data_4087 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; E2 DNA-binding domain from papillomavirus bpv-1 ; _BMRB_accession_number 4087 _BMRB_flat_file_name bmr4087.str _Entry_type update _Submission_date 1999-05-22 _Accession_date 1999-12-06 _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 Veeraraghavan S. . . 2 Mello C. C. . 3 Androphy E. J. . 4 Baleja J. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 604 "13C chemical shifts" 336 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-27 updated author ; Authors have sent an updated chemical shift table. They have also added a more recent publication. The original publication including the deposition number is also shown at the end of this file (citation_one). ; stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Correlates for Enhanced Stability in the E2 DNA-Binding Domain from Bovine Papillomavirus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20056031 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Veeraraghavan S. . . 2 Mello C. C. . 3 Androphy E. J. . 4 Baleja J. D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16115 _Page_last 16124 _Year 1999 _Details . loop_ _Keyword 'DNA-binding domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Veeraraghavan, S.; Mello, C. C.; Lee, K. M.; Androphy, E. J. and Baleja, J. D. "1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein". J. Biomol. NMR, 11, 457-458 (1998). ; _Citation_title '1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9691287 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Veeraraghavan S . . 2 Mello 'C C' C. . 3 Lee 'K M' M. . 4 Androphy 'E J' J. . 5 Baleja 'J D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 11 _Journal_issue 4 _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 457 _Page_last 458 _Year 1998 _Details . save_ ################################## # Molecular system description # ################################## save_system_E2 _Saveframe_category molecular_system _Mol_system_name E2 _Abbreviation_common E2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label E2 $E2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state homodimer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common E2 _Name_variant none _Abbreviation_common E2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; APRRTTNDGFHLLKAGGSCF ALISGTANQVKCYRFRVKKN HRHRYENCTTTWFTVADNGA ERQGQAQILITFGSPSQRQD FLKHVPLPPGMNISGFTASL DF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 ALA 2 -1 PRO 3 1 ARG 4 2 ARG 5 3 THR 6 4 THR 7 5 ASN 8 6 ASP 9 7 GLY 10 8 PHE 11 9 HIS 12 10 LEU 13 11 LEU 14 12 LYS 15 13 ALA 16 14 GLY 17 15 GLY 18 16 SER 19 17 CYS 20 18 PHE 21 19 ALA 22 20 LEU 23 21 ILE 24 22 SER 25 23 GLY 26 24 THR 27 25 ALA 28 26 ASN 29 27 GLN 30 28 VAL 31 29 LYS 32 30 CYS 33 31 TYR 34 32 ARG 35 33 PHE 36 34 ARG 37 35 VAL 38 36 LYS 39 37 LYS 40 38 ASN 41 39 HIS 42 40 ARG 43 41 HIS 44 42 ARG 45 43 TYR 46 44 GLU 47 45 ASN 48 46 CYS 49 47 THR 50 48 THR 51 49 THR 52 50 TRP 53 51 PHE 54 52 THR 55 53 VAL 56 54 ALA 57 55 ASP 58 56 ASN 59 57 GLY 60 58 ALA 61 59 GLU 62 60 ARG 63 61 GLN 64 62 GLY 65 63 GLN 66 64 ALA 67 65 GLN 68 66 ILE 69 67 LEU 70 68 ILE 71 69 THR 72 70 PHE 73 71 GLY 74 72 SER 75 73 PRO 76 74 SER 77 75 GLN 78 76 ARG 79 77 GLN 80 78 ASP 81 79 PHE 82 80 LEU 83 81 LYS 84 82 HIS 85 83 VAL 86 84 PRO 87 85 LEU 88 86 PRO 89 87 PRO 90 88 GLY 91 89 MET 92 90 ASN 93 91 ILE 94 92 SER 95 93 GLY 96 94 PHE 97 95 THR 98 96 ALA 99 97 SER 100 98 LEU 101 99 ASP 102 100 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1DBD "E2 Dna-Binding Domain From Papillomavirus Bpv-1" 97.06 100 100.00 100.00 2.76e-67 PDB 1JJH "E2 Dna-Binding Domain From Bovine Papillomavirus Type 1" 84.31 86 98.84 98.84 1.43e-56 PDB 2BOP "Crystal Structure At 1.7 Angstroms Of The Bovine Papillomavirus-1 E2 Dna-Binding Domain Bound To Its Dna Target" 83.33 85 100.00 100.00 2.01e-56 DBJ BAL04334 "E2 protein [Bovine papillomavirus type 1]" 99.02 410 99.01 100.00 8.16e-66 GB AFV52369 "E2 [Bovine papillomavirus type 1]" 99.02 410 99.01 100.00 3.90e-66 GB AGM20697 "E2 protein, partial [Bovine papillomavirus type 1]" 53.92 55 100.00 100.00 1.43e-31 GB AGM20699 "E2 protein, partial [Bovine papillomavirus type 1]" 53.92 55 100.00 100.00 1.43e-31 GB AGM20701 "E2 protein, partial [Bovine papillomavirus type 1]" 53.92 55 100.00 100.00 1.43e-31 GB AGM20703 "E2 protein, partial [Bovine papillomavirus type 1]" 53.92 55 100.00 100.00 1.43e-31 SP P03122 "RecName: Full=Regulatory protein E2" 99.02 410 100.00 100.00 1.25e-66 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $E2 BPV-1 10559 . . Bovine papillomavirus 'type 1' 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 $E2 'recombinant technology' 'Escherichia coli' Escherichia coli 'BL21(DE3) pLysS' . 