data_4379 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of the Human Prion Protein Domain reveals Species Dependent Structural Disorder and Intramolecular Association with the Flexible Tail ; _BMRB_accession_number 4379 _BMRB_flat_file_name bmr4379.str _Entry_type original _Submission_date 1999-08-18 _Accession_date 1999-08-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zahn Ralph . . 2 Aizhuo Liu . . 3 Luhrs Thorsten . . 4 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 667 "13C chemical shifts" 354 "15N chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-02-01 original author . stop_ _Original_release_date 2000-02-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Solution Structure of the Human Prion Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20087216 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zahn Ralph . . 2 Liu Aizhuo . . 3 Luhrs Thorsten . . 4 Riek Roland . . 5 'von Schroetter' Christine . . 6 'Lopez Garcia' Francisco . . 7 Billeter Martin . . 8 Calzolai Luigi . . 9 Wider Gerhard . . 10 Wuthrich Kurt . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 97 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 145 _Page_last 150 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_hPrP(121-230) _Saveframe_category molecular_system _Mol_system_name 'human prion protein fragment 121-230' _Abbreviation_common hPrP(121-230) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hPrP(121-230) $hPrP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state unknown _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hPrP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human prion protein' _Abbreviation_common hPrP _Molecular_mass 13246 _Mol_thiol_state . _Details 'The N-terminal two residues (GS) are a cloning artefact.' ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; GSVVGGLGGYMLGSAMSRPI IHFGSDYEDRYYRENMHRYP NQVYYRPMDEYSNQNNFVHD 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 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 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 . _Sequence_homology_query_revised_last_date 2015-08-04 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 BMRB 15676 V129/D178N_prion_protein 100.00 146 97.32 100.00 2.10e-75 BMRB 16743 "HuPrP(90-231 M129 Q212P)" 100.00 148 98.21 99.11 8.86e-76 BMRB 17714 HuPrP 100.00 147 98.21 100.00 1.23e-76 BMRB 17756 hPrP(121-230) 98.21 113 100.00 100.00 4.71e-75 BMRB 17757 hPrP(121-230) 98.21 113 98.18 98.18 2.15e-72 BMRB 17780 Hpp_E219K 100.00 142 98.21 100.00 2.25e-76 BMRB 18426 entity 100.00 142 99.11 100.00 6.41e-77 BMRB 18550 V210I 100.00 147 98.21 100.00 1.23e-76 BMRB 19268 MAJOR_PRION_PROTEIN 100.00 146 98.21 100.00 2.70e-76 BMRB 4402 "human prion protein" 100.00 210 99.11 100.00 3.59e-77 BMRB 4434 "human prion protein" 100.00 143 99.11 100.00 7.63e-77 BMRB 4620 "prion protein" 100.00 112 99.11 100.00 2.24e-76 BMRB 4641 "PRION PROTEIN" 100.00 146 98.21 100.00 2.79e-76 BMRB 4736 "human prion protein" 100.00 112 99.11 100.00 3.79e-76 PDB 1E1G "Human Prion Protein Variant M166v" 91.96 104 99.03 100.00 3.32e-69 PDB 1E1J "Human Prion Protein Variant M166v" 91.96 104 99.03 100.00 3.32e-69 PDB 1E1P "Human Prion Protein Variant S170n" 91.96 104 99.03 100.00 2.98e-69 PDB 1E1S "Human Prion Protein Variant S170n" 91.96 104 99.03 100.00 2.98e-69 PDB 1E1U "Human Prion Protein Variant R220k" 91.96 104 99.03 100.00 1.71e-69 PDB 1E1W "Human Prion Protein Variant R220k" 91.96 104 99.03 100.00 1.71e-69 PDB 1FKC "Human Prion Protein (Mutant E200k) Fragment 90-231" 100.00 142 98.21 100.00 2.25e-76 PDB 1FO7 "Human Prion Protein Mutant E200k Fragment 90-231" 100.00 142 98.21 100.00 2.25e-76 PDB 1H0L "Human Prion Protein 121-230 M166c/e221c" 99.11 112 98.20 98.20 1.39e-73 PDB 1HJM "Human Prion Protein At Ph 7.0" 91.96 104 100.00 100.00 6.83e-70 PDB 1HJN "Human Prion Protein At Ph 7.0" 91.96 104 100.00 100.00 6.83e-70 PDB 1I4M "Crystal Structure Of The Human Prion Protein Reveals A Mechanism For Oligomerization" 96.43 108 99.07 100.00 2.07e-73 PDB 1QLX "Human Prion Protein" 100.00 210 99.11 100.00 3.59e-77 PDB 1QLZ "Human Prion Protein" 100.00 210 99.11 100.00 3.59e-77 PDB 1QM0 "Human Prion Protein Fragment 90-230" 100.00 143 99.11 100.00 7.63e-77 PDB 1QM1 "Human Prion Protein Fragment 90-230" 100.00 143 99.11 100.00 7.63e-77 PDB 1QM2 "Human Prion Protein Fragment 121-230" 100.00 112 100.00 100.00 9.07e-77 PDB 1QM3 "Human Prion Protein Fragment 121-230" 100.00 112 100.00 100.00 9.07e-77 PDB 2K1D "Nmr Studies Of A Pathogenic Mutant (d178n) Of The Human Prion Protein" 100.00 146 97.32 100.00 2.10e-75 PDB 2KUN "Three Dimensional Structure Of Huprp(90-231 M129 Q212p)" 100.00 148 98.21 99.11 8.86e-76 PDB 2LEJ "Human Prion Protein Mutant Huprp(90-231, M129, V210i)" 100.00 147 98.21 100.00 1.23e-76 PDB 2LFT "Human Prion Protein With E219k Protective Polymorphism" 100.00 142 98.21 100.00 2.25e-76 PDB 2LSB "Solution-State Nmr Structure Of The Human