data_4620 #Corrected using PDB structure: 1QLXA # #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 3.88 2.99 # 39 Y HA 4.98 4.24 # 52 S HA 4.57 2.99 #100 Y HA 2.89 4.14 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 50 E CB 29.25 34.44 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 8 G N 109.78 121.27 # 45 Y N 110.88 121.16 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.03 0.20 0.25 N/A -0.12 -0.10 # #bmr4620.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4620.str file): #HA CA CB CO N HN #N/A +0.22 +0.22 N/A -0.12 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.17 +/-0.17 N/A +/-0.28 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.709 0.965 0.995 N/A 0.717 0.481 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.154 0.861 0.843 N/A 1.354 0.337 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human prion protein variant R220K ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Calzonai L. . . 2 Lysek D. A. . 3 Guntert P. . . 4 "Von Schroetter" C. . . 5 Zahn R. . . 6 Riek R. . . 7 Wuthrich K. . . stop_ _BMRB_accession_number 4620 _BMRB_flat_file_name bmr4620.str _Entry_type new _Submission_date 2000-05-11 _Accession_date 2000-09-07 _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' 125 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 published _Citation_type journal _MEDLINE_UI_code 20359708 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Calzonai L. . . 2 Lysek D. A. . 3 Guntert P. . . 4 "Von Schroetter" C. . . 5 Zahn R. . . 6 Riek R. . . 7 Wuthrich K. . . stop_ _Journal_abbreviation "Proc. Natl. Acad. Sci. U. S. A." _Journal_volume 97 _Page_first 8340 _Page_last 8345 _Year 2000 loop_ _Keyword "prion protein" stop_ save_ ################################## # Molecular system description # ################################## save_system_prion_protein _Saveframe_category molecular_system _Mol_system_name "prion protein" _Abbreviation_common "prion protein" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "prion protein" $prion_protein stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' 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_prion_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "prion protein" _Name_variant R220K _Abbreviation_common "prion protein" _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; GSVVGGLGGYMLGSAMSRPI IHFGSDYEDRYYRENMHRYP NQVYYRPMDEYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCITQY EKESQAYYQRGS ; 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 MET 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 LYS 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 1E1U "A Chain A, Human Prion Protein Variant R220k" 107.69 104 100 100 2e-57 PDB 1E1W "A Chain A, Human Prion Protein Variant R220k" 107.69 104 100 100 2e-57 PDB 1HJM "A Chain A, Human Prion Protein At Ph 7.0" 107.69 104 99 100 5e-57 PDB 1HJN "A Chain A, Human Prion Protein At Ph 7.0" 107.69 104 99 100 5e-57 PDB 1E1G "A Chain A, Human Prion Protein Variant M166v" 107.69 104 98 100 2e-56 PDB 1E1J "A Chain A, Human Prion Protein Variant M166v" 107.69 104 98 100 2e-56 PDB 1E1P "A Chain A, Human Prion Protein Variant S170n" 107.69 104 98 100 10e-57 PDB 1E1S "A Chain A, Human Prion Protein Variant S170n" 107.69 104 98 100 10e-57 PDB 1I4M "A Chain A, Crystal Structure Of The HumanPrion Protein Reveals A Mechanism For Oligomerization" 103.70 108 98 100 2e-59 PDB 1QM2 "A Chain A, Human Prion Protein Fragment 121-230" 100.00 112 99 100 4e-62 PDB 1QM3 "A Chain A, Human Prion Protein Fragment 121-230" 100.00 112 99 100 4e-62 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_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "prion protein" 61 CYS SG "prion protein" 96 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $prion_protein 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 $prion_protein 'recombinant technology' "Escherichia coli" Escherichia coli 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 $prion_protein 1.0 mM '[U-13C; U-15N]' 'sodium acetate' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCA HN(CO)CA HCCH-TOCSY 15N-resolved (1H,1H)NOESY 13C-resolved (1H,1H)NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . n/a temperature 293 . K 'ionic strength' 50 . mM 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 _Reference_correction_type H2O H 1 protons ppm 4.78 internal direct internal . . . 