data_4127 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C, and 15N Resonance Assignment of the Origin DNA-binding Domain of SV40 T Antigen ; _BMRB_accession_number 4127 _BMRB_flat_file_name bmr4127.str _Entry_type original _Submission_date 1998-03-20 _Accession_date 1998-03-20 _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 Luo Xuelian . . 2 Sanford David G. . 3 Bullock Peter A. . 4 Bachovchin William W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 743 "13C chemical shifts" 475 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-03-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6535 'Tag-OBD (131-259) - RPA32C complex' stop_ _Original_release_date 1999-03-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Luo, X., Sanford, D. G., Bullock, P. A., Bachovchin, W. W., "Solution Structure of the Origin DNA-binding Domain of SV40 T-antigen," Nature Struct. Biol. 3, 1034-1039, (1996). ; _Citation_title 'Solution Structure of the Origin DNA-binding Domain of SV40 T-antigen' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 97102430 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Luo Xuelian . . 2 Sanford David G. . 3 Bullock Peter A. . 4 Bachovchin William W. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 3 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1034 _Page_last 1039 _Year 1996 _Details ; The data reported here represents the origin DNA-binding domain (residues 131-260) of simian virus 40 large T antigen. ; loop_ _Keyword 'NMR structure' 'resonance assignment' 'SV40 T antigen DNA-binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_T-Ag_OBD _Saveframe_category molecular_system _Mol_system_name 'Origin DNA-binding domain of SV40 T-antigen' _Abbreviation_common T-Ag_OBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label T-Ag_OBD $T-Ag_OBD stop_ _System_molecular_weight 15390 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_T-Ag_OBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Origin DNA-binding domain of SV40 T-antigen' _Abbreviation_common T-Ag_OBD _Molecular_mass 15390 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; GSKVEDPKDFPSELLSFLSH AVFSNRTLACFAIYTTKEKA ALLYKKIMEKYSVTFISRHN SYNHNILFFLTPHRHRVSAI NNYAQKLCTFSFLICKGVNK EYLMYSALTRDPFSVIEESL PGGLKEHDFNPESS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 131 LYS 4 132 VAL 5 133 GLU 6 134 ASP 7 135 PRO 8 136 LYS 9 137 ASP 10 138 PHE 11 139 PRO 12 140 SER 13 141 GLU 14 142 LEU 15 143 LEU 16 144 SER 17 145 PHE 18 146 LEU 19 147 SER 20 148 HIS 21 149 ALA 22 150 VAL 23 151 PHE 24 152 SER 25 153 ASN 26 154 ARG 27 155 THR 28 156 LEU 29 157 ALA 30 158 CYS 31 159 PHE 32 160 ALA 33 161 ILE 34 162 TYR 35 163 THR 36 164 THR 37 165 LYS 38 166 GLU 39 167 LYS 40 168 ALA 41 169 ALA 42 170 LEU 43 171 LEU 44 172 TYR 45 173 LYS 46 174 LYS 47 175 ILE 48 176 MET 49 177 GLU 50 178 LYS 51 179 TYR 52 180 SER 53 181 VAL 54 182 THR 55 183 PHE 56 184 ILE 57 185 SER 58 186 ARG 59 187 HIS 60 188 ASN 61 189 SER 62 190 TYR 63 191 ASN 64 192 HIS 65 193 ASN 66 194 ILE 67 195 LEU 68 196 PHE 69 197 PHE 70 198 LEU 71 199 THR 72 200 PRO 73 201 HIS 74 202 ARG 75 203 HIS 76 204 ARG 77 205 VAL 78 206 SER 79 207 ALA 80 208 ILE 81 209 ASN 82 210 ASN 83 211 TYR 84 212 ALA 85 213 GLN 86 214 LYS 87 215 LEU 88 216 CYS 89 217 THR 90 218 PHE 91 219 SER 92 220 PHE 93 221 LEU 94 222 ILE 95 223 CYS 96 224 LYS 97 225 GLY 98 226 VAL 99 227 ASN 100 228 LYS 101 229 GLU 102 230 TYR 103 231 LEU 104 232 MET 105 233 TYR 106 234 SER 107 235 ALA 108 236 LEU 109 237 THR 110 238 ARG 111 239 ASP 112 240 PRO 113 241 PHE 114 242 SER 115 243 VAL 116 244 ILE 117 245 GLU 118 246 GLU 119 247 SER 120 248 LEU 121 249 PRO 122 250 GLY 123 251 GLY 124 252 LEU 125 253 LYS 126 254 GLU 127 255 HIS 128 256 ASP 129 257 PHE 130 258 ASN 131 259 PRO 132 260 GLU 133 . SER 134 . SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 1TBD "Solution Structure Of The Origin Dna Binding Domain Of Sv40 T-Antigen, Nmr, Minimized Average Structure" 100.00 134 100.00 100.00 1.30e-92 PDB 1Z1D "Structural Model For The Interaction Between Rpa32 C- Terminal Domain And Sv40 T Antigen Origin Binding Domain" 97.76 131 100.00 100.00 1.29e-90 PDB 2FUF "Crystal Structure Of The Sv40 Large T Antigen Origin-Binding Domain" 100.00 134 98.51 98.51 2.30e-90 PDB 2IF9 "Crystal Structure Of Sv40 T-Antigen Origin Binding Domain Disulfide-Linked Dimer" 100.00 134 100.00 100.00 1.30e-92 PDB 2IPR "Origin Binding Domain Of The Sv40 Large T Antigen (Residues 131-259). P21 Crystal Form" 96.27 133 100.00 100.00 6.21e-89 PDB 2ITJ "Origin Binding Domain Of The Sv40 Large T Antigen (Residues 131-259). P212121 Crystal Form" 96.27 133 100.00 100.00 6.21e-89 PDB 2ITL "The Origin Binding Domain Of The Sv40 Large T Antigen Bound To The Functional Pen Palindrome Dna (23 Bp)" 96.27 133 100.00 100.00 6.21e-89 PDB 2NL8 "The Origin Binding Domain Of The Sv40 Large T Antigen Bound Non Specifically To A 17 Bp Palindrome Dna (Sites 1 And 3)" 96.27 133 99.22 99.22 1.25e-87 PDB 2NTC "Crystal Structure Of Sv40 Large T Antigen Origin Binding Domain With Dna" 100.00 134 100.00 100.00 1.30e-92 PDB 2TBD "Sv40 T Antigen Dna-Binding Domain, Nmr, 30 Structures" 100.00 134 100.00 100.00 1.30e-92 PDB 3QK2 "Structure-Based Analysis Of The Interaction Between The Simian Virus 40 T-Antigen Origin Binding Domain And Single-Stranded Dna" 100.00 134 99.25 99.25 3.43e-91 PDB 3QN2 "Structure-Based Design Of A Disulfide-Linked Oligomeric Form Of The Simian Virus 40 (Sv40) Large T Antigen Dna Binding Domain" 100.00 134 97.76 97.76 2.20e-88 PDB 4FGN "Crystal Structure Of The Sv40 Large T-antigen Origin Bining Domain Bound To Site I Dna" 98.51 132 100.00 100.00 2.37e-91 PDB 4GDF "A Crystal Structure Of Sv40 Large T Antigen" 98.51 497 98.48 99.24 1.10e-86 PDB 5D9I "Sv40 Large T Antigen Origin Binding Domain Bound To Artificial Dna Fork" 100.00 134 99.25 99.25 3.43e-91 EMBL CAB82893 "large T antigen [Simian virus 40]" 98.51 711 98.48 99.24 1.17e-84 EMBL CBL79143 "large T antigen [Simian virus 40]" 97.01 701 98.46 100.00 5.01e-84 GB AAB59924 "large T