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 $E2 1.7 mM '[U-99% 13C]' Na_posphate 20 mM . Na_chloride 100 mM . dithiothreitol 5 mM . EDTA 0.05 mM . Na_azide 0.01 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling E2 1.7 mM '[U-99% 15N]' Na_posphate 20 mM . Na_chloride 100 mM . dithiothreitol 5 mM . EDTA 0.05 mM . Na_azide 0.01 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.75 . n/a pressure 1 . atm temperature 308.3 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 E2 C 13 . ppm 116.5 . indirect . . . 0.101329118 water H 1 . ppm 4.66 internal direct . . . . E2 N 15 . ppm 47.5 . indirect . . . 0.251449530 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name E2 _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 ALA HA H 4.38 . 1 2 . 1 ALA CA C 51.0 . 1 3 . 2 PRO HA H 4.51 . 1 4 . 2 PRO HB2 H 2.32 . 2 5 . 2 PRO HB3 H 1.87 . 2 6 . 2 PRO HG2 H 2.04 . 1 7 . 2 PRO HG3 H 2.04 . 1 8 . 2 PRO HD2 H 3.61 . 2 9 . 2 PRO HD3 H 3.73 . 2 10 . 2 PRO CA C 63.1 . 1 11 . 2 PRO CB C 32.0 . 1 12 . 2 PRO CG C 27.8 . 1 13 . 2 PRO CD C 50.6 . 1 14 . 3 ARG H H 8.54 . 1 15 . 3 ARG HA H 4.47 . 1 16 . 3 ARG HB2 H 1.81 . 2 17 . 3 ARG HB3 H 1.94 . 2 18 . 3 ARG HG2 H 1.67 . 1 19 . 3 ARG HG3 H 1.67 . 1 20 . 3 ARG HD2 H 3.22 . 1 21 . 3 ARG HD3 H 3.22 . 1 22 . 3 ARG CA C 56.2 . 1 23 . 3 ARG CB C 31.2 . 1 24 . 3 ARG CG C 26.8 . 1 25 . 3 ARG CD C 43.6 . 1 26 . 3 ARG N N 120.9 . 1 27 . 4 ARG H H 8.44 . 1 28 . 4 ARG HA H 4.35 . 1 29 . 4 ARG HB2 H 1.82 . 2 30 . 4 ARG HB3 H 1.84 . 2 31 . 4 ARG HG2 H 1.66 . 1 32 . 4 ARG HG3 H 1.66 . 1 33 . 4 ARG HD2 H 3.22 . 1 34 . 4 ARG HD3 H 3.22 . 1 35 . 4 ARG CA C 56.6 . 1 36 . 4 ARG CB C 31.2 . 1 37 . 4 ARG CG C 26.8 . 1 38 . 4 ARG CD C 43.6 . 1 39 . 4 ARG N N 119.5 . 1 40 . 5 THR H H 8.32 . 1 41 . 5 THR HA H 4.46 . 1 42 . 5 THR HB H 4.27 . 1 43 . 5 THR HG2 H 1.21 . 1 44 . 5 THR CA C 61.8 . 1 45 . 5 THR CB C 70.0 . 1 46 . 5 THR CG2 C 21.2 . 1 47 . 5 THR N N 113.3 . 1 48 . 6 THR H H 8.12 . 1 49 . 6 THR HA H 4.37 . 1 50 . 6 THR HB H 4.25 . 1 51 . 6 THR HG2 H 1.18 . 1 52 . 6 THR CA C 61.9 . 1 53 . 6 THR CB C 70.0 . 1 54 . 6 THR CG2 C 21.8 . 1 55 . 6 THR N N 112.7 . 1 56 . 7 ASN H H 8.05 . 1 57 . 7 ASN HA H 4.74 . 1 58 . 7 ASN HB2 H 2.83 . 2 59 . 7 ASN HB3 H 2.94 . 2 60 . 7 ASN HD21 H 6.85 . 2 61 . 7 ASN HD22 H 7.53 . 2 62 . 7 ASN CA C 52.8 . 1 63 . 7 ASN CB C 39.0 . 1 64 . 7 ASN N N 113.6 . 1 65 . 7 ASN ND2 N 109.4 . 1 66 . 8 ASP H H 8.20 . 1 67 . 8 ASP HA H 4.52 . 1 68 . 8 ASP HB2 H 2.63 . 2 69 . 8 ASP HB3 H 2.68 . 2 70 . 8 ASP CA C 54.6 . 1 71 . 8 ASP CB C 41.5 . 1 72 . 8 ASP N N 118.3 . 1 73 . 9 GLY H H 8.20 . 1 74 . 9 GLY HA2 H 3.78 . 2 75 . 9 GLY HA3 H 3.84 . 2 76 . 9 GLY CA C 45.5 . 1 77 . 9 GLY N N 105.8 . 1 78 . 10 PHE H H 7.98 . 1 79 . 10 PHE HA H 4.46 . 1 80 . 10 PHE HB2 H 2.98 . 1 81 . 10 PHE HB3 H 2.98 . 1 82 . 10 PHE HD1 H 7.13 . 1 83 . 10 PHE HD2 H 7.13 . 1 84 . 10 PHE HE1 H 7.26 . 1 85 . 10 PHE HE2 H 7.26 . 1 86 . 10 PHE HZ H 7.20 . 1 87 . 10 PHE CA C 58.3 . 1 88 . 10 PHE CB C 39.2 . 1 89 . 10 PHE CD1 C 131.7 . 1 90 . 10 PHE CD2 C 131.7 . 1 91 . 10 PHE CE1 C 131.4 . 1 92 . 10 PHE CE2 C 131.4 . 1 93 . 10 PHE CZ C 129.5 . 1 94 . 10 PHE N N 116.8 . 1 95 . 11 HIS H H 7.82 . 1 96 . 11 HIS HA H 4.53 . 1 97 . 11 HIS HB2 H 2.97 . 2 98 . 11 HIS HB3 H 3.04 . 2 99 . 11 HIS HD2 H 7.06 . 1 100 . 11 HIS HE1 H 7.79 . 1 101 . 11 HIS CA C 54.7 . 1 102 . 11 HIS CB C 30.3 . 1 103 . 11 HIS CD2 C 119.2 . 1 104 . 11 HIS CE1 C 138.0 . 1 105 . 11 HIS N N 118.9 . 1 106 . 12 LEU H H 8.43 . 1 107 . 12 LEU HA H 3.95 . 1 108 . 12 LEU HB2 H 1.73 . 2 109 . 12 LEU HB3 H 1.38 . 2 110 . 12 LEU HG H 1.58 . 1 111 . 12 LEU HD1 H 0.63 . 2 112 . 12 LEU HD2 H 0.84 . 2 113 . 12 LEU CA C 57.7 . 1 114 . 12 LEU CB C 41.9 . 1 115 . 12 LEU CD1 C 19.4 . 1 116 . 12 LEU CD2 C 23.5 . 1 117 . 12 LEU N N 120.6 . 1 118 . 13 LEU H H 7.36 . 