data_19242 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The solution NMR structure of E. coli apo-HisJ ; _BMRB_accession_number 19242 _BMRB_flat_file_name bmr19242.str _Entry_type original _Submission_date 2013-05-15 _Accession_date 2013-05-15 _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 Chu Byron 'C. H.' . 2 Vogel Hans J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 229 "13C chemical shifts" 697 "15N chemical shifts" 229 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-09 update BMRB 'update entry citation' 2013-09-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19243 'Backbone chemical shifts of isolated Domain 1 from E. coli HisJ' 19244 'Backbone chemical shifts of isolated Domain 2 from E. coli HisJ' 19245 'Backbone chemical shifts from E. coli HisJ complexed with Histidine' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24036119 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chu Byron C.H. . 2 Dewolf Timothy . . 3 Vogel Hans J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31409 _Page_last 31422 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name apo-HisJ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label apo-HisJ $apo-HisJ stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_apo-HisJ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common apo-HisJ _Molecular_mass 26264.783 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 241 _Mol_residue_sequence ; GGMAIPQNIRIGTDPTYAPF ESKNSQGELVGFDIDLAKEL CKRINTQCTFVENPLDALIP SLKAKKIDAIMSSLSITEKR QQEIAFTDKLYAADSRLVVA KNSDIQPTVESLKGKRVGVL QGTTQETFGNEHWAPKGIEI VSYQGQDNIYSDLTAGRIDA AFQDEVAASEGFLKQPVGKD YKFGGPSVKDEKLFGVGTGM GLRKEDNELREALNKAFAEM RADGTYEKLAKKYFDFDVYG G ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLY 3 MET 4 ALA 5 ILE 6 PRO 7 GLN 8 ASN 9 ILE 10 ARG 11 ILE 12 GLY 13 THR 14 ASP 15 PRO 16 THR 17 TYR 18 ALA 19 PRO 20 PHE 21 GLU 22 SER 23 LYS 24 ASN 25 SER 26 GLN 27 GLY 28 GLU 29 LEU 30 VAL 31 GLY 32 PHE 33 ASP 34 ILE 35 ASP 36 LEU 37 ALA 38 LYS 39 GLU 40 LEU 41 CYS 42 LYS 43 ARG 44 ILE 45 ASN 46 THR 47 GLN 48 CYS 49 THR 50 PHE 51 VAL 52 GLU 53 ASN 54 PRO 55 LEU 56 ASP 57 ALA 58 LEU 59 ILE 60 PRO 61 SER 62 LEU 63 LYS 64 ALA 65 LYS 66 LYS 67 ILE 68 ASP 69 ALA 70 ILE 71 MET 72 SER 73 SER 74 LEU 75 SER 76 ILE 77 THR 78 GLU 79 LYS 80 ARG 81 GLN 82 GLN 83 GLU 84 ILE 85 ALA 86 PHE 87 THR 88 ASP 89 LYS 90 LEU 91 TYR 92 ALA 93 ALA 94 ASP 95 SER 96 ARG 97 LEU 98 VAL 99 VAL 100 ALA 101 LYS 102 ASN 103 SER 104 ASP 105 ILE 106 GLN 107 PRO 108 THR 109 VAL 110 GLU 111 SER 112 LEU 113 LYS 114 GLY 115 LYS 116 ARG 117 VAL 118 GLY 119 VAL 120 LEU 121 GLN 122 GLY 123 THR 124 THR 125 GLN 126 GLU 127 THR 128 PHE 129 GLY 130 ASN 131 GLU 132 HIS 133 TRP 134 ALA 135 PRO 136 LYS 137 GLY 138 ILE 139 GLU 140 ILE 141 VAL 142 SER 143 TYR 144 GLN 145 GLY 146 GLN 147 ASP 148 ASN 149 ILE 150 TYR 151 SER 152 ASP 153 LEU 154 THR 155 ALA 156 GLY 157 ARG 158 ILE 159 ASP 160 ALA 161 ALA 162 PHE 163 GLN 164 ASP 165 GLU 166 VAL 167 ALA 168 ALA 169 SER 170 GLU 171 GLY 172 PHE 173 LEU 174 LYS 175 GLN 176 PRO 177 VAL 178 GLY 179 LYS 180 ASP 181 TYR 182 LYS 183 PHE 184 GLY 185 GLY 186 PRO 187 SER 188 VAL 189 LYS 190 ASP 191 GLU 192 LYS 193 LEU 194 PHE 195 GLY 196 VAL 197 GLY 198 THR 199 GLY 200 MET 201 GLY 202 LEU 203 ARG 204 LYS 205 GLU 206 ASP 207 ASN 208 GLU 209 LEU 210 ARG 211 GLU 212 ALA 213 LEU 214 ASN 215 LYS 216 ALA 217 PHE 218 ALA 219 GLU 220 MET 221 ARG 222 ALA 223 ASP 224 GLY 225 THR 226 TYR 227 GLU 228 LYS 229 LEU 230 ALA 231 LYS 232 LYS 233 TYR 234 PHE 235 ASP 236 PHE 237 ASP 238 VAL 239 TYR 240 GLY 241 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 BMRB 16204 HisJ 98.76 238 100.00 100.00 3.06e-172 BMRB 16205 HisJ 98.76 238 100.00 100.00 3.06e-172 BMRB 19245 Holo-HisJ 100.00 241 100.00 100.00 5.37e-175 PDB 1HPB "The Bacterial Periplasmic Histidine-Binding Protein: Structure(Slash)function Analysis Of The Ligand-Binding Site And Compariso" 98.76 238 98.32 99.16 1.15e-169 PDB 1HSL "Refined 1.89 Angstroms Structure Of The Histidine-Binding Protein Complexed With Histidine And Its Relationship With Many Other" 98.76 238 98.32 99.16 1.15e-169 PDB 2M8C "The Solution Nmr Structure Of E. Coli Apo-hisj" 100.00 241 100.00 100.00 5.37e-175 DBJ BAA16155 "histidine/lysine/arginine/ornithine transporter subunit [Escherichia coli str. K12 substr. W3110]" 98.76 260 100.00 100.00 4.26e-173 DBJ BAB36616 "histidine transport system histidine-binding periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 98.76 260 100.00 100.00 4.26e-173 DBJ BAG66608 "histidine/lysine/arginine/ornithine transporter subunit [Escherichia coli O111:H-]" 98.76 260 99.58 100.00 7.95e-173 DBJ BAG78142 "histidine ABC transporter substrate binding component [Escherichia coli SE11]" 98.76 260 100.00 100.00 4.26e-173 DBJ BAI26504 "histidine/lysine/arginine/ornithine transporter subunit HisJ [Escherichia coli O26:H11 str. 11368]" 98.76 260 100.00 100.00 4.26e-173 EMBL CAA24658 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 98.76 260 98.32 99.16 2.13e-170 EMBL CAA24659 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 98.76 260 98.32 99.16 2.13e-170 EMBL CAD07586 "histidine-binding periplasmic protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 98.76 260 97.48 98.74 1.54e-169 EMBL CAJ55342 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 59.75 164 97.92 98.61 1.92e-97 EMBL CAJ55343 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 59.75 164 97.92 98.61 1.98e-97 GB AAA75578 "J protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 98.76 260 98.32 99.16 2.13e-170 GB AAA85769 "histidine-binding periplasmic protein HisJ [Escherichia coli]" 98.76 260 99.58 99.58 3.02e-172 GB AAC75369 "histidine ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 98.76 260 100.00 100.00 4.26e-173 GB AAG57438 "histidine-binding periplasmic protein of high-affinity histidine transport system [Escherichia coli O157:H7 str. EDL933]" 98.76 260 100.00 100.00 4.26e-173 GB AAL21255 "histidine transport protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 98.76 260 98.32 99.16 2.13e-170 PIR AH0800 "histidine-binding periplasmic protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 98.76 260 97.48 98.74 1.54e-169 PRF 0809313B "protein