data_5693 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments of Grb2 complexed with ligand peptides for SH3 and SH2 domains ; _BMRB_accession_number 5693 _BMRB_flat_file_name bmr5693.str _Entry_type original _Submission_date 2003-02-13 _Accession_date 2003-02-13 _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 Yuzawa Satoru . . 2 Ogura Kenji . . 3 Hatanaka Hideki . . 4 Miura Kin-ichiro . . 5 Inagaki Fuyuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 "13C chemical shifts" 608 "15N chemical shifts" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-07 original author . stop_ _Original_release_date 2003-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone assignments of Grb2 complexed with ligand peptides for SH3 and SH2 domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuzawa Satoru . . 2 Ogura Kenji . . 3 Hatanaka Hideki . . 4 Miura Kin-ichiro . . 5 Inagaki Fuyuhiko . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 185 _Page_last 186 _Year 2003 _Details . loop_ _Keyword 'growth factor receptor-bound protein 2' grb2 multidomain 'sh2 domain' 'sh3 domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995). ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ ################################## # Molecular system description # ################################## save_ligand-loaded_Grb2 _Saveframe_category molecular_system _Mol_system_name 'Ligand loaded growth factor receptor-bound protein 2' _Abbreviation_common 'ligand-loaded Grb2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Grb2 $Grb2 'EGF Receptor phosphorylated peptide' $EGFR-peptide 'Sos peptide' $Sos-peptide stop_ _System_molecular_weight 28375 _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'signal transduction' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Grb2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'growth factor receptor-bound protein 2' _Name_variant C32S/C198A _Abbreviation_common Grb2 _Molecular_mass 25157 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 217 _Mol_residue_sequence ; MEAIAKYDFKATADDELSFK RGDILKVLNEESDQNWYKAE LNGKDGFIPKNYIEMKPHPW FFGKIPRAKAEEMLSKQRHD GAFLIRESESAPGDFSLSVK FGNDVQHFKVLRDGAGKYFL WVVKFNSLNELVDYHRSTSV SRNQQIFLRDIEQVPQQPTY VQALFDFDPQEDGELGFRRG DFIHVMDNSDPNWWKGAAHG QTGMFPRNYVTPVNRNV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 ALA 4 ILE 5 ALA 6 LYS 7 TYR 8 ASP 9 PHE 10 LYS 11 ALA 12 THR 13 ALA 14 ASP 15 ASP 16 GLU 17 LEU 18 SER 19 PHE 20 LYS 21 ARG 22 GLY 23 ASP 24 ILE 25 LEU 26 LYS 27 VAL 28 LEU 29 ASN 30 GLU 31 GLU 32 SER 33 ASP 34 GLN 35 ASN 36 TRP 37 TYR 38 LYS 39 ALA 40 GLU 41 LEU 42 ASN 43 GLY 44 LYS 45 ASP 46 GLY 47 PHE 48 ILE 49 PRO 50 LYS 51 ASN 52 TYR 53 ILE 54 GLU 55 MET 56 LYS 57 PRO 58 HIS 59 PRO 60 TRP 61 PHE 62 PHE 63 GLY 64 LYS 65 ILE 66 PRO 67 ARG 68 ALA 69 LYS 70 ALA 71 GLU 72 GLU 73 MET 74 LEU 75 SER 76 LYS 77 GLN 78 ARG 79 HIS 80 ASP 81 GLY 82 ALA 83 PHE 84 LEU 85 ILE 86 ARG 87 GLU 88 SER 89 GLU 90 SER 91 ALA 92 PRO 93 GLY 94 ASP 95 PHE 96 SER 97 LEU 98 SER 99 VAL 100 LYS 101 PHE 102 GLY 103 ASN 104 ASP 105 VAL 106 GLN 107 HIS 108 PHE 109 LYS 110 VAL 111 LEU 112 ARG 113 ASP 114 GLY 115 ALA 116 GLY 117 LYS 118 TYR 119 PHE 120 LEU 121 TRP 122 VAL 123 VAL 124 LYS 125 PHE 126 ASN 127 SER 128 LEU 129 ASN 130 GLU 131 LEU 132 VAL 133 ASP 134 TYR 135 HIS 136 ARG 137 SER 138 THR 139 SER 140 VAL 141 SER 142 ARG 143 ASN 144 GLN 145 GLN 146 ILE 147 PHE 148 LEU 149 ARG 150 ASP 151 ILE 152 GLU 153 GLN 154 VAL 155 PRO 156 GLN 157 GLN 158 PRO 159 THR 160 TYR 161 VAL 162 GLN 163 ALA 164 LEU 165 PHE 166 ASP 167 PHE 168 ASP 169 PRO 170 GLN 171 GLU 172 ASP 173 GLY 174 GLU 175 LEU 176 GLY 177 PHE 178 ARG 179 ARG 180 GLY 181 ASP 182 PHE 183 ILE 184 HIS 185 VAL 186 MET 187 ASP 188 ASN 189 SER 190 ASP 191 PRO 192 ASN 193 TRP 194 TRP 195 LYS 196 GLY 197 ALA 198 ALA 199 HIS 200 GLY 201 GLN 202 THR 203 GLY 204 MET 205 PHE 206 PRO 207 ARG 208 ASN 209 TYR 210 VAL 211 THR 212 PRO 213 VAL 214 ASN 215 ARG 216 ASN 217 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_EGFR-peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'EGF Receptor phosphorylated peptide' _Abbreviation_common EGFR-peptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 7 _Mol_residue_sequence EXINSQV loop_ _Residue_seq_code _Residue_label 1 GLU 2 PTR 3 ILE 4 ASN 5 SER 6 GLN 7 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Sos-peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sos peptide' _Abbreviation_common Sos-peptide _Molecular_mass 1170 _Mol_thiol_state 'not present' _Details . _Residue_count 10 _Mol_residue_sequence VPPPVPPRRR loop_ _Residue_seq_code _Residue_label 1 VAL 2 PRO 3 PRO 4 PRO 5 VAL 6 PRO 7 PRO 8 ARG 9 ARG 10 ARG stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2003-08-21 save_ ###################### # Polymer residues # ###################### save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code PTR _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CG CG C . 