1 119 . 13 LEU HA H 4.38 . 1 120 . 13 LEU HB2 H 0.86 . 2 121 . 13 LEU HB3 H 1.32 . 2 122 . 13 LEU HG H 1.01 . 1 123 . 13 LEU HD1 H -0.12 . 2 124 . 13 LEU HD2 H 0.26 . 2 125 . 13 LEU CA C 53.8 . 1 126 . 13 LEU CB C 42.8 . 1 127 . 13 LEU CG C 27.0 . 1 128 . 13 LEU CD1 C 24.7 . 2 129 . 13 LEU CD2 C 23.1 . 2 130 . 13 LEU N N 113.0 . 1 131 . 14 LYS H H 8.06 . 1 132 . 14 LYS HA H 4.33 . 1 133 . 14 LYS HB2 H 1.79 . 2 134 . 14 LYS HB3 H 1.92 . 2 135 . 14 LYS HG2 H 1.42 . 1 136 . 14 LYS HG3 H 1.42 . 1 137 . 14 LYS HD2 H 1.70 . 1 138 . 14 LYS HD3 H 1.70 . 1 139 . 14 LYS HE2 H 3.04 . 1 140 . 14 LYS HE3 H 3.04 . 1 141 . 14 LYS CA C 56.3 . 1 142 . 14 LYS CB C 34.4 . 1 143 . 14 LYS CG C 24.2 . 1 144 . 14 LYS CD C 27.5 . 1 145 . 14 LYS CE C 42.2 . 1 146 . 14 LYS N N 117.9 . 1 147 . 15 ALA H H 8.31 . 1 148 . 15 ALA HA H 4.31 . 1 149 . 15 ALA HB H 1.39 . 1 150 . 15 ALA CA C 52.8 . 1 151 . 15 ALA CB C 19.7 . 1 152 . 15 ALA N N 119.5 . 1 153 . 16 GLY H H 8.41 . 1 154 . 16 GLY HA2 H 4.01 . 2 155 . 16 GLY HA3 H 4.07 . 2 156 . 16 GLY CA C 45.5 . 1 157 . 16 GLY N N 104.9 . 1 158 . 17 GLY H H 8.48 . 1 159 . 17 GLY HA2 H 4.07 . 2 160 . 17 GLY HA3 H 4.37 . 2 161 . 17 GLY CA C 45.4 . 1 162 . 17 GLY N N 108.9 . 1 163 . 18 SER H H 8.38 . 1 164 . 18 SER HA H 4.90 . 1 165 . 18 SER HB2 H 3.97 . 1 166 . 18 SER HB3 H 3.97 . 1 167 . 18 SER CA C 58.7 . 1 168 . 18 SER CB C 65.9 . 1 169 . 18 SER N N 114.9 . 1 170 . 19 CYS H H 9.12 . 1 171 . 19 CYS HA H 5.30 . 1 172 . 19 CYS HB2 H 2.97 . 2 173 . 19 CYS HB3 H 3.03 . 2 174 . 19 CYS CA C 58.1 . 1 175 . 19 CYS CB C 29.0 . 1 176 . 19 CYS N N 121.8 . 1 177 . 20 PHE H H 9.17 . 1 178 . 20 PHE HA H 6.03 . 1 179 . 20 PHE HB2 H 2.96 . 2 180 . 20 PHE HB3 H 3.22 . 2 181 . 20 PHE HD1 H 6.96 . 1 182 . 20 PHE HD2 H 6.96 . 1 183 . 20 PHE HE1 H 6.72 . 1 184 . 20 PHE HE2 H 6.72 . 1 185 . 20 PHE HZ H 6.37 . 1 186 . 20 PHE CA C 56.5 . 1 187 . 20 PHE CB C 42.2 . 1 188 . 20 PHE CD1 C 133.1 . 1 189 . 20 PHE CD2 C 133.1 . 1 190 . 20 PHE CZ C 128.7 . 1 191 . 20 PHE N N 116.9 . 1 192 . 21 ALA H H 10.13 . 1 193 . 21 ALA HA H 5.55 . 1 194 . 21 ALA HB H 1.45 . 1 195 . 21 ALA CA C 51.2 . 1 196 . 21 ALA CB C 22.5 . 1 197 . 21 ALA N N 120.7 . 1 198 . 22 LEU H H 9.14 . 1 199 . 22 LEU HA H 5.31 . 1 200 . 22 LEU HB2 H 1.50 . 2 201 . 22 LEU HB3 H 1.75 . 2 202 . 22 LEU HG H 1.57 . 1 203 . 22 LEU HD1 H 0.88 . 1 204 . 22 LEU HD2 H 0.88 . 1 205 . 22 LEU CA C 54.1 . 1 206 . 22 LEU CB C 45.7 . 1 207 . 22 LEU CG C 28.3 . 1 208 . 22 LEU CD1 C 24.1 . 2 209 . 22 LEU CD2 C 25.8 . 2 210 . 22 LEU N N 120.0 . 1 211 . 23 ILE H H 8.47 . 1 212 . 23 ILE HA H 5.05 . 1 213 . 23 ILE HB H 1.43 . 1 214 . 23 ILE HG12 H 1.24 . 2 215 . 23 ILE HG13 H 1.34 . 2 216 . 23 ILE HG2 H 0.35 . 1 217 . 23 ILE HD1 H 0.91 . 1 218 . 23 ILE CA C 60.0 . 1 219 . 23 ILE CB C 40.2 . 1 220 . 23 ILE CG1 C 27.2 . 1 221 . 23 ILE CG2 C 19.1 . 1 222 . 23 ILE CD1 C 15.2 . 1 223 . 23 ILE N N 126.2 . 1 224 . 24 SER H H 8.70 . 1 225 . 24 SER HA H 5.60 . 1 226 . 24 SER HB2 H 3.48 . 2 227 . 24 SER HB3 H 3.68 . 2 228 . 24 SER CA C 55.5 . 1 229 . 24 SER CB C 67.5 . 1 230 . 24 SER N N 114.1 . 1 231 . 25 GLY H H 8.18 . 1 232 . 25 GLY HA2 H 3.91 . 2 233 . 25 GLY HA3 H 4.19 . 2 234 . 25 GLY CA C 45.9 . 1 235 . 25 GLY N N 104.2 . 1 236 . 26 THR H H 8.75 . 1 237 . 26 THR HA H 4.76 . 1 238 . 26 THR HB H 4.78 . 1 239 . 26 THR HG2 H 1.35 . 1 240 . 26 THR CA C 61.9 . 1 241 . 26 THR CB C 70.6 . 1 242 . 26 THR CG2 C 22.2 . 1 243 . 26 THR N N 108.9 . 1 244 . 27 ALA H H 9.20 . 1 245 . 27 ALA HA H 3.75 . 1 246 . 27 ALA HB H 1.65 . 1 247 . 27 ALA CA C 56.5 . 1 248 . 27 ALA CB C 17.9 . 1 249 . 27 ALA N N 121.0 . 1 250 . 28 ASN H H 8.80 . 1 251 . 28 ASN HA H 4.54 . 1 252 . 28 ASN HB2 H 2.77 . 2 253 . 28 ASN HB3 H 2.82 . 2 254 . 28 ASN HD21 H 6.99 . 2 255 . 28 ASN HD22 H 7.65 . 2 256 . 28 ASN CA C 56.5 . 1 257 . 28 ASN CB C 38.8 . 1 258 . 28 ASN N N 112.6 . 1 259 . 28 ASN ND2 N 110.7 . 1 260 . 29 GLN H H 7.85 . 1 261 . 29 GLN HA H 4.00 . 1 262 . 29 GLN HB2 H 2.34 . 1 263 . 29 GLN HB3 H 2.34 . 1 264 . 29 GLN HG2 H 2.34 . 2 265 . 29 GLN HG3 H 2.58 . 2 266 . 29 GLN HE21 H 6.73 . 2 267 . 29 GLN HE22 H 7.28 . 2 268 . 29 GLN CA C 59.5 . 1 269 . 29 GLN CB C 28.4 . 1 270 . 29 GLN CG C 34.9 . 1 271 . 29 GLN N N 117.4 . 1 272 . 29 GLN NE2 N 108.8 . 1 273 . 30 VAL H H 8.50 . 1 274 . 30 VAL HA H 3.38 . 