data_5706 #Corrected using PDB structure: 1NY9A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 97 C HA 4.75 3.70 #106 G HA 3.17 3.95 #110 V HA 4.06 5.02 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #104 C CB 26.51 31.60 #112 D CB 42.62 37.34 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted #111 S H 8.17 10.43 #127 A H 10.54 8.35 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 -0.33 -0.08 -0.23 -1.06 -0.03 # #bmr5706.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5706.str file): #HA CA CB CO N HN #N/A -0.20 -0.20 -0.23 -1.06 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.20 +/-0.21 +/-0.18 +/-0.43 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.632 0.960 0.989 0.804 0.805 0.372 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.152 0.922 0.924 0.788 1.961 0.360 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kahmann Jan D. . 2 Sass "Hans Juergen" . . 3 Allan Martin G. . 4 Seto Haruo . . 5 Thompson Charles J. . 6 Grzesiek Stephan . . stop_ _BMRB_accession_number 5706 _BMRB_flat_file_name bmr5706.str _Entry_type new _Submission_date 2003-02-21 _Accession_date 2003-02-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 395 '15N chemical shifts' 103 '13C chemical shifts' 345 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural Basis for Antibiotic Recognition by the TipA Class of Multidrug-resistance Transcriptional Regulators ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 22568288 _PubMed_ID 12682015 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kahmann Jan D. . 2 Sass "Hans Juergen" . . 3 Allan Martin G. . 4 Seto Haruo . . 5 Thompson Charles J. . 6 Grzesiek Stephan . . stop_ _Journal_abbreviation "EMBO J." _Journal_volume 22 _Journal_issue 8 _Page_first 1824 _Page_last 1834 _Year 2003 loop_ _Keyword "Antibiotic recognition" "globin fold" "heteronuclear NMR" "protein dynamics" stop_ save_ ################################## # Molecular system description # ################################## save_system_TipAS _Saveframe_category molecular_system _Mol_system_name TipAS _Abbreviation_common TipAS _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TipAS $TipAS stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function ; Antibiotic binding domain of a multidrug resistance transcriptional regulator ; stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1NY9 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_TipAS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Transcriptional activator tipA" _Name_variant "Transcriptional activator tipAS" _Abbreviation_common TipAS _Molecular_mass 16432 _Mol_thiol_state 'not reported' ############################## # Polymer residue sequence # ############################## _Residue_count 143 _Mol_residue_sequence ; GINLTPEEKFEVFGDFDPDQ YEEEVRERWGNTDAYRQSKE KTASYTKEDWQRIQDEADEL TRRFVALMDAGEPADSEGAM DAAEDHRQGIARNHYDCGYE MHTCLGEMYVSDERFTRNID AAKPGLAAYMRDAILANAVR HTP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 111 GLY 2 112 ILE 3 113 ASN 4 114 LEU 5 115 THR 6 116 PRO 7 117 GLU 8 118 GLU 9 119 LYS 10 120 PHE 11 121 GLU 12 122 VAL 13 123 PHE 14 124 GLY 15 125 ASP 16 126 PHE 17 127 ASP 18 128 PRO 19 129 ASP 20 130 GLN 21 131 TYR 22 132 GLU 23 133 GLU 24 134 GLU 25 135 VAL 26 136 ARG 27 137 GLU 28 138 ARG 29 139 TRP 30 140 GLY 31 141 ASN 32 142 THR 33 143 ASP 34 144 ALA 35 145 TYR 36 146 ARG 37 147 GLN 38 148 SER 39 149 LYS 40 150 GLU 41 151 LYS 42 152 THR 43 153 ALA 44 154 SER 45 155 TYR 46 156 THR 47 157 LYS 48 158 GLU 49 159 ASP 50 160 TRP 51 161 GLN 52 162 ARG 53 163 ILE 54 164 GLN 55 165 ASP 56 166 GLU 57 167 ALA 58 168 ASP 59 169 