data_4736 #Corrected using PDB structure: 1QLZA # #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 # 33 R HA 3.89 3.18 # 44 Y HA 5.53 4.71 # 52 S HA 4.52 3.72 # 54 Q HA 2.92 4.29 #100 Y HA 2.88 4.22 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 51 Y CA 27.03 55.86 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 45 Y N 110.51 121.68 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.00 0.33 0.53 N/A -0.49 -0.14 # #bmr4736.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4736.str file): #HA CA CB CO N HN #N/A +0.43 +0.43 N/A -0.49 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.18 +/-0.18 N/A +/-0.29 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.715 0.839 0.995 N/A 0.742 0.400 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.149 0.905 0.863 N/A 1.433 0.348 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N Chemical Shift Assignment for the human prion protein variant M166V ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Calzolai Luigi . . 6 Zahn Ralph . . 3 Guntert Peter . . 7 Wuthrich Kurt . . 4 "von Schroetter" Christine . . 5 Riek Roland . . 2 Lysek Dominikus . . stop_ _BMRB_accession_number 4736 _BMRB_flat_file_name bmr4736.str _Entry_type new _Submission_date 2000-05-10 _Accession_date 2000-05-10 _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' 668 '13C chemical shifts' 355 '15N chemical shifts' 126 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR structures of three single-residue variants of the human prion protein ; _Citation_status submitted _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Calzolai Luigi . . 6 Zahn Ralph . . 3 Guntert Peter . . 7 Wuthrich Kurt . . 4 "von Schroetter" Christine . . 5 Riek Roland . . 2 Lysek Dominikus . . stop_ _Journal_abbreviation "Proc. Natl. Acad. Sci. U.S.A." _Journal_volume ? _Page_first ? _Page_last ? _Year ? loop_ _Keyword "prion protein" stop_ save_ ################################## # Molecular system description # ################################## save_hPrP(M166V) _Saveframe_category molecular_system _Mol_system_name "human prion protein variant M166V" _Abbreviation_common hPrP(M166V) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hPrP $hPrP stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1QM2A " Chain A, Human Prion Protein Fragment 121-230" . PDB 1QM3A " Chain A, Human Prion Protein Fragment 121-230" . PDB 1QM0A " Chain A, Human Prion Protein Fragment 90-230" . PDB 1QM1A " Chain A, Human Prion Protein Fragment 90-230" . PDB 1QLXA " Chain A, Human Prion Protein" . PDB 1QLZA " Chain A, Human Prion Protein" . stop_ save_ ######################## # Monomeric polymers # ######################## save_hPrP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "human prion protein" _Name_variant M166V _Abbreviation_common hPrP _Mol_thiol_state 'not reported' ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; GSVVGGLGGYMLGSAMSRPI IHFGSDYEDRYYRENMHRYP NQVYYRPVDEYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCITQY ERESQAYYQRGS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 119 GLY 2 120 SER 3 121 VAL 4 122 VAL 5 123 GLY 6 124 GLY 7 125 LEU 8 126 GLY 9 127 GLY 10 128 TYR 11 129 MET 12 130 LEU 13 131 GLY 14 132 SER 15 133 ALA 16 134 MET 17 135 SER 18 136 ARG 19 137 PRO 20 138 ILE 21 139 ILE 22 140 HIS 23 141 PHE 24 142 GLY 25 143 SER 26 144 ASP 27 145 TYR 28 146 GLU 29 147 ASP 30 148 ARG 31 149 TYR 32 150 TYR 33 151 ARG 34 152 GLU 35 153 ASN 36 154 MET 37 155 HIS 38 156 ARG 39 157 TYR 40 158 PRO 41 159 ASN 42 160 GLN 43 161 VAL 44 162 TYR 45 163 TYR 46 164 ARG 47 165 PRO 48 166 VAL 49 167 ASP 50 168 GLU 51 169 TYR 52 170 SER 53 171 ASN 54 172 GLN 55 173 ASN 56 174 ASN 57 175 PHE 58 176 VAL 59 177 HIS 60 178 ASP 61 179 CYS 62 180 VAL 63 181 ASN 64 182 ILE 65 183 THR 66 184 ILE 67 185 LYS 68 186 GLN 69 187 HIS 70 188 THR 71 189 VAL 72 190 THR 73 191 THR 74 192 THR 75 193 THR 76 194 LYS 77 195 GLY 78 196 GLU 79 197 ASN 80 198 PHE 81 199 THR 82 200 GLU 83 201 THR 84 202 ASP 85 203 VAL 86 204 LYS 87 205 MET 88 206 MET 89 207 GLU 90 208 ARG 91 209 VAL 92 210 VAL 93 211 GLU 94 212 GLN 95 213 MET 96 214 CYS 97 215 ILE 98 216 THR 99 217 GLN 100 218 TYR 101 219 GLU 102 220 ARG 103 221 GLU 104 222 SER 105 223 GLN 106 224 ALA 107 225 TYR 108 226 TYR 109 227 GLN 110 228 ARG 111 229 GLY 112 230 SER 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 1E1G "A Chain A, Human Prion Protein Variant M166v" 107.69 104 100 100 3e-57 PDB 1E1J "A Chain A, Human Prion Protein Variant M166v" 107.69 104 100 100 3e-57 PDB 1HJM "A Chain A, Human Prion Protein At Ph 7.0" 107.69 104 99 100 7e-57 PDB 1HJN "A Chain A, Human Prion Protein At Ph 7.0" 107.69 