0 . ? CZ CZ C . 0 . ? H H 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 . ? HN2 HN2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? O O O . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? OH OH O . 0 . ? OXT OXT O . 0 . ? P P P . 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 HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $Grb2 Human 9606 Eukaryota Metazoa Homo sapiens cytoplasm $EGFR-peptide Human 9606 Eukaryota Metazoa Homo sapiens 'cell membrane' $Sos-peptide Human 9606 Eukaryota Metazoa Homo sapiens cytoplasm stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $Grb2 'recombinant technology' 'E. coli' . . BL21 DE3 plasmid pET3a $EGFR-peptide 'chemical synthesis' . . . . . . . $Sos-peptide 'chemical synthesis' . . . . . . . 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 $Grb2 1.2 mM '[U-80% 2H; U-98% 13C; U-98% 15N]' $EGFR-peptide 1.44 mM . $Sos-peptide 6.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'raw spectral data processing' stop_ _Details . _Citation_label $ref_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVAplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_NH(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name NH(COCA)CB _Sample_label $sample_1 save_ save_HN(CA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name NH(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.05 n/a temperature 298 0.1 K 'ionic strength' 0.03 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_label _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_label _Mol_system_component_name Grb2 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET C C 173.6 0.14 1 2 . 1 MET CA C 55.2 0.14 1 3 . 1 MET CB C 33.5 0.14 1 4 . 2 GLU H H 8.69 0.01 1 5 . 2 GLU C C 174.4 0.14 1 6 . 2 GLU CA C 55.5 0.14 1 7 . 2 GLU CB C 32.0 0.14 1 8 . 2 GLU N N 123.4 0.07 1 9 . 3 ALA H H 8.97 0.01 1 10 . 3 ALA C C 174.4 0.14 1 11 . 3 ALA CA C 50.0 0.14 1 12 . 3 ALA CB C 23.9 0.14 1 13 . 3 ALA N N 123.2 0.07 1 14 . 4 ILE H H 8.74 0.01 1 15 . 4 ILE C C 176.3 0.14 1 16 . 4 ILE CA C 58.4 0.14 1 17 . 4 ILE CB C 39.9 0.14 1 18 . 4 ILE N N 118.6 0.07 1 19 . 5 ALA H H 8.87 0.01 1 20 . 5 ALA C C 179.0 0.14 1 21 . 5 ALA CA C 52.4 0.14 1 22 . 5 ALA CB C 21.1 0.14 1 23 . 5 ALA N N 128.0 0.07 1 24 . 6 LYS H H 9.40 0.01 1 25 . 6 LYS C C 174.5 0.14 1 26 . 6 LYS CA C 56.6 0.14 1 27 . 6 LYS CB C 32.7 0.14 1 28 . 6 LYS N N 125.5 0.07 1 29 . 7 TYR H H 7.37 0.01 1 30 . 7 TYR C C 173.4 0.14 1 31 . 7 TYR CA C 53.9 0.14 1 32 . 7 TYR CB C 42.6 0.14 1 33 . 7 TYR N N 112.3 0.07 1 34 . 8 ASP H H 8.42 0.01 1 35 . 8 ASP C C 175.7 0.14 1 36 . 8 ASP CA C 54.3 0.14 1 37 . 8 ASP CB C 41.0 0.14 1 38 . 8 ASP N N 117.6 0.07 1 39 . 9 PHE H H 8.49 0.01 1 40 . 9 PHE C C 172.8 0.14 1 41 . 9 PHE CA C 56.8 0.14 1 42 . 9 PHE CB C 42.0 0.14 1 43 . 9 PHE N N 121.0 0.07 1 44 . 10 LYS H H 7.38 0.01 1 45 . 10 LYS C C 173.3 0.14 1 46 . 10 LYS CA C 53.0 0.14 1 47 . 10 LYS CB C 32.2 0.14 1 48 . 10 LYS N N 128.3 0.07 1 49 . 11 ALA H H 8.18 0.01 1 50 . 11 ALA C C 178.4 0.14 1 51 . 11 ALA CA C 52.8 0.14 1 52 . 11 ALA CB C 20.2 0.14 1 53 . 11 ALA N N 126.2 0.07 1 54 . 12 THR H H 9.05 0.01 1 55 . 12 THR C C 173.5 0.14 1 56 . 12 THR CA C 61.4 0.14 1 57 . 12 THR CB C 69.5 0.14 1 58 . 12 THR N N 113.3 0.07 1 59 . 13 ALA H H 7.52 0.01 1 60 . 13 ALA C C 178.4 0.14 1 61 . 13 ALA CA C 50.3 0.14 1 62 . 13 ALA CB C 21.9 0.14 1 63 . 13 ALA N N 123.1 0.07 1 64 . 14 ASP H H 8.74 0.01 1 65 . 14 ASP C C 175.9 0.14 1 66 . 14 ASP CA C 56.4 0.14 1 67 . 14 ASP CB C 39.9 0.14 1 68 . 14 ASP N N 118.6 0.07 1 69 . 15 ASP H H 8.22 0.01 1 70 . 15 ASP C C 176.2 0.14 1 71 . 15 ASP CA C 52.3 0.14 1 72 . 15 ASP CB C 39.0 0.14 1 73 . 15 ASP N N 114.9 0.07 1 74 . 16 GLU H H 7.59 0.01 1 75 . 16 GLU C C 175.1 0.14 1 76 . 16 GLU CA C 54.7 0.14 1 77 . 16 GLU CB C 31.8 0.14 1 78 . 16 GLU N N 119.6 0.07 1 79 . 17 LEU H H 8.29 0.01 1 80 . 17 LEU C C 174.4 0.14 1 81 . 17 LEU CA C 53.2 0.14 1 82 . 17 LEU CB C 44.3 0.14 1 83 . 17 LEU N N 124.2 0.07 1 84 . 18 SER H H 7.88 0.01 1 85 . 18 SER C C 173.9 0.14 1 86 . 18 SER CA C 58.5 0.14 1 87 . 18 SER CB C 64.0 0.14 1 88 . 18 SER N N 117.4 0.07 1 89 . 19 PHE H H 8.74 0.01 1 90 . 19 PHE C C 173.8 0.14 1 91 . 