Prion Protein" 100.00 142 99.11 100.00 6.41e-77 PDB 2LV1 "Solution-state Nmr Structure Of Prion Protein Mutant V210i At Neutral Ph" 100.00 147 98.21 100.00 1.23e-76 PDB 2M8T "Solution Nmr Structure Of The V209m Variant Of The Human Prion Protein (residues 90-231)" 100.00 146 98.21 100.00 2.70e-76 PDB 2W9E "Structure Of Icsm 18 (Anti-Prp Therapeutic Antibody) Fab Fragment Complexed With Human Prp Fragment 119-231" 100.00 113 99.11 100.00 1.55e-76 PDB 3HAF "Human Prion Protein Variant V129 Domain Swapped Dimer" 100.00 142 98.21 100.00 3.08e-76 PDB 3HAK "Human Prion Protein Variant V129" 91.96 103 99.03 100.00 2.40e-69 PDB 3HEQ "Human Prion Protein Variant D178n With M129" 100.00 142 98.21 100.00 3.05e-76 PDB 3HER "Human Prion Protein Variant F198s With V129" 100.00 142 97.32 99.11 4.77e-75 PDB 3HES "Human Prion Protein Variant F198s With M129" 100.00 142 98.21 99.11 8.98e-76 PDB 3HJ5 "Human Prion Protein Variant V129 Domain Swapped Dimer" 100.00 142 98.21 100.00 3.08e-76 PDB 3HJX "Human Prion Protein Variant D178n With V129" 93.75 106 98.10 100.00 3.90e-70 PDB 4DGI "Structure Of Pom1 Fab Fragment Complexed With Human Prpc Fragment 120- 230" 99.11 111 99.10 100.00 1.25e-75 PDB 4KML "Probing The N-terminal Beta-sheet Conversion In The Crystal Structure Of The Full-length Human Prion Protein Bound To A Nanobod" 100.00 241 99.11 100.00 4.99e-77 PDB 4N9O "Probing The N-terminal Beta-sheet Conversion In The Crystal Structure Of The Human Prion Protein Bound To A Nanobody" 100.00 142 99.11 100.00 6.41e-77 DBJ BAA00011 "prion protein [Homo sapiens]" 100.00 245 99.11 100.00 3.05e-76 DBJ BAF62360 "prion protein, transcript variant 2 [Pan troglodytes verus]" 100.00 253 97.32 100.00 5.61e-75 DBJ BAG32276 "prion [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 DBJ BAG32277 "prion [Homo sapiens]" 100.00 253 98.21 100.00 2.02e-75 DBJ BAG32278 "alternatively spliced variant form of prion [Homo sapiens]" 88.39 230 98.99 100.00 1.22e-66 EMBL CAA58442 "prion protein [Homo sapiens]" 100.00 245 99.11 100.00 3.48e-76 EMBL CAG46836 "PRNP [Homo sapiens]" 100.00 253 98.21 100.00 2.35e-75 EMBL CAG46869 "PRNP [Homo sapiens]" 100.00 253 98.21 100.00 2.02e-75 GB AAA19664 "prion protein [Homo sapiens]" 100.00 245 99.11 100.00 3.05e-76 GB AAA60182 "prion protein [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 GB AAA68632 "major prion protein precursor [Pan troglodytes]" 100.00 253 97.32 100.00 5.61e-75 GB AAA68633 "major prion protein precursor [Gorilla gorilla]" 100.00 253 98.21 100.00 9.45e-76 GB AAB59442 "prion protein, partial [Homo sapiens]" 100.00 224 99.11 100.00 1.72e-76 REF NP_000302 "major prion protein preproprotein [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 REF NP_001009093 "major prion protein preproprotein [Pan troglodytes]" 100.00 253 97.32 100.00 5.61e-75 REF NP_001073590 "major prion protein preproprotein [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 REF NP_001073591 "major prion protein preproprotein [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 REF NP_001073592 "major prion protein preproprotein [Homo sapiens]" 100.00 253 99.11 100.00 3.55e-76 SP P04156 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=ASCR; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_" 100.00 253 99.11 100.00 3.55e-76 SP P40252 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" 100.00 253 98.21 100.00 9.24e-76 SP P61766 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" 100.00 253 97.32 100.00 5.61e-75 SP P61767 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" 100.00 253 97.32 100.00 5.61e-75 SP P61768 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" 100.00 253 97.32 100.00 5.61e-75 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 _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hPrP 1.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hPrP 1.0 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hPrP 1.0 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Saveframe_category software _Name PROSA _Version . _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _Sample_label . save_ save_1H-1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-13C NOESY' _Sample_label . save_ save_HCCH_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _Sample_label . save_ save_HCCH_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 . M pH 4.5 0.1 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_CSS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H-15N NOESY' '1H-1H-13C NOESY' 'HCCH COSY' 'HCCH TOCSY' HNCA HNCACB stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name hPrP(121-230) _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY CA C 43.0 . 1 2 . 1 GLY HA2 H 3.89 . 1 3 . 1 GLY HA3 H 3.89 . 1 4 . 2 SER N N 115.7 . 1 5 . 2 SER H H 8.64 . 1 6 . 2 SER CA C 57.9 . 1 7 . 2 SER HA H 4.52 . 1 8 . 2 SER CB C 63.7 . 1 9 . 2 SER HB2 H 3.80 . 1 10 . 2 SER HB3 H 3.80 . 1 11 . 3 VAL N N 122.2 . 1 12 . 3 VAL H H 8.36 . 