data_19245 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shifts from E. coli HisJ complexed with Histidine ; _BMRB_accession_number 19245 _BMRB_flat_file_name bmr19245.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" 228 "13C chemical shifts" 697 "15N chemical shifts" 228 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-06 update BMRB 'update entry citation' 2013-09-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19242 'E. coli apo-HisJ' 19243 'Backbone chemical shifts of isolated Domain 1 from E. coli HisJ' 19244 'Backbone chemical shifts of isolated Domain 2 from E. coli HisJ' 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 . loop_ _Keyword 'E. coli' HisJ Histidine 'Periplasmic binding protein' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HisJ and Histidine' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protein $Holo-HisJ ligand $entity_HIS 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_Holo-HisJ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Holo-HisJ _Molecular_mass . _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 19242 apo-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_ ###################### # Polymer residues # ###################### save_chem_comp_HIS _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common HISTIDINE _BMRB_code HIS _PDB_code HIS _Standard_residue_derivative . _Molecular_mass 156.162 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? ND1 ND1 N . 1 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? NE2 NE2 N . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG ND1 ? ? DOUB CG CD2 ? ? DOUB ND1 CE1 ? ? SING ND1 HD1 ? ? SING CD2 NE2 ? ? SING CD2 HD2 ? ? SING CE1 NE2 ? ? SING CE1 HE1 ? ? SING NE2 HE2 ? ? SING OXT HXT ? ? stop_ save_ ############# # Ligands # ############# save_HIS _Saveframe_category ligand _Mol_type non-polymer _Name_common HISTIDINE _Molecular_mass 156.162 _Details . _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 _Strain $Holo-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 $Holo-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 $Holo-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' $entity_HIS 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_NMRPipe _Saveframe_category software _Name NMRPipe _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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 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 protein _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 . 1 2 2 2 GLY CA C 44.7300 . 1 3 3 3 MET H H 8.4420 . 1 4 3 3 MET C C 176.0000 . 1 5 3 3 MET CA C 55.0200 . 1 6 3 3 MET CB C 32.3600 . 1 7 3 3 MET N N 121.2000 . 1 8 4 4 ALA H H 8.3830 . 1 9 4 4 ALA C C 177.3000 . 1 10 4 4 ALA CA C 52.1700 . 1 11 4 4 ALA CB C 18.3400 . 1 12 4 4 ALA N N 125.7000 . 1 13 5 5 ILE H H 7.8670 . 1 14 5 5 ILE C C 174.3000 . 1 15 5 5 ILE CA C 57.7400 . 1 16 5 5 ILE CB C 37.3100 . 1 17 5 5 ILE N N 121.3000 . 1 18 6 6 PRO C C 176.1000 . 1 19 6 6 PRO CA C 62.2000 . 1 20 6 6 PRO CB C 31.6200 . 1 21 7 7 GLN H H 8.3830 . 1 22 7 7 GLN C C 175.6000 . 1 23 7 7 GLN CA C 57.1800 . 1 24 7 7 GLN CB C 28.5400 . 1 25 7 7 GLN N N 119.3000 . 1 26 8 8 ASN H H 7.4800 . 1 27 8 8 ASN C C 173.6000 . 1 28 8 8 ASN CA C 51.7500 . 1 29 8 8 ASN CB C 40.5700 . 1 30 8 8 ASN N N 116.3000 . 1 31 9 9 ILE H H 8.4260 . 1 32 9 9 ILE C C 174.7000 . 1 33 9 9 ILE CA C 59.5200 . 1 34 9 9 ILE CB C 39.7900 . 1 35 9 9 ILE N N 120.9000 . 1 36 10 10 ARG H H 9.1070 . 1 37 10 10 ARG C C 175.9000 . 1 38 10 10 ARG CA C 53.9300 . 1 39 10 10 ARG CB C 30.5500 . 1 40 10 10 ARG N N 126.5000 . 1 41 11 11 ILE H H 9.3380 . 1 42 11 11 ILE C C 175.7000 . 1 43 11 11 ILE CA C 59.5200 . 1 44 11 11 ILE CB C 37.3900 . 1 45 11 11 ILE N N 127.5000 . 1 46 12 12 GLY H H 9.3870 . 1 47 12 12 GLY C C 171.7000 . 1 48 12 12 GLY CA C 44.7000 . 1 49 12 12 GLY N N 114.8000 . 1 50 13 13 THR H H 8.6700 . 1 51 13 13 THR C C 181.3000 . 1 52 13 13 THR CA C 61.5400 . 1 53 13 13 THR CB C 70.1300 . 1 54 13 13 THR N N 121.1000 . 1 55 14 14 ASP H H 8.1520 . 1 56 14 14 ASP C C 176.9000 . 1 57 14 14 ASP CA C 49.6600 . 1 58 14 14 ASP CB C 40.8600 . 1 59 14 14 ASP N N 127.4000 . 1 60 15 15 PRO C C 175.9000 . 1 61 15 15 PRO CA C 61.7600 . 1 62 15 15 PRO CB C 27.9900 . 1 63 16 16 THR H H 8.8410 . 1 64 16 16 THR C C 173.8000 . 1 65 16 16 THR CA C 59.7900 . 1 66 16 16 THR CB C 69.8100 . 1 67 16 16 THR N N 115.8000 . 1 68 17 17 TYR H H 9.1680 . 1 69 17 17 TYR C C 175.3000 . 1 70 17 17 TYR CA C 56.1400 . 1 71 17 17 TYR CB C 40.9700 . 1 72 17 17 TYR N N 130.5000 . 1 73 18 18 ALA H H 8.6330 . 1 74 18 18 ALA C C 174.7000 . 1 75 18 18 ALA CA C 51.4300 . 1 76 18 18 ALA CB C 16.4600 . 1 77 18 18 ALA N N 129.8000 . 1 78 19 19 PRO C C 173.9000 . 1 79 19 19 PRO CA C 62.9100 . 1 80 19 19 PRO CB C 31.7300 . 1 81 20 20 PHE H H 8.4020 . 1 82 20 20 PHE C C 176.5000 . 1 83 20 20 PHE CA C 62.6100 . 1 84 20 20 PHE CB C 38.1400 . 