hisJ" 98.76 260 98.32 99.16 2.13e-170 REF NP_311220 "histidine transport system histidine-binding periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 98.76 260 100.00 100.00 4.26e-173 REF NP_416812 "histidine ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 98.76 260 100.00 100.00 4.26e-173 REF NP_456896 "histidine ABC transporter substrate-binding protein HisJ [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 98.76 260 97.48 98.74 1.54e-169 REF NP_461296 "histidine ABC transporter substrate-binding protein HisJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 98.76 260 98.32 99.16 2.13e-170 REF NP_708191 "histidine ABC transporter substrate-binding protein HisJ [Shigella flexneri 2a str. 301]" 94.61 264 99.56 100.00 1.43e-164 SP P02910 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 98.76 260 98.32 99.16 2.13e-170 SP P0AEU0 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 98.76 260 100.00 100.00 4.26e-173 SP P0AEU1 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 98.76 260 100.00 100.00 4.26e-173 SP P0AEU2 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 98.76 260 100.00 100.00 4.26e-173 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $apo-HisJ 'E. coli' 562 Bacteria . Escherichia coli K12 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 $apo-HisJ 'recombinant technology' . Escherichia coli BL21 pET-15 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 $apo-HisJ 1 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' DSS 0.5 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apo-HisJ 1 mM '[U-13C; U-15N]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' DSS 0.5 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apo-HisJ 1 mM '[U-13C; U-15N]' 'sodium phosphate' 50 mM 'natural abundance' D2O 100 % 'natural abundance' DSS 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_3 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H chemical shifts were referenced to the methyl signal of DSS, and 15N and 13C chemical shifts were indirectly referenced to DSS (0 ppm for 1H).' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name apo-HisJ _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 GLY C C 174.1000 0.005 1 2 2 2 GLY CA C 44.7100 0.010 1 3 3 3 MET H H 8.4440 0.002 1 4 3 3 MET C C 176.0000 0.005 1 5 3 3 MET CA C 55.0700 0.010 1 6 3 3 MET CB C 32.3700 0.010 1 7 3 3 MET N N 121.2000 0.017 1 8 4 4 ALA H H 8.3790 0.002 1 9 4 4 ALA C C 177.3000 0.005 1 10 4 4 ALA CA C 52.1400 0.010 1 11 4 4 ALA CB C 18.3200 0.010 1 12 4 4 ALA N N 125.7000 0.017 1 13 5 5 ILE H H 7.8680 0.002 1 14 5 5 ILE C C 174.3000 0.005 1 15 5 5 ILE CA C 57.7100 0.010 1 16 5 5 ILE CB C 37.2600 0.010 1 17 5 5 ILE N N 121.3000 0.017 1 18 6 6 PRO C C 176.1000 0.005 1 19 6 6 PRO CA C 62.1800 0.010 1 20 6 6 PRO CB C 31.6200 0.010 1 21 7 7 GLN H H 8.3800 0.002 1 22 7 7 GLN C C 175.6000 0.005 1 23 7 7 GLN CA C 57.1900 0.010 1 24 7 7 GLN CB C 28.5000 0.010 1 25 7 7 GLN N N 119.2000 0.017 1 26 8 8 ASN H H 7.4720 0.002 1 27 8 8 ASN C C 173.6000 0.005 1 28 8 8 ASN CA C 51.7200 0.010 1 29 8 8 ASN CB C 40.5400 0.010 1 30 8 8 ASN N N 116.3000 0.017 1 31 9 9 ILE H H 8.4160 0.002 1 32 9 9 ILE C C 174.7000 0.005 1 33 9 9 ILE CA C 59.4800 0.010 1 34 9 9 ILE CB C 39.7400 0.010 1 35 9 9 ILE N N 121.0000 0.017 1 36 10 10 ARG H H 9.0980 0.002 1 37 10 10 ARG C C 175.8000 0.005 1 38 10 10 ARG CA C 53.9500 0.010 1 39 10 10 ARG CB C 30.6700 0.010 1 40 10 10 ARG N N 126.5000 0.017 1 41 11 11 ILE H H 9.2790 0.002 1 42 11 11 ILE C C 175.6000 0.005 1 43 11 11 ILE CA C 59.4800 0.010 1 44 11 11 ILE CB C 37.4600 0.010 1 45 11 11 ILE N N 127.5000 0.017 1 46 12 12 GLY H H 9.3820 0.002 1 47 12 12 GLY C C 171.7000 0.005 1 48 12 12 GLY CA C 44.5400 0.010 1 49 12 12 GLY N N 114.8000 0.017 1 50 13 13 THR H H 8.5940 0.002 1 51 13 13 THR C C 181.6000 0.005 1 52 13 13 THR CA C 61.4700 0.010 1 53 13 13 THR CB C 69.9700 0.010 1 54 13 13 THR N N 120.6000 0.017 1 55 14 14 ASP H H 8.2000 0.002 1 56 14 14 ASP C C 177.5000 0.005 1 57 14 14 ASP CA C 49.7600 0.010 1 58 14 14 ASP CB C 40.5800 0.010 1 59 14 14 ASP N N 127.0000 0.017 1 60 15 15 PRO C C 175.4000 0.005 1 61 15 15 PRO CA C 61.9200 0.010 1 62 15 15 PRO CB C 27.8900 0.010 1 63 16 16 THR H H 8.7390 0.002 1 64 16 16 THR C C 174.0000 0.005 1 65 16 16 THR CA C 59.5600 0.010 1 66 16 16 THR CB C 68.6500 0.010 1 67 16 16 THR N N 116.2000 0.017 1 68 17 17 TYR H H 8.9430 0.002 1 69 17 17 TYR C C 175.2000 0.005 1 70 17 17 TYR CA C 54.1800 0.010 1 71 17 17 TYR CB C 38.7000 0.010 1 72 17 17 TYR N N 125.8000 0.017 1 73 18 18 ALA H H 8.9450 0.002 1 74 18 18 ALA C C 176.0000 0.005 1 75 18 18 ALA CA C 51.4900 0.010 1 76 18 18 ALA CB C 16.0700 0.010 1 77 18 18 ALA N N 132.1000 0.017 1 78 19 19 PRO C C 173.5000 0.005 1 79 19 19 PRO CA C 62.8900 0.010 1 80 19 19 PRO CB C 31.7900 0.010 1 81 20 20 PHE H H 8.1170 0.002 1 82 20 20 PHE C C 176.7000 0.005 1 83 20 20 PHE CA C 62.4200 0.010 1 84 20 20 PHE CB C 37.9800 0.010 1 85 20 20 PHE N N 125.1000 0.017 1 86 21 21 GLU H H 7.7010 0.002 1 87 21 21 GLU C C 173.6000 0.005 1 88 21 21 GLU CA C 54.4000 0.010 1 89 21 21 GLU CB C 28.7700 0.010 1 90 21 21 GLU N N 111.8000 0.017 1 91 22 22 SER H H 8.7500 0.002 1 92 22 22 SER C C 171.5000 0.005 1 93 22 22 SER CA C 57.2900 0.010 1 94 22 22 SER CB C 62.9400 0.010 1 95 22 22 SER N N 117.2000 0.017 1 96 23 23 LYS H H 8.2380 0.002 1 97 23 23 LYS C C 177.6000 0.005 1 98 23 23 LYS CA C 53.7000 0.010 1 99 23 23 LYS CB C 33.3300 0.010 1 100 23 23 LYS N N 117.4000 0.017 1 101 24 24 ASN H H 8.5840 0.002 1 102 24 24 ASN C C 178.0000 0.005 1 103 24 24 ASN CA C 50.6000 0.010 1 104 24 24 ASN CB C 38.1400 0.010 1 105 24 24 ASN N N 122.4000 0.017 1 106 25 25 SER C C 175.4000 0.005 1 107 25 25 SER CA C 60.9700 0.010 1 108 25 25 SER CB C 62.4100 0.010 1 109 26 26 GLN H H 7.5200 0.002 1 110 26 26 GLN C C 176.2000 0.005 1 111 26 26 GLN CA C 55.1800 0.010 1 112 26 26 GLN CB C 28.2600 0.010 1 113 26 26 GLN N N 119.3000 0.017 1 114 27 27 GLY H H 8.1690 0.002 1 115 27 27 GLY C C 173.7000 0.005 1 116 27 27 GLY CA C 45.0500 0.010 1 117 27 27 GLY N N 108.8000 0.017 1 118 28 28 GLU H H 7.8360 0.002 1 119 28 28 GLU C C 175.8000 0.005 1 120 28 28 GLU CA C 54.4900 0.010 1 121 28 28 GLU CB C 29.7500 0.010 1 122 28 28 GLU N N 