data_4035 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the DNA-Binding Domain of a Human Papillomavirus E2 Protein: Evidence for Flexible DNA-Binding Regions ; _BMRB_accession_number 4035 _BMRB_flat_file_name bmr4035.str _Entry_type original _Submission_date 1997-06-16 _Accession_date 1997-06-16 _Entry_origination BMRB _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 Liang Heng . . 2 Petros Andrew M. . 3 Meadows Robert P. . 4 Yoon Ho S. . 5 Egan David A. . 6 Walter Karl . . 7 Holzman Thomas F. . 8 Robins Terry . . 9 Fesik Stephen W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 491 "13C chemical shifts" 296 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1997-03-02 version_update BMRB 'converted to NMR-STAR 2.1' 2005-04-21 update BMRB 'authors added to entry citation' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Liang, H., Petros, A. M., Meadows, R. P., Yoon, H. S., Egan, D. A., Walter, K., Holzman, T. F., Robins, T., and Fesik, S. W., "Solution Structure of the DNA-Binding Domain of a Human Papillomavirus E2 Protein: Evidence for Flexible DNA-Binding Regions," Biochemistry 35, 2095-2103 (1996). ; _Citation_title ; Solution Structure of the DNA-Binding Domain of a Human Papillomavirus E2 Protein: Evidence for Flexible DNA-Binding Regions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96194130 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liang Heng . . 2 Petros Andrew M. . 3 Meadows Robert P. . 4 Yoon Ho S. . 5 Egan David A. . 6 Walter Karl . . 7 Holzman Thomas F. . 8 Robins Terry . . 9 Fesik Stephen W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 35 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2095 _Page_last 2103 _Year 1996 _Details . loop_ _Keyword 'Human Papillomavirus (HPV)' NMR 'Nuclear Magnetic Resonance' stop_ save_ ################################## # Molecular system description # ################################## save_system_E2-HPV _Saveframe_category molecular_system _Mol_system_name 'Regulatory protein E2' _Abbreviation_common E2-HPV _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label E2-HPV $E2-HPV stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; E2 is a transcription factor for the Human papillomavirus,and is required for replication of DNA ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E2-HPV _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Regulatory protein E2' _Abbreviation_common E2-HPV _Molecular_mass . _Mol_thiol_state . _Details ; The E2 protein consists of three functional domains: an N-terminal transactivation domain, a hinge domain, and a C-terminal domain of approximately 82 amino acides that is responsible for both DNA-binding and dimerization ; ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; MATTPIIHLKGDANILKCLR YRLSKYKQLYEQVSSTWHWT CTDGKHKNAIVTLTYISTSQ RDDFLNTVKIPNTVSVSTGY MTI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 THR 4 4 THR 5 5 PRO 6 6 ILE 7 7 ILE 8 8 HIS 9 9 LEU 10 10 LYS 11 11 GLY 12 12 ASP 13 13 ALA 14 14 ASN 15 15 ILE 16 16 LEU 17 17 LYS 18 18 CYS 19 19 LEU 20 20 ARG 21 21 TYR 22 22 ARG 23 23 LEU 24 24 SER 25 25 LYS 26 26 TYR 27 27 LYS 28 28 GLN 29 29 LEU 30 30 TYR 31 31 GLU 32 32 GLN 33 33 VAL 34 34 SER 35 35 SER 36 36 THR 37 37 TRP 38 38 HIS 39 39 TRP 40 40 THR 41 41 CYS 42 42 THR 43 43 ASP 44 44 GLY 45 45 LYS 46 46 HIS 47 47 LYS 48 48 ASN 49 49 ALA 50 50 ILE 51 51 VAL 52 52 THR 53 53 LEU 54 54 THR 55 55 TYR 56 56 ILE 57 57 SER 58 58 THR 59 59 SER 60 60 GLN 61 61 ARG 62 62 ASP 63 63 ASP 64 64 PHE 65 65 LEU 66 66 ASN 67 67 THR 68 68 VAL 69 69 LYS 70 70 ILE 71 71 PRO 72 72 ASN 73 73 THR 74 74 VAL 75 75 SER 76 76 VAL 77 77 SER 78 78 THR 79 79 GLY 80 80 TYR 81 81 MET 82 82 THR 83 83 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1A7G "The Crystal Structure Of The E2 Dna-Binding Domain From Human Papillomavirus At 2.4 Angstroms" 98.80 82 98.78 98.78 2.95e-51 PDB 1DHM "Dna-Binding Domain Of E2 From Human Papillomavirus-31, Nmr, Minimized Average Structure" 100.00 83 100.00 100.00 3.56e-53 EMBL CRH59757 "E2 (early) protein%2C N terminal [Chlamydia trachomatis]" 98.80 372 98.78 98.78 1.38e-48 EMBL CRH70730 "E2 (early) protein%2C N terminal [Chlamydia trachomatis]" 98.80 372 98.78 100.00 3.66e-49 GB AAA46953 "regulatory protein [Human papillomavirus type 31]" 98.80 372 100.00 100.00 2.55e-49 GB AEI60921 "early protein E2 [Human papillomavirus type 31]" 98.80 372 100.00 100.00 2.55e-49 GB AEI60929 "early protein E2 [Human papillomavirus type 31]" 98.80 372 100.00 100.00 2.55e-49 GB AEI60937 "early protein E2 [Human papillomavirus type 31]" 98.80 372 100.00 100.00 2.55e-49 GB AEI60945 "early protein E2 [Human papillomavirus type 31]" 98.80 372 98.78 98.78 5.05e-48 REF WP_057257005 "hypothetical protein [Chlamydia trachomatis]" 98.80 372 98.78 98.78 1.38e-48 SP P17383 "RecName: Full=Regulatory protein E2" 98.80 372 100.00 100.00 2.55e-49 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $E2-HPV 'human Papillomavirus' 47.0.1.0.019 10566 . . Papillomavirus 'human papillomavirus' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $E2-HPV 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS plasmid pET-3b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E2-HPV 1.7 mM [U-15N;U-13C] D2O 10 % . H2O 90 % . sodium_phosphate 20 mM . dithiothreitol 5 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E2-HPV 1.7 mM [U-15N;U-13C] D2O 100 % . sodium_phosphate 20 mM . dithiothreitol 5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX600 _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX500 _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 303 . 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 . C 13 . ppm . . . . . . . H 1 . ppm . . . . . . . N 15 . ppm . . . . . . 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_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name E2-HPV _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 HA H 4.14 . 1 2 . 1 MET HB2 H 2.61 . 1 3 . 1 MET HB3 H 2.61 . 1 4 . 1 MET HG2 H 2.12 . 1 5 . 1 MET HG3 H 2.12 . 1 6 . 1 MET CA C 53.56 . 1 7 . 1 MET CB C 29.33 . 1 8 . 1 MET CG C 31.81 . 1 9 . 2 ALA HA H 4.26 . 1 10 . 2 ALA HB H 1.63 . 1 11 . 2 ALA CA C 49.98 . 1 12 . 2 ALA CB C 17.77 . 1 13 . 3 THR H H 8.47 . 1 14 . 3 THR HA H 4.85 . 1 15 . 3 THR HB H 4.05 . 1 16 . 3 THR HG2 H 1.12 . 1 17 . 3 THR CA C 60.30 . 1 18 . 3 THR CB C 68.44 . 1 19 . 3 THR CG2 C 19.97 . 1 20 . 3 THR N N 115.69 . 1 21 . 4 THR H H 9.04 . 1 22 . 4 THR HA H 5.06 . 1 23 . 4 THR HB H 4.30 . 1 24 . 4 THR HG2 H 1.46 . 1 25 . 4 THR CA C 58.25 . 1 26 . 4 THR CB C 70.36 . 1 27 . 4 THR CG2 C 19.14 . 1 28 . 4 THR N N 123.61 . 1 29 . 5 PRO HA H 4.61 . 1 30 . 5 PRO HB2 H 2.06 . 2 31 . 5 PRO HB3 H 1.66 . 2 32 . 5 PRO HG2 H 2.02 . 2 33 . 5 PRO HG3 H 1.83 . 2 34 . 5 PRO HD2 H 4.19 . 1 35 . 5 PRO HD3 H 4.19 . 1 36 . 5 PRO CA C 61.00 . 1 37 . 5 PRO CB C 29.88 . 1 38 . 5 PRO CD C 49.44 . 1 39 . 6 ILE H H 8.29 . 1 40 . 6 ILE HA H 5.94 . 1 41 . 6 ILE HB H 1.95 . 1 42 . 6 ILE HG12 H 0.74 . 2 43 . 6 ILE HG13 H 0.51 . 2 44 . 6 ILE HG2 H 1.03 . 1 45 . 6 ILE HD1 H 0.43 . 1 46 . 6 ILE CA C 57.15 . 1 47 . 6 ILE CB C 42.83 . 1 48 . 6 ILE CG2 C 17.49 . 1 49 . 6 ILE CD1 C 12.81 . 1 50 . 6 ILE N N 114.03 . 1 51 . 7 ILE H H 8.77 . 1 52 . 7 ILE HA H 4.89 . 1 53 . 7 ILE HB H 1.90 . 1 54 . 7 ILE HG12 H 1.51 . 2 55 . 7 ILE HG13 H 1.20 . 2 56 . 7 ILE HG2 H 0.90 . 1 57 . 7 ILE HD1 H 0.78 . 1 58 . 7 ILE CA C 59.35 . 1 59 . 7 ILE CB C 41.17 . 1 60 . 7 ILE CG1 C 26.30 . 1 61 . 7 ILE CG2 C 16.39 . 1 62 . 7 ILE CD1 C 11.71 . 1 63 . 7 ILE N N 118.76 . 