1 85 20 20 PHE N N 125.5000 . 1 86 21 21 GLU H H 7.6680 . 1 87 21 21 GLU C C 173.7000 . 1 88 21 21 GLU CA C 54.4900 . 1 89 21 21 GLU CB C 28.9200 . 1 90 21 21 GLU N N 112.2000 . 1 91 22 22 SER H H 8.9160 . 1 92 22 22 SER C C 171.6000 . 1 93 22 22 SER CA C 57.3100 . 1 94 22 22 SER CB C 62.9900 . 1 95 22 22 SER N N 117.9000 . 1 96 23 23 LYS H H 8.2880 . 1 97 23 23 LYS C C 177.6000 . 1 98 23 23 LYS CA C 53.7500 . 1 99 23 23 LYS CB C 33.7200 . 1 100 23 23 LYS N N 117.5000 . 1 101 24 24 ASN H H 8.5640 . 1 102 24 24 ASN C C 178.0000 . 1 103 24 24 ASN CA C 50.5900 . 1 104 24 24 ASN CB C 38.1800 . 1 105 24 24 ASN N N 122.2000 . 1 106 25 25 SER C C 175.4000 . 1 107 25 25 SER CA C 60.9500 . 1 108 25 25 SER CB C 62.4600 . 1 109 26 26 GLN H H 7.5300 . 1 110 26 26 GLN C C 176.2000 . 1 111 26 26 GLN CA C 55.2000 . 1 112 26 26 GLN CB C 28.2800 . 1 113 26 26 GLN N N 119.3000 . 1 114 27 27 GLY H H 8.1790 . 1 115 27 27 GLY C C 173.8000 . 1 116 27 27 GLY CA C 45.0800 . 1 117 27 27 GLY N N 108.8000 . 1 118 28 28 GLU H H 7.8440 . 1 119 28 28 GLU C C 175.8000 . 1 120 28 28 GLU CA C 54.5100 . 1 121 28 28 GLU CB C 29.7400 . 1 122 28 28 GLU N N 121.2000 . 1 123 29 29 LEU H H 8.2920 . 1 124 29 29 LEU C C 176.5000 . 1 125 29 29 LEU CA C 54.3800 . 1 126 29 29 LEU CB C 41.2100 . 1 127 29 29 LEU N N 123.4000 . 1 128 30 30 VAL H H 8.9450 . 1 129 30 30 VAL C C 175.2000 . 1 130 30 30 VAL CA C 58.3800 . 1 131 30 30 VAL CB C 36.1400 . 1 132 30 30 VAL N N 118.4000 . 1 133 31 31 GLY H H 8.5280 . 1 134 31 31 GLY C C 174.7000 . 1 135 31 31 GLY CA C 43.8700 . 1 136 31 31 GLY N N 109.4000 . 1 137 32 32 PHE H H 8.0620 . 1 138 32 32 PHE C C 177.9000 . 1 139 32 32 PHE CA C 59.9600 . 1 140 32 32 PHE CB C 38.9800 . 1 141 32 32 PHE N N 119.8000 . 1 142 33 33 ASP H H 9.0740 . 1 143 33 33 ASP C C 179.2000 . 1 144 33 33 ASP CA C 56.2600 . 1 145 33 33 ASP CB C 38.5700 . 1 146 33 33 ASP N N 116.1000 . 1 147 34 34 ILE H H 6.6070 . 1 148 34 34 ILE C C 178.0000 . 1 149 34 34 ILE CA C 60.9500 . 1 150 34 34 ILE CB C 33.6600 . 1 151 34 34 ILE N N 119.2000 . 1 152 35 35 ASP H H 8.4770 . 1 153 35 35 ASP C C 180.3000 . 1 154 35 35 ASP CA C 57.1300 . 1 155 35 35 ASP CB C 40.3400 . 1 156 35 35 ASP N N 120.9000 . 1 157 36 36 LEU H H 8.4720 . 1 158 36 36 LEU C C 178.4000 . 1 159 36 36 LEU CA C 57.7900 . 1 160 36 36 LEU CB C 42.2700 . 1 161 36 36 LEU N N 120.4000 . 1 162 37 37 ALA H H 8.4490 . 1 163 37 37 ALA C C 178.5000 . 1 164 37 37 ALA CA C 55.1400 . 1 165 37 37 ALA CB C 17.3200 . 1 166 37 37 ALA N N 120.0000 . 1 167 38 38 LYS H H 8.7830 . 1 168 38 38 LYS C C 180.1000 . 1 169 38 38 LYS CA C 60.5400 . 1 170 38 38 LYS CB C 31.8500 . 1 171 38 38 LYS N N 116.4000 . 1 172 39 39 GLU H H 7.6970 . 1 173 39 39 GLU C C 178.3000 . 1 174 39 39 GLU CA C 58.4000 . 1 175 39 39 GLU CB C 27.9600 . 1 176 39 39 GLU N N 121.5000 . 1 177 40 40 LEU H H 8.5760 . 1 178 40 40 LEU C C 178.6000 . 1 179 40 40 LEU CA C 58.4800 . 1 180 40 40 LEU CB C 40.2300 . 1 181 40 40 LEU N N 121.5000 . 1 182 41 41 CYS H H 8.6170 . 1 183 41 41 CYS C C 175.8000 . 1 184 41 41 CYS CA C 62.5200 . 1 185 41 41 CYS CB C 46.9400 . 1 186 41 41 CYS N N 115.7000 . 1 187 42 42 LYS H H 7.4940 . 1 188 42 42 LYS C C 180.8000 . 1 189 42 42 LYS CA C 58.8100 . 1 190 42 42 LYS CB C 31.4000 . 1 191 42 42 LYS N N 119.3000 . 1 192 43 43 ARG H H 8.0780 . 1 193 43 43 ARG C C 178.7000 . 1 194 43 43 ARG CA C 58.8000 . 1 195 43 43 ARG CB C 29.9900 . 1 196 43 43 ARG N N 119.6000 . 1 197 44 44 ILE H H 7.7680 . 1 198 44 44 ILE C C 175.0000 . 1 199 44 44 ILE CA C 60.9500 . 1 200 44 44 ILE CB C 36.6200 . 1 201 44 44 ILE N N 111.7000 . 1 202 45 45 ASN H H 7.7580 . 1 203 45 45 ASN C C 173.6000 . 1 204 45 45 ASN CA C 53.6200 . 1 205 45 45 ASN CB C 36.6300 . 1 206 45 45 ASN N N 118.8000 . 1 207 46 46 THR H H 7.9240 . 1 208 46 46 THR C C 173.1000 . 1 209 46 46 THR CA C 60.0300 . 1 210 46 46 THR CB C 70.5000 . 1 211 46 46 THR N N 112.8000 . 1 212 47 47 GLN H H 8.0400 . 1 213 47 47 GLN C C 175.4000 . 1 214 47 47 GLN CA C 54.5800 . 1 215 47 47 GLN CB C 28.6600 . 1 216 47 47 GLN N N 123.5000 . 1 217 48 48 CYS H H 8.8790 . 1 218 48 48 CYS C C 173.7000 . 1 219 48 48 CYS CA C 53.1400 . 1 220 48 48 CYS CB C 47.4700 . 1 221 48 48 CYS N N 123.8000 . 1 222 49 49 THR H H 8.3340 . 1 223 49 49 THR C C 172.6000 . 1 224 49 49 THR CA C 60.1000 . 1 225 49 49 THR CB C 71.0000 . 1 226 49 49 THR N N 118.5000 . 1 227 50 50 PHE H H 8.9730 . 1 228 50 50 PHE C C 175.8000 . 1 229 50 50 PHE CA C 57.3800 . 1 230 50 50 PHE CB C 40.7600 . 1 231 50 50 PHE N N 123.4000 . 1 232 51 51 VAL H H 9.2710 . 1 233 51 51 VAL C C 174.7000 . 1 234 51 51 VAL CA C 60.7700 . 1 235 51 51 VAL CB C 33.5900 . 1 236 51 51 VAL N N 126.6000 . 1 237 52 52 GLU H H 8.5990 . 1 238 52 52 GLU C C 176.9000 . 1 239 52 52 GLU CA C 54.3900 . 1 240 52 52 GLU CB C 29.4900 . 1 241 52 52 GLU N N 126.9000 . 1 242 53 53 ASN H H 9.0230 . 1 243 53 53 ASN C C 170.6400 . 1 244 53 53 ASN CA C 51.4000 . 