antigen [Simian virus 40]" 98.51 708 98.48 99.24 1.07e-84 GB AAC59346 "large tumor antigen T-ag [Simian virus 40]" 98.51 707 98.48 99.24 1.07e-84 GB AAD38846 "large tumor antigen [Simian virus 40]" 98.51 709 98.48 99.24 1.06e-84 GB AAD38993 "large tumor antigen [Simian virus 40]" 98.51 709 98.48 99.24 1.06e-84 GB AAD39001 "large tumor antigen [Simian virus 40]" 98.51 711 98.48 99.24 1.17e-84 REF YP_003708382 "large T antigen [Simian virus 40]" 98.51 708 98.48 99.24 1.07e-84 SP P03070 "RecName: Full=Large T antigen; Short=LT; Short=LT-AG" 98.51 708 98.48 99.24 1.22e-84 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $T-Ag_OBD 'simian virus 40' 10633 . . Polyomavirus 'Simian virus 40' 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 $T-Ag_OBD 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pGEX-1lamdaT 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 $T-Ag_OBD 3 mM [U-15N;U-13C] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 na temperature 303 1 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 DSS C 13 'methyl carbon' ppm 0.00 . . . . . H2O H 1 protons ppm 4.72 . . . . . 'liquid NH3' N 15 nitrogen ppm 0.00 . . . . . 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 stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name T-Ag_OBD _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 . 3 LYS H H 8.42 0.01 1 2 . 3 LYS HA H 4.34 0.01 1 3 . 3 LYS HB2 H 1.77 0.01 2 4 . 3 LYS HB3 H 1.71 0.01 2 5 . 3 LYS HG2 H 1.37 0.01 2 6 . 3 LYS HG3 H 1.33 0.01 2 7 . 3 LYS HD2 H 1.62 0.01 2 8 . 3 LYS HE2 H 2.95 0.01 2 9 . 3 LYS C C 171.2 0.1 1 10 . 3 LYS CA C 53.5 0.1 1 11 . 3 LYS N N 119.3 0.1 1 12 . 4 VAL H H 8.23 0.01 1 13 . 4 VAL HA H 4.04 0.01 1 14 . 4 VAL HB H 1.97 0.01 1 15 . 4 VAL HG1 H 0.87 0.01 1 16 . 4 VAL HG2 H 0.87 0.01 1 17 . 4 VAL C C 173.4 0.1 1 18 . 4 VAL CA C 59.3 0.1 1 19 . 4 VAL CB C 29.5 0.1 1 20 . 4 VAL CG1 C 17.50 0.01 1 21 . 4 VAL CG2 C 17.50 0.01 1 22 . 4 VAL N N 118.5 0.1 1 23 . 5 GLU H H 8.43 0.01 1 24 . 5 GLU HA H 4.23 0.01 1 25 . 5 GLU HB2 H 2.18 0.01 2 26 . 5 GLU HB3 H 2.13 0.01 2 27 . 5 GLU HG2 H 1.87 0.01 2 28 . 5 GLU HG3 H 1.73 0.01 2 29 . 5 GLU C C 172.9 0.1 1 30 . 5 GLU CA C 52.9 0.1 1 31 . 5 GLU N N 121.0 0.1 1 32 . 6 ASP H H 8.28 0.01 1 33 . 6 ASP HA H 4.35 0.01 1 34 . 6 ASP HB2 H 2.15 0.01 2 35 . 6 ASP HB3 H 1.81 0.01 2 36 . 6 ASP C C 173.1 0.1 1 37 . 6 ASP CA C 49.7 0.1 1 38 . 6 ASP CB C 36.2 0.1 1 39 . 6 ASP N N 119.5 0.1 1 40 . 7 PRO HA H 4.08 0.01 1 41 . 7 PRO HG2 H 1.48 0.01 2 42 . 7 PRO HG3 H 0.82 0.01 2 43 . 7 PRO HD2 H 3.04 0.01 2 44 . 7 PRO HD3 H 0.99 0.01 2 45 . 7 PRO CA C 59.8 0.1 1 46 . 7 PRO CD C 46.3 0.1 1 47 . 8 LYS H H 8.45 0.01 1 48 . 8 LYS HA H 4.25 0.01 1 49 . 8 LYS HB2 H 1.64 0.01 2 50 . 8 LYS HB3 H 1.58 0.01 2 51 . 8 LYS HG2 H 1.36 0.01 2 52 . 8 LYS HG3 H 1.77 0.01 2 53 . 8 LYS HD2 H 1.92 0.01 2 54 . 8 LYS HD3 H 1.79 0.01 2 55 . 8 LYS HE2 H 2.94 0.01 2 56 . 8 LYS HE3 H 2.16 0.01 2 57 . 8 LYS C C 172.4 0.1 1 58 . 8 LYS CA C 52.4 0.1 1 59 . 8 LYS N N 113.4 0.1 1 60 . 9 ASP H H 7.79 0.01 1 61 . 9 ASP HA H 4.72 0.01 1 62 . 9 ASP HB2 H 2.76 0.01 2 63 . 9 ASP HB3 H 2.52 0.01 2 64 . 9 ASP C C 172.8 0.1 1 65 . 9 ASP CA C 48.8 0.1 1 66 . 9 ASP CB C 40.9 0.1 1 67 . 9 ASP N N 112.7 0.1 1 68 . 10 PHE H H 10.33 0.01 1 69 . 10 PHE HA H 4.11 0.01 1 70 . 10 PHE HB2 H 2.51 0.01 2 71 . 10 PHE HD1 H 7.03 0.01 3 72 . 10 PHE HE1 H 7.00 0.01 3 73 . 10 PHE C C 172.9 0.1 1 74 . 10 PHE CA C 55.4 0.1 1 75 . 10 PHE CB C 36.6 0.1 9 76 . 10 PHE N N 115.3 0.1 1 77 . 11 PRO HA H 4.38 0.01 1 78 . 11 PRO HB2 H 2.67 0.01 2 79 . 11 PRO HG2 H 2.19 0.01 2 80 . 11 PRO HG3 H 2.11 0.01 2 81 . 11 PRO HD2 H 3.20 0.01 2 82 . 11 PRO HD3 H 3.14 0.01 2 83 . 11 PRO CA C 60.4 0.1 1 84 . 11 PRO CG C 23.8 0.1 9 85 . 11 PRO CD C 47.7 0.1 1 86 . 12 SER H H 8.45 0.01 1 87 . 12 SER HA H 3.91 0.01 1 88 . 12 SER HB2 H 3.88 0.01 2 89 . 12 SER C C 174.3 0.1 1 90 . 12 SER CA C 58.9 0.1 1 91 . 12 SER CB C 60.0 0.1 1 92 . 12 SER N N 115.0 0.1 1 93 . 13 GLU H H 10.82 0.01 1 94 . 13 GLU HA H 4.08 0.01 1 95 . 13 GLU HB2 H 2.20 0.01 2 96 . 13 GLU HB3 H 2.12 0.01 2 97 . 13 GLU HG2 H 2.54 0.01 2 98 . 13 GLU HG3 H 2.42 0.01 2 99 . 13 GLU C C 173.1 0.1 1 100 . 13 GLU CA C 56.6 0.1 1 101 . 13 GLU CG C 33.6 0.1 1 102 . 13 GLU N N 117.2 0.1 1 103 . 14 LEU H H 8.08 0.01 1 104 . 14 LEU HA H 4.46 0.01 1 105 . 14 LEU HB2 H 1.53 0.01 2 106 . 14 LEU HB3 H 0.91 0.01 2 107 . 14 LEU HG H 1.43 0.01 1 108 . 14 LEU HD1 H 0.58 0.01 2 109 . 14 LEU HD2 H 0.43 0.01 2 110 . 14 LEU C C 174.6 0.1 1 111 . 14 LEU CA C 50.5 0.1 1 112 . 14 LEU CD1 C 18.3 0.1 2 113 . 14 LEU CD2 C 24.4 0.1 2 114 . 14 LEU N N 111.5 0.1 1 115 . 15 LEU H H 6.98 0.01 1 116 . 15 LEU HA H 3.64 0.01 1 117 . 15 LEU HB2 H 1.70 0.01 2 118 . 15 LEU HB3 H 1.39 0.01 2 119 . 15 LEU HG H 1.75 0.01 1 120 . 15 LEU HD1 H 0.83 0.01 2 121 . 15 LEU HD2 H 0.73 0.01 2 122 . 15 LEU C C 174.4 0.1 1 123 . 15 LEU CA C 55.7 0.1 1 124 . 15 LEU CB C 38.4 0.1 1 125 . 15 LEU CD1 C 22.0 0.1 2 126 . 15 LEU CD2 C 20.3 0.1 2 127 . 15 LEU N N 111.8 0.1 1 128 . 16 SER H H 8.16 0.01 1 129 . 16 SER HA H 4.18 0.01 1 130 . 16 SER HB2 H 3.51 0.01 2 131 . 16 SER C C 176.7 0.1 1 132 . 16 SER CA C 57.4 0.1 1 133 . 16 SER CB C 59.3 0.1 1 134 . 16 SER N N 107.8 0.1 1 135 . 17 PHE H H 7.16 0.01 1 136 . 17 PHE HA H 4.72 0.01 1 137 . 17 PHE HB2 H 3.53 0.01 2 138 . 17 PHE HB3 H 2.96 0.01 2 139 . 17 PHE HD1 H 6.98 0.01 3 140 . 17 PHE HE1 H 7.15 0.01 3 141 . 17 PHE HZ H 6.98 0.01 1 142 . 17 PHE C C 172.1 0.1 1 143 . 17 PHE CA C 52.1 0.1 1 144 . 17 PHE CB C 36.7 0.1 1 145 . 17 PHE CD1 C 127.7 0.1 3 146 . 17 PHE CE1 C 128.9 0.1 3 147 . 17 PHE N N 114.1 0.1 1 148 . 18 LEU H H 7.08 0.01 1 149 . 18 LEU HA H 4.45 0.01 1 150 . 18 LEU HB2 H 1.28 0.01 2 151 . 18 LEU HB3 H 0.96 0.01 2 152 . 18 LEU HG H 1.55 0.01 1 153 . 18 LEU HD1 H 0.22 0.01 2 154 . 18 LEU HD2 H 0.03 0.01 2 155 . 18 LEU C C 173.0 0.1 1 156 . 18 LEU CA C 50.7 0.1 1 157 . 18 LEU CB C 41.3 0.1 1 158 . 18 LEU CD1 C 20.3 0.1 2 159 . 18 LEU CD2 C 23.8 0.1 2 160 . 18 LEU N N 113.9 0.1 1 161 . 19 SER H H 8.11 0.01 1 162 . 19 SER HA H 4.34 0.01 1 163 . 