121.2000 0.017 1 123 29 29 LEU H H 8.2810 0.002 1 124 29 29 LEU C C 176.4000 0.005 1 125 29 29 LEU CA C 54.3100 0.010 1 126 29 29 LEU CB C 41.1800 0.010 1 127 29 29 LEU N N 123.5000 0.017 1 128 30 30 VAL H H 8.9000 0.002 1 129 30 30 VAL C C 175.3000 0.005 1 130 30 30 VAL CA C 58.3600 0.010 1 131 30 30 VAL CB C 36.0800 0.010 1 132 30 30 VAL N N 118.2000 0.017 1 133 31 31 GLY H H 8.6110 0.002 1 134 31 31 GLY C C 174.4000 0.005 1 135 31 31 GLY CA C 43.8300 0.010 1 136 31 31 GLY N N 109.8000 0.017 1 137 32 32 PHE H H 8.2950 0.002 1 138 32 32 PHE C C 177.9000 0.005 1 139 32 32 PHE CA C 59.8000 0.010 1 140 32 32 PHE CB C 38.9500 0.010 1 141 32 32 PHE N N 119.9000 0.017 1 142 33 33 ASP H H 8.9350 0.002 1 143 33 33 ASP C C 179.1000 0.005 1 144 33 33 ASP CA C 56.1800 0.010 1 145 33 33 ASP CB C 38.6100 0.010 1 146 33 33 ASP N N 116.5000 0.017 1 147 34 34 ILE H H 6.5350 0.002 1 148 34 34 ILE C C 178.0000 0.005 1 149 34 34 ILE CA C 60.9500 0.010 1 150 34 34 ILE CB C 33.6200 0.010 1 151 34 34 ILE N N 118.8000 0.017 1 152 35 35 ASP H H 8.5360 0.002 1 153 35 35 ASP C C 180.3000 0.005 1 154 35 35 ASP CA C 57.1000 0.010 1 155 35 35 ASP CB C 40.4200 0.010 1 156 35 35 ASP N N 121.0000 0.017 1 157 36 36 LEU H H 8.5080 0.002 1 158 36 36 LEU C C 178.5000 0.005 1 159 36 36 LEU CA C 57.7200 0.010 1 160 36 36 LEU CB C 42.2300 0.010 1 161 36 36 LEU N N 120.5000 0.017 1 162 37 37 ALA H H 8.3830 0.002 1 163 37 37 ALA C C 178.6000 0.005 1 164 37 37 ALA CA C 55.1700 0.010 1 165 37 37 ALA CB C 17.3400 0.010 1 166 37 37 ALA N N 120.2000 0.017 1 167 38 38 LYS H H 8.7800 0.002 1 168 38 38 LYS C C 180.1000 0.005 1 169 38 38 LYS CA C 60.5300 0.010 1 170 38 38 LYS CB C 31.8400 0.010 1 171 38 38 LYS N N 116.4000 0.017 1 172 39 39 GLU H H 7.6920 0.002 1 173 39 39 GLU C C 178.3000 0.005 1 174 39 39 GLU CA C 58.4300 0.010 1 175 39 39 GLU CB C 27.9900 0.010 1 176 39 39 GLU N N 121.5000 0.017 1 177 40 40 LEU H H 8.5630 0.002 1 178 40 40 LEU C C 178.7000 0.005 1 179 40 40 LEU CA C 58.4900 0.010 1 180 40 40 LEU CB C 40.2500 0.010 1 181 40 40 LEU N N 121.5000 0.017 1 182 41 41 CYS H H 8.5980 0.002 1 183 41 41 CYS C C 175.8000 0.005 1 184 41 41 CYS CA C 62.3900 0.010 1 185 41 41 CYS CB C 46.8600 0.010 1 186 41 41 CYS N N 115.7000 0.017 1 187 42 42 LYS H H 7.4900 0.002 1 188 42 42 LYS C C 180.8000 0.005 1 189 42 42 LYS CA C 58.8100 0.010 1 190 42 42 LYS CB C 31.4300 0.010 1 191 42 42 LYS N N 119.3000 0.017 1 192 43 43 ARG H H 8.0570 0.002 1 193 43 43 ARG C C 178.7000 0.005 1 194 43 43 ARG CA C 58.7600 0.010 1 195 43 43 ARG CB C 29.9800 0.010 1 196 43 43 ARG N N 119.5000 0.017 1 197 44 44 ILE H H 7.7650 0.002 1 198 44 44 ILE C C 175.0000 0.005 1 199 44 44 ILE CA C 60.9400 0.010 1 200 44 44 ILE CB C 36.6300 0.010 1 201 44 44 ILE N N 111.8000 0.017 1 202 45 45 ASN H H 7.7520 0.002 1 203 45 45 ASN C C 173.6000 0.005 1 204 45 45 ASN CA C 53.6700 0.010 1 205 45 45 ASN CB C 36.6200 0.010 1 206 45 45 ASN N N 118.8000 0.017 1 207 46 46 THR H H 7.9200 0.002 1 208 46 46 THR C C 173.1000 0.005 1 209 46 46 THR CA C 60.0200 0.010 1 210 46 46 THR CB C 70.5000 0.010 1 211 46 46 THR N N 112.8000 0.017 1 212 47 47 GLN H H 8.0370 0.002 1 213 47 47 GLN C C 175.4000 0.005 1 214 47 47 GLN CA C 54.5500 0.010 1 215 47 47 GLN CB C 28.6700 0.010 1 216 47 47 GLN N N 123.5000 0.017 1 217 48 48 CYS H H 8.8810 0.002 1 218 48 48 CYS C C 173.8000 0.005 1 219 48 48 CYS CA C 53.1700 0.010 1 220 48 48 CYS CB C 47.2900 0.010 1 221 48 48 CYS N N 123.8000 0.017 1 222 49 49 THR H H 8.3240 0.002 1 223 49 49 THR C C 172.7000 0.005 1 224 49 49 THR CA C 60.2100 0.010 1 225 49 49 THR CB C 70.9800 0.010 1 226 49 49 THR N N 118.6000 0.017 1 227 50 50 PHE H H 8.9820 0.002 1 228 50 50 PHE C C 175.8000 0.005 1 229 50 50 PHE CA C 57.3700 0.010 1 230 50 50 PHE CB C 40.7300 0.010 1 231 50 50 PHE N N 123.8000 0.017 1 232 51 51 VAL H H 9.2710 0.002 1 233 51 51 VAL C C 174.7000 0.005 1 234 51 51 VAL CA C 60.6500 0.010 1 235 51 51 VAL CB C 33.7000 0.010 1 236 51 51 VAL N N 126.3000 0.017 1 237 52 52 GLU H H 8.6170 0.002 1 238 52 52 GLU C C 176.9000 0.005 1 239 52 52 GLU CA C 54.4800 0.010 1 240 52 52 GLU CB C 29.3500 0.010 1 241 52 52 GLU N N 126.9000 0.017 1 242 53 53 ASN H H 8.9170 0.002 1 243 53 53 ASN C C 170.6000 0.005 1 244 53 53 ASN CA C 51.2200 0.010 1 245 53 53 ASN CB C 43.9800 0.010 1 246 53 53 ASN N N 127.1000 0.017 1 247 54 54 PRO C C 178.6000 0.005 1 248 54 54 PRO CA C 61.6500 0.010 1 249 54 54 PRO CB C 31.4600 0.010 1 250 55 55 LEU H H 9.0960 0.002 1 251 55 55 LEU C C 179.6000 0.005 1 252 55 55 LEU CA C 58.1300 0.010 1 253 55 55 LEU CB C 41.4700 0.010 1 254 55 55 LEU N N 124.2000 0.017 1 255 56 56 ASP H H 8.6510 0.002 1 256 56 56 ASP C C 176.5000 0.005 1 257 56 56 ASP CA C 56.0800 0.010 1 258 56 56 ASP CB C 39.6400 0.010 1 259 56 56 ASP N N 115.4000 0.017 1 260 57 57 ALA H H 8.0790 0.002 1 261 57 57 ALA C C 180.0000 0.005 1 262 57 57 ALA CA C 51.4400 0.010 1 263 57 57 ALA CB C 19.1700 0.010 1 264 57 57 ALA N N 120.4000 0.017 1 265 58 58 LEU H H 7.7830 0.002 1 266 58 58 LEU C C 177.8000 0.005 1 267 58 58 LEU CA C 58.9600 0.010 1 268 58 58 LEU CB C 40.1500 0.010 1 269 58 58 LEU N N 122.3000 0.017 1 270 59 59 ILE H H 9.0940 0.002 1 271 59 59 ILE C C 176.4000 0.005 1 272 59 59 ILE CA C 68.1700 0.010 1 273 59 59 ILE CB C 33.9800 0.010 1 274 59 59 ILE N N 119.6000 0.017 1 275 60 60 PRO C C 180.1000 0.005 1 276 60 60 PRO CA C 65.8900 0.010 1 277 60 60 PRO CB C 29.9800 0.010 1 278 61 61 SER H H 7.8650 0.002 1 279 61 61 SER C C 175.5000 0.005 1 280 61 61 SER CA C 62.1700 0.010 1 281 61 61 SER N N 114.8000 0.017 1 282 62 62 LEU H H 8.2960 0.002 1 283 62 62 LEU C C 181.0000 0.005 1 284 62 62 LEU CA C 57.4000 0.010 1 285 62 62 LEU CB C 41.8200 0.010 1 286 62 62 LEU N N 126.2000 0.017 1 287 63 63 LYS H H 8.4610 0.002 1 288 63 63 LYS C C 178.0000 0.005 1 289 63 63 LYS CA C 59.5000 0.010 1 290 63 63 LYS CB C 30.7700 0.010 1 291 63 63 LYS N N 121.0000 0.017 1 292 64 64 ALA H H 7.6860 0.002 1 293 64 64 ALA C C 176.2000 0.005 1 294 64 64 ALA CA C 51.6800 0.010 1 295 64 64 ALA CB C 18.1400 0.010 1 296 64 64 ALA N N 118.7000 0.017 1 297 65 65 LYS H H 7.7510 0.002 1 298 65 65 LYS C C 176.0000 0.005 1 299 65 65 LYS CA C 57.8000 0.010 1 300 65 65 LYS CB C 27.7300 0.010 1 301 65 65 LYS N N 112.2000 0.017 1 302 