19 PHE CA C 56.4 0.14 1 92 . 19 PHE CB C 39.6 0.14 1 93 . 19 PHE N N 115.5 0.07 1 94 . 20 LYS H H 9.69 0.01 1 95 . 20 LYS C C 175.8 0.14 1 96 . 20 LYS CA C 53.2 0.14 1 97 . 20 LYS CB C 34.6 0.14 1 98 . 20 LYS N N 121.1 0.07 1 99 . 21 ARG H H 9.18 0.01 1 100 . 21 ARG C C 177.0 0.14 1 101 . 21 ARG CA C 58.0 0.14 1 102 . 21 ARG CB C 29.2 0.14 1 103 . 21 ARG N N 120.5 0.07 1 104 . 22 GLY H H 8.95 0.01 1 105 . 22 GLY C C 174.0 0.14 1 106 . 22 GLY CA C 44.5 0.14 1 107 . 22 GLY N N 115.0 0.07 1 108 . 23 ASP H H 8.56 0.01 1 109 . 23 ASP C C 174.8 0.14 1 110 . 23 ASP CA C 55.6 0.14 1 111 . 23 ASP CB C 41.0 0.14 1 112 . 23 ASP N N 121.8 0.07 1 113 . 24 ILE H H 8.21 0.01 1 114 . 24 ILE C C 175.7 0.14 1 115 . 24 ILE CA C 59.3 0.14 1 116 . 24 ILE CB C 36.6 0.14 1 117 . 24 ILE N N 119.4 0.07 1 118 . 25 LEU H H 9.03 0.01 1 119 . 25 LEU C C 175.3 0.14 1 120 . 25 LEU CA C 53.1 0.14 1 121 . 25 LEU CB C 43.6 0.14 1 122 . 25 LEU N N 127.7 0.07 1 123 . 26 LYS H H 8.19 0.01 1 124 . 26 LYS C C 175.8 0.14 1 125 . 26 LYS CA C 55.0 0.14 1 126 . 26 LYS CB C 32.2 0.14 1 127 . 26 LYS N N 121.3 0.07 1 128 . 27 VAL H H 8.61 0.01 1 129 . 27 VAL C C 175.8 0.14 1 130 . 27 VAL CA C 62.7 0.14 1 131 . 27 VAL CB C 31.7 0.14 1 132 . 27 VAL N N 125.1 0.07 1 133 . 28 LEU H H 8.93 0.01 1 134 . 28 LEU C C 177.1 0.14 1 135 . 28 LEU CA C 54.6 0.14 1 136 . 28 LEU CB C 41.5 0.14 1 137 . 28 LEU N N 127.9 0.07 1 138 . 29 ASN H H 8.18 0.01 1 139 . 29 ASN C C 174.3 0.14 1 140 . 29 ASN CA C 53.1 0.14 1 141 . 29 ASN CB C 38.8 0.14 1 142 . 29 ASN N N 117.1 0.07 1 143 . 30 GLU C C 175.8 0.14 1 144 . 30 GLU CA C 55.9 0.14 1 145 . 30 GLU CB C 30.6 0.14 1 146 . 31 GLU H H 8.51 0.01 1 147 . 31 GLU C C 176.4 0.14 1 148 . 31 GLU CA C 56.2 0.14 1 149 . 31 GLU CB C 29.7 0.14 1 150 . 31 GLU N N 121.8 0.07 1 151 . 32 SER H H 8.46 0.01 1 152 . 32 SER C C 174.2 0.14 1 153 . 32 SER CA C 59.0 0.14 1 154 . 32 SER CB C 64.0 0.14 1 155 . 32 SER N N 116.2 0.07 1 156 . 33 ASP H H 8.40 0.01 1 157 . 33 ASP C C 175.9 0.14 1 158 . 33 ASP CA C 53.7 0.14 1 159 . 33 ASP CB C 41.8 0.14 1 160 . 33 ASP N N 121.0 0.07 1 161 . 34 GLN H H 8.43 0.01 1 162 . 34 GLN C C 176.2 0.14 1 163 . 34 GLN CA C 56.8 0.14 1 164 . 34 GLN CB C 28.8 0.14 1 165 . 34 GLN N N 119.2 0.07 1 166 . 35 ASN H H 9.08 0.01 1 167 . 35 ASN C C 173.6 0.14 1 168 . 35 ASN CA C 53.8 0.14 1 169 . 35 ASN CB C 39.8 0.14 1 170 . 35 ASN N N 114.7 0.07 1 171 . 36 TRP H H 7.91 0.01 1 172 . 36 TRP C C 175.2 0.14 1 173 . 36 TRP CA C 56.3 0.14 1 174 . 36 TRP CB C 31.6 0.14 1 175 . 36 TRP N N 119.5 0.07 1 176 . 37 TYR H H 9.23 0.01 1 177 . 37 TYR C C 176.1 0.14 1 178 . 37 TYR CA C 54.6 0.14 1 179 . 37 TYR CB C 41.2 0.14 1 180 . 37 TYR N N 118.8 0.07 1 181 . 38 LYS H H 9.28 0.01 1 182 . 38 LYS C C 174.8 0.14 1 183 . 38 LYS CA C 55.9 0.14 1 184 . 38 LYS CB C 32.2 0.14 1 185 . 38 LYS N N 122.3 0.07 1 186 . 39 ALA H H 9.17 0.01 1 187 . 39 ALA C C 174.0 0.14 1 188 . 39 ALA CA C 50.2 0.14 1 189 . 39 ALA CB C 25.0 0.14 1 190 . 39 ALA N N 128.9 0.07 1 191 . 40 GLU H H 8.81 0.01 1 192 . 40 GLU C C 175.2 0.14 1 193 . 40 GLU CA C 53.9 0.14 1 194 . 40 GLU CB C 33.5 0.14 1 195 . 40 GLU N N 116.6 0.07 1 196 . 41 LEU H H 8.93 0.01 1 197 . 41 LEU C C 175.9 0.14 1 198 . 41 LEU CA C 54.9 0.14 1 199 . 41 LEU CB C 44.9 0.14 1 200 . 41 LEU N N 124.9 0.07 1 201 . 42 ASN H H 9.60 0.01 1 202 . 42 ASN C C 175.8 0.14 1 203 . 42 ASN CA C 55.0 0.14 1 204 . 42 ASN CB C 39.4 0.14 1 205 . 42 ASN N N 128.8 0.07 1 206 . 43 GLY H H 9.00 0.01 1 207 . 43 GLY C C 173.7 0.14 1 208 . 43 GLY CA C 45.2 0.14 1 209 . 43 GLY N N 104.1 0.07 1 210 . 44 LYS H H 7.84 0.01 1 211 . 44 LYS C C 173.8 0.14 1 212 . 44 LYS CA C 54.3 0.14 1 213 . 44 LYS CB C 34.1 0.14 1 214 . 44 LYS N N 121.6 0.07 1 215 . 45 ASP H H 8.34 0.01 1 216 . 45 ASP C C 175.9 0.14 1 217 . 45 ASP CA C 51.6 0.14 1 218 . 45 ASP CB C 43.9 0.14 1 219 . 45 ASP N N 118.6 0.07 1 220 . 46 GLY H H 8.64 0.01 1 221 . 46 GLY C C 171.3 0.14 1 222 . 46 GLY CA C 44.8 0.14 1 223 . 46 GLY N N 103.9 0.07 1 224 . 47 PHE H H 9.42 0.01 1 225 . 47 PHE C C 176.9 0.14 1 226 . 47 PHE CA C 58.7 0.14 1 227 . 47 PHE CB C 40.5 0.14 1 228 . 47 PHE N N 118.9 0.07 1 229 . 48 ILE H H 9.78 0.01 1 230 . 48 ILE C C 172.6 0.14 1 231 . 48 ILE CA C 57.0 0.14 1 232 . 48 ILE CB C 40.1 0.14 1 233 . 48 ILE N N 113.2 0.07 1 234 . 49 PRO C C 178.6 0.14 1 235 . 49 PRO CA C 60.9 0.14 1 236 . 49 PRO CB C 29.5 0.14 1 237 . 50 LYS H H 8.13 0.01 1 238 . 50 LYS C C 176.5 0.14 1 239 . 50 LYS CA C 58.8 0.14 1 240 . 50 LYS CB C 32.0 0.14 1 241 . 50 LYS N N 121.7 0.07 1 242 . 51 ASN H H 8.49 0.01 1 243 . 51 ASN C C 175.3 0.14 1 244 . 