1 275 . 30 VAL HB H 1.75 . 1 276 . 30 VAL HG1 H 0.57 . 1 277 . 30 VAL HG2 H 0.57 . 1 278 . 30 VAL CA C 67.1 . 1 279 . 30 VAL CB C 31.1 . 1 280 . 30 VAL CG1 C 23.7 . 1 281 . 30 VAL CG2 C 23.7 . 1 282 . 30 VAL N N 115.5 . 1 283 . 31 LYS H H 7.88 . 1 284 . 31 LYS HA H 3.93 . 1 285 . 31 LYS HB2 H 2.01 . 2 286 . 31 LYS HB3 H 2.14 . 2 287 . 31 LYS HG2 H 1.34 . 2 288 . 31 LYS HG3 H 1.52 . 2 289 . 31 LYS HD2 H 1.75 . 1 290 . 31 LYS HD3 H 1.75 . 1 291 . 31 LYS HE2 H 2.98 . 1 292 . 31 LYS HE3 H 2.98 . 1 293 . 31 LYS CA C 60.2 . 1 294 . 31 LYS CB C 32.5 . 1 295 . 31 LYS CG C 25.0 . 1 296 . 31 LYS CD C 29.8 . 1 297 . 31 LYS CE C 42.1 . 1 298 . 31 LYS N N 118.5 . 1 299 . 32 CYS H H 7.90 . 1 300 . 32 CYS HA H 4.23 . 1 301 . 32 CYS HB2 H 2.98 . 2 302 . 32 CYS HB3 H 3.08 . 2 303 . 32 CYS CA C 63.4 . 1 304 . 32 CYS CB C 26.9 . 1 305 . 32 CYS N N 114.8 . 1 306 . 33 TYR H H 8.37 . 1 307 . 33 TYR HA H 4.08 . 1 308 . 33 TYR HB2 H 2.91 . 2 309 . 33 TYR HB3 H 3.03 . 2 310 . 33 TYR HD1 H 6.72 . 1 311 . 33 TYR HD2 H 6.72 . 1 312 . 33 TYR HE1 H 6.65 . 1 313 . 33 TYR HE2 H 6.65 . 1 314 . 33 TYR CA C 61.9 . 1 315 . 33 TYR CB C 39.8 . 1 316 . 33 TYR CD1 C 132.3 . 1 317 . 33 TYR CD2 C 132.3 . 1 318 . 33 TYR CE1 C 118.0 . 1 319 . 33 TYR CE2 C 118.0 . 1 320 . 33 TYR N N 119.7 . 1 321 . 34 ARG H H 8.68 . 1 322 . 34 ARG HA H 3.81 . 1 323 . 34 ARG HB2 H 1.90 . 2 324 . 34 ARG HB3 H 2.09 . 2 325 . 34 ARG HG2 H 1.61 . 2 326 . 34 ARG HG3 H 1.75 . 2 327 . 34 ARG HD2 H 3.22 . 2 328 . 34 ARG HD3 H 3.35 . 2 329 . 34 ARG CA C 59.8 . 1 330 . 34 ARG CD C 45.3 . 1 331 . 34 ARG N N 114.1 . 1 332 . 35 PHE H H 8.05 . 1 333 . 35 PHE HA H 4.20 . 1 334 . 35 PHE HB2 H 3.25 . 2 335 . 35 PHE HB3 H 3.33 . 2 336 . 35 PHE HD1 H 7.31 . 1 337 . 35 PHE HD2 H 7.31 . 1 338 . 35 PHE HE1 H 7.41 . 1 339 . 35 PHE HE2 H 7.41 . 1 340 . 35 PHE HZ H 7.27 . 4 341 . 35 PHE CA C 61.5 . 1 342 . 35 PHE CB C 39.0 . 1 343 . 35 PHE CD1 C 132.5 . 1 344 . 35 PHE CD2 C 132.5 . 1 345 . 35 PHE CE1 C 131.7 . 1 346 . 35 PHE CE2 C 131.7 . 1 347 . 35 PHE CZ C 132.6 . 4 348 . 35 PHE N N 114.8 . 1 349 . 36 ARG H H 7.95 . 1 350 . 36 ARG HA H 3.95 . 1 351 . 36 ARG HB2 H 1.37 . 2 352 . 36 ARG HB3 H 1.50 . 2 353 . 36 ARG HG2 H 1.23 . 2 354 . 36 ARG HG3 H 1.36 . 2 355 . 36 ARG HD2 H 2.87 . 1 356 . 36 ARG HD3 H 2.87 . 1 357 . 36 ARG CA C 55.9 . 1 358 . 36 ARG CB C 29.5 . 1 359 . 36 ARG CG C 27.2 . 1 360 . 36 ARG CD C 43.4 . 1 361 . 36 ARG N N 115.6 . 1 362 . 37 VAL H H 8.29 . 1 363 . 37 VAL HA H 3.88 . 1 364 . 37 VAL HB H 2.04 . 1 365 . 37 VAL HG1 H 0.67 . 2 366 . 37 VAL HG2 H 0.68 . 2 367 . 37 VAL CA C 66.3 . 1 368 . 37 VAL CB C 31.1 . 1 369 . 37 VAL CG1 C 23.3 . 2 370 . 37 VAL CG2 C 21.8 . 2 371 . 37 VAL N N 115.3 . 1 372 . 38 LYS H H 8.15 . 1 373 . 38 LYS HA H 4.46 . 1 374 . 38 LYS HB2 H 1.86 . 2 375 . 38 LYS HB3 H 2.06 . 2 376 . 38 LYS HG2 H 1.58 . 2 377 . 38 LYS HG3 H 1.47 . 2 378 . 38 LYS HD2 H 1.66 . 1 379 . 38 LYS HD3 H 1.66 . 1 380 . 38 LYS HE2 H 2.97 . 1 381 . 38 LYS HE3 H 2.97 . 1 382 . 38 LYS CA C 59.0 . 1 383 . 38 LYS CB C 33.0 . 4 384 . 38 LYS CG C 25.0 . 4 385 . 38 LYS CD C 30.2 . 1 386 . 38 LYS CE C 42.1 . 1 387 . 38 LYS N N 118.8 . 1 388 . 39 LYS H H 7.65 . 1 389 . 39 LYS HA H 4.08 . 1 390 . 39 LYS HB2 H 1.54 . 2 391 . 39 LYS HB3 H 1.57 . 2 392 . 39 LYS HG2 H 1.23 . 1 393 . 39 LYS HG3 H 1.23 . 1 394 . 39 LYS HD2 H 1.23 . 1 395 . 39 LYS HD3 H 1.23 . 1 396 . 39 LYS HE2 H 2.96 . 1 397 . 39 LYS HE3 H 2.96 . 1 398 . 39 LYS CA C 58.3 . 1 399 . 39 LYS CB C 33.2 . 1 400 . 39 LYS CG C 24.7 . 1 401 . 39 LYS CD C 29.9 . 9 402 . 39 LYS CE C 42.1 . 1 403 . 39 LYS N N 113.2 . 1 404 . 40 ASN H H 7.96 . 1 405 . 40 ASN HA H 4.86 . 1 406 . 40 ASN HB2 H 2.32 . 2 407 . 40 ASN HB3 H 2.48 . 2 408 . 40 ASN HD21 H 6.72 . 2 409 . 40 ASN HD22 H 7.43 . 2 410 . 40 ASN CA C 54.3 . 1 411 . 40 ASN CB C 41.5 . 1 412 . 40 ASN N N 109.8 . 1 413 . 40 ASN ND2 N 110.0 . 1 414 . 41 HIS H H 8.03 . 1 415 . 41 HIS HA H 4.95 . 1 416 . 41 HIS HB2 H 2.96 . 2 417 . 41 HIS HB3 H 3.22 . 2 418 . 41 HIS HD2 H 6.48 . 1 419 . 41 HIS HE1 H 7.67 . 1 420 . 41 HIS CA C 55.1 . 1 421 . 41 HIS CB C 32.8 . 1 422 . 41 HIS CD2 C 118.0 . 1 423 . 41 HIS CE1 C 139.3 . 1 424 . 41 HIS N N 114.8 . 1 425 . 42 ARG H H 8.16 . 1 426 . 42 ARG HA H 4.22 . 1 427 . 42 ARG HB2 H 1.78 . 2 428 . 42 ARG HB3 H 2.25 . 2 429 . 42 ARG HG2 H 1.74 . 2 430 . 