GLU 60 170 LEU 61 171 THR 62 172 ARG 63 173 ARG 64 174 PHE 65 175 VAL 66 176 ALA 67 177 LEU 68 178 MET 69 179 ASP 70 180 ALA 71 181 GLY 72 182 GLU 73 183 PRO 74 184 ALA 75 185 ASP 76 186 SER 77 187 GLU 78 188 GLY 79 189 ALA 80 190 MET 81 191 ASP 82 192 ALA 83 193 ALA 84 194 GLU 85 195 ASP 86 196 HIS 87 197 ARG 88 198 GLN 89 199 GLY 90 200 ILE 91 201 ALA 92 202 ARG 93 203 ASN 94 204 HIS 95 205 TYR 96 206 ASP 97 207 CYS 98 208 GLY 99 209 TYR 100 210 GLU 101 211 MET 102 212 HIS 103 213 THR 104 214 CYS 105 215 LEU 106 216 GLY 107 217 GLU 108 218 MET 109 219 TYR 110 220 VAL 111 221 SER 112 222 ASP 113 223 GLU 114 224 ARG 115 225 PHE 116 226 THR 117 227 ARG 118 228 ASN 119 229 ILE 120 230 ASP 121 231 ALA 122 232 ALA 123 233 LYS 124 234 PRO 125 235 GLY 126 236 LEU 127 237 ALA 128 238 ALA 129 239 TYR 130 240 MET 131 241 ARG 132 242 ASP 133 243 ALA 134 244 ILE 135 245 LEU 136 246 ALA 137 247 ASN 138 248 ALA 139 249 VAL 140 250 ARG 141 251 HIS 142 252 THR 143 253 PRO stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1NY9 "A Chain A, Antibiotic Binding Domain Of ATipa-Class Multidrug Resistance TranscriptionalRegulator" 100.00 143 100 100 4e-81 DBJ BAD11210.1 "TipA [Expression vector pTip-NH1]" 56.52 253 100 100 4e-81 DBJ BAD11216.1 "TipA [Expression vector pTip-CH1]" 56.52 253 100 100 4e-81 DBJ BAD11222.1 "TipA [Expression vector pTip-NH2]" 56.52 253 100 100 4e-81 DBJ BAD11228.1 "TipA [Expression vector pTip-CH2]" 56.52 253 100 100 4e-81 DBJ BAD11234.1 "TipA [Expression vector pTip-LNH1]" 56.52 253 100 100 4e-81 EMBL CAB42766.1 "transcriptional regulator [Streptomycescoelicolor A3(2)]" 56.52 253 100 100 4e-81 GenBank AAC13653.1 "thiostreptin-induced protein" 99.31 144 100 100 4e-81 GenBank AAB27737.1 "TipAL-AS [Streptomyces lividans]" 56.52 253 100 100 4e-81 PIR S35354 "tipA protein - Streptomyces lividans" 56.52 253 100 100 4e-81 PIR T36339 "transcription regulator - Streptomycescoelicolor" 56.52 253 100 100 4e-81 REF NP_627619.1 "transcriptional regulator[Streptomyces coelicolor A3(2)]" 56.52 253 100 100 4e-81 SWISS-PROT P32184 "TIPA_STRCO HTH-type transcriptional activatortipA" 56.52 253 100 100 4e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TipAS "Streptomyces lividans" 1916 Eubacteria . Streptomyces lividans 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 $TipAS 'recombinant tecHology' "E. coli" Escherichia lividans "XL-1 Blue cells" plasmid "pREP4 and pDS8" stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TipAS 1.5 mM "[U-15N]" stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TipAS 1.5 mM "[U-13C; U-15N]" stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.1 loop_ _Task processing stop_ save_ save_Pipp _Saveframe_category software _Name Pipp _Version 4.3.2 loop_ _Task "data analysis" stop_ save_ save_Xeasy _Saveframe_category software _Name Xeasy _Version 1.2 loop_ _Task "data analysis" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer DRX _Model Bruker _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer DRX _Model Bruker _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCA HN(CO)CA HN(CA)CO HNCO CBCACONH CBCANH HCCH-TOCSY 1H-15N NOESY 1H-13C NOESY ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.9 0.1 n/a temperature 298 0.5 K 'ionic strength' 0.006 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_cs1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TipAS loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 GLY N N 112.93 . 1 2 1 GLY H H 8.23 . 1 3 1 GLY CA C 45.11 . 1 4 1 GLY HA2 H 3.91 . 1 5 1 GLY C C 175.61 . 1 6 2 ILE N N 117.92 . 1 7 2 ILE H H 8.03 . 1 8 2 ILE CA C 60.83 . 