66 66 LYS H H 8.4150 0.002 1 303 66 66 LYS C C 176.6000 0.005 1 304 66 66 LYS CA C 57.2000 0.010 1 305 66 66 LYS CB C 32.1700 0.010 1 306 66 66 LYS N N 118.3000 0.017 1 307 67 67 ILE H H 7.0340 0.002 1 308 67 67 ILE C C 174.0000 0.005 1 309 67 67 ILE CA C 59.0500 0.010 1 310 67 67 ILE CB C 40.4700 0.010 1 311 67 67 ILE N N 107.5000 0.017 1 312 68 68 ASP H H 9.7390 0.002 1 313 68 68 ASP C C 172.2000 0.005 1 314 68 68 ASP CA C 55.5600 0.010 1 315 68 68 ASP CB C 44.2100 0.010 1 316 68 68 ASP N N 119.0000 0.017 1 317 69 69 ALA H H 7.6600 0.002 1 318 69 69 ALA C C 175.9000 0.005 1 319 69 69 ALA CA C 50.1200 0.010 1 320 69 69 ALA CB C 21.9600 0.010 1 321 69 69 ALA N N 117.4000 0.017 1 322 70 70 ILE H H 9.4020 0.002 1 323 70 70 ILE C C 174.5000 0.005 1 324 70 70 ILE CA C 60.0600 0.010 1 325 70 70 ILE CB C 41.1900 0.010 1 326 70 70 ILE N N 120.5000 0.017 1 327 71 71 MET H H 8.4310 0.002 1 328 71 71 MET C C 172.5000 0.005 1 329 71 71 MET CA C 53.0400 0.010 1 330 71 71 MET CB C 33.9400 0.010 1 331 71 71 MET N N 128.3000 0.017 1 332 72 72 SER H H 8.7170 0.002 1 333 72 72 SER C C 172.8000 0.005 1 334 72 72 SER CA C 57.6300 0.010 1 335 72 72 SER CB C 64.5900 0.010 1 336 72 72 SER N N 122.7000 0.017 1 337 73 73 SER H H 8.5700 0.002 1 338 73 73 SER C C 174.9000 0.005 1 339 73 73 SER CA C 58.5900 0.010 1 340 73 73 SER CB C 62.9200 0.010 1 341 73 73 SER N N 120.6000 0.017 1 342 74 74 LEU H H 8.6780 0.002 1 343 74 74 LEU C C 175.3000 0.005 1 344 74 74 LEU CA C 54.3200 0.010 1 345 74 74 LEU CB C 42.3500 0.010 1 346 74 74 LEU N N 120.7000 0.017 1 347 75 75 SER H H 8.1420 0.002 1 348 75 75 SER C C 174.5000 0.005 1 349 75 75 SER CA C 59.2500 0.010 1 350 75 75 SER CB C 63.0600 0.010 1 351 75 75 SER N N 122.0000 0.017 1 352 76 76 ILE H H 8.3070 0.002 1 353 76 76 ILE C C 175.5000 0.005 1 354 76 76 ILE CA C 61.3400 0.010 1 355 76 76 ILE CB C 35.7900 0.010 1 356 76 76 ILE N N 125.2000 0.017 1 357 77 77 THR H H 6.5130 0.002 1 358 77 77 THR C C 174.8000 0.005 1 359 77 77 THR CA C 57.7600 0.010 1 360 77 77 THR CB C 71.5700 0.010 1 361 77 77 THR N N 116.6000 0.017 1 362 78 78 GLU H H 8.9350 0.002 1 363 78 78 GLU C C 179.5000 0.005 1 364 78 78 GLU CA C 59.1400 0.010 1 365 78 78 GLU CB C 28.6300 0.010 1 366 78 78 GLU N N 124.5000 0.017 1 367 79 79 LYS H H 8.4150 0.002 1 368 79 79 LYS C C 180.6000 0.005 1 369 79 79 LYS CA C 58.8900 0.010 1 370 79 79 LYS CB C 31.6100 0.010 1 371 79 79 LYS N N 118.4000 0.017 1 372 80 80 ARG H H 7.6780 0.002 1 373 80 80 ARG C C 179.1000 0.005 1 374 80 80 ARG CA C 59.5800 0.010 1 375 80 80 ARG CB C 30.3800 0.010 1 376 80 80 ARG N N 118.5000 0.017 1 377 81 81 GLN H H 8.4180 0.002 1 378 81 81 GLN C C 176.6000 0.005 1 379 81 81 GLN CA C 57.5100 0.010 1 380 81 81 GLN CB C 28.8800 0.010 1 381 81 81 GLN N N 119.0000 0.017 1 382 82 82 GLN H H 7.2970 0.002 1 383 82 82 GLN C C 177.4000 0.005 1 384 82 82 GLN CA C 57.2800 0.010 1 385 82 82 GLN CB C 27.9500 0.010 1 386 82 82 GLN N N 115.3000 0.017 1 387 83 83 GLU H H 7.6270 0.002 1 388 83 83 GLU C C 176.4000 0.005 1 389 83 83 GLU CA C 56.9500 0.010 1 390 83 83 GLU CB C 33.0900 0.010 1 391 83 83 GLU N N 115.6000 0.017 1 392 84 84 ILE H H 8.2750 0.002 1 393 84 84 ILE C C 172.6000 0.005 1 394 84 84 ILE CA C 59.3800 0.010 1 395 84 84 ILE CB C 40.8300 0.010 1 396 84 84 ILE N N 115.1000 0.017 1 397 85 85 ALA H H 8.6790 0.002 1 398 85 85 ALA C C 175.0000 0.005 1 399 85 85 ALA CA C 49.1500 0.010 1 400 85 85 ALA CB C 22.2800 0.010 1 401 85 85 ALA N N 120.6000 0.017 1 402 86 86 PHE H H 8.2830 0.002 1 403 86 86 PHE C C 178.8000 0.005 1 404 86 86 PHE CA C 55.8500 0.010 1 405 86 86 PHE CB C 44.3000 0.010 1 406 86 86 PHE N N 115.5000 0.017 1 407 87 87 THR H H 7.8980 0.002 1 408 87 87 THR C C 174.7000 0.005 1 409 87 87 THR CA C 61.9300 0.010 1 410 87 87 THR CB C 72.7400 0.010 1 411 87 87 THR N N 108.2000 0.017 1 412 88 88 ASP H H 8.7890 0.002 1 413 88 88 ASP C C 174.3000 0.005 1 414 88 88 ASP CA C 55.0300 0.010 1 415 88 88 ASP CB C 40.8700 0.010 1 416 88 88 ASP N N 118.4000 0.017 1 417 89 89 LYS H H 7.6660 0.002 1 418 89 89 LYS C C 176.2000 0.005 1 419 89 89 LYS CA C 55.5700 0.010 1 420 89 89 LYS CB C 31.8500 0.010 1 421 89 89 LYS N N 118.1000 0.017 1 422 90 90 LEU H H 8.7780 0.002 1 423 90 90 LEU C C 178.0000 0.005 1 424 90 90 LEU CA C 54.4500 0.010 1 425 90 90 LEU CB C 41.7100 0.010 1 426 90 90 LEU N N 123.4000 0.017 1 427 91 91 TYR H H 6.8100 0.002 1 428 91 91 TYR C C 172.6000 0.005 1 429 91 91 TYR CA C 56.0700 0.010 1 430 91 91 TYR CB C 37.6700 0.010 1 431 91 91 TYR N N 110.5000 0.017 1 432 92 92 ALA H H 8.1350 0.002 1 433 92 92 ALA C C 175.6000 0.005 1 434 92 92 ALA CA C 51.9400 0.010 1 435 92 92 ALA CB C 20.3200 0.010 1 436 92 92 ALA N N 123.1000 0.017 1 437 93 93 ALA H H 8.6580 0.002 1 438 93 93 ALA C C 175.7000 0.005 1 439 93 93 ALA CA C 51.0200 0.010 1 440 93 93 ALA CB C 18.3100 0.010 1 441 93 93 ALA N N 127.0000 0.017 1 442 94 94 ASP H H 8.4970 0.002 1 443 94 94 ASP C C 175.3000 0.005 1 444 94 94 ASP CA C 53.9100 0.010 1 445 94 94 ASP CB C 42.0300 0.010 1 446 94 94 ASP N N 122.9000 0.017 1 447 95 95 SER H H 6.8440 0.002 1 448 95 95 SER C C 171.6000 0.005 1 449 95 95 SER CA C 57.8500 0.010 1 450 95 95 SER CB C 66.4100 0.010 1 451 95 95 SER N N 110.3000 0.017 1 452 96 96 ARG H H 9.2270 0.002 1 453 96 96 ARG C C 173.7000 0.005 1 454 96 96 ARG CA C 57.4500 0.010 1 455 96 96 ARG CB C 34.0700 0.010 1 456 96 96 ARG N N 124.3000 0.017 1 457 97 97 LEU H H 9.3430 0.002 1 458 97 97 LEU C C 177.6000 0.005 1 459 97 97 LEU CA C 54.1500 0.010 1 460 97 97 LEU CB C 42.6400 0.010 1 461 97 97 LEU N N 124.1000 0.017 1 462 98 98 VAL H H 9.5000 0.002 1 463 98 98 VAL C C 175.7000 0.005 1 464 98 98 VAL CA C 61.7700 0.010 1 465 98 98 VAL CB C 32.9500 0.010 1 466 98 98 VAL N N 124.5000 0.017 1 467 99 99 VAL H H 9.1920 0.002 1 468 99 99 VAL C C 174.6000 0.005 1 469 99 99 VAL CA C 58.1900 0.010 1 470 99 99 VAL CB C 36.7800 0.010 1 471 99 99 VAL N N 116.8000 0.017 1 472 100 100 ALA H H 9.0430 0.002 1 473 100 100 ALA C C 179.2000 0.005 1 474 100 100 ALA CA C 52.6900 0.010 1 475 100 100 ALA CB C 18.1600 0.010 1 476 100 100 ALA N N 123.4000 0.017 1 477 101 101 LYS H H 7.8400 0.002 1 478 101 101 LYS C C 176.8000 0.005 1 479 101 101 LYS CA C 59.3600 0.010 1 480 101 101 LYS CB C 31.3800 0.010 1 481 101 