19 SER HB2 H 3.51 0.01 2 164 . 19 SER HB3 H 3.41 0.01 2 165 . 19 SER C C 172.2 0.1 1 166 . 19 SER CA C 53.8 0.1 1 167 . 19 SER CB C 59.8 0.1 1 168 . 19 SER N N 108.4 0.1 1 169 . 20 HIS H H 4.60 0.01 1 170 . 20 HIS HB2 H 3.28 0.01 2 171 . 20 HIS HB3 H 2.85 0.01 2 172 . 20 HIS HD2 H 7.01 0.01 1 173 . 20 HIS HE1 H 7.54 0.01 1 174 . 20 HIS CA C 53.5 0.1 1 175 . 20 HIS CB C 27.9 0.1 1 176 . 20 HIS CD2 C 116.2 0.1 1 177 . 20 HIS CE1 C 134.8 0.1 1 178 . 21 ALA H H 7.66 0.01 1 179 . 21 ALA HA H 4.53 0.01 1 180 . 21 ALA HB H 1.27 0.01 1 181 . 21 ALA CA C 48.6 0.1 1 182 . 21 ALA CB C 14.9 0.1 1 183 . 21 ALA N N 120.8 0.1 1 184 . 22 VAL H H 8.24 0.01 1 185 . 22 VAL HA H 3.94 0.01 1 186 . 22 VAL HB H 1.97 0.01 1 187 . 22 VAL HG1 H 0.78 0.01 1 188 . 22 VAL HG2 H 0.63 0.01 1 189 . 22 VAL C C 175.2 0.1 1 190 . 22 VAL CA C 61.0 0.1 1 191 . 22 VAL CB C 28.7 0.1 1 192 . 22 VAL CG1 C 18.60 0.01 1 193 . 22 VAL CG2 C 16.50 0.01 1 194 . 22 VAL N N 116.4 0.1 1 195 . 23 PHE H H 8.32 0.01 1 196 . 23 PHE HA H 4.82 0.01 1 197 . 23 PHE HB2 H 2.95 0.01 1 198 . 23 PHE HB3 H 3.32 0.01 1 199 . 23 PHE HD1 H 7.25 0.01 3 200 . 23 PHE HE1 H 7.32 0.01 3 201 . 23 PHE C C 173.5 0.1 1 202 . 23 PHE CA C 54.1 0.1 1 203 . 23 PHE CB C 35.5 0.1 1 204 . 23 PHE CD1 C 128.9 0.1 3 205 . 23 PHE CE1 C 128.9 0.1 3 206 . 23 PHE N N 116.0 0.1 1 207 . 24 SER H H 7.76 0.01 1 208 . 24 SER HA H 4.40 0.01 1 209 . 24 SER HB2 H 4.05 0.01 2 210 . 24 SER HB3 H 3.79 0.01 2 211 . 24 SER C C 172.7 0.1 1 212 . 24 SER CA C 55.5 0.1 1 213 . 24 SER CB C 61.9 0.1 1 214 . 24 SER N N 111.1 0.1 1 215 . 25 ASN HA H 4.70 0.01 1 216 . 25 ASN HB2 H 2.82 0.01 2 217 . 25 ASN HD21 H 7.57 0.01 1 218 . 25 ASN HD22 H 6.93 0.01 1 219 . 25 ASN CA C 50.1 0.1 1 220 . 25 ASN ND2 N 108.2 0.1 1 221 . 26 ARG H H 8.08 0.01 1 222 . 26 ARG HA H 4.28 0.01 1 223 . 26 ARG HB2 H 1.73 0.01 2 224 . 26 ARG HG2 H 1.54 0.01 2 225 . 26 ARG HD2 H 3.15 0.01 2 226 . 26 ARG C C 172.1 0.1 1 227 . 26 ARG CA C 53.5 0.1 1 228 . 26 ARG N N 116.9 0.1 1 229 . 27 THR H H 8.39 0.01 1 230 . 27 THR HA H 4.53 0.01 1 231 . 27 THR HB H 3.91 0.01 1 232 . 27 THR HG2 H 1.09 0.01 1 233 . 27 THR C C 172.8 0.1 1 234 . 27 THR CA C 56.6 0.1 1 235 . 27 THR CB C 67.0 0.1 1 236 . 27 THR CG2 C 18.9 0.1 1 237 . 27 THR N N 110.3 0.1 1 238 . 28 LEU H H 8.88 0.01 1 239 . 28 LEU HA H 4.65 0.01 1 240 . 28 LEU HB2 H 1.41 0.01 2 241 . 28 LEU HB3 H 1.34 0.01 2 242 . 28 LEU HG H 1.45 0.01 1 243 . 28 LEU HD1 H 0.75 0.01 2 244 . 28 LEU HD2 H 0.70 0.01 2 245 . 28 LEU C C 171.0 0.1 1 246 . 28 LEU CA C 51.7 0.1 1 247 . 28 LEU CB C 43.7 0.1 1 248 . 28 LEU CG C 24.5 0.1 1 249 . 28 LEU CD1 C 21.8 0.1 2 250 . 28 LEU CD2 C 23.5 0.1 2 251 . 28 LEU N N 118.4 0.1 1 252 . 29 ALA H H 8.72 0.01 1 253 . 29 ALA HA H 4.99 0.01 1 254 . 29 ALA HB H 1.32 0.01 1 255 . 29 ALA C C 171.6 0.1 1 256 . 29 ALA CA C 47.5 0.1 1 257 . 29 ALA CB C 17.4 0.1 1 258 . 29 ALA N N 116.0 0.1 1 259 . 30 CYS H H 6.15 0.01 1 260 . 30 CYS HA H 4.95 0.01 1 261 . 30 CYS HB2 H 2.61 0.01 1 262 . 30 CYS HB3 H 2.32 0.01 1 263 . 30 CYS C C 172.0 0.1 1 264 . 30 CYS CA C 54.5 0.1 1 265 . 30 CYS N N 115.1 0.1 1 266 . 31 PHE H H 8.04 0.01 1 267 . 31 PHE HA H 4.67 0.01 1 268 . 31 PHE HB2 H 2.28 0.01 2 269 . 31 PHE HB3 H 1.09 0.01 2 270 . 31 PHE HD1 H 6.47 0.01 3 271 . 31 PHE HE1 H 7.07 0.01 3 272 . 31 PHE HZ H 7.39 0.01 1 273 . 31 PHE C C 169.0 0.1 1 274 . 31 PHE CA C 53.1 0.1 1 275 . 31 PHE CB C 41.9 0.1 1 276 . 31 PHE N N 120.5 0.1 1 277 . 32 ALA H H 8.77 0.01 1 278 . 32 ALA HA H 5.78 0.01 1 279 . 32 ALA HB H 1.12 0.01 1 280 . 32 ALA C C 168.8 0.1 1 281 . 32 ALA CA C 46.9 0.1 1 282 . 32 ALA CB C 20.1 0.1 1 283 . 32 ALA N N 113.9 0.1 1 284 . 33 ILE H H 9.55 0.01 1 285 . 33 ILE HA H 5.42 0.01 1 286 . 33 ILE HB H 1.71 0.01 1 287 . 33 ILE HG12 H 1.89 0.01 2 288 . 33 ILE HG13 H 1.10 0.01 2 289 . 33 ILE HG2 H 0.69 0.01 1 290 . 33 ILE HD1 H 0.86 0.01 1 291 . 33 ILE C C 172.9 0.1 1 292 . 33 ILE CA C 57.0 0.1 1 293 . 33 ILE CB C 40.9 0.1 1 294 . 33 ILE CG2 C 13.8 0.1 1 295 . 33 ILE CD1 C 10.8 0.1 1 296 . 33 ILE N N 116.2 0.1 1 297 . 34 TYR H H 9.50 0.01 1 298 . 34 TYR HA H 5.70 0.01 1 299 . 34 TYR HB2 H 1.70 0.01 1 300 . 34 TYR HB3 H 2.64 0.01 1 301 . 34 TYR HD1 H 7.02 0.01 3 302 . 34 TYR HE1 H 6.92 0.01 3 303 . 34 TYR C C 170.4 0.1 1 304 . 34 TYR CA C 48.8 0.1 1 305 . 34 TYR CB C 36.1 0.1 1 306 . 34 TYR CE1 C 115.2 0.1 3 307 . 34 TYR N N 127.7 0.1 1 308 . 35 THR H H 8.73 0.01 1 309 . 35 THR HA H 3.18 0.01 1 310 . 35 THR HB H 3.96 0.01 1 311 . 35 THR HG2 H 0.96 0.01 1 312 . 35 THR C C 170.7 0.1 1 313 . 35 THR CA C 57.1 0.1 1 314 . 35 THR CB C 64.5 0.1 1 315 . 35 THR CG2 C 14.1 0.1 1 316 . 35 THR N N 115.8 0.1 1 317 . 36 THR H H 8.24 0.01 1 318 . 36 THR HA H 4.84 0.01 1 319 . 36 THR HB H 4.90 0.01 1 320 . 36 THR HG2 H 1.50 0.01 1 321 . 36 THR C C 170.0 0.1 1 322 . 36 THR CA C 57.7 0.1 1 323 . 36 THR CB C 67.9 0.1 1 324 . 36 THR CG2 C 20.5 0.1 1 325 . 36 THR N N 106.5 0.1 1 326 . 37 LYS H H 9.62 0.01 1 327 . 37 LYS HA H 3.85 0.01 1 328 . 37 LYS HB2 H 1.87 0.01 2 329 . 37 LYS HB3 H 1.75 0.01 2 330 . 37 LYS HG2 H 1.44 0.01 2 331 . 37 LYS HG3 H 1.39 0.01 2 332 . 37 LYS HD2 H 1.70 0.01 2 333 . 37 LYS HD3 H 1.67 0.01 2 334 . 37 LYS HE2 H 2.97 0.01 2 335 . 37 LYS C C 172.8 0.1 1 336 . 37 LYS CA C 57.0 0.1 1 337 . 37 LYS CB C 29.0 0.1 1 338 . 37 LYS CG C 21.3 0.1 1 339 . 37 LYS CD C 26.3 0.1 1 340 . 37 LYS CE C 38.4 0.1 1 341 . 37 LYS N N 117.4 0.1 1 342 . 38 GLU H H 8.82 0.01 1 343 . 38 GLU HA H 3.99 0.01 1 344 . 38 GLU HB2 H 2.05 0.01 2 345 . 38 GLU HB3 H 1.94 0.01 2 346 . 38 GLU HG2 H 2.31 0.01 2 347 . 38 GLU HG3 H 2.27 0.01 2 348 . 38 GLU C C 175.3 0.1 1 349 . 38 GLU CA C 56.9 0.1 1 350 . 38 GLU N N 113.1 0.1 1 351 . 39 LYS H H 7.42 0.01 1 352 . 39 LYS HA H 4.12 0.01 1 353 . 39 LYS HB2 H 2.14 0.01 2 354 . 39 LYS HB3 H 1.73 0.01 2 355 . 39 LYS HG2 H 1.52 0.01 2 356 . 39 LYS HE2 H 2.89 0.01 9 357 . 39 LYS C C 177.0 0.1 1 358 . 39 LYS CA C 53.5 0.1 1 359 . 39 LYS N N 112.6 0.1 1 360 . 40 ALA H H 9.14 0.01 1 361 . 40 ALA HA H 3.84 0.01 1 362 . 40 ALA HB H 1.45 0.01 1 363 . 40 ALA C C 175.6 0.1 1 364 . 40 ALA CA C 52.4 0.1 1 365 . 40 ALA CB C 16.5 0.1 1 366 . 