104 99 100 7e-57 PDB 1E1P "A Chain A, Human Prion Protein Variant S170n" 107.69 104 98 100 2e-56 PDB 1E1S "A Chain A, Human Prion Protein Variant S170n" 107.69 104 98 100 2e-56 PDB 1E1U "A Chain A, Human Prion Protein Variant R220k" 107.69 104 98 100 2e-56 PDB 1E1W "A Chain A, Human Prion Protein Variant R220k" 107.69 104 98 100 2e-56 PDB 1I4M "A Chain A, Crystal Structure Of The HumanPrion Protein Reveals A Mechanism For Oligomerization" 103.70 108 98 100 3e-59 PDB 1QM2 "A Chain A, Human Prion Protein Fragment 121-230" 100.00 112 99 100 6e-62 PDB 1QM3 "A Chain A, Human Prion Protein Fragment 121-230" 100.00 112 99 100 6e-62 PDB 1H0L "A Chain A, Human Prion Protein 121-230M166cE221C" 100.00 112 98 98 5e-60 PDB 1QM0 "A Chain A, Human Prion Protein Fragment 90-230" 78.32 143 98 100 10e-62 PDB 1QM1 "A Chain A, Human Prion Protein Fragment 90-230" 78.32 143 98 100 10e-62 PDB 1QLX "A Chain A, Human Prion Protein" 53.33 210 98 100 10e-62 PDB 1QLZ "A Chain A, Human Prion Protein" 53.33 210 98 100 10e-62 DBJ BAA00011.1 "prion protein [Homo sapiens]" 45.71 245 98 100 10e-62 EMBL CAA58442.1 "prion protein [Homo sapiens]" 45.71 245 98 100 10e-62 EMBL CAB75503.1 "dJ1068H6.2 (prion protein (p27-30)(Creutzfeld-Jakob disease, Gerstmann-Strausler-Scheinkersyndrome, fatal familial insomnia)) [Homo sapiens]" 44.27 253 98 100 10e-62 GenBank AAB59443.1 "prion protein" 48.07 233 98 100 10e-62 GenBank AAO83635.1 "prion protein [Homo sapiens]" 47.06 238 98 100 10e-62 GenBank AAA19664.1 "prion protein" 45.71 245 98 100 10e-62 GenBank AAR21603.1 "prion protein [Homo sapiens]" 40.43 277 98 100 10e-62 GenBank AAC62750.2 "prion protein precursor; PRNP [Homosapiens]" 39.30 285 98 100 10e-62 PIR UJHU "major prion protein precursor - human" 44.27 253 98 100 10e-62 REF NP_000302.1 "prion protein preproprotein;prion-related protein; major prion protein; CD230antigen [Homo sapiens]" 44.27 253 98 100 10e-62 REF NP_898902.1 "prion protein preproprotein;prion-related protein; major prion protein; CD230antigen [Homo sapiens]" 44.27 253 98 100 10e-62 SWISS-PROT P04156 "PRIO_HUMAN Major prion protein precursor (PrP)(PrP27-30) (PrP33-35C) (ASCR) (CD230 antigen)" 44.27 253 98 100 10e-62 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hPrP human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $hPrP 'recombinant technology' . . . . . 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 $hPrP 1.2 mM "[U-95% 13C; U-95% 15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.1 n/a temperature 293 0.2 K 'ionic strength' 0.05 . 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 . . . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name hPrP 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 CA C 43.43 . 1 2 1 GLY HA3 H 3.87 . 1 3 1 GLY HA2 H 3.87 . 1 4 2 SER N N 115.21 . 1 5 2 SER H H 8.64 . 1 6 2 SER CA C 58.13 . 1 7 2 SER HA H 4.56 . 1 8 2 SER CB C 63.93 . 1 9 2 SER HB2 H 3.80 . 1 10 2 SER HB3 H 3.80 . 1 11 3 VAL N N 121.71 . 1 12 3 VAL H H 8.37 . 1 13 3 VAL CA C 62.33 . 1 14 3 VAL HA H 4.16 . 1 15 3 VAL CB C 32.73 . 1 16 3 VAL HB H 2.01 . 1 17 3 VAL HG1 H 0.84 . 2 18 3 VAL HG2 H 0.88 . 2 19 3 VAL CG1 C 21.33 . 1 20 3 VAL CG2 C 20.83 . 1 21 4 VAL N N 124.21 . 1 22 4 VAL H H 8.29 . 1 23 4 VAL CA C 62.53 . 1 24 4 VAL HA H 4.06 . 1 25 4 VAL CB C 32.73 . 1 26 4 VAL HB H 1.99 . 1 27 4 VAL HG1 H 0.85 . 2 28 4 VAL HG2 H 0.88 . 2 29 4 VAL CG1 C 21.33 . 1 30 4 VAL CG2 C 20.93 . 1 31 5 GLY N N 112.91 . 1 32 5 GLY H H 8.57 . 1 33 5 GLY CA C 45.53 . 1 34 5 GLY HA3 H 3.91 . 1 35 5 GLY HA2 H 3.91 . 1 36 6 GLY N N 108.11 . 1 37 6 GLY H H 8.28 . 1 38 6 GLY CA C 45.43 . 1 39 6 GLY HA3 H 3.91 . 1 40 6 GLY HA2 H 3.91 . 1 41 7 LEU N N 121.31 . 1 42 7 LEU H H 8.23 . 1 43 7 LEU CA C 54.83 . 1 44 7 LEU HA H 4.33 . 1 45 7 LEU CB C 42.53 . 1 46 7 LEU HB2 H 1.51 . 2 47 7 LEU HB3 H 1.59 . 2 48 7 LEU CG C 26.93 . 1 49 7 LEU HG H 1.48 . 1 50 7 LEU HD1 H 0.66 . 2 51 7 LEU HD2 H 0.56 . 2 52 7 LEU CD1 C 24.83 . 1 53 7 LEU CD2 C 23.73 . 1 54 8 GLY N N 109.41 . 1 55 8 GLY H H 8.54 . 1 56 8 GLY CA C 46.43 . 1 57 8 GLY HA3 H 3.83 . 2 58 8 GLY HA2 H 3.88 . 2 59 9 GLY N N 108.71 . 1 60 9 GLY H H 8.35 . 1 61 9 GLY CA C 45.13 . 1 62 9 GLY HA3 H 3.73 . 2 63 9 GLY HA2 H 3.88 . 2 64 10 TYR N N 117.31 . 1 65 10 TYR H H 7.72 . 1 66 10 TYR CA C 58.13 . 1 67 10 TYR HA H 4.42 . 1 68 10 TYR CB C 40.23 . 1 69 10 TYR HB2 H 2.89 . 2 70 10 TYR HB3 H 2.81 . 2 71 10 TYR HD1 H 6.82 . 1 72 10 TYR HD2 H 6.82 . 1 73 10 TYR HE1 H 6.62 . 1 74 10 TYR HE2 H 6.62 . 1 75 10 TYR CD1 C 133.23 . 1 76 10 TYR CE1 C 118.43 . 1 77 11 MET N N 120.71 . 1 78 11 MET H H 9.05 . 1 79 11 MET CA C 53.93 . 1 80 11 MET HA H 4.48 . 1 81 11 MET CB C 34.83 . 1 82 11 MET HB2 H 0.93 . 