101 LYS N N 119.6000 0.017 1 482 102 102 ASN H H 7.9410 0.002 1 483 102 102 ASN C C 175.5000 0.005 1 484 102 102 ASN CA C 52.3300 0.010 1 485 102 102 ASN CB C 36.9900 0.010 1 486 102 102 ASN N N 114.4000 0.017 1 487 103 103 SER H H 7.7000 0.002 1 488 103 103 SER C C 176.0000 0.005 1 489 103 103 SER CA C 58.1800 0.010 1 490 103 103 SER CB C 64.3100 0.010 1 491 103 103 SER N N 114.8000 0.017 1 492 104 104 ASP H H 8.5480 0.002 1 493 104 104 ASP C C 176.7000 0.005 1 494 104 104 ASP CA C 52.9900 0.010 1 495 104 104 ASP CB C 40.3300 0.010 1 496 104 104 ASP N N 128.5000 0.017 1 497 105 105 ILE H H 7.8260 0.002 1 498 105 105 ILE C C 173.8000 0.005 1 499 105 105 ILE CA C 63.5800 0.010 1 500 105 105 ILE CB C 37.4900 0.010 1 501 105 105 ILE N N 122.8000 0.017 1 502 106 106 GLN H H 8.1740 0.002 1 503 106 106 GLN C C 174.7000 0.005 1 504 106 106 GLN CA C 51.3800 0.010 1 505 106 106 GLN CB C 31.0500 0.010 1 506 106 106 GLN N N 124.6000 0.017 1 507 107 107 PRO C C 175.3000 0.005 1 508 107 107 PRO CA C 61.8800 0.010 1 509 107 107 PRO CB C 26.8600 0.010 1 510 108 108 THR H H 8.5310 0.002 1 511 108 108 THR C C 174.0000 0.005 1 512 108 108 THR CA C 57.6900 0.010 1 513 108 108 THR CB C 71.0200 0.010 1 514 108 108 THR N N 114.6000 0.017 1 515 109 109 VAL H H 8.7750 0.002 1 516 109 109 VAL C C 177.3000 0.005 1 517 109 109 VAL CA C 65.6000 0.010 1 518 109 109 VAL CB C 30.5800 0.010 1 519 109 109 VAL N N 121.8000 0.017 1 520 110 110 GLU H H 8.4140 0.002 1 521 110 110 GLU C C 178.4000 0.005 1 522 110 110 GLU CA C 59.2600 0.010 1 523 110 110 GLU CB C 28.1700 0.010 1 524 110 110 GLU N N 116.9000 0.017 1 525 111 111 SER H H 7.3870 0.002 1 526 111 111 SER C C 176.5000 0.005 1 527 111 111 SER CA C 59.3700 0.010 1 528 111 111 SER CB C 63.7300 0.010 1 529 111 111 SER N N 113.2000 0.017 1 530 112 112 LEU H H 7.6760 0.002 1 531 112 112 LEU C C 176.7000 0.005 1 532 112 112 LEU CA C 54.5800 0.010 1 533 112 112 LEU CB C 42.6500 0.010 1 534 112 112 LEU N N 116.1000 0.017 1 535 113 113 LYS H H 7.4450 0.002 1 536 113 113 LYS C C 178.2000 0.005 1 537 113 113 LYS CA C 58.8500 0.010 1 538 113 113 LYS CB C 30.8500 0.010 1 539 113 113 LYS N N 121.0000 0.017 1 540 114 114 GLY H H 8.4540 0.002 1 541 114 114 GLY C C 174.2000 0.005 1 542 114 114 GLY CA C 45.2400 0.010 1 543 114 114 GLY N N 113.9000 0.017 1 544 115 115 LYS H H 8.5300 0.002 1 545 115 115 LYS C C 174.8000 0.005 1 546 115 115 LYS CA C 53.7100 0.010 1 547 115 115 LYS CB C 31.9900 0.010 1 548 115 115 LYS N N 120.6000 0.017 1 549 116 116 ARG H H 9.4550 0.002 1 550 116 116 ARG C C 176.0000 0.005 1 551 116 116 ARG CA C 54.7200 0.010 1 552 116 116 ARG CB C 32.3100 0.010 1 553 116 116 ARG N N 119.3000 0.017 1 554 117 117 VAL H H 9.2170 0.002 1 555 117 117 VAL C C 175.3000 0.005 1 556 117 117 VAL CA C 60.0900 0.010 1 557 117 117 VAL CB C 33.6200 0.010 1 558 117 117 VAL N N 126.1000 0.017 1 559 118 118 GLY H H 9.3670 0.002 1 560 118 118 GLY C C 172.3000 0.005 1 561 118 118 GLY CA C 45.0100 0.010 1 562 118 118 GLY N N 114.0000 0.017 1 563 119 119 VAL H H 9.1660 0.002 1 564 119 119 VAL C C 174.1000 0.005 1 565 119 119 VAL CA C 58.2700 0.010 1 566 119 119 VAL CB C 36.3700 0.010 1 567 119 119 VAL N N 116.4000 0.017 1 568 120 120 LEU H H 8.9610 0.002 1 569 120 120 LEU C C 176.9000 0.005 1 570 120 120 LEU CA C 53.6900 0.010 1 571 120 120 LEU CB C 41.2400 0.010 1 572 120 120 LEU N N 124.4000 0.017 1 573 121 121 GLN H H 9.3050 0.002 1 574 121 121 GLN C C 176.9000 0.005 1 575 121 121 GLN CA C 56.6800 0.010 1 576 121 121 GLN CB C 27.9200 0.010 1 577 121 121 GLN N N 128.0000 0.017 1 578 122 122 GLY H H 9.3830 0.002 1 579 122 122 GLY C C 175.1000 0.005 1 580 122 122 GLY CA C 45.2400 0.010 1 581 122 122 GLY N N 113.6000 0.017 1 582 123 123 THR H H 7.2200 0.002 1 583 123 123 THR C C 176.8000 0.005 1 584 123 123 THR CA C 60.2600 0.010 1 585 123 123 THR CB C 73.5300 0.010 1 586 123 123 THR N N 108.4000 0.017 1 587 124 124 THR H H 8.9340 0.002 1 588 124 124 THR C C 178.1000 0.005 1 589 124 124 THR CA C 63.9900 0.010 1 590 124 124 THR CB C 67.7400 0.010 1 591 124 124 THR N N 113.9000 0.017 1 592 125 125 GLN H H 7.5210 0.002 1 593 125 125 GLN C C 178.3000 0.005 1 594 125 125 GLN CA C 61.6700 0.010 1 595 125 125 GLN CB C 25.3100 0.010 1 596 125 125 GLN N N 120.6000 0.017 1 597 126 126 GLU H H 7.7170 0.002 1 598 126 126 GLU C C 177.6000 0.005 1 599 126 126 GLU CA C 59.6300 0.010 1 600 126 126 GLU CB C 28.7300 0.010 1 601 126 126 GLU N N 121.9000 0.017 1 602 127 127 THR H H 8.1750 0.002 1 603 127 127 THR C C 176.2000 0.005 1 604 127 127 THR CA C 66.3400 0.010 1 605 127 127 THR CB C 67.5900 0.010 1 606 127 127 THR N N 117.8000 0.017 1 607 128 128 PHE H H 8.8820 0.002 1 608 128 128 PHE C C 178.0000 0.005 1 609 128 128 PHE CA C 61.5900 0.010 1 610 128 128 PHE CB C 38.8100 0.010 1 611 128 128 PHE N N 121.9000 0.017 1 612 129 129 GLY H H 8.9000 0.002 1 613 129 129 GLY C C 176.1000 0.005 1 614 129 129 GLY CA C 46.6900 0.010 1 615 129 129 GLY N N 107.0000 0.017 1 616 130 130 ASN H H 8.9150 0.002 1 617 130 130 ASN C C 176.2000 0.005 1 618 130 130 ASN CA C 55.4000 0.010 1 619 130 130 ASN CB C 37.5700 0.010 1 620 130 130 ASN N N 123.0000 0.017 1 621 131 131 GLU H H 7.9070 0.002 1 622 131 131 GLU C C 177.9000 0.005 1 623 131 131 GLU CA C 57.9400 0.010 1 624 131 131 GLU CB C 29.3500 0.010 1 625 131 131 GLU N N 119.0000 0.017 1 626 132 132 HIS H H 7.8770 0.002 1 627 132 132 HIS C C 175.9000 0.005 1 628 132 132 HIS CA C 56.9100 0.010 1 629 132 132 HIS CB C 30.5100 0.010 1 630 132 132 HIS N N 112.6000 0.017 1 631 133 133 TRP H H 7.6530 0.002 1 632 133 133 TRP C C 176.8000 0.005 1 633 133 133 TRP CA C 55.5700 0.010 1 634 133 133 TRP CB C 30.4000 0.010 1 635 133 133 TRP N N 119.3000 0.017 1 636 134 134 ALA H H 8.7110 0.002 1 637 134 134 ALA C C 177.7000 0.005 1 638 134 134 ALA CA C 55.4100 0.010 1 639 134 134 ALA CB C 15.9900 0.010 1 640 134 134 ALA N N 125.4000 0.017 1 641 135 135 PRO C C 177.2000 0.005 1 642 135 135 PRO CA C 64.5100 0.010 1 643 135 135 PRO CB C 30.8000 0.010 1 644 136 136 LYS H H 7.6650 0.002 1 645 136 136 LYS C C 176.5000 0.005 1 646 136 136 LYS CA C 53.5300 0.010 1 647 136 136 LYS CB C 31.4300 0.010 1 648 136 136 LYS N N 115.8000 0.017 1 649 137 137 GLY H H 7.8640 0.002 1 650 137 137 GLY C C 174.3000 0.005 1 