40 ALA N N 118.9 0.1 1 367 . 41 ALA H H 7.95 0.01 1 368 . 41 ALA HA H 3.71 0.01 1 369 . 41 ALA HB H 1.40 0.01 1 370 . 41 ALA C C 176.0 0.1 1 371 . 41 ALA CA C 52.5 0.1 1 372 . 41 ALA CB C 14.6 0.1 1 373 . 41 ALA N N 115.3 0.1 1 374 . 42 LEU H H 6.94 0.01 1 375 . 42 LEU HA H 4.19 0.01 1 376 . 42 LEU HB2 H 1.84 0.01 2 377 . 42 LEU HB3 H 1.73 0.01 2 378 . 42 LEU HG H 1.49 0.01 1 379 . 42 LEU HD1 H 0.90 0.01 2 380 . 42 LEU HD2 H 0.86 0.01 2 381 . 42 LEU C C 176.5 0.1 1 382 . 42 LEU CA C 54.6 0.1 1 383 . 42 LEU CB C 39.4 0.1 1 384 . 42 LEU CD1 C 21.0 0.1 2 385 . 42 LEU CD2 C 22.4 0.1 2 386 . 42 LEU N N 114.2 0.1 1 387 . 43 LEU H H 8.82 0.01 1 388 . 43 LEU HA H 3.74 0.01 1 389 . 43 LEU HB2 H 1.87 0.01 1 390 . 43 LEU HB3 H 1.15 0.01 1 391 . 43 LEU HG H 1.84 0.01 9 392 . 43 LEU HD1 H 0.72 0.01 2 393 . 43 LEU HD2 H 0.70 0.01 2 394 . 43 LEU C C 176.0 0.1 1 395 . 43 LEU CA C 54.5 0.1 1 396 . 43 LEU CB C 39.9 0.1 1 397 . 43 LEU CD1 C 20.9 0.1 2 398 . 43 LEU CD2 C 23.2 0.1 2 399 . 43 LEU N N 114.3 0.1 1 400 . 44 TYR H H 8.29 0.01 1 401 . 44 TYR HA H 3.77 0.01 1 402 . 44 TYR HB2 H 2.98 0.01 2 403 . 44 TYR HB3 H 2.94 0.01 2 404 . 44 TYR HD1 H 6.64 0.01 3 405 . 44 TYR HE1 H 6.34 0.01 3 406 . 44 TYR HH H 5.96 0.01 1 407 . 44 TYR C C 174.3 0.1 1 408 . 44 TYR CA C 59.3 0.1 1 409 . 44 TYR CD1 C 130.1 0.1 3 410 . 44 TYR CE1 C 115.1 0.1 3 411 . 44 TYR N N 116.2 0.1 1 412 . 45 LYS H H 6.86 0.01 1 413 . 45 LYS HA H 4.01 0.01 1 414 . 45 LYS HB2 H 1.93 0.01 2 415 . 45 LYS HB3 H 1.88 0.01 2 416 . 45 LYS HG2 H 1.69 0.01 9 417 . 45 LYS HG3 H 1.47 0.01 9 418 . 45 LYS HE2 H 3.00 0.01 2 419 . 45 LYS HE3 H 2.15 0.01 9 420 . 45 LYS C C 174.3 0.1 9 421 . 45 LYS CA C 55.5 0.1 1 422 . 45 LYS N N 108.6 0.1 1 423 . 46 LYS H H 7.76 0.01 1 424 . 46 LYS HA H 4.04 0.01 1 425 . 46 LYS HB2 H 1.64 0.01 2 426 . 46 LYS HG2 H 1.54 0.01 2 427 . 46 LYS HG3 H 1.32 0.01 2 428 . 46 LYS HD2 H 2.28 0.01 2 429 . 46 LYS HD3 H 2.25 0.01 2 430 . 46 LYS HE2 H 2.93 0.01 2 431 . 46 LYS HE3 H 2.80 0.01 2 432 . 46 LYS C C 176.5 0.1 1 433 . 46 LYS CA C 55.0 0.1 1 434 . 46 LYS N N 113.3 0.1 1 435 . 47 ILE H H 9.35 0.01 1 436 . 47 ILE HA H 3.44 0.01 1 437 . 47 ILE HB H 1.53 0.01 1 438 . 47 ILE HG12 H 1.33 0.01 2 439 . 47 ILE HG13 H 1.02 0.01 2 440 . 47 ILE HG2 H -0.43 0.01 1 441 . 47 ILE HD1 H 0.47 0.01 1 442 . 47 ILE C C 176.3 0.1 1 443 . 47 ILE CA C 61.0 0.1 1 444 . 47 ILE CB C 32.7 0.1 1 445 . 47 ILE CG1 C 26.7 0.1 1 446 . 47 ILE CG2 C 13.2 0.1 1 447 . 47 ILE CD1 C 9.4 0.1 1 448 . 47 ILE N N 115.5 0.1 1 449 . 48 MET H H 6.78 0.01 1 450 . 48 MET HA H 3.70 0.01 1 451 . 48 MET HB2 H 2.14 0.01 9 452 . 48 MET HB3 H 2.05 0.01 9 453 . 48 MET HG2 H 2.30 0.01 2 454 . 48 MET HG3 H 2.20 0.01 2 455 . 48 MET HE H 1.70 0.01 1 456 . 48 MET C C 174.4 0.1 1 457 . 48 MET CA C 56.9 0.1 1 458 . 48 MET CG C 27.6 0.1 1 459 . 48 MET CE C 13.6 0.1 1 460 . 48 MET N N 113.2 0.1 1 461 . 49 GLU H H 7.20 0.01 1 462 . 49 GLU HA H 3.98 0.01 1 463 . 49 GLU HB2 H 1.94 0.01 2 464 . 49 GLU HG2 H 2.30 0.01 2 465 . 49 GLU HG3 H 2.13 0.01 2 466 . 49 GLU C C 174.5 0.1 1 467 . 49 GLU CA C 55.3 0.1 1 468 . 49 GLU CG C 32.6 0.1 1 469 . 49 GLU N N 111.3 0.1 1 470 . 50 LYS H H 8.21 0.01 1 471 . 50 LYS HA H 3.71 0.01 1 472 . 50 LYS HB2 H 1.43 0.01 2 473 . 50 LYS HB3 H 0.93 0.01 2 474 . 50 LYS HG2 H -0.56 0.01 2 475 . 50 LYS HG3 H -0.59 0.01 2 476 . 50 LYS HD2 H 1.03 0.01 2 477 . 50 LYS HD3 H 0.65 0.01 2 478 . 50 LYS HE2 H 2.26 0.01 2 479 . 50 LYS HE3 H 2.14 0.01 2 480 . 50 LYS C C 171.8 0.1 9 481 . 50 LYS CA C 54.9 0.1 1 482 . 50 LYS CB C 29.1 0.1 1 483 . 50 LYS CG C 20.2 0.1 1 484 . 50 LYS CD C 24.4 0.1 1 485 . 50 LYS CE C 38.7 0.1 1 486 . 50 LYS N N 115.5 0.1 1 487 . 51 TYR H H 7.82 0.01 1 488 . 51 TYR HA H 4.42 0.01 1 489 . 51 TYR HB2 H 3.09 0.01 2 490 . 51 TYR HB3 H 2.15 0.01 2 491 . 51 TYR HD1 H 6.49 0.01 3 492 . 51 TYR HE1 H 5.89 0.01 3 493 . 51 TYR C C 174.8 0.1 1 494 . 51 TYR CA C 55.2 0.1 1 495 . 51 TYR CD1 C 128.7 0.1 3 496 . 51 TYR CE1 C 114.0 0.1 3 497 . 51 TYR N N 107.2 0.1 1 498 . 52 SER H H 7.42 0.01 1 499 . 52 SER HA H 4.09 0.01 1 500 . 52 SER HB2 H 3.88 0.01 2 501 . 52 SER C C 172.1 0.1 1 502 . 52 SER CA C 55.0 0.1 1 503 . 52 SER N N 110.1 0.1 1 504 . 53 VAL H H 6.41 0.01 1 505 . 53 VAL HA H 3.99 0.01 1 506 . 53 VAL HB H 2.68 0.01 1 507 . 53 VAL HG1 H 0.82 0.01 1 508 . 53 VAL HG2 H 0.64 0.01 1 509 . 53 VAL C C 171.8 0.1 1 510 . 53 VAL CA C 59.4 0.1 1 511 . 53 VAL CB C 27.7 0.1 1 512 . 53 VAL CG1 C 20.80 0.01 1 513 . 53 VAL CG2 C 16.50 0.01 1 514 . 53 VAL N N 101.5 0.1 1 515 . 54 THR H H 8.51 0.01 1 516 . 54 THR HA H 4.12 0.01 1 517 . 54 THR HB H 3.92 0.01 1 518 . 54 THR HG2 H 1.13 0.01 1 519 . 54 THR C C 172.7 0.1 1 520 . 54 THR CA C 60.5 0.1 1 521 . 54 THR CB C 65.5 0.1 1 522 . 54 THR CG2 C 19.7 0.1 1 523 . 54 THR N N 111.8 0.1 1 524 . 55 PHE H H 7.45 0.01 1 525 . 55 PHE HA H 4.17 0.01 1 526 . 55 PHE HB2 H 3.22 0.01 1 527 . 55 PHE HB3 H 2.32 0.01 1 528 . 55 PHE HD1 H 7.05 0.01 3 529 . 55 PHE HE1 H 7.75 0.01 3 530 . 55 PHE HZ H 8.03 0.01 1 531 . 55 PHE C C 172.9 0.1 1 532 . 55 PHE CA C 55.6 0.1 1 533 . 55 PHE CB C 40.1 0.1 1 534 . 55 PHE CE1 C 128.6 0.1 3 535 . 55 PHE CZ C 129.7 0.1 1 536 . 55 PHE N N 115.0 0.1 1 537 . 56 ILE H H 7.65 0.01 1 538 . 56 ILE HA H 5.34 0.01 1 539 . 56 ILE HB H 1.57 0.01 1 540 . 56 ILE HG12 H 1.88 0.01 2 541 . 56 ILE HG13 H 1.00 0.01 2 542 . 56 ILE HG2 H 0.30 0.01 1 543 . 56 ILE HD1 H 0.48 0.01 1 544 . 56 ILE C C 169.0 0.1 1 545 . 56 ILE CA C 56.1 0.1 1 546 . 56 ILE CB C 38.1 0.1 1 547 . 56 ILE CG2 C 11.0 0.1 1 548 . 56 ILE CD1 C 12.6 0.1 1 549 . 56 ILE N N 122.2 0.1 1 550 . 57 SER H H 9.91 0.01 1 551 . 57 SER HA H 5.12 0.01 1 552 . 57 SER HB2 H 4.36 0.01 2 553 . 57 SER HB3 H 3.87 0.01 2 554 . 57 SER C C 166.9 0.1 1 555 . 57 SER CA C 55.1 0.1 1 556 . 57 SER CB C 62.9 0.1 1 557 . 57 SER N N 114.4 0.1 1 558 . 58 ARG H H 9.13 0.01 1 559 . 58 ARG HA H 5.59 0.01 1 560 . 58 ARG HB2 H 1.84 0.01 2 561 . 58 ARG HB3 H 1.26 0.01 2 562 . 58 ARG HG2 H 1.46 0.01 2 563 . 58 ARG HG3 H 1.40 0.01 2 564 . 58 ARG HD2 H 3.43 0.01 2 565 . 58 ARG HD3 H 2.71 0.01 2 566 . 58 ARG C C 169.5 0.1 1 567 . 