42 ARG HG3 H 1.95 . 2 431 . 42 ARG HD2 H 3.13 . 1 432 . 42 ARG HD3 H 3.13 . 1 433 . 42 ARG CA C 57.6 . 1 434 . 42 ARG N N 118.8 . 1 435 . 43 HIS H H 8.65 . 1 436 . 43 HIS HA H 4.63 . 1 437 . 43 HIS HB2 H 3.03 . 2 438 . 43 HIS HB3 H 3.27 . 2 439 . 43 HIS HD2 H 6.79 . 1 440 . 43 HIS HE1 H 8.27 . 1 441 . 43 HIS CA C 56.0 . 1 442 . 43 HIS CB C 29.0 . 1 443 . 43 HIS CD2 C 118.3 . 1 444 . 43 HIS CE1 C 136.8 . 1 445 . 43 HIS N N 108.1 . 1 446 . 44 ARG H H 8.17 . 1 447 . 44 ARG HA H 4.62 . 1 448 . 44 ARG HB2 H 2.05 . 2 449 . 44 ARG HB3 H 2.16 . 2 450 . 44 ARG CA C 61.8 . 1 451 . 44 ARG N N 116.3 . 1 452 . 45 TYR H H 7.28 . 1 453 . 45 TYR HA H 4.83 . 1 454 . 45 TYR HB2 H 2.42 . 2 455 . 45 TYR HB3 H 2.57 . 2 456 . 45 TYR HD1 H 6.77 . 1 457 . 45 TYR HD2 H 6.77 . 1 458 . 45 TYR HE1 H 6.44 . 1 459 . 45 TYR HE2 H 6.44 . 1 460 . 45 TYR CA C 56.0 . 1 461 . 45 TYR CB C 40.7 . 1 462 . 45 TYR CD1 C 133.8 . 1 463 . 45 TYR CD2 C 133.8 . 1 464 . 45 TYR CE1 C 117.8 . 1 465 . 45 TYR CE2 C 117.8 . 1 466 . 45 TYR N N 109.5 . 1 467 . 46 GLU H H 8.86 . 1 468 . 46 GLU HA H 4.45 . 1 469 . 46 GLU HB2 H 1.80 . 1 470 . 46 GLU HB3 H 1.80 . 1 471 . 46 GLU HG2 H 2.04 . 2 472 . 46 GLU HG3 H 2.07 . 2 473 . 46 GLU CA C 59.0 . 1 474 . 46 GLU CB C 30.0 . 1 475 . 46 GLU CG C 37.6 . 1 476 . 46 GLU N N 117.9 . 1 477 . 47 ASN H H 7.96 . 1 478 . 47 ASN HA H 5.32 . 1 479 . 47 ASN HB2 H 2.59 . 2 480 . 47 ASN HB3 H 2.67 . 2 481 . 47 ASN HD21 H 7.12 . 2 482 . 47 ASN HD22 H 8.07 . 2 483 . 47 ASN CA C 52.8 . 1 484 . 47 ASN CB C 44.6 . 1 485 . 47 ASN N N 114.2 . 1 486 . 47 ASN ND2 N 113.5 . 1 487 . 48 CYS H H 9.22 . 1 488 . 48 CYS HA H 5.65 . 1 489 . 48 CYS HB2 H 2.64 . 2 490 . 48 CYS HB3 H 2.73 . 2 491 . 48 CYS CA C 56.6 . 1 492 . 48 CYS CB C 31.1 . 1 493 . 48 CYS N N 112.8 . 1 494 . 49 THR H H 7.88 . 1 495 . 49 THR HA H 5.71 . 1 496 . 49 THR HB H 4.80 . 1 497 . 49 THR HG2 H 0.80 . 1 498 . 49 THR CA C 61.6 . 1 499 . 49 THR CB C 74.3 . 1 500 . 49 THR CG2 C 23.1 . 1 501 . 49 THR N N 108.7 . 1 502 . 50 THR H H 8.87 . 1 503 . 50 THR HA H 4.26 . 1 504 . 50 THR HB H 5.08 . 1 505 . 50 THR HG2 H 1.58 . 1 506 . 50 THR CA C 63.4 . 1 507 . 50 THR CB C 69.8 . 1 508 . 50 THR CG2 C 24.3 . 1 509 . 50 THR N N 106.1 . 1 510 . 51 THR H H 8.75 . 1 511 . 51 THR HA H 4.19 . 1 512 . 51 THR HB H 4.12 . 1 513 . 51 THR HG2 H 0.95 . 1 514 . 51 THR CA C 64.0 . 1 515 . 51 THR CB C 70.1 . 1 516 . 51 THR CG2 C 24.5 . 1 517 . 51 THR N N 115.8 . 1 518 . 52 TRP H H 9.00 . 1 519 . 52 TRP HA H 4.88 . 1 520 . 52 TRP HB2 H 3.05 . 2 521 . 52 TRP HB3 H 3.51 . 2 522 . 52 TRP HD1 H 6.82 . 1 523 . 52 TRP HE1 H 7.12 . 1 524 . 52 TRP HE3 H 6.44 . 1 525 . 52 TRP HZ2 H 6.43 . 1 526 . 52 TRP HZ3 H 6.67 . 1 527 . 52 TRP HH2 H 7.18 . 1 528 . 52 TRP CA C 54.7 . 1 529 . 52 TRP CB C 33.4 . 1 530 . 52 TRP CD1 C 130.7 . 1 531 . 52 TRP CE3 C 123.2 . 1 532 . 52 TRP CZ2 C 111.8 . 1 533 . 52 TRP CZ3 C 123.3 . 1 534 . 52 TRP CH2 C 120.5 . 1 535 . 52 TRP NE1 N 119.7 . 1 536 . 53 PHE H H 8.78 . 1 537 . 53 PHE HA H 4.95 . 1 538 . 53 PHE HB2 H 2.79 . 2 539 . 53 PHE HB3 H 3.37 . 2 540 . 53 PHE HD1 H 7.19 . 1 541 . 53 PHE HD2 H 7.19 . 1 542 . 53 PHE HE1 H 7.30 . 1 543 . 53 PHE HE2 H 7.30 . 1 544 . 53 PHE HZ H 7.26 . 1 545 . 53 PHE CA C 56.3 . 1 546 . 53 PHE CB C 43.6 . 1 547 . 53 PHE CD1 C 132.8 . 1 548 . 53 PHE CD2 C 132.8 . 1 549 . 53 PHE CE1 C 133.0 . 1 550 . 53 PHE CE2 C 133.0 . 1 551 . 53 PHE CZ C 131.8 . 1 552 . 53 PHE N N 112.2 . 1 553 . 54 THR H H 9.37 . 1 554 . 54 THR HA H 4.57 . 1 555 . 54 THR HB H 4.16 . 1 556 . 54 THR HG2 H 1.25 . 1 557 . 54 THR CA C 64.0 . 1 558 . 54 THR CB C 68.6 . 1 559 . 54 THR CG2 C 23.5 . 1 560 . 54 THR N N 117.8 . 1 561 . 55 VAL H H 8.83 . 1 562 . 55 VAL HA H 3.94 . 1 563 . 55 VAL HB H 2.11 . 1 564 . 55 VAL HG1 H 0.97 . 1 565 . 55 VAL HG2 H 0.97 . 1 566 . 55 VAL CA C 62.9 . 1 567 . 55 VAL CB C 31.1 . 1 568 . 55 VAL CG1 C 21.8 . 1 569 . 55 VAL CG2 C 21.8 . 1 570 . 55 VAL N N 125.5 . 1 571 . 56 ALA H H 8.35 . 1 572 . 56 ALA HA H 4.57 . 1 573 . 56 ALA HB H 1.41 . 1 574 . 56 ALA CA C 51.4 . 1 575 . 56 ALA CB C 19.5 . 1 576 . 56 ALA N N 128.1 . 1 577 . 57 ASP H H 8.62 . 1 578 . 57 ASP HA H 4.57 . 1 579 . 57 ASP HB2 H 2.58 . 2 580 . 57 ASP HB3 H 2.76 . 2 581 . 57 ASP CA C 56.2 . 1 582 . 57 ASP CB C 41.6 . 1 583 . 57 ASP N N 118.8 . 1 584 . 58 ASN H H 8.44 . 1 585 . 58 ASN HA H 4.76 . 