'temperature (20C)' . C 13 . ppm 0 . . . . . . . . N 15 . ppm 0 . . . . . . . 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "prion protein" 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 43.22 . 1 2 1 GLY HA3 H 3.90 . 1 3 1 GLY HA2 H 3.90 . 1 4 2 SER N N 115.58 . 1 5 2 SER H H 8.67 . 1 6 2 SER CA C 58.12 . 1 7 2 SER HA H 4.58 . 1 8 2 SER CB C 63.92 . 1 9 2 SER HB2 H 3.82 . 1 10 2 SER HB3 H 3.82 . 1 11 3 VAL N N 121.88 . 1 12 3 VAL H H 8.39 . 1 13 3 VAL CA C 62.22 . 1 14 3 VAL HA H 4.18 . 1 15 3 VAL CB C 32.72 . 1 16 3 VAL HB H 2.04 . 1 17 3 VAL HG1 H 0.87 . 2 18 3 VAL HG2 H 0.90 . 2 19 3 VAL CG1 C 21.12 . 1 20 3 VAL CG2 C 20.52 . 1 21 4 VAL N N 124.68 . 1 22 4 VAL H H 8.34 . 1 23 4 VAL CA C 62.62 . 1 24 4 VAL HA H 4.08 . 1 25 4 VAL CB C 32.62 . 1 26 4 VAL HB H 2.02 . 1 27 4 VAL HG1 H 0.91 . 1 28 4 VAL HG2 H 0.91 . 1 29 4 VAL CG1 C 21.12 . 1 30 4 VAL CG2 C 20.72 . 1 31 5 GLY N N 113.28 . 1 32 5 GLY H H 8.59 . 1 33 5 GLY CA C 45.42 . 1 34 5 GLY HA3 H 3.94 . 1 35 5 GLY HA2 H 3.94 . 1 36 6 GLY N N 108.48 . 1 37 6 GLY H H 8.30 . 1 38 6 GLY CA C 45.22 . 1 39 6 GLY HA3 H 3.92 . 1 40 6 GLY HA2 H 3.92 . 1 41 7 LEU N N 121.68 . 1 42 7 LEU H H 8.27 . 1 43 7 LEU CA C 54.92 . 1 44 7 LEU HA H 4.36 . 1 45 7 LEU CB C 42.42 . 1 46 7 LEU HB2 H 1.50 . 2 47 7 LEU HB3 H 1.60 . 2 48 7 LEU CG C 26.92 . 1 49 7 LEU HG H 1.47 . 1 50 7 LEU HD1 H 0.65 . 2 51 7 LEU HD2 H 0.54 . 2 52 7 LEU CD1 C 24.82 . 1 53 7 LEU CD2 C 23.72 . 1 54 8 GLY N N 109.78 . 1 55 8 GLY H H 8.55 . 1 56 8 GLY CA C 46.22 . 1 57 8 GLY HA3 H 3.83 . 2 58 8 GLY HA2 H 3.90 . 2 59 9 GLY N N 109.08 . 1 60 9 GLY H H 8.38 . 1 61 9 GLY CA C 45.02 . 1 62 9 GLY HA3 H 3.73 . 2 63 9 GLY HA2 H 3.88 . 2 64 10 TYR N N 117.38 . 1 65 10 TYR H H 7.72 . 1 66 10 TYR CA C 58.02 . 1 67 10 TYR HA H 4.49 . 1 68 10 TYR CB C 40.32 . 1 69 10 TYR HB2 H 2.87 . 2 70 10 TYR HB3 H 2.74 . 2 71 10 TYR HD1 H 6.79 . 1 72 10 TYR HD2 H 6.79 . 1 73 10 TYR HE1 H 6.62 . 1 74 10 TYR HE2 H 6.62 . 1 75 10 TYR CD1 C 132.92 . 1 76 10 TYR CE1 C 118.22 . 1 77 11 MET N N 120.58 . 1 78 11 MET H H 9.02 . 1 79 11 MET CA C 53.62 . 1 80 11 MET HA H 4.52 . 1 81 11 MET CB C 34.92 . 1 82 11 MET HB2 H 0.94 . 2 83 11 MET HB3 H 1.56 . 2 84 11 MET CG C 32.02 . 1 85 11 MET HG2 H 2.21 . 1 86 11 MET HG3 H 2.21 . 1 87 11 MET HE H 2.00 . 1 88 11 MET CE C 17.12 . 1 89 12 LEU N N 121.28 . 1 90 12 LEU H H 8.09 . 1 91 12 LEU CA C 53.32 . 1 92 12 LEU HA H 4.47 . 1 93 12 LEU CB C 43.42 . 1 94 12 LEU HB2 H 0.97 . 2 95 12 LEU HB3 H 1.59 . 2 96 12 LEU CG C 26.32 . 1 97 12 LEU HG H 1.38 . 1 98 12 LEU HD1 H -0.01 . 2 99 12 LEU HD2 H 0.59 . 2 100 12 LEU CD1 C 21.62 . 1 101 12 LEU CD2 C 26.02 . 1 102 13 GLY N N 114.68 . 1 103 13 GLY H H 9.38 . 1 104 13 GLY CA C 44.82 . 1 105 13 GLY HA3 H 4.04 . 2 106 13 GLY HA2 H 4.41 . 2 107 14 SER N N 113.48 . 1 108 14 SER H H 8.32 . 1 109 14 SER CA C 58.42 . 1 110 14 SER HA H 4.39 . 1 111 14 SER CB C 64.02 . 1 112 14 SER HB2 H 3.95 . 2 113 14 SER HB3 H 3.88 . 2 114 15 ALA N N 125.48 . 1 115 15 ALA H H 8.75 . 1 116 15 ALA CA C 52.92 . 1 117 15 ALA HA H 4.42 . 1 118 15 ALA HB H 1.25 . 1 119 15 ALA CB C 18.42 . 1 120 16 MET N N 120.98 . 1 121 16 MET H H 8.78 . 1 122 16 MET CA C 54.02 . 1 123 16 MET HA H 4.73 . 1 124 16 MET CB C 37.12 . 1 125 16 MET HB2 H 2.03 . 2 126 16 MET HB3 H 1.96 . 2 127 16 MET CG C 31.62 . 1 128 16 MET HG2 H 2.51 . 2 129 16 MET HG3 H 2.43 . 2 130 16 MET HE H 2.18 . 1 131 16 MET CE C 17.92 . 1 132 17 SER N N 116.08 . 1 133 17 SER H H 8.45 . 1 134 17 SER CA C 58.52 . 1 135 17 SER HA H 4.34 . 1 136 17 SER CB C 62.92 . 1 137 17 SER HB2 H 3.81 . 2 138 17 SER HB3 H 3.73 . 2 139 18 ARG N N 126.38 . 1 140 18 ARG H H 8.66 . 1 141 18 ARG CA C 54.82 . 1 142 18 ARG HA H 4.40 . 1 143 18 ARG CB C 29.42 . 1 144 18 ARG HB2 H 1.74 . 1 145 18 ARG HB3 H 1.74 . 1 146 18 ARG CG C 28.82 . 1 147 18 ARG HG2 H 1.86 . 2 148 18 ARG HG3 H 1.79 . 2 149 18 ARG CD C 44.12 . 1 150 18 ARG HD2 H 3.12 . 2 151 18 ARG HD3 H 3.04 . 2 152 18 ARG NE N 85.90 . 1 153 18 ARG HE H 6.72 . 1 154 19 PRO CD C 50.62 . 1 155 19 PRO CA C 62.42 . 1 156 19 PRO HA H 4.42 . 1 157 19 PRO CB C 32.42 . 1 158 19 PRO HB2 H 1.75 . 2 159 19 PRO HB3 H 2.24 . 2 160 19 PRO CG C 27.42 . 1 161 19 PRO HG2 H 1.96 . 2 162 19 PRO HG3 H 2.02 . 2 163 19 PRO HD2 H 3.62 . 