651 137 137 GLY CA C 45.7400 0.010 1 652 137 137 GLY N N 106.1000 0.017 1 653 138 138 ILE H H 6.8890 0.002 1 654 138 138 ILE C C 174.4000 0.005 1 655 138 138 ILE CA C 60.4600 0.010 1 656 138 138 ILE CB C 38.0800 0.010 1 657 138 138 ILE N N 124.4000 0.017 1 658 139 139 GLU H H 8.2300 0.002 1 659 139 139 GLU C C 173.9000 0.005 1 660 139 139 GLU CA C 56.0500 0.010 1 661 139 139 GLU CB C 29.4900 0.010 1 662 139 139 GLU N N 128.4000 0.017 1 663 140 140 ILE H H 8.6420 0.002 1 664 140 140 ILE C C 176.1000 0.005 1 665 140 140 ILE CA C 57.1000 0.010 1 666 140 140 ILE CB C 34.4400 0.010 1 667 140 140 ILE N N 129.5000 0.017 1 668 141 141 VAL H H 9.3870 0.002 1 669 141 141 VAL C C 174.4000 0.005 1 670 141 141 VAL CA C 61.0600 0.010 1 671 141 141 VAL CB C 32.4100 0.010 1 672 141 141 VAL N N 133.0000 0.017 1 673 142 142 SER H H 8.4900 0.002 1 674 142 142 SER C C 175.0000 0.005 1 675 142 142 SER CA C 57.7100 0.010 1 676 142 142 SER CB C 63.7100 0.010 1 677 142 142 SER N N 122.9000 0.017 1 678 143 143 TYR H H 8.9790 0.002 1 679 143 143 TYR C C 175.9000 0.005 1 680 143 143 TYR CA C 57.3000 0.010 1 681 143 143 TYR CB C 42.3000 0.010 1 682 143 143 TYR N N 123.4000 0.017 1 683 144 144 GLN H H 8.9740 0.002 1 684 144 144 GLN C C 176.0000 0.005 1 685 144 144 GLN CA C 56.4900 0.010 1 686 144 144 GLN CB C 28.4700 0.010 1 687 144 144 GLN N N 119.5000 0.017 1 688 145 145 GLY H H 7.5310 0.002 1 689 145 145 GLY C C 173.5000 0.005 1 690 145 145 GLY CA C 44.3000 0.010 1 691 145 145 GLY N N 106.8000 0.017 1 692 146 146 GLN H H 8.9490 0.002 1 693 146 146 GLN C C 177.2000 0.005 1 694 146 146 GLN CA C 57.8000 0.010 1 695 146 146 GLN CB C 28.1900 0.010 1 696 146 146 GLN N N 124.3000 0.017 1 697 147 147 ASP H H 8.7460 0.002 1 698 147 147 ASP C C 178.9000 0.005 1 699 147 147 ASP CA C 56.6500 0.010 1 700 147 147 ASP CB C 38.8900 0.010 1 701 147 147 ASP N N 117.9000 0.017 1 702 148 148 ASN H H 7.4960 0.002 1 703 148 148 ASN C C 176.7000 0.005 1 704 148 148 ASN CA C 55.1600 0.010 1 705 148 148 ASN CB C 38.7000 0.010 1 706 148 148 ASN N N 117.5000 0.017 1 707 149 149 ILE H H 6.7930 0.002 1 708 149 149 ILE C C 177.4000 0.005 1 709 149 149 ILE CA C 64.4500 0.010 1 710 149 149 ILE CB C 35.9000 0.010 1 711 149 149 ILE N N 120.0000 0.017 1 712 150 150 TYR H H 6.8970 0.002 1 713 150 150 TYR C C 178.8000 0.005 1 714 150 150 TYR CA C 59.7300 0.010 1 715 150 150 TYR CB C 35.9700 0.010 1 716 150 150 TYR N N 117.4000 0.017 1 717 151 151 SER H H 8.1860 0.002 1 718 151 151 SER C C 177.0000 0.005 1 719 151 151 SER CA C 61.3000 0.010 1 720 151 151 SER CB C 62.1000 0.010 1 721 151 151 SER N N 117.0000 0.017 1 722 152 152 ASP H H 7.5410 0.002 1 723 152 152 ASP C C 179.0000 0.005 1 724 152 152 ASP CA C 56.5800 0.010 1 725 152 152 ASP CB C 38.2400 0.010 1 726 152 152 ASP N N 122.3000 0.017 1 727 153 153 LEU H H 8.3720 0.002 1 728 153 153 LEU C C 180.3000 0.005 1 729 153 153 LEU CA C 58.1600 0.010 1 730 153 153 LEU CB C 41.6300 0.010 1 731 153 153 LEU N N 124.1000 0.017 1 732 154 154 THR H H 8.3890 0.002 1 733 154 154 THR C C 176.7000 0.005 1 734 154 154 THR CA C 63.9200 0.010 1 735 154 154 THR CB C 68.7000 0.010 1 736 154 154 THR N N 111.9000 0.017 1 737 155 155 ALA H H 7.4440 0.002 1 738 155 155 ALA C C 178.2000 0.005 1 739 155 155 ALA CA C 51.6400 0.010 1 740 155 155 ALA CB C 18.9900 0.010 1 741 155 155 ALA N N 121.8000 0.017 1 742 156 156 GLY H H 7.9210 0.002 1 743 156 156 GLY C C 175.1000 0.005 1 744 156 156 GLY CA C 45.4200 0.010 1 745 156 156 GLY N N 107.8000 0.017 1 746 157 157 ARG H H 8.4430 0.002 1 747 157 157 ARG C C 176.6000 0.005 1 748 157 157 ARG CA C 57.2600 0.010 1 749 157 157 ARG CB C 30.4000 0.010 1 750 157 157 ARG N N 119.0000 0.017 1 751 158 158 ILE H H 7.1090 0.002 1 752 158 158 ILE C C 173.7000 0.005 1 753 158 158 ILE CA C 59.9000 0.010 1 754 158 158 ILE CB C 40.0700 0.010 1 755 158 158 ILE N N 108.9000 0.017 1 756 159 159 ASP H H 8.7370 0.002 1 757 159 159 ASP C C 174.7000 0.005 1 758 159 159 ASP CA C 55.9000 0.010 1 759 159 159 ASP CB C 43.6300 0.010 1 760 159 159 ASP N N 119.1000 0.017 1 761 160 160 ALA H H 7.7020 0.002 1 762 160 160 ALA C C 174.9000 0.005 1 763 160 160 ALA CA C 50.1900 0.010 1 764 160 160 ALA CB C 23.0300 0.010 1 765 160 160 ALA N N 116.4000 0.017 1 766 161 161 ALA H H 8.9150 0.002 1 767 161 161 ALA C C 175.5000 0.005 1 768 161 161 ALA CA C 49.7300 0.010 1 769 161 161 ALA CB C 21.1100 0.010 1 770 161 161 ALA N N 123.4000 0.017 1 771 162 162 PHE H H 8.9710 0.002 1 772 162 162 PHE C C 172.9000 0.005 1 773 162 162 PHE CA C 54.5000 0.010 1 774 162 162 PHE CB C 39.4000 0.010 1 775 162 162 PHE N N 125.1000 0.017 1 776 163 163 GLN H H 7.9040 0.002 1 777 163 163 GLN C C 173.4000 0.005 1 778 163 163 GLN CA C 53.5500 0.010 1 779 163 163 GLN CB C 34.3900 0.010 1 780 163 163 GLN N N 124.6000 0.017 1 781 164 164 ASP H H 8.3040 0.002 1 782 164 164 ASP C C 175.8000 0.005 1 783 164 164 ASP CA C 55.5400 0.010 1 784 164 164 ASP CB C 42.3700 0.010 1 785 164 164 ASP N N 122.3000 0.017 1 786 165 165 GLU H H 8.6050 0.002 1 787 165 165 GLU C C 177.7000 0.005 1 788 165 165 GLU CA C 60.2300 0.010 1 789 165 165 GLU CB C 30.0200 0.010 1 790 165 165 GLU N N 128.6000 0.017 1 791 166 166 VAL H H 8.7480 0.002 1 792 166 166 VAL C C 178.3000 0.005 1 793 166 166 VAL CA C 66.8000 0.010 1 794 166 166 VAL CB C 30.0700 0.010 1 795 166 166 VAL N N 120.1000 0.017 1 796 167 167 ALA H H 8.6550 0.002 1 797 167 167 ALA C C 182.5000 0.005 1 798 167 167 ALA CA C 54.9800 0.010 1 799 167 167 ALA CB C 17.9100 0.010 1 800 167 167 ALA N N 123.2000 0.017 1 801 168 168 ALA H H 8.3490 0.002 1 802 168 168 ALA C C 179.8000 0.005 1 803 168 168 ALA CA C 54.1800 0.010 1 804 168 168 ALA CB C 18.7500 0.010 1 805 168 168 ALA N N 121.3000 0.017 1 806 169 169 SER H H 8.0580 0.002 1 807 169 169 SER C C 175.7000 0.005 1 808 169 169 SER CA C 61.0500 0.010 1 809 169 169 SER CB C 63.0500 0.010 1 810 169 169 SER N N 113.4000 0.017 1 811 170 170 GLU H H 8.8240 0.002 1 812 170 170 GLU C C 178.8000 0.005 1 813 170 170 GLU CA C 57.6100 0.010 1 814 170 170 GLU CB C 29.7900 0.010 1 815 170 170 GLU N N 115.6000 0.017 1 816 171 171 GLY H H 8.1540 0.002 1 817 171 171 GLY C C 173.7000 0.005 1 818 171 171 GLY CA C 44.9700 0.010 1 819 171 171 GLY N N 103.4000 0.017 1 820 172 172 PHE H H 7.2970 0.002 