1 9 2 ILE HA H 4.18 . 1 10 2 ILE CB C 38.78 . 1 11 2 ILE C C 175.59 . 1 12 3 ASN N N 121.25 . 1 13 3 ASN H H 8.55 . 1 14 3 ASN CA C 52.91 . 1 15 3 ASN CB C 37.68 . 1 16 3 ASN ND2 N 112.36 . 1 17 3 ASN HD21 H 7.55 . 1 18 3 ASN HD22 H 6.89 . 1 19 3 ASN C C 174.50 . 1 20 4 LEU N N 121.75 . 1 21 4 LEU H H 8.24 . 1 22 4 LEU CA C 54.87 . 1 23 4 LEU HA H 4.43 . 1 24 4 LEU CB C 42.43 . 1 25 5 THR CA C 58.56 . 1 26 5 THR CB C 70.24 . 1 27 12 VAL CA C 61.00 . 1 28 12 VAL CB C 31.44 . 1 29 12 VAL C C 178.57 . 1 30 13 PHE N N 114.50 . 1 31 13 PHE H H 7.45 . 1 32 13 PHE CA C 57.52 . 1 33 13 PHE CB C 39.80 . 1 34 13 PHE C C 175.99 . 1 35 14 GLY N N 109.09 . 1 36 14 GLY H H 8.17 . 1 37 14 GLY CA C 45.18 . 1 38 14 GLY HA2 H 3.84 . 1 39 14 GLY C C 173.17 . 1 40 15 ASP N N 119.20 . 1 41 15 ASP H H 8.11 . 1 42 15 ASP CA C 53.93 . 1 43 15 ASP HA H 4.60 . 1 44 15 ASP CB C 41.00 . 1 45 16 PHE N N 118.87 . 1 46 16 PHE H H 8.01 . 1 47 16 PHE CA C 57.21 . 1 48 16 PHE HA H 3.41 . 1 49 16 PHE CB C 39.91 . 1 50 29 TRP C C 176.73 . 1 51 30 GLY N N 107.67 . 1 52 30 GLY H H 7.98 . 1 53 30 GLY CA C 45.90 . 1 54 30 GLY HA2 H 3.87 . 1 55 30 GLY HA3 H 3.73 . 1 56 30 GLY C C 173.57 . 1 57 31 ASN N N 116.19 . 1 58 31 ASN H H 8.21 . 1 59 31 ASN CA C 52.70 . 1 60 31 ASN HA H 4.88 . 1 61 31 ASN CB C 38.70 . 1 62 32 THR CA C 62.00 . 1 63 32 THR CB C 69.80 . 1 64 33 ASP CA C 55.50 . 1 65 33 ASP CB C 40.50 . 1 66 34 ALA CA C 53.10 . 1 67 34 ALA CB C 18.90 . 1 68 35 TYR CA C 58.56 . 1 69 35 TYR CB C 38.12 . 1 70 43 ALA CA C 53.90 . 1 71 43 ALA CB C 18.70 . 1 72 43 ALA C C 178.12 . 1 73 44 SER N N 109.31 . 1 74 44 SER H H 7.61 . 1 75 44 SER CA C 57.80 . 1 76 44 SER CB C 63.70 . 1 77 45 TYR CA C 55.00 . 1 78 45 TYR CB C 36.80 . 1 79 46 THR CA C 59.80 . 1 80 46 THR CB C 72.00 . 1 81 47 LYS CA C 60.20 . 1 82 47 LYS CB C 32.00 . 1 83 48 GLU CA C 59.80 . 1 84 48 GLU CB C 28.60 . 1 85 49 ASP CA C 57.20 . 1 86 49 ASP CB C 40.24 . 1 87 50 TRP N N 116.79 . 1 88 50 TRP H H 7.99 . 1 89 50 TRP CA C 60.04 . 1 90 50 TRP HA H 4.43 . 1 91 50 TRP CB C 29.30 . 1 92 51 GLN CA C 58.30 . 1 93 51 GLN CB C 28.50 . 1 94 52 ARG CA C 59.50 . 1 95 52 ARG CB C 29.00 . 1 96 53 ILE CA C 65.50 . 1 97 53 ILE HA H 4.19 . 1 98 53 ILE CB C 39.00 . 1 99 53 ILE HB H 38.70 . 1 100 54 GLN CA C 58.60 . 1 101 54 GLN CB C 28.10 . 1 102 55 ASP N N 120.45 . 1 103 55 ASP H H 8.73 . 1 104 55 ASP CA C 57.80 . 1 105 55 ASP HA H 4.43 . 1 106 55 ASP CB C 39.80 . 1 107 55 ASP HB2 H 3.00 . 1 108 55 ASP HB3 H 2.72 . 1 109 55 ASP C C 179.76 . 1 110 56 GLU N N 119.71 . 1 111 56 GLU H H 8.35 . 1 112 56 GLU CA C 59.24 . 1 113 56 GLU HA H 4.02 . 1 114 56 GLU CB C 29.44 . 1 115 56 GLU HB2 H 2.19 . 1 116 56 GLU HB3 H 2.03 . 1 117 56 GLU CG C 36.41 . 1 118 56 GLU HG2 H 2.64 . 1 119 56 GLU HG3 H 2.19 . 1 120 56 GLU C C 179.62 . 1 121 57 ALA N N 122.89 . 1 122 57 ALA H H 8.11 . 1 123 57 ALA CA C 55.24 . 1 124 57 ALA HA H 4.30 . 1 125 57 ALA HB H 1.62 . 1 126 57 ALA CB C 18.00 . 1 127 57 ALA C C 180.42 . 1 128 58 ASP N N 119.48 . 1 129 58 ASP H H 8.94 . 1 130 58 ASP CA C 57.28 . 1 131 58 ASP HA H 4.47 . 1 132 58 ASP CB C 40.35 . 1 133 58 ASP HB2 H 2.96 . 1 134 58 ASP HB3 H 2.76 . 1 135 58 ASP C C 178.53 . 1 136 59 GLU N N 119.92 . 1 137 59 GLU H H 8.05 . 1 138 59 GLU CA C 59.17 . 1 139 59 GLU HA H 4.14 . 1 140 59 GLU CB C 28.94 . 1 141 59 GLU HB2 H 2.15 . 1 142 59 GLU CG C 35.87 . 1 143 59 GLU HG2 H 2.35 . 1 144 59 GLU C C 178.66 . 1 145 60 LEU N N 119.67 . 1 146 60 LEU H H 7.74 . 1 147 60 LEU CA C 58.02 . 1 148 60 LEU HA H 4.18 . 1 149 60 LEU CB C 41.78 . 1 150 60 LEU HB2 H 2.15 . 1 151 60 LEU HB3 H 1.88 . 1 152 60 LEU CG C 27.66 . 1 153 60 LEU HG H 1.96 . 