2 164 19 PRO HD3 H 3.92 . 2 165 20 ILE N N 122.28 . 1 166 20 ILE H H 8.67 . 1 167 20 ILE CA C 60.92 . 1 168 20 ILE HA H 4.14 . 1 169 20 ILE CB C 36.32 . 1 170 20 ILE HB H 1.91 . 1 171 20 ILE HG2 H 0.71 . 1 172 20 ILE CG2 C 17.32 . 1 173 20 ILE CG1 C 27.22 . 1 174 20 ILE HG12 H 1.57 . 2 175 20 ILE HG13 H 1.38 . 2 176 20 ILE HD1 H 0.89 . 1 177 20 ILE CD1 C 11.22 . 1 178 21 ILE N N 126.68 . 1 179 21 ILE H H 6.46 . 1 180 21 ILE CA C 58.82 . 1 181 21 ILE HA H 3.90 . 1 182 21 ILE CB C 39.42 . 1 183 21 ILE HB H 0.82 . 1 184 21 ILE HG2 H -0.06 . 1 185 21 ILE CG2 C 17.22 . 1 186 21 ILE CG1 C 26.72 . 1 187 21 ILE HG12 H 0.92 . 2 188 21 ILE HG13 H 0.77 . 2 189 21 ILE HD1 H 0.47 . 1 190 21 ILE CD1 C 12.82 . 1 191 22 HIS N N 121.88 . 1 192 22 HIS H H 8.26 . 1 193 22 HIS CA C 54.02 . 1 194 22 HIS HA H 4.91 . 1 195 22 HIS CB C 29.42 . 1 196 22 HIS HB2 H 3.30 . 2 197 22 HIS HB3 H 2.93 . 2 198 22 HIS CD2 C 119.82 . 1 199 22 HIS CE1 C 136.22 . 1 200 22 HIS HD2 H 7.21 . 1 201 22 HIS HE1 H 8.56 . 1 202 23 PHE N N 123.48 . 1 203 23 PHE H H 10.25 . 1 204 23 PHE CA C 59.32 . 1 205 23 PHE HA H 4.35 . 1 206 23 PHE CB C 41.42 . 1 207 23 PHE HB2 H 2.79 . 2 208 23 PHE HB3 H 3.33 . 2 209 23 PHE HD1 H 7.30 . 1 210 23 PHE HD2 H 7.30 . 1 211 23 PHE HE1 H 6.85 . 1 212 23 PHE HE2 H 6.85 . 1 213 23 PHE CD1 C 132.12 . 1 214 23 PHE CE1 C 131.22 . 1 215 23 PHE CZ C 129.02 . 1 216 23 PHE HZ H 6.70 . 1 217 24 GLY N N 108.38 . 1 218 24 GLY H H 9.02 . 1 219 24 GLY CA C 45.72 . 1 220 24 GLY HA3 H 3.80 . 2 221 24 GLY HA2 H 4.17 . 2 222 25 SER N N 111.58 . 1 223 25 SER H H 7.32 . 1 224 25 SER CA C 56.52 . 1 225 25 SER HA H 4.80 . 1 226 25 SER CB C 65.92 . 1 227 25 SER HB2 H 4.12 . 2 228 25 SER HB3 H 3.91 . 2 229 26 ASP N N 124.38 . 1 230 26 ASP H H 9.07 . 1 231 26 ASP CA C 57.62 . 1 232 26 ASP HA H 4.49 . 1 233 26 ASP CB C 40.52 . 1 234 26 ASP HB2 H 2.75 . 1 235 26 ASP HB3 H 2.75 . 1 236 27 TYR N N 118.78 . 1 237 27 TYR H H 8.61 . 1 238 27 TYR CA C 61.42 . 1 239 27 TYR HA H 4.18 . 1 240 27 TYR CB C 38.12 . 1 241 27 TYR HB2 H 3.25 . 2 242 27 TYR HB3 H 2.83 . 2 243 27 TYR HD1 H 7.03 . 1 244 27 TYR HD2 H 7.03 . 1 245 27 TYR HE1 H 6.72 . 1 246 27 TYR HE2 H 6.72 . 1 247 27 TYR CD1 C 133.32 . 1 248 27 TYR CE1 C 118.02 . 1 249 28 GLU N N 118.78 . 1 250 28 GLU H H 7.74 . 1 251 28 GLU CA C 59.82 . 1 252 28 GLU HA H 3.59 . 1 253 28 GLU CB C 30.22 . 1 254 28 GLU HB2 H 1.96 . 2 255 28 GLU HB3 H 1.56 . 2 256 28 GLU CG C 37.72 . 1 257 28 GLU HG2 H 2.27 . 2 258 28 GLU HG3 H 1.92 . 2 259 29 ASP N N 119.58 . 1 260 29 ASP H H 8.23 . 1 261 29 ASP CA C 58.42 . 1 262 29 ASP HA H 4.66 . 1 263 29 ASP CB C 40.22 . 1 264 29 ASP HB2 H 2.88 . 2 265 29 ASP HB3 H 3.03 . 2 266 30 ARG N N 120.18 . 1 267 30 ARG H H 8.23 . 1 268 30 ARG CA C 59.62 . 1 269 30 ARG HA H 4.00 . 1 270 30 ARG CB C 29.92 . 1 271 30 ARG HB2 H 1.88 . 1 272 30 ARG HB3 H 1.88 . 1 273 30 ARG CG C 27.92 . 1 274 30 ARG HG2 H 1.74 . 2 275 30 ARG HG3 H 1.53 . 2 276 30 ARG CD C 43.62 . 1 277 30 ARG HD2 H 3.19 . 2 278 30 ARG HD3 H 3.21 . 2 279 30 ARG NE N 85.50 . 1 280 30 ARG HE H 7.49 . 1 281 31 TYR N N 121.18 . 1 282 31 TYR H H 8.32 . 1 283 31 TYR CA C 62.32 . 1 284 31 TYR HA H 3.81 . 1 285 31 TYR CB C 38.22 . 1 286 31 TYR HB2 H 2.87 . 2 287 31 TYR HB3 H 2.59 . 2 288 31 TYR HD1 H 6.91 . 1 289 31 TYR HD2 H 6.91 . 1 290 31 TYR HE1 H 6.73 . 1 291 31 TYR HE2 H 6.73 . 1 292 31 TYR CD1 C 133.42 . 1 293 31 TYR CE1 C 118.22 . 1 294 32 TYR N N 120.48 . 1 295 32 TYR H H 8.99 . 1 296 32 TYR CA C 63.02 . 1 297 32 TYR HA H 4.11 . 1 298 32 TYR CB C 38.12 . 1 299 32 TYR HB2 H 3.53 . 2 300 32 TYR HB3 H 3.25 . 2 301 32 TYR HD1 H 7.52 . 1 302 32 TYR HD2 H 7.52 . 1 303 32 TYR HE1 H 6.99 . 1 304 32 TYR HE2 H 6.99 . 1 305 32 TYR CD1 C 133.62 . 1 306 32 TYR CE1 C 118.22 . 1 307 33 ARG N N 117.68 . 1 308 33 ARG H H 8.01 . 1 309 33 ARG CA C 60.02 . 1 310 33 ARG HA H 3.91 . 1 311 33 ARG CB C 30.02 . 1 312 33 ARG HB2 H 2.07 . 2 313 33 ARG HB3 H 1.94 . 2 314 33 ARG CG C 28.32 . 1 315 33 ARG HG2 H 1.72 . 2 316 33 ARG HG3 H 2.02 . 2 317 33 ARG CD C 43.22 . 1 318 33 ARG HD2 H 3.38 . 2 319 33 ARG HD3 H 3.27 . 2 320 33 ARG NE N 84.40 . 1 321 33 ARG HE H 7.52 . 1 322 34 GLU N N 116.28 . 1 323 34 GLU H H 8.08 . 1 324 34 GLU CA C 58.02 . 1 325 34 GLU HA H 4.05 . 1 326 34 GLU CB C 29.52 . 1 327 34 GLU HB2 H 1.88 . 1 328 34 GLU HB3 H 1.88 . 1 329 34 GLU CG C 36.02 . 