1 64 . 8 HIS H H 8.67 . 1 65 . 8 HIS HA H 5.65 . 1 66 . 8 HIS HB2 H 2.84 . 2 67 . 8 HIS HB3 H 2.58 . 2 68 . 8 HIS HD2 H 6.94 . 1 69 . 8 HIS HE1 H 7.67 . 1 70 . 8 HIS CA C 52.19 . 1 71 . 8 HIS CB C 32.09 . 1 72 . 8 HIS CD2 C 115.90 . 1 73 . 8 HIS CE1 C 135.90 . 1 74 . 8 HIS N N 120.08 . 1 75 . 9 LEU H H 9.44 . 1 76 . 9 LEU HA H 5.15 . 1 77 . 9 LEU HB2 H 1.83 . 2 78 . 9 LEU HB3 H 0.98 . 2 79 . 9 LEU HG H 1.63 . 1 80 . 9 LEU HD1 H 0.85 . 2 81 . 9 LEU HD2 H 0.73 . 2 82 . 9 LEU CA C 50.81 . 1 83 . 9 LEU CB C 41.45 . 1 84 . 9 LEU CG C 24.38 . 1 85 . 9 LEU CD1 C 23.55 . 2 86 . 9 LEU CD2 C 24.65 . 2 87 . 9 LEU N N 124.05 . 1 88 . 10 LYS H H 8.57 . 1 89 . 10 LYS HA H 5.54 . 1 90 . 10 LYS HB2 H 1.68 . 2 91 . 10 LYS HB3 H 1.62 . 2 92 . 10 LYS HG2 H 1.23 . 2 93 . 10 LYS HG3 H 1.17 . 2 94 . 10 LYS HD2 H 1.56 . 1 95 . 10 LYS HD3 H 1.56 . 1 96 . 10 LYS HE2 H 2.76 . 2 97 . 10 LYS HE3 H 2.68 . 2 98 . 10 LYS CA C 52.46 . 1 99 . 10 LYS CB C 33.74 . 1 100 . 10 LYS CG C 23.55 . 1 101 . 10 LYS CD C 27.68 . 1 102 . 10 LYS CE C 39.80 . 1 103 . 10 LYS N N 119.64 . 1 104 . 11 GLY H H 8.48 . 1 105 . 11 GLY HA2 H 4.15 . 2 106 . 11 GLY HA3 H 4.02 . 2 107 . 11 GLY CA C 43.10 . 1 108 . 11 GLY N N 109.73 . 1 109 . 12 ASP H H 8.65 . 1 110 . 12 ASP HA H 4.54 . 1 111 . 12 ASP HB2 H 2.70 . 2 112 . 12 ASP HB3 H 2.65 . 2 113 . 12 ASP CA C 52.59 . 1 114 . 12 ASP CB C 41.04 . 1 115 . 12 ASP N N 121.52 . 1 116 . 13 ALA H H 9.03 . 1 117 . 13 ALA HA H 3.74 . 1 118 . 13 ALA HB H 1.44 . 1 119 . 13 ALA CA C 54.39 . 1 120 . 13 ALA CB C 16.94 . 1 121 . 13 ALA N N 127.02 . 1 122 . 14 ASN H H 8.76 . 1 123 . 14 ASN HA H 4.54 . 1 124 . 14 ASN HB2 H 2.95 . 2 125 . 14 ASN HB3 H 2.79 . 2 126 . 14 ASN HD21 H 7.89 . 2 127 . 14 ASN HD22 H 7.04 . 2 128 . 14 ASN CA C 54.67 . 1 129 . 14 ASN CB C 35.94 . 1 130 . 14 ASN N N 116.34 . 1 131 . 14 ASN ND2 N 114.46 . 1 132 . 15 ILE H H 7.68 . 1 133 . 15 ILE HA H 3.86 . 1 134 . 15 ILE HB H 2.02 . 1 135 . 15 ILE HG12 H 1.64 . 2 136 . 15 ILE HG13 H 1.31 . 2 137 . 15 ILE HG2 H 0.82 . 1 138 . 15 ILE HD1 H 0.94 . 1 139 . 15 ILE CA C 62.10 . 1 140 . 15 ILE CB C 35.39 . 1 141 . 15 ILE CG1 C 26.86 . 1 142 . 15 ILE CG2 C 15.29 . 1 143 . 15 ILE CD1 C 10.06 . 1 144 . 15 ILE N N 122.73 . 1 145 . 16 LEU H H 8.21 . 1 146 . 16 LEU HA H 3.83 . 1 147 . 16 LEU HB2 H 1.70 . 2 148 . 16 LEU HB3 H 1.20 . 2 149 . 16 LEU HG H 1.49 . 1 150 . 16 LEU HD1 H 0.58 . 1 151 . 16 LEU HD2 H 0.54 . 1 152 . 16 LEU CA C 56.04 . 1 153 . 16 LEU CB C 39.25 . 1 154 . 16 LEU CG C 24.65 . 1 155 . 16 LEU CD1 C 24.10 . 2 156 . 16 LEU CD2 C 21.35 . 2 157 . 16 LEU N N 119.75 . 1 158 . 17 LYS H H 7.95 . 1 159 . 17 LYS HA H 3.89 . 1 160 . 17 LYS HB2 H 2.08 . 2 161 . 17 LYS HB3 H 2.04 . 2 162 . 17 LYS HG2 H 1.57 . 2 163 . 17 LYS HG3 H 1.41 . 2 164 . 17 LYS HD2 H 1.78 . 1 165 . 17 LYS HD3 H 1.78 . 1 166 . 17 LYS HE2 H 3.06 . 1 167 . 17 LYS HE3 H 3.06 . 1 168 . 17 LYS CA C 58.25 . 1 169 . 17 LYS CB C 30.43 . 1 170 . 17 LYS CG C 23.27 . 1 171 . 17 LYS CD C 27.68 . 1 172 . 17 LYS CE C 40.07 . 1 173 . 17 LYS N N 119.31 . 1 174 . 18 CYS H H 7.39 . 1 175 . 18 CYS HA H 4.30 . 1 176 . 18 CYS HB2 H 3.13 . 2 177 . 18 CYS HB3 H 3.08 . 2 178 . 18 CYS CA C 60.45 . 1 179 . 18 CYS CB C 24.65 . 1 180 . 18 CYS N N 117.22 . 1 181 . 19 LEU H H 8.25 . 1 182 . 19 LEU HA H 4.18 . 1 183 . 19 LEU HB2 H 1.85 . 2 184 . 19 LEU HB3 H 1.66 . 2 185 . 19 LEU HG H 1.66 . 1 186 . 19 LEU HD1 H 0.97 . 2 187 . 19 LEU HD2 H 0.90 . 2 188 . 19 LEU CA C 55.77 . 1 189 . 19 LEU CB C 40.35 . 1 190 . 19 LEU CG C 25.48 . 1 191 . 19 LEU CD1 C 22.45 . 2 192 . 19 LEU CD2 C 24.93 . 2 193 . 19 LEU N N 121.52 . 1 194 . 20 ARG H H 8.53 . 1 195 . 20 ARG HA H 3.79 . 1 196 . 20 ARG HB2 H 2.04 . 2 197 . 20 ARG HB3 H 1.71 . 2 198 . 20 ARG HG2 H 1.67 . 2 199 . 20 ARG HG3 H 1.57 . 2 200 . 20 ARG HD2 H 3.26 . 