1 245 53 53 ASN CB C 43.9400 . 1 246 53 53 ASN N N 127.0000 . 1 247 54 54 PRO C C 178.2000 . 1 248 54 54 PRO CA C 62.0300 . 1 249 54 54 PRO CB C 31.6200 . 1 250 55 55 LEU H H 8.5410 . 1 251 55 55 LEU C C 179.9000 . 1 252 55 55 LEU CA C 57.6700 . 1 253 55 55 LEU CB C 40.7600 . 1 254 55 55 LEU N N 123.5000 . 1 255 56 56 ASP H H 8.4760 . 1 256 56 56 ASP C C 175.2000 . 1 257 56 56 ASP CA C 55.9500 . 1 258 56 56 ASP CB C 39.8900 . 1 259 56 56 ASP N N 114.4000 . 1 260 57 57 ALA H H 7.9080 . 1 261 57 57 ALA C C 180.3000 . 1 262 57 57 ALA CA C 51.3300 . 1 263 57 57 ALA CB C 19.0700 . 1 264 57 57 ALA N N 120.8000 . 1 265 58 58 LEU H H 7.8180 . 1 266 58 58 LEU C C 177.7000 . 1 267 58 58 LEU CA C 59.0000 . 1 268 58 58 LEU CB C 39.8000 . 1 269 58 58 LEU N N 121.8000 . 1 270 59 59 ILE H H 9.3860 . 1 271 59 59 ILE C C 176.4000 . 1 272 59 59 ILE CA C 68.4200 . 1 273 59 59 ILE CB C 34.0700 . 1 274 59 59 ILE N N 120.6000 . 1 275 60 60 PRO C C 180.1000 . 1 276 60 60 PRO CA C 65.8700 . 1 277 60 60 PRO CB C 30.0100 . 1 278 61 61 SER H H 7.7900 . 1 279 61 61 SER C C 175.5000 . 1 280 61 61 SER CA C 62.2300 . 1 281 61 61 SER N N 114.8000 . 1 282 62 62 LEU H H 8.3610 . 1 283 62 62 LEU C C 181.0000 . 1 284 62 62 LEU CA C 57.4000 . 1 285 62 62 LEU CB C 41.8400 . 1 286 62 62 LEU N N 126.1000 . 1 287 63 63 LYS H H 8.3480 . 1 288 63 63 LYS C C 178.0000 . 1 289 63 63 LYS CA C 59.4900 . 1 290 63 63 LYS CB C 30.7900 . 1 291 63 63 LYS N N 120.9000 . 1 292 64 64 ALA H H 7.6510 . 1 293 64 64 ALA C C 176.2000 . 1 294 64 64 ALA CA C 51.6800 . 1 295 64 64 ALA CB C 18.1500 . 1 296 64 64 ALA N N 118.6000 . 1 297 65 65 LYS H H 7.7390 . 1 298 65 65 LYS C C 175.9000 . 1 299 65 65 LYS CA C 57.8500 . 1 300 65 65 LYS CB C 27.7900 . 1 301 65 65 LYS N N 112.2000 . 1 302 66 66 LYS H H 8.3980 . 1 303 66 66 LYS C C 176.4000 . 1 304 66 66 LYS CA C 57.2100 . 1 305 66 66 LYS CB C 32.2300 . 1 306 66 66 LYS N N 118.2000 . 1 307 67 67 ILE H H 7.0250 . 1 308 67 67 ILE C C 174.0000 . 1 309 67 67 ILE CA C 59.0400 . 1 310 67 67 ILE CB C 40.4700 . 1 311 67 67 ILE N N 107.4000 . 1 312 68 68 ASP H H 9.7530 . 1 313 68 68 ASP C C 172.2000 . 1 314 68 68 ASP CA C 55.5100 . 1 315 68 68 ASP CB C 44.1600 . 1 316 68 68 ASP N N 119.2000 . 1 317 69 69 ALA H H 7.6950 . 1 318 69 69 ALA C C 175.9000 . 1 319 69 69 ALA CA C 50.0800 . 1 320 69 69 ALA CB C 21.8900 . 1 321 69 69 ALA N N 117.3000 . 1 322 70 70 ILE H H 9.4320 . 1 323 70 70 ILE C C 174.7000 . 1 324 70 70 ILE CA C 60.1500 . 1 325 70 70 ILE CB C 41.1900 . 1 326 70 70 ILE N N 120.5000 . 1 327 71 71 MET H H 8.4780 . 1 328 71 71 MET C C 172.5000 . 1 329 71 71 MET CA C 53.0700 . 1 330 71 71 MET CB C 34.0000 . 1 331 71 71 MET N N 127.9000 . 1 332 72 72 SER H H 8.7710 . 1 333 72 72 SER C C 173.9000 . 1 334 72 72 SER CA C 58.0700 . 1 335 72 72 SER CB C 64.6200 . 1 336 72 72 SER N N 123.3000 . 1 337 73 73 SER H H 8.7470 . 1 338 73 73 SER C C 174.4000 . 1 339 73 73 SER CA C 58.9300 . 1 340 73 73 SER CB C 64.2500 . 1 341 73 73 SER N N 124.2000 . 1 342 74 74 LEU H H 9.0120 . 1 343 74 74 LEU C C 175.2000 . 1 344 74 74 LEU CA C 54.4200 . 1 345 74 74 LEU CB C 42.6500 . 1 346 74 74 LEU N N 122.2000 . 1 347 75 75 SER H H 9.4530 . 1 348 75 75 SER C C 173.0000 . 1 349 75 75 SER CA C 60.0200 . 1 350 75 75 SER CB C 63.2000 . 1 351 75 75 SER N N 124.6000 . 1 352 76 76 ILE H H 8.3600 . 1 353 76 76 ILE C C 175.5000 . 1 354 76 76 ILE CA C 60.9600 . 1 355 76 76 ILE CB C 36.3900 . 1 356 76 76 ILE N N 125.2000 . 1 357 77 77 THR H H 6.0830 . 1 358 77 77 THR C C 174.9000 . 1 359 77 77 THR CA C 57.3200 . 1 360 77 77 THR CB C 72.0000 . 1 361 77 77 THR N N 115.3000 . 1 362 78 78 GLU H H 9.0480 . 1 363 78 78 GLU C C 179.2000 . 1 364 78 78 GLU CA C 59.0800 . 1 365 78 78 GLU CB C 28.9800 . 1 366 78 78 GLU N N 124.0000 . 1 367 79 79 LYS H H 8.4930 . 1 368 79 79 LYS C C 180.7000 . 1 369 79 79 LYS CA C 58.9000 . 1 370 79 79 LYS CB C 31.6700 . 1 371 79 79 LYS N N 119.3000 . 1 372 80 80 ARG H H 7.5680 . 1 373 80 80 ARG C C 179.2000 . 1 374 80 80 ARG CA C 59.3400 . 1 375 80 80 ARG CB C 30.5700 . 1 376 80 80 ARG N N 118.7000 . 1 377 81 81 GLN H H 8.5820 . 1 378 81 81 GLN C C 176.6000 . 1 379 81 81 GLN CA C 57.2700 . 1 380 81 81 GLN CB C 28.6900 . 1 381 81 81 GLN N N 119.7000 . 1 382 82 82 GLN H H 7.2540 . 1 383 82 82 GLN C C 177.4000 . 1 384 82 82 GLN CA C 57.3100 . 1 385 82 82 GLN CB C 27.9800 . 1 386 82 82 GLN N N 115.4000 . 1 387 83 83 GLU H H 7.6870 . 1 388 83 83 GLU C C 176.3000 . 1 389 83 83 GLU CA C 56.8000 . 1 390 83 83 GLU CB C 33.1300 . 1 391 83 83 GLU N N 115.3000 . 1 392 84 84 ILE H H 8.3470 . 1 393 84 84 ILE C C 172.4000 . 1 394 84 84 ILE CA C 59.4900 . 1 395 84 84 ILE CB C 40.8000 . 1 396 84 84 ILE N N 115.4000 . 1 397 85 85 ALA H H 8.7740 . 1 398 85 85 ALA C C 174.9000 . 1 399 85 85 ALA CA C 49.0600 . 1 400 85 85 ALA CB C 22.4900 . 1 401 85 85 ALA N N 120.5000 . 1 402 86 86 PHE H H 8.3300 . 1 403 86 86 PHE C C 178.5000 . 1 404 86 86 PHE CA C 55.7000 . 