1 330 34 GLU HG2 H 2.42 . 2 331 34 GLU HG3 H 2.23 . 2 332 35 ASN N N 114.58 . 1 333 35 ASN H H 7.63 . 1 334 35 ASN CA C 54.92 . 1 335 35 ASN HA H 4.27 . 1 336 35 ASN CB C 41.02 . 1 337 35 ASN HB2 H 2.14 . 1 338 35 ASN HB3 H 2.14 . 1 339 35 ASN ND2 N 117.10 . 1 340 35 ASN HD21 H 6.70 . 2 341 35 ASN HD22 H 6.60 . 2 342 36 MET N N 119.58 . 1 343 36 MET H H 8.13 . 1 344 36 MET CA C 59.32 . 1 345 36 MET HA H 3.42 . 1 346 36 MET CB C 30.52 . 1 347 36 MET HB2 H 1.31 . 2 348 36 MET HB3 H 1.64 . 2 349 36 MET CG C 30.62 . 1 350 36 MET HG2 H 2.53 . 2 351 36 MET HG3 H 2.14 . 2 352 36 MET HE H 2.01 . 1 353 36 MET CE C 17.62 . 1 354 37 HIS N N 114.98 . 1 355 37 HIS H H 8.10 . 1 356 37 HIS CA C 57.62 . 1 357 37 HIS HA H 4.21 . 1 358 37 HIS CB C 27.12 . 1 359 37 HIS HB2 H 3.06 . 2 360 37 HIS HB3 H 3.30 . 2 361 37 HIS CD2 C 120.42 . 1 362 37 HIS HD2 H 7.30 . 1 363 38 ARG N N 117.68 . 1 364 38 ARG H H 7.63 . 1 365 38 ARG CA C 56.22 . 1 366 38 ARG HA H 4.13 . 1 367 38 ARG CB C 30.62 . 1 368 38 ARG HB2 H 1.40 . 2 369 38 ARG HB3 H 2.10 . 2 370 38 ARG CG C 27.42 . 1 371 38 ARG HG2 H 1.37 . 2 372 38 ARG HG3 H 0.31 . 2 373 38 ARG CD C 44.12 . 1 374 38 ARG HD2 H 3.08 . 2 375 38 ARG HD3 H 3.24 . 2 376 38 ARG NE N 84.40 . 1 377 38 ARG HE H 7.41 . 1 378 39 TYR N N 120.58 . 1 379 39 TYR H H 7.49 . 1 380 39 TYR CA C 52.72 . 1 381 39 TYR HA H 5.01 . 1 382 39 TYR CB C 35.02 . 1 383 39 TYR HB2 H 3.10 . 1 384 39 TYR HB3 H 3.10 . 1 385 39 TYR HD1 H 6.82 . 1 386 39 TYR HD2 H 6.82 . 1 387 39 TYR HE1 H 6.51 . 1 388 39 TYR HE2 H 6.51 . 1 389 39 TYR CD1 C 131.32 . 1 390 39 TYR CE1 C 117.22 . 1 391 40 PRO CD C 50.22 . 1 392 40 PRO CA C 63.72 . 1 393 40 PRO HA H 4.39 . 1 394 40 PRO CB C 32.42 . 1 395 40 PRO HB2 H 1.64 . 2 396 40 PRO HB3 H 2.44 . 2 397 40 PRO CG C 27.42 . 1 398 40 PRO HG2 H 1.53 . 2 399 40 PRO HG3 H 1.28 . 2 400 40 PRO HD2 H 3.09 . 2 401 40 PRO HD3 H 3.30 . 2 402 41 ASN N N 115.98 . 1 403 41 ASN H H 8.57 . 1 404 41 ASN CA C 51.92 . 1 405 41 ASN HA H 4.68 . 1 406 41 ASN CB C 38.62 . 1 407 41 ASN HB2 H 3.68 . 2 408 41 ASN HB3 H 2.42 . 2 409 41 ASN ND2 N 109.10 . 1 410 41 ASN HD21 H 7.49 . 2 411 41 ASN HD22 H 6.79 . 2 412 42 GLN N N 113.78 . 1 413 42 GLN H H 7.28 . 1 414 42 GLN CA C 54.22 . 1 415 42 GLN HA H 4.56 . 1 416 42 GLN CB C 33.72 . 1 417 42 GLN HB2 H 1.69 . 2 418 42 GLN HB3 H 1.97 . 2 419 42 GLN CG C 34.12 . 1 420 42 GLN HG2 H 2.16 . 2 421 42 GLN HG3 H 2.01 . 2 422 42 GLN NE2 N 112.70 . 1 423 42 GLN HE21 H 7.90 . 2 424 42 GLN HE22 H 7.02 . 2 425 43 VAL N N 112.68 . 1 426 43 VAL H H 8.54 . 1 427 43 VAL CA C 58.72 . 1 428 43 VAL HA H 4.91 . 1 429 43 VAL CB C 33.92 . 1 430 43 VAL HB H 2.61 . 1 431 43 VAL HG1 H 0.95 . 2 432 43 VAL HG2 H 0.76 . 2 433 43 VAL CG1 C 23.92 . 1 434 43 VAL CG2 C 18.42 . 1 435 44 TYR N N 121.08 . 1 436 44 TYR H H 8.47 . 1 437 44 TYR CA C 57.12 . 1 438 44 TYR HA H 5.50 . 1 439 44 TYR CB C 42.12 . 1 440 44 TYR HB2 H 2.53 . 2 441 44 TYR HB3 H 2.58 . 2 442 44 TYR HD1 H 6.87 . 1 443 44 TYR HD2 H 6.87 . 1 444 44 TYR HE1 H 6.73 . 1 445 44 TYR HE2 H 6.73 . 1 446 44 TYR CD1 C 133.02 . 1 447 44 TYR CE1 C 118.42 . 1 448 45 TYR N N 110.88 . 1 449 45 TYR H H 8.61 . 1 450 45 TYR CA C 55.92 . 1 451 45 TYR HA H 4.75 . 1 452 45 TYR CB C 40.52 . 1 453 45 TYR HB2 H 2.59 . 2 454 45 TYR HB3 H 2.64 . 2 455 45 TYR HD1 H 6.96 . 1 456 45 TYR HD2 H 6.96 . 1 457 45 TYR HE1 H 6.43 . 1 458 45 TYR HE2 H 6.43 . 1 459 45 TYR CD1 C 134.02 . 1 460 45 TYR CE1 C 117.52 . 1 461 46 ARG N N 120.88 . 1 462 46 ARG H H 8.07 . 1 463 46 ARG CA C 53.12 . 1 464 46 ARG HA H 4.59 . 1 465 46 ARG CB C 30.22 . 1 466 46 ARG HB2 H 1.60 . 1 467 46 ARG HB3 H 1.60 . 1 468 46 ARG CG C 27.52 . 1 469 46 ARG HG2 H 1.14 . 1 470 46 ARG HG3 H 1.14 . 1 471 46 ARG CD C 43.42 . 1 472 46 ARG HD2 H 2.87 . 1 473 46 ARG HD3 H 2.87 . 1 474 46 ARG NE N 85.30 . 1 475 46 ARG HE H 6.96 . 1 476 47 PRO CD C 50.52 . 1 477 47 PRO CA C 63.42 . 1 478 47 PRO HA H 4.49 . 1 479 47 PRO CB C 32.42 . 1 480 47 PRO HB2 H 2.45 . 2 481 47 PRO HB3 H 1.91 . 2 482 47 PRO CG C 28.12 . 1 483 47 PRO HG2 H 2.08 . 2 484 47 PRO HG3 H 1.92 . 2 485 47 PRO HD2 H 3.50 . 2 486 47 PRO HD3 H 3.63 . 2 487 48 MET N N 120.18 . 1 488 48 MET H H 8.80 . 1 489 48 MET CA C 57.22 . 1 490 48 MET HA H 4.44 . 1 491 48 MET CB C 32.22 . 1 492 48 MET HB2 H 2.33 . 1 493 48 MET HB3 H 2.33 . 1 494 48 MET CG C 32.92 . 1 495 48 MET HG2 H 1.79 . 