2 83 11 MET HB3 H 1.56 . 2 84 11 MET CG C 32.33 . 1 85 11 MET HG2 H 2.20 . 1 86 11 MET HG3 H 2.20 . 1 87 11 MET HE H 1.95 . 1 88 11 MET CE C 17.43 . 1 89 12 LEU N N 120.91 . 1 90 12 LEU H H 8.09 . 1 91 12 LEU CA C 53.43 . 1 92 12 LEU HA H 4.40 . 1 93 12 LEU CB C 43.73 . 1 94 12 LEU HB2 H 0.92 . 2 95 12 LEU HB3 H 1.58 . 2 96 12 LEU CG C 26.23 . 1 97 12 LEU HG H 1.35 . 1 98 12 LEU HD1 H -0.06 . 2 99 12 LEU HD2 H 0.59 . 2 100 12 LEU CD1 C 21.83 . 1 101 12 LEU CD2 C 26.03 . 1 102 13 GLY N N 114.51 . 1 103 13 GLY H H 9.35 . 1 104 13 GLY CA C 44.83 . 1 105 13 GLY HA3 H 4.01 . 2 106 13 GLY HA2 H 4.37 . 2 107 14 SER N N 113.11 . 1 108 14 SER H H 8.39 . 1 109 14 SER CA C 58.63 . 1 110 14 SER HA H 4.38 . 1 111 14 SER CB C 64.03 . 1 112 14 SER HB2 H 3.96 . 2 113 14 SER HB3 H 3.87 . 2 114 15 ALA N N 125.11 . 1 115 15 ALA H H 8.77 . 1 116 15 ALA CA C 53.03 . 1 117 15 ALA HA H 4.41 . 1 118 15 ALA HB H 1.24 . 1 119 15 ALA CB C 18.53 . 1 120 16 MET N N 120.61 . 1 121 16 MET H H 8.73 . 1 122 16 MET CA C 53.93 . 1 123 16 MET HA H 4.71 . 1 124 16 MET CB C 37.13 . 1 125 16 MET HB2 H 1.98 . 1 126 16 MET HB3 H 1.98 . 1 127 16 MET CG C 31.13 . 1 128 16 MET HG2 H 2.37 . 2 129 16 MET HG3 H 2.43 . 2 130 16 MET HE H 2.13 . 1 131 16 MET CE C 17.83 . 1 132 17 SER N N 115.71 . 1 133 17 SER H H 8.44 . 1 134 17 SER CA C 58.53 . 1 135 17 SER HA H 4.30 . 1 136 17 SER CB C 63.03 . 1 137 17 SER HB2 H 3.79 . 2 138 17 SER HB3 H 3.71 . 2 139 18 ARG N N 126.31 . 1 140 18 ARG H H 8.65 . 1 141 18 ARG CA C 54.93 . 1 142 18 ARG HA H 4.37 . 1 143 18 ARG CB C 29.73 . 1 144 18 ARG HB2 H 1.69 . 1 145 18 ARG HB3 H 1.69 . 1 146 18 ARG HG2 H 1.84 . 2 147 18 ARG HG3 H 1.77 . 2 148 18 ARG CD C 43.93 . 1 149 18 ARG HD2 H 2.99 . 2 150 18 ARG HD3 H 3.08 . 2 151 18 ARG NE N 85.50 . 1 152 18 ARG HE H 6.69 . 1 153 19 PRO CD C 50.73 . 1 154 19 PRO CA C 62.33 . 1 155 19 PRO HA H 4.39 . 1 156 19 PRO CB C 32.53 . 1 157 19 PRO HB2 H 1.71 . 2 158 19 PRO HB3 H 2.21 . 2 159 19 PRO CG C 27.63 . 1 160 19 PRO HG2 H 1.95 . 2 161 19 PRO HG3 H 1.99 . 2 162 19 PRO HD2 H 3.59 . 2 163 19 PRO HD3 H 3.89 . 2 164 20 ILE N N 121.91 . 1 165 20 ILE H H 8.64 . 1 166 20 ILE CA C 60.93 . 1 167 20 ILE HA H 4.11 . 1 168 20 ILE CB C 36.43 . 1 169 20 ILE HB H 1.88 . 1 170 20 ILE HG2 H 0.69 . 1 171 20 ILE CG2 C 17.63 . 1 172 20 ILE CG1 C 27.43 . 1 173 20 ILE HG12 H 1.54 . 2 174 20 ILE HG13 H 1.34 . 2 175 20 ILE HD1 H 0.85 . 1 176 20 ILE CD1 C 11.53 . 1 177 21 ILE N N 126.31 . 1 178 21 ILE H H 6.44 . 1 179 21 ILE CA C 58.83 . 1 180 21 ILE HA H 3.86 . 1 181 21 ILE CB C 39.43 . 1 182 21 ILE HB H 0.78 . 1 183 21 ILE HG2 H -0.10 . 1 184 21 ILE CG2 C 17.43 . 1 185 21 ILE CG1 C 26.73 . 1 186 21 ILE HG12 H 0.90 . 2 187 21 ILE HG13 H 0.74 . 2 188 21 ILE HD1 H 0.44 . 1 189 21 ILE CD1 C 12.73 . 1 190 22 HIS N N 121.51 . 1 191 22 HIS H H 8.24 . 1 192 22 HIS CA C 54.13 . 1 193 22 HIS HA H 4.89 . 1 194 22 HIS CB C 29.43 . 1 195 22 HIS HB2 H 3.29 . 2 196 22 HIS HB3 H 2.91 . 2 197 22 HIS CD2 C 120.03 . 1 198 22 HIS CE1 C 136.43 . 1 199 22 HIS HD2 H 7.22 . 1 200 22 HIS HE1 H 8.52 . 1 201 23 PHE N N 123.51 . 1 202 23 PHE H H 10.21 . 1 203 23 PHE CA C 59.53 . 1 204 23 PHE HA H 4.33 . 1 205 23 PHE CB C 41.53 . 1 206 23 PHE HB2 H 2.77 . 2 207 23 PHE HB3 H 3.30 . 2 208 23 PHE HD1 H 7.26 . 1 209 23 PHE HD2 H 7.26 . 1 210 23 PHE HE1 H 6.82 . 1 211 23 PHE HE2 H 6.82 . 1 212 23 PHE CD1 C 132.33 . 1 213 23 PHE CE1 C 131.43 . 1 214 23 PHE CZ C 129.43 . 1 215 23 PHE HZ H 6.69 . 1 216 24 GLY N N 108.01 . 1 217 24 GLY H H 9.01 . 1 218 24 GLY CA C 45.73 . 1 219 24 GLY HA3 H 3.77 . 2 220 24 GLY HA2 H 4.16 . 2 221 25 SER N N 111.21 . 1 222 25 SER H H 7.29 . 1 223 25 SER CA C 56.73 . 1 224 25 SER HA H 4.75 . 1 225 25 SER CB C 66.03 . 1 226 25 SER HB2 H 4.09 . 2 227 25 SER HB3 H 3.85 . 2 228 26 ASP N N 124.01 . 1 229 26 ASP H H 9.05 . 1 230 26 ASP CA C 57.73 . 1 231 26 ASP HA H 4.47 . 1 232 26 ASP CB C 40.63 . 1 233 26 ASP HB2 H 2.73 . 1 234 26 ASP HB3 H 2.73 . 1 235 27 TYR N N 118.41 . 1 236 27 TYR H H 8.58 . 1 237 27 TYR CA C 61.43 . 1 238 27 TYR HA H 4.16 . 1 239 27 TYR CB C 38.13 . 1 240 27 TYR HB2 H 3.22 . 2 241 27 TYR HB3 H 2.80 . 2 242 27 TYR HD1 H 7.00 . 1 243 27 TYR HD2 H 7.00 . 1 244 27 TYR HE1 H 6.74 . 1 245 27 TYR HE2 H 6.74 . 1 246 27 TYR CD1 C 133.53 . 1 247 27 TYR CE1 C 118.23 . 1 248 28 GLU N N 118.41 . 1 249 28 GLU H H 7.71 . 1 250 28 GLU CA C 59.73 . 1 251 28 GLU HA H 3.59 . 1 252 28 GLU CB C 29.73 . 1 253 28 GLU HB2 H 1.92 . 2 254 28 GLU HB3 H 1.54 . 2 255 28 GLU CG C 36.93 . 1 256 28 GLU HG2 H 2.29 . 2 257 28 GLU HG3 H 1.92 . 2 258 29 ASP N N 119.21 . 1 259 29 ASP H H 8.20 . 1 260 29 ASP CA C 58.53 . 1 261 29 ASP HA H 4.65 . 1 262 29 ASP CB C 40.43 . 