1 13 . 3 VAL CA C 62.0 . 1 14 . 3 VAL HA H 4.16 . 1 15 . 3 VAL CB C 32.5 . 1 16 . 3 VAL HB H 2.04 . 1 17 . 3 VAL HG1 H 0.85 . 1 18 . 3 VAL HG2 H 0.88 . 1 19 . 3 VAL CG1 C 20.9 . 1 20 . 3 VAL CG2 C 20.3 . 1 21 . 4 VAL N N 125.0 . 1 22 . 4 VAL H H 8.31 . 1 23 . 4 VAL CA C 62.5 . 1 24 . 4 VAL HA H 4.06 . 1 25 . 4 VAL CB C 32.4 . 1 26 . 4 VAL HB H 2.00 . 1 27 . 4 VAL HG1 H 0.88 . 1 28 . 4 VAL HG2 H 0.90 . 1 29 . 4 VAL CG1 C 20.9 . 1 30 . 4 VAL CG2 C 20.5 . 1 31 . 5 GLY N N 113.2 . 1 32 . 5 GLY H H 8.56 . 1 33 . 5 GLY CA C 45.2 . 1 34 . 5 GLY HA2 H 3.93 . 1 35 . 5 GLY HA3 H 3.93 . 1 36 . 6 GLY N N 108.6 . 1 37 . 6 GLY H H 8.28 . 1 38 . 6 GLY CA C 45.0 . 1 39 . 6 GLY HA2 H 3.93 . 1 40 . 6 GLY HA3 H 3.93 . 1 41 . 7 LEU N N 121.8 . 1 42 . 7 LEU H H 8.24 . 1 43 . 7 LEU CA C 54.7 . 1 44 . 7 LEU HA H 4.34 . 1 45 . 7 LEU CB C 42.2 . 1 46 . 7 LEU HB2 H 1.51 . 2 47 . 7 LEU HB3 H 1.59 . 2 48 . 7 LEU CG C 26.7 . 1 49 . 7 LEU HG H 1.48 . 1 50 . 7 LEU HD1 H 0.67 . 1 51 . 7 LEU HD2 H 0.55 . 1 52 . 7 LEU CD1 C 24.5 . 1 53 . 7 LEU CD2 C 23.3 . 1 54 . 8 GLY N N 109.9 . 1 55 . 8 GLY H H 8.52 . 1 56 . 8 GLY CA C 46.0 . 1 57 . 8 GLY HA2 H 3.83 . 2 58 . 8 GLY HA3 H 3.90 . 2 59 . 9 GLY N N 109.2 . 1 60 . 9 GLY H H 8.34 . 1 61 . 9 GLY CA C 44.8 . 1 62 . 9 GLY HA2 H 3.71 . 2 63 . 9 GLY HA3 H 3.87 . 2 64 . 10 TYR N N 117.5 . 1 65 . 10 TYR H H 7.68 . 1 66 . 10 TYR CA C 57.8 . 1 67 . 10 TYR HA H 4.50 . 1 68 . 10 TYR CB C 40.1 . 1 69 . 10 TYR HB2 H 2.87 . 2 70 . 10 TYR HB3 H 2.80 . 2 71 . 10 TYR HD1 H 6.80 . 1 72 . 10 TYR HD2 H 6.80 . 1 73 . 10 TYR HE1 H 6.63 . 1 74 . 10 TYR HE2 H 6.63 . 1 75 . 10 TYR CD1 C 132.7 . 1 76 . 10 TYR CE1 C 118.0 . 1 77 . 11 MET N N 120.7 . 1 78 . 11 MET H H 8.99 . 1 79 . 11 MET CA C 53.4 . 1 80 . 11 MET HA H 4.52 . 1 81 . 11 MET CB C 34.5 . 1 82 . 11 MET HB2 H 0.93 . 2 83 . 11 MET HB3 H 1.57 . 2 84 . 11 MET CG C 31.8 . 1 85 . 11 MET HG2 H 2.21 . 1 86 . 11 MET HG3 H 2.21 . 1 87 . 11 MET HE H 1.98 . 1 88 . 11 MET CE C 16.9 . 1 89 . 12 LEU N N 121.4 . 1 90 . 12 LEU H H 8.08 . 1 91 . 12 LEU CA C 53.1 . 1 92 . 12 LEU HA H 4.42 . 1 93 . 12 LEU CB C 43.2 . 1 94 . 12 LEU HB2 H 0.95 . 2 95 . 12 LEU HB3 H 1.60 . 2 96 . 12 LEU CG C 25.7 . 1 97 . 12 LEU HG H 1.35 . 1 98 . 12 LEU HD1 H -0.06 . 1 99 . 12 LEU HD2 H 0.59 . 1 100 . 12 LEU CD1 C 21.4 . 1 101 . 12 LEU CD2 C 25.5 . 1 102 . 13 GLY N N 115.0 . 1 103 . 13 GLY H H 9.34 . 1 104 . 13 GLY CA C 44.6 . 1 105 . 13 GLY HA2 H 4.01 . 2 106 . 13 GLY HA3 H 4.40 . 2 107 . 14 SER N N 113.6 . 1 108 . 14 SER H H 8.39 . 1 109 . 14 SER CA C 58.2 . 1 110 . 14 SER HA H 4.39 . 1 111 . 14 SER CB C 63.8 . 1 112 . 14 SER HB2 H 3.97 . 2 113 . 14 SER HB3 H 3.88 . 2 114 . 15 ALA N N 125.6 . 1 115 . 15 ALA H H 8.79 . 1 116 . 15 ALA CA C 52.7 . 1 117 . 15 ALA HA H 4.43 . 1 118 . 15 ALA HB H 1.25 . 1 119 . 15 ALA CB C 18.2 . 1 120 . 16 MET N N 120.7 . 1 121 . 16 MET H H 8.71 . 1 122 . 16 MET CA C 53.6 . 1 123 . 16 MET HA H 4.73 . 1 124 . 16 MET CB C 36.9 . 1 125 . 16 MET HB2 H 1.99 . 1 126 . 16 MET HB3 H 1.99 . 1 127 . 16 MET CG C 30.7 . 1 128 . 16 MET HG2 H 2.43 . 2 129 . 16 MET HG3 H 2.38 . 2 130 . 16 MET HE H 2.13 . 1 131 . 16 MET CE C 17.4 . 1 132 . 17 SER N N 116.2 . 1 133 . 17 SER H H 8.44 . 1 134 . 17 SER CA C 58.3 . 1 135 . 17 SER HA H 4.31 . 1 136 . 17 SER CB C 62.7 . 1 137 . 17 SER HB2 H 3.80 . 2 138 . 17 SER HB3 H 3.72 . 2 139 . 18 ARG N N 126.5 . 1 140 . 18 ARG H H 8.64 . 1 141 . 18 ARG CA C 54.6 . 1 142 . 18 ARG HA H 4.38 . 1 143 . 18 ARG CB C 29.2 . 1 144 . 18 ARG HB2 H 1.70 . 1 145 . 18 ARG HB3 H 1.70 . 1 146 . 18 ARG CG C 28.6 . 1 147 . 18 ARG HG2 H 1.85 . 2 148 . 18 ARG HG3 H 1.77 . 2 149 . 18 ARG CD C 43.9 . 1 150 . 18 ARG HD2 H 3.11 . 2 151 . 18 ARG HD3 H 3.03 . 2 152 . 18 ARG NE N 85.9 . 1 153 . 18 ARG HE H 6.71 . 1 154 . 19 PRO CD C 50.4 . 1 155 . 19 PRO CA C 62.2 . 1 156 . 19 PRO HA H 4.40 . 1 157 . 19 PRO CB C 32.2 . 1 158 . 19 PRO HB2 H 1.73 . 2 159 . 19 PRO HB3 H 2.23 . 2 160 . 19 PRO CG C 27.2 . 1 161 . 19 PRO HG2 H 1.96 . 2 162 . 19 PRO HG3 H 2.02 . 2 163 . 19 PRO HD2 H 3.61 . 2 164 . 19 PRO HD3 H 3.90 . 2 165 . 20 ILE N N 122.5 . 1 166 . 20 ILE H H 8.64 . 1 167 . 20 ILE CA C 60.7 . 1 168 . 20 ILE HA H 4.12 . 1 169 . 20 ILE CB C 36.1 . 1 170 . 20 ILE HB H 1.89 . 1 171 . 20 ILE HG2 H 0.70 . 1 172 . 20 ILE CG2 C 17.1 . 1 173 . 20 ILE CG1 C 27.0 . 1 174 . 20 ILE HG12 H 1.56 . 2 175 . 20 ILE HG13 H 1.36 . 2 176 . 20 ILE HD1 H 0.87 . 1 177 . 20 ILE CD1 C 11.0 . 1 178 . 21 ILE N N 126.8 . 1 179 . 21 ILE H H 6.45 . 1 180 . 21 ILE CA C 58.6 . 1 181 . 21 ILE HA H 3.88 . 1 182 . 21 ILE CB C 39.2 . 1 183 . 21 ILE HB H 0.80 . 1 184 . 21 ILE HG2 H -0.10 . 1 185 . 21 ILE CG2 C 17.0 . 1 186 . 21 ILE CG1 C 26.5 . 1 187 . 21 ILE HG12 H 0.91 . 2 188 . 21 ILE HG13 H 0.77 . 2 189 . 21 ILE HD1 H 0.46 . 1 190 . 21 ILE CD1 C 12.4 . 1 191 . 22 HIS N N 122.0 . 1 192 . 22 HIS H H 8.24 . 1 193 . 22 HIS CA C 53.8 . 1 194 . 22 HIS HA H 4.90 . 1 195 . 22 HIS CB C 29.2 . 1 196 . 22 HIS HB2 H 2.92 . 1 197 . 22 HIS HB3 H 3.29 . 1 198 . 