2 496 48 MET HG3 H 1.68 . 2 497 48 MET HE H 1.64 . 1 498 48 MET CE C 17.12 . 1 499 49 ASP N N 118.78 . 1 500 49 ASP H H 8.46 . 1 501 49 ASP CA C 54.22 . 1 502 49 ASP HA H 4.51 . 1 503 49 ASP CB C 40.52 . 1 504 49 ASP HB2 H 2.98 . 2 505 49 ASP HB3 H 2.73 . 2 506 50 GLU N N 116.58 . 1 507 50 GLU H H 8.39 . 1 508 50 GLU CA C 55.12 . 1 509 50 GLU HA H 4.65 . 1 510 50 GLU CB C 29.22 . 1 511 50 GLU HB2 H 3.16 . 2 512 50 GLU HB3 H 3.04 . 2 513 51 TYR HA H 4.42 . 1 514 51 TYR HD1 H 7.11 . 1 515 51 TYR HD2 H 7.11 . 1 516 51 TYR HE1 H 6.84 . 1 517 51 TYR HE2 H 6.84 . 1 518 51 TYR CD1 C 133.42 . 1 519 51 TYR CE1 C 118.72 . 1 520 52 SER CA C 58.92 . 1 521 52 SER HA H 4.60 . 1 522 52 SER CB C 64.32 . 1 523 52 SER HB2 H 3.95 . 2 524 52 SER HB3 H 3.94 . 2 525 53 ASN CA C 52.32 . 1 526 53 ASN HA H 4.76 . 1 527 53 ASN CB C 39.82 . 1 528 53 ASN HB2 H 3.10 . 2 529 53 ASN HB3 H 3.03 . 2 530 53 ASN ND2 N 113.20 . 1 531 53 ASN HD21 H 7.59 . 2 532 53 ASN HD22 H 6.73 . 2 533 54 GLN N N 120.08 . 1 534 54 GLN H H 8.69 . 1 535 54 GLN CA C 59.42 . 1 536 54 GLN HA H 2.89 . 1 537 54 GLN CB C 29.12 . 1 538 54 GLN HB2 H 1.61 . 2 539 54 GLN HB3 H 1.57 . 2 540 54 GLN CG C 33.42 . 1 541 54 GLN HG2 H 1.86 . 2 542 54 GLN HG3 H 1.20 . 2 543 54 GLN NE2 N 111.80 . 1 544 54 GLN HE21 H 7.49 . 2 545 54 GLN HE22 H 6.81 . 2 546 55 ASN N N 116.68 . 1 547 55 ASN H H 8.39 . 1 548 55 ASN CA C 56.52 . 1 549 55 ASN HA H 4.24 . 1 550 55 ASN CB C 37.92 . 1 551 55 ASN HB2 H 2.65 . 2 552 55 ASN HB3 H 2.73 . 2 553 55 ASN ND2 N 112.90 . 1 554 55 ASN HD21 H 7.61 . 2 555 55 ASN HD22 H 6.97 . 2 556 56 ASN N N 118.38 . 1 557 56 ASN H H 8.68 . 1 558 56 ASN CA C 55.92 . 1 559 56 ASN HA H 4.55 . 1 560 56 ASN CB C 37.82 . 1 561 56 ASN HB2 H 2.99 . 2 562 56 ASN HB3 H 2.93 . 2 563 56 ASN ND2 N 112.20 . 1 564 56 ASN HD21 H 7.50 . 2 565 56 ASN HD22 H 6.82 . 2 566 57 PHE HD1 H 7.62 . 1 567 57 PHE HD2 H 7.62 . 1 568 57 PHE HE1 H 6.68 . 1 569 57 PHE HE2 H 6.68 . 1 570 57 PHE CD1 C 131.72 . 1 571 57 PHE CE1 C 129.42 . 1 572 58 VAL N N 120.08 . 1 573 58 VAL H H 8.99 . 1 574 58 VAL CA C 67.82 . 1 575 58 VAL HA H 3.52 . 1 576 58 VAL CB C 32.02 . 1 577 58 VAL HB H 2.25 . 1 578 58 VAL HG1 H 1.02 . 2 579 58 VAL HG2 H 1.07 . 2 580 58 VAL CG1 C 21.82 . 1 581 58 VAL CG2 C 24.72 . 1 582 59 HIS N N 116.58 . 1 583 59 HIS H H 8.38 . 1 584 59 HIS CA C 59.42 . 1 585 59 HIS HA H 4.30 . 1 586 59 HIS CB C 28.62 . 1 587 59 HIS HB2 H 3.32 . 2 588 59 HIS HB3 H 3.39 . 2 589 59 HIS CD2 C 120.22 . 1 590 59 HIS CE1 C 136.22 . 1 591 59 HIS HD2 H 7.36 . 1 592 59 HIS HE1 H 8.62 . 1 593 60 ASP N N 118.38 . 1 594 60 ASP H H 7.80 . 1 595 60 ASP CA C 57.22 . 1 596 60 ASP HA H 4.53 . 1 597 60 ASP CB C 41.02 . 1 598 60 ASP HB2 H 2.96 . 2 599 60 ASP HB3 H 2.87 . 2 600 61 CYS N N 119.08 . 1 601 61 CYS H H 8.13 . 1 602 61 CYS CA C 58.72 . 1 603 61 CYS HA H 4.75 . 1 604 61 CYS CB C 40.82 . 1 605 61 CYS HB2 H 2.99 . 2 606 61 CYS HB3 H 3.37 . 2 607 62 VAL N N 124.58 . 1 608 62 VAL H H 9.18 . 1 609 62 VAL CA C 66.42 . 1 610 62 VAL HA H 3.65 . 1 611 62 VAL CB C 31.92 . 1 612 62 VAL HB H 2.16 . 1 613 62 VAL HG1 H 0.96 . 2 614 62 VAL HG2 H 1.07 . 2 615 62 VAL CG1 C 21.82 . 1 616 62 VAL CG2 C 23.62 . 1 617 63 ASN N N 116.18 . 1 618 63 ASN H H 7.71 . 1 619 63 ASN CA C 56.62 . 1 620 63 ASN HA H 4.30 . 1 621 63 ASN CB C 38.62 . 1 622 63 ASN HB2 H 2.85 . 2 623 63 ASN HB3 H 2.77 . 2 624 63 ASN ND2 N 112.00 . 1 625 63 ASN HD21 H 7.67 . 2 626 63 ASN HD22 H 6.80 . 2 627 64 ILE N N 118.38 . 1 628 64 ILE H H 8.71 . 1 629 64 ILE CA C 62.22 . 1 630 64 ILE HA H 3.75 . 1 631 64 ILE CB C 36.72 . 1 632 64 ILE HB H 1.56 . 1 633 64 ILE HG2 H 0.26 . 1 634 64 ILE CG2 C 18.82 . 1 635 64 ILE CG1 C 27.52 . 1 636 64 ILE HG12 H 0.84 . 2 637 64 ILE HG13 H 0.79 . 2 638 64 ILE HD1 H 0.39 . 1 639 64 ILE CD1 C 11.52 . 1 640 65 THR N N 118.18 . 1 641 65 THR H H 8.16 . 1 642 65 THR CA C 68.92 . 1 643 65 THR HA H 4.06 . 1 644 65 THR CB C 68.22 . 1 645 65 THR HB H 4.48 . 1 646 65 THR HG2 H 1.48 . 1 647 65 THR HG1 H 6.38 . 1 648 65 THR CG2 C 22.22 . 1 649 66 ILE N N 120.68 . 1 650 66 ILE H H 8.53 . 1 651 66 ILE CA C 65.52 . 1 652 66 ILE HA H 3.70 . 1 653 66 ILE CB C 36.62 . 1 654 66 ILE HB H 2.09 . 1 655 66 ILE HG2 H 0.87 . 1 656 66 ILE CG2 C 16.82 . 1 657 66 ILE CG1 C 30.12 . 1 658 66 ILE HG12 H 1.81 . 2 659 66 ILE HG13 H 1.20 . 2 660 66 ILE HD1 H 0.76 . 