51 ASN CA C 53.3 0.14 1 245 . 51 ASN CB C 35.0 0.14 1 246 . 51 ASN N N 111.4 0.07 1 247 . 52 TYR H H 7.78 0.01 1 248 . 52 TYR C C 175.1 0.14 1 249 . 52 TYR CA C 58.4 0.14 1 250 . 52 TYR CB C 39.2 0.14 1 251 . 52 TYR N N 119.3 0.07 1 252 . 53 ILE H H 7.38 0.01 1 253 . 53 ILE C C 173.8 0.14 1 254 . 53 ILE CA C 58.3 0.14 1 255 . 53 ILE CB C 41.1 0.14 1 256 . 53 ILE N N 111.0 0.07 1 257 . 54 GLU H H 8.82 0.01 1 258 . 54 GLU C C 175.6 0.14 1 259 . 54 GLU CA C 54.1 0.14 1 260 . 54 GLU CB C 32.0 0.14 1 261 . 54 GLU N N 120.2 0.07 1 262 . 55 MET H H 8.93 0.01 1 263 . 55 MET C C 176.4 0.14 1 264 . 55 MET CA C 54.9 0.14 1 265 . 55 MET CB C 31.6 0.14 1 266 . 55 MET N N 124.9 0.07 1 267 . 56 LYS H H 8.61 0.01 1 268 . 56 LYS C C 174.1 0.14 1 269 . 56 LYS N N 124.4 0.07 1 270 . 61 PHE C C 174.9 0.14 1 271 . 61 PHE CA C 57.7 0.14 1 272 . 61 PHE CB C 37.2 0.14 1 273 . 62 PHE H H 8.78 0.01 1 274 . 62 PHE C C 175.2 0.14 1 275 . 62 PHE CA C 57.2 0.14 1 276 . 62 PHE CB C 39.9 0.14 1 277 . 62 PHE N N 126.9 0.07 1 278 . 63 GLY H H 5.51 0.01 1 279 . 63 GLY C C 174.5 0.14 1 280 . 63 GLY CA C 46.9 0.14 1 281 . 63 GLY N N 103.5 0.07 1 282 . 64 LYS H H 8.81 0.01 1 283 . 64 LYS C C 175.4 0.14 1 284 . 64 LYS CA C 55.9 0.14 1 285 . 64 LYS CB C 30.4 0.14 1 286 . 64 LYS N N 127.4 0.07 1 287 . 65 ILE H H 7.42 0.01 1 288 . 65 ILE C C 173.1 0.14 1 289 . 65 ILE CA C 57.2 0.14 1 290 . 65 ILE CB C 39.0 0.14 1 291 . 65 ILE N N 121.5 0.07 1 292 . 66 PRO C C 176.9 0.14 1 293 . 66 PRO CA C 62.1 0.14 1 294 . 66 PRO CB C 32.8 0.14 1 295 . 67 ARG H H 9.13 0.01 1 296 . 67 ARG C C 178.4 0.14 1 297 . 67 ARG CA C 60.3 0.14 1 298 . 67 ARG CB C 30.0 0.14 1 299 . 67 ARG N N 125.7 0.07 1 300 . 68 ALA H H 9.28 0.01 1 301 . 68 ALA C C 180.9 0.14 1 302 . 68 ALA CA C 54.6 0.14 1 303 . 68 ALA CB C 17.7 0.14 1 304 . 68 ALA N N 117.8 0.07 1 305 . 69 LYS H H 6.96 0.01 1 306 . 69 LYS C C 178.6 0.14 1 307 . 69 LYS CA C 56.8 0.14 1 308 . 69 LYS CB C 30.6 0.14 1 309 . 69 LYS N N 117.3 0.07 1 310 . 70 ALA H H 8.13 0.01 1 311 . 70 ALA C C 179.2 0.14 1 312 . 70 ALA CA C 54.6 0.14 1 313 . 70 ALA CB C 17.5 0.14 1 314 . 70 ALA N N 122.1 0.07 1 315 . 71 GLU H H 8.30 0.01 1 316 . 71 GLU C C 178.5 0.14 1 317 . 71 GLU CA C 59.7 0.14 1 318 . 71 GLU CB C 27.9 0.14 1 319 . 71 GLU N N 115.0 0.07 1 320 . 72 GLU H H 7.92 0.01 1 321 . 72 GLU C C 179.2 0.14 1 322 . 72 GLU CA C 59.2 0.14 1 323 . 72 GLU CB C 29.1 0.14 1 324 . 72 GLU N N 120.7 0.07 1 325 . 73 MET H H 8.17 0.01 1 326 . 73 MET C C 179.8 0.14 1 327 . 73 MET CA C 58.6 0.14 1 328 . 73 MET CB C 32.9 0.14 1 329 . 73 MET N N 116.7 0.07 1 330 . 74 LEU H H 8.31 0.01 1 331 . 74 LEU C C 179.1 0.14 1 332 . 74 LEU CA C 56.9 0.14 1 333 . 74 LEU CB C 41.1 0.14 1 334 . 74 LEU N N 117.7 0.07 1 335 . 75 SER H H 8.33 0.01 1 336 . 75 SER C C 175.3 0.14 1 337 . 75 SER CA C 61.1 0.14 1 338 . 75 SER CB C 62.6 0.14 1 339 . 75 SER N N 114.0 0.07 1 340 . 76 LYS H H 6.88 0.01 1 341 . 76 LYS C C 177.6 0.14 1 342 . 76 LYS CA C 55.6 0.14 1 343 . 76 LYS CB C 32.2 0.14 1 344 . 76 LYS N N 117.0 0.07 1 345 . 77 GLN H H 7.43 0.01 1 346 . 77 GLN C C 175.9 0.14 1 347 . 77 GLN CA C 54.5 0.14 1 348 . 77 GLN CB C 28.0 0.14 1 349 . 77 GLN N N 117.7 0.07 1 350 . 78 ARG H H 8.74 0.01 1 351 . 78 ARG C C 177.0 0.14 1 352 . 78 ARG CA C 56.6 0.14 1 353 . 78 ARG CB C 30.1 0.14 1 354 . 78 ARG N N 118.1 0.07 1 355 . 79 HIS H H 7.83 0.01 1 356 . 79 HIS C C 174.4 0.14 1 357 . 79 HIS CA C 54.7 0.14 1 358 . 79 HIS CB C 31.7 0.14 1 359 . 79 HIS N N 116.5 0.07 1 360 . 80 ASP H H 8.68 0.01 1 361 . 80 ASP C C 177.8 0.14 1 362 . 80 ASP CA C 55.4 0.14 1 363 . 80 ASP CB C 40.4 0.14 1 364 . 80 ASP N N 122.4 0.07 1 365 . 81 GLY H H 9.54 0.01 1 366 . 81 GLY C C 174.6 0.14 1 367 . 81 GLY CA C 45.0 0.14 1 368 . 81 GLY N N 111.3 0.07 1 369 . 82 ALA H H 7.59 0.01 1 370 . 82 ALA C C 177.5 0.14 1 371 . 82 ALA CA C 52.8 0.14 1 372 . 82 ALA CB C 17.7 0.14 1 373 . 82 ALA N N 124.5 0.07 1 374 . 83 PHE H H 7.43 0.01 1 375 . 83 PHE C C 171.4 0.14 1 376 . 83 PHE CA C 55.2 0.14 1 377 . 83 PHE CB C 43.6 0.14 1 378 . 83 PHE N N 118.3 0.07 1 379 . 84 LEU H H 8.87 0.01 1 380 . 84 LEU C C 175.6 0.14 1 381 . 84 LEU CA C 54.1 0.14 1 382 . 84 LEU CB C 44.6 0.14 1 383 . 84 LEU N N 111.7 0.07 1 384 . 85 ILE H H 9.44 0.01 1 385 . 85 ILE C C 173.1 0.14 1 386 . 85 ILE CA C 59.6 0.14 1 387 . 85 ILE CB C 38.5 0.14 1 388 . 85 ILE N N 119.4 0.07 1 389 . 86 ARG H H 9.31 0.01 1 390 . 86 ARG C C 174.9 0.14 1 391 . 86 ARG CA C 51.6 0.14 1 392 . 86 ARG CB C 33.2 0.14 1 393 . 86 ARG N N 122.9 0.07 1 394 . 87 GLU H H 8.64 0.01 1 395 . 87 GLU C C 176.2 0.14 1 396 . 87 GLU CA C 56.2 0.14 1 397 . 