58 ARG CA C 52.2 0.1 1 568 . 58 ARG N N 117.7 0.1 1 569 . 59 HIS H H 9.81 0.01 1 570 . 59 HIS HA H 5.45 0.01 1 571 . 59 HIS HB2 H 2.89 0.01 1 572 . 59 HIS HB3 H 3.23 0.01 1 573 . 59 HIS HD2 H 6.98 0.01 1 574 . 59 HIS HE1 H 6.94 0.01 1 575 . 59 HIS C C 172.2 0.1 1 576 . 59 HIS CA C 52.2 0.1 1 577 . 59 HIS CE1 C 134.4 0.1 1 578 . 59 HIS N N 120.6 0.1 1 579 . 60 ASN H H 8.97 0.01 1 580 . 60 ASN HA H 4.77 0.01 1 581 . 60 ASN HB2 H 2.90 0.01 2 582 . 60 ASN HB3 H 2.65 0.01 2 583 . 60 ASN HD21 H 7.61 0.01 1 584 . 60 ASN HD22 H 7.02 0.01 1 585 . 60 ASN C C 173.2 0.1 1 586 . 60 ASN CA C 52.1 0.1 1 587 . 60 ASN CB C 37.1 0.1 1 588 . 60 ASN N N 118.1 0.1 1 589 . 60 ASN ND2 N 111.2 0.1 1 590 . 61 SER H H 7.96 0.01 1 591 . 61 SER HA H 4.72 0.01 1 592 . 61 SER HB2 H 3.76 0.01 2 593 . 61 SER HB3 H 3.68 0.01 2 594 . 61 SER C C 171.6 0.1 1 595 . 61 SER CA C 54.0 0.1 1 596 . 61 SER CB C 61.1 0.1 1 597 . 61 SER N N 111.1 0.1 1 598 . 62 TYR H H 9.21 0.01 1 599 . 62 TYR HA H 3.78 0.01 1 600 . 62 TYR HB2 H 3.26 0.01 1 601 . 62 TYR HB3 H 3.10 0.01 1 602 . 62 TYR HD1 H 7.11 0.01 3 603 . 62 TYR HE1 H 6.74 0.01 3 604 . 62 TYR C C 170.2 0.1 1 605 . 62 TYR CA C 57.9 0.1 1 606 . 62 TYR CB C 32.6 0.1 1 607 . 62 TYR CD1 C 130.1 0.1 3 608 . 62 TYR CE1 C 114.7 0.1 3 609 . 62 TYR N N 122.6 0.1 1 610 . 63 ASN H H 8.67 0.01 1 611 . 63 ASN HA H 4.50 0.01 1 612 . 63 ASN HB2 H 2.75 0.01 1 613 . 63 ASN HB3 H 2.65 0.01 1 614 . 63 ASN HD21 H 7.52 0.01 1 615 . 63 ASN HD22 H 6.94 0.01 1 616 . 63 ASN C C 172.5 0.1 1 617 . 63 ASN CA C 52.0 0.1 1 618 . 63 ASN CB C 35.3 0.1 1 619 . 63 ASN N N 110.0 0.1 1 620 . 63 ASN ND2 N 109.3 0.1 1 621 . 64 HIS H H 8.59 0.01 1 622 . 64 HIS HA H 5.27 0.01 1 623 . 64 HIS HB2 H 3.21 0.01 1 624 . 64 HIS HB3 H 3.99 0.01 1 625 . 64 HIS HD2 H 6.86 0.01 1 626 . 64 HIS HE1 H 7.79 0.01 1 627 . 64 HIS C C 171.4 0.1 1 628 . 64 HIS CA C 52.7 0.1 1 629 . 64 HIS CB C 29.8 0.1 1 630 . 64 HIS CD2 C 115.2 0.1 1 631 . 64 HIS CE1 C 135.9 0.1 1 632 . 64 HIS N N 116.5 0.1 1 633 . 65 ASN H H 9.54 0.01 1 634 . 65 ASN HA H 6.23 0.01 1 635 . 65 ASN HB2 H 2.54 0.01 1 636 . 65 ASN HB3 H 2.43 0.01 1 637 . 65 ASN HD21 H 7.87 0.01 1 638 . 65 ASN HD22 H 6.76 0.01 1 639 . 65 ASN C C 173.4 0.1 1 640 . 65 ASN CA C 48.9 0.1 1 641 . 65 ASN CB C 43.6 0.1 1 642 . 65 ASN N N 117.6 0.1 1 643 . 65 ASN ND2 N 105.8 0.1 1 644 . 66 ILE H H 8.95 0.01 1 645 . 66 ILE HA H 5.68 0.01 1 646 . 66 ILE HB H 1.33 0.01 1 647 . 66 ILE HG12 H 1.73 0.01 2 648 . 66 ILE HG13 H 0.77 0.01 2 649 . 66 ILE HG2 H 0.94 0.01 1 650 . 66 ILE HD1 H 0.40 0.01 1 651 . 66 ILE C C 170.4 0.1 1 652 . 66 ILE CA C 56.4 0.1 1 653 . 66 ILE CB C 40.2 0.1 9 654 . 66 ILE CG1 C 27.4 0.1 1 655 . 66 ILE CG2 C 14.7 0.1 1 656 . 66 ILE CD1 C 11.8 0.1 1 657 . 66 ILE N N 113.5 0.1 1 658 . 67 LEU H H 10.01 0.01 1 659 . 67 LEU HA H 5.87 0.01 1 660 . 67 LEU HB2 H 1.74 0.01 1 661 . 67 LEU HB3 H 1.82 0.01 1 662 . 67 LEU HG H 1.77 0.01 1 663 . 67 LEU HD1 H 1.13 0.01 1 664 . 67 LEU HD2 H 1.07 0.01 1 665 . 67 LEU C C 172.8 0.1 1 666 . 67 LEU CA C 50.1 0.1 1 667 . 67 LEU CB C 43.6 0.1 1 668 . 67 LEU CG C 24.5 0.1 1 669 . 67 LEU CD1 C 22.6 0.1 1 670 . 67 LEU CD2 C 23.5 0.1 1 671 . 67 LEU N N 124.2 0.1 1 672 . 68 PHE H H 9.79 0.01 1 673 . 68 PHE HA H 5.43 0.01 1 674 . 68 PHE HB2 H 3.84 0.01 1 675 . 68 PHE HB3 H 2.57 0.01 1 676 . 68 PHE HD1 H 7.33 0.01 3 677 . 68 PHE HE1 H 7.04 0.01 3 678 . 68 PHE HZ H 6.97 0.01 1 679 . 68 PHE C C 171.4 0.1 1 680 . 68 PHE CA C 53.7 0.1 1 681 . 68 PHE CB C 39.4 0.1 1 682 . 68 PHE CE1 C 127.7 0.1 3 683 . 68 PHE N N 123.4 0.1 1 684 . 69 PHE H H 8.25 0.01 1 685 . 69 PHE HA H 5.34 0.01 1 686 . 69 PHE HB2 H 3.39 0.01 2 687 . 69 PHE HB3 H 2.91 0.01 2 688 . 69 PHE HD1 H 6.72 0.01 3 689 . 69 PHE HE1 H 6.62 0.01 3 690 . 69 PHE HZ H 6.64 0.01 1 691 . 69 PHE C C 170.7 0.1 1 692 . 69 PHE CA C 53.5 0.1 1 693 . 69 PHE CB C 37.2 0.1 1 694 . 69 PHE CD1 C 130.1 0.1 3 695 . 69 PHE N N 115.5 0.1 1 696 . 70 LEU H H 8.48 0.01 1 697 . 70 LEU HA H 5.52 0.01 1 698 . 70 LEU HB2 H 1.51 0.01 1 699 . 70 LEU HB3 H 1.71 0.01 1 700 . 70 LEU HG H 1.56 0.01 1 701 . 70 LEU HD1 H 0.81 0.01 1 702 . 70 LEU HD2 H 0.81 0.01 1 703 . 70 LEU C C 168.9 0.1 9 704 . 70 LEU CA C 50.7 0.1 1 705 . 70 LEU CB C 43.3 0.1 1 706 . 70 LEU CG C 25.5 0.1 1 707 . 70 LEU CD1 C 23.1 0.1 1 708 . 70 LEU CD2 C 23.1 0.1 1 709 . 70 LEU N N 116.2 0.1 1 710 . 71 THR H H 9.26 0.01 1 711 . 71 THR HA H 5.01 0.01 1 712 . 71 THR HB H 4.98 0.01 1 713 . 71 THR HG2 H 1.29 0.01 1 714 . 71 THR C C 174.4 0.1 1 715 . 71 THR CA C 55.4 0.1 1 716 . 71 THR CB C 65.6 0.1 1 717 . 71 THR CG2 C 17.2 0.1 1 718 . 71 THR N N 108.5 0.1 1 719 . 72 PRO HA H 4.11 0.01 1 720 . 72 PRO HB2 H 2.27 0.01 2 721 . 72 PRO HG2 H 1.87 0.01 2 722 . 72 PRO HD2 H 4.12 0.01 2 723 . 72 PRO HD3 H 3.77 0.01 2 724 . 72 PRO CA C 60.6 0.1 1 725 . 72 PRO CD C 48.9 0.1 1 726 . 73 HIS H H 7.11 0.01 1 727 . 73 HIS HA H 4.81 0.01 1 728 . 73 HIS HB2 H 3.08 0.01 2 729 . 73 HIS HB3 H 2.66 0.01 2 730 . 73 HIS HD2 H 6.99 0.01 1 731 . 73 HIS HE1 H 7.82 0.01 1 732 . 73 HIS C C 173.2 0.1 1 733 . 73 HIS CA C 50.2 0.1 1 734 . 73 HIS CB C 30.2 0.1 1 735 . 73 HIS CD2 C 116.1 0.1 1 736 . 73 HIS N N 111.7 0.1 1 737 . 74 ARG H H 8.50 0.01 1 738 . 74 ARG HA H 4.61 0.01 1 739 . 74 ARG HB2 H 1.48 0.01 2 740 . 74 ARG HB3 H 1.66 0.01 9 741 . 74 ARG HG2 H 1.08 0.01 2 742 . 74 ARG HD2 H 3.09 0.01 2 743 . 74 ARG HD3 H 2.89 0.01 2 744 . 74 ARG CA C 52.9 0.1 1 745 . 74 ARG CD C 40.1 0.1 1 746 . 74 ARG N N 115.7 0.1 1 747 . 75 HIS H H 9.43 0.01 1 748 . 75 HIS HA H 4.91 0.01 1 749 . 75 HIS HB2 H 2.51 0.01 1 750 . 75 HIS HB3 H 2.95 0.01 1 751 . 75 HIS HD2 H 7.07 0.01 1 752 . 75 HIS HE1 H 7.80 0.01 1 753 . 75 HIS C C 173.1 0.1 1 754 . 75 HIS CA C 52.2 0.1 1 755 . 75 HIS CB C 33.1 0.1 1 756 . 75 HIS CD2 C 117.1 0.1 1 757 . 75 HIS N N 113.3 0.1 1 758 . 76 ARG H H 9.17 0.01 1 759 . 76 ARG HA H 4.76 0.01 1 760 . 76 ARG HB2 H 1.72 0.01 2 761 . 76 ARG HB3 H 1.77 0.01 9 762 . 76 ARG HG2 H 2.12 0.01 2 763 . 76 ARG HG3 H 1.64 0.01 2 764 . 76 ARG HD2 H 3.27 0.01 2 765 . 76 ARG HD3 H 3.23 0.01 2 766 . 76 ARG C C 172.7 0.1 1 767 . 76 ARG CA C 53.3 0.1 1 768 . 