1 661 66 ILE CD1 C 13.22 . 1 662 67 LYS N N 122.68 . 1 663 67 LYS H H 8.07 . 1 664 67 LYS CA C 60.02 . 1 665 67 LYS HA H 4.05 . 1 666 67 LYS CB C 32.22 . 1 667 67 LYS HB2 H 1.89 . 2 668 67 LYS HB3 H 1.94 . 2 669 67 LYS CG C 25.02 . 1 670 67 LYS HG2 H 1.47 . 2 671 67 LYS HG3 H 1.37 . 2 672 67 LYS CD C 29.22 . 1 673 67 LYS HD2 H 1.60 . 1 674 67 LYS HD3 H 1.60 . 1 675 67 LYS CE C 42.12 . 1 676 67 LYS HE2 H 2.89 . 1 677 67 LYS HE3 H 2.89 . 1 678 68 GLN N N 115.98 . 1 679 68 GLN H H 8.37 . 1 680 68 GLN CA C 57.62 . 1 681 68 GLN HA H 4.02 . 1 682 68 GLN CB C 28.12 . 1 683 68 GLN HB2 H 1.89 . 2 684 68 GLN HB3 H 1.99 . 2 685 68 GLN CG C 33.72 . 1 686 68 GLN HG2 H 2.08 . 2 687 68 GLN HG3 H 1.61 . 2 688 68 GLN NE2 N 110.10 . 1 689 68 GLN HE21 H 6.81 . 2 690 68 GLN HE22 H 6.72 . 2 691 69 HIS N N 117.88 . 1 692 69 HIS H H 8.15 . 1 693 69 HIS CA C 59.12 . 1 694 69 HIS HA H 4.58 . 1 695 69 HIS CB C 30.92 . 1 696 69 HIS HB2 H 3.33 . 2 697 69 HIS HB3 H 3.26 . 2 698 69 HIS CD2 C 118.62 . 1 699 69 HIS HD2 H 7.10 . 1 700 70 THR N N 113.58 . 1 701 70 THR H H 8.25 . 1 702 70 THR CA C 65.42 . 1 703 70 THR HA H 4.18 . 1 704 70 THR CB C 69.32 . 1 705 70 THR HB H 4.42 . 1 706 70 THR HG2 H 1.24 . 1 707 70 THR CG2 C 21.42 . 1 708 71 VAL N N 121.98 . 1 709 71 VAL H H 8.02 . 1 710 71 VAL CA C 65.22 . 1 711 71 VAL HA H 3.99 . 1 712 71 VAL CB C 32.12 . 1 713 71 VAL HB H 2.20 . 1 714 71 VAL HG1 H 0.95 . 2 715 71 VAL HG2 H 1.03 . 2 716 71 VAL CG1 C 21.82 . 1 717 71 VAL CG2 C 21.82 . 1 718 72 THR N N 114.88 . 1 719 72 THR H H 8.08 . 1 720 72 THR CA C 63.62 . 1 721 72 THR HA H 4.21 . 1 722 72 THR CB C 69.42 . 1 723 72 THR HB H 4.26 . 1 724 72 THR HG2 H 1.26 . 1 725 72 THR CG2 C 21.62 . 1 726 73 THR N N 114.68 . 1 727 73 THR H H 8.02 . 1 728 73 THR CA C 64.22 . 1 729 73 THR HA H 4.19 . 1 730 73 THR CB C 69.32 . 1 731 73 THR HB H 4.16 . 1 732 73 THR HG2 H 1.01 . 1 733 73 THR CG2 C 21.62 . 1 734 74 THR N N 116.28 . 1 735 74 THR H H 8.20 . 1 736 74 THR CA C 63.72 . 1 737 74 THR HA H 4.38 . 1 738 74 THR CB C 69.32 . 1 739 74 THR HB H 4.35 . 1 740 74 THR HG2 H 1.27 . 1 741 74 THR CG2 C 21.62 . 1 742 75 THR N N 115.98 . 1 743 75 THR H H 7.94 . 1 744 75 THR CA C 63.62 . 1 745 75 THR HA H 4.25 . 1 746 75 THR CB C 69.52 . 1 747 75 THR HB H 4.25 . 1 748 75 THR HG2 H 1.26 . 1 749 75 THR CG2 C 21.62 . 1 750 76 LYS N N 120.98 . 1 751 76 LYS H H 7.86 . 1 752 76 LYS CA C 56.62 . 1 753 76 LYS HA H 4.34 . 1 754 76 LYS CB C 32.52 . 1 755 76 LYS HB2 H 1.96 . 2 756 76 LYS HB3 H 1.82 . 2 757 76 LYS CG C 24.82 . 1 758 76 LYS HG2 H 1.50 . 2 759 76 LYS HG3 H 1.45 . 2 760 76 LYS CD C 28.92 . 1 761 76 LYS HD2 H 1.67 . 1 762 76 LYS HD3 H 1.67 . 1 763 76 LYS CE C 41.92 . 1 764 76 LYS HE2 H 2.96 . 1 765 76 LYS HE3 H 2.96 . 1 766 77 GLY N N 108.78 . 1 767 77 GLY H H 8.14 . 1 768 77 GLY CA C 45.52 . 1 769 77 GLY HA3 H 4.07 . 2 770 77 GLY HA2 H 3.83 . 2 771 78 GLU N N 119.88 . 1 772 78 GLU H H 7.73 . 1 773 78 GLU CA C 55.72 . 1 774 78 GLU HA H 4.25 . 1 775 78 GLU CB C 30.42 . 1 776 78 GLU HB2 H 1.64 . 1 777 78 GLU HB3 H 1.64 . 1 778 78 GLU CG C 35.62 . 1 779 78 GLU HG2 H 2.10 . 1 780 78 GLU HG3 H 2.10 . 1 781 79 ASN N N 119.58 . 1 782 79 ASN H H 8.48 . 1 783 79 ASN CA C 52.92 . 1 784 79 ASN HA H 4.65 . 1 785 79 ASN CB C 40.52 . 1 786 79 ASN HB2 H 2.68 . 2 787 79 ASN HB3 H 2.61 . 2 788 79 ASN ND2 N 112.80 . 1 789 79 ASN HD21 H 7.56 . 2 790 79 ASN HD22 H 6.84 . 2 791 80 PHE N N 121.78 . 1 792 80 PHE H H 8.69 . 1 793 80 PHE CA C 56.82 . 1 794 80 PHE HA H 5.27 . 1 795 80 PHE CB C 40.02 . 1 796 80 PHE HB2 H 3.15 . 2 797 80 PHE HB3 H 2.96 . 2 798 80 PHE HD1 H 7.32 . 1 799 80 PHE HD2 H 7.32 . 1 800 80 PHE HE1 H 7.42 . 1 801 80 PHE HE2 H 7.42 . 1 802 80 PHE CD1 C 131.62 . 1 803 80 PHE CE1 C 130.22 . 1 804 81 THR N N 115.98 . 1 805 81 THR H H 9.53 . 1 806 81 THR CA C 60.62 . 1 807 81 THR HA H 4.60 . 1 808 81 THR CB C 72.12 . 1 809 81 THR HB H 4.83 . 1 810 81 THR HG2 H 1.42 . 1 811 81 THR CG2 C 21.62 . 1 812 82 GLU N N 119.78 . 1 813 82 GLU H H 9.14 . 1 814 82 GLU CA C 59.62 . 1 815 82 GLU HA H 4.08 . 1 816 82 GLU CB C 28.82 . 1 817 82 GLU HB2 H 2.13 . 2 818 82 GLU HB3 H 2.05 . 2 819 82 GLU CG C 36.02 . 1 820 82 GLU HG2 H 2.43 . 2 821 82 GLU HG3 H 2.37 . 2 822 83 THR N N 116.08 . 1 823 83 THR H H 7.98 . 1 824 83 THR CA C 67.02 . 1 825 83 THR HA H 3.79 . 1 826 83 THR CB C 68.62 . 1 827 83 THR HB H 3.70 . 