87 GLU CB C 29.5 0.14 1 398 . 87 GLU N N 122.7 0.07 1 399 . 88 SER H H 8.67 0.01 1 400 . 88 SER C C 175.5 0.14 1 401 . 88 SER CA C 57.8 0.14 1 402 . 88 SER CB C 62.9 0.14 1 403 . 88 SER N N 120.5 0.07 1 404 . 89 GLU H H 9.16 0.01 1 405 . 89 GLU C C 177.8 0.14 1 406 . 89 GLU CA C 57.8 0.14 1 407 . 89 GLU CB C 30.0 0.14 1 408 . 89 GLU N N 127.6 0.07 1 409 . 90 SER H H 8.44 0.01 1 410 . 90 SER C C 174.8 0.14 1 411 . 90 SER CA C 59.2 0.14 1 412 . 90 SER CB C 63.0 0.14 1 413 . 90 SER N N 113.5 0.07 1 414 . 91 ALA H H 7.62 0.01 1 415 . 91 ALA C C 171.7 0.14 1 416 . 91 ALA CA C 48.8 0.14 1 417 . 91 ALA CB C 18.6 0.14 1 418 . 91 ALA N N 126.5 0.07 1 419 . 92 PRO C C 178.3 0.14 1 420 . 92 PRO CA C 63.6 0.14 1 421 . 92 PRO CB C 30.7 0.14 1 422 . 93 GLY H H 9.14 0.01 1 423 . 93 GLY C C 173.3 0.14 1 424 . 93 GLY CA C 44.7 0.14 1 425 . 93 GLY N N 113.7 0.07 1 426 . 94 ASP H H 8.07 0.01 1 427 . 94 ASP C C 175.3 0.14 1 428 . 94 ASP CA C 52.6 0.14 1 429 . 94 ASP CB C 42.0 0.14 1 430 . 94 ASP N N 120.5 0.07 1 431 . 95 PHE H H 9.31 0.01 1 432 . 95 PHE C C 174.8 0.14 1 433 . 95 PHE CA C 56.7 0.14 1 434 . 95 PHE CB C 41.5 0.14 1 435 . 95 PHE N N 118.5 0.07 1 436 . 96 SER H H 9.61 0.01 1 437 . 96 SER C C 170.8 0.14 1 438 . 96 SER CA C 56.8 0.14 1 439 . 96 SER CB C 65.3 0.14 1 440 . 96 SER N N 115.6 0.07 1 441 . 97 LEU H H 9.72 0.01 1 442 . 97 LEU C C 175.2 0.14 1 443 . 97 LEU CA C 53.6 0.14 1 444 . 97 LEU CB C 44.6 0.14 1 445 . 97 LEU N N 127.5 0.07 1 446 . 98 SER H H 9.31 0.01 1 447 . 98 SER C C 172.2 0.14 1 448 . 98 SER CA C 58.3 0.14 1 449 . 98 SER CB C 65.6 0.14 1 450 . 98 SER N N 124.6 0.07 1 451 . 99 VAL H H 9.34 0.01 1 452 . 99 VAL C C 173.4 0.14 1 453 . 99 VAL CA C 59.2 0.14 1 454 . 99 VAL CB C 35.6 0.14 1 455 . 99 VAL N N 122.0 0.07 1 456 . 100 LYS H H 9.30 0.01 1 457 . 100 LYS C C 175.7 0.14 1 458 . 100 LYS CA C 56.2 0.14 1 459 . 100 LYS CB C 34.1 0.14 1 460 . 100 LYS N N 128.7 0.07 1 461 . 101 PHE H H 8.75 0.01 1 462 . 101 PHE C C 174.9 0.14 1 463 . 101 PHE CA C 58.8 0.14 1 464 . 101 PHE CB C 40.4 0.14 1 465 . 101 PHE N N 128.0 0.07 1 466 . 102 GLY H H 9.45 0.01 1 467 . 102 GLY C C 174.7 0.14 1 468 . 102 GLY CA C 46.2 0.14 1 469 . 102 GLY N N 120.7 0.07 1 470 . 103 ASN H H 8.84 0.01 1 471 . 103 ASN C C 174.1 0.14 1 472 . 103 ASN CA C 52.7 0.14 1 473 . 103 ASN CB C 38.1 0.14 1 474 . 103 ASN N N 123.7 0.07 1 475 . 104 ASP H H 8.00 0.01 1 476 . 104 ASP C C 174.6 0.14 1 477 . 104 ASP CA C 52.8 0.14 1 478 . 104 ASP CB C 44.3 0.14 1 479 . 104 ASP N N 118.9 0.07 1 480 . 105 VAL H H 8.36 0.01 1 481 . 105 VAL C C 174.6 0.14 1 482 . 105 VAL CA C 61.2 0.14 1 483 . 105 VAL CB C 33.0 0.14 1 484 . 105 VAL N N 120.0 0.07 1 485 . 106 GLN H H 9.13 0.01 1 486 . 106 GLN C C 174.5 0.14 1 487 . 106 GLN CA C 54.2 0.14 1 488 . 106 GLN CB C 30.0 0.14 1 489 . 106 GLN N N 125.5 0.07 1 490 . 107 HIS H H 8.63 0.01 1 491 . 107 HIS C C 174.1 0.14 1 492 . 107 HIS CA C 54.3 0.14 1 493 . 107 HIS CB C 33.5 0.14 1 494 . 107 HIS N N 118.5 0.07 1 495 . 108 PHE H H 10.38 0.01 1 496 . 108 PHE C C 175.1 0.14 1 497 . 108 PHE CA C 55.8 0.14 1 498 . 108 PHE CB C 41.5 0.14 1 499 . 108 PHE N N 121.3 0.07 1 500 . 109 LYS H H 9.75 0.01 1 501 . 109 LYS C C 175.7 0.14 1 502 . 109 LYS CA C 54.9 0.14 1 503 . 109 LYS CB C 30.8 0.14 1 504 . 109 LYS N N 125.9 0.07 1 505 . 110 VAL H H 8.36 0.01 1 506 . 110 VAL C C 174.9 0.14 1 507 . 110 VAL CA C 62.5 0.14 1 508 . 110 VAL CB C 29.0 0.14 1 509 . 110 VAL N N 124.6 0.07 1 510 . 111 LEU H H 8.41 0.01 1 511 . 111 LEU C C 175.0 0.14 1 512 . 111 LEU CA C 54.0 0.14 1 513 . 111 LEU CB C 40.0 0.14 1 514 . 111 LEU N N 132.1 0.07 1 515 . 112 ARG H H 7.86 0.01 1 516 . 112 ARG C C 177.8 0.14 1 517 . 112 ARG CA C 52.2 0.14 1 518 . 112 ARG CB C 31.8 0.14 1 519 . 112 ARG N N 115.2 0.07 1 520 . 113 ASP H H 8.05 0.01 1 521 . 113 ASP CA C 51.3 0.14 1 522 . 113 ASP CB C 41.7 0.14 1 523 . 113 ASP N N 121.2 0.07 1 524 . 114 GLY C C 174.5 0.14 1 525 . 114 GLY CA C 46.1 0.14 1 526 . 115 ALA H H 7.98 0.01 1 527 . 115 ALA C C 177.5 0.14 1 528 . 115 ALA CA C 50.9 0.14 1 529 . 115 ALA CB C 18.6 0.14 1 530 . 115 ALA N N 122.2 0.07 1 531 . 116 GLY H H 8.13 0.01 1 532 . 116 GLY C C 175.6 0.14 1 533 . 116 GLY CA C 44.8 0.14 1 534 . 116 GLY N N 107.3 0.07 1 535 . 117 LYS H H 8.72 0.01 1 536 . 117 LYS C C 175.6 0.14 1 537 . 117 LYS CA C 55.7 0.14 1 538 . 117 LYS CB C 31.7 0.14 1 539 . 117 LYS N N 121.3 0.07 1 540 . 118 TYR H H 8.97 0.01 1 541 . 118 TYR C C 176.8 0.14 1 542 . 118 TYR CA C 56.4 0.14 1 543 . 118 TYR CB C 41.1 0.14 1 544 . 118 TYR N N 117.7 0.07 1 545 . 119 PHE H H 9.24 0.01 1 546 . 