76 ARG CD C 40.5 0.1 1 769 . 76 ARG N N 117.7 0.1 1 770 . 77 VAL H H 9.25 0.01 1 771 . 77 VAL HA H 3.47 0.01 1 772 . 77 VAL HB H 2.13 0.01 1 773 . 77 VAL HG1 H 0.99 0.01 1 774 . 77 VAL HG2 H 1.21 0.01 1 775 . 77 VAL C C 175.0 0.1 1 776 . 77 VAL CA C 64.0 0.1 1 777 . 77 VAL CB C 28.5 0.1 1 778 . 77 VAL CG1 C 18.90 0.01 1 779 . 77 VAL CG2 C 20.80 0.01 1 780 . 77 VAL N N 120.9 0.1 1 781 . 78 SER H H 8.57 0.01 1 782 . 78 SER HA H 4.09 0.01 1 783 . 78 SER HB2 H 3.94 0.01 2 784 . 78 SER C C 174.9 0.1 1 785 . 78 SER CA C 57.6 0.1 1 786 . 78 SER N N 107.8 0.1 1 787 . 79 ALA H H 7.07 0.01 1 788 . 79 ALA HA H 4.24 0.01 1 789 . 79 ALA HB H 1.61 0.01 1 790 . 79 ALA C C 173.4 0.1 1 791 . 79 ALA CA C 52.0 0.1 1 792 . 79 ALA CB C 15.7 0.1 1 793 . 79 ALA N N 121.1 0.1 1 794 . 80 ILE H H 6.96 0.01 1 795 . 80 ILE HA H 3.70 0.01 1 796 . 80 ILE HB H 1.56 0.01 1 797 . 80 ILE HG12 H 0.52 0.01 2 798 . 80 ILE HG13 H -0.46 0.01 2 799 . 80 ILE HG2 H 0.52 0.01 1 800 . 80 ILE HD1 H -0.78 0.01 1 801 . 80 ILE C C 177.0 0.1 1 802 . 80 ILE CA C 59.4 0.1 1 803 . 80 ILE CB C 32.3 0.1 1 804 . 80 ILE CG1 C 23.2 0.1 1 805 . 80 ILE CG2 C 14.7 0.1 1 806 . 80 ILE CD1 C 5.1 0.1 1 807 . 80 ILE N N 115.7 0.1 1 808 . 81 ASN H H 8.64 0.01 1 809 . 81 ASN HA H 4.17 0.01 1 810 . 81 ASN HB2 H 2.48 0.01 1 811 . 81 ASN HB3 H 2.73 0.01 1 812 . 81 ASN HD21 H 7.52 0.01 1 813 . 81 ASN HD22 H 6.86 0.01 1 814 . 81 ASN C C 175.1 0.1 1 815 . 81 ASN CA C 54.5 0.1 1 816 . 81 ASN N N 113.3 0.1 1 817 . 81 ASN ND2 N 108.7 0.1 1 818 . 82 ASN H H 8.31 0.01 1 819 . 82 ASN HA H 4.32 0.01 1 820 . 82 ASN HB2 H 2.93 0.01 2 821 . 82 ASN HB3 H 2.78 0.01 2 822 . 82 ASN HD21 H 7.61 0.01 1 823 . 82 ASN HD22 H 6.95 0.01 1 824 . 82 ASN C C 173.7 0.1 1 825 . 82 ASN CA C 53.3 0.1 1 826 . 82 ASN CB C 35.4 0.1 1 827 . 82 ASN N N 111.9 0.1 1 828 . 82 ASN ND2 N 107.6 0.1 1 829 . 83 TYR H H 7.57 0.01 1 830 . 83 TYR HA H 4.08 0.01 1 831 . 83 TYR HB2 H 3.20 0.01 1 832 . 83 TYR HB3 H 3.06 0.01 1 833 . 83 TYR HD1 H 6.89 0.01 3 834 . 83 TYR HE1 H 6.38 0.01 3 835 . 83 TYR C C 174.3 0.1 1 836 . 83 TYR CA C 58.5 0.1 1 837 . 83 TYR CD1 C 130.1 0.1 3 838 . 83 TYR CE1 C 114.1 0.1 3 839 . 83 TYR N N 115.4 0.1 1 840 . 84 ALA H H 8.37 0.01 1 841 . 84 ALA HA H 3.55 0.01 1 842 . 84 ALA HB H 1.28 0.01 1 843 . 84 ALA C C 174.0 0.1 1 844 . 84 ALA CA C 51.9 0.1 1 845 . 84 ALA CB C 15.5 0.1 1 846 . 84 ALA N N 115.1 0.1 1 847 . 85 GLN H H 8.81 0.01 1 848 . 85 GLN HA H 3.75 0.01 1 849 . 85 GLN HB2 H 1.99 0.01 2 850 . 85 GLN HG2 H 2.42 0.01 2 851 . 85 GLN HG3 H 2.36 0.01 2 852 . 85 GLN HE21 H 7.30 0.01 2 853 . 85 GLN HE22 H 6.82 0.01 2 854 . 85 GLN C C 176.3 0.1 1 855 . 85 GLN CA C 55.9 0.1 1 856 . 85 GLN CB C 25.0 0.1 1 857 . 85 GLN CG C 30.9 0.1 1 858 . 85 GLN N N 111.5 0.1 1 859 . 85 GLN NE2 N 107.3 0.1 1 860 . 86 LYS H H 7.15 0.01 1 861 . 86 LYS HA H 3.90 0.01 1 862 . 86 LYS HB2 H 1.73 0.01 2 863 . 86 LYS HG2 H 1.59 0.01 9 864 . 86 LYS HD2 H 1.37 0.01 9 865 . 86 LYS HE2 H 2.91 0.01 2 866 . 86 LYS C C 175.5 0.1 1 867 . 86 LYS CA C 55.2 0.1 1 868 . 86 LYS CB C 28.8 0.1 1 869 . 86 LYS N N 112.7 0.1 1 870 . 87 LEU H H 6.98 0.01 1 871 . 87 LEU HA H 4.12 0.01 1 872 . 87 LEU HB2 H 1.52 0.01 1 873 . 87 LEU HB3 H 1.33 0.01 1 874 . 87 LEU HG H 1.31 0.01 1 875 . 87 LEU HD1 H 0.62 0.01 1 876 . 87 LEU HD2 H 0.46 0.01 1 877 . 87 LEU C C 175.0 0.1 1 878 . 87 LEU CA C 52.8 0.1 1 879 . 87 LEU CB C 40.1 0.1 1 880 . 87 LEU CD1 C 22.5 0.1 1 881 . 87 LEU CD2 C 20.3 0.1 1 882 . 87 LEU N N 112.9 0.1 1 883 . 88 CYS H H 7.61 0.01 1 884 . 88 CYS HA H 4.26 0.01 1 885 . 88 CYS HB2 H 2.73 0.01 2 886 . 88 CYS HB3 H 2.51 0.01 2 887 . 88 CYS C C 174.7 0.1 1 888 . 88 CYS CA C 56.2 0.1 1 889 . 88 CYS CB C 24.9 0.1 1 890 . 88 CYS N N 112.3 0.1 1 891 . 89 THR HA H 3.81 0.01 1 892 . 89 THR HB H 3.81 0.01 1 893 . 89 THR HG2 H 0.85 0.01 1 894 . 89 THR CA C 59.8 0.1 1 895 . 89 THR CB C 66.2 0.1 1 896 . 89 THR CG2 C 18.7 0.1 1 897 . 90 PHE H H 8.58 0.01 1 898 . 90 PHE HA H 4.51 0.01 1 899 . 90 PHE HB2 H 3.23 0.01 2 900 . 90 PHE HB3 H 3.02 0.01 2 901 . 90 PHE HD1 H 7.21 0.01 3 902 . 90 PHE HE1 H 7.31 0.01 9 903 . 90 PHE CA C 55.3 0.1 1 904 . 90 PHE CB C 35.5 0.1 1 905 . 90 PHE N N 115.7 0.1 1 906 . 91 SER HA H 4.66 0.01 1 907 . 91 SER HB2 H 3.74 0.01 2 908 . 91 SER HB3 H 3.61 0.01 2 909 . 91 SER CA C 55.7 0.1 1 910 . 91 SER CB C 61.9 0.1 1 911 . 92 PHE H H 8.21 0.01 1 912 . 92 PHE HA H 4.48 0.01 1 913 . 92 PHE HB2 H 2.82 0.01 1 914 . 92 PHE HB3 H 3.06 0.01 1 915 . 92 PHE HD1 H 6.73 0.01 3 916 . 92 PHE HE1 H 5.84 0.01 3 917 . 92 PHE HZ H 5.57 0.01 1 918 . 92 PHE C C 170.0 0.1 1 919 . 92 PHE CA C 54.3 0.1 1 920 . 92 PHE CD1 C 128.7 0.1 3 921 . 92 PHE CE1 C 127.7 0.1 3 922 . 92 PHE CZ C 125.4 0.1 1 923 . 92 PHE N N 118.5 0.1 1 924 . 93 LEU H H 8.12 0.01 1 925 . 93 LEU HA H 4.33 0.01 1 926 . 93 LEU HB2 H 1.40 0.01 1 927 . 93 LEU HB3 H 1.45 0.01 1 928 . 93 LEU HG H 1.63 0.01 1 929 . 93 LEU HD1 H 1.16 0.01 1 930 . 93 LEU HD2 H 0.60 0.01 1 931 . 93 LEU C C 168.9 0.1 1 932 . 93 LEU CA C 52.8 0.1 1 933 . 93 LEU CB C 40.0 0.1 9 934 . 93 LEU CD1 C 23.3 0.1 1 935 . 93 LEU CD2 C 24.8 0.1 1 936 . 93 LEU N N 119.7 0.1 1 937 . 94 ILE H H 8.84 0.01 1 938 . 94 ILE HA H 4.48 0.01 1 939 . 94 ILE HB H 1.71 0.01 1 940 . 94 ILE HG12 H 1.37 0.01 2 941 . 94 ILE HG13 H 1.19 0.01 2 942 . 94 ILE HG2 H 1.14 0.01 1 943 . 94 ILE HD1 H 0.63 0.01 1 944 . 94 ILE C C 171.8 0.1 1 945 . 94 ILE CA C 57.2 0.1 1 946 . 94 ILE CB C 36.3 0.1 1 947 . 94 ILE CG1 C 23.9 0.1 1 948 . 94 ILE CG2 C 15.7 0.1 1 949 . 94 ILE CD1 C 10.0 0.1 1 950 . 94 ILE N N 122.5 0.1 1 951 . 95 CYS H H 8.99 0.01 1 952 . 95 CYS HA H 5.56 0.01 1 953 . 95 CYS HB2 H 2.46 0.01 1 954 . 95 CYS HB3 H 2.87 0.01 1 955 . 95 CYS C C 171.4 0.1 1 956 . 95 CYS CA C 53.9 0.1 1 957 . 95 CYS CB C 25.1 0.1 1 958 . 95 CYS N N 124.8 0.1 1 959 . 96 LYS H H 9.15 0.01 1 960 . 96 LYS HA H 4.89 0.01 1 961 . 96 LYS HB2 H 1.46 0.01 2 962 . 96 LYS HB3 H 1.43 0.01 9 963 . 96 LYS HG2 H 1.02 0.01 9 964 . 96 LYS HD2 H 1.25 0.01 9 965 . 96 LYS HE2 H 2.50 0.01 2 966 . 96 LYS C C 170.3 0.1 1 967 . 96 LYS CA C 52.4 0.1 1 968 . 96 LYS N N 121.0 0.1 1 969 . 