1 263 29 ASP HB2 H 2.85 . 2 264 29 ASP HB3 H 3.02 . 2 265 30 ARG N N 119.81 . 1 266 30 ARG H H 8.21 . 1 267 30 ARG CA C 59.73 . 1 268 30 ARG HA H 3.98 . 1 269 30 ARG CB C 29.73 . 1 270 30 ARG HB2 H 1.87 . 1 271 30 ARG HB3 H 1.87 . 1 272 30 ARG CG C 27.93 . 1 273 30 ARG HG2 H 1.51 . 2 274 30 ARG HG3 H 1.72 . 2 275 30 ARG CD C 43.43 . 1 276 30 ARG HD2 H 3.16 . 2 277 30 ARG HD3 H 3.18 . 2 278 30 ARG NE N 84.70 . 1 279 30 ARG HE H 7.45 . 1 280 31 TYR N N 120.81 . 1 281 31 TYR H H 8.30 . 1 282 31 TYR CA C 62.23 . 1 283 31 TYR HA H 3.80 . 1 284 31 TYR CB C 38.13 . 1 285 31 TYR HB2 H 2.85 . 2 286 31 TYR HB3 H 2.60 . 2 287 31 TYR HD1 H 6.92 . 1 288 31 TYR HD2 H 6.92 . 1 289 31 TYR HE1 H 6.73 . 1 290 31 TYR HE2 H 6.73 . 1 291 31 TYR CD1 C 133.63 . 1 292 31 TYR CE1 C 118.43 . 1 293 32 TYR N N 120.11 . 1 294 32 TYR H H 8.97 . 1 295 32 TYR CA C 63.03 . 1 296 32 TYR HA H 4.09 . 1 297 32 TYR CB C 38.13 . 1 298 32 TYR HB2 H 3.50 . 2 299 32 TYR HB3 H 3.23 . 2 300 32 TYR HD1 H 7.48 . 1 301 32 TYR HD2 H 7.48 . 1 302 32 TYR HE1 H 6.95 . 1 303 32 TYR HE2 H 6.95 . 1 304 32 TYR CD1 C 133.83 . 1 305 32 TYR CE1 C 118.43 . 1 306 33 ARG N N 117.31 . 1 307 33 ARG H H 7.99 . 1 308 33 ARG CA C 59.73 . 1 309 33 ARG HA H 3.89 . 1 310 33 ARG CB C 29.93 . 1 311 33 ARG HB2 H 2.05 . 2 312 33 ARG HB3 H 1.92 . 2 313 33 ARG CG C 28.33 . 1 314 33 ARG HG2 H 1.70 . 2 315 33 ARG HG3 H 1.98 . 2 316 33 ARG CD C 43.43 . 1 317 33 ARG HD2 H 3.35 . 2 318 33 ARG HD3 H 3.25 . 2 319 33 ARG NE N 84.00 . 1 320 33 ARG HE H 7.50 . 1 321 34 GLU N N 115.91 . 1 322 34 GLU H H 8.06 . 1 323 34 GLU CA C 58.13 . 1 324 34 GLU HA H 4.05 . 1 325 34 GLU CB C 29.43 . 1 326 34 GLU HB2 H 1.86 . 1 327 34 GLU HB3 H 1.86 . 1 328 34 GLU CG C 35.33 . 1 329 34 GLU HG2 H 2.41 . 2 330 34 GLU HG3 H 2.24 . 2 331 35 ASN N N 114.21 . 1 332 35 ASN H H 7.61 . 1 333 35 ASN CA C 54.83 . 1 334 35 ASN HA H 4.24 . 1 335 35 ASN CB C 41.13 . 1 336 35 ASN HB2 H 2.12 . 1 337 35 ASN HB3 H 2.12 . 1 338 35 ASN ND2 N 117.10 . 1 339 35 ASN HD21 H 6.69 . 2 340 35 ASN HD22 H 6.58 . 2 341 36 MET N N 119.31 . 1 342 36 MET H H 8.13 . 1 343 36 MET CA C 59.23 . 1 344 36 MET HA H 3.41 . 1 345 36 MET CB C 30.43 . 1 346 36 MET HB2 H 1.28 . 2 347 36 MET HB3 H 1.62 . 2 348 36 MET CG C 30.63 . 1 349 36 MET HG2 H 2.49 . 2 350 36 MET HG3 H 2.10 . 2 351 36 MET HE H 1.98 . 1 352 36 MET CE C 17.83 . 1 353 37 HIS N N 114.61 . 1 354 37 HIS H H 8.09 . 1 355 37 HIS CA C 57.63 . 1 356 37 HIS HA H 4.18 . 1 357 37 HIS CB C 27.33 . 1 358 37 HIS HB2 H 3.06 . 2 359 37 HIS HB3 H 3.28 . 2 360 37 HIS CD2 C 120.73 . 1 361 37 HIS HD2 H 7.36 . 1 362 38 ARG N N 117.61 . 1 363 38 ARG H H 7.60 . 1 364 38 ARG CA C 56.23 . 1 365 38 ARG HA H 4.10 . 1 366 38 ARG CB C 30.63 . 1 367 38 ARG HB2 H 1.41 . 2 368 38 ARG HB3 H 2.06 . 2 369 38 ARG CG C 27.33 . 1 370 38 ARG HG2 H 1.35 . 2 371 38 ARG HG3 H 0.36 . 2 372 38 ARG CD C 44.13 . 1 373 38 ARG HD2 H 3.06 . 2 374 38 ARG HD3 H 3.21 . 2 375 38 ARG NE N 83.80 . 1 376 38 ARG HE H 7.39 . 1 377 39 TYR N N 120.61 . 1 378 39 TYR H H 7.48 . 1 379 39 TYR CA C 52.73 . 1 380 39 TYR HA H 4.99 . 1 381 39 TYR CB C 35.03 . 1 382 39 TYR HB2 H 3.08 . 1 383 39 TYR HB3 H 3.08 . 1 384 39 TYR HD1 H 6.82 . 1 385 39 TYR HD2 H 6.82 . 1 386 39 TYR HE1 H 6.50 . 1 387 39 TYR HE2 H 6.50 . 1 388 39 TYR CD1 C 131.63 . 1 389 39 TYR CE1 C 117.43 . 1 390 40 PRO CD C 50.23 . 1 391 40 PRO CA C 63.73 . 1 392 40 PRO HA H 4.43 . 1 393 40 PRO CB C 32.53 . 1 394 40 PRO HB2 H 1.67 . 2 395 40 PRO HB3 H 2.42 . 2 396 40 PRO CG C 27.33 . 1 397 40 PRO HG2 H 1.52 . 2 398 40 PRO HG3 H 1.30 . 2 399 40 PRO HD2 H 3.12 . 2 400 40 PRO HD3 H 3.36 . 2 401 41 ASN N N 115.81 . 1 402 41 ASN H H 8.56 . 1 403 41 ASN CA C 52.03 . 1 404 41 ASN HA H 4.69 . 1 405 41 ASN CB C 38.33 . 1 406 41 ASN HB2 H 3.69 . 2 407 41 ASN HB3 H 2.38 . 2 408 41 ASN ND2 N 109.00 . 1 409 41 ASN HD21 H 7.47 . 2 410 41 ASN HD22 H 6.76 . 2 411 42 GLN N N 113.41 . 1 412 42 GLN H H 7.26 . 1 413 42 GLN CA C 53.93 . 1 414 42 GLN HA H 4.51 . 1 415 42 GLN CB C 33.93 . 1 416 42 GLN HB2 H 1.67 . 2 417 42 GLN HB3 H 1.95 . 2 418 42 GLN CG C 34.33 . 1 419 42 GLN HG2 H 2.12 . 2 420 42 GLN HG3 H 2.00 . 2 421 42 GLN NE2 N 112.70 . 1 422 42 GLN HE21 H 7.92 . 2 423 42 GLN HE22 H 6.99 . 2 424 43 VAL N N 112.31 . 1 425 43 VAL H H 8.50 . 1 426 43 VAL CA C 58.83 . 1 427 43 VAL HA H 4.90 . 1 428 43 VAL CB C 34.13 . 1 429 43 VAL HB H 2.58 . 1 430 43 VAL HG1 H 0.92 . 2 431 43 VAL HG2 H 0.70 . 2 432 43 VAL CG1 C 23.73 . 1 433 43 VAL CG2 C 18.53 . 1 434 44 TYR N N 120.71 . 1 435 44 TYR H H 8.43 . 1 436 44 TYR CA C 57.03 . 1 437 44 TYR HA H 5.53 . 1 438 44 TYR CB C 42.03 . 1 439 44 TYR HB2 H 2.54 . 2 440 44 TYR HB3 H 2.86 . 2 441 44 TYR HD1 H 6.87 . 1 442 44 TYR HD2 H 6.87 . 