22 HIS CD2 C 119.6 . 1 199 . 22 HIS CE1 C 136.0 . 1 200 . 22 HIS HD2 H 7.21 . 1 201 . 22 HIS HE1 H 8.57 . 1 202 . 23 PHE N N 124.0 . 1 203 . 23 PHE H H 10.20 . 1 204 . 23 PHE CA C 59.1 . 1 205 . 23 PHE HA H 4.33 . 1 206 . 23 PHE CB C 41.2 . 1 207 . 23 PHE HB2 H 3.31 . 1 208 . 23 PHE HB3 H 2.78 . 1 209 . 23 PHE HD1 H 7.31 . 1 210 . 23 PHE HD2 H 7.31 . 1 211 . 23 PHE HE1 H 6.86 . 1 212 . 23 PHE HE2 H 6.86 . 1 213 . 23 PHE CD1 C 131.9 . 1 214 . 23 PHE CE1 C 131.1 . 1 215 . 23 PHE CZ C 128.8 . 1 216 . 23 PHE HZ H 6.70 . 1 217 . 24 GLY N N 108.5 . 1 218 . 24 GLY H H 9.00 . 1 219 . 24 GLY CA C 45.5 . 1 220 . 24 GLY HA2 H 3.79 . 2 221 . 24 GLY HA3 H 4.16 . 2 222 . 25 SER N N 111.7 . 1 223 . 25 SER H H 7.28 . 1 224 . 25 SER CA C 56.3 . 1 225 . 25 SER HA H 4.78 . 1 226 . 25 SER CB C 65.7 . 1 227 . 25 SER HB2 H 4.11 . 2 228 . 25 SER HB3 H 3.88 . 2 229 . 26 ASP N N 124.5 . 1 230 . 26 ASP H H 9.05 . 1 231 . 26 ASP CA C 57.4 . 1 232 . 26 ASP HA H 4.48 . 1 233 . 26 ASP CB C 40.3 . 1 234 . 26 ASP HB2 H 2.74 . 1 235 . 26 ASP HB3 H 2.74 . 1 236 . 27 TYR N N 118.9 . 1 237 . 27 TYR H H 8.58 . 1 238 . 27 TYR CA C 61.2 . 1 239 . 27 TYR HA H 4.17 . 1 240 . 27 TYR CB C 37.9 . 1 241 . 27 TYR HB2 H 3.24 . 1 242 . 27 TYR HB3 H 2.82 . 1 243 . 27 TYR HD1 H 7.03 . 1 244 . 27 TYR HD2 H 7.03 . 1 245 . 27 TYR HE1 H 6.73 . 1 246 . 27 TYR HE2 H 6.73 . 1 247 . 27 TYR CD1 C 133.1 . 1 248 . 27 TYR CE1 C 117.7 . 1 249 . 28 GLU N N 118.9 . 1 250 . 28 GLU H H 7.70 . 1 251 . 28 GLU CA C 59.4 . 1 252 . 28 GLU HA H 3.59 . 1 253 . 28 GLU CB C 29.5 . 1 254 . 28 GLU HB2 H 1.94 . 1 255 . 28 GLU HB3 H 1.54 . 1 256 . 28 GLU CG C 36.9 . 1 257 . 28 GLU HG2 H 1.92 . 1 258 . 28 GLU HG3 H 2.28 . 1 259 . 29 ASP N N 119.7 . 1 260 . 29 ASP H H 8.20 . 1 261 . 29 ASP CA C 58.2 . 1 262 . 29 ASP HA H 4.65 . 1 263 . 29 ASP CB C 40.0 . 1 264 . 29 ASP HB2 H 2.87 . 2 265 . 29 ASP HB3 H 3.02 . 2 266 . 30 ARG N N 120.3 . 1 267 . 30 ARG H H 8.21 . 1 268 . 30 ARG CA C 59.4 . 1 269 . 30 ARG HA H 3.99 . 1 270 . 30 ARG CB C 29.7 . 1 271 . 30 ARG HB2 H 1.88 . 1 272 . 30 ARG HB3 H 1.88 . 1 273 . 30 ARG CG C 27.7 . 1 274 . 30 ARG HG2 H 1.51 . 1 275 . 30 ARG HG3 H 1.74 . 1 276 . 30 ARG CD C 43.4 . 1 277 . 30 ARG HD2 H 3.17 . 2 278 . 30 ARG HD3 H 3.21 . 2 279 . 30 ARG NE N 85.2 . 1 280 . 30 ARG HE H 7.45 . 1 281 . 31 TYR N N 121.3 . 1 282 . 31 TYR H H 8.29 . 1 283 . 31 TYR CA C 62.1 . 1 284 . 31 TYR HA H 3.80 . 1 285 . 31 TYR CB C 38.0 . 1 286 . 31 TYR HB2 H 2.59 . 1 287 . 31 TYR HB3 H 2.86 . 1 288 . 31 TYR HD1 H 6.92 . 1 289 . 31 TYR HD2 H 6.92 . 1 290 . 31 TYR HE1 H 6.74 . 1 291 . 31 TYR HE2 H 6.74 . 1 292 . 31 TYR CD1 C 133.2 . 1 293 . 31 TYR CE1 C 117.9 . 1 294 . 32 TYR N N 120.6 . 1 295 . 32 TYR H H 8.95 . 1 296 . 32 TYR CA C 62.8 . 1 297 . 32 TYR HA H 4.09 . 1 298 . 32 TYR CB C 37.9 . 1 299 . 32 TYR HB2 H 3.51 . 1 300 . 32 TYR HB3 H 3.24 . 1 301 . 32 TYR HD1 H 7.52 . 1 302 . 32 TYR HD2 H 7.52 . 1 303 . 32 TYR HE1 H 6.98 . 1 304 . 32 TYR HE2 H 6.98 . 1 305 . 32 TYR CD1 C 133.4 . 1 306 . 32 TYR CE1 C 118.0 . 1 307 . 33 ARG N N 117.8 . 1 308 . 33 ARG H H 7.97 . 1 309 . 33 ARG CA C 59.8 . 1 310 . 33 ARG HA H 3.90 . 1 311 . 33 ARG CB C 29.7 . 1 312 . 33 ARG HB2 H 2.05 . 1 313 . 33 ARG HB3 H 1.93 . 1 314 . 33 ARG CG C 28.1 . 1 315 . 33 ARG HG2 H 1.71 . 1 316 . 33 ARG HG3 H 2.01 . 1 317 . 33 ARG CD C 43.0 . 1 318 . 33 ARG HD2 H 3.36 . 2 319 . 33 ARG HD3 H 3.26 . 2 320 . 33 ARG NE N 84.2 . 1 321 . 33 ARG HE H 7.47 . 1 322 . 34 GLU N N 116.4 . 1 323 . 34 GLU H H 8.05 . 1 324 . 34 GLU CA C 57.8 . 1 325 . 34 GLU HA H 4.05 . 1 326 . 34 GLU CB C 29.3 . 1 327 . 34 GLU HB2 H 1.87 . 1 328 . 34 GLU HB3 H 1.87 . 1 329 . 34 GLU CG C 35.3 . 1 330 . 34 GLU HG2 H 2.25 . 2 331 . 34 GLU HG3 H 2.42 . 2 332 . 35 ASN N N 114.7 . 1 333 . 35 ASN H H 7.60 . 1 334 . 35 ASN CA C 54.7 . 1 335 . 35 ASN HA H 4.25 . 1 336 . 35 ASN CB C 40.8 . 1 337 . 35 ASN HB2 H 2.13 . 1 338 . 35 ASN HB3 H 2.13 . 1 339 . 35 ASN ND2 N 117.1 . 1 340 . 35 ASN HD21 H 6.68 . 1 341 . 35 ASN HD22 H 6.58 . 1 342 . 36 MET N N 119.7 . 1 343 . 36 MET H H 8.11 . 1 344 . 36 MET CA C 59.1 . 1 345 . 36 MET HA H 3.43 . 1 346 . 36 MET CB C 30.0 . 1 347 . 36 MET HB2 H 1.63 . 1 348 . 36 MET HB3 H 1.29 . 1 349 . 36 MET CG C 30.4 . 1 350 . 36 MET HG2 H 2.51 . 2 351 . 36 MET HG3 H 2.12 . 2 352 . 36 MET HE H 2.00 . 1 353 . 36 MET CE C 17.4 . 1 354 . 37 HIS N N 115.1 . 1 355 . 37 HIS H H 8.07 . 1 356 . 37 HIS CA C 57.4 . 1 357 . 37 HIS HA H 4.20 . 1 358 . 37 HIS CB C 26.9 . 1 359 . 37 HIS HB2 H 3.06 . 2 360 . 37 HIS HB3 H 3.30 . 2 361 . 37 HIS CD2 C 120.3 . 1 362 . 37 HIS HD2 H 7.35 . 1 363 . 38 ARG N N 117.8 . 1 364 . 38 ARG H H 7.60 . 1 365 . 38 ARG CA C 56.0 . 1 366 . 38 ARG HA H 4.11 . 1 367 . 38 ARG CB C 30.4 . 1 368 . 38 ARG HB2 H 1.38 . 2 369 . 38 ARG HB3 H 2.05 . 2 370 . 38 ARG CG C 27.2 . 1 371 . 38 ARG HG2 H 1.36 . 2 372 . 38 ARG HG3 H 0.34 . 2 373 . 38 ARG CD C 43.9 . 1 374 . 38 ARG HD2 H 3.06 . 2 375 . 38 ARG HD3 H 3.22 . 2 376 . 38 ARG NE N 84.2 . 1 377 . 38 ARG HE H 7.34 . 1 378 . 