1 828 83 THR HG2 H 0.71 . 1 829 83 THR CG2 C 21.02 . 1 830 84 ASP N N 119.98 . 1 831 84 ASP H H 7.51 . 1 832 84 ASP CA C 58.02 . 1 833 84 ASP HA H 4.57 . 1 834 84 ASP CB C 41.92 . 1 835 84 ASP HB2 H 3.34 . 2 836 84 ASP HB3 H 2.57 . 2 837 85 VAL N N 119.48 . 1 838 85 VAL H H 8.25 . 1 839 85 VAL CA C 67.72 . 1 840 85 VAL HA H 3.29 . 1 841 85 VAL CB C 31.62 . 1 842 85 VAL HB H 2.11 . 1 843 85 VAL HG1 H 0.88 . 2 844 85 VAL HG2 H 0.98 . 2 845 85 VAL CG1 C 21.12 . 1 846 85 VAL CG2 C 22.92 . 1 847 86 LYS N N 118.98 . 1 848 86 LYS H H 7.74 . 1 849 86 LYS CA C 59.42 . 1 850 86 LYS HA H 4.05 . 1 851 86 LYS CB C 32.02 . 1 852 86 LYS HB2 H 1.95 . 2 853 86 LYS HB3 H 1.90 . 2 854 86 LYS CG C 25.22 . 1 855 86 LYS HG2 H 1.64 . 2 856 86 LYS HG3 H 1.44 . 2 857 86 LYS CD C 29.02 . 1 858 86 LYS HD2 H 1.68 . 1 859 86 LYS HD3 H 1.68 . 1 860 86 LYS CE C 41.82 . 1 861 86 LYS HE2 H 2.92 . 1 862 86 LYS HE3 H 2.92 . 1 863 87 MET N N 118.58 . 1 864 87 MET H H 8.25 . 1 865 87 MET CA C 60.22 . 1 866 87 MET HA H 4.13 . 1 867 87 MET CB C 32.92 . 1 868 87 MET HB2 H 2.28 . 2 869 87 MET HB3 H 1.95 . 2 870 87 MET CG C 34.42 . 1 871 87 MET HG2 H 2.14 . 2 872 87 MET HG3 H 2.94 . 2 873 87 MET HE H 1.46 . 1 874 87 MET CE C 18.62 . 1 875 88 MET N N 118.18 . 1 876 88 MET H H 8.77 . 1 877 88 MET CA C 59.62 . 1 878 88 MET HA H 3.55 . 1 879 88 MET CB C 32.82 . 1 880 88 MET HB2 H 1.91 . 2 881 88 MET HB3 H 1.65 . 2 882 88 MET CG C 32.82 . 1 883 88 MET HG2 H 1.69 . 2 884 88 MET HG3 H 1.93 . 2 885 88 MET HE H 1.39 . 1 886 88 MET CE C 16.22 . 1 887 89 GLU N N 118.08 . 1 888 89 GLU H H 8.42 . 1 889 89 GLU CA C 60.52 . 1 890 89 GLU HA H 3.67 . 1 891 89 GLU CB C 27.92 . 1 892 89 GLU HB2 H 2.06 . 2 893 89 GLU HB3 H 2.22 . 2 894 89 GLU CG C 35.32 . 1 895 89 GLU HG2 H 2.22 . 2 896 89 GLU HG3 H 2.57 . 2 897 90 ARG N N 116.78 . 1 898 90 ARG H H 7.35 . 1 899 90 ARG CA C 58.42 . 1 900 90 ARG HA H 4.20 . 1 901 90 ARG CB C 29.92 . 1 902 90 ARG HB2 H 1.95 . 2 903 90 ARG HB3 H 2.10 . 2 904 90 ARG CG C 27.22 . 1 905 90 ARG HG2 H 1.84 . 2 906 90 ARG HG3 H 1.76 . 2 907 90 ARG CD C 42.52 . 1 908 90 ARG HD2 H 3.25 . 2 909 90 ARG HD3 H 3.15 . 2 910 90 ARG NE N 83.10 . 1 911 90 ARG HE H 7.30 . 1 912 91 VAL N N 118.98 . 1 913 91 VAL H H 8.29 . 1 914 91 VAL CA C 66.12 . 1 915 91 VAL HA H 3.81 . 1 916 91 VAL CB C 32.12 . 1 917 91 VAL HB H 2.35 . 1 918 91 VAL HG1 H 1.28 . 2 919 91 VAL HG2 H 1.33 . 2 920 91 VAL CG1 C 21.02 . 1 921 91 VAL CG2 C 24.22 . 1 922 92 VAL N N 121.18 . 1 923 92 VAL H H 9.00 . 1 924 92 VAL CA C 66.82 . 1 925 92 VAL HA H 3.58 . 1 926 92 VAL CB C 31.22 . 1 927 92 VAL HB H 2.25 . 1 928 92 VAL HG1 H 1.22 . 2 929 92 VAL HG2 H 0.95 . 2 930 92 VAL CG1 C 24.62 . 1 931 92 VAL CG2 C 24.32 . 1 932 93 GLU N N 120.28 . 1 933 93 GLU H H 8.17 . 1 934 93 GLU CA C 61.02 . 1 935 93 GLU HA H 3.60 . 1 936 93 GLU CB C 29.12 . 1 937 93 GLU HB2 H 2.15 . 2 938 93 GLU HB3 H 2.23 . 2 939 93 GLU CG C 35.82 . 1 940 93 GLU HG2 H 2.15 . 1 941 93 GLU HG3 H 2.15 . 1 942 94 GLN N N 114.68 . 1 943 94 GLN H H 7.27 . 1 944 94 GLN CA C 59.32 . 1 945 94 GLN HA H 3.98 . 1 946 94 GLN CB C 27.92 . 1 947 94 GLN HB2 H 2.13 . 2 948 94 GLN HB3 H 2.20 . 2 949 94 GLN CG C 33.72 . 1 950 94 GLN HG2 H 2.44 . 2 951 94 GLN HG3 H 2.42 . 2 952 94 GLN NE2 N 113.20 . 1 953 94 GLN HE21 H 7.55 . 2 954 94 GLN HE22 H 6.91 . 2 955 95 MET N N 118.98 . 1 956 95 MET H H 8.29 . 1 957 95 MET CA C 60.02 . 1 958 95 MET HA H 4.13 . 1 959 95 MET CB C 34.62 . 1 960 95 MET HB2 H 2.17 . 2 961 95 MET HB3 H 2.23 . 2 962 95 MET CG C 32.82 . 1 963 95 MET HG2 H 2.83 . 2 964 95 MET HG3 H 2.48 . 2 965 95 MET HE H 1.89 . 1 966 95 MET CE C 17.02 . 1 967 96 CYS N N 119.18 . 1 968 96 CYS H H 9.23 . 1 969 96 CYS CA C 60.02 . 1 970 96 CYS HA H 4.42 . 1 971 96 CYS CB C 41.82 . 1 972 96 CYS HB2 H 3.54 . 2 973 96 CYS HB3 H 2.88 . 2 974 97 ILE N N 123.68 . 1 975 97 ILE H H 8.36 . 1 976 97 ILE CA C 66.72 . 1 977 97 ILE HA H 3.57 . 1 978 97 ILE CB C 38.02 . 1 979 97 ILE HB H 2.00 . 1 980 97 ILE HG2 H 0.89 . 1 981 97 ILE CG2 C 17.12 . 1 982 97 ILE CG1 C 31.22 . 1 983 97 ILE HG12 H 1.97 . 2 984 97 ILE HG13 H 0.85 . 2 985 97 ILE HD1 H 0.84 . 1 986 97 ILE CD1 C 14.12 . 1 987 98 THR N N 118.48 . 1 988 98 THR H H 8.17 . 1 989 98 THR CA C 67.22 . 1 990 98 THR HA H 3.91 . 1 991 98 THR CB C 68.22 . 1 992 98 THR HB H 4.30 . 1 993 98 THR HG2 H 1.24 . 1 994 98 THR CG2 C 22.52 . 