1 443 44 TYR HE1 H 6.72 . 1 444 44 TYR HE2 H 6.72 . 1 445 44 TYR CD1 C 133.23 . 1 446 44 TYR CE1 C 118.63 . 1 447 45 TYR N N 110.51 . 1 448 45 TYR H H 8.57 . 1 449 45 TYR CA C 55.83 . 1 450 45 TYR HA H 4.71 . 1 451 45 TYR HB2 H 2.58 . 2 452 45 TYR HB3 H 2.82 . 2 453 45 TYR HD1 H 7.08 . 1 454 45 TYR HD2 H 7.08 . 1 455 45 TYR HE1 H 6.42 . 1 456 45 TYR HE2 H 6.42 . 1 457 45 TYR CD1 C 134.23 . 1 458 45 TYR CE1 C 117.73 . 1 459 46 ARG N N 120.01 . 1 460 46 ARG H H 7.94 . 1 461 46 ARG CA C 53.73 . 1 462 46 ARG HA H 4.59 . 1 463 46 ARG CB C 30.13 . 1 464 46 ARG HB2 H 1.67 . 1 465 46 ARG HB3 H 1.67 . 1 466 46 ARG CG C 28.03 . 1 467 46 ARG HG2 H 1.07 . 2 468 46 ARG HG3 H 0.94 . 2 469 46 ARG CD C 43.43 . 1 470 46 ARG HD2 H 2.81 . 2 471 46 ARG HD3 H 2.76 . 2 472 46 ARG NE N 84.20 . 1 473 46 ARG HE H 6.80 . 1 474 47 PRO CD C 50.43 . 1 475 47 PRO CA C 63.73 . 1 476 47 PRO HA H 4.52 . 1 477 47 PRO CB C 32.73 . 1 478 47 PRO HB2 H 2.43 . 2 479 47 PRO HB3 H 1.88 . 2 480 47 PRO CG C 28.33 . 1 481 47 PRO HG2 H 2.10 . 2 482 47 PRO HG3 H 1.97 . 2 483 47 PRO HD2 H 3.42 . 2 484 47 PRO HD3 H 3.60 . 2 485 48 VAL N N 118.91 . 1 486 48 VAL H H 8.49 . 1 487 48 VAL CA C 65.33 . 1 488 48 VAL HA H 4.21 . 1 489 48 VAL CB C 32.23 . 1 490 48 VAL HB H 1.97 . 1 491 48 VAL HG1 H 0.71 . 2 492 48 VAL HG2 H 0.74 . 2 493 48 VAL CG1 C 51.63 . 1 494 48 VAL CG2 C 51.83 . 1 495 49 ASP N N 118.01 . 1 496 49 ASP H H 8.44 . 1 497 49 ASP CA C 54.13 . 1 498 49 ASP HA H 4.49 . 1 499 49 ASP CB C 38.83 . 1 500 49 ASP HB2 H 2.97 . 2 501 49 ASP HB3 H 2.58 . 2 502 50 GLU N N 116.61 . 1 503 50 GLU H H 8.35 . 1 504 50 GLU CA C 55.63 . 1 505 50 GLU HA H 4.50 . 1 506 50 GLU CB C 29.23 . 1 507 50 GLU HB2 H 3.28 . 2 508 50 GLU HB3 H 3.21 . 2 509 51 TYR CA C 27.13 . 1 510 51 TYR HA H 4.88 . 1 511 51 TYR CB C 42.03 . 1 512 51 TYR HB2 H 3.29 . 2 513 51 TYR HB3 H 3.02 . 2 514 51 TYR HD1 H 7.31 . 1 515 51 TYR HD2 H 7.31 . 1 516 51 TYR HE1 H 6.88 . 1 517 51 TYR HE2 H 6.88 . 1 518 51 TYR CD1 C 134.23 . 1 519 51 TYR CE1 C 118.93 . 1 520 52 SER CA C 59.03 . 1 521 52 SER HA H 4.52 . 1 522 52 SER CB C 63.93 . 1 523 52 SER HB2 H 4.00 . 2 524 52 SER HB3 H 3.94 . 2 525 53 ASN CA C 52.53 . 1 526 53 ASN HA H 4.73 . 1 527 53 ASN CB C 40.23 . 1 528 53 ASN HB2 H 3.14 . 2 529 53 ASN HB3 H 2.98 . 2 530 53 ASN ND2 N 113.40 . 1 531 53 ASN HD21 H 7.51 . 2 532 53 ASN HD22 H 6.69 . 2 533 54 GLN N N 119.51 . 1 534 54 GLN H H 8.66 . 1 535 54 GLN CA C 59.03 . 1 536 54 GLN HA H 2.92 . 1 537 54 GLN CB C 29.23 . 1 538 54 GLN HB2 H 1.66 . 2 539 54 GLN HB3 H 1.55 . 2 540 54 GLN CG C 33.43 . 1 541 54 GLN HG2 H 1.73 . 2 542 54 GLN HG3 H 1.03 . 2 543 54 GLN NE2 N 111.00 . 1 544 54 GLN HE21 H 6.94 . 2 545 54 GLN HE22 H 6.93 . 2 546 55 ASN N N 117.11 . 1 547 55 ASN H H 8.43 . 1 548 55 ASN CA C 56.43 . 1 549 55 ASN HA H 4.19 . 1 550 55 ASN CB C 37.83 . 1 551 55 ASN HB2 H 2.61 . 2 552 55 ASN HB3 H 2.71 . 2 553 55 ASN ND2 N 112.90 . 1 554 55 ASN HD21 H 7.58 . 2 555 55 ASN HD22 H 6.94 . 2 556 56 ASN N N 118.01 . 1 557 56 ASN H H 8.63 . 1 558 56 ASN CA C 56.03 . 1 559 56 ASN HA H 4.54 . 1 560 56 ASN CB C 38.13 . 1 561 56 ASN HB2 H 2.90 . 2 562 56 ASN HB3 H 3.15 . 2 563 56 ASN ND2 N 111.90 . 1 564 56 ASN HD21 H 7.64 . 2 565 56 ASN HD22 H 7.18 . 2 566 57 PHE HD1 H 6.71 . 1 567 57 PHE HD2 H 6.71 . 1 568 57 PHE HE1 H 7.86 . 1 569 57 PHE HE2 H 7.86 . 1 570 57 PHE CD1 C 129.63 . 1 571 57 PHE CE1 C 132.63 . 1 572 57 PHE CZ C 133.23 . 1 573 57 PHE HZ H 7.22 . 1 574 58 VAL N N 119.81 . 1 575 58 VAL H H 8.89 . 1 576 58 VAL CA C 67.63 . 1 577 58 VAL HA H 3.41 . 1 578 58 VAL CB C 32.23 . 1 579 58 VAL HB H 2.18 . 1 580 58 VAL HG1 H 0.99 . 2 581 58 VAL HG2 H 1.03 . 2 582 58 VAL CG1 C 22.03 . 1 583 58 VAL CG2 C 24.83 . 1 584 59 HIS N N 116.01 . 1 585 59 HIS H H 8.39 . 1 586 59 HIS CA C 59.23 . 1 587 59 HIS HA H 4.27 . 1 588 59 HIS CB C 28.53 . 1 589 59 HIS HB2 H 3.32 . 2 590 59 HIS HB3 H 3.36 . 2 591 59 HIS CD2 C 120.43 . 1 592 59 HIS CE1 C 136.43 . 1 593 59 HIS HD2 H 7.38 . 1 594 59 HIS HE1 H 8.63 . 1 595 60 ASP N N 118.01 . 1 596 60 ASP H H 7.51 . 1 597 60 ASP CA C 57.23 . 1 598 60 ASP HA H 4.55 . 1 599 60 ASP CB C 41.13 . 1 600 60 ASP HB2 H 2.94 . 2 601 60 ASP HB3 H 2.90 . 2 602 61 CYS N N 118.71 . 1 603 61 CYS H H 8.11 . 1 604 61 CYS CA C 58.63 . 1 605 61 CYS HA H 4.64 . 1 606 61 CYS CB C 40.63 . 1 607 61 CYS HB2 H 2.85 . 2 608 61 CYS HB3 H 3.21 . 2 609 62 VAL N N 124.41 . 1 610 62 VAL H H 9.15 . 1 611 62 VAL CA C 66.53 . 1 612 62 VAL HA H 3.62 . 1 613 62 VAL CB C 32.13 . 1 614 62 VAL HB H 2.13 . 1 615 62 VAL HG1 H 0.92 . 2 616 62 VAL HG2 H 1.05 . 2 617 62 VAL CG1 C 21.83 . 1 618 62 VAL CG2 C 23.63 . 1 619 63 ASN N N 115.81 . 1 620 63 ASN H H 7.59 . 1 621 63 ASN CA C 56.53 . 