39 TYR N N 120.7 . 1 379 . 39 TYR H H 7.46 . 1 380 . 39 TYR CA C 52.5 . 1 381 . 39 TYR HA H 5.01 . 1 382 . 39 TYR CB C 34.8 . 1 383 . 39 TYR HB2 H 3.11 . 1 384 . 39 TYR HB3 H 3.11 . 1 385 . 39 TYR HD1 H 6.86 . 1 386 . 39 TYR HD2 H 6.86 . 1 387 . 39 TYR HE1 H 6.51 . 1 388 . 39 TYR HE2 H 6.51 . 1 389 . 39 TYR CD1 C 131.1 . 1 390 . 39 TYR CE1 C 117.0 . 1 391 . 40 PRO CD C 50.0 . 1 392 . 40 PRO CA C 63.5 . 1 393 . 40 PRO HA H 4.44 . 1 394 . 40 PRO CB C 32.2 . 1 395 . 40 PRO HB2 H 1.70 . 2 396 . 40 PRO HB3 H 2.44 . 2 397 . 40 PRO CG C 27.2 . 1 398 . 40 PRO HG2 H 1.55 . 2 399 . 40 PRO HG3 H 1.34 . 2 400 . 40 PRO HD2 H 3.15 . 2 401 . 40 PRO HD3 H 3.39 . 2 402 . 41 ASN N N 116.1 . 1 403 . 41 ASN H H 8.54 . 1 404 . 41 ASN CA C 51.7 . 1 405 . 41 ASN HA H 4.71 . 1 406 . 41 ASN CB C 38.0 . 1 407 . 41 ASN HB2 H 3.68 . 2 408 . 41 ASN HB3 H 2.40 . 2 409 . 41 ASN ND2 N 109.1 . 1 410 . 41 ASN HD21 H 7.48 . 1 411 . 41 ASN HD22 H 6.76 . 1 412 . 42 GLN N N 113.6 . 1 413 . 42 GLN H H 7.25 . 1 414 . 42 GLN CA C 54.0 . 1 415 . 42 GLN HA H 4.52 . 1 416 . 42 GLN CB C 33.5 . 1 417 . 42 GLN HB2 H 1.68 . 1 418 . 42 GLN HB3 H 1.97 . 1 419 . 42 GLN CG C 33.9 . 1 420 . 42 GLN HG2 H 2.14 . 2 421 . 42 GLN HG3 H 2.01 . 2 422 . 42 GLN NE2 N 112.7 . 1 423 . 42 GLN HE21 H 7.91 . 1 424 . 42 GLN HE22 H 6.99 . 1 425 . 43 VAL N N 112.8 . 1 426 . 43 VAL H H 8.53 . 1 427 . 43 VAL CA C 58.5 . 1 428 . 43 VAL HA H 4.89 . 1 429 . 43 VAL CB C 33.7 . 1 430 . 43 VAL HB H 2.60 . 1 431 . 43 VAL HG1 H 0.94 . 1 432 . 43 VAL HG2 H 0.74 . 1 433 . 43 VAL CG1 C 23.4 . 1 434 . 43 VAL CG2 C 18.2 . 1 435 . 44 TYR N N 121.2 . 1 436 . 44 TYR H H 8.44 . 1 437 . 44 TYR CA C 56.9 . 1 438 . 44 TYR HA H 5.50 . 1 439 . 44 TYR CB C 41.7 . 1 440 . 44 TYR HB2 H 2.52 . 2 441 . 44 TYR HB3 H 2.58 . 2 442 . 44 TYR HD1 H 6.88 . 1 443 . 44 TYR HD2 H 6.88 . 1 444 . 44 TYR HE1 H 6.74 . 1 445 . 44 TYR HE2 H 6.74 . 1 446 . 44 TYR CD1 C 132.8 . 1 447 . 44 TYR CE1 C 118.2 . 1 448 . 45 TYR N N 111.1 . 1 449 . 45 TYR H H 8.59 . 1 450 . 45 TYR CA C 55.7 . 1 451 . 45 TYR HA H 4.78 . 1 452 . 45 TYR CB C 40.3 . 1 453 . 45 TYR HB2 H 2.59 . 2 454 . 45 TYR HB3 H 2.71 . 2 455 . 45 TYR HD1 H 6.98 . 1 456 . 45 TYR HD2 H 6.98 . 1 457 . 45 TYR HE1 H 6.44 . 1 458 . 45 TYR HE2 H 6.44 . 1 459 . 45 TYR CD1 C 133.8 . 1 460 . 45 TYR CE1 C 117.3 . 1 461 . 46 ARG N N 121.0 . 1 462 . 46 ARG H H 8.01 . 1 463 . 46 ARG CA C 52.9 . 1 464 . 46 ARG HA H 4.60 . 1 465 . 46 ARG CB C 30.0 . 1 466 . 46 ARG HB2 H 1.61 . 1 467 . 46 ARG HB3 H 1.61 . 1 468 . 46 ARG CG C 27.3 . 1 469 . 46 ARG HG2 H 1.13 . 1 470 . 46 ARG HG3 H 1.13 . 1 471 . 46 ARG CD C 43.2 . 1 472 . 46 ARG HD2 H 2.83 . 1 473 . 46 ARG HD3 H 2.83 . 1 474 . 46 ARG NE N 85.0 . 1 475 . 46 ARG HE H 6.90 . 1 476 . 47 PRO CD C 50.3 . 1 477 . 47 PRO CA C 63.2 . 1 478 . 47 PRO HA H 4.49 . 1 479 . 47 PRO CB C 32.2 . 1 480 . 47 PRO HB2 H 2.45 . 1 481 . 47 PRO HB3 H 1.92 . 1 482 . 47 PRO CG C 27.9 . 1 483 . 47 PRO HG2 H 2.09 . 2 484 . 47 PRO HG3 H 1.92 . 2 485 . 47 PRO HD2 H 3.50 . 2 486 . 47 PRO HD3 H 3.62 . 2 487 . 48 MET N N 120.3 . 1 488 . 48 MET H H 8.83 . 1 489 . 48 MET CA C 57.5 . 1 490 . 48 MET HA H 4.45 . 1 491 . 48 MET CB C 32.0 . 1 492 . 48 MET HB2 H 2.35 . 1 493 . 48 MET HB3 H 2.35 . 1 494 . 48 MET CG C 32.7 . 1 495 . 48 MET HG2 H 1.83 . 2 496 . 48 MET HG3 H 1.77 . 2 497 . 48 MET HE H 1.65 . 1 498 . 48 MET CE C 16.9 . 1 499 . 49 ASP N N 118.5 . 1 500 . 49 ASP H H 8.44 . 1 501 . 49 ASP CA C 54.0 . 1 502 . 49 ASP HA H 4.53 . 1 503 . 49 ASP CB C 39.6 . 1 504 . 49 ASP HB2 H 3.01 . 2 505 . 49 ASP HB3 H 2.76 . 2 506 . 50 GLU N N 117.1 . 1 507 . 50 GLU H H 8.35 . 1 508 . 50 GLU CA C 54.9 . 1 509 . 50 GLU HA H 4.66 . 1 510 . 50 GLU CB C 29.0 . 1 511 . 50 GLU HB2 H 3.16 . 2 512 . 50 GLU HB3 H 3.04 . 2 513 . 51 TYR HA H 4.36 . 1 514 . 51 TYR HD1 H 7.17 . 1 515 . 51 TYR HD2 H 7.17 . 1 516 . 51 TYR HE1 H 6.86 . 1 517 . 51 TYR HE2 H 6.86 . 1 518 . 51 TYR CD1 C 133.2 . 1 519 . 51 TYR CE1 C 118.5 . 1 520 . 52 SER CA C 58.7 . 1 521 . 52 SER HA H 4.58 . 1 522 . 52 SER CB C 64.1 . 1 523 . 52 SER HB2 H 3.97 . 2 524 . 52 SER HB3 H 3.94 . 2 525 . 53 ASN CA C 52.1 . 1 526 . 53 ASN HA H 4.75 . 1 527 . 53 ASN CB C 39.6 . 1 528 . 53 ASN HB2 H 3.11 . 2 529 . 53 ASN HB3 H 3.02 . 2 530 . 53 ASN ND2 N 113.2 . 1 531 . 53 ASN HD21 H 7.55 . 1 532 . 53 ASN HD22 H 6.70 . 1 533 . 54 GLN N N 120.2 . 1 534 . 54 GLN H H 8.66 . 1 535 . 54 GLN CA C 59.2 . 1 536 . 54 GLN HA H 2.89 . 1 537 . 54 GLN CB C 28.9 . 1 538 . 54 GLN HB2 H 1.60 . 2 539 . 54 GLN HB3 H 1.57 . 2 540 . 54 GLN CG C 33.2 . 1 541 . 54 GLN HG2 H 1.45 . 2 542 . 54 GLN HG3 H 1.13 . 2 543 . 54 GLN NE2 N 111.8 . 1 544 . 54 GLN HE21 H 7.46 . 1 545 . 54 GLN HE22 H 6.78 . 1 546 . 55 ASN N N 116.8 . 1 547 . 55 ASN H H 8.37 . 1 548 . 55 ASN CA C 56.3 . 1 549 . 55 ASN HA H 4.22 . 1 550 . 55 ASN CB C 37.7 . 1 551 . 55 ASN HB2 H 2.64 . 1 552 . 55 ASN HB3 H 2.73 . 1 553 . 55 ASN ND2 N 112.9 . 1 554 . 55 ASN HD21 H 7.58 . 1 555 . 55 ASN HD22 H 6.94 . 1 556 . 56 ASN N N 118.5 . 1 557 . 56 ASN H H 8.65 . 