1 201 . 20 ARG HD3 H 3.26 . 1 202 . 20 ARG CA C 58.52 . 1 203 . 20 ARG CB C 27.68 . 1 204 . 20 ARG CG C 26.30 . 1 205 . 20 ARG CD C 42.27 . 1 206 . 20 ARG N N 118.65 . 1 207 . 21 TYR H H 7.54 . 1 208 . 21 TYR HA H 4.49 . 1 209 . 21 TYR HB2 H 3.29 . 1 210 . 21 TYR HB3 H 3.29 . 1 211 . 21 TYR HD1 H 7.29 . 1 212 . 21 TYR HD2 H 7.29 . 1 213 . 21 TYR HE1 H 6.91 . 1 214 . 21 TYR HE2 H 6.91 . 1 215 . 21 TYR CA C 59.07 . 1 216 . 21 TYR CB C 35.67 . 1 217 . 21 TYR CD1 C 131.22 . 1 218 . 21 TYR CD2 C 131.22 . 1 219 . 21 TYR CE1 C 116.35 . 1 220 . 21 TYR CE2 C 116.35 . 1 221 . 21 TYR N N 117.55 . 1 222 . 22 ARG H H 7.82 . 1 223 . 22 ARG HA H 4.21 . 1 224 . 22 ARG HB2 H 2.16 . 1 225 . 22 ARG HB3 H 2.16 . 1 226 . 22 ARG HG2 H 2.04 . 2 227 . 22 ARG HG3 H 1.84 . 2 228 . 22 ARG HD2 H 3.34 . 1 229 . 22 ARG HD3 H 3.34 . 1 230 . 22 ARG CA C 56.87 . 1 231 . 22 ARG CB C 28.51 . 1 232 . 22 ARG CG C 25.75 . 1 233 . 22 ARG CD C 42.00 . 1 234 . 22 ARG N N 119.86 . 1 235 . 23 LEU H H 8.31 . 1 236 . 23 LEU HA H 4.34 . 1 237 . 23 LEU HB2 H 2.09 . 2 238 . 23 LEU HB3 H 1.66 . 2 239 . 23 LEU HG H 2.15 . 1 240 . 23 LEU HD1 H 0.87 . 2 241 . 23 LEU HD2 H 0.71 . 2 242 . 23 LEU CA C 55.49 . 1 243 . 23 LEU CB C 38.97 . 1 244 . 23 LEU CG C 24.10 . 1 245 . 23 LEU CD1 C 21.35 . 2 246 . 23 LEU CD2 C 23.82 . 2 247 . 23 LEU N N 116.12 . 1 248 . 24 SER H H 7.82 . 1 249 . 24 SER HA H 4.42 . 1 250 . 24 SER HB2 H 4.09 . 1 251 . 24 SER HB3 H 4.09 . 1 252 . 24 SER CA C 59.62 . 1 253 . 24 SER CB C 60.72 . 1 254 . 24 SER N N 116.12 . 1 255 . 25 LYS H H 7.32 . 1 256 . 25 LYS HA H 4.24 . 1 257 . 25 LYS HB2 H 1.60 . 2 258 . 25 LYS HB3 H 1.52 . 2 259 . 25 LYS HG2 H 1.18 . 1 260 . 25 LYS HG3 H 1.18 . 1 261 . 25 LYS HD2 H 1.58 . 1 262 . 25 LYS HD3 H 1.58 . 1 263 . 25 LYS HE2 H 2.90 . 1 264 . 25 LYS HE3 H 2.90 . 1 265 . 25 LYS CA C 55.49 . 1 266 . 25 LYS CB C 30.16 . 1 267 . 25 LYS CG C 22.72 . 1 268 . 25 LYS CD C 26.86 . 1 269 . 25 LYS CE C 40.07 . 1 270 . 25 LYS N N 119.53 . 1 271 . 26 TYR H H 7.96 . 1 272 . 26 TYR HA H 5.03 . 1 273 . 26 TYR HB2 H 3.56 . 2 274 . 26 TYR HB3 H 2.79 . 2 275 . 26 TYR HD1 H 7.12 . 1 276 . 26 TYR HD2 H 7.12 . 1 277 . 26 TYR HE1 H 6.77 . 1 278 . 26 TYR HE2 H 6.77 . 1 279 . 26 TYR CA C 54.67 . 1 280 . 26 TYR CB C 36.49 . 1 281 . 26 TYR CD1 C 131.77 . 1 282 . 26 TYR CD2 C 131.77 . 1 283 . 26 TYR CE1 C 116.07 . 1 284 . 26 TYR CE2 C 116.07 . 1 285 . 26 TYR N N 118.98 . 1 286 . 27 LYS H H 7.24 . 1 287 . 27 LYS HA H 3.66 . 1 288 . 27 LYS HB2 H 1.84 . 1 289 . 27 LYS HB3 H 1.84 . 1 290 . 27 LYS HG2 H 1.54 . 2 291 . 27 LYS HG3 H 1.44 . 2 292 . 27 LYS HD2 H 1.70 . 1 293 . 27 LYS HD3 H 1.70 . 1 294 . 27 LYS HE2 H 3.01 . 1 295 . 27 LYS HE3 H 3.01 . 1 296 . 27 LYS CA C 56.59 . 1 297 . 27 LYS CB C 30.16 . 1 298 . 27 LYS CG C 22.17 . 1 299 . 27 LYS CD C 26.58 . 1 300 . 27 LYS CE C 39.80 . 1 301 . 27 LYS N N 117.99 . 1 302 . 28 GLN H H 8.82 . 1 303 . 28 GLN HA H 4.38 . 1 304 . 28 GLN HB2 H 2.19 . 2 305 . 28 GLN HB3 H 2.15 . 2 306 . 28 GLN HG2 H 2.58 . 2 307 . 28 GLN HG3 H 2.40 . 2 308 . 28 GLN HE21 H 7.64 . 2 309 . 28 GLN HE22 H 6.98 . 2 310 . 28 GLN CA C 55.22 . 1 311 . 28 GLN CB C 25.75 . 1 312 . 28 GLN CG C 32.09 . 1 313 . 28 GLN N N 115.24 . 1 314 . 28 GLN NE2 N 110.94 . 1 315 . 29 LEU H H 8.56 . 1 316 . 29 LEU HA H 4.67 . 1 317 . 29 LEU HB2 H 2.36 . 2 318 . 29 LEU HB3 H 2.24 . 2 319 . 29 LEU HG H 1.74 . 1 320 . 29 LEU HD1 H 1.03 . 2 321 . 29 LEU HD2 H 1.02 . 2 322 . 29 LEU CA C 52.74 . 1 323 . 29 LEU CB C 42.00 . 1 324 . 29 LEU CD1 C 24.93 . 2 325 . 29 LEU CD2 C 21.35 . 2 326 . 29 LEU N N 118.98 . 1 327 . 30 TYR H H 7.16 . 1 328 . 30 TYR HA H 4.54 . 1 329 . 30 TYR HB2 H 2.68 . 2 330 . 30 TYR HB3 H 2.36 . 2 331 . 30 TYR HD1 H 6.69 . 1 332 . 30 TYR HD2 H 6.69 . 1 333 . 30 TYR HE1 H 6.68 . 1 334 . 30 TYR HE2 H 6.68 . 