1 586 . 58 ASN HB2 H 2.74 . 2 587 . 58 ASN HB3 H 2.83 . 2 588 . 58 ASN HD21 H 6.85 . 2 589 . 58 ASN HD22 H 6.73 . 2 590 . 58 ASN CA C 53.4 . 1 591 . 58 ASN CB C 39.0 . 1 592 . 58 ASN N N 118.2 . 1 593 . 58 ASN ND2 N 110.0 . 1 594 . 59 GLY H H 8.26 . 1 595 . 59 GLY HA2 H 3.73 . 2 596 . 59 GLY HA3 H 4.13 . 2 597 . 59 GLY CA C 45.5 . 1 598 . 59 GLY N N 105.9 . 1 599 . 60 ALA H H 7.93 . 1 600 . 60 ALA HA H 4.33 . 1 601 . 60 ALA HB H 1.39 . 1 602 . 60 ALA CA C 52.6 . 1 603 . 60 ALA CB C 19.5 . 1 604 . 60 ALA N N 121.1 . 1 605 . 61 GLU H H 8.35 . 1 606 . 61 GLU HA H 4.20 . 1 607 . 61 GLU HB2 H 1.97 . 2 608 . 61 GLU HB3 H 2.09 . 2 609 . 61 GLU HG2 H 2.18 . 2 610 . 61 GLU HG3 H 2.42 . 2 611 . 61 GLU CA C 58.1 . 1 612 . 61 GLU CB C 30.5 . 1 613 . 61 GLU CG C 37.0 . 1 614 . 61 GLU N N 116.5 . 1 615 . 62 ARG H H 7.95 . 1 616 . 62 ARG HA H 3.93 . 1 617 . 62 ARG HB2 H 1.98 . 2 618 . 62 ARG HB3 H 2.10 . 2 619 . 62 ARG HG2 H 1.63 . 2 620 . 62 ARG HG3 H 2.03 . 2 621 . 62 ARG HD2 H 3.27 . 2 622 . 62 ARG HD3 H 3.33 . 2 623 . 62 ARG CA C 59.7 . 1 624 . 62 ARG CB C 30.8 . 1 625 . 62 ARG CG C 27.7 . 1 626 . 62 ARG CD C 43.8 . 1 627 . 62 ARG N N 115.4 . 1 628 . 63 GLN H H 8.29 . 1 629 . 63 GLN HA H 4.46 . 1 630 . 63 GLN HB2 H 1.90 . 2 631 . 63 GLN HB3 H 2.08 . 2 632 . 63 GLN HG2 H 2.20 . 1 633 . 63 GLN HG3 H 2.20 . 1 634 . 63 GLN HE21 H 7.04 . 2 635 . 63 GLN HE22 H 7.36 . 2 636 . 63 GLN CA C 55.5 . 1 637 . 63 GLN CB C 31.3 . 1 638 . 63 GLN CG C 34.0 . 1 639 . 63 GLN N N 118.1 . 1 640 . 63 GLN NE2 N 110.1 . 1 641 . 64 GLY H H 8.45 . 1 642 . 64 GLY HA2 H 4.03 . 1 643 . 64 GLY HA3 H 4.06 . 1 644 . 64 GLY CA C 45.5 . 1 645 . 64 GLY N N 106.4 . 1 646 . 65 GLN H H 8.24 . 1 647 . 65 GLN HA H 4.32 . 1 648 . 65 GLN HB2 H 1.83 . 2 649 . 65 GLN HB3 H 2.09 . 2 650 . 65 GLN HG2 H 2.20 . 2 651 . 65 GLN HG3 H 2.29 . 2 652 . 65 GLN HE21 H 6.68 . 2 653 . 65 GLN HE22 H 7.38 . 2 654 . 65 GLN CA C 56.3 . 1 655 . 65 GLN CB C 30.4 . 1 656 . 65 GLN CG C 34.5 . 1 657 . 65 GLN N N 116.2 . 1 658 . 65 GLN NE2 N 108.6 . 1 659 . 66 ALA H H 8.19 . 1 660 . 66 ALA HA H 3.44 . 1 661 . 66 ALA HB H 0.87 . 1 662 . 66 ALA CA C 51.1 . 1 663 . 66 ALA CB C 19.6 . 1 664 . 66 ALA N N 124.2 . 1 665 . 67 GLN H H 7.96 . 1 666 . 67 GLN HA H 4.97 . 1 667 . 67 GLN HB2 H -0.70 . 2 668 . 67 GLN HB3 H 0.52 . 2 669 . 67 GLN HG2 H 1.58 . 1 670 . 67 GLN HG3 H 1.58 . 1 671 . 67 GLN HE21 H 6.69 . 2 672 . 67 GLN HE22 H 7.37 . 2 673 . 67 GLN CA C 54.1 . 1 674 . 67 GLN CB C 31.6 . 1 675 . 67 GLN CG C 35.2 . 1 676 . 67 GLN N N 115.4 . 1 677 . 67 GLN NE2 N 105.1 . 1 678 . 68 ILE H H 7.67 . 1 679 . 68 ILE HA H 3.95 . 1 680 . 68 ILE HB H 2.12 . 1 681 . 68 ILE HG12 H 1.25 . 2 682 . 68 ILE HG13 H 1.58 . 2 683 . 68 ILE HG2 H 0.97 . 1 684 . 68 ILE HD1 H 0.78 . 1 685 . 68 ILE CA C 64.4 . 1 686 . 68 ILE CG1 C 27.2 . 9 687 . 68 ILE CG2 C 23.3 . 1 688 . 68 ILE CD1 C 13.7 . 1 689 . 68 ILE N N 105.9 . 1 690 . 69 LEU H H 7.63 . 1 691 . 69 LEU HA H 5.40 . 1 692 . 69 LEU HB2 H 1.11 . 2 693 . 69 LEU HB3 H 1.32 . 2 694 . 69 LEU HG H 1.44 . 1 695 . 69 LEU HD1 H 0.02 . 2 696 . 69 LEU HD2 H 0.53 . 2 697 . 69 LEU CA C 54.0 . 1 698 . 69 LEU CB C 45.6 . 1 699 . 69 LEU CG C 28.2 . 1 700 . 69 LEU CD1 C 25.3 . 2 701 . 69 LEU CD2 C 24.8 . 2 702 . 69 LEU N N 118.1 . 1 703 . 70 ILE H H 8.68 . 1 704 . 70 ILE HA H 4.82 . 1 705 . 70 ILE HB H 1.23 . 1 706 . 70 ILE HG12 H 0.69 . 2 707 . 70 ILE HG13 H 1.46 . 2 708 . 70 ILE HG2 H 0.21 . 1 709 . 70 ILE HD1 H 0.56 . 1 710 . 70 ILE CA C 60.1 . 1 711 . 70 ILE CB C 41.8 . 1 712 . 70 ILE CG1 C 28.2 . 1 713 . 70 ILE CG2 C 18.3 . 1 714 . 70 ILE CD1 C 14.4 . 1 715 . 70 ILE N N 119.5 . 1 716 . 71 THR H H 9.07 . 1 717 . 71 THR HA H 4.81 . 1 718 . 71 THR HB H 4.52 . 1 719 . 71 THR HG2 H 0.93 . 1 720 . 71 THR CA C 59.8 . 1 721 . 71 THR CB C 71.1 . 1 722 . 71 THR CG2 C 23.9 . 1 723 . 71 THR N N 113.6 . 1 724 . 72 PHE H H 8.27 . 1 725 . 72 PHE HA H 4.97 . 1 726 . 72 PHE HB2 H 2.63 . 2 727 . 72 PHE HB3 H 3.52 . 2 728 . 72 PHE HD1 H 7.52 . 3 729 . 72 PHE HD2 H 7.66 . 3 730 . 72 PHE HE1 H 7.00 . 1 731 . 72 PHE HE2 H 7.00 . 1 732 . 72 PHE HZ H 5.96 . 1 733 . 72 PHE CA C 57.0 . 1 734 . 72 PHE CB C 44.0 . 1 735 . 72 PHE CE1 C 130.3 . 1 736 . 72 PHE CE2 C 130.3 . 1 737 . 72 PHE CZ C 128.7 . 1 738 . 72 PHE N N 112.3 . 1 739 . 73 GLY H H 9.82 . 1 740 . 73 GLY HA2 H 3.95 . 2 741 . 