1 558 . 56 ASN CA C 55.7 . 1 559 . 56 ASN HA H 4.54 . 1 560 . 56 ASN CB C 37.6 . 1 561 . 56 ASN HB2 H 2.90 . 2 562 . 56 ASN HB3 H 3.04 . 2 563 . 56 ASN ND2 N 112.2 . 1 564 . 56 ASN HD21 H 7.47 . 1 565 . 56 ASN HD22 H 6.82 . 1 566 . 57 PHE HD1 H 7.66 . 1 567 . 57 PHE HD2 H 7.66 . 1 568 . 57 PHE HE1 H 6.70 . 1 569 . 57 PHE HE2 H 6.70 . 1 570 . 57 PHE CD1 C 131.5 . 1 571 . 57 PHE CE1 C 129.2 . 1 572 . 58 VAL N N 120.2 . 1 573 . 58 VAL H H 8.95 . 1 574 . 58 VAL CA C 67.6 . 1 575 . 58 VAL HA H 3.50 . 1 576 . 58 VAL CB C 31.8 . 1 577 . 58 VAL HB H 2.21 . 1 578 . 58 VAL HG1 H 1.02 . 1 579 . 58 VAL HG2 H 1.06 . 1 580 . 58 VAL CG1 C 21.6 . 1 581 . 58 VAL CG2 C 24.5 . 1 582 . 59 HIS N N 116.7 . 1 583 . 59 HIS H H 8.35 . 1 584 . 59 HIS CA C 59.2 . 1 585 . 59 HIS HA H 4.29 . 1 586 . 59 HIS CB C 28.0 . 1 587 . 59 HIS HB2 H 3.32 . 2 588 . 59 HIS HB3 H 3.37 . 2 589 . 59 HIS CD2 C 119.9 . 1 590 . 59 HIS CE1 C 136.0 . 1 591 . 59 HIS HD2 H 7.38 . 1 592 . 59 HIS HE1 H 8.63 . 1 593 . 60 ASP N N 118.5 . 1 594 . 60 ASP H H 7.73 . 1 595 . 60 ASP CA C 57.0 . 1 596 . 60 ASP HA H 4.53 . 1 597 . 60 ASP CB C 40.8 . 1 598 . 60 ASP HB2 H 2.96 . 2 599 . 60 ASP HB3 H 2.87 . 2 600 . 61 CYS N N 119.2 . 1 601 . 61 CYS H H 8.06 . 1 602 . 61 CYS CA C 58.5 . 1 603 . 61 CYS HA H 4.72 . 1 604 . 61 CYS CB C 40.2 . 1 605 . 61 CYS HB2 H 2.97 . 1 606 . 61 CYS HB3 H 3.34 . 1 607 . 62 VAL N N 124.9 . 1 608 . 62 VAL H H 9.13 . 1 609 . 62 VAL CA C 66.2 . 1 610 . 62 VAL HA H 3.61 . 1 611 . 62 VAL CB C 31.7 . 1 612 . 62 VAL HB H 2.15 . 1 613 . 62 VAL HG1 H 0.94 . 1 614 . 62 VAL HG2 H 1.07 . 1 615 . 62 VAL CG1 C 21.6 . 1 616 . 62 VAL CG2 C 23.4 . 1 617 . 63 ASN N N 116.3 . 1 618 . 63 ASN H H 7.65 . 1 619 . 63 ASN CA C 56.4 . 1 620 . 63 ASN HA H 4.29 . 1 621 . 63 ASN CB C 38.4 . 1 622 . 63 ASN HB2 H 2.84 . 1 623 . 63 ASN HB3 H 2.77 . 1 624 . 63 ASN ND2 N 112.0 . 1 625 . 63 ASN HD21 H 7.64 . 1 626 . 63 ASN HD22 H 6.77 . 1 627 . 64 ILE N N 118.5 . 1 628 . 64 ILE H H 8.67 . 1 629 . 64 ILE CA C 62.0 . 1 630 . 64 ILE HA H 3.74 . 1 631 . 64 ILE CB C 36.5 . 1 632 . 64 ILE HB H 1.52 . 1 633 . 64 ILE HG2 H 0.24 . 1 634 . 64 ILE CG2 C 18.3 . 1 635 . 64 ILE CG1 C 27.3 . 1 636 . 64 ILE HG12 H 0.81 . 2 637 . 64 ILE HG13 H 0.77 . 2 638 . 64 ILE HD1 H 0.38 . 1 639 . 64 ILE CD1 C 11.3 . 1 640 . 65 THR N N 118.3 . 1 641 . 65 THR H H 8.15 . 1 642 . 65 THR CA C 68.7 . 1 643 . 65 THR HA H 4.04 . 1 644 . 65 THR CB C 68.0 . 1 645 . 65 THR HB H 4.47 . 1 646 . 65 THR HG2 H 1.47 . 1 647 . 65 THR HG1 H 6.31 . 1 648 . 65 THR CG2 C 22.0 . 1 649 . 66 ILE N N 120.8 . 1 650 . 66 ILE H H 8.51 . 1 651 . 66 ILE CA C 65.3 . 1 652 . 66 ILE HA H 3.70 . 1 653 . 66 ILE CB C 36.4 . 1 654 . 66 ILE HB H 2.09 . 1 655 . 66 ILE HG2 H 0.86 . 1 656 . 66 ILE CG2 C 16.6 . 1 657 . 66 ILE CG1 C 29.4 . 1 658 . 66 ILE HG12 H 1.77 . 2 659 . 66 ILE HG13 H 1.26 . 2 660 . 66 ILE HD1 H 0.75 . 1 661 . 66 ILE CD1 C 12.4 . 1 662 . 67 LYS N N 122.8 . 1 663 . 67 LYS H H 8.01 . 1 664 . 67 LYS CA C 59.8 . 1 665 . 67 LYS HA H 4.04 . 1 666 . 67 LYS CB C 32.0 . 1 667 . 67 LYS HB2 H 1.86 . 2 668 . 67 LYS HB3 H 1.92 . 2 669 . 67 LYS CG C 24.8 . 1 670 . 67 LYS HG2 H 1.46 . 2 671 . 67 LYS HG3 H 1.36 . 2 672 . 67 LYS CD C 29.0 . 1 673 . 67 LYS HD2 H 1.58 . 1 674 . 67 LYS HD3 H 1.58 . 1 675 . 67 LYS CE C 41.5 . 1 676 . 67 LYS HE2 H 2.88 . 1 677 . 67 LYS HE3 H 2.88 . 1 678 . 68 GLN N N 116.3 . 1 679 . 68 GLN H H 8.33 . 1 680 . 68 GLN CA C 57.4 . 1 681 . 68 GLN HA H 4.01 . 1 682 . 68 GLN CB C 27.9 . 1 683 . 68 GLN HB2 H 1.85 . 2 684 . 68 GLN HB3 H 1.96 . 2 685 . 68 GLN CG C 33.1 . 1 686 . 68 GLN HG2 H 2.08 . 2 687 . 68 GLN HG3 H 1.53 . 2 688 . 68 GLN NE2 N 110.1 . 1 689 . 68 GLN HE21 H 6.73 . 1 690 . 68 GLN HE22 H 6.69 . 1 691 . 69 HIS N N 118.0 . 1 692 . 69 HIS H H 8.10 . 1 693 . 69 HIS CA C 58.1 . 1 694 . 69 HIS HA H 4.58 . 1 695 . 69 HIS CB C 29.7 . 1 696 . 69 HIS HB2 H 3.31 . 2 697 . 69 HIS HB3 H 3.29 . 2 698 . 69 HIS CD2 C 118.8 . 1 699 . 69 HIS HD2 H 7.29 . 1 700 . 70 THR N N 113.7 . 1 701 . 70 THR H H 8.19 . 1 702 . 70 THR CA C 64.4 . 1 703 . 70 THR HA H 4.22 . 1 704 . 70 THR CB C 69.1 . 1 705 . 70 THR HB H 4.38 . 1 706 . 70 THR HG2 H 1.21 . 1 707 . 70 THR CG2 C 21.2 . 1 708 . 71 VAL N N 122.1 . 1 709 . 71 VAL H H 7.97 . 1 710 . 71 VAL CA C 64.4 . 1 711 . 71 VAL HA H 4.02 . 1 712 . 71 VAL CB C 31.9 . 1 713 . 71 VAL HB H 2.19 . 1 714 . 71 VAL HG1 H 0.93 . 1 715 . 71 VAL HG2 H 1.00 . 1 716 . 71 VAL CG1 C 20.9 . 1 717 . 71 VAL CG2 C 21.2 . 1 718 . 72 THR N N 115.0 . 1 719 . 72 THR H H 8.06 . 1 720 . 72 THR CA C 63.4 . 1 721 . 72 THR HA H 4.25 . 1 722 . 72 THR CB C 69.2 . 1 723 . 72 THR HB H 4.24 . 1 724 . 72 THR HG2 H 1.24 . 1 725 . 72 THR CG2 C 21.4 . 1 726 . 73 THR N N 114.8 . 1 727 . 73 THR H H 7.99 . 1 728 . 73 THR CA C 63.4 . 1 729 . 73 THR HA H 4.25 . 1 730 . 73 THR CB C 69.1 . 1 731 . 73 THR HB H 4.18 . 1 732 . 73 THR HG2 H 1.04 . 1 733 . 73 THR CG2 C 21.2 . 1 734 . 74 THR N N 116.4 . 1 735 . 74 THR H H 8.16 . 1 736 . 74 THR CA C 63.5 . 1 737 . 74 THR HA H 4.38 . 