1 154 60 LEU HD1 H 1.13 . 1 155 60 LEU CD1 C 25.35 . 1 156 60 LEU C C 178.79 . 1 157 61 THR N N 117.00 . 1 158 61 THR H H 8.77 . 1 159 61 THR CA C 68.17 . 1 160 61 THR HA H 4.06 . 1 161 61 THR HB H 4.50 . 1 162 61 THR HG2 H 1.23 . 1 163 61 THR CG2 C 22.13 . 1 164 61 THR C C 175.77 . 1 165 62 ARG N N 117.97 . 1 166 62 ARG H H 8.15 . 1 167 62 ARG CA C 60.17 . 1 168 62 ARG HA H 3.91 . 1 169 62 ARG CB C 28.41 . 1 170 62 ARG HB2 H 2.07 . 1 171 62 ARG HB3 H 1.91 . 1 172 62 ARG HG3 H 1.62 . 1 173 62 ARG CD C 43.54 . 1 174 62 ARG HD2 H 3.29 . 1 175 62 ARG C C 179.38 . 1 176 63 ARG N N 119.61 . 1 177 63 ARG H H 8.04 . 1 178 63 ARG CA C 59.46 . 1 179 63 ARG HA H 4.06 . 1 180 63 ARG CB C 30.65 . 1 181 63 ARG HB2 H 2.03 . 1 182 63 ARG HB3 H 1.90 . 1 183 63 ARG CG C 26.35 . 1 184 63 ARG HG2 H 1.91 . 1 185 63 ARG HG3 H 1.50 . 1 186 63 ARG CD C 44.62 . 1 187 63 ARG HD2 H 3.28 . 1 188 63 ARG NE N 82.17 . 1 189 63 ARG HE H 7.39 . 1 190 63 ARG C C 179.39 . 1 191 64 PHE N N 117.30 . 1 192 64 PHE H H 8.52 . 1 193 64 PHE CA C 63.45 . 1 194 64 PHE HA H 4.35 . 1 195 64 PHE CB C 40.35 . 1 196 64 PHE HB2 H 3.21 . 1 197 64 PHE HB3 H 3.04 . 1 198 64 PHE HD1 H 7.46 . 1 199 64 PHE HE1 H 7.18 . 1 200 64 PHE HZ H 6.87 . 1 201 64 PHE C C 177.84 . 1 202 65 VAL N N 117.85 . 1 203 65 VAL H H 8.72 . 1 204 65 VAL CA C 67.28 . 1 205 65 VAL HA H 3.37 . 1 206 65 VAL CB C 31.58 . 1 207 65 VAL HB H 2.11 . 1 208 65 VAL HG1 H 0.93 . 1 209 65 VAL HG2 H 1.05 . 1 210 65 VAL CG1 C 24.36 . 1 211 65 VAL CG2 C 21.52 . 1 212 65 VAL C C 176.88 . 1 213 66 ALA N N 119.18 . 1 214 66 ALA H H 8.02 . 1 215 66 ALA CA C 55.04 . 1 216 66 ALA HA H 4.18 . 1 217 66 ALA HB H 1.50 . 1 218 66 ALA CB C 17.88 . 1 219 66 ALA C C 181.43 . 1 220 67 LEU N N 120.40 . 1 221 67 LEU H H 7.69 . 1 222 67 LEU CA C 58.53 . 1 223 67 LEU HA H 3.98 . 1 224 67 LEU CB C 41.56 . 1 225 67 LEU HB2 H 2.23 . 1 226 67 LEU HB3 H 1.82 . 1 227 67 LEU CG C 26.20 . 1 228 67 LEU HG H 1.74 . 1 229 67 LEU HD1 H 0.81 . 1 230 67 LEU HD2 H 0.64 . 1 231 67 LEU CD1 C 23.44 . 1 232 67 LEU C C 178.44 . 1 233 68 MET N N 117.65 . 1 234 68 MET H H 7.95 . 1 235 68 MET CA C 59.68 . 1 236 68 MET HA H 3.58 . 1 237 68 MET CB C 33.36 . 1 238 68 MET HB2 H 1.86 . 1 239 68 MET HB3 H 1.74 . 1 240 68 MET CG C 30.65 . 1 241 68 MET HG2 H 1.94 . 1 242 68 MET HG3 H 1.09 . 1 243 68 MET C C 181.38 . 1 244 69 ASP N N 120.29 . 1 245 69 ASP H H 9.03 . 1 246 69 ASP CA C 56.91 . 1 247 69 ASP HA H 4.39 . 1 248 69 ASP CB C 39.99 . 1 249 69 ASP HB2 H 2.72 . 1 250 69 ASP HB3 H 2.60 . 1 251 69 ASP C C 177.55 . 1 252 70 ALA N N 119.13 . 1 253 70 ALA H H 7.68 . 1 254 70 ALA CA C 52.18 . 1 255 70 ALA HA H 4.39 . 1 256 70 ALA HB H 1.62 . 1 257 70 ALA CB C 19.11 . 1 258 70 ALA C C 177.74 . 1 259 71 GLY N N 106.03 . 1 260 71 GLY H H 7.93 . 1 261 71 GLY CA C 45.46 . 1 262 71 GLY HA2 H 4.14 . 1 263 71 GLY HA3 H 3.82 . 1 264 71 GLY C C 175.44 . 1 265 72 GLU N N 119.12 . 1 266 72 GLU H H 7.90 . 1 267 72 GLU CA C 54.02 . 1 268 72 GLU HA H 4.73 . 1 269 72 GLU CB C 28.45 . 1 270 72 GLU HB2 H 2.19 . 1 271 72 GLU HB3 H 1.82 . 1 272 72 GLU HG2 H 2.41 . 1 273 73 PRO CD C 50.76 . 1 274 73 PRO CA C 62.67 . 1 275 73 PRO HA H 4.75 . 1 276 73 PRO CB C 32.94 . 1 277 73 PRO HB2 H 2.48 . 1 278 73 PRO HB3 H 2.27 . 1 279 73 PRO CG C 27.58 . 1 280 73 PRO HG3 H 2.15 . 1 281 73 PRO HD2 H 4.10 . 1 282 73 PRO C C 176.95 . 1 283 74 ALA N N 123.97 . 1 284 74 ALA H H 9.11 . 1 285 74 ALA CA C 54.26 . 1 286 74 ALA HA H 3.41 . 1 287 74 ALA HB H 0.93 . 1 288 74 ALA CB C 19.32 . 1 289 74 ALA C C 173.21 . 1 290 75 ASP N N 106.01 . 1 291 75 ASP H H 7.39 . 1 292 75 ASP CA C 50.78 . 1 293 75 ASP HA H 4.51 . 1 294 75 ASP CB C 39.42 . 