119 PHE C C 171.7 0.14 1 547 . 119 PHE CA C 57.0 0.14 1 548 . 119 PHE CB C 41.1 0.14 1 549 . 119 PHE N N 116.1 0.07 1 550 . 121 TRP C C 174.5 0.14 1 551 . 122 VAL H H 8.64 0.01 1 552 . 122 VAL C C 174.5 0.14 1 553 . 122 VAL CA C 63.4 0.14 1 554 . 122 VAL CB C 34.3 0.14 1 555 . 122 VAL N N 118.4 0.07 1 556 . 123 VAL H H 8.30 0.01 1 557 . 123 VAL C C 174.4 0.14 1 558 . 123 VAL CA C 63.4 0.14 1 559 . 123 VAL CB C 31.1 0.14 1 560 . 123 VAL N N 121.7 0.07 1 561 . 124 LYS H H 7.74 0.01 1 562 . 124 LYS C C 176.2 0.14 1 563 . 124 LYS CA C 54.0 0.14 1 564 . 124 LYS CB C 34.6 0.14 1 565 . 124 LYS N N 121.6 0.07 1 566 . 125 PHE H H 9.35 0.01 1 567 . 125 PHE C C 176.2 0.14 1 568 . 125 PHE CA C 56.2 0.14 1 569 . 125 PHE CB C 42.7 0.14 1 570 . 125 PHE N N 117.5 0.07 1 571 . 126 ASN H H 9.51 0.01 1 572 . 126 ASN C C 175.0 0.14 1 573 . 126 ASN CA C 54.5 0.14 1 574 . 126 ASN CB C 38.9 0.14 1 575 . 126 ASN N N 118.0 0.07 1 576 . 127 SER H H 7.61 0.01 1 577 . 127 SER C C 173.8 0.14 1 578 . 127 SER CA C 56.4 0.14 1 579 . 127 SER CB C 66.3 0.14 1 580 . 127 SER N N 109.0 0.07 1 581 . 128 LEU H H 8.75 0.01 1 582 . 128 LEU C C 178.0 0.14 1 583 . 128 LEU CA C 56.5 0.14 1 584 . 128 LEU CB C 40.9 0.14 1 585 . 128 LEU N N 120.4 0.07 1 586 . 129 ASN H H 8.40 0.01 1 587 . 129 ASN C C 176.8 0.14 1 588 . 129 ASN CA C 56.5 0.14 1 589 . 129 ASN CB C 37.8 0.14 1 590 . 129 ASN N N 114.6 0.07 1 591 . 130 GLU H H 7.73 0.01 1 592 . 130 GLU C C 178.0 0.14 1 593 . 130 GLU CA C 58.8 0.14 1 594 . 130 GLU CB C 30.5 0.14 1 595 . 130 GLU N N 117.7 0.07 1 596 . 131 LEU H H 6.92 0.01 1 597 . 131 LEU N N 122.4 0.07 1 598 . 132 VAL C C 177.0 0.14 1 599 . 132 VAL CA C 65.9 0.14 1 600 . 132 VAL CB C 30.7 0.14 1 601 . 133 ASP H H 7.86 0.01 1 602 . 133 ASP C C 180.2 0.14 1 603 . 133 ASP CA C 57.2 0.14 1 604 . 133 ASP CB C 39.5 0.14 1 605 . 133 ASP N N 115.5 0.07 1 606 . 134 TYR H H 7.97 0.01 1 607 . 134 TYR C C 178.9 0.14 1 608 . 134 TYR CA C 61.0 0.14 1 609 . 134 TYR N N 121.0 0.07 1 610 . 135 HIS C C 174.1 0.14 1 611 . 135 HIS CA C 57.6 0.14 1 612 . 135 HIS CB C 30.7 0.14 1 613 . 136 ARG H H 7.47 0.01 1 614 . 136 ARG C C 178.4 0.14 1 615 . 136 ARG CA C 57.6 0.14 1 616 . 136 ARG CB C 29.4 0.14 1 617 . 136 ARG N N 116.1 0.07 1 618 . 137 SER H H 7.21 0.01 1 619 . 137 SER C C 172.7 0.14 1 620 . 137 SER CA C 57.6 0.14 1 621 . 137 SER CB C 64.2 0.14 1 622 . 137 SER N N 107.1 0.07 1 623 . 138 THR H H 7.33 0.01 1 624 . 138 THR CA C 62.6 0.14 1 625 . 138 THR CB C 69.8 0.14 1 626 . 138 THR N N 119.9 0.07 1 627 . 139 SER C C 176.8 0.14 1 628 . 139 SER CA C 57.1 0.14 1 629 . 139 SER CB C 63.5 0.14 1 630 . 140 VAL H H 8.39 0.01 1 631 . 140 VAL C C 173.6 0.14 1 632 . 140 VAL CA C 62.3 0.14 1 633 . 140 VAL CB C 31.1 0.14 1 634 . 140 VAL N N 120.1 0.07 1 635 . 141 SER H H 8.77 0.01 1 636 . 141 SER C C 174.8 0.14 1 637 . 141 SER CA C 54.7 0.14 1 638 . 141 SER CB C 63.9 0.14 1 639 . 141 SER N N 110.8 0.07 1 640 . 142 ARG H H 8.72 0.01 1 641 . 142 ARG C C 176.5 0.14 1 642 . 142 ARG CA C 56.9 0.14 1 643 . 142 ARG CB C 29.5 0.14 1 644 . 142 ARG N N 124.1 0.07 1 645 . 143 ASN H H 8.16 0.01 1 646 . 143 ASN C C 174.2 0.14 1 647 . 143 ASN CA C 53.1 0.14 1 648 . 143 ASN CB C 39.5 0.14 1 649 . 143 ASN N N 114.9 0.07 1 650 . 144 GLN H H 7.64 0.01 1 651 . 144 GLN C C 174.2 0.14 1 652 . 144 GLN CA C 53.6 0.14 1 653 . 144 GLN CB C 31.6 0.14 1 654 . 144 GLN N N 117.6 0.07 1 655 . 145 GLN C C 172.9 0.14 1 656 . 145 GLN CA C 54.4 0.14 1 657 . 145 GLN CB C 27.7 0.14 1 658 . 146 ILE H H 8.02 0.01 1 659 . 146 ILE C C 172.8 0.14 1 660 . 146 ILE CA C 60.3 0.14 1 661 . 146 ILE CB C 39.2 0.14 1 662 . 146 ILE N N 124.1 0.07 1 663 . 147 PHE H H 8.53 0.01 1 664 . 147 PHE C C 175.5 0.14 1 665 . 147 PHE CA C 54.3 0.14 1 666 . 147 PHE CB C 39.5 0.14 1 667 . 147 PHE N N 125.9 0.07 1 668 . 148 LEU H H 8.23 0.01 1 669 . 148 LEU C C 177.4 0.14 1 670 . 148 LEU CA C 55.0 0.14 1 671 . 148 LEU CB C 38.4 0.14 1 672 . 148 LEU N N 118.9 0.07 1 673 . 149 ARG H H 8.36 0.01 1 674 . 149 ARG C C 173.9 0.14 1 675 . 149 ARG CA C 53.9 0.14 1 676 . 149 ARG CB C 33.2 0.14 1 677 . 149 ARG N N 123.0 0.07 1 678 . 150 ASP H H 8.70 0.01 1 679 . 150 ASP C C 178.4 0.14 1 680 . 150 ASP CA C 54.9 0.14 1 681 . 150 ASP CB C 40.0 0.14 1 682 . 150 ASP N N 121.8 0.07 1 683 . 151 ILE C C 176.1 0.14 1 684 . 151 ILE CA C 62.7 0.14 1 685 . 151 ILE CB C 38.6 0.14 1 686 . 152 GLU H H 8.93 0.01 1 687 . 152 GLU C C 176.4 0.14 1 688 . 152 GLU CA C 54.9 0.14 1 689 . 152 GLU CB C 31.1 0.14 1 690 . 152 GLU N N 124.7 0.07 1 691 . 153 GLN H H 8.80 0.01 1 692 . 153 GLN C C 175.8 0.14 1 693 . 153 GLN CA C 55.5 0.14 1 694 . 