1 405 86 86 PHE CB C 44.9100 . 1 406 86 86 PHE N N 115.1000 . 1 407 87 87 THR H H 7.8530 . 1 408 87 87 THR C C 174.6000 . 1 409 87 87 THR CA C 61.8500 . 1 410 87 87 THR CB C 72.8500 . 1 411 87 87 THR N N 107.8000 . 1 412 88 88 ASP H H 8.8020 . 1 413 88 88 ASP C C 174.0000 . 1 414 88 88 ASP CA C 54.9100 . 1 415 88 88 ASP CB C 41.0300 . 1 416 88 88 ASP N N 118.2000 . 1 417 89 89 LYS H H 7.6780 . 1 418 89 89 LYS C C 176.5000 . 1 419 89 89 LYS CA C 55.7900 . 1 420 89 89 LYS CB C 31.6000 . 1 421 89 89 LYS N N 117.9000 . 1 422 90 90 LEU H H 8.9990 . 1 423 90 90 LEU C C 178.1000 . 1 424 90 90 LEU CA C 54.7000 . 1 425 90 90 LEU CB C 41.5000 . 1 426 90 90 LEU N N 124.4000 . 1 427 91 91 TYR H H 6.6060 . 1 428 91 91 TYR C C 173.4000 . 1 429 91 91 TYR CA C 56.1700 . 1 430 91 91 TYR CB C 37.8800 . 1 431 91 91 TYR N N 109.5000 . 1 432 92 92 ALA H H 7.8760 . 1 433 92 92 ALA C C 176.5000 . 1 434 92 92 ALA CA C 52.2400 . 1 435 92 92 ALA CB C 19.8000 . 1 436 92 92 ALA N N 123.7000 . 1 437 93 93 ALA H H 7.4750 . 1 438 93 93 ALA C C 174.8000 . 1 439 93 93 ALA CA C 52.3400 . 1 440 93 93 ALA CB C 20.9400 . 1 441 93 93 ALA N N 121.3000 . 1 442 94 94 ASP H H 8.1030 . 1 443 94 94 ASP C C 175.1000 . 1 444 94 94 ASP CA C 52.8800 . 1 445 94 94 ASP CB C 44.5900 . 1 446 94 94 ASP N N 121.9000 . 1 447 95 95 SER H H 9.6410 . 1 448 95 95 SER C C 172.5000 . 1 449 95 95 SER CA C 59.0200 . 1 450 95 95 SER CB C 64.2200 . 1 451 95 95 SER N N 118.9000 . 1 452 96 96 ARG H H 8.5500 . 1 453 96 96 ARG C C 174.7000 . 1 454 96 96 ARG CA C 56.9900 . 1 455 96 96 ARG CB C 34.7600 . 1 456 96 96 ARG N N 124.6000 . 1 457 97 97 LEU H H 9.7430 . 1 458 97 97 LEU C C 177.8000 . 1 459 97 97 LEU CA C 54.7200 . 1 460 97 97 LEU CB C 43.5500 . 1 461 97 97 LEU N N 128.2000 . 1 462 98 98 VAL H H 9.2380 . 1 463 98 98 VAL C C 175.0000 . 1 464 98 98 VAL CA C 61.6500 . 1 465 98 98 VAL CB C 33.7300 . 1 466 98 98 VAL N N 122.9000 . 1 467 99 99 VAL H H 9.1930 . 1 468 99 99 VAL C C 174.5000 . 1 469 99 99 VAL CA C 58.3900 . 1 470 99 99 VAL CB C 36.6700 . 1 471 99 99 VAL N N 117.2000 . 1 472 100 100 ALA H H 9.1290 . 1 473 100 100 ALA C C 179.2000 . 1 474 100 100 ALA CA C 52.7700 . 1 475 100 100 ALA CB C 18.2200 . 1 476 100 100 ALA N N 123.3000 . 1 477 101 101 LYS H H 7.9860 . 1 478 101 101 LYS C C 176.8000 . 1 479 101 101 LYS CA C 59.2700 . 1 480 101 101 LYS CB C 31.3600 . 1 481 101 101 LYS N N 119.9000 . 1 482 102 102 ASN C C 175.3000 . 1 483 102 102 ASN CA C 52.3100 . 1 484 102 102 ASN CB C 36.9700 . 1 485 103 103 SER H H 7.6800 . 1 486 103 103 SER C C 175.7000 . 1 487 103 103 SER CA C 58.0600 . 1 488 103 103 SER CB C 64.4900 . 1 489 103 103 SER N N 114.9000 . 1 490 104 104 ASP H H 8.5160 . 1 491 104 104 ASP C C 176.6000 . 1 492 104 104 ASP CA C 52.9900 . 1 493 104 104 ASP CB C 40.3000 . 1 494 104 104 ASP N N 128.0000 . 1 495 105 105 ILE H H 7.8000 . 1 496 105 105 ILE C C 174.0000 . 1 497 105 105 ILE CA C 63.6700 . 1 498 105 105 ILE CB C 37.6600 . 1 499 105 105 ILE N N 122.3000 . 1 500 106 106 GLN H H 8.1920 . 1 501 106 106 GLN C C 174.7000 . 1 502 106 106 GLN CA C 51.4000 . 1 503 106 106 GLN CB C 30.9300 . 1 504 106 106 GLN N N 125.3000 . 1 505 107 107 PRO C C 175.0000 . 1 506 107 107 PRO CA C 61.8200 . 1 507 107 107 PRO CB C 26.9200 . 1 508 108 108 THR H H 8.5840 . 1 509 108 108 THR C C 173.9000 . 1 510 108 108 THR CA C 57.7500 . 1 511 108 108 THR CB C 71.1100 . 1 512 108 108 THR N N 114.8000 . 1 513 109 109 VAL H H 8.7430 . 1 514 109 109 VAL C C 177.5000 . 1 515 109 109 VAL CA C 65.4200 . 1 516 109 109 VAL CB C 30.6100 . 1 517 109 109 VAL N N 121.7000 . 1 518 110 110 GLU H H 8.4510 . 1 519 110 110 GLU C C 178.5000 . 1 520 110 110 GLU CA C 59.2100 . 1 521 110 110 GLU CB C 28.1700 . 1 522 110 110 GLU N N 116.8000 . 1 523 111 111 SER H H 7.3540 . 1 524 111 111 SER C C 176.5000 . 1 525 111 111 SER CA C 59.4000 . 1 526 111 111 SER CB C 63.7400 . 1 527 111 111 SER N N 113.0000 . 1 528 112 112 LEU H H 7.5470 . 1 529 112 112 LEU C C 176.5000 . 1 530 112 112 LEU CA C 54.5300 . 1 531 112 112 LEU CB C 42.7000 . 1 532 112 112 LEU N N 116.9000 . 1 533 113 113 LYS H H 7.3310 . 1 534 113 113 LYS C C 178.2000 . 1 535 113 113 LYS CA C 58.8900 . 1 536 113 113 LYS CB C 30.9600 . 1 537 113 113 LYS N N 121.2000 . 1 538 114 114 GLY H H 8.4210 . 1 539 114 114 GLY C C 174.2000 . 1 540 114 114 GLY CA C 45.2600 . 1 541 114 114 GLY N N 113.8000 . 1 542 115 115 LYS H H 8.5360 . 1 543 115 115 LYS C C 174.8000 . 1 544 115 115 LYS CA C 53.6300 . 1 545 115 115 LYS CB C 32.1500 . 1 546 115 115 LYS N N 120.5000 . 1 547 116 116 ARG H H 9.4970 . 1 548 116 116 ARG C C 176.2000 . 1 549 116 116 ARG CA C 54.6000 . 1 550 116 116 ARG CB C 32.4900 . 1 551 116 116 ARG N N 119.1000 . 1 552 117 117 VAL H H 9.3650 . 1 553 117 117 VAL C C 175.2000 . 1 554 117 117 VAL CA C 60.2100 . 1 555 117 117 VAL CB C 33.6200 . 1 556 117 117 VAL N N 126.2000 . 1 557 118 118 GLY H H 9.4380 . 1 558 118 118 GLY C C 172.0000 . 