1 295 75 ASP HB2 H 2.27 . 1 296 75 ASP HB3 H 3.03 . 1 297 75 ASP C C 176.58 . 1 298 76 SER N N 112.37 . 1 299 76 SER H H 7.70 . 1 300 76 SER CA C 57.72 . 1 301 76 SER HA H 4.39 . 1 302 76 SER CB C 65.95 . 1 303 76 SER HB3 H 4.14 . 1 304 76 SER C C 174.54 . 1 305 77 GLU N N 120.85 . 1 306 77 GLU H H 9.09 . 1 307 77 GLU CA C 60.59 . 1 308 77 GLU HA H 3.73 . 1 309 77 GLU CB C 29.35 . 1 310 77 GLU HB2 H 2.03 . 1 311 77 GLU CG C 36.41 . 1 312 77 GLU HG2 H 2.31 . 1 313 77 GLU C C 178.05 . 1 314 78 GLY N N 102.40 . 1 315 78 GLY H H 8.71 . 1 316 78 GLY CA C 47.25 . 1 317 78 GLY HA2 H 3.82 . 1 318 78 GLY HA3 H 3.70 . 1 319 78 GLY C C 176.67 . 1 320 79 ALA N N 124.71 . 1 321 79 ALA H H 7.74 . 1 322 79 ALA CA C 55.39 . 1 323 79 ALA HA H 4.06 . 1 324 79 ALA HB H 1.58 . 1 325 79 ALA CB C 18.43 . 1 326 79 ALA C C 179.39 . 1 327 80 MET N N 116.42 . 1 328 80 MET H H 8.61 . 1 329 80 MET CA C 60.37 . 1 330 80 MET HA H 4.10 . 1 331 80 MET CB C 33.72 . 1 332 80 MET HB2 H 2.31 . 1 333 80 MET HB3 H 1.91 . 1 334 80 MET CG C 31.95 . 1 335 80 MET HG2 H 3.05 . 1 336 80 MET HG3 H 2.15 . 1 337 80 MET HE H 1.90 . 1 338 80 MET C C 178.51 . 1 339 81 ASP N N 118.83 . 1 340 81 ASP H H 8.87 . 1 341 81 ASP CA C 57.15 . 1 342 81 ASP HA H 4.31 . 1 343 81 ASP CB C 39.00 . 1 344 81 ASP HB2 H 2.68 . 1 345 81 ASP HB3 H 2.80 . 1 346 81 ASP C C 178.35 . 1 347 82 ALA N N 122.79 . 1 348 82 ALA H H 7.55 . 1 349 82 ALA CA C 55.26 . 1 350 82 ALA HA H 3.94 . 1 351 82 ALA HB H 0.64 . 1 352 82 ALA CB C 15.90 . 1 353 82 ALA C C 178.88 . 1 354 83 ALA N N 119.80 . 1 355 83 ALA H H 8.44 . 1 356 83 ALA CA C 55.48 . 1 357 83 ALA HA H 4.39 . 1 358 83 ALA HB H 1.78 . 1 359 83 ALA CB C 18.32 . 1 360 83 ALA C C 179.32 . 1 361 84 GLU N N 121.06 . 1 362 84 GLU H H 8.83 . 1 363 84 GLU CA C 58.67 . 1 364 84 GLU HA H 4.42 . 1 365 84 GLU CB C 27.23 . 1 366 84 GLU HB2 H 2.48 . 1 367 84 GLU HB3 H 2.23 . 1 368 84 GLU CG C 34.41 . 1 369 84 GLU HG2 H 2.72 . 1 370 84 GLU HG3 H 2.35 . 1 371 84 GLU C C 178.35 . 1 372 85 ASP N N 120.32 . 1 373 85 ASP H H 8.30 . 1 374 85 ASP CA C 57.38 . 1 375 85 ASP HA H 4.47 . 1 376 85 ASP CB C 39.57 . 1 377 85 ASP HB2 H 2.68 . 1 378 85 ASP HB3 H 2.92 . 1 379 85 ASP C C 179.85 . 1 380 86 HIS N N 123.48 . 1 381 86 HIS H H 8.83 . 1 382 86 HIS CA C 61.28 . 1 383 86 HIS HA H 4.22 . 1 384 86 HIS CB C 31.58 . 1 385 86 HIS HB2 H 3.41 . 1 386 86 HIS HD2 H 6.82 . 1 387 86 HIS C C 177.41 . 1 388 87 ARG N N 121.52 . 1 389 87 ARG H H 8.37 . 1 390 87 ARG CA C 59.98 . 1 391 87 ARG HA H 3.05 . 1 392 87 ARG CB C 30.65 . 1 393 87 ARG HB2 H 1.17 . 1 394 87 ARG HB3 H 1.86 . 1 395 87 ARG HG2 H 2.36 . 1 396 87 ARG HG3 H 0.57 . 1 397 87 ARG NE N 79.83 . 1 398 87 ARG HE H 6.67 . 1 399 87 ARG C C 178.51 . 1 400 88 GLN N N 114.30 . 1 401 88 GLN H H 8.49 . 1 402 88 GLN CA C 58.41 . 1 403 88 GLN HA H 3.82 . 1 404 88 GLN CB C 27.73 . 1 405 88 GLN HB2 H 2.12 . 1 406 88 GLN HB3 H 2.03 . 1 407 88 GLN CG C 33.80 . 1 408 88 GLN HG2 H 2.68 . 1 409 88 GLN HG3 H 2.36 . 1 410 88 GLN NE2 N 112.42 . 1 411 88 GLN C C 178.94 . 1 412 89 GLY N N 107.86 . 1 413 89 GLY H H 8.25 . 1 414 89 GLY CA C 46.90 . 1 415 89 GLY HA2 H 3.90 . 1 416 89 GLY HA3 H 3.69 . 1 417 89 GLY C C 175.44 . 1 418 90 ILE N N 122.21 . 1 419 90 ILE H H 7.65 . 1 420 90 ILE CA C 65.02 . 1 421 90 ILE HA H 3.62 . 1 422 90 ILE HB H 1.94 . 1 423 90 ILE HG2 H 0.72 . 1 424 90 ILE HD1 H 0.68 . 1 425 90 ILE C C 178.43 . 1 426 91 ALA N N 120.58 . 1 427 91 ALA H H 7.93 . 1 428 91 ALA CA C 53.44 . 1 429 91 ALA HA H 4.39 . 1 430 91 ALA HB H 1.34 . 1 431 91 ALA CB C 18.29 . 1 432 91 ALA C C 179.31 . 1 433 92 ARG N N 114.83 . 1 434 92 ARG H H 8.03 . 1 435 92 ARG CA C 58.25 . 