1 622 63 ASN HA H 4.28 . 1 623 63 ASN CB C 38.83 . 1 624 63 ASN HB2 H 2.85 . 2 625 63 ASN HB3 H 2.77 . 2 626 63 ASN ND2 N 112.00 . 1 627 63 ASN HD21 H 7.66 . 2 628 63 ASN HD22 H 6.77 . 2 629 64 ILE N N 118.41 . 1 630 64 ILE H H 8.77 . 1 631 64 ILE CA C 62.13 . 1 632 64 ILE HA H 3.70 . 1 633 64 ILE CB C 36.63 . 1 634 64 ILE HB H 1.53 . 1 635 64 ILE HG2 H 0.19 . 1 636 64 ILE CG2 C 18.53 . 1 637 64 ILE CG1 C 27.83 . 1 638 64 ILE HG12 H 0.84 . 2 639 64 ILE HG13 H 0.80 . 2 640 64 ILE HD1 H 0.36 . 1 641 64 ILE CD1 C 11.63 . 1 642 65 THR N N 117.61 . 1 643 65 THR H H 8.13 . 1 644 65 THR CA C 68.63 . 1 645 65 THR HA H 4.03 . 1 646 65 THR CB C 68.43 . 1 647 65 THR HB H 4.45 . 1 648 65 THR HG2 H 1.46 . 1 649 65 THR HG1 H 6.34 . 1 650 65 THR CG2 C 22.43 . 1 651 66 ILE N N 120.31 . 1 652 66 ILE H H 8.52 . 1 653 66 ILE CA C 65.83 . 1 654 66 ILE HA H 3.68 . 1 655 66 ILE CB C 36.73 . 1 656 66 ILE HB H 2.07 . 1 657 66 ILE HG2 H 0.85 . 1 658 66 ILE CG2 C 16.93 . 1 659 66 ILE CG1 C 29.73 . 1 660 66 ILE HG12 H 1.76 . 2 661 66 ILE HG13 H 1.24 . 2 662 66 ILE HD1 H 0.72 . 1 663 66 ILE CD1 C 12.93 . 1 664 67 LYS N N 122.41 . 1 665 67 LYS H H 8.06 . 1 666 67 LYS CA C 59.93 . 1 667 67 LYS HA H 4.02 . 1 668 67 LYS CB C 32.33 . 1 669 67 LYS HB2 H 1.83 . 2 670 67 LYS HB3 H 1.93 . 2 671 67 LYS CG C 25.23 . 1 672 67 LYS HG2 H 1.44 . 2 673 67 LYS HG3 H 1.34 . 2 674 67 LYS CD C 29.23 . 1 675 67 LYS HD2 H 1.57 . 1 676 67 LYS HD3 H 1.57 . 1 677 67 LYS CE C 41.83 . 1 678 67 LYS HE2 H 2.86 . 1 679 67 LYS HE3 H 2.86 . 1 680 68 GLN N N 115.81 . 1 681 68 GLN H H 8.36 . 1 682 68 GLN CA C 57.63 . 1 683 68 GLN HA H 4.00 . 1 684 68 GLN CB C 28.33 . 1 685 68 GLN HB2 H 1.83 . 2 686 68 GLN HB3 H 1.95 . 2 687 68 GLN CG C 33.63 . 1 688 68 GLN HG2 H 2.06 . 2 689 68 GLN HG3 H 1.50 . 2 690 68 GLN NE2 N 110.10 . 1 691 68 GLN HE21 H 6.76 . 2 692 68 GLN HE22 H 6.69 . 2 693 69 HIS N N 117.51 . 1 694 69 HIS H H 8.16 . 1 695 69 HIS CA C 58.53 . 1 696 69 HIS HA H 4.56 . 1 697 69 HIS CB C 29.93 . 1 698 69 HIS HB2 H 3.31 . 2 699 69 HIS HB3 H 3.27 . 2 700 69 HIS CD2 C 119.23 . 1 701 69 HIS HD2 H 7.29 . 1 702 70 THR N N 113.21 . 1 703 70 THR H H 8.23 . 1 704 70 THR CA C 65.03 . 1 705 70 THR HA H 4.23 . 1 706 70 THR CB C 69.33 . 1 707 70 THR HB H 4.38 . 1 708 70 THR HG2 H 1.20 . 1 709 70 THR CG2 C 21.53 . 1 710 71 VAL N N 121.61 . 1 711 71 VAL H H 8.00 . 1 712 71 VAL CA C 64.63 . 1 713 71 VAL HA H 4.02 . 1 714 71 VAL CB C 32.23 . 1 715 71 VAL HB H 2.17 . 1 716 71 VAL HG1 H 0.93 . 2 717 71 VAL HG2 H 0.98 . 2 718 71 VAL CG1 C 21.33 . 1 719 71 VAL CG2 C 21.53 . 1 720 72 THR N N 114.51 . 1 721 72 THR H H 8.08 . 1 722 72 THR CA C 64.63 . 1 723 72 THR HA H 4.02 . 1 724 72 THR CB C 69.53 . 1 725 72 THR HB H 4.24 . 1 726 72 THR HG2 H 1.23 . 1 727 72 THR CG2 C 21.83 . 1 728 73 THR N N 114.31 . 1 729 73 THR H H 8.01 . 1 730 73 THR CA C 63.43 . 1 731 73 THR HA H 4.25 . 1 732 73 THR CB C 69.33 . 1 733 73 THR HB H 4.18 . 1 734 73 THR HG2 H 1.04 . 1 735 73 THR CG2 C 21.63 . 1 736 74 THR N N 116.21 . 1 737 74 THR H H 8.19 . 1 738 74 THR CA C 63.73 . 1 739 74 THR HA H 4.26 . 1 740 74 THR CB C 69.33 . 1 741 74 THR HB H 4.33 . 1 742 74 THR HG2 H 1.20 . 1 743 74 THR CG2 C 21.53 . 1 744 75 THR N N 115.61 . 1 745 75 THR H H 7.92 . 1 746 75 THR CA C 63.43 . 1 747 75 THR HA H 4.37 . 1 748 75 THR CB C 69.53 . 1 749 75 THR HB H 4.33 . 1 750 75 THR HG2 H 1.23 . 1 751 75 THR CG2 C 21.83 . 1 752 76 LYS N N 120.61 . 1 753 76 LYS H H 7.83 . 1 754 76 LYS CA C 56.73 . 1 755 76 LYS HA H 4.28 . 1 756 76 LYS CB C 32.53 . 1 757 76 LYS HB2 H 1.90 . 2 758 76 LYS HB3 H 1.78 . 2 759 76 LYS CG C 25.13 . 1 760 76 LYS HG2 H 1.47 . 2 761 76 LYS HG3 H 1.41 . 2 762 76 LYS CD C 29.03 . 1 763 76 LYS HD2 H 1.66 . 1 764 76 LYS HD3 H 1.66 . 1 765 76 LYS CE C 41.83 . 1 766 76 LYS HE2 H 2.92 . 1 767 76 LYS HE3 H 2.92 . 1 768 77 GLY N N 108.41 . 1 769 77 GLY H H 8.12 . 1 770 77 GLY CA C 45.63 . 1 771 77 GLY HA3 H 4.16 . 2 772 77 GLY HA2 H 3.77 . 2 773 78 GLU N N 119.51 . 1 774 78 GLU H H 7.70 . 1 775 78 GLU CA C 55.83 . 1 776 78 GLU HA H 4.23 . 1 777 78 GLU CB C 30.43 . 1 778 78 GLU HB2 H 1.68 . 1 779 78 GLU HB3 H 1.68 . 1 780 78 GLU CG C 35.33 . 1 781 78 GLU HG2 H 2.12 . 1 782 78 GLU HG3 H 2.12 . 1 783 79 ASN N N 119.21 . 1 784 79 ASN H H 8.45 . 1 785 79 ASN CA C 53.03 . 1 786 79 ASN HA H 4.62 . 1 787 79 ASN CB C 39.93 . 1 788 79 ASN HB2 H 2.67 . 2 789 79 ASN HB3 H 2.58 . 2 790 79 ASN ND2 N 113.00 . 1 791 79 ASN HD21 H 7.53 . 2 792 79 ASN HD22 H 6.82 . 2 793 80 PHE N N 121.41 . 1 794 80 PHE H H 8.67 . 1 795 80 PHE CA C 56.93 . 1 796 80 PHE HA H 5.21 . 1 797 80 PHE CB C 40.23 . 1 798 80 PHE HB2 H 3.13 . 2 799 80 PHE HB3 H 2.95 . 2 800 80 PHE HD1 H 7.27 . 1 801 80 PHE HD2 H 7.27 . 