73 GLY HA3 H 4.16 . 2 742 . 73 GLY CA C 46.3 . 1 743 . 73 GLY N N 107.4 . 1 744 . 74 SER H H 7.42 . 1 745 . 74 SER HA H 5.10 . 1 746 . 74 SER HB2 H 4.18 . 2 747 . 74 SER HB3 H 4.30 . 2 748 . 74 SER CA C 56.6 . 1 749 . 74 SER CB C 56.5 . 1 750 . 74 SER N N 106.3 . 1 751 . 75 PRO HA H 4.44 . 1 752 . 75 PRO HB2 H 2.12 . 2 753 . 75 PRO HB3 H 2.18 . 2 754 . 75 PRO HG2 H 2.25 . 2 755 . 75 PRO HG3 H 2.43 . 2 756 . 75 PRO HD2 H 3.99 . 2 757 . 75 PRO HD3 H 4.05 . 2 758 . 75 PRO CA C 65.3 . 1 759 . 75 PRO CG C 28.4 . 1 760 . 75 PRO CD C 51.4 . 1 761 . 76 SER H H 7.85 . 1 762 . 76 SER HA H 4.28 . 1 763 . 76 SER HB2 H 3.92 . 1 764 . 76 SER HB3 H 3.92 . 1 765 . 76 SER CA C 61.7 . 1 766 . 76 SER CB C 62.1 . 1 767 . 76 SER N N 117.4 . 1 768 . 77 GLN H H 8.02 . 1 769 . 77 GLN HA H 4.27 . 1 770 . 77 GLN HB2 H 2.20 . 2 771 . 77 GLN HB3 H 2.53 . 2 772 . 77 GLN HG2 H 2.64 . 2 773 . 77 GLN HG3 H 2.83 . 2 774 . 77 GLN HE21 H 6.53 . 2 775 . 77 GLN HE22 H 6.97 . 2 776 . 77 GLN CA C 59.3 . 1 777 . 77 GLN CB C 29.8 . 1 778 . 77 GLN CG C 34.8 . 1 779 . 77 GLN N N 123.6 . 1 780 . 77 GLN NE2 N 109.3 . 1 781 . 78 ARG H H 7.42 . 1 782 . 78 ARG HA H 2.98 . 1 783 . 78 ARG HB2 H 2.00 . 1 784 . 78 ARG HB3 H 2.00 . 1 785 . 78 ARG HG2 H 0.78 . 1 786 . 78 ARG HG3 H 0.78 . 1 787 . 78 ARG HD2 H 1.99 . 2 788 . 78 ARG HD3 H 4.40 . 2 789 . 78 ARG CA C 59.8 . 1 790 . 78 ARG CD C 44.3 . 1 791 . 78 ARG N N 115.9 . 1 792 . 79 GLN H H 7.94 . 1 793 . 79 GLN HA H 3.87 . 1 794 . 79 GLN HB2 H 2.13 . 2 795 . 79 GLN HB3 H 2.16 . 2 796 . 79 GLN HG2 H 2.35 . 2 797 . 79 GLN HG3 H 2.41 . 2 798 . 79 GLN HE21 H 6.48 . 2 799 . 79 GLN HE22 H 7.43 . 2 800 . 79 GLN CA C 59.1 . 1 801 . 79 GLN CB C 28.6 . 1 802 . 79 GLN CG C 34.1 . 1 803 . 79 GLN N N 115.6 . 1 804 . 79 GLN NE2 N 107.9 . 1 805 . 80 ASP H H 7.85 . 1 806 . 80 ASP HA H 4.50 . 1 807 . 80 ASP HB2 H 2.83 . 2 808 . 80 ASP HB3 H 3.07 . 2 809 . 80 ASP CA C 58.3 . 1 810 . 80 ASP CB C 42.2 . 1 811 . 80 ASP N N 117.9 . 1 812 . 81 PHE H H 8.63 . 1 813 . 81 PHE HA H 3.93 . 1 814 . 81 PHE HB2 H 3.55 . 2 815 . 81 PHE HB3 H 3.96 . 2 816 . 81 PHE HD1 H 7.19 . 1 817 . 81 PHE HD2 H 7.19 . 1 818 . 81 PHE HE1 H 7.39 . 1 819 . 81 PHE HE2 H 7.39 . 1 820 . 81 PHE HZ H 7.35 . 1 821 . 81 PHE CA C 62.4 . 1 822 . 81 PHE CB C 38.8 . 1 823 . 81 PHE CD1 C 132.2 . 3 824 . 81 PHE CD2 C 132.3 . 3 825 . 81 PHE CE1 C 131.1 . 1 826 . 81 PHE CE2 C 131.1 . 1 827 . 81 PHE CZ C 130.1 . 1 828 . 81 PHE N N 120.0 . 1 829 . 82 LEU H H 8.26 . 1 830 . 82 LEU HA H 3.95 . 1 831 . 82 LEU HB2 H 1.37 . 2 832 . 82 LEU HB3 H 1.75 . 2 833 . 82 LEU HG H 1.90 . 1 834 . 82 LEU HD1 H 0.56 . 2 835 . 82 LEU HD2 H 0.84 . 2 836 . 82 LEU CA C 57.2 . 1 837 . 82 LEU CB C 41.8 . 1 838 . 82 LEU CG C 27.4 . 1 839 . 82 LEU CD1 C 25.9 . 2 840 . 82 LEU CD2 C 23.0 . 2 841 . 82 LEU N N 114.4 . 1 842 . 83 LYS H H 7.73 . 1 843 . 83 LYS HA H 3.93 . 1 844 . 83 LYS HB2 H 1.59 . 2 845 . 83 LYS HB3 H 1.75 . 2 846 . 83 LYS HG2 H 1.12 . 2 847 . 83 LYS HG3 H 1.31 . 2 848 . 83 LYS HD2 H 1.56 . 1 849 . 83 LYS HD3 H 1.56 . 1 850 . 83 LYS HE2 H 2.85 . 1 851 . 83 LYS HE3 H 2.85 . 1 852 . 83 LYS CA C 57.8 . 1 853 . 83 LYS CB C 33.1 . 1 854 . 83 LYS CG C 25.2 . 1 855 . 83 LYS CD C 30.4 . 1 856 . 83 LYS CE C 42.0 . 1 857 . 83 LYS N N 113.3 . 1 858 . 84 HIS H H 7.42 . 1 859 . 84 HIS HA H 4.45 . 1 860 . 84 HIS HB2 H 2.56 . 2 861 . 84 HIS HB3 H 3.23 . 2 862 . 84 HIS HD2 H 7.57 . 1 863 . 84 HIS HE1 H 8.54 . 1 864 . 84 HIS CA C 58.0 . 1 865 . 84 HIS CB C 30.7 . 1 866 . 84 HIS CD2 C 121.5 . 1 867 . 84 HIS CE1 C 136.9 . 1 868 . 84 HIS N N 110.6 . 1 869 . 85 VAL H H 7.69 . 1 870 . 85 VAL HA H 3.84 . 1 871 . 85 VAL HB H 1.13 . 1 872 . 85 VAL HG1 H -0.58 . 2 873 . 85 VAL HG2 H 0.19 . 2 874 . 85 VAL CA C 59.8 . 1 875 . 85 VAL CB C 31.0 . 1 876 . 85 VAL CG1 C 18.6 . 2 877 . 85 VAL CG2 C 21.9 . 2 878 . 85 VAL N N 118.9 . 1 879 . 86 PRO HA H 4.28 . 1 880 . 86 PRO HB2 H 1.74 . 2 881 . 86 PRO HB3 H 2.21 . 2 882 . 86 PRO HG2 H 1.93 . 2 883 . 86 PRO HG3 H 1.97 . 2 884 . 86 PRO HD2 H 3.49 . 2 885 . 86 PRO HD3 H 3.68 . 2 886 . 86 PRO CA C 63.1 . 1 887 . 86 PRO CB C 32.3 . 1 888 . 86 PRO CG C 27.5 . 1 889 . 86 PRO CD C 51.0 . 1 890 . 87 LEU H H 8.44 . 1 891 . 87 LEU HA H 4.78 . 1 892 . 87 LEU HB2 H 1.47 . 2 893 . 87 LEU HB3 H 1.84 . 2 894 . 87 LEU HG H 1.47 . 1 895 . 87 LEU HD1 H 0.73 . 2 896 . 87 LEU HD2 H 0.77 . 