1 436 92 ARG HA H 3.98 . 1 437 92 ARG CB C 31.23 . 1 438 92 ARG HB2 H 1.82 . 1 439 92 ARG HB3 H 1.71 . 1 440 92 ARG CG C 27.66 . 1 441 92 ARG CD C 43.47 . 1 442 92 ARG C C 177.61 . 1 443 93 ASN N N 111.19 . 1 444 93 ASN H H 7.82 . 1 445 93 ASN CA C 53.69 . 1 446 93 ASN HA H 4.59 . 1 447 93 ASN CB C 40.13 . 1 448 97 CYS CA C 58.10 . 1 449 97 CYS HA H 4.79 . 1 450 97 CYS CB C 27.02 . 1 451 97 CYS C C 172.87 . 1 452 98 GLY N N 112.06 . 1 453 98 GLY H H 8.18 . 1 454 98 GLY CA C 44.55 . 1 455 98 GLY C C 173.41 . 1 456 99 TYR N N 115.75 . 1 457 99 TYR H H 8.33 . 1 458 99 TYR CA C 65.09 . 1 459 99 TYR HA H 4.02 . 1 460 99 TYR CB C 38.07 . 1 461 99 TYR HB2 H 2.84 . 1 462 99 TYR HB3 H 3.12 . 1 463 99 TYR HD1 H 7.36 . 1 464 99 TYR HE1 H 6.67 . 1 465 99 TYR C C 177.82 . 1 466 100 GLU N N 118.88 . 1 467 100 GLU H H 8.95 . 1 468 100 GLU CA C 60.05 . 1 469 100 GLU HA H 4.14 . 1 470 100 GLU CB C 29.92 . 1 471 100 GLU HB2 H 2.15 . 1 472 100 GLU HB3 H 2.07 . 1 473 100 GLU CG C 36.64 . 1 474 100 GLU HG2 H 2.35 . 1 475 100 GLU C C 179.37 . 1 476 101 MET N N 119.48 . 1 477 101 MET H H 8.04 . 1 478 101 MET CA C 58.20 . 1 479 101 MET HA H 4.02 . 1 480 101 MET CB C 32.44 . 1 481 101 MET C C 177.55 . 1 482 102 HIS N N 119.54 . 1 483 102 HIS H H 8.80 . 1 484 102 HIS CA C 59.12 . 1 485 102 HIS HA H 4.10 . 1 486 102 HIS CB C 33.36 . 1 487 102 HIS HB2 H 3.24 . 1 488 102 HIS HB3 H 3.00 . 1 489 102 HIS C C 177.76 . 1 490 103 THR N N 106.86 . 1 491 103 THR H H 8.28 . 1 492 103 THR CA C 65.66 . 1 493 103 THR HA H 4.30 . 1 494 103 THR CB C 68.73 . 1 495 103 THR HB H 3.90 . 1 496 103 THR HG2 H 1.38 . 1 497 103 THR C C 176.46 . 1 498 104 CYS N N 120.60 . 1 499 104 CYS H H 7.42 . 1 500 104 CYS CA C 62.90 . 1 501 104 CYS HA H 4.14 . 1 502 104 CYS CB C 26.38 . 1 503 104 CYS HB2 H 3.25 . 1 504 104 CYS HB3 H 2.96 . 1 505 104 CYS C C 177.32 . 1 506 105 LEU N N 121.00 . 1 507 105 LEU H H 8.08 . 1 508 105 LEU CA C 57.86 . 1 509 105 LEU HA H 4.10 . 1 510 105 LEU CB C 41.14 . 1 511 105 LEU HB2 H 1.83 . 1 512 105 LEU HB3 H 1.38 . 1 513 105 LEU HG H 1.56 . 1 514 105 LEU HD2 H 0.91 . 1 515 105 LEU CD1 C 25.89 . 1 516 105 LEU CD2 C 23.90 . 1 517 105 LEU C C 177.22 . 1 518 106 GLY N N 101.68 . 1 519 106 GLY H H 8.14 . 1 520 106 GLY CA C 47.33 . 1 521 106 GLY HA2 H 3.29 . 1 522 106 GLY HA3 H 3.13 . 1 523 106 GLY C C 174.66 . 1 524 107 GLU N N 115.68 . 1 525 107 GLU H H 7.70 . 1 526 107 GLU CA C 58.23 . 1 527 107 GLU HA H 4.18 . 1 528 107 GLU CB C 28.99 . 1 529 107 GLU HB2 H 2.03 . 1 530 107 GLU CG C 34.95 . 1 531 107 GLU HG2 H 2.35 . 1 532 107 GLU C C 180.04 . 1 533 108 MET N N 121.09 . 1 534 108 MET H H 7.82 . 1 535 108 MET CA C 58.61 . 1 536 108 MET HA H 4.15 . 1 537 108 MET CB C 32.19 . 1 538 108 MET HB2 H 2.60 . 1 539 108 MET HB3 H 2.35 . 1 540 108 MET HG2 H 2.10 . 1 541 108 MET C C 177.47 . 1 542 109 TYR N N 114.63 . 1 543 109 TYR H H 7.77 . 1 544 109 TYR CA C 57.37 . 1 545 109 TYR HA H 4.43 . 1 546 109 TYR CB C 35.93 . 1 547 109 TYR HB2 H 3.38 . 1 548 109 TYR HB3 H 2.93 . 1 549 109 TYR C C 176.53 . 1 550 110 VAL N N 108.44 . 1 551 110 VAL H H 6.95 . 1 552 110 VAL CA C 62.22 . 1 553 110 VAL HA H 4.10 . 1 554 110 VAL CB C 32.94 . 1 555 110 VAL HB H 2.15 . 1 556 110 VAL CG1 C 21.59 . 1 557 110 VAL CG2 C 17.45 . 1 558 110 VAL HG1 H 0.89 . 1 559 110 VAL C C 176.12 . 1 560 111 SER N N 113.76 . 1 561 111 SER H H 8.20 . 1 562 111 SER CA C 59.74 . 1 563 111 SER HA H 4.46 . 1 564 111 SER CB C 64.16 . 1 565 111 SER HB2 H 3.98 . 1 566 111 SER HB3 H 3.86 . 1 567 111 SER C C 173.76 . 1 568 112 ASP N N 121.96 . 1 569 112 ASP H H 8.12 . 1 570 112 ASP CA C 52.91 . 1 571 112 ASP HA H 4.92 . 1 572 112 ASP CB C 42.49 . 