1 802 80 PHE HE1 H 7.45 . 1 803 80 PHE HE2 H 7.45 . 1 804 80 PHE CD1 C 131.83 . 1 805 80 PHE CE1 C 130.33 . 1 806 81 THR N N 115.61 . 1 807 81 THR H H 9.51 . 1 808 81 THR CA C 60.63 . 1 809 81 THR HA H 4.58 . 1 810 81 THR CB C 72.03 . 1 811 81 THR HB H 4.75 . 1 812 81 THR HG2 H 1.39 . 1 813 81 THR CG2 C 21.83 . 1 814 82 GLU N N 119.41 . 1 815 82 GLU H H 9.12 . 1 816 82 GLU CA C 60.03 . 1 817 82 GLU HA H 4.07 . 1 818 82 GLU CB C 28.73 . 1 819 82 GLU HB2 H 2.12 . 2 820 82 GLU HB3 H 2.04 . 2 821 82 GLU CG C 35.33 . 1 822 82 GLU HG2 H 2.41 . 2 823 82 GLU HG3 H 2.37 . 2 824 83 THR N N 115.71 . 1 825 83 THR H H 7.96 . 1 826 83 THR CA C 66.93 . 1 827 83 THR HA H 3.76 . 1 828 83 THR CB C 68.63 . 1 829 83 THR HB H 3.70 . 1 830 83 THR HG2 H 0.69 . 1 831 83 THR CG2 C 21.13 . 1 832 84 ASP N N 119.61 . 1 833 84 ASP H H 7.49 . 1 834 84 ASP CA C 58.13 . 1 835 84 ASP HA H 4.53 . 1 836 84 ASP CB C 41.53 . 1 837 84 ASP HB2 H 3.28 . 2 838 84 ASP HB3 H 2.51 . 2 839 85 VAL N N 119.11 . 1 840 85 VAL H H 8.24 . 1 841 85 VAL CA C 67.73 . 1 842 85 VAL HA H 3.28 . 1 843 85 VAL CB C 31.63 . 1 844 85 VAL HB H 2.09 . 1 845 85 VAL HG1 H 0.86 . 2 846 85 VAL HG2 H 0.97 . 2 847 85 VAL CG1 C 21.33 . 1 848 85 VAL CG2 C 22.73 . 1 849 86 LYS N N 118.61 . 1 850 86 LYS H H 7.74 . 1 851 86 LYS CA C 59.73 . 1 852 86 LYS HA H 4.02 . 1 853 86 LYS CB C 32.33 . 1 854 86 LYS HB2 H 1.94 . 2 855 86 LYS HB3 H 1.88 . 2 856 86 LYS CG C 25.13 . 1 857 86 LYS HG2 H 1.61 . 2 858 86 LYS HG3 H 1.43 . 2 859 86 LYS CD C 29.13 . 1 860 86 LYS HD2 H 1.64 . 1 861 86 LYS HD3 H 1.64 . 1 862 86 LYS CE C 41.83 . 1 863 86 LYS HE2 H 2.90 . 1 864 86 LYS HE3 H 2.90 . 1 865 87 MET N N 118.41 . 1 866 87 MET H H 8.23 . 1 867 87 MET CA C 60.23 . 1 868 87 MET HA H 4.11 . 1 869 87 MET CB C 32.73 . 1 870 87 MET HB2 H 2.27 . 2 871 87 MET HB3 H 1.92 . 2 872 87 MET CG C 34.33 . 1 873 87 MET HG2 H 2.10 . 2 874 87 MET HG3 H 2.90 . 2 875 87 MET HE H 1.43 . 1 876 87 MET CE C 18.33 . 1 877 88 MET N N 117.81 . 1 878 88 MET H H 8.75 . 1 879 88 MET CA C 60.03 . 1 880 88 MET HA H 3.54 . 1 881 88 MET CB C 33.43 . 1 882 88 MET HB2 H 1.89 . 2 883 88 MET HB3 H 1.68 . 2 884 88 MET CG C 32.73 . 1 885 88 MET HG2 H 1.69 . 2 886 88 MET HG3 H 1.90 . 2 887 88 MET HE H 1.39 . 1 888 88 MET CE C 16.13 . 1 889 89 GLU N N 117.61 . 1 890 89 GLU H H 8.43 . 1 891 89 GLU CA C 60.73 . 1 892 89 GLU HA H 3.65 . 1 893 89 GLU CB C 28.03 . 1 894 89 GLU HB2 H 2.06 . 2 895 89 GLU HB3 H 2.21 . 2 896 89 GLU CG C 34.63 . 1 897 89 GLU HG2 H 2.22 . 2 898 89 GLU HG3 H 2.57 . 2 899 90 ARG N N 116.41 . 1 900 90 ARG H H 7.30 . 1 901 90 ARG CA C 58.33 . 1 902 90 ARG HA H 4.16 . 1 903 90 ARG CB C 30.23 . 1 904 90 ARG HB2 H 1.91 . 2 905 90 ARG HB3 H 2.08 . 2 906 90 ARG CG C 26.93 . 1 907 90 ARG HG2 H 1.80 . 2 908 90 ARG HG3 H 1.73 . 2 909 90 ARG CD C 42.53 . 1 910 90 ARG HD2 H 3.22 . 2 911 90 ARG HD3 H 3.12 . 2 912 90 ARG NE N 83.10 . 1 913 90 ARG HE H 7.28 . 1 914 91 VAL N N 118.71 . 1 915 91 VAL H H 8.28 . 1 916 91 VAL CA C 66.03 . 1 917 91 VAL HA H 3.77 . 1 918 91 VAL CB C 32.33 . 1 919 91 VAL HB H 2.32 . 1 920 91 VAL HG1 H 1.25 . 2 921 91 VAL HG2 H 0.93 . 2 922 91 VAL CG1 C 21.13 . 1 923 91 VAL CG2 C 24.13 . 1 924 92 VAL N N 120.91 . 1 925 92 VAL H H 9.05 . 1 926 92 VAL CA C 66.73 . 1 927 92 VAL HA H 3.62 . 1 928 92 VAL CB C 31.33 . 1 929 92 VAL HB H 2.24 . 1 930 92 VAL HG1 H 1.19 . 2 931 92 VAL HG2 H 0.93 . 2 932 92 VAL CG1 C 24.83 . 1 933 92 VAL CG2 C 24.43 . 1 934 93 GLU N N 120.01 . 1 935 93 GLU H H 8.04 . 1 936 93 GLU CA C 61.23 . 1 937 93 GLU HA H 3.58 . 1 938 93 GLU CB C 28.73 . 1 939 93 GLU HB2 H 2.13 . 2 940 93 GLU HB3 H 2.19 . 2 941 93 GLU CG C 35.33 . 1 942 93 GLU HG2 H 2.16 . 1 943 93 GLU HG3 H 2.16 . 1 944 94 GLN N N 114.31 . 1 945 94 GLN H H 7.15 . 1 946 94 GLN CA C 59.03 . 1 947 94 GLN HA H 3.94 . 1 948 94 GLN CB C 28.03 . 1 949 94 GLN HB2 H 2.09 . 2 950 94 GLN HB3 H 2.18 . 2 951 94 GLN CG C 33.93 . 1 952 94 GLN HG2 H 2.42 . 2 953 94 GLN HG3 H 2.40 . 2 954 94 GLN NE2 N 113.20 . 1 955 94 GLN HE21 H 7.53 . 2 956 94 GLN HE22 H 6.89 . 2 957 95 MET N N 118.91 . 1 958 95 MET H H 8.26 . 1 959 95 MET CA C 59.93 . 1 960 95 MET HA H 4.14 . 1 961 95 MET CB C 34.63 . 1 962 95 MET HB2 H 2.10 . 1 963 95 MET HB3 H 2.10 . 1 964 95 MET CG C 32.43 . 1 965 95 MET HG2 H 2.80 . 2 966 95 MET HG3 H 2.45 . 2 967 95 MET HE H 1.86 . 1 968 95 MET CE C 16.73 . 1 969 96 CYS N N 118.81 . 1 970 96 CYS H H 9.19 . 1 971 96 CYS CA C 60.23 . 1 972 96 CYS HA H 4.38 . 1 973 96 CYS CB C 42.03 . 1 974 96 CYS HB2 H 3.50 . 2 975 96 CYS HB3 H 2.83 . 2 976 97 ILE N N 123.31 . 1 977 97 ILE H H 8.24 . 1 978 97 ILE CA C 66.73 . 1 979 97 ILE HA H 3.50 . 1 980 97 ILE CB C 38.13 . 1 981 97 ILE HB H 1.98 . 