1 821 172 172 PHE C C 175.2000 0.005 1 822 172 172 PHE CA C 60.6900 0.010 1 823 172 172 PHE CB C 40.7400 0.010 1 824 172 172 PHE N N 120.1000 0.017 1 825 173 173 LEU H H 8.4700 0.002 1 826 173 173 LEU C C 179.0000 0.005 1 827 173 173 LEU CA C 57.6700 0.010 1 828 173 173 LEU CB C 40.0200 0.010 1 829 173 173 LEU N N 117.8000 0.017 1 830 174 174 LYS H H 8.0180 0.002 1 831 174 174 LYS C C 176.9000 0.005 1 832 174 174 LYS CA C 56.4500 0.010 1 833 174 174 LYS CB C 31.7700 0.010 1 834 174 174 LYS N N 114.6000 0.017 1 835 175 175 GLN H H 7.1510 0.002 1 836 175 175 GLN C C 176.0000 0.005 1 837 175 175 GLN CA C 52.5100 0.010 1 838 175 175 GLN CB C 26.7400 0.010 1 839 175 175 GLN N N 118.8000 0.017 1 840 176 176 PRO C C 179.3000 0.005 1 841 176 176 PRO CA C 66.1000 0.010 1 842 176 176 PRO CB C 30.7200 0.010 1 843 177 177 VAL H H 7.4800 0.002 1 844 177 177 VAL C C 175.9000 0.005 1 845 177 177 VAL CA C 62.8600 0.010 1 846 177 177 VAL CB C 30.6600 0.010 1 847 177 177 VAL N N 112.3000 0.017 1 848 178 178 GLY H H 7.1730 0.002 1 849 178 178 GLY C C 175.0000 0.005 1 850 178 178 GLY CA C 44.0800 0.010 1 851 178 178 GLY N N 109.7000 0.017 1 852 179 179 LYS H H 6.9720 0.002 1 853 179 179 LYS C C 177.1000 0.005 1 854 179 179 LYS CA C 58.3600 0.010 1 855 179 179 LYS CB C 31.2600 0.010 1 856 179 179 LYS N N 120.9000 0.017 1 857 180 180 ASP H H 8.0360 0.002 1 858 180 180 ASP C C 173.9000 0.005 1 859 180 180 ASP CA C 53.9200 0.010 1 860 180 180 ASP CB C 39.6900 0.010 1 861 180 180 ASP N N 117.2000 0.017 1 862 181 181 TYR H H 7.7680 0.002 1 863 181 181 TYR C C 172.3000 0.005 1 864 181 181 TYR CA C 57.8900 0.010 1 865 181 181 TYR CB C 41.8600 0.010 1 866 181 181 TYR N N 120.5000 0.017 1 867 182 182 LYS H H 9.4970 0.002 1 868 182 182 LYS C C 174.9000 0.005 1 869 182 182 LYS CA C 54.3300 0.010 1 870 182 182 LYS CB C 35.6100 0.010 1 871 182 182 LYS N N 116.9000 0.017 1 872 183 183 PHE H H 8.4700 0.002 1 873 183 183 PHE C C 177.8000 0.005 1 874 183 183 PHE CA C 56.7800 0.010 1 875 183 183 PHE CB C 38.3200 0.010 1 876 183 183 PHE N N 117.9000 0.017 1 877 184 184 GLY H H 9.1070 0.002 1 878 184 184 GLY C C 173.3000 0.005 1 879 184 184 GLY CA C 46.9000 0.010 1 880 184 184 GLY N N 113.7000 0.017 1 881 185 185 GLY H H 7.7020 0.002 1 882 185 185 GLY C C 171.1000 0.005 1 883 185 185 GLY CA C 44.5300 0.010 1 884 185 185 GLY N N 111.0000 0.017 1 885 186 186 PRO C C 175.5000 0.005 1 886 186 186 PRO CA C 61.9200 0.010 1 887 186 186 PRO CB C 32.6400 0.010 1 888 187 187 SER H H 8.4520 0.002 1 889 187 187 SER C C 173.5000 0.005 1 890 187 187 SER CA C 57.9300 0.010 1 891 187 187 SER CB C 63.2600 0.010 1 892 187 187 SER N N 113.5000 0.017 1 893 188 188 VAL H H 9.0800 0.002 1 894 188 188 VAL C C 173.9000 0.005 1 895 188 188 VAL CA C 61.8000 0.010 1 896 188 188 VAL CB C 32.6800 0.010 1 897 188 188 VAL N N 123.3000 0.017 1 898 189 189 LYS H H 8.1230 0.002 1 899 189 189 LYS C C 176.7000 0.005 1 900 189 189 LYS CA C 54.6800 0.010 1 901 189 189 LYS CB C 33.7800 0.010 1 902 189 189 LYS N N 125.2000 0.017 1 903 190 190 ASP H H 8.8230 0.002 1 904 190 190 ASP C C 175.3000 0.005 1 905 190 190 ASP CA C 55.6100 0.010 1 906 190 190 ASP CB C 42.6200 0.010 1 907 190 190 ASP N N 120.3000 0.017 1 908 191 191 GLU H H 9.2390 0.002 1 909 191 191 GLU C C 177.3000 0.005 1 910 191 191 GLU CA C 59.3100 0.010 1 911 191 191 GLU CB C 28.4200 0.010 1 912 191 191 GLU N N 129.1000 0.017 1 913 192 192 LYS H H 7.9180 0.002 1 914 192 192 LYS C C 178.2000 0.005 1 915 192 192 LYS CA C 58.1400 0.010 1 916 192 192 LYS CB C 31.6900 0.010 1 917 192 192 LYS N N 118.0000 0.017 1 918 193 193 LEU H H 8.3620 0.002 1 919 193 193 LEU C C 177.7000 0.005 1 920 193 193 LEU CA C 55.7900 0.010 1 921 193 193 LEU CB C 42.3300 0.010 1 922 193 193 LEU N N 118.2000 0.017 1 923 194 194 PHE H H 8.0360 0.002 1 924 194 194 PHE C C 178.2000 0.005 1 925 194 194 PHE CA C 54.6200 0.010 1 926 194 194 PHE CB C 37.3900 0.010 1 927 194 194 PHE N N 116.8000 0.017 1 928 195 195 GLY H H 7.5100 0.002 1 929 195 195 GLY C C 174.2000 0.005 1 930 195 195 GLY CA C 44.1200 0.010 1 931 195 195 GLY N N 106.9000 0.017 1 932 196 196 VAL H H 8.0640 0.002 1 933 196 196 VAL C C 175.3000 0.005 1 934 196 196 VAL CA C 60.7200 0.010 1 935 196 196 VAL CB C 30.6300 0.010 1 936 196 196 VAL N N 112.4000 0.017 1 937 197 197 GLY H H 7.7880 0.002 1 938 197 197 GLY C C 172.3000 0.005 1 939 197 197 GLY CA C 43.2100 0.010 1 940 197 197 GLY N N 108.1000 0.017 1 941 198 198 THR H H 7.7960 0.002 1 942 198 198 THR C C 172.8000 0.005 1 943 198 198 THR CA C 59.0900 0.010 1 944 198 198 THR CB C 71.0800 0.010 1 945 198 198 THR N N 109.2000 0.017 1 946 199 199 GLY H H 7.9280 0.002 1 947 199 199 GLY C C 171.8000 0.005 1 948 199 199 GLY CA C 43.8400 0.010 1 949 199 199 GLY N N 103.9000 0.017 1 950 200 200 MET H H 7.9710 0.002 1 951 200 200 MET C C 176.2000 0.005 1 952 200 200 MET CA C 55.2600 0.010 1 953 200 200 MET CB C 33.3900 0.010 1 954 200 200 MET N N 121.4000 0.017 1 955 201 201 GLY H H 8.8180 0.002 1 956 201 201 GLY C C 172.0000 0.005 1 957 201 201 GLY CA C 44.5400 0.010 1 958 201 201 GLY N N 112.2000 0.017 1 959 202 202 LEU H H 8.7670 0.002 1 960 202 202 LEU C C 176.0000 0.005 1 961 202 202 LEU CA C 53.7400 0.010 1 962 202 202 LEU CB C 46.0100 0.010 1 963 202 202 LEU N N 124.7000 0.017 1 964 203 203 ARG H H 10.2700 0.002 1 965 203 203 ARG C C 180.4000 0.005 1 966 203 203 ARG CA C 57.1300 0.010 1 967 203 203 ARG CB C 29.6500 0.010 1 968 203 203 ARG N N 121.6000 0.017 1 969 204 204 LYS H H 9.2310 0.002 1 970 204 204 LYS C C 178.2000 0.005 1 971 204 204 LYS CA C 59.5700 0.010 1 972 204 204 LYS CB C 31.8400 0.010 1 973 204 204 LYS N N 123.2000 0.017 1 974 205 205 GLU H H 9.0260 0.002 1 975 205 205 GLU C C 177.7000 0.005 1 976 205 205 GLU CA C 57.2300 0.010 1 977 205 205 GLU CB C 27.7700 0.010 1 978 205 205 GLU N N 113.8000 0.017 1 979 206 206 ASP H H 7.2530 0.002 1 980 206 206 ASP C C 177.3000 0.005 1 981 206 206 ASP CA C 53.7100 0.010 1 982 206 206 ASP CB C 37.5300 0.010 1 983 206 206 ASP N N 126.0000 0.017 1 984 207 207 ASN H H 7.8390 0.002 1 985 207 207 ASN C C 176.9000 0.005 1 986 207 207 ASN CA C 56.9500 0.010 1 987 207 207 ASN CB C 38.8200 0.010 1 988 207 207 ASN N N 120.1000 0.017 1 989 208 208 GLU H H 8.7760 0.002 1 990 208 208 GLU C C 179.9000 