1 738 . 74 THR CB C 69.1 . 1 739 . 74 THR HB H 4.34 . 1 740 . 74 THR HG2 H 1.24 . 1 741 . 74 THR CG2 C 21.4 . 1 742 . 75 THR N N 116.1 . 1 743 . 75 THR H H 7.93 . 1 744 . 75 THR CA C 63.4 . 1 745 . 75 THR HA H 4.25 . 1 746 . 75 THR CB C 69.3 . 1 747 . 75 THR HB H 4.25 . 1 748 . 75 THR HG2 H 1.23 . 1 749 . 75 THR CG2 C 21.4 . 1 750 . 76 LYS N N 121.4 . 1 751 . 76 LYS H H 7.87 . 1 752 . 76 LYS CA C 56.4 . 1 753 . 76 LYS HA H 4.30 . 1 754 . 76 LYS CB C 32.3 . 1 755 . 76 LYS HB2 H 1.91 . 2 756 . 76 LYS HB3 H 1.79 . 2 757 . 76 LYS CG C 24.6 . 1 758 . 76 LYS HG2 H 1.48 . 2 759 . 76 LYS HG3 H 1.42 . 2 760 . 76 LYS CD C 28.7 . 1 761 . 76 LYS HD2 H 1.65 . 1 762 . 76 LYS HD3 H 1.65 . 1 763 . 76 LYS CE C 41.7 . 1 764 . 76 LYS HE2 H 2.95 . 1 765 . 76 LYS HE3 H 2.95 . 1 766 . 77 GLY N N 108.9 . 1 767 . 77 GLY H H 8.13 . 1 768 . 77 GLY CA C 45.3 . 1 769 . 77 GLY HA2 H 4.02 . 2 770 . 77 GLY HA3 H 3.84 . 2 771 . 78 GLU N N 120.0 . 1 772 . 78 GLU H H 7.73 . 1 773 . 78 GLU CA C 55.5 . 1 774 . 78 GLU HA H 4.24 . 1 775 . 78 GLU CB C 30.2 . 1 776 . 78 GLU HB2 H 1.68 . 1 777 . 78 GLU HB3 H 1.68 . 1 778 . 78 GLU CG C 35.1 . 1 779 . 78 GLU HG2 H 2.12 . 1 780 . 78 GLU HG3 H 2.12 . 1 781 . 79 ASN N N 119.7 . 1 782 . 79 ASN H H 8.44 . 1 783 . 79 ASN CA C 52.7 . 1 784 . 79 ASN HA H 4.63 . 1 785 . 79 ASN CB C 39.6 . 1 786 . 79 ASN HB2 H 2.69 . 2 787 . 79 ASN HB3 H 2.60 . 2 788 . 79 ASN ND2 N 112.8 . 1 789 . 79 ASN HD21 H 7.53 . 1 790 . 79 ASN HD22 H 6.82 . 1 791 . 80 PHE N N 121.9 . 1 792 . 80 PHE H H 8.65 . 1 793 . 80 PHE CA C 56.6 . 1 794 . 80 PHE HA H 5.23 . 1 795 . 80 PHE CB C 39.8 . 1 796 . 80 PHE HB2 H 3.14 . 2 797 . 80 PHE HB3 H 2.96 . 2 798 . 80 PHE HD1 H 7.34 . 1 799 . 80 PHE HD2 H 7.34 . 1 800 . 80 PHE HE1 H 7.42 . 1 801 . 80 PHE HE2 H 7.42 . 1 802 . 80 PHE CD1 C 131.4 . 1 803 . 80 PHE CE1 C 129.7 . 1 804 . 81 THR N N 116.1 . 1 805 . 81 THR H H 9.48 . 1 806 . 81 THR CA C 60.4 . 1 807 . 81 THR HA H 4.59 . 1 808 . 81 THR CB C 71.9 . 1 809 . 81 THR HB H 4.80 . 1 810 . 81 THR HG2 H 1.40 . 1 811 . 81 THR CG2 C 21.4 . 1 812 . 82 GLU N N 119.9 . 1 813 . 82 GLU H H 9.10 . 1 814 . 82 GLU CA C 59.4 . 1 815 . 82 GLU HA H 4.08 . 1 816 . 82 GLU CB C 28.3 . 1 817 . 82 GLU HB2 H 2.12 . 2 818 . 82 GLU HB3 H 2.05 . 2 819 . 82 GLU CG C 34.8 . 1 820 . 82 GLU HG2 H 2.44 . 2 821 . 82 GLU HG3 H 2.39 . 2 822 . 83 THR N N 116.2 . 1 823 . 83 THR H H 7.95 . 1 824 . 83 THR CA C 66.8 . 1 825 . 83 THR HA H 3.77 . 1 826 . 83 THR CB C 68.4 . 1 827 . 83 THR HB H 3.70 . 1 828 . 83 THR HG2 H 0.69 . 1 829 . 83 THR CG2 C 20.8 . 1 830 . 84 ASP N N 120.1 . 1 831 . 84 ASP H H 7.47 . 1 832 . 84 ASP CA C 57.8 . 1 833 . 84 ASP HA H 4.54 . 1 834 . 84 ASP CB C 41.2 . 1 835 . 84 ASP HB2 H 3.27 . 1 836 . 84 ASP HB3 H 2.50 . 1 837 . 85 VAL N N 119.6 . 1 838 . 85 VAL H H 8.21 . 1 839 . 85 VAL CA C 67.5 . 1 840 . 85 VAL HA H 3.30 . 1 841 . 85 VAL CB C 31.4 . 1 842 . 85 VAL HB H 2.10 . 1 843 . 85 VAL HG1 H 0.88 . 1 844 . 85 VAL HG2 H 0.98 . 1 845 . 85 VAL CG1 C 20.9 . 1 846 . 85 VAL CG2 C 22.7 . 1 847 . 86 LYS N N 119.1 . 1 848 . 86 LYS H H 7.73 . 1 849 . 86 LYS CA C 59.2 . 1 850 . 86 LYS HA H 4.04 . 1 851 . 86 LYS CB C 31.8 . 1 852 . 86 LYS HB2 H 1.95 . 2 853 . 86 LYS HB3 H 1.90 . 2 854 . 86 LYS CG C 25.0 . 1 855 . 86 LYS HG2 H 1.62 . 2 856 . 86 LYS HG3 H 1.43 . 2 857 . 86 LYS CD C 28.8 . 1 858 . 86 LYS HD2 H 1.66 . 1 859 . 86 LYS HD3 H 1.66 . 1 860 . 86 LYS CE C 41.6 . 1 861 . 86 LYS HE2 H 2.92 . 1 862 . 86 LYS HE3 H 2.92 . 1 863 . 87 MET N N 118.7 . 1 864 . 87 MET H H 8.21 . 1 865 . 87 MET CA C 60.0 . 1 866 . 87 MET HA H 4.12 . 1 867 . 87 MET CB C 32.5 . 1 868 . 87 MET HB2 H 2.28 . 1 869 . 87 MET HB3 H 1.93 . 1 870 . 87 MET CG C 34.0 . 1 871 . 87 MET HG2 H 2.13 . 1 872 . 87 MET HG3 H 2.91 . 1 873 . 87 MET HE H 1.44 . 1 874 . 87 MET CE C 18.0 . 1 875 . 88 MET N N 118.3 . 1 876 . 88 MET H H 8.74 . 1 877 . 88 MET CA C 59.4 . 1 878 . 88 MET HA H 3.55 . 1 879 . 88 MET CB C 33.1 . 1 880 . 88 MET HB2 H 1.88 . 2 881 . 88 MET HB3 H 1.70 . 2 882 . 88 MET CG C 32.4 . 1 883 . 88 MET HG2 H 1.73 . 1 884 . 88 MET HG3 H 1.93 . 1 885 . 88 MET HE H 1.42 . 1 886 . 88 MET CE C 15.9 . 1 887 . 89 GLU N N 118.2 . 1 888 . 89 GLU H H 8.38 . 1 889 . 89 GLU CA C 60.3 . 1 890 . 89 GLU HA H 3.66 . 1 891 . 89 GLU CB C 27.7 . 1 892 . 89 GLU HB2 H 2.07 . 1 893 . 89 GLU HB3 H 2.21 . 1 894 . 89 GLU CG C 34.4 . 1 895 . 89 GLU HG2 H 2.25 . 2 896 . 89 GLU HG3 H 2.57 . 2 897 . 90 ARG N N 116.9 . 1 898 . 90 ARG H H 7.30 . 1 899 . 90 ARG CA C 58.2 . 1 900 . 90 ARG HA H 4.17 . 1 901 . 90 ARG CB C 29.7 . 1 902 . 90 ARG HB2 H 1.94 . 2 903 . 90 ARG HB3 H 2.09 . 2 904 . 90 ARG CG C 26.7 . 1 905 . 90 ARG HG2 H 1.82 . 2 906 . 90 ARG HG3 H 1.74 . 2 907 . 90 ARG CD C 42.3 . 1 908 . 90 ARG HD2 H 3.24 . 2 909 . 90 ARG HD3 H 3.13 . 2 910 . 90 ARG NE N 83.1 . 1 911 . 90 ARG HE H 7.26 . 1 912 . 91 VAL N N 119.1 . 1 913 . 91 VAL H H 8.26 . 1 914 . 91 VAL CA C 65.9 . 1 915 . 91 VAL HA H 3.78 . 1 916 . 91 VAL CB C 31.9 . 1 917 . 91 VAL HB H 2.33 . 1 918 . 91 VAL HG1 H 1.26 . 