1 982 97 ILE HG2 H 0.83 . 1 983 97 ILE CG2 C 17.43 . 1 984 97 ILE CG1 C 30.83 . 1 985 97 ILE HG12 H 1.94 . 2 986 97 ILE HG13 H 0.80 . 2 987 97 ILE HD1 H 0.81 . 1 988 97 ILE CD1 C 14.13 . 1 989 98 THR N N 117.81 . 1 990 98 THR H H 8.10 . 1 991 98 THR CA C 67.23 . 1 992 98 THR HA H 3.87 . 1 993 98 THR CB C 68.23 . 1 994 98 THR HB H 4.28 . 1 995 98 THR HG2 H 1.19 . 1 996 98 THR CG2 C 22.23 . 1 997 99 GLN N N 121.91 . 1 998 99 GLN H H 8.78 . 1 999 99 GLN CA C 58.63 . 1 1000 99 GLN HA H 3.59 . 1 1001 99 GLN CB C 28.33 . 1 1002 99 GLN HB2 H 2.29 . 2 1003 99 GLN HB3 H 2.07 . 2 1004 99 GLN CG C 32.73 . 1 1005 99 GLN HG2 H 1.72 . 2 1006 99 GLN HG3 H 1.59 . 2 1007 99 GLN NE2 N 115.20 . 1 1008 99 GLN HE21 H 7.33 . 2 1009 99 GLN HE22 H 6.64 . 2 1010 100 TYR N N 120.01 . 1 1011 100 TYR H H 8.51 . 1 1012 100 TYR CA C 62.33 . 1 1013 100 TYR HA H 2.88 . 1 1014 100 TYR CB C 37.23 . 1 1015 100 TYR HB2 H 3.04 . 2 1016 100 TYR HB3 H 2.68 . 2 1017 100 TYR HD1 H 6.14 . 1 1018 100 TYR HD2 H 6.14 . 1 1019 100 TYR HE1 H 6.52 . 1 1020 100 TYR HE2 H 6.52 . 1 1021 100 TYR CD1 C 132.83 . 1 1022 100 TYR CE1 C 118.03 . 1 1023 101 GLU N N 119.81 . 1 1024 101 GLU H H 8.25 . 1 1025 101 GLU CA C 59.03 . 1 1026 101 GLU HA H 3.71 . 1 1027 101 GLU CB C 27.83 . 1 1028 101 GLU HB2 H 2.31 . 2 1029 101 GLU HB3 H 2.02 . 2 1030 101 GLU CG C 33.93 . 1 1031 101 GLU HG2 H 2.67 . 2 1032 101 GLU HG3 H 2.45 . 2 1033 102 ARG N N 118.41 . 1 1034 102 ARG H H 8.09 . 1 1035 102 ARG CA C 59.23 . 1 1036 102 ARG HA H 3.93 . 1 1037 102 ARG CB C 30.63 . 1 1038 102 ARG HB2 H 1.77 . 2 1039 102 ARG HB3 H 1.87 . 2 1040 102 ARG CG C 27.23 . 1 1041 102 ARG HG2 H 1.79 . 2 1042 102 ARG HG3 H 1.55 . 2 1043 102 ARG CD C 44.13 . 1 1044 102 ARG HD2 H 2.88 . 2 1045 102 ARG HD3 H 3.02 . 2 1046 102 ARG NE N 83.80 . 1 1047 102 ARG HE H 7.20 . 1 1048 103 GLU N N 116.71 . 1 1049 103 GLU H H 8.24 . 1 1050 103 GLU CA C 57.43 . 1 1051 103 GLU HA H 4.04 . 1 1052 103 GLU CB C 29.43 . 1 1053 103 GLU HB2 H 1.57 . 1 1054 103 GLU HB3 H 1.57 . 1 1055 103 GLU CG C 35.33 . 1 1056 103 GLU HG2 H 2.12 . 2 1057 103 GLU HG3 H 2.41 . 2 1058 104 SER N N 114.51 . 1 1059 104 SER H H 8.24 . 1 1060 104 SER CA C 60.63 . 1 1061 104 SER HA H 3.99 . 1 1062 104 SER CB C 63.03 . 1 1063 104 SER HB2 H 3.56 . 2 1064 104 SER HB3 H 3.32 . 2 1065 105 GLN N N 119.81 . 1 1066 105 GLN H H 7.64 . 1 1067 105 GLN CA C 57.63 . 1 1068 105 GLN HA H 4.11 . 1 1069 105 GLN CB C 28.53 . 1 1070 105 GLN HB2 H 2.04 . 1 1071 105 GLN HB3 H 2.04 . 1 1072 105 GLN CG C 33.93 . 1 1073 105 GLN HG2 H 2.41 . 2 1074 105 GLN HG3 H 2.34 . 2 1075 105 GLN NE2 N 111.80 . 1 1076 105 GLN HE21 H 7.45 . 2 1077 105 GLN HE22 H 6.79 . 2 1078 106 ALA N N 120.81 . 1 1079 106 ALA H H 7.63 . 1 1080 106 ALA CA C 53.73 . 1 1081 106 ALA HA H 4.14 . 1 1082 106 ALA HB H 1.32 . 1 1083 106 ALA CB C 18.63 . 1 1084 107 TYR N N 118.01 . 1 1085 107 TYR H H 7.89 . 1 1086 107 TYR CA C 59.53 . 1 1087 107 TYR HA H 4.26 . 1 1088 107 TYR CB C 38.83 . 1 1089 107 TYR HB2 H 2.92 . 2 1090 107 TYR HB3 H 2.80 . 2 1091 107 TYR HD1 H 6.76 . 1 1092 107 TYR HD2 H 6.76 . 1 1093 107 TYR HE1 H 6.69 . 1 1094 107 TYR HE2 H 6.69 . 1 1095 107 TYR CD1 C 133.33 . 1 1096 107 TYR CE1 C 118.13 . 1 1097 108 TYR N N 118.41 . 1 1098 108 TYR H H 7.86 . 1 1099 108 TYR CA C 58.53 . 1 1100 108 TYR HA H 4.36 . 1 1101 108 TYR CB C 38.53 . 1 1102 108 TYR HB2 H 3.06 . 2 1103 108 TYR HB3 H 2.89 . 2 1104 108 TYR HD1 H 7.14 . 1 1105 108 TYR HD2 H 7.14 . 1 1106 108 TYR HE1 H 6.83 . 1 1107 108 TYR HE2 H 6.83 . 1 1108 108 TYR CD1 C 133.53 . 1 1109 108 TYR CE1 C 118.33 . 1 1110 109 GLN N N 119.61 . 1 1111 109 GLN H H 7.92 . 1 1112 109 GLN CA C 56.03 . 1 1113 109 GLN HA H 4.21 . 1 1114 109 GLN CB C 28.83 . 1 1115 109 GLN HB2 H 2.06 . 2 1116 109 GLN HB3 H 1.96 . 2 1117 109 GLN CG C 34.13 . 1 1118 109 GLN HG2 H 2.28 . 1 1119 109 GLN HG3 H 2.28 . 1 1120 109 GLN NE2 N 112.10 . 1 1121 109 GLN HE21 H 7.48 . 2 1122 109 GLN HE22 H 6.81 . 2 1123 110 ARG N N 119.91 . 1 1124 110 ARG H H 7.92 . 1 1125 110 ARG CA C 56.73 . 1 1126 110 ARG HA H 4.26 . 1 1127 110 ARG CB C 30.83 . 1 1128 110 ARG HB2 H 1.76 . 2 1129 110 ARG HB3 H 1.84 . 2 1130 110 ARG CG C 27.13 . 1 1131 110 ARG HG2 H 1.63 . 2 1132 110 ARG HG3 H 1.60 . 2 1133 110 ARG CD C 43.43 . 1 1134 110 ARG HD2 H 3.13 . 1 1135 110 ARG HD3 H 3.13 . 1 1136 110 ARG NE N 84.50 . 1 1137 110 ARG HE H 7.14 . 1 1138 111 GLY N N 109.71 . 1 1139 111 GLY H H 8.38 . 1 1140 111 GLY CA C 45.43 . 1 1141 111 GLY HA3 H 3.91 . 1 1142 111 GLY HA2 H 3.91 . 1 1143 112 SER N N 115.21 . 1 1144 112 SER H H 8.14 . 1 1145 112 SER CA C 58.73 . 1 1146 112 SER HA H 4.46 . 1 1147 112 SER CB C 64.03 . 1 1148 112 SER HB2 H 3.87 . 1 1149 112 SER HB3 H 3.87 . 1 stop_ save_