97 GLY H H 9.08 0.01 1 970 . 97 GLY HA2 H 4.16 0.01 2 971 . 97 GLY HA3 H 3.20 0.01 2 972 . 97 GLY C C 172.4 0.1 1 973 . 97 GLY CA C 41.8 0.1 1 974 . 97 GLY N N 102.6 0.1 1 975 . 98 VAL H H 7.69 0.01 1 976 . 98 VAL HA H 3.93 0.01 1 977 . 98 VAL HB H 1.60 0.01 1 978 . 98 VAL HG1 H 0.68 0.01 1 979 . 98 VAL HG2 H 0.58 0.01 1 980 . 98 VAL C C 168.5 0.1 1 981 . 98 VAL CA C 58.4 0.1 1 982 . 98 VAL CB C 30.3 0.1 1 983 . 98 VAL CG1 C 19.50 0.01 1 984 . 98 VAL CG2 C 17.80 0.01 1 985 . 98 VAL N N 118.9 0.1 1 986 . 99 ASN H H 8.14 0.01 1 987 . 99 ASN HA H 4.74 0.01 1 988 . 99 ASN HB2 H 2.60 0.01 2 989 . 99 ASN HB3 H 2.46 0.01 2 990 . 99 ASN C C 171.3 0.1 1 991 . 99 ASN CA C 50.5 0.1 1 992 . 99 ASN N N 118.8 0.1 1 993 . 100 LYS H H 7.17 0.01 1 994 . 100 LYS HA H 4.60 0.01 1 995 . 100 LYS HB2 H 1.77 0.01 2 996 . 100 LYS HB3 H 1.70 0.01 2 997 . 100 LYS HG2 H 1.54 0.01 2 998 . 100 LYS HG3 H 1.38 0.01 9 999 . 100 LYS HE2 H 3.10 0.01 2 1000 . 100 LYS HE3 H 2.93 0.01 2 1001 . 100 LYS C C 172.2 0.1 1 1002 . 100 LYS CA C 50.6 0.1 1 1003 . 100 LYS CE C 40.3 0.1 1 1004 . 100 LYS N N 115.4 0.1 1 1005 . 101 GLU H H 9.24 0.01 1 1006 . 101 GLU HA H 3.63 0.01 1 1007 . 101 GLU HB2 H 1.87 0.01 2 1008 . 101 GLU HB3 H 1.74 0.01 2 1009 . 101 GLU HG2 H 2.28 0.01 2 1010 . 101 GLU HG3 H 2.14 0.01 9 1011 . 101 GLU C C 171.9 0.1 1 1012 . 101 GLU CA C 58.1 0.1 1 1013 . 101 GLU CB C 33.7 0.1 1 1014 . 101 GLU N N 117.3 0.1 1 1015 . 102 TYR H H 8.43 0.01 1 1016 . 102 TYR HA H 3.46 0.01 1 1017 . 102 TYR HB2 H 2.71 0.01 1 1018 . 102 TYR HB3 H 2.60 0.01 1 1019 . 102 TYR HD1 H 6.75 0.01 3 1020 . 102 TYR HE1 H 6.68 0.01 3 1021 . 102 TYR C C 173.9 0.1 1 1022 . 102 TYR CA C 58.3 0.1 1 1023 . 102 TYR CD1 C 130.1 0.1 3 1024 . 102 TYR CE1 C 114.7 0.1 3 1025 . 102 TYR N N 113.7 0.1 1 1026 . 103 LEU H H 7.94 0.01 1 1027 . 103 LEU HA H 3.25 0.01 1 1028 . 103 LEU HB2 H 1.55 0.01 1 1029 . 103 LEU HB3 H 1.58 0.01 1 1030 . 103 LEU HG H 0.50 0.01 1 1031 . 103 LEU HD1 H 0.87 0.01 1 1032 . 103 LEU HD2 H 0.70 0.01 1 1033 . 103 LEU C C 175.4 0.1 1 1034 . 103 LEU CA C 54.5 0.1 1 1035 . 103 LEU CG C 37.8 0.1 1 1036 . 103 LEU CD1 C 22.6 0.1 1 1037 . 103 LEU CD2 C 18.9 0.1 1 1038 . 103 LEU N N 114.9 0.1 1 1039 . 104 MET H H 7.31 0.01 1 1040 . 104 MET HA H 3.35 0.01 1 1041 . 104 MET HB2 H 2.14 0.01 2 1042 . 104 MET HB3 H 2.07 0.01 2 1043 . 104 MET HG2 H 2.34 0.01 2 1044 . 104 MET HG3 H 2.14 0.01 2 1045 . 104 MET HE H 1.73 0.01 1 1046 . 104 MET C C 175.5 0.1 1 1047 . 104 MET CA C 55.6 0.1 1 1048 . 104 MET CE C 17.1 0.1 1 1049 . 104 MET N N 113.5 0.1 1 1050 . 105 TYR H H 7.38 0.01 1 1051 . 105 TYR HA H 3.36 0.01 1 1052 . 105 TYR HB2 H 2.78 0.01 2 1053 . 105 TYR HB3 H 2.05 0.01 2 1054 . 105 TYR HD1 H 6.58 0.01 3 1055 . 105 TYR HE1 H 6.95 0.01 3 1056 . 105 TYR C C 172.4 0.1 1 1057 . 105 TYR CA C 59.0 0.1 1 1058 . 105 TYR CD1 C 130.1 0.1 3 1059 . 105 TYR CE1 C 115.9 0.1 3 1060 . 105 TYR N N 113.1 0.1 1 1061 . 106 SER H H 7.93 0.01 1 1062 . 106 SER HA H 4.83 0.01 1 1063 . 106 SER HB2 H 3.36 0.01 2 1064 . 106 SER HB3 H 3.28 0.01 2 1065 . 106 SER C C 173.0 0.1 1 1066 . 106 SER CA C 58.5 0.1 1 1067 . 106 SER CB C 59.6 0.1 1 1068 . 106 SER N N 105.3 0.1 1 1069 . 107 ALA H H 7.49 0.01 1 1070 . 107 ALA HA H 3.80 0.01 1 1071 . 107 ALA HB H 1.24 0.01 1 1072 . 107 ALA C C 175.1 0.1 1 1073 . 107 ALA CA C 52.3 0.1 1 1074 . 107 ALA CB C 14.7 0.1 1 1075 . 107 ALA N N 119.8 0.1 1 1076 . 108 LEU H H 7.19 0.01 1 1077 . 108 LEU HA H 3.55 0.01 1 1078 . 108 LEU HB2 H 0.96 0.01 1 1079 . 108 LEU HB3 H -0.31 0.01 1 1080 . 108 LEU HG H 1.19 0.01 1 1081 . 108 LEU HD1 H -0.01 0.01 1 1082 . 108 LEU HD2 H -0.15 0.01 1 1083 . 108 LEU C C 176.5 0.1 1 1084 . 108 LEU CA C 52.9 0.1 1 1085 . 108 LEU CB C 36.7 0.1 1 1086 . 108 LEU CG C 21.7 0.1 1 1087 . 108 LEU CD1 C 23.5 0.1 1 1088 . 108 LEU CD2 C 20.5 0.1 1 1089 . 108 LEU N N 111.0 0.1 1 1090 . 109 THR H H 7.13 0.01 1 1091 . 109 THR HA H 4.31 0.01 1 1092 . 109 THR HB H 4.28 0.01 1 1093 . 109 THR HG2 H 0.66 0.01 1 1094 . 109 THR C C 172.9 0.1 1 1095 . 109 THR CA C 57.8 0.1 1 1096 . 109 THR CB C 67.3 0.1 1 1097 . 109 THR CG2 C 17.9 0.1 1 1098 . 109 THR N N 102.9 0.1 1 1099 . 110 ARG H H 7.51 0.01 1 1100 . 110 ARG HA H 4.68 0.01 1 1101 . 110 ARG HB2 H 1.79 0.01 2 1102 . 110 ARG HG2 H 1.66 0.01 2 1103 . 110 ARG HG3 H 1.55 0.01 2 1104 . 110 ARG HD2 H 3.16 0.01 2 1105 . 110 ARG HD3 H 3.07 0.01 2 1106 . 110 ARG C C 170.9 0.1 1 1107 . 110 ARG CA C 51.4 0.1 1 1108 . 110 ARG CB C 31.0 0.1 1 1109 . 110 ARG CG C 24.0 0.1 1 1110 . 110 ARG CD C 40.3 0.1 1 1111 . 110 ARG N N 118.2 0.1 1 1112 . 111 ASP H H 8.17 0.01 1 1113 . 111 ASP HA H 4.29 0.01 1 1114 . 111 ASP HB2 H 2.50 0.01 2 1115 . 111 ASP C C 171.3 0.1 1 1116 . 111 ASP CA C 50.7 0.1 1 1117 . 111 ASP N N 116.2 0.1 1 1118 . 112 PRO HA H 4.54 0.01 1 1119 . 112 PRO HB2 H 1.76 0.01 2 1120 . 112 PRO HB3 H 1.45 0.01 2 1121 . 112 PRO HG2 H 1.53 0.01 2 1122 . 112 PRO HG3 H -0.05 0.01 2 1123 . 112 PRO HD2 H 3.26 0.01 2 1124 . 112 PRO HD3 H 3.23 0.01 2 1125 . 112 PRO CA C 61.1 0.1 1 1126 . 112 PRO CG C 20.3 0.1 1 1127 . 112 PRO CD C 47.7 0.1 1 1128 . 113 PHE H H 9.03 0.01 1 1129 . 113 PHE HA H 4.90 0.01 1 1130 . 113 PHE HB2 H 3.02 0.01 1 1131 . 113 PHE HB3 H 3.24 0.01 1 1132 . 113 PHE HD1 H 7.78 0.01 3 1133 . 113 PHE HE1 H 7.40 0.01 3 1134 . 113 PHE HZ H 7.08 0.01 1 1135 . 113 PHE C C 172.3 0.1 1 1136 . 113 PHE CA C 54.2 0.1 1 1137 . 113 PHE CB C 38.3 0.1 1 1138 . 113 PHE CD1 C 129.8 0.1 3 1139 . 113 PHE CE1 C 128.0 0.1 3 1140 . 113 PHE N N 126.9 0.1 1 1141 . 114 SER H H 7.24 0.01 1 1142 . 114 SER HA H 4.48 0.01 1 1143 . 114 SER HB2 H 4.01 0.01 2 1144 . 114 SER HB3 H 3.75 0.01 2 1145 . 114 SER C C 170.5 0.1 1 1146 . 114 SER CA C 54.4 0.1 1 1147 . 114 SER CB C 62.0 0.1 1 1148 . 114 SER N N 102.6 0.1 1 1149 . 115 VAL H H 9.12 0.01 1 1150 . 115 VAL HA H 3.70 0.01 1 1151 . 115 VAL HB H 1.93 0.01 1 1152 . 115 VAL HG1 H 0.65 0.01 1 1153 . 115 VAL HG2 H 0.92 0.01 1 1154 . 115 VAL C C 171.6 0.1 1 1155 . 115 VAL CA C 60.4 0.1 1 1156 . 115 VAL CB C 30.3 0.1 1 1157 . 115 VAL CG1 C 17.40 0.01 1 1158 . 115 VAL CG2 C 20.00 0.01 1 1159 . 115 VAL N N 118.4 0.1 1 1160 . 