1 559 118 118 GLY CA C 45.0600 . 1 560 118 118 GLY N N 114.5000 . 1 561 119 119 VAL H H 9.2350 . 1 562 119 119 VAL C C 173.6000 . 1 563 119 119 VAL CA C 58.0100 . 1 564 119 119 VAL CB C 36.0800 . 1 565 119 119 VAL N N 116.0000 . 1 566 120 120 LEU H H 8.6580 . 1 567 120 120 LEU C C 177.4000 . 1 568 120 120 LEU CA C 53.4700 . 1 569 120 120 LEU CB C 41.3900 . 1 570 120 120 LEU N N 124.4000 . 1 571 121 121 GLN H H 9.8160 . 1 572 121 121 GLN C C 176.9000 . 1 573 121 121 GLN CA C 57.7300 . 1 574 121 121 GLN CB C 28.0400 . 1 575 121 121 GLN N N 131.7000 . 1 576 122 122 GLY H H 9.5130 . 1 577 122 122 GLY C C 175.1000 . 1 578 122 122 GLY CA C 44.5800 . 1 579 122 122 GLY N N 113.3000 . 1 580 123 123 THR H H 7.4360 . 1 581 123 123 THR C C 177.4000 . 1 582 123 123 THR CA C 60.2500 . 1 583 123 123 THR CB C 74.0900 . 1 584 123 123 THR N N 106.7000 . 1 585 124 124 THR H H 8.5390 . 1 586 124 124 THR C C 178.3000 . 1 587 124 124 THR CA C 63.4200 . 1 588 124 124 THR CB C 66.3500 . 1 589 124 124 THR N N 113.9000 . 1 590 125 125 GLN H H 7.0710 . 1 591 125 125 GLN C C 178.0000 . 1 592 125 125 GLN CA C 61.2900 . 1 593 125 125 GLN CB C 24.5500 . 1 594 125 125 GLN N N 118.5000 . 1 595 126 126 GLU H H 7.6390 . 1 596 126 126 GLU C C 177.2000 . 1 597 126 126 GLU CA C 59.7400 . 1 598 126 126 GLU CB C 29.0900 . 1 599 126 126 GLU N N 121.9000 . 1 600 127 127 THR H H 7.9790 . 1 601 127 127 THR C C 176.4000 . 1 602 127 127 THR CA C 66.4500 . 1 603 127 127 THR CB C 68.2100 . 1 604 127 127 THR N N 117.2000 . 1 605 128 128 PHE H H 8.6210 . 1 606 128 128 PHE C C 177.6000 . 1 607 128 128 PHE CA C 61.2500 . 1 608 128 128 PHE CB C 39.7100 . 1 609 128 128 PHE N N 121.3000 . 1 610 129 129 GLY H H 9.0510 . 1 611 129 129 GLY C C 176.1000 . 1 612 129 129 GLY CA C 46.5000 . 1 613 129 129 GLY N N 107.4000 . 1 614 130 130 ASN H H 8.8000 . 1 615 130 130 ASN C C 176.1000 . 1 616 130 130 ASN CA C 55.6300 . 1 617 130 130 ASN CB C 37.5600 . 1 618 130 130 ASN N N 122.4000 . 1 619 131 131 GLU H H 7.6210 . 1 620 131 131 GLU C C 177.6000 . 1 621 131 131 GLU CA C 58.1500 . 1 622 131 131 GLU CB C 29.4700 . 1 623 131 131 GLU N N 118.6000 . 1 624 132 132 HIS H H 7.9250 . 1 625 132 132 HIS C C 176.0000 . 1 626 132 132 HIS CA C 57.0900 . 1 627 132 132 HIS CB C 31.4200 . 1 628 132 132 HIS N N 112.7000 . 1 629 133 133 TRP H H 7.6760 . 1 630 133 133 TRP C C 176.8000 . 1 631 133 133 TRP CA C 55.6500 . 1 632 133 133 TRP CB C 30.5500 . 1 633 133 133 TRP N N 119.8000 . 1 634 134 134 ALA H H 8.8940 . 1 635 134 134 ALA C C 177.9000 . 1 636 134 134 ALA CA C 55.3300 . 1 637 134 134 ALA CB C 15.8900 . 1 638 134 134 ALA N N 125.6000 . 1 639 135 135 PRO C C 177.1000 . 1 640 135 135 PRO CA C 64.4700 . 1 641 135 135 PRO CB C 30.8000 . 1 642 136 136 LYS H H 7.6670 . 1 643 136 136 LYS C C 176.5000 . 1 644 136 136 LYS CA C 53.4700 . 1 645 136 136 LYS CB C 31.5400 . 1 646 136 136 LYS N N 115.9000 . 1 647 137 137 GLY H H 7.8450 . 1 648 137 137 GLY C C 174.3000 . 1 649 137 137 GLY CA C 45.8000 . 1 650 137 137 GLY N N 106.0000 . 1 651 138 138 ILE H H 6.9370 . 1 652 138 138 ILE C C 174.4000 . 1 653 138 138 ILE CA C 60.5300 . 1 654 138 138 ILE CB C 38.2300 . 1 655 138 138 ILE N N 124.6000 . 1 656 139 139 GLU H H 8.2870 . 1 657 139 139 GLU C C 174.1000 . 1 658 139 139 GLU CA C 56.0500 . 1 659 139 139 GLU CB C 29.6500 . 1 660 139 139 GLU N N 128.1000 . 1 661 140 140 ILE H H 8.7620 . 1 662 140 140 ILE C C 175.9000 . 1 663 140 140 ILE CA C 57.2000 . 1 664 140 140 ILE CB C 34.3900 . 1 665 140 140 ILE N N 129.4000 . 1 666 141 141 VAL H H 9.4240 . 1 667 141 141 VAL C C 174.6000 . 1 668 141 141 VAL CA C 61.1800 . 1 669 141 141 VAL CB C 32.4100 . 1 670 141 141 VAL N N 133.0000 . 1 671 142 142 SER H H 8.5600 . 1 672 142 142 SER C C 175.0000 . 1 673 142 142 SER CA C 57.9300 . 1 674 142 142 SER CB C 63.9600 . 1 675 142 142 SER N N 123.4000 . 1 676 143 143 TYR H H 8.8180 . 1 677 143 143 TYR C C 175.9000 . 1 678 143 143 TYR CA C 57.4400 . 1 679 143 143 TYR CB C 42.8300 . 1 680 143 143 TYR N N 122.8000 . 1 681 144 144 GLN H H 8.5600 . 1 682 144 144 GLN C C 175.8000 . 1 683 144 144 GLN CA C 55.6900 . 1 684 144 144 GLN CB C 29.5600 . 1 685 144 144 GLN N N 118.9000 . 1 686 145 145 GLY H H 8.9330 . 1 687 145 145 GLY C C 174.6000 . 1 688 145 145 GLY CA C 44.5600 . 1 689 145 145 GLY N N 114.0000 . 1 690 146 146 GLN H H 7.6010 . 1 691 146 146 GLN C C 177.5000 . 1 692 146 146 GLN CA C 58.4700 . 1 693 146 146 GLN CB C 26.0100 . 1 694 146 146 GLN N N 126.8000 . 1 695 147 147 ASP H H 8.6560 . 1 696 147 147 ASP C C 178.7000 . 1 697 147 147 ASP CA C 56.5900 . 1 698 147 147 ASP CB C 38.4300 . 1 699 147 147 ASP N N 116.1000 . 1 700 148 148 ASN H H 7.3780 . 1 701 148 148 ASN C C 176.8000 . 1 702 148 148 ASN CA C 55.5400 . 1 703 148 148 ASN CB C 37.7600 . 1 704 148 148 ASN N N 118.2000 . 1 705 149 149 ILE H H 6.8640 . 1 706 149 149 ILE C C 177.9000 . 1 707 149 149 ILE CA C 64.7500 . 1 708 149 149 ILE CB C 35.1500 . 