1 335 . 30 TYR CA C 54.29 . 1 336 . 30 TYR CB C 37.86 . 1 337 . 30 TYR CD1 C 132.05 . 1 338 . 30 TYR CD2 C 132.05 . 1 339 . 30 TYR CE1 C 116.08 . 1 340 . 30 TYR CE2 C 116.08 . 1 341 . 30 TYR N N 111.50 . 1 342 . 31 GLU H H 8.64 . 1 343 . 31 GLU HA H 4.44 . 1 344 . 31 GLU HB2 H 1.82 . 2 345 . 31 GLU HB3 H 1.66 . 2 346 . 31 GLU HG2 H 2.12 . 1 347 . 31 GLU HG3 H 2.00 . 2 348 . 31 GLU CA C 55.22 . 1 349 . 31 GLU CB C 27.13 . 1 350 . 31 GLU CG C 34.84 . 1 351 . 31 GLU N N 118.65 . 1 352 . 32 GLN H H 7.43 . 1 353 . 32 GLN HA H 4.79 . 1 354 . 32 GLN HB2 H 1.71 . 2 355 . 32 GLN HB3 H 1.21 . 2 356 . 32 GLN HG2 H 1.90 . 2 357 . 32 GLN HG3 H 1.65 . 2 358 . 32 GLN HE21 H 6.37 . 2 359 . 32 GLN HE22 H 5.88 . 2 360 . 32 GLN CA C 52.19 . 1 361 . 32 GLN CB C 31.39 . 1 362 . 32 GLN CG C 32.09 . 1 363 . 32 GLN N N 115.79 . 1 364 . 32 GLN NE2 N 108.52 . 1 365 . 33 VAL H H 8.98 . 1 366 . 33 VAL HA H 5.53 . 1 367 . 33 VAL HB H 1.77 . 1 368 . 33 VAL HG1 H 1.05 . 2 369 . 33 VAL HG2 H 0.94 . 2 370 . 33 VAL CA C 57.42 . 1 371 . 33 VAL CB C 32.91 . 1 372 . 33 VAL CG1 C 17.49 . 2 373 . 33 VAL CG2 C 20.25 . 2 374 . 33 VAL N N 117.00 . 1 375 . 34 SER H H 9.72 . 1 376 . 34 SER HA H 5.23 . 1 377 . 34 SER HB2 H 4.19 . 2 378 . 34 SER HB3 H 3.68 . 2 379 . 34 SER CA C 57.42 . 1 380 . 34 SER CB C 65.41 . 1 381 . 34 SER N N 127.35 . 1 382 . 35 SER H H 8.73 . 1 383 . 35 SER HA H 4.35 . 1 384 . 35 SER HB2 H 4.27 . 2 385 . 35 SER HB3 H 3.02 . 2 386 . 35 SER CA C 56.77 . 1 387 . 35 SER CB C 61.51 . 1 388 . 35 SER N N 113.26 . 1 389 . 36 THR H H 8.98 . 1 390 . 36 THR HA H 4.70 . 1 391 . 36 THR HB H 4.07 . 1 392 . 36 THR HG2 H 1.16 . 1 393 . 36 THR CA C 61.28 . 1 394 . 36 THR CB C 66.78 . 1 395 . 36 THR CG2 C 21.90 . 1 396 . 36 THR N N 118.65 . 1 397 . 37 TRP H H 9.68 . 1 398 . 37 TRP HA H 4.78 . 1 399 . 37 TRP HB2 H 2.88 . 2 400 . 37 TRP HB3 H 2.60 . 2 401 . 37 TRP HD1 H 6.99 . 1 402 . 37 TRP HE1 H 8.55 . 1 403 . 37 TRP HE3 H 6.38 . 1 404 . 37 TRP HZ2 H 6.28 . 3 405 . 37 TRP HZ3 H 3.91 . 3 406 . 37 TRP HH2 H 6.07 . 1 407 . 37 TRP CA C 53.29 . 1 408 . 37 TRP CB C 29.61 . 1 409 . 37 TRP CD1 C 126.82 . 1 410 . 37 TRP CE3 C 117.45 . 1 411 . 37 TRP CZ2 C 111.40 . 3 412 . 37 TRP CZ3 C 117.50 . 3 413 . 37 TRP CH2 C 120.21 . 1 414 . 37 TRP N N 130.00 . 1 415 . 37 TRP NE1 N 126.47 . 1 416 . 38 HIS H H 8.02 . 1 417 . 38 HIS HA H 4.21 . 1 418 . 38 HIS HB2 H 3.14 . 2 419 . 38 HIS HB3 H 3.05 . 2 420 . 38 HIS HD2 H 7.29 . 1 421 . 38 HIS CA C 52.74 . 1 422 . 38 HIS CB C 29.88 . 1 423 . 38 HIS CD2 C 118.56 . 1 424 . 38 HIS N N 110.62 . 1 425 . 39 TRP H H 8.50 . 1 426 . 39 TRP HA H 5.22 . 1 427 . 39 TRP HB2 H 3.40 . 2 428 . 39 TRP HB3 H 3.01 . 2 429 . 39 TRP HD1 H 7.09 . 1 430 . 39 TRP HE1 H 9.88 . 1 431 . 39 TRP HE3 H 6.89 . 1 432 . 39 TRP HZ2 H 7.37 . 3 433 . 39 TRP HZ3 H 6.83 . 3 434 . 39 TRP HH2 H 6.77 . 1 435 . 39 TRP CA C 54.29 . 1 436 . 39 TRP CB C 28.22 . 1 437 . 39 TRP CD1 C 125.99 . 1 438 . 39 TRP CE3 C 119.38 . 1 439 . 39 TRP CZ2 C 112.22 . 1 440 . 39 TRP CZ3 C 121.04 . 1 441 . 39 TRP CH2 C 122.41 . 1 442 . 39 TRP N N 120.31 . 1 443 . 39 TRP NE1 N 128.01 . 1 444 . 40 THR H H 9.07 . 1 445 . 40 THR HA H 4.61 . 1 446 . 40 THR HB H 4.47 . 1 447 . 40 THR HG2 H 1.33 . 1 448 . 40 THR CA C 62.10 . 1 449 . 40 THR CB C 67.88 . 1 450 . 40 THR CG2 C 19.42 . 1 451 . 40 THR N N 117.33 . 1 452 . 41 CYS CA C 60.53 . 1 453 . 42 THR H H 8.39 . 1 454 . 42 THR HA H 4.43 . 1 455 . 42 THR HB H 4.37 . 1 456 . 42 THR HG2 H 1.30 . 1 457 . 42 THR CA C 60.73 . 1 458 . 42 THR CB C 67.88 . 1 459 . 42 THR CG2 C 19.70 . 1 460 . 42 THR N N 130.44 . 1 461 . 43 ASP H H 8.29 . 1 462 . 43 ASP HA H 4.65 . 1 463 . 43 ASP HB2 H 2.84 . 2 464 . 43 ASP HB3 H 2.73 . 2 465 . 43 ASP CA C 52.19 . 1 466 . 43 ASP CB C 39.25 . 1 467 . 43 ASP N N 120.42 . 1 468 . 44 GLY H H 8.19 . 