1 573 112 ASP HB2 H 3.37 . 1 574 112 ASP HB3 H 2.52 . 1 575 112 ASP C C 175.87 . 1 576 113 GLU N N 124.96 . 1 577 113 GLU H H 8.89 . 1 578 113 GLU CA C 59.04 . 1 579 113 GLU HA H 4.18 . 1 580 113 GLU CB C 29.44 . 1 581 113 GLU HB2 H 2.11 . 1 582 113 GLU CG C 35.87 . 1 583 113 GLU HG2 H 2.35 . 1 584 113 GLU C C 177.18 . 1 585 114 ARG N N 116.76 . 1 586 114 ARG H H 8.30 . 1 587 114 ARG CA C 58.91 . 1 588 114 ARG HA H 3.94 . 1 589 114 ARG HG2 H 1.60 . 1 590 114 ARG NE N 83.25 . 1 591 114 ARG HE H 7.67 . 1 592 115 PHE N N 116.14 . 1 593 115 PHE H H 7.87 . 1 594 115 PHE CA C 59.63 . 1 595 115 PHE C C 177.92 . 1 596 116 THR N N 115.52 . 1 597 116 THR H H 8.57 . 1 598 116 THR CA C 67.04 . 1 599 116 THR HA H 3.76 . 1 600 116 THR CB C 69.23 . 1 601 116 THR HB H 3.94 . 1 602 116 THR HG2 H 1.25 . 1 603 116 THR C C 175.93 . 1 604 117 ARG N N 115.14 . 1 605 117 ARG H H 8.25 . 1 606 117 ARG CA C 58.99 . 1 607 117 ARG HA H 4.02 . 1 608 117 ARG CB C 30.08 . 1 609 117 ARG HB2 H 1.95 . 1 610 117 ARG HB3 H 1.82 . 1 611 117 ARG CG C 27.20 . 1 612 117 ARG HG2 H 1.74 . 1 613 117 ARG HG3 H 1.66 . 1 614 117 ARG CD C 43.62 . 1 615 117 ARG HD2 H 3.19 . 1 616 117 ARG NE N 83.06 . 1 617 117 ARG HE H 7.38 . 1 618 117 ARG C C 178.37 . 1 619 118 ASN N N 114.92 . 1 620 118 ASN H H 7.12 . 1 621 118 ASN CA C 55.87 . 1 622 118 ASN HA H 4.47 . 1 623 118 ASN CB C 39.57 . 1 624 118 ASN HB2 H 2.71 . 1 625 118 ASN C C 176.50 . 1 626 119 ILE N N 120.14 . 1 627 119 ILE H H 8.19 . 1 628 119 ILE CA C 64.67 . 1 629 119 ILE HA H 3.73 . 1 630 119 ILE CB C 39.07 . 1 631 119 ILE HB H 1.66 . 1 632 119 ILE HG2 H 0.77 . 1 633 119 ILE CG2 C 17.30 . 1 634 119 ILE HD1 H 0.32 . 1 635 119 ILE C C 177.99 . 1 636 120 ASP N N 117.35 . 1 637 120 ASP H H 8.67 . 1 638 120 ASP CA C 55.47 . 1 639 120 ASP HA H 4.71 . 1 640 120 ASP CB C 39.00 . 1 641 120 ASP HB2 H 2.68 . 1 642 120 ASP HB3 H 2.84 . 1 643 120 ASP C C 177.32 . 1 644 121 ALA N N 121.39 . 1 645 121 ALA H H 7.05 . 1 646 121 ALA CA C 54.58 . 1 647 121 ALA HA H 4.06 . 1 648 121 ALA HB H 1.46 . 1 649 121 ALA CB C 18.32 . 1 650 121 ALA C C 179.25 . 1 651 122 ALA N N 115.93 . 1 652 122 ALA H H 7.58 . 1 653 122 ALA CA C 53.58 . 1 654 122 ALA HA H 4.22 . 1 655 122 ALA HB H 1.38 . 1 656 122 ALA CB C 19.25 . 1 657 122 ALA C C 177.98 . 1 658 123 LYS N N 115.63 . 1 659 123 LYS H H 6.74 . 1 660 123 LYS CA C 54.07 . 1 661 123 LYS HA H 4.47 . 1 662 123 LYS HB2 H 1.62 . 1 663 123 LYS HB3 H 2.11 . 1 664 123 LYS HG2 H 1.45 . 1 665 123 LYS HG3 H 1.38 . 1 666 123 LYS HD2 H 1.78 . 1 667 124 PRO CD C 51.22 . 1 668 124 PRO CA C 64.09 . 1 669 124 PRO CB C 31.65 . 1 670 124 PRO HB2 H 2.35 . 1 671 124 PRO HB3 H 1.87 . 1 672 124 PRO CG C 27.73 . 1 673 124 PRO HG3 H 2.02 . 1 674 124 PRO HD2 H 3.90 . 1 675 124 PRO C C 177.23 . 1 676 125 GLY N N 111.11 . 1 677 125 GLY H H 8.62 . 1 678 125 GLY CA C 45.06 . 1 679 125 GLY HA2 H 4.26 . 1 680 125 GLY HA3 H 3.94 . 1 681 125 GLY C C 174.68 . 1 682 126 LEU N N 125.24 . 1 683 126 LEU H H 7.96 . 1 684 126 LEU CA C 57.72 . 1 685 126 LEU HA H 4.29 . 1 686 126 LEU CB C 41.63 . 1 687 126 LEU HB2 H 2.03 . 1 688 126 LEU CG C 27.27 . 1 689 126 LEU HG H 1.27 . 1 690 126 LEU HD1 H 0.93 . 1 691 126 LEU HD2 H 0.76 . 1 692 126 LEU C C 177.06 . 1 693 127 ALA N N 124.27 . 1 694 127 ALA H H 10.57 . 1 695 127 ALA CA C 56.36 . 1 696 127 ALA HA H 3.74 . 1 697 127 ALA HB H 1.38 . 1 698 127 ALA CB C 17.83 . 1 699 127 ALA C C 178.82 . 1 700 128 ALA N N 117.42 . 1 701 128 ALA H H 8.25 . 1 702 128 ALA CA C 54.59 . 1 703 128 ALA HA H 3.82 . 1 704 128 ALA HB H 1.38 . 1 705 128 ALA CB C 17.78 . 1 706 128 ALA C C 178.53 . 1 707 129 TYR N N 119.83 . 1 708 129 TYR H H 7.94 . 