1 709 149 149 ILE N N 121.3000 . 1 710 150 150 TYR H H 6.5750 . 1 711 150 150 TYR C C 178.5000 . 1 712 150 150 TYR CA C 57.8900 . 1 713 150 150 TYR CB C 35.9200 . 1 714 150 150 TYR N N 116.5000 . 1 715 151 151 SER H H 8.0870 . 1 716 151 151 SER C C 177.4000 . 1 717 151 151 SER CA C 61.1100 . 1 718 151 151 SER CB C 62.3500 . 1 719 151 151 SER N N 113.2000 . 1 720 152 152 ASP H H 7.6730 . 1 721 152 152 ASP C C 179.0000 . 1 722 152 152 ASP CA C 56.3800 . 1 723 152 152 ASP CB C 38.2500 . 1 724 152 152 ASP N N 123.6000 . 1 725 153 153 LEU H H 8.1700 . 1 726 153 153 LEU C C 180.4000 . 1 727 153 153 LEU CA C 58.1100 . 1 728 153 153 LEU CB C 40.8200 . 1 729 153 153 LEU N N 124.2000 . 1 730 154 154 THR H H 8.2680 . 1 731 154 154 THR C C 176.7000 . 1 732 154 154 THR CA C 63.9000 . 1 733 154 154 THR CB C 68.4900 . 1 734 154 154 THR N N 112.5000 . 1 735 155 155 ALA H H 7.5510 . 1 736 155 155 ALA C C 178.2000 . 1 737 155 155 ALA CA C 51.6100 . 1 738 155 155 ALA CB C 18.9100 . 1 739 155 155 ALA N N 122.0000 . 1 740 156 156 GLY H H 7.9810 . 1 741 156 156 GLY C C 175.1000 . 1 742 156 156 GLY CA C 45.4200 . 1 743 156 156 GLY N N 107.9000 . 1 744 157 157 ARG H H 8.3310 . 1 745 157 157 ARG C C 176.2000 . 1 746 157 157 ARG CA C 57.2400 . 1 747 157 157 ARG CB C 30.4500 . 1 748 157 157 ARG N N 118.9000 . 1 749 158 158 ILE H H 7.1470 . 1 750 158 158 ILE C C 173.6000 . 1 751 158 158 ILE CA C 59.7200 . 1 752 158 158 ILE CB C 40.3200 . 1 753 158 158 ILE N N 109.0000 . 1 754 159 159 ASP H H 8.8160 . 1 755 159 159 ASP C C 174.7000 . 1 756 159 159 ASP CA C 55.6200 . 1 757 159 159 ASP CB C 43.6700 . 1 758 159 159 ASP N N 118.8000 . 1 759 160 160 ALA H H 7.7490 . 1 760 160 160 ALA C C 174.1000 . 1 761 160 160 ALA CA C 50.0000 . 1 762 160 160 ALA CB C 22.7500 . 1 763 160 160 ALA N N 117.0000 . 1 764 161 161 ALA H H 9.1050 . 1 765 161 161 ALA C C 175.8000 . 1 766 161 161 ALA CA C 50.1100 . 1 767 161 161 ALA CB C 21.8700 . 1 768 161 161 ALA N N 125.7000 . 1 769 162 162 PHE H H 9.2290 . 1 770 162 162 PHE C C 172.2000 . 1 771 162 162 PHE CA C 52.7400 . 1 772 162 162 PHE CB C 40.9700 . 1 773 162 162 PHE N N 128.5000 . 1 774 163 163 GLN H H 7.4960 . 1 775 163 163 GLN C C 174.5000 . 1 776 163 163 GLN CA C 55.9200 . 1 777 163 163 GLN CB C 29.1500 . 1 778 163 163 GLN N N 122.6000 . 1 779 164 164 ASP H H 7.2860 . 1 780 164 164 ASP C C 177.5000 . 1 781 164 164 ASP CA C 54.8900 . 1 782 164 164 ASP CB C 40.0500 . 1 783 164 164 ASP N N 116.3000 . 1 784 165 165 GLU H H 9.6800 . 1 785 165 165 GLU C C 177.8000 . 1 786 165 165 GLU CA C 59.4900 . 1 787 165 165 GLU CB C 30.3300 . 1 788 165 165 GLU N N 128.6000 . 1 789 166 166 VAL H H 9.5910 . 1 790 166 166 VAL C C 178.2000 . 1 791 166 166 VAL CA C 66.1500 . 1 792 166 166 VAL CB C 30.5500 . 1 793 166 166 VAL N N 119.8000 . 1 794 167 167 ALA H H 6.1740 . 1 795 167 167 ALA C C 178.6000 . 1 796 167 167 ALA CA C 54.1100 . 1 797 167 167 ALA CB C 17.1300 . 1 798 167 167 ALA N N 118.1000 . 1 799 168 168 ALA H H 7.4130 . 1 800 168 168 ALA C C 180.8000 . 1 801 168 168 ALA CA C 53.7300 . 1 802 168 168 ALA CB C 19.9400 . 1 803 168 168 ALA N N 117.3000 . 1 804 169 169 SER H H 8.9420 . 1 805 169 169 SER C C 175.6000 . 1 806 169 169 SER CA C 60.8700 . 1 807 169 169 SER CB C 62.9700 . 1 808 169 169 SER N N 113.6000 . 1 809 170 170 GLU H H 8.2490 . 1 810 170 170 GLU C C 179.0000 . 1 811 170 170 GLU CA C 56.6700 . 1 812 170 170 GLU CB C 28.8300 . 1 813 170 170 GLU N N 112.7000 . 1 814 171 171 GLY H H 8.4020 . 1 815 171 171 GLY C C 173.5000 . 1 816 171 171 GLY CA C 44.7000 . 1 817 171 171 GLY N N 106.4000 . 1 818 172 172 PHE H H 7.0360 . 1 819 172 172 PHE C C 174.8000 . 1 820 172 172 PHE CA C 60.3100 . 1 821 172 172 PHE CB C 40.1400 . 1 822 172 172 PHE N N 118.7000 . 1 823 173 173 LEU H H 9.0310 . 1 824 173 173 LEU C C 178.9000 . 1 825 173 173 LEU CA C 57.5000 . 1 826 173 173 LEU CB C 39.9400 . 1 827 173 173 LEU N N 119.2000 . 1 828 174 174 LYS H H 7.6310 . 1 829 174 174 LYS C C 176.9000 . 1 830 174 174 LYS CA C 56.4300 . 1 831 174 174 LYS CB C 31.8100 . 1 832 174 174 LYS N N 113.4000 . 1 833 175 175 GLN H H 7.1720 . 1 834 175 175 GLN C C 175.9000 . 1 835 175 175 GLN CA C 52.3200 . 1 836 175 175 GLN CB C 26.4300 . 1 837 175 175 GLN N N 118.7000 . 1 838 176 176 PRO C C 179.3000 . 1 839 176 176 PRO CA C 66.1900 . 1 840 176 176 PRO CB C 30.7400 . 1 841 177 177 VAL H H 7.4750 . 1 842 177 177 VAL C C 176.2000 . 1 843 177 177 VAL CA C 62.8500 . 1 844 177 177 VAL CB C 30.7900 . 1 845 177 177 VAL N N 111.6000 . 1 846 178 178 GLY H H 7.2290 . 1 847 178 178 GLY C C 174.8000 . 1 848 178 178 GLY CA C 44.0500 . 1 849 178 178 GLY N N 109.7000 . 1 850 179 179 LYS H H 6.8770 . 1 851 179 179 LYS C C 177.0000 . 1 852 179 179 LYS CA C 58.3400 . 1 853 179 179 LYS CB C 31.3600 . 1 854 179 179 LYS N N 120.3000 . 1 855 180 180 ASP H H 7.9920 . 1 856 180 180 ASP C C 173.9000 . 1 857 180 180 ASP CA C 53.9100 . 1 858 180 180 ASP CB C 39.6100 . 