0.005 1 991 208 208 GLU CA C 59.8700 0.010 1 992 208 208 GLU CB C 27.6300 0.010 1 993 208 208 GLU N N 120.5000 0.017 1 994 209 209 LEU H H 8.3660 0.002 1 995 209 209 LEU C C 177.1000 0.005 1 996 209 209 LEU CA C 57.4000 0.010 1 997 209 209 LEU CB C 40.6600 0.010 1 998 209 209 LEU N N 122.9000 0.017 1 999 210 210 ARG H H 7.5820 0.002 1 1000 210 210 ARG C C 177.4000 0.005 1 1001 210 210 ARG CA C 59.9700 0.010 1 1002 210 210 ARG CB C 30.1100 0.010 1 1003 210 210 ARG N N 119.1000 0.017 1 1004 211 211 GLU H H 8.4070 0.002 1 1005 211 211 GLU C C 179.8000 0.005 1 1006 211 211 GLU CA C 59.1500 0.010 1 1007 211 211 GLU CB C 28.6000 0.010 1 1008 211 211 GLU N N 116.2000 0.017 1 1009 212 212 ALA H H 8.1280 0.002 1 1010 212 212 ALA C C 181.3000 0.005 1 1011 212 212 ALA CA C 54.8100 0.010 1 1012 212 212 ALA CB C 17.1700 0.010 1 1013 212 212 ALA N N 123.5000 0.017 1 1014 213 213 LEU H H 8.3640 0.002 1 1015 213 213 LEU C C 178.4000 0.005 1 1016 213 213 LEU CA C 57.7100 0.010 1 1017 213 213 LEU CB C 41.4500 0.010 1 1018 213 213 LEU N N 121.2000 0.017 1 1019 214 214 ASN H H 8.4350 0.002 1 1020 214 214 ASN C C 179.7000 0.005 1 1021 214 214 ASN CA C 55.2600 0.010 1 1022 214 214 ASN CB C 37.1200 0.010 1 1023 214 214 ASN N N 119.2000 0.017 1 1024 215 215 LYS H H 8.0800 0.002 1 1025 215 215 LYS C C 178.4000 0.005 1 1026 215 215 LYS CA C 59.0900 0.010 1 1027 215 215 LYS CB C 31.7400 0.010 1 1028 215 215 LYS N N 123.8000 0.017 1 1029 216 216 ALA H H 7.9350 0.002 1 1030 216 216 ALA C C 179.5000 0.005 1 1031 216 216 ALA CA C 54.1400 0.010 1 1032 216 216 ALA CB C 18.7000 0.010 1 1033 216 216 ALA N N 122.2000 0.017 1 1034 217 217 PHE H H 8.9160 0.002 1 1035 217 217 PHE C C 177.2000 0.005 1 1036 217 217 PHE CA C 61.3900 0.010 1 1037 217 217 PHE CB C 38.0000 0.010 1 1038 217 217 PHE N N 119.5000 0.017 1 1039 218 218 ALA H H 7.9560 0.002 1 1040 218 218 ALA C C 182.1000 0.005 1 1041 218 218 ALA CA C 54.8100 0.010 1 1042 218 218 ALA CB C 16.6500 0.010 1 1043 218 218 ALA N N 121.3000 0.017 1 1044 219 219 GLU H H 7.9520 0.002 1 1045 219 219 GLU C C 178.6000 0.005 1 1046 219 219 GLU CA C 59.0400 0.010 1 1047 219 219 GLU CB C 28.3200 0.010 1 1048 219 219 GLU N N 120.0000 0.017 1 1049 220 220 MET H H 8.1900 0.002 1 1050 220 220 MET C C 179.0000 0.005 1 1051 220 220 MET CA C 57.4300 0.010 1 1052 220 220 MET CB C 32.6200 0.010 1 1053 220 220 MET N N 120.9000 0.017 1 1054 221 221 ARG H H 7.7620 0.002 1 1055 221 221 ARG C C 179.3000 0.005 1 1056 221 221 ARG CA C 58.7100 0.010 1 1057 221 221 ARG CB C 27.4800 0.010 1 1058 221 221 ARG N N 119.2000 0.017 1 1059 222 222 ALA H H 7.8380 0.002 1 1060 222 222 ALA C C 179.3000 0.005 1 1061 222 222 ALA CA C 54.1800 0.010 1 1062 222 222 ALA CB C 18.0300 0.010 1 1063 222 222 ALA N N 122.5000 0.017 1 1064 223 223 ASP H H 8.0910 0.002 1 1065 223 223 ASP C C 177.9000 0.005 1 1066 223 223 ASP CA C 53.0200 0.010 1 1067 223 223 ASP CB C 39.5700 0.010 1 1068 223 223 ASP N N 115.1000 0.017 1 1069 224 224 GLY H H 7.1990 0.002 1 1070 224 224 GLY C C 176.0000 0.005 1 1071 224 224 GLY CA C 45.0700 0.010 1 1072 224 224 GLY N N 106.7000 0.017 1 1073 225 225 THR H H 9.0950 0.002 1 1074 225 225 THR C C 175.7000 0.005 1 1075 225 225 THR CA C 67.6100 0.010 1 1076 225 225 THR CB C 66.8400 0.010 1 1077 225 225 THR N N 122.4000 0.017 1 1078 226 226 TYR H H 8.0400 0.002 1 1079 226 226 TYR C C 176.0000 0.005 1 1080 226 226 TYR CA C 62.5300 0.010 1 1081 226 226 TYR CB C 38.4100 0.010 1 1082 226 226 TYR N N 121.5000 0.017 1 1083 227 227 GLU H H 8.1530 0.002 1 1084 227 227 GLU C C 178.2000 0.005 1 1085 227 227 GLU CA C 58.9400 0.010 1 1086 227 227 GLU CB C 28.8100 0.010 1 1087 227 227 GLU N N 118.2000 0.017 1 1088 228 228 LYS H H 7.5580 0.002 1 1089 228 228 LYS C C 179.5000 0.005 1 1090 228 228 LYS CA C 59.2600 0.010 1 1091 228 228 LYS CB C 31.5200 0.010 1 1092 228 228 LYS N N 119.1000 0.017 1 1093 229 229 LEU H H 8.0550 0.002 1 1094 229 229 LEU C C 179.3000 0.005 1 1095 229 229 LEU CA C 56.9700 0.010 1 1096 229 229 LEU CB C 41.5200 0.010 1 1097 229 229 LEU N N 119.1000 0.017 1 1098 230 230 ALA H H 8.9010 0.002 1 1099 230 230 ALA C C 180.5000 0.005 1 1100 230 230 ALA CA C 54.8900 0.010 1 1101 230 230 ALA CB C 17.5700 0.010 1 1102 230 230 ALA N N 121.2000 0.017 1 1103 231 231 LYS H H 8.0620 0.002 1 1104 231 231 LYS C C 177.7000 0.005 1 1105 231 231 LYS CA C 57.3700 0.010 1 1106 231 231 LYS CB C 31.3300 0.010 1 1107 231 231 LYS N N 117.2000 0.017 1 1108 232 232 LYS H H 7.0530 0.002 1 1109 232 232 LYS C C 176.8000 0.005 1 1110 232 232 LYS CA C 57.8900 0.010 1 1111 232 232 LYS CB C 31.1500 0.010 1 1112 232 232 LYS N N 117.6000 0.017 1 1113 233 233 TYR H H 7.0130 0.002 1 1114 233 233 TYR C C 175.1000 0.005 1 1115 233 233 TYR CA C 58.1100 0.010 1 1116 233 233 TYR CB C 39.3600 0.010 1 1117 233 233 TYR N N 114.0000 0.017 1 1118 234 234 PHE H H 8.0380 0.002 1 1119 234 234 PHE C C 175.8000 0.005 1 1120 234 234 PHE CA C 54.9200 0.010 1 1121 234 234 PHE CB C 41.2600 0.010 1 1122 234 234 PHE N N 116.4000 0.017 1 1123 235 235 ASP H H 8.8790 0.002 1 1124 235 235 ASP C C 174.5000 0.005 1 1125 235 235 ASP CA C 52.6800 0.010 1 1126 235 235 ASP CB C 39.8600 0.010 1 1127 235 235 ASP N N 123.0000 0.017 1 1128 236 236 PHE H H 6.7930 0.002 1 1129 236 236 PHE C C 173.6000 0.005 1 1130 236 236 PHE CA C 53.9500 0.010 1 1131 236 236 PHE CB C 39.8600 0.010 1 1132 236 236 PHE N N 115.5000 0.017 1 1133 237 237 ASP H H 8.8310 0.002 1 1134 237 237 ASP C C 175.8000 0.005 1 1135 237 237 ASP CA C 52.9800 0.010 1 1136 237 237 ASP CB C 39.2100 0.010 1 1137 237 237 ASP N N 119.7000 0.017 1 1138 238 238 VAL H H 7.3760 0.002 1 1139 238 238 VAL C C 175.2000 0.005 1 1140 238 238 VAL CA C 61.8400 0.010 1 1141 238 238 VAL CB C 32.5000 0.010 1 1142 238 238 VAL N N 129.9000 0.017 1 1143 239 239 TYR H H 8.3140 0.002 1 1144 239 239 TYR C C 176.5000 0.005 1 1145 239 239 TYR CA C 61.9200 0.010 1 1146 239 239 TYR CB C 38.0100 0.010 1 1147 239 239 TYR N N 123.5000 0.017 1 1148 240 240 GLY H H 7.4280 0.002 1 1149 240 240 GLY C C 174.6000 0.005 1 1150 240 240 GLY CA C 45.9300 0.010 1 1151 240 240 GLY N N 104.1000 0.017 1 1152 241 241 GLY H H 8.0310 0.002 1 1153 241 241 GLY C C 179.2000 0.005 1 1154 241 241 GLY CA C 45.7200 0.010 1 1155 241 241 GLY N N 115.7000 0.017 1 stop_ save_