2 897 . 87 LEU CA C 52.3 . 1 898 . 87 LEU CB C 43.3 . 1 899 . 87 LEU CG C 26.8 . 1 900 . 87 LEU CD1 C 24.6 . 2 901 . 87 LEU CD2 C 26.5 . 2 902 . 87 LEU N N 123.3 . 1 903 . 88 PRO HA H 4.36 . 1 904 . 88 PRO HB2 H 2.34 . 2 905 . 88 PRO HB3 H 2.11 . 2 906 . 88 PRO HG2 H 1.89 . 2 907 . 88 PRO HG3 H 2.03 . 2 908 . 88 PRO HD2 H 3.62 . 2 909 . 88 PRO HD3 H 3.90 . 2 910 . 88 PRO CA C 63.8 . 1 911 . 88 PRO CB C 32.3 . 1 912 . 88 PRO CG C 27.5 . 9 913 . 88 PRO CD C 50.9 . 1 914 . 89 PRO HA H 4.43 . 1 915 . 89 PRO HB2 H 2.07 . 2 916 . 89 PRO HB3 H 2.47 . 2 917 . 89 PRO HG2 H 2.01 . 2 918 . 89 PRO HG3 H 2.06 . 2 919 . 89 PRO HD2 H 3.41 . 2 920 . 89 PRO HD3 H 3.43 . 2 921 . 89 PRO CA C 65.3 . 1 922 . 89 PRO CB C 32.8 . 1 923 . 89 PRO CG C 26.6 . 1 924 . 89 PRO CD C 49.7 . 1 925 . 90 GLY H H 8.63 . 1 926 . 90 GLY HA2 H 3.65 . 2 927 . 90 GLY HA3 H 4.40 . 2 928 . 90 GLY CA C 45.3 . 1 929 . 90 GLY N N 108.7 . 1 930 . 91 MET H H 7.55 . 1 931 . 91 MET HA H 4.87 . 1 932 . 91 MET HB2 H 1.88 . 2 933 . 91 MET HB3 H 2.06 . 2 934 . 91 MET HG2 H 2.22 . 2 935 . 91 MET HG3 H 2.28 . 2 936 . 91 MET HE H 1.35 . 1 937 . 91 MET CA C 56.0 . 1 938 . 91 MET CB C 34.7 . 1 939 . 91 MET CG C 33.2 . 1 940 . 91 MET CE C 16.8 . 1 941 . 91 MET N N 116.5 . 1 942 . 92 ASN H H 8.40 . 1 943 . 92 ASN HA H 5.15 . 1 944 . 92 ASN HB2 H 2.53 . 2 945 . 92 ASN HB3 H 2.66 . 2 946 . 92 ASN HD21 H 6.74 . 2 947 . 92 ASN HD22 H 7.42 . 2 948 . 92 ASN CA C 52.7 . 1 949 . 92 ASN CB C 43.4 . 1 950 . 92 ASN N N 114.5 . 1 951 . 92 ASN ND2 N 111.2 . 1 952 . 93 ILE H H 8.62 . 1 953 . 93 ILE HA H 5.42 . 1 954 . 93 ILE HB H 1.73 . 4 955 . 93 ILE HG12 H 1.73 . 4 956 . 93 ILE HG13 H 1.73 . 4 957 . 93 ILE HG2 H 1.05 . 1 958 . 93 ILE HD1 H 1.03 . 1 959 . 93 ILE CA C 59.7 . 1 960 . 93 ILE CB C 42.0 . 1 961 . 93 ILE CG2 C 15.7 . 1 962 . 93 ILE CD1 C 14.4 . 1 963 . 93 ILE N N 116.6 . 1 964 . 94 SER H H 8.38 . 1 965 . 94 SER HA H 4.70 . 1 966 . 94 SER HB2 H 3.43 . 2 967 . 94 SER HB3 H 3.58 . 2 968 . 94 SER CA C 57.5 . 1 969 . 94 SER CB C 67.1 . 1 970 . 94 SER N N 119.0 . 1 971 . 95 GLY H H 8.17 . 1 972 . 95 GLY HA2 H 3.90 . 2 973 . 95 GLY HA3 H 4.40 . 2 974 . 95 GLY CA C 51.7 . 1 975 . 95 GLY N N 110.0 . 1 976 . 96 PHE H H 7.87 . 1 977 . 96 PHE HA H 5.12 . 1 978 . 96 PHE HB2 H 0.68 . 2 979 . 96 PHE HB3 H 2.32 . 2 980 . 96 PHE HD1 H 6.44 . 1 981 . 96 PHE HD2 H 6.44 . 1 982 . 96 PHE HE1 H 6.95 . 1 983 . 96 PHE HE2 H 6.95 . 1 984 . 96 PHE HZ H 6.92 . 1 985 . 96 PHE CA C 56.9 . 1 986 . 96 PHE CB C 45.4 . 1 987 . 96 PHE CD1 C 131.7 . 1 988 . 96 PHE CD2 C 131.7 . 1 989 . 96 PHE CE1 C 131.4 . 1 990 . 96 PHE CE2 C 131.4 . 1 991 . 96 PHE CZ C 131.4 . 1 992 . 96 PHE N N 117.3 . 1 993 . 97 THR H H 8.37 . 1 994 . 97 THR HA H 5.00 . 1 995 . 97 THR HB H 4.08 . 1 996 . 97 THR HG2 H 1.19 . 1 997 . 97 THR CA C 63.4 . 1 998 . 97 THR CB C 70.9 . 1 999 . 97 THR CG2 C 20.8 . 1 1000 . 97 THR N N 114.3 . 1 1001 . 98 ALA H H 9.42 . 1 1002 . 98 ALA HA H 5.71 . 1 1003 . 98 ALA HB H 1.56 . 1 1004 . 98 ALA CA C 50.6 . 1 1005 . 98 ALA CB C 22.9 . 1 1006 . 98 ALA N N 125.8 . 1 1007 . 99 SER H H 8.97 . 1 1008 . 99 SER HA H 4.83 . 1 1009 . 99 SER HB2 H 3.85 . 2 1010 . 99 SER HB3 H 3.89 . 2 1011 . 99 SER CA C 57.1 . 1 1012 . 99 SER CB C 65.1 . 1 1013 . 99 SER N N 114.7 . 1 1014 . 100 LEU H H 8.47 . 1 1015 . 100 LEU HA H 3.95 . 1 1016 . 100 LEU HB2 H 1.34 . 2 1017 . 100 LEU HB3 H 1.73 . 2 1018 . 100 LEU HG H 1.08 . 1 1019 . 100 LEU HD1 H 0.47 . 2 1020 . 100 LEU HD2 H 0.67 . 2 1021 . 100 LEU CA C 55.6 . 1 1022 . 100 LEU CB C 41.1 . 1 1023 . 100 LEU CG C 27.2 . 1 1024 . 100 LEU CD1 C 25.3 . 2 1025 . 100 LEU CD2 C 26.3 . 2 1026 . 100 LEU N N 123.9 . 1 1027 . 101 ASP H H 8.93 . 1 1028 . 101 ASP HA H 4.68 . 1 1029 . 101 ASP HB2 H 1.70 . 2 1030 . 101 ASP HB3 H 2.70 . 2 1031 . 101 ASP CA C 56.1 . 1 1032 . 101 ASP CB C 42.8 . 1 1033 . 101 ASP N N 127.0 . 1 1034 . 102 PHE H H 7.13 . 1 1035 . 102 PHE HA H 4.23 . 1 1036 . 102 PHE HB2 H 3.03 . 2 1037 . 102 PHE HB3 H 3.28 . 2 1038 . 102 PHE HD1 H 7.04 . 1 1039 . 102 PHE HD2 H 7.04 . 1 1040 . 102 PHE HE1 H 6.71 . 1 1041 . 102 PHE HE2 H 6.71 . 1 1042 . 102 PHE HZ H 6.88 . 1 1043 . 102 PHE CA C 59.0 . 1 1044 . 102 PHE CB C 39.6 . 1 1045 . 102 PHE CD1 C 133.4 . 1 1046 . 102 PHE CD2 C 133.4 . 1 1047 . 102 PHE CZ C 130.0 . 1 1048 . 102 PHE N N 116.9 . 1 stop_ save_