1 859 180 180 ASP N N 117.2000 . 1 860 181 181 TYR H H 7.7160 . 1 861 181 181 TYR C C 172.4000 . 1 862 181 181 TYR CA C 58.1000 . 1 863 181 181 TYR CB C 41.5200 . 1 864 181 181 TYR N N 120.2000 . 1 865 182 182 LYS H H 9.4370 . 1 866 182 182 LYS C C 175.0000 . 1 867 182 182 LYS CA C 54.3400 . 1 868 182 182 LYS CB C 35.5800 . 1 869 182 182 LYS N N 117.0000 . 1 870 183 183 PHE H H 8.5400 . 1 871 183 183 PHE C C 177.6000 . 1 872 183 183 PHE CA C 58.1900 . 1 873 183 183 PHE CB C 38.2100 . 1 874 183 183 PHE N N 117.9000 . 1 875 184 184 GLY H H 8.9190 . 1 876 184 184 GLY C C 173.4000 . 1 877 184 184 GLY CA C 46.9600 . 1 878 184 184 GLY N N 113.5000 . 1 879 185 185 GLY H H 7.6490 . 1 880 185 185 GLY C C 171.1000 . 1 881 185 185 GLY CA C 44.5200 . 1 882 185 185 GLY N N 110.3000 . 1 883 186 186 PRO C C 176.2000 . 1 884 186 186 PRO CA C 61.8500 . 1 885 186 186 PRO CB C 32.5900 . 1 886 187 187 SER H H 8.3680 . 1 887 187 187 SER C C 173.9000 . 1 888 187 187 SER CA C 58.6300 . 1 889 187 187 SER CB C 63.0300 . 1 890 187 187 SER N N 113.8000 . 1 891 188 188 VAL H H 8.1240 . 1 892 188 188 VAL C C 174.4000 . 1 893 188 188 VAL CA C 61.3300 . 1 894 188 188 VAL CB C 31.6300 . 1 895 188 188 VAL N N 123.9000 . 1 896 189 189 LYS H H 8.4920 . 1 897 189 189 LYS C C 177.0000 . 1 898 189 189 LYS CA C 54.9500 . 1 899 189 189 LYS CB C 32.0900 . 1 900 189 189 LYS N N 126.9000 . 1 901 190 190 ASP H H 8.8510 . 1 902 190 190 ASP C C 174.9000 . 1 903 190 190 ASP CA C 55.5400 . 1 904 190 190 ASP CB C 40.5600 . 1 905 190 190 ASP N N 123.7000 . 1 906 191 191 GLU H H 9.2080 . 1 907 191 191 GLU C C 178.5000 . 1 908 191 191 GLU CA C 59.8400 . 1 909 191 191 GLU CB C 28.4900 . 1 910 191 191 GLU N N 128.4000 . 1 911 192 192 LYS H H 7.9410 . 1 912 192 192 LYS C C 178.6000 . 1 913 192 192 LYS CA C 58.6500 . 1 914 192 192 LYS CB C 31.6600 . 1 915 192 192 LYS N N 118.3000 . 1 916 193 193 LEU H H 7.9950 . 1 917 193 193 LEU C C 178.1000 . 1 918 193 193 LEU CA C 55.9700 . 1 919 193 193 LEU CB C 41.5500 . 1 920 193 193 LEU N N 118.0000 . 1 921 194 194 PHE H H 8.3670 . 1 922 194 194 PHE C C 179.5000 . 1 923 194 194 PHE CA C 57.3100 . 1 924 194 194 PHE CB C 39.7800 . 1 925 194 194 PHE N N 112.5000 . 1 926 195 195 GLY H H 7.5570 . 1 927 195 195 GLY C C 173.1000 . 1 928 195 195 GLY CA C 44.4200 . 1 929 195 195 GLY N N 107.6000 . 1 930 196 196 VAL H H 9.1050 . 1 931 196 196 VAL C C 177.4000 . 1 932 196 196 VAL CA C 60.3300 . 1 933 196 196 VAL CB C 32.1300 . 1 934 196 196 VAL N N 109.9000 . 1 935 197 197 GLY H H 7.6420 . 1 936 197 197 GLY C C 170.5000 . 1 937 197 197 GLY CA C 44.5900 . 1 938 197 197 GLY N N 110.0000 . 1 939 198 198 THR H H 7.8640 . 1 940 198 198 THR C C 172.1000 . 1 941 198 198 THR CA C 58.9000 . 1 942 198 198 THR CB C 71.4700 . 1 943 198 198 THR N N 107.9000 . 1 944 199 199 GLY H H 8.4160 . 1 945 199 199 GLY C C 172.2000 . 1 946 199 199 GLY CA C 44.0200 . 1 947 199 199 GLY N N 104.3000 . 1 948 200 200 MET H H 8.1080 . 1 949 200 200 MET C C 176.4000 . 1 950 200 200 MET CA C 55.5100 . 1 951 200 200 MET CB C 33.3200 . 1 952 200 200 MET N N 121.0000 . 1 953 201 201 GLY H H 8.7570 . 1 954 201 201 GLY C C 172.0000 . 1 955 201 201 GLY CA C 44.3200 . 1 956 201 201 GLY N N 111.7000 . 1 957 202 202 LEU H H 8.7830 . 1 958 202 202 LEU C C 175.9000 . 1 959 202 202 LEU CA C 53.7200 . 1 960 202 202 LEU CB C 46.0900 . 1 961 202 202 LEU N N 124.8000 . 1 962 203 203 ARG H H 10.3400 . 1 963 203 203 ARG C C 180.4000 . 1 964 203 203 ARG CA C 57.1200 . 1 965 203 203 ARG CB C 29.6100 . 1 966 203 203 ARG N N 121.9000 . 1 967 204 204 LYS H H 9.2860 . 1 968 204 204 LYS C C 178.2000 . 1 969 204 204 LYS CA C 59.6000 . 1 970 204 204 LYS CB C 31.8300 . 1 971 204 204 LYS N N 123.2000 . 1 972 205 205 GLU H H 9.0270 . 1 973 205 205 GLU C C 177.6000 . 1 974 205 205 GLU CA C 57.2200 . 1 975 205 205 GLU CB C 27.7200 . 1 976 205 205 GLU N N 113.8000 . 1 977 206 206 ASP H H 7.2610 . 1 978 206 206 ASP C C 177.4000 . 1 979 206 206 ASP CA C 53.6700 . 1 980 206 206 ASP CB C 37.5300 . 1 981 206 206 ASP N N 126.1000 . 1 982 207 207 ASN H H 7.8370 . 1 983 207 207 ASN C C 176.9000 . 1 984 207 207 ASN CA C 56.9700 . 1 985 207 207 ASN CB C 38.8900 . 1 986 207 207 ASN N N 120.2000 . 1 987 208 208 GLU H H 8.7820 . 1 988 208 208 GLU C C 179.9000 . 1 989 208 208 GLU CA C 59.8400 . 1 990 208 208 GLU CB C 27.6200 . 1 991 208 208 GLU N N 120.5000 . 1 992 209 209 LEU H H 8.3650 . 1 993 209 209 LEU C C 177.1000 . 1 994 209 209 LEU CA C 57.4200 . 1 995 209 209 LEU CB C 40.6800 . 1 996 209 209 LEU N N 122.9000 . 1 997 210 210 ARG H H 7.5690 . 1 998 210 210 ARG C C 177.5000 . 1 999 210 210 ARG CA C 59.9500 . 1 1000 210 210 ARG CB C 30.0700 . 1 1001 210 210 ARG N N 119.2000 . 1 1002 211 211 GLU H H 8.4150 . 1 1003 211 211 GLU C C 179.8000 . 1 1004 211 211 GLU CA C 59.1500 . 1 1005 211 211 GLU CB C 28.5800 . 1 1006 211 211 GLU N N 116.2000 . 1 1007 212 212 ALA H H 8.1610 . 1 1008 212 212 ALA C C 181.3000 . 