARG H H 7.94 0.02 1 841 . 259 ARG C C 175.9 0.1 1 842 . 259 ARG CA C 52.7 0.1 1 843 . 259 ARG CB C 29.7 0.1 1 844 . 259 ARG N N 118.9 0.1 1 845 . 260 ALA H H 9.07 0.02 1 846 . 260 ALA C C 177.5 0.1 1 847 . 260 ALA CA C 63 0.1 1 848 . 260 ALA CB C 19.4 0.1 1 849 . 260 ALA N N 124.8 0.1 1 850 . 261 THR H H 8.29 0.02 1 851 . 261 THR C C 171.1 0.1 1 852 . 261 THR CA C 61.2 0.1 1 853 . 261 THR CB C 70 0.1 1 854 . 261 THR N N 119.4 0.1 1 855 . 262 PHE H H 8.28 0.02 1 856 . 262 PHE C C 174 0.1 1 857 . 262 PHE CA C 55.1 0.1 1 858 . 262 PHE CB C 43.3 0.1 1 859 . 262 PHE N N 124.3 0.1 1 860 . 263 TYR H H 9.01 0.02 1 861 . 263 TYR C C 170.9 0.1 1 862 . 263 TYR CA C 56.2 0.1 1 863 . 263 TYR CB C 40 0.1 1 864 . 263 TYR N N 117.5 0.1 1 865 . 264 CYS H H 9.42 0.02 1 866 . 264 CYS C C 176.4 0.1 1 867 . 264 CYS CA C 56.2 0.1 1 868 . 264 CYS CB C 31.1 0.1 1 869 . 264 CYS N N 122.1 0.1 1 870 . 265 ARG H H 8.91 0.02 1 871 . 265 ARG C C 175.5 0.1 1 872 . 265 ARG CA C 56.7 0.1 1 873 . 265 ARG CB C 30 0.1 1 874 . 265 ARG N N 125.9 0.1 1 875 . 266 GLN H H 9.14 0.02 1 876 . 266 GLN C C 177.7 0.1 1 877 . 266 GLN CA C 56.9 0.1 1 878 . 266 GLN CB C 30.7 0.1 1 879 . 266 GLN N N 124.4 0.1 1 880 . 267 CYS H H 9.62 0.02 1 881 . 267 CYS C C 175.7 0.1 1 882 . 267 CYS CA C 63.5 0.1 1 883 . 267 CYS CB C 31.1 0.1 1 884 . 267 CYS N N 121.2 0.1 1 885 . 268 GLN H H 7.49 0.02 1 886 . 268 GLN C C 173.1 0.1 1 887 . 268 GLN CA C 55.1 0.1 1 888 . 268 GLN CB C 31.6 0.1 1 889 . 268 GLN N N 115 0.1 1 890 . 269 LYS H H 7.73 0.02 1 891 . 269 LYS CA C 56.5 0.1 1 892 . 269 LYS CB C 29.3 0.1 1 893 . 269 LYS N N 125.8 0.1 1 stop_ save_