1 995 99 GLN N N 122.08 . 1 996 99 GLN H H 8.71 . 1 997 99 GLN CA C 58.72 . 1 998 99 GLN HA H 3.64 . 1 999 99 GLN CB C 28.42 . 1 1000 99 GLN HB2 H 2.32 . 2 1001 99 GLN HB3 H 2.12 . 2 1002 99 GLN CG C 32.92 . 1 1003 99 GLN HG2 H 1.69 . 2 1004 99 GLN HG3 H 1.67 . 2 1005 99 GLN NE2 N 114.70 . 1 1006 99 GLN HE21 H 7.18 . 2 1007 99 GLN HE22 H 6.84 . 2 1008 100 TYR N N 120.58 . 1 1009 100 TYR H H 8.59 . 1 1010 100 TYR CA C 62.12 . 1 1011 100 TYR HA H 2.92 . 1 1012 100 TYR CB C 37.42 . 1 1013 100 TYR HB2 H 3.07 . 2 1014 100 TYR HB3 H 2.75 . 2 1015 100 TYR HD1 H 6.18 . 1 1016 100 TYR HD2 H 6.18 . 1 1017 100 TYR HE1 H 6.52 . 1 1018 100 TYR HE2 H 6.52 . 1 1019 100 TYR CD1 C 132.62 . 1 1020 100 TYR CE1 C 117.82 . 1 1021 101 GLU N N 120.08 . 1 1022 101 GLU H H 8.32 . 1 1023 101 GLU CA C 59.32 . 1 1024 101 GLU HA H 3.69 . 1 1025 101 GLU CB C 28.42 . 1 1026 101 GLU HB2 H 2.31 . 2 1027 101 GLU HB3 H 2.04 . 2 1028 101 GLU CG C 34.92 . 1 1029 101 GLU HG2 H 2.67 . 2 1030 101 GLU HG3 H 2.44 . 2 1031 102 LYS N N 118.98 . 1 1032 102 LYS H H 7.77 . 1 1033 102 LYS CA C 59.32 . 1 1034 102 LYS HA H 3.98 . 1 1035 102 LYS CB C 32.62 . 1 1036 102 LYS HB2 H 1.83 . 2 1037 102 LYS HB3 H 1.89 . 2 1038 102 LYS CG C 25.12 . 1 1039 102 LYS HG2 H 1.34 . 2 1040 102 LYS HG3 H 1.54 . 2 1041 102 LYS CD C 29.52 . 1 1042 102 LYS HD2 H 1.58 . 1 1043 102 LYS HD3 H 1.58 . 1 1044 102 LYS CE C 41.82 . 1 1045 102 LYS HE2 H 2.88 . 1 1046 102 LYS HE3 H 2.88 . 1 1047 103 GLU N N 118.58 . 1 1048 103 GLU H H 8.42 . 1 1049 103 GLU CA C 57.62 . 1 1050 103 GLU HA H 4.03 . 1 1051 103 GLU CB C 29.32 . 1 1052 103 GLU HB2 H 1.64 . 1 1053 103 GLU HB3 H 1.64 . 1 1054 103 GLU CG C 36.02 . 1 1055 103 GLU HG2 H 2.17 . 2 1056 103 GLU HG3 H 2.41 . 2 1057 104 SER N N 115.48 . 1 1058 104 SER H H 8.46 . 1 1059 104 SER CA C 61.22 . 1 1060 104 SER HA H 3.90 . 1 1061 104 SER CB C 62.72 . 1 1062 104 SER HB2 H 3.57 . 2 1063 104 SER HB3 H 3.35 . 2 1064 105 GLN N N 120.18 . 1 1065 105 GLN H H 7.56 . 1 1066 105 GLN CA C 58.42 . 1 1067 105 GLN HA H 4.11 . 1 1068 105 GLN CB C 28.32 . 1 1069 105 GLN HB2 H 2.10 . 1 1070 105 GLN HB3 H 2.10 . 1 1071 105 GLN CG C 34.22 . 1 1072 105 GLN HG2 H 2.49 . 2 1073 105 GLN HG3 H 2.37 . 2 1074 105 GLN NE2 N 111.80 . 1 1075 105 GLN HE21 H 7.48 . 2 1076 105 GLN HE22 H 6.82 . 2 1077 106 ALA N N 120.28 . 1 1078 106 ALA H H 7.49 . 1 1079 106 ALA CA C 53.82 . 1 1080 106 ALA HA H 4.16 . 1 1081 106 ALA HB H 1.40 . 1 1082 106 ALA CB C 18.62 . 1 1083 107 TYR N N 118.98 . 1 1084 107 TYR H H 8.01 . 1 1085 107 TYR CA C 60.02 . 1 1086 107 TYR HA H 4.18 . 1 1087 107 TYR CB C 39.32 . 1 1088 107 TYR HB2 H 3.00 . 2 1089 107 TYR HB3 H 2.80 . 2 1090 107 TYR HD1 H 6.64 . 1 1091 107 TYR HD2 H 6.64 . 1 1092 107 TYR HE1 H 6.84 . 1 1093 107 TYR HE2 H 6.84 . 1 1094 107 TYR CD1 C 133.12 . 1 1095 107 TYR CE1 C 117.92 . 1 1096 108 TYR N N 118.08 . 1 1097 108 TYR H H 7.97 . 1 1098 108 TYR CA C 58.92 . 1 1099 108 TYR HA H 4.37 . 1 1100 108 TYR CB C 38.22 . 1 1101 108 TYR HB2 H 3.15 . 2 1102 108 TYR HB3 H 2.92 . 2 1103 108 TYR HD1 H 7.17 . 1 1104 108 TYR HD2 H 7.17 . 1 1105 108 TYR HE1 H 6.83 . 1 1106 108 TYR HE2 H 6.83 . 1 1107 108 TYR CD1 C 133.32 . 1 1108 108 TYR CE1 C 118.12 . 1 1109 109 GLN N N 119.48 . 1 1110 109 GLN H H 7.85 . 1 1111 109 GLN CA C 56.12 . 1 1112 109 GLN HA H 4.23 . 1 1113 109 GLN CB C 28.82 . 1 1114 109 GLN HB2 H 2.12 . 2 1115 109 GLN HB3 H 2.04 . 2 1116 109 GLN CG C 33.82 . 1 1117 109 GLN HG2 H 2.36 . 1 1118 109 GLN HG3 H 2.36 . 1 1119 109 GLN NE2 N 111.80 . 1 1120 109 GLN HE21 H 7.50 . 2 1121 109 GLN HE22 H 6.84 . 2 1122 110 ARG N N 120.68 . 1 1123 110 ARG H H 7.97 . 1 1124 110 ARG CA C 56.72 . 1 1125 110 ARG HA H 4.27 . 1 1126 110 ARG CB C 30.72 . 1 1127 110 ARG HB2 H 1.80 . 2 1128 110 ARG HB3 H 1.85 . 2 1129 110 ARG CG C 27.02 . 1 1130 110 ARG HG2 H 1.65 . 2 1131 110 ARG HG3 H 1.62 . 2 1132 110 ARG CD C 43.32 . 1 1133 110 ARG HD2 H 3.14 . 1 1134 110 ARG HD3 H 3.14 . 1 1135 110 ARG NE N 84.90 . 1 1136 110 ARG HE H 7.17 . 1 1137 111 GLY N N 108.48 . 1 1138 111 GLY H H 8.31 . 1 1139 111 GLY CA C 45.22 . 1 1140 111 GLY HA3 H 3.95 . 1 1141 111 GLY HA2 H 3.95 . 1 1142 112 SER N N 115.58 . 1 1143 112 SER H H 8.16 . 1 1144 112 SER CA C 58.52 . 1 1145 112 SER HA H 4.49 . 1 1146 112 SER CB C 63.72 . 1 1147 112 SER HB2 H 3.88 . 1 1148 112 SER HB3 H 3.88 . 1 stop_ save_