1 1009 212 212 ALA CA C 54.7600 . 1 1010 212 212 ALA CB C 17.1800 . 1 1011 212 212 ALA N N 123.5000 . 1 1012 213 213 LEU H H 8.3770 . 1 1013 213 213 LEU C C 178.5000 . 1 1014 213 213 LEU CA C 57.6600 . 1 1015 213 213 LEU CB C 41.5300 . 1 1016 213 213 LEU N N 121.1000 . 1 1017 214 214 ASN H H 8.4320 . 1 1018 214 214 ASN C C 179.7000 . 1 1019 214 214 ASN CA C 55.2200 . 1 1020 214 214 ASN CB C 37.1000 . 1 1021 214 214 ASN N N 119.2000 . 1 1022 215 215 LYS H H 8.1080 . 1 1023 215 215 LYS C C 178.4000 . 1 1024 215 215 LYS CA C 59.1100 . 1 1025 215 215 LYS CB C 31.7300 . 1 1026 215 215 LYS N N 123.9000 . 1 1027 216 216 ALA H H 7.9560 . 1 1028 216 216 ALA C C 179.5000 . 1 1029 216 216 ALA CA C 54.1700 . 1 1030 216 216 ALA CB C 18.7000 . 1 1031 216 216 ALA N N 122.1000 . 1 1032 217 217 PHE H H 8.9280 . 1 1033 217 217 PHE C C 177.2000 . 1 1034 217 217 PHE CA C 61.2700 . 1 1035 217 217 PHE CB C 37.9500 . 1 1036 217 217 PHE N N 119.5000 . 1 1037 218 218 ALA H H 7.9970 . 1 1038 218 218 ALA C C 182.1000 . 1 1039 218 218 ALA CA C 54.8000 . 1 1040 218 218 ALA CB C 16.6700 . 1 1041 218 218 ALA N N 121.4000 . 1 1042 219 219 GLU H H 7.9910 . 1 1043 219 219 GLU C C 178.6000 . 1 1044 219 219 GLU CA C 59.0800 . 1 1045 219 219 GLU CB C 28.3000 . 1 1046 219 219 GLU N N 120.1000 . 1 1047 220 220 MET H H 8.2330 . 1 1048 220 220 MET C C 179.2000 . 1 1049 220 220 MET CA C 57.4500 . 1 1050 220 220 MET CB C 32.7100 . 1 1051 220 220 MET N N 120.9000 . 1 1052 221 221 ARG H H 7.8010 . 1 1053 221 221 ARG C C 179.2000 . 1 1054 221 221 ARG CA C 58.7100 . 1 1055 221 221 ARG CB C 27.5100 . 1 1056 221 221 ARG N N 119.4000 . 1 1057 222 222 ALA H H 7.8320 . 1 1058 222 222 ALA C C 179.3000 . 1 1059 222 222 ALA CA C 54.1500 . 1 1060 222 222 ALA CB C 18.0800 . 1 1061 222 222 ALA N N 122.4000 . 1 1062 223 223 ASP H H 8.1600 . 1 1063 223 223 ASP C C 177.9000 . 1 1064 223 223 ASP CA C 53.0800 . 1 1065 223 223 ASP CB C 39.5900 . 1 1066 223 223 ASP N N 115.2000 . 1 1067 224 224 GLY H H 7.1940 . 1 1068 224 224 GLY C C 176.0000 . 1 1069 224 224 GLY CA C 45.0700 . 1 1070 224 224 GLY N N 106.7000 . 1 1071 225 225 THR H H 9.1350 . 1 1072 225 225 THR C C 175.7000 . 1 1073 225 225 THR CA C 67.6300 . 1 1074 225 225 THR CB C 66.8000 . 1 1075 225 225 THR N N 122.5000 . 1 1076 226 226 TYR H H 8.0900 . 1 1077 226 226 TYR C C 176.0000 . 1 1078 226 226 TYR CA C 62.5800 . 1 1079 226 226 TYR CB C 38.3400 . 1 1080 226 226 TYR N N 121.6000 . 1 1081 227 227 GLU H H 8.1560 . 1 1082 227 227 GLU C C 178.2000 . 1 1083 227 227 GLU CA C 58.9300 . 1 1084 227 227 GLU CB C 28.8000 . 1 1085 227 227 GLU N N 118.2000 . 1 1086 228 228 LYS H H 7.6190 . 1 1087 228 228 LYS C C 179.5000 . 1 1088 228 228 LYS CA C 59.3300 . 1 1089 228 228 LYS CB C 31.6100 . 1 1090 228 228 LYS N N 119.4000 . 1 1091 229 229 LEU H H 8.1390 . 1 1092 229 229 LEU C C 179.4000 . 1 1093 229 229 LEU CA C 56.9800 . 1 1094 229 229 LEU CB C 41.4500 . 1 1095 229 229 LEU N N 119.1000 . 1 1096 230 230 ALA H H 8.9350 . 1 1097 230 230 ALA C C 180.5000 . 1 1098 230 230 ALA CA C 54.8900 . 1 1099 230 230 ALA CB C 17.4600 . 1 1100 230 230 ALA N N 121.2000 . 1 1101 231 231 LYS H H 8.1220 . 1 1102 231 231 LYS C C 177.7000 . 1 1103 231 231 LYS CA C 57.4000 . 1 1104 231 231 LYS CB C 31.3400 . 1 1105 231 231 LYS N N 117.4000 . 1 1106 232 232 LYS H H 7.0460 . 1 1107 232 232 LYS C C 176.7000 . 1 1108 232 232 LYS CA C 57.8900 . 1 1109 232 232 LYS CB C 31.2300 . 1 1110 232 232 LYS N N 117.8000 . 1 1111 233 233 TYR H H 6.9680 . 1 1112 233 233 TYR C C 175.2000 . 1 1113 233 233 TYR CA C 58.0800 . 1 1114 233 233 TYR CB C 38.8600 . 1 1115 233 233 TYR N N 113.8000 . 1 1116 234 234 PHE H H 8.1210 . 1 1117 234 234 PHE C C 175.8000 . 1 1118 234 234 PHE CA C 54.4400 . 1 1119 234 234 PHE CB C 41.1700 . 1 1120 234 234 PHE N N 116.1000 . 1 1121 235 235 ASP H H 8.6070 . 1 1122 235 235 ASP C C 174.3000 . 1 1123 235 235 ASP CA C 52.2000 . 1 1124 235 235 ASP CB C 39.4200 . 1 1125 235 235 ASP N N 123.3000 . 1 1126 236 236 PHE H H 6.6390 . 1 1127 236 236 PHE C C 173.7000 . 1 1128 236 236 PHE CA C 53.7700 . 1 1129 236 236 PHE CB C 39.9800 . 1 1130 236 236 PHE N N 115.0000 . 1 1131 237 237 ASP H H 8.7280 . 1 1132 237 237 ASP C C 175.8000 . 1 1133 237 237 ASP CA C 53.1100 . 1 1134 237 237 ASP CB C 39.4100 . 1 1135 237 237 ASP N N 119.2000 . 1 1136 238 238 VAL H H 7.5440 . 1 1137 238 238 VAL C C 175.6000 . 1 1138 238 238 VAL CA C 61.6600 . 1 1139 238 238 VAL CB C 32.4800 . 1 1140 238 238 VAL N N 129.4000 . 1 1141 239 239 TYR H H 8.3820 . 1 1142 239 239 TYR C C 176.8000 . 1 1143 239 239 TYR CA C 62.2900 . 1 1144 239 239 TYR CB C 38.0400 . 1 1145 239 239 TYR N N 124.5000 . 1 1146 240 240 GLY H H 7.6180 . 1 1147 240 240 GLY C C 174.3000 . 1 1148 240 240 GLY CA C 45.4400 . 1 1149 240 240 GLY N N 104.7000 . 1 1150 241 241 GLY H H 7.9330 . 1 1151 241 241 GLY C C 179.1000 . 1 1152 241 241 GLY CA C 45.6500 . 1 1153 241 241 GLY N N 115.6000 . 1 stop_ save_