1 469 . 44 GLY HA2 H 3.95 . 2 470 . 44 GLY HA3 H 3.84 . 2 471 . 44 GLY CA C 43.65 . 1 472 . 44 GLY N N 108.52 . 1 473 . 45 LYS H H 8.05 . 1 474 . 45 LYS HA H 4.26 . 1 475 . 45 LYS HB2 H 1.69 . 1 476 . 45 LYS HB3 H 1.69 . 1 477 . 45 LYS HG2 H 1.29 . 2 478 . 45 LYS HG3 H 1.25 . 2 479 . 45 LYS HD2 H 1.61 . 1 480 . 45 LYS HD3 H 1.61 . 1 481 . 45 LYS HE2 H 2.95 . 1 482 . 45 LYS HE3 H 2.95 . 1 483 . 45 LYS CA C 54.67 . 1 484 . 45 LYS CB C 30.71 . 1 485 . 45 LYS CG C 23.00 . 1 486 . 45 LYS CD C 26.86 . 1 487 . 45 LYS CE C 40.07 . 1 488 . 45 LYS N N 120.08 . 1 489 . 46 HIS H H 8.17 . 1 490 . 46 HIS HA H 4.67 . 1 491 . 46 HIS HB2 H 3.17 . 2 492 . 46 HIS HB3 H 3.10 . 2 493 . 46 HIS HD2 H 6.97 . 1 494 . 46 HIS CA C 54.39 . 1 495 . 46 HIS CB C 28.23 . 1 496 . 46 HIS CD2 C 118.30 . 1 497 . 46 HIS N N 118.87 . 1 498 . 47 LYS HA H 4.23 . 1 499 . 47 LYS HB2 H 1.84 . 2 500 . 47 LYS HB3 H 1.75 . 2 501 . 47 LYS HG2 H 1.39 . 2 502 . 47 LYS HG3 H 1.34 . 2 503 . 47 LYS HD2 H 1.67 . 1 504 . 47 LYS HD3 H 1.67 . 1 505 . 47 LYS HE2 H 2.99 . 1 506 . 47 LYS HE3 H 2.99 . 1 507 . 47 LYS CA C 54.94 . 1 508 . 47 LYS CB C 30.98 . 1 509 . 47 LYS CG C 23.00 . 1 510 . 47 LYS CD C 27.41 . 1 511 . 47 LYS CE C 40.07 . 1 512 . 48 ASN H H 8.00 . 1 513 . 48 ASN HA H 4.71 . 1 514 . 48 ASN HB2 H 2.73 . 1 515 . 48 ASN HB3 H 2.73 . 1 516 . 48 ASN HD21 H 7.46 . 2 517 . 48 ASN HD22 H 6.90 . 2 518 . 48 ASN CA C 51.09 . 1 519 . 48 ASN CB C 37.87 . 1 520 . 48 ASN N N 117.00 . 1 521 . 48 ASN ND2 N 112.48 . 1 522 . 49 ALA H H 8.23 . 1 523 . 49 ALA HA H 4.53 . 1 524 . 49 ALA HB H 1.28 . 1 525 . 49 ALA CA C 49.16 . 1 526 . 49 ALA CB C 18.87 . 1 527 . 49 ALA N N 124.27 . 1 528 . 50 ILE H H 8.46 . 1 529 . 50 ILE HA H 4.73 . 1 530 . 50 ILE HB H -1.12 . 1 531 . 50 ILE HG12 H 0.69 . 2 532 . 50 ILE HG13 H 0.02 . 2 533 . 50 ILE HG2 H -0.06 . 1 534 . 50 ILE HD1 H -0.62 . 1 535 . 50 ILE CA C 58.52 . 1 536 . 50 ILE CB C 38.97 . 1 537 . 50 ILE CG1 C 25.20 . 1 538 . 50 ILE CG2 C 15.84 . 1 539 . 50 ILE CD1 C 10.88 . 1 540 . 50 ILE N N 119.09 . 1 541 . 51 VAL H H 8.46 . 1 542 . 51 VAL HA H 3.93 . 1 543 . 51 VAL HB H 1.65 . 1 544 . 51 VAL HG1 H 0.87 . 2 545 . 51 VAL HG2 H 0.83 . 2 546 . 51 VAL CA C 60.17 . 1 547 . 51 VAL CB C 34.45 . 1 548 . 51 VAL CG1 C 20.25 . 2 549 . 51 VAL CG2 C 23.27 . 2 550 . 51 VAL N N 122.07 . 1 551 . 52 THR H H 9.20 . 1 552 . 52 THR HA H 5.50 . 1 553 . 52 THR HB H 3.63 . 1 554 . 52 THR HG2 H 1.39 . 1 555 . 52 THR CA C 59.90 . 1 556 . 52 THR CB C 68.99 . 1 557 . 52 THR CG2 C 21.07 . 1 558 . 52 THR N N 125.15 . 1 559 . 53 LEU H H 9.17 . 1 560 . 53 LEU HA H 5.50 . 1 561 . 53 LEU HB2 H 1.40 . 2 562 . 53 LEU HB3 H 1.12 . 2 563 . 53 LEU HG H 1.42 . 1 564 . 53 LEU HD1 H 0.64 . 2 565 . 53 LEU HD2 H 0.15 . 2 566 . 53 LEU CA C 53.29 . 1 567 . 53 LEU CB C 43.65 . 1 568 . 53 LEU CG C 27.68 . 1 569 . 53 LEU CD1 C 24.65 . 2 570 . 53 LEU CD2 C 25.20 . 2 571 . 53 LEU N N 126.91 . 1 572 . 54 THR H H 8.44 . 1 573 . 54 THR HA H 5.11 . 1 574 . 54 THR HB H 4.11 . 1 575 . 54 THR HG2 H 0.90 . 1 576 . 54 THR CA C 56.87 . 1 577 . 54 THR CB C 68.99 . 1 578 . 54 THR CG2 C 21.35 . 1 579 . 54 THR N N 108.41 . 1 580 . 55 TYR H H 7.33 . 1 581 . 55 TYR HA H 4.82 . 1 582 . 55 TYR HB2 H 3.67 . 2 583 . 55 TYR HB3 H 2.27 . 2 584 . 55 TYR HD1 H 6.78 . 1 585 . 55 TYR HD2 H 6.78 . 1 586 . 55 TYR HE1 H 6.33 . 1 587 . 55 TYR HE2 H 6.33 . 1 588 . 55 TYR CA C 55.49 . 1 589 . 55 TYR CB C 41.17 . 1 590 . 55 TYR CD1 C 130.94 . 1 591 . 55 TYR CD2 C 130.94 . 1 592 . 55 TYR CE1 C 115.25 . 1 593 . 55 TYR CE2 C 115.25 . 1 594 . 55 TYR N N 114.58 . 1 595 . 56 ILE H H 9.35 . 1 596 . 56 ILE HA H 4.26 . 1 597 . 56 ILE HB H 1.87 . 1 598 . 56 ILE HG12 H 1.50 . 2 599 . 56 ILE HG13 H 1.24 . 2 600 . 56 ILE HG2 H 0.96 . 1 601 . 56 ILE HD1 H 0.90 . 1 602 . 56 ILE CA C 59.62 . 1 603 . 