116 ILE H H 9.33 0.01 1 1161 . 116 ILE HA H 3.89 0.01 1 1162 . 116 ILE HB H 1.07 0.01 1 1163 . 116 ILE HG12 H 1.48 0.01 2 1164 . 116 ILE HG13 H 0.90 0.01 2 1165 . 116 ILE HG2 H 0.68 0.01 1 1166 . 116 ILE HD1 H 0.70 0.01 1 1167 . 116 ILE C C 172.5 0.1 1 1168 . 116 ILE CA C 60.4 0.1 1 1169 . 116 ILE CB C 37.3 0.1 1 1170 . 116 ILE CG2 C 13.8 0.1 1 1171 . 116 ILE CD1 C 12.3 0.1 1 1172 . 116 ILE N N 124.7 0.1 1 1173 . 117 GLU H H 7.33 0.01 1 1174 . 117 GLU HA H 4.60 0.01 1 1175 . 117 GLU HB2 H 1.53 0.01 2 1176 . 117 GLU HB3 H 1.47 0.01 9 1177 . 117 GLU HG2 H 1.72 0.01 2 1178 . 117 GLU HG3 H 1.67 0.01 2 1179 . 117 GLU C C 172.7 0.1 1 1180 . 117 GLU CA C 51.2 0.1 1 1181 . 117 GLU N N 109.8 0.1 1 1182 . 118 GLU H H 8.34 0.01 1 1183 . 118 GLU HA H 5.36 0.01 1 1184 . 118 GLU HB2 H 2.14 0.01 2 1185 . 118 GLU HB3 H 2.12 0.01 2 1186 . 118 GLU HG2 H 2.24 0.01 2 1187 . 118 GLU HG3 H 2.17 0.01 2 1188 . 118 GLU C C 169.3 0.1 1 1189 . 118 GLU CA C 52.2 0.1 1 1190 . 118 GLU CB C 30.1 0.1 1 1191 . 118 GLU N N 112.6 0.1 1 1192 . 119 SER H H 8.83 0.01 1 1193 . 119 SER HA H 4.00 0.01 1 1194 . 119 SER HB2 H 3.99 0.01 2 1195 . 119 SER HB3 H 3.58 0.01 2 1196 . 119 SER C C 174.5 0.1 1 1197 . 119 SER CA C 58.2 0.1 1 1198 . 119 SER CB C 60.0 0.1 1 1199 . 119 SER N N 110.7 0.1 1 1200 . 120 LEU H H 6.82 0.01 1 1201 . 120 LEU HA H 5.05 0.01 1 1202 . 120 LEU HB2 H 1.72 0.01 1 1203 . 120 LEU HB3 H 1.75 0.01 1 1204 . 120 LEU HG H 1.61 0.01 1 1205 . 120 LEU HD1 H 0.96 0.01 1 1206 . 120 LEU HD2 H 0.86 0.01 1 1207 . 120 LEU C C 171.5 0.1 1 1208 . 120 LEU CA C 48.9 0.1 1 1209 . 120 LEU CB C 41.8 0.1 1 1210 . 120 LEU CG C 24.1 0.1 1 1211 . 120 LEU CD1 C 21.4 0.1 1 1212 . 120 LEU CD2 C 21.8 0.1 1 1213 . 120 LEU N N 118.4 0.1 1 1214 . 121 PRO HA H 4.43 0.01 1 1215 . 121 PRO HB2 H 2.29 0.01 2 1216 . 121 PRO HB3 H 1.98 0.01 2 1217 . 121 PRO HG2 H 2.18 0.01 2 1218 . 121 PRO HG3 H 2.00 0.01 2 1219 . 121 PRO HD2 H 3.89 0.01 2 1220 . 121 PRO HD3 H 3.74 0.01 2 1221 . 121 PRO CA C 60.8 0.1 1 1222 . 121 PRO CG C 24.4 0.1 1 1223 . 121 PRO CD C 48.3 0.1 1 1224 . 122 GLY H H 9.19 0.01 1 1225 . 122 GLY HA2 H 4.27 0.01 2 1226 . 122 GLY HA3 H 3.77 0.01 2 1227 . 122 GLY C C 175.3 0.1 1 1228 . 122 GLY CA C 42.4 0.1 1 1229 . 122 GLY N N 111.5 0.1 1 1230 . 123 GLY H H 8.25 0.01 1 1231 . 123 GLY HA2 H 3.88 0.01 2 1232 . 123 GLY HA3 H 3.46 0.01 2 1233 . 123 GLY C C 172.2 0.1 1 1234 . 123 GLY CA C 43.5 0.1 1 1235 . 123 GLY N N 103.6 0.1 1 1236 . 124 LEU H H 5.59 0.01 1 1237 . 124 LEU HA H 3.96 0.01 1 1238 . 124 LEU HB2 H 0.49 0.01 1 1239 . 124 LEU HB3 H 0.99 0.01 1 1240 . 124 LEU HG H 0.46 0.01 1 1241 . 124 LEU HD1 H 0.23 0.01 1 1242 . 124 LEU HD2 H 0.01 0.01 1 1243 . 124 LEU C C 169.7 0.1 1 1244 . 124 LEU CA C 51.2 0.1 1 1245 . 124 LEU CB C 39.8 0.1 1 1246 . 124 LEU CG C 23.8 0.1 1 1247 . 124 LEU CD1 C 22.4 0.1 1 1248 . 124 LEU CD2 C 20.3 0.1 1 1249 . 124 LEU N N 114.7 0.1 1 1250 . 125 LYS H H 8.42 0.01 1 1251 . 125 LYS HA H 4.40 0.01 1 1252 . 125 LYS HB2 H 1.73 0.01 2 1253 . 125 LYS HB3 H 1.62 0.01 2 1254 . 125 LYS HG2 H 1.40 0.01 2 1255 . 125 LYS HG3 H 1.36 0.01 2 1256 . 125 LYS HD2 H 1.55 0.01 2 1257 . 125 LYS HD3 H 1.25 0.01 2 1258 . 125 LYS HE2 H 3.28 0.01 2 1259 . 125 LYS C C 173.3 0.1 9 1260 . 125 LYS CA C 52.1 0.1 1 1261 . 125 LYS CG C 22.0 0.1 1 1262 . 125 LYS CD C 25.3 0.1 1 1263 . 125 LYS CE C 56.0 0.1 1 1264 . 125 LYS N N 116.5 0.1 1 1265 . 126 GLU H H 8.08 0.01 1 1266 . 126 GLU HA H 4.32 0.01 1 1267 . 126 GLU HB2 H 1.75 0.01 2 1268 . 126 GLU HB3 H 2.81 0.01 9 1269 . 126 GLU HG2 H 3.38 0.01 2 1270 . 126 GLU HG3 H 3.02 0.01 9 1271 . 126 GLU C C 174.2 0.1 1 1272 . 126 GLU CA C 55.9 0.1 1 1273 . 126 GLU N N 116.4 0.1 1 1274 . 127 HIS H H 7.86 0.01 1 1275 . 127 HIS HA H 4.39 0.01 1 1276 . 127 HIS HB2 H 2.94 0.01 2 1277 . 127 HIS HB3 H 2.87 0.01 2 1278 . 127 HIS HD2 H 6.84 0.01 1 1279 . 127 HIS HE1 H 7.86 0.01 1 1280 . 127 HIS C C 174.4 0.1 1 1281 . 127 HIS CA C 53.2 0.1 1 1282 . 127 HIS CB C 26.7 0.1 1 1283 . 127 HIS CD2 C 116.5 0.1 1 1284 . 127 HIS CE1 C 134.9 0.1 1 1285 . 127 HIS N N 110.0 0.1 1 1286 . 128 ASP H H 7.73 0.01 1 1287 . 128 ASP HA H 4.39 0.01 1 1288 . 128 ASP HB2 H 2.35 0.01 2 1289 . 128 ASP HB3 H 2.26 0.01 2 1290 . 128 ASP C C 171.6 0.1 1 1291 . 128 ASP CA C 52.1 0.1 1 1292 . 128 ASP CB C 38.4 0.1 1 1293 . 128 ASP N N 115.1 0.1 1 1294 . 129 PHE H H 7.61 0.01 1 1295 . 129 PHE HA H 4.33 0.01 1 1296 . 129 PHE HB2 H 2.71 0.01 1 1297 . 129 PHE HB3 H 3.06 0.01 1 1298 . 129 PHE HD1 H 7.19 0.01 3 1299 . 129 PHE HE1 H 7.03 0.01 3 1300 . 129 PHE HZ H 6.84 0.01 1 1301 . 129 PHE C C 172.7 0.1 1 1302 . 129 PHE CA C 55.1 0.1 1 1303 . 129 PHE CB C 37.2 0.1 1 1304 . 129 PHE CD1 C 128.9 0.1 3 1305 . 129 PHE N N 113.9 0.1 1 1306 . 130 ASN H H 8.21 0.01 1 1307 . 130 ASN HA H 4.85 0.01 1 1308 . 130 ASN HB2 H 2.72 0.01 2 1309 . 130 ASN HB3 H 2.56 0.01 2 1310 . 130 ASN HD21 H 7.69 0.01 1 1311 . 130 ASN HD22 H 6.88 0.01 1 1312 . 130 ASN C C 175.3 0.1 9 1313 . 130 ASN CA C 48.3 0.1 1 1314 . 130 ASN CB C 36.1 0.1 1 1315 . 130 ASN N N 115.3 0.1 1 1316 . 130 ASN ND2 N 109.0 0.1 1 1317 . 131 PRO HA H 4.36 0.01 1 1318 . 131 PRO HB2 H 2.21 0.01 2 1319 . 131 PRO HB3 H 1.92 0.01 2 1320 . 131 PRO HG2 H 1.91 0.01 2 1321 . 131 PRO HD2 H 3.66 0.01 2 1322 . 131 PRO HD3 H 3.57 0.01 2 1323 . 131 PRO CA C 60.4 0.1 1 1324 . 131 PRO CB C 28.7 0.1 1 1325 . 131 PRO CD C 47.5 0.1 1 1326 . 132 GLU H H 8.42 0.01 1 1327 . 132 GLU HA H 4.25 0.01 1 1328 . 132 GLU HB2 H 2.24 0.01 2 1329 . 132 GLU HB3 H 2.19 0.01 2 1330 . 132 GLU HG2 H 2.03 0.01 2 1331 . 132 GLU HG3 H 1.89 0.01 2 1332 . 132 GLU C C 174.0 0.1 1 1333 . 132 GLU CA C 53.7 0.1 1 1334 . 132 GLU CG C 26.7 0.1 1 1335 . 132 GLU N N 115.9 0.1 1 1336 . 133 SER H H 8.15 0.01 1 1337 . 133 SER HA H 4.45 0.01 1 1338 . 133 SER HB2 H 3.81 0.01 2 1339 . 133 SER C C 173.5 0.1 1 1340 . 133 SER CA C 55.2 0.1 1 1341 . 133 SER CB C 60.8 0.1 1 1342 . 133 SER N N 112.4 0.1 1 1343 . 134 SER H H 7.96 0.01 1 1344 . 134 SER HA H 4.22 0.01 1 1345 . 134 SER HB2 H 3.76 0.01 2 1346 . 134 SER C C 170.7 0.1 1 1347 . 134 SER CA C 57.0 0.1 1 1348 . 134 SER N N 118.9 0.1 1 stop_ save_