153 GLN CB C 28.6 0.14 1 695 . 153 GLN N N 123.3 0.07 1 696 . 154 VAL H H 8.36 0.01 1 697 . 154 VAL C C 174.5 0.14 1 698 . 154 VAL CA C 59.4 0.14 1 699 . 154 VAL CB C 31.9 0.14 1 700 . 154 VAL N N 123.0 0.07 1 701 . 155 PRO C C 176.8 0.14 1 702 . 155 PRO CA C 62.7 0.14 1 703 . 155 PRO CB C 31.4 0.14 1 704 . 156 GLN H H 8.52 0.01 1 705 . 156 GLN C C 175.9 0.14 1 706 . 156 GLN CA C 55.3 0.14 1 707 . 156 GLN CB C 29.0 0.14 1 708 . 156 GLN N N 120.5 0.07 1 709 . 157 GLN H H 8.48 0.01 1 710 . 157 GLN C C 173.9 0.14 1 711 . 157 GLN CA C 53.2 0.14 1 712 . 157 GLN CB C 28.4 0.14 1 713 . 157 GLN N N 122.4 0.07 1 714 . 158 PRO C C 176.1 0.14 1 715 . 158 PRO CA C 62.6 0.14 1 716 . 158 PRO CB C 31.3 0.14 1 717 . 159 THR H H 8.61 0.01 1 718 . 159 THR C C 173.4 0.14 1 719 . 159 THR CA C 62.1 0.14 1 720 . 159 THR CB C 69.6 0.14 1 721 . 159 THR N N 116.2 0.07 1 722 . 160 TYR H H 8.81 0.01 1 723 . 160 TYR C C 175.8 0.14 1 724 . 160 TYR CA C 56.8 0.14 1 725 . 160 TYR CB C 41.7 0.14 1 726 . 160 TYR N N 122.5 0.07 1 727 . 161 VAL H H 8.88 0.01 1 728 . 161 VAL C C 173.3 0.14 1 729 . 161 VAL CA C 58.1 0.14 1 730 . 161 VAL CB C 35.0 0.14 1 731 . 161 VAL N N 111.9 0.07 1 732 . 162 GLN H H 9.20 0.01 1 733 . 162 GLN C C 175.4 0.14 1 734 . 162 GLN CA C 52.7 0.14 1 735 . 162 GLN CB C 30.9 0.14 1 736 . 162 GLN N N 120.4 0.07 1 737 . 163 ALA H H 8.79 0.01 1 738 . 163 ALA C C 179.0 0.14 1 739 . 163 ALA CA C 52.4 0.14 1 740 . 163 ALA CB C 20.6 0.14 1 741 . 163 ALA N N 126.9 0.07 1 742 . 164 LEU H H 9.54 0.01 1 743 . 164 LEU C C 175.0 0.14 1 744 . 164 LEU CA C 54.9 0.14 1 745 . 164 LEU CB C 43.2 0.14 1 746 . 164 LEU N N 126.1 0.07 1 747 . 165 PHE H H 7.29 0.01 1 748 . 165 PHE C C 173.5 0.14 1 749 . 165 PHE CA C 54.3 0.14 1 750 . 165 PHE CB C 43.5 0.14 1 751 . 165 PHE N N 112.6 0.07 1 752 . 166 ASP H H 8.53 0.01 1 753 . 166 ASP C C 175.6 0.14 1 754 . 166 ASP CA C 54.5 0.14 1 755 . 166 ASP CB C 40.9 0.14 1 756 . 166 ASP N N 118.1 0.07 1 757 . 167 PHE H H 8.41 0.01 1 758 . 167 PHE C C 172.8 0.14 1 759 . 167 PHE CA C 56.7 0.14 1 760 . 167 PHE CB C 41.8 0.14 1 761 . 167 PHE N N 121.3 0.07 1 762 . 168 ASP H H 7.70 0.01 1 763 . 168 ASP C C 172.3 0.14 1 764 . 168 ASP CA C 49.7 0.14 1 765 . 168 ASP CB C 41.1 0.14 1 766 . 168 ASP N N 127.7 0.07 1 767 . 169 PRO C C 176.8 0.14 1 768 . 169 PRO CA C 62.2 0.14 1 769 . 169 PRO CB C 32.7 0.14 1 770 . 170 GLN H H 8.93 0.01 1 771 . 170 GLN C C 175.4 0.14 1 772 . 170 GLN CA C 55.3 0.14 1 773 . 170 GLN CB C 30.7 0.14 1 774 . 170 GLN N N 119.7 0.07 1 775 . 171 GLU H H 7.43 0.01 1 776 . 171 GLU C C 176.1 0.14 1 777 . 171 GLU CA C 53.5 0.14 1 778 . 171 GLU CB C 31.7 0.14 1 779 . 171 GLU N N 116.4 0.07 1 780 . 172 ASP H H 8.69 0.01 1 781 . 172 ASP C C 177.2 0.14 1 782 . 172 ASP CA C 55.7 0.14 1 783 . 172 ASP CB C 40.4 0.14 1 784 . 172 ASP N N 121.0 0.07 1 785 . 173 GLY H H 8.81 0.01 1 786 . 173 GLY C C 175.3 0.14 1 787 . 173 GLY CA C 44.8 0.14 1 788 . 173 GLY N N 110.2 0.07 1 789 . 174 GLU H H 7.65 0.01 1 790 . 174 GLU C C 175.2 0.14 1 791 . 174 GLU CA C 55.5 0.14 1 792 . 174 GLU CB C 30.7 0.14 1 793 . 174 GLU N N 119.9 0.07 1 794 . 175 LEU H H 9.27 0.01 1 795 . 175 LEU C C 173.4 0.14 1 796 . 175 LEU CA C 53.3 0.14 1 797 . 175 LEU CB C 44.7 0.14 1 798 . 175 LEU N N 126.8 0.07 1 799 . 176 GLY H H 8.26 0.01 1 800 . 176 GLY C C 173.8 0.14 1 801 . 176 GLY CA C 44.3 0.14 1 802 . 176 GLY N N 108.2 0.07 1 803 . 177 PHE H H 8.12 0.01 1 804 . 177 PHE C C 174.6 0.14 1 805 . 177 PHE CA C 56.3 0.14 1 806 . 177 PHE CB C 39.0 0.14 1 807 . 177 PHE N N 112.9 0.07 1 808 . 178 ARG H H 9.41 0.01 1 809 . 178 ARG C C 175.7 0.14 1 810 . 178 ARG CA C 52.7 0.14 1 811 . 178 ARG CB C 32.3 0.14 1 812 . 178 ARG N N 120.3 0.07 1 813 . 179 ARG H H 9.23 0.01 1 814 . 179 ARG C C 176.3 0.14 1 815 . 179 ARG CA C 58.0 0.14 1 816 . 179 ARG CB C 29.1 0.14 1 817 . 179 ARG N N 120.4 0.07 1 818 . 180 GLY H H 8.69 0.01 1 819 . 180 GLY C C 174.5 0.14 1 820 . 180 GLY CA C 44.1 0.14 1 821 . 180 GLY N N 114.8 0.07 1 822 . 181 ASP H H 8.42 0.01 1 823 . 181 ASP C C 175.3 0.14 1 824 . 181 ASP CA C 55.0 0.14 1 825 . 181 ASP CB C 40.9 0.14 1 826 . 181 ASP N N 122.1 0.07 1 827 . 182 PHE H H 8.54 0.01 1 828 . 182 PHE C C 176.1 0.14 1 829 . 182 PHE CA C 57.1 0.14 1 830 . 182 PHE CB C 39.9 0.14 1 831 . 182 PHE N N 117.8 0.07 1 832 . 183 ILE H H 9.11 0.01 1 833 . 183 ILE C C 175.0 0.14 1 834 . 183 ILE CA C 60.1 0.14 1 835 . 183 ILE CB C 40.4 0.14 1 836 . 183 ILE N N 123.2 0.07 1 837 . 184 HIS H H 8.65 0.01 1 838 . 184 HIS C C 175.0 0.14 1 839 . 184 HIS CA C 53.9 0.14 1 840 . 184 HIS CB C 31.3 0.14 1 841 . 184 HIS N N 127.3 0.07 1 842 . 