1 709 129 TYR CA C 62.07 . 1 710 129 TYR HA H 4.10 . 1 711 129 TYR CB C 39.85 . 1 712 129 TYR HB2 H 3.04 . 1 713 129 TYR HB3 H 3.29 . 1 714 129 TYR HD1 H 7.00 . 1 715 129 TYR C C 177.55 . 1 716 130 MET N N 115.25 . 1 717 130 MET H H 9.02 . 1 718 130 MET CA C 60.14 . 1 719 130 MET HA H 3.29 . 1 720 130 MET CB C 33.08 . 1 721 130 MET HB2 H 1.98 . 1 722 130 MET CG C 31.26 . 1 723 130 MET HG2 H 2.19 . 1 724 130 MET HG3 H 0.63 . 1 725 130 MET HE H 1.46 . 1 726 130 MET C C 177.69 . 1 727 131 ARG N N 117.53 . 1 728 131 ARG H H 8.45 . 1 729 131 ARG CA C 60.72 . 1 730 131 ARG HA H 3.49 . 1 731 131 ARG CB C 28.16 . 1 732 131 ARG HB2 H 2.02 . 1 733 131 ARG HB3 H 1.94 . 1 734 131 ARG CG C 26.20 . 1 735 131 ARG HG2 H 1.58 . 1 736 131 ARG HG3 H 1.21 . 1 737 131 ARG CD C 42.54 . 1 738 131 ARG HD2 H 3.17 . 1 739 131 ARG NE N 82.93 . 1 740 131 ARG HE H 7.45 . 1 741 131 ARG C C 178.27 . 1 742 132 ASP N N 118.85 . 1 743 132 ASP H H 8.25 . 1 744 132 ASP CA C 57.44 . 1 745 132 ASP HA H 4.18 . 1 746 132 ASP CB C 39.85 . 1 747 132 ASP HB2 H 2.64 . 1 748 132 ASP HB3 H 2.27 . 1 749 132 ASP C C 178.50 . 1 750 133 ALA N N 126.17 . 1 751 133 ALA H H 8.61 . 1 752 133 ALA CA C 54.80 . 1 753 133 ALA HA H 4.43 . 1 754 133 ALA HB H 1.50 . 1 755 133 ALA CB C 19.11 . 1 756 133 ALA C C 179.76 . 1 757 134 ILE N N 119.71 . 1 758 134 ILE H H 8.85 . 1 759 134 ILE CA C 65.70 . 1 760 134 ILE HA H 3.62 . 1 761 134 ILE CB C 37.71 . 1 762 134 ILE HB H 1.91 . 1 763 134 ILE HG2 H 0.35 . 1 764 134 ILE CG2 C 15.44 . 1 765 134 ILE CG1 C 29.96 . 1 766 134 ILE HD1 H 0.28 . 1 767 134 ILE C C 179.38 . 1 768 135 LEU N N 120.75 . 1 769 135 LEU H H 8.37 . 1 770 135 LEU CA C 58.31 . 1 771 135 LEU HA H 4.06 . 1 772 135 LEU CB C 41.21 . 1 773 135 LEU HB2 H 1.78 . 1 774 135 LEU HB3 H 1.66 . 1 775 135 LEU CG C 27.73 . 1 776 135 LEU CD1 C 23.97 . 1 777 135 LEU HD1 H 0.89 . 1 778 135 LEU C C 178.80 . 1 779 136 ALA N N 120.20 . 1 780 136 ALA H H 8.20 . 1 781 136 ALA CA C 55.17 . 1 782 136 ALA HA H 4.11 . 1 783 136 ALA HB H 1.54 . 1 784 136 ALA CB C 17.03 . 1 785 136 ALA C C 180.68 . 1 786 137 ASN N N 116.28 . 1 787 137 ASN H H 8.97 . 1 788 137 ASN CA C 56.36 . 1 789 137 ASN HA H 4.63 . 1 790 137 ASN CB C 40.35 . 1 791 137 ASN HB2 H 2.92 . 1 792 137 ASN HB3 H 3.21 . 1 793 137 ASN ND2 N 120.71 . 1 794 137 ASN HD21 H 9.51 . 1 795 137 ASN HD22 H 8.82 . 1 796 137 ASN C C 176.99 . 1 797 138 ALA N N 123.55 . 1 798 138 ALA H H 8.42 . 1 799 138 ALA CA C 55.78 . 1 800 138 ALA HA H 3.94 . 1 801 138 ALA HB H 1.66 . 1 802 138 ALA CB C 18.39 . 1 803 138 ALA C C 180.72 . 1 804 139 VAL N N 119.46 . 1 805 139 VAL H H 8.28 . 1 806 139 VAL CA C 66.54 . 1 807 139 VAL HA H 3.62 . 1 808 139 VAL CB C 31.44 . 1 809 139 VAL HB H 2.23 . 1 810 139 VAL HG1 H 0.93 . 1 811 139 VAL HG2 H 1.09 . 1 812 139 VAL CG1 C 22.90 . 1 813 139 VAL CG2 C 21.13 . 1 814 139 VAL C C 179.41 . 1 815 140 ARG N N 115.61 . 1 816 140 ARG H H 7.63 . 1 817 140 ARG CA C 57.85 . 1 818 140 ARG HA H 4.31 . 1 819 140 ARG CB C 28.94 . 1 820 140 ARG HB2 H 1.89 . 1 821 140 ARG HB3 H 1.86 . 1 822 140 ARG CG C 26.12 . 1 823 140 ARG HG3 H 1.09 . 1 824 140 ARG CD C 44.16 . 1 825 140 ARG HD2 H 3.09 . 1 826 140 ARG NE N 83.31 . 1 827 140 ARG HE H 6.89 . 1 828 140 ARG C C 176.05 . 1 829 141 HIS N N 114.94 . 1 830 141 HIS H H 7.20 . 1 831 141 HIS CA C 56.56 . 1 832 141 HIS HA H 4.51 . 1 833 141 HIS CB C 28.66 . 1 834 141 HIS HB2 H 1.91 . 1 835 141 HIS HB3 H 3.16 . 1 836 141 HIS HE1 H 8.66 . 1 837 141 HIS C C 173.07 . 1 838 142 THR N N 117.25 . 1 839 142 THR H H 7.49 . 1 840 142 THR CA C 60.59 . 1 841 142 THR HA H 4.55 . 1 842 142 THR HB H 4.23 . 1 843 142 THR HG2 H 1.30 . 1 stop_ save_