56 ILE CB C 37.32 . 1 604 . 56 ILE CG1 C 26.03 . 1 605 . 56 ILE CG2 C 16.11 . 1 606 . 56 ILE CD1 C 11.98 . 1 607 . 56 ILE N N 117.99 . 1 608 . 57 SER H H 7.49 . 1 609 . 57 SER HA H 4.90 . 1 610 . 57 SER HB2 H 4.37 . 2 611 . 57 SER HB3 H 4.10 . 2 612 . 57 SER CA C 54.39 . 1 613 . 57 SER CB C 64.03 . 1 614 . 57 SER N N 110.06 . 1 615 . 58 THR HA H 3.80 . 1 616 . 58 THR HB H 4.43 . 1 617 . 58 THR HG2 H 1.38 . 1 618 . 58 THR CA C 63.75 . 1 619 . 58 THR CB C 65.68 . 1 620 . 58 THR CG2 C 20.80 . 1 621 . 59 SER H H 7.97 . 1 622 . 59 SER HA H 4.37 . 1 623 . 59 SER HB2 H 3.94 . 1 624 . 59 SER HB3 H 3.94 . 1 625 . 59 SER CA C 59.62 . 1 626 . 59 SER CB C 60.45 . 1 627 . 59 SER N N 118.21 . 1 628 . 60 GLN H H 7.96 . 1 629 . 60 GLN HA H 4.22 . 1 630 . 60 GLN HB2 H 2.55 . 1 631 . 60 GLN HB3 H 2.55 . 1 632 . 60 GLN HG2 H 2.06 . 1 633 . 60 GLN HG3 H 2.06 . 1 634 . 60 GLN CA C 57.06 . 1 635 . 60 GLN CB C 27.75 . 1 636 . 60 GLN N N 123.94 . 1 637 . 61 ARG H H 7.19 . 1 638 . 61 ARG HA H 3.13 . 1 639 . 61 ARG HB2 H 1.99 . 1 640 . 61 ARG HB3 H 1.99 . 1 641 . 61 ARG HG2 H 0.46 . 1 642 . 61 ARG HG3 H 0.46 . 1 643 . 61 ARG HD2 H 2.90 . 1 644 . 61 ARG HD3 H 2.24 . 1 645 . 61 ARG CA C 57.69 . 1 646 . 61 ARG N N 118.32 . 1 647 . 62 ASP H H 8.29 . 1 648 . 62 ASP HA H 4.37 . 1 649 . 62 ASP HB2 H 2.93 . 2 650 . 62 ASP HB3 H 2.64 . 2 651 . 62 ASP CA C 55.77 . 1 652 . 62 ASP CB C 37.87 . 1 653 . 62 ASP N N 119.75 . 1 654 . 63 ASP H H 8.17 . 1 655 . 63 ASP HA H 4.50 . 1 656 . 63 ASP HB2 H 3.05 . 2 657 . 63 ASP HB3 H 2.77 . 2 658 . 63 ASP CA C 55.77 . 1 659 . 63 ASP CB C 38.42 . 1 660 . 63 ASP N N 121.63 . 1 661 . 64 PHE H H 9.02 . 1 662 . 64 PHE HA H 4.05 . 1 663 . 64 PHE HB2 H 4.14 . 2 664 . 64 PHE HB3 H 3.79 . 2 665 . 64 PHE HD1 H 7.37 . 1 666 . 64 PHE HD2 H 7.37 . 1 667 . 64 PHE HE1 H 7.16 . 1 668 . 64 PHE HE2 H 7.16 . 1 669 . 64 PHE HZ H 7.00 . 1 670 . 64 PHE CA C 60.73 . 1 671 . 64 PHE CB C 35.94 . 1 672 . 64 PHE CD1 C 131.22 . 1 673 . 64 PHE CD2 C 131.22 . 1 674 . 64 PHE CE1 C 129.84 . 1 675 . 64 PHE CE2 C 129.84 . 1 676 . 64 PHE CZ C 128.19 . 1 677 . 64 PHE N N 123.06 . 1 678 . 65 LEU H H 8.55 . 1 679 . 65 LEU HA H 4.14 . 1 680 . 65 LEU HB2 H 2.05 . 2 681 . 65 LEU HB3 H 1.53 . 2 682 . 65 LEU HG H 1.92 . 1 683 . 65 LEU HD1 H 1.01 . 2 684 . 65 LEU HD2 H 0.90 . 2 685 . 65 LEU CA C 55.22 . 1 686 . 65 LEU CB C 39.80 . 1 687 . 65 LEU CG C 25.75 . 1 688 . 65 LEU CD1 C 20.52 . 2 689 . 65 LEU CD2 C 23.82 . 2 690 . 65 LEU N N 119.42 . 1 691 . 66 ASN H H 8.10 . 1 692 . 66 ASN HA H 4.70 . 1 693 . 66 ASN HB2 H 2.90 . 1 694 . 66 ASN HB3 H 2.90 . 1 695 . 66 ASN HD21 H 7.69 . 2 696 . 66 ASN HD22 H 6.84 . 2 697 . 66 ASN CA C 52.46 . 1 698 . 66 ASN CB C 37.59 . 1 699 . 66 ASN N N 115.35 . 1 700 . 66 ASN ND2 N 113.03 . 1 701 . 67 THR H H 7.60 . 1 702 . 67 THR HA H 4.14 . 1 703 . 67 THR HB H 3.76 . 1 704 . 67 THR HG2 H 1.06 . 1 705 . 67 THR CA C 63.20 . 1 706 . 67 THR CB C 68.44 . 1 707 . 67 THR CG2 C 19.14 . 1 708 . 67 THR N N 114.91 . 1 709 . 68 VAL H H 7.92 . 1 710 . 68 VAL HA H 3.12 . 1 711 . 68 VAL HB H 1.02 . 1 712 . 68 VAL HG1 H 0.20 . 2 713 . 68 VAL HG2 H -0.24 . 2 714 . 68 VAL CA C 61.28 . 1 715 . 68 VAL CB C 29.33 . 1 716 . 68 VAL CG1 C 18.32 . 2 717 . 68 VAL CG2 C 18.59 . 2 718 . 68 VAL N N 121.63 . 1 719 . 69 LYS H H 7.96 . 1 720 . 69 LYS HA H 4.22 . 1 721 . 69 LYS HB2 H 1.71 . 2 722 . 69 LYS HB3 H 1.65 . 2 723 . 69 LYS HG2 H 1.39 . 2 724 . 69 LYS HG3 H 1.31 . 2 725 . 69 LYS HD2 H 1.61 . 1 726 . 69 LYS HD3 H 1.61 . 1 727 . 69 LYS HE2 H 2.97 . 1 728 . 69 LYS HE3 H 2.97 . 1 729 . 69 LYS CA C 53.56 . 1 730 . 69 LYS CB C 29.33 . 1 731 . 69 LYS CG C 22.72 . 1 732 . 69 LYS CD C 26.86 . 1 733 . 69 LYS CE C 40.07 . 1 734 . 69 LYS N N 125.70 . 1 735 . 70 ILE H H 8.54 . 1 736 . 70 ILE HA H 4.37 . 1 737 . 70 ILE HB H 1.89 . 