185 VAL H H 8.83 0.01 1 843 . 185 VAL C C 174.4 0.14 1 844 . 185 VAL CA C 64.3 0.14 1 845 . 185 VAL CB C 31.2 0.14 1 846 . 185 VAL N N 128.5 0.07 1 847 . 186 MET H H 9.20 0.01 1 848 . 186 MET C C 175.8 0.14 1 849 . 186 MET CA C 55.7 0.14 1 850 . 186 MET CB C 34.6 0.14 1 851 . 186 MET N N 125.7 0.07 1 852 . 187 ASP H H 7.61 0.01 1 853 . 187 ASP C C 174.7 0.14 1 854 . 187 ASP CA C 54.4 0.14 1 855 . 187 ASP CB C 42.9 0.14 1 856 . 187 ASP N N 116.3 0.07 1 857 . 188 ASN H H 8.17 0.01 1 858 . 188 ASN C C 174.8 0.14 1 859 . 188 ASN CA C 50.4 0.14 1 860 . 188 ASN CB C 35.5 0.14 1 861 . 188 ASN N N 125.9 0.07 1 862 . 189 SER H H 8.23 0.01 1 863 . 189 SER C C 175.1 0.14 1 864 . 189 SER CA C 61.1 0.14 1 865 . 189 SER CB C 62.9 0.14 1 866 . 189 SER N N 115.3 0.07 1 867 . 190 ASP H H 8.60 0.01 1 868 . 190 ASP C C 174.5 0.14 1 869 . 190 ASP CA C 51.6 0.14 1 870 . 190 ASP CB C 43.8 0.14 1 871 . 190 ASP N N 126.5 0.07 1 872 . 191 PRO C C 176.7 0.14 1 873 . 191 PRO CA C 63.9 0.14 1 874 . 191 PRO CB C 31.7 0.14 1 875 . 192 ASN H H 8.66 0.01 1 876 . 192 ASN C C 174.5 0.14 1 877 . 192 ASN CA C 54.0 0.14 1 878 . 192 ASN CB C 42.0 0.14 1 879 . 192 ASN N N 113.0 0.07 1 880 . 193 TRP H H 8.96 0.01 1 881 . 193 TRP C C 174.4 0.14 1 882 . 193 TRP CA C 56.1 0.14 1 883 . 193 TRP CB C 30.5 0.14 1 884 . 193 TRP N N 122.2 0.07 1 885 . 194 TRP H H 8.66 0.01 1 886 . 194 TRP C C 173.3 0.14 1 887 . 194 TRP CA C 53.0 0.14 1 888 . 194 TRP CB C 32.7 0.14 1 889 . 194 TRP N N 125.5 0.07 1 890 . 195 LYS H H 8.67 0.01 1 891 . 195 LYS C C 177.7 0.14 1 892 . 195 LYS CA C 54.6 0.14 1 893 . 195 LYS CB C 35.4 0.14 1 894 . 195 LYS N N 119.2 0.07 1 895 . 196 GLY H H 9.81 0.01 1 896 . 196 GLY C C 182.9 0.14 1 897 . 196 GLY CA C 46.0 0.14 1 898 . 196 GLY N N 114.9 0.07 1 899 . 197 ALA H H 8.99 0.01 1 900 . 197 ALA C C 176.7 0.14 1 901 . 197 ALA CA C 50.4 0.14 1 902 . 197 ALA CB C 22.8 0.14 1 903 . 197 ALA N N 120.6 0.07 1 904 . 198 ALA H H 8.73 0.01 1 905 . 198 ALA C C 176.9 0.14 1 906 . 198 ALA CA C 52.4 0.14 1 907 . 198 ALA CB C 21.3 0.14 1 908 . 198 ALA N N 123.1 0.07 1 909 . 199 HIS C C 175.3 0.14 1 910 . 199 HIS CA C 55.9 0.14 1 911 . 199 HIS CB C 27.1 0.14 1 912 . 200 GLY H H 8.87 0.01 1 913 . 200 GLY C C 173.9 0.14 1 914 . 200 GLY CA C 45.5 0.14 1 915 . 200 GLY N N 105.2 0.07 1 916 . 201 GLN H H 8.19 0.01 1 917 . 201 GLN C C 174.7 0.14 1 918 . 201 GLN CA C 53.7 0.14 1 919 . 201 GLN CB C 31.8 0.14 1 920 . 201 GLN N N 120.2 0.07 1 921 . 202 THR H H 8.48 0.01 1 922 . 202 THR C C 174.8 0.14 1 923 . 202 THR CA C 60.0 0.14 1 924 . 202 THR CB C 71.7 0.14 1 925 . 202 THR N N 112.6 0.07 1 926 . 203 GLY H H 9.17 0.01 1 927 . 203 GLY C C 171.5 0.14 1 928 . 203 GLY CA C 45.5 0.14 1 929 . 203 GLY N N 108.0 0.07 1 930 . 204 MET H H 9.06 0.01 1 931 . 204 MET C C 177.4 0.14 1 932 . 204 MET CA C 52.9 0.14 1 933 . 204 MET CB C 32.3 0.14 1 934 . 204 MET N N 117.2 0.07 1 935 . 205 PHE H H 9.72 0.01 1 936 . 205 PHE C C 170.7 0.14 1 937 . 205 PHE CA C 54.9 0.14 1 938 . 205 PHE CB C 40.2 0.14 1 939 . 205 PHE N N 118.2 0.07 1 940 . 206 PRO C C 178.0 0.14 1 941 . 206 PRO CA C 60.5 0.14 1 942 . 206 PRO CB C 29.8 0.14 1 943 . 207 ARG H H 7.84 0.01 1 944 . 207 ARG C C 176.6 0.14 1 945 . 207 ARG CA C 56.8 0.14 1 946 . 207 ARG CB C 26.9 0.14 1 947 . 207 ARG N N 125.0 0.07 1 948 . 208 ASN H H 8.55 0.01 1 949 . 208 ASN C C 174.7 0.14 1 950 . 208 ASN CA C 53.6 0.14 1 951 . 208 ASN CB C 35.1 0.14 1 952 . 208 ASN N N 114.0 0.07 1 953 . 209 TYR H H 7.84 0.01 1 954 . 209 TYR C C 175.6 0.14 1 955 . 209 TYR CA C 58.5 0.14 1 956 . 209 TYR CB C 38.3 0.14 1 957 . 209 TYR N N 119.2 0.07 1 958 . 210 VAL H H 7.55 0.01 1 959 . 210 VAL C C 173.3 0.14 1 960 . 210 VAL CA C 58.5 0.14 1 961 . 210 VAL CB C 35.3 0.14 1 962 . 210 VAL N N 109.7 0.07 1 963 . 211 THR H H 8.65 0.01 1 964 . 211 THR C C 171.5 0.14 1 965 . 211 THR CA C 57.3 0.14 1 966 . 211 THR CB C 71.9 0.14 1 967 . 211 THR N N 113.4 0.07 1 968 . 212 PRO C C 176.2 0.14 1 969 . 212 PRO CA C 63.5 0.14 1 970 . 212 PRO CB C 31.8 0.14 1 971 . 213 VAL H H 8.09 0.01 1 972 . 213 VAL C C 174.9 0.14 1 973 . 213 VAL CA C 61.0 0.14 1 974 . 213 VAL CB C 33.3 0.14 1 975 . 213 VAL N N 118.9 0.07 1 976 . 214 ASN H H 8.69 0.01 1 977 . 214 ASN C C 174.8 0.14 1 978 . 214 ASN CA C 52.6 0.14 1 979 . 214 ASN CB C 38.6 0.14 1 980 . 214 ASN N N 122.2 0.07 1 981 . 216 ASN C C 174.0 0.14 1 982 . 216 ASN CA C 53.1 0.14 1 983 . 216 ASN CB C 38.3 0.14 1 984 . 217 VAL H H 7.57 0.01 1 985 . 217 VAL C C 180.7 0.14 1 986 . 217 VAL CA C 63.0 0.14 1 987 . 217 VAL CB C 32.7 0.14 1 988 . 217 VAL N N 123.2 0.07 1 stop_ save_