1 738 . 70 ILE HG12 H 1.45 . 2 739 . 70 ILE HG13 H 1.23 . 2 740 . 70 ILE HG2 H 0.93 . 1 741 . 70 ILE HD1 H 0.76 . 1 742 . 70 ILE CA C 54.94 . 1 743 . 70 ILE CB C 37.04 . 1 744 . 70 ILE CG1 C 25.20 . 1 745 . 70 ILE CG2 C 15.01 . 1 746 . 70 ILE CD1 C 9.51 . 1 747 . 70 ILE N N 128.01 . 1 748 . 71 PRO HA H 4.53 . 1 749 . 71 PRO HB2 H 2.46 . 2 750 . 71 PRO HB3 H 2.02 . 2 751 . 71 PRO HG2 H 2.05 . 2 752 . 71 PRO HG3 H 1.96 . 2 753 . 71 PRO HD2 H 3.44 . 2 754 . 71 PRO HD3 H 3.85 . 2 755 . 71 PRO CA C 61.00 . 1 756 . 71 PRO CB C 30.98 . 1 757 . 71 PRO CG C 25.48 . 1 758 . 71 PRO CD C 49.43 . 1 759 . 72 ASN H H 8.13 . 1 760 . 72 ASN HA H 4.58 . 1 761 . 72 ASN HB2 H 3.07 . 2 762 . 72 ASN HB3 H 2.94 . 2 763 . 72 ASN HD21 H 7.63 . 2 764 . 72 ASN HD22 H 6.90 . 2 765 . 72 ASN CA C 53.29 . 1 766 . 72 ASN CB C 35.67 . 1 767 . 72 ASN N N 126.69 . 1 768 . 72 ASN ND2 N 111.49 . 1 769 . 73 THR H H 7.28 . 1 770 . 73 THR HA H 4.18 . 1 771 . 73 THR HB H 4.49 . 1 772 . 73 THR HG2 H 1.29 . 1 773 . 73 THR CA C 59.62 . 1 774 . 73 THR CB C 66.69 . 1 775 . 73 THR CG2 C 20.80 . 1 776 . 73 THR N N 107.20 . 1 777 . 74 VAL H H 7.85 . 1 778 . 74 VAL HA H 4.59 . 1 779 . 74 VAL HB H 2.04 . 1 780 . 74 VAL HG1 H 0.74 . 1 781 . 74 VAL HG2 H 0.74 . 1 782 . 74 VAL CA C 59.07 . 1 783 . 74 VAL CB C 32.09 . 1 784 . 74 VAL CG1 C 20.80 . 1 785 . 74 VAL CG2 C 20.80 . 1 786 . 74 VAL N N 123.94 . 1 787 . 75 SER H H 9.01 . 1 788 . 75 SER HA H 4.78 . 1 789 . 75 SER HB2 H 3.92 . 1 790 . 75 SER HB3 H 3.86 . 1 791 . 75 SER CA C 55.22 . 1 792 . 75 SER CB C 62.65 . 1 793 . 75 SER N N 120.75 . 1 794 . 76 VAL H H 8.66 . 1 795 . 76 VAL HA H 4.73 . 1 796 . 76 VAL HB H 2.05 . 1 797 . 76 VAL HG1 H 0.95 . 1 798 . 76 VAL HG2 H 0.91 . 1 799 . 76 VAL CA C 59.90 . 1 800 . 76 VAL CB C 32.36 . 1 801 . 76 VAL CG1 C 19.97 . 2 802 . 76 VAL CG2 C 19.42 . 2 803 . 76 VAL N N 124.71 . 1 804 . 77 SER H H 8.85 . 1 805 . 77 SER HA H 5.11 . 1 806 . 77 SER HB2 H 4.01 . 2 807 . 77 SER HB3 H 3.80 . 2 808 . 77 SER CA C 54.94 . 1 809 . 77 SER CB C 63.48 . 1 810 . 77 SER N N 122.73 . 1 811 . 78 THR H H 8.62 . 1 812 . 78 THR HA H 4.85 . 1 813 . 78 THR HB H 4.06 . 1 814 . 78 THR HG2 H 1.12 . 1 815 . 78 THR CA C 57.97 . 1 816 . 78 THR CB C 68.44 . 1 817 . 78 THR CG2 C 20.25 . 1 818 . 78 THR N N 114.36 . 1 819 . 79 GLY H H 7.50 . 1 820 . 79 GLY HA2 H 4.34 . 2 821 . 79 GLY HA3 H 4.16 . 2 822 . 79 GLY CA C 44.20 . 1 823 . 79 GLY N N 107.75 . 1 824 . 80 TYR H H 8.96 . 1 825 . 80 TYR HA H 5.46 . 1 826 . 80 TYR HB2 H 2.97 . 2 827 . 80 TYR HB3 H 2.64 . 2 828 . 80 TYR HD1 H 6.88 . 1 829 . 80 TYR HD2 H 6.88 . 1 830 . 80 TYR HE1 H 6.79 . 1 831 . 80 TYR HE2 H 6.79 . 1 832 . 80 TYR CA C 55.22 . 1 833 . 80 TYR CB C 41.45 . 1 834 . 80 TYR CD1 C 131.77 . 1 835 . 80 TYR CD2 C 131.77 . 1 836 . 80 TYR CE1 C 116.07 . 1 837 . 80 TYR CE2 C 116.07 . 1 838 . 80 TYR N N 119.86 . 1 839 . 81 MET H H 9.18 . 1 840 . 81 MET HA H 5.36 . 1 841 . 81 MET HB2 H 2.17 . 1 842 . 81 MET HB3 H 2.13 . 1 843 . 81 MET HG2 H 2.76 . 1 844 . 81 MET HG3 H 2.57 . 1 845 . 81 MET HE H 2.29 . 1 846 . 81 MET CA C 53.29 . 1 847 . 81 MET CB C 36.22 . 1 848 . 81 MET CG C 29.33 . 1 849 . 81 MET CE C 14.74 . 1 850 . 81 MET N N 119.20 . 1 851 . 82 THR H H 8.94 . 1 852 . 82 THR HA H 5.16 . 1 853 . 82 THR HB H 4.02 . 1 854 . 82 THR HG2 H 1.39 . 1 855 . 82 THR CA C 60.45 . 1 856 . 82 THR CB C 68.71 . 1 857 . 82 THR CG2 C 19.70 . 1 858 . 82 THR N N 122.84 . 1 859 . 83 ILE H H 8.31 . 1 860 . 83 ILE HA H 4.33 . 1 861 . 83 ILE HB H 1.88 . 1 862 . 83 ILE HG12 H 1.48 . 2 863 . 83 ILE HG13 H 1.23 . 2 864 . 83 ILE HG2 H 0.96 . 1 865 . 83 ILE HD1 H 0.65 . 1 866 . 83 ILE CA C 60.73 . 1 867 . 83 ILE CB C 38.15 . 1 868 . 83 ILE CG1 C 26.03 . 1 869 . 83 ILE CG2 C 16.11 . 1 870 . 83 ILE CD1 C 11.71 . 1 871 . 83 ILE N N 130.44 . 1 stop_ save_