1 919 . 91 VAL HG2 H 1.31 . 1 920 . 91 VAL CG1 C 20.8 . 1 921 . 91 VAL CG2 C 24.0 . 1 922 . 92 VAL N N 121.3 . 1 923 . 92 VAL H H 9.02 . 1 924 . 92 VAL CA C 66.6 . 1 925 . 92 VAL HA H 3.62 . 1 926 . 92 VAL CB C 31.0 . 1 927 . 92 VAL HB H 2.26 . 1 928 . 92 VAL HG1 H 1.20 . 1 929 . 92 VAL HG2 H 0.94 . 1 930 . 92 VAL CG1 C 24.4 . 1 931 . 92 VAL CG2 C 24.1 . 1 932 . 93 GLU N N 120.4 . 1 933 . 93 GLU H H 8.05 . 1 934 . 93 GLU CA C 60.8 . 1 935 . 93 GLU HA H 3.60 . 1 936 . 93 GLU CB C 28.5 . 1 937 . 93 GLU HB2 H 2.15 . 2 938 . 93 GLU HB3 H 2.22 . 2 939 . 93 GLU CG C 35.1 . 1 940 . 93 GLU HG2 H 2.18 . 1 941 . 93 GLU HG3 H 2.18 . 1 942 . 94 GLN N N 114.8 . 1 943 . 94 GLN H H 7.18 . 1 944 . 94 GLN CA C 58.8 . 1 945 . 94 GLN HA H 3.97 . 1 946 . 94 GLN CB C 27.7 . 1 947 . 94 GLN HB2 H 2.12 . 2 948 . 94 GLN HB3 H 2.19 . 2 949 . 94 GLN CG C 33.5 . 1 950 . 94 GLN HG2 H 2.44 . 2 951 . 94 GLN HG3 H 2.41 . 2 952 . 94 GLN NE2 N 113.2 . 1 953 . 94 GLN HE21 H 7.53 . 1 954 . 94 GLN HE22 H 6.88 . 1 955 . 95 MET N N 119.1 . 1 956 . 95 MET H H 8.27 . 1 957 . 95 MET CA C 59.7 . 1 958 . 95 MET HA H 4.16 . 1 959 . 95 MET CB C 34.4 . 1 960 . 95 MET HB2 H 2.12 . 1 961 . 95 MET HB3 H 2.12 . 1 962 . 95 MET CG C 32.2 . 1 963 . 95 MET HG2 H 2.46 . 1 964 . 95 MET HG3 H 2.83 . 1 965 . 95 MET HE H 1.88 . 1 966 . 95 MET CE C 16.3 . 1 967 . 96 CYS N N 119.3 . 1 968 . 96 CYS H H 9.19 . 1 969 . 96 CYS CA C 59.8 . 1 970 . 96 CYS HA H 4.42 . 1 971 . 96 CYS CB C 41.6 . 1 972 . 96 CYS HB2 H 3.51 . 1 973 . 96 CYS HB3 H 2.87 . 1 974 . 97 ILE N N 123.8 . 1 975 . 97 ILE H H 8.22 . 1 976 . 97 ILE CA C 66.5 . 1 977 . 97 ILE HA H 3.56 . 1 978 . 97 ILE CB C 37.8 . 1 979 . 97 ILE HB H 2.01 . 1 980 . 97 ILE HG2 H 0.87 . 1 981 . 97 ILE CG2 C 16.9 . 1 982 . 97 ILE CG1 C 30.6 . 1 983 . 97 ILE HG12 H 1.96 . 2 984 . 97 ILE HG13 H 0.83 . 2 985 . 97 ILE HD1 H 0.83 . 1 986 . 97 ILE CD1 C 13.7 . 1 987 . 98 THR N N 118.6 . 1 988 . 98 THR H H 8.10 . 1 989 . 98 THR CA C 66.9 . 1 990 . 98 THR HA H 3.89 . 1 991 . 98 THR CB C 68.0 . 1 992 . 98 THR HB H 4.31 . 1 993 . 98 THR HG2 H 1.21 . 1 994 . 98 THR CG2 C 21.9 . 1 995 . 99 GLN N N 122.2 . 1 996 . 99 GLN H H 8.76 . 1 997 . 99 GLN CA C 58.5 . 1 998 . 99 GLN HA H 3.61 . 1 999 . 99 GLN CB C 27.9 . 1 1000 . 99 GLN HB2 H 2.29 . 2 1001 . 99 GLN HB3 H 2.12 . 2 1002 . 99 GLN CG C 32.7 . 1 1003 . 99 GLN HG2 H 1.75 . 2 1004 . 99 GLN HG3 H 1.64 . 2 1005 . 99 GLN NE2 N 115.7 . 1 1006 . 99 GLN HE21 H 7.33 . 1 1007 . 99 GLN HE22 H 6.74 . 1 1008 . 100 TYR N N 121.3 . 1 1009 . 100 TYR H H 8.54 . 1 1010 . 100 TYR CA C 61.9 . 1 1011 . 100 TYR HA H 2.92 . 1 1012 . 100 TYR CB C 36.9 . 1 1013 . 100 TYR HB2 H 3.09 . 2 1014 . 100 TYR HB3 H 2.70 . 2 1015 . 100 TYR HD1 H 6.20 . 1 1016 . 100 TYR HD2 H 6.20 . 1 1017 . 100 TYR HE1 H 6.54 . 1 1018 . 100 TYR HE2 H 6.54 . 1 1019 . 100 TYR CD1 C 132.4 . 1 1020 . 100 TYR CE1 C 117.6 . 1 1021 . 101 GLU N N 120.5 . 1 1022 . 101 GLU H H 8.25 . 1 1023 . 101 GLU CA C 58.9 . 1 1024 . 101 GLU HA H 3.73 . 1 1025 . 101 GLU CB C 27.4 . 1 1026 . 101 GLU HB2 H 2.35 . 2 1027 . 101 GLU HB3 H 2.06 . 2 1028 . 101 GLU CG C 33.8 . 1 1029 . 101 GLU HG2 H 2.67 . 2 1030 . 101 GLU HG3 H 2.47 . 2 1031 . 102 ARG N N 119.3 . 1 1032 . 102 ARG H H 7.95 . 1 1033 . 102 ARG CA C 58.8 . 1 1034 . 102 ARG HA H 3.95 . 1 1035 . 102 ARG CB C 30.1 . 1 1036 . 102 ARG HB2 H 1.79 . 2 1037 . 102 ARG HB3 H 1.93 . 2 1038 . 102 ARG CG C 26.6 . 1 1039 . 102 ARG HG2 H 1.58 . 1 1040 . 102 ARG HG3 H 1.81 . 1 1041 . 102 ARG CD C 43.9 . 1 1042 . 102 ARG HD2 H 2.88 . 1 1043 . 102 ARG HD3 H 3.04 . 1 1044 . 102 ARG NE N 84.2 . 1 1045 . 102 ARG HE H 7.23 . 1 1046 . 103 GLU N N 118.7 . 1 1047 . 103 GLU H H 8.32 . 1 1048 . 103 GLU CA C 57.4 . 1 1049 . 103 GLU HA H 4.00 . 1 1050 . 103 GLU CB C 28.8 . 1 1051 . 103 GLU HB2 H 1.68 . 1 1052 . 103 GLU HB3 H 1.68 . 1 1053 . 103 GLU CG C 35.1 . 1 1054 . 103 GLU HG2 H 2.18 . 2 1055 . 103 GLU HG3 H 2.41 . 2 1056 . 104 SER N N 115.7 . 1 1057 . 104 SER H H 8.38 . 1 1058 . 104 SER CA C 60.7 . 1 1059 . 104 SER HA H 3.92 . 1 1060 . 104 SER CB C 62.5 . 1 1061 . 104 SER HB2 H 3.60 . 2 1062 . 104 SER HB3 H 3.39 . 2 1063 . 105 GLN N N 120.3 . 1 1064 . 105 GLN H H 7.60 . 1 1065 . 105 GLN CA C 57.7 . 1 1066 . 105 GLN HA H 4.11 . 1 1067 . 105 GLN CB C 28.1 . 1 1068 . 105 GLN HB2 H 2.07 . 1 1069 . 105 GLN HB3 H 2.07 . 1 1070 . 105 GLN CG C 33.6 . 1 1071 . 105 GLN HG2 H 2.46 . 2 1072 . 105 GLN HG3 H 2.36 . 2 1073 . 105 GLN NE2 N 111.8 . 1 1074 . 105 GLN HE21 H 7.45 . 1 1075 . 105 GLN HE22 H 6.79 . 1 1076 . 106 ALA N N 120.7 . 1 1077 . 106 ALA H H 7.50 . 1 1078 . 106 ALA CA C 53.6 . 1 1079 . 106 ALA HA H 4.16 . 1 1080 . 106 ALA HB H 1.37 . 1 1081 . 106 ALA CB C 18.3 . 1 1082 . 107 TYR N N 119.1 . 1 1083 . 107 TYR H H 8.01 . 1 1084 . 107 TYR CA C 59.8 . 1 1085 . 107 TYR HA H 4.20 . 1 1086 . 107 TYR CB C 38.8 . 1 1087 . 107 TYR HB2 H 2.99 . 1 1088 . 107 TYR HB3 H 2.80 . 1 1089 . 107 TYR HD1 H 6.69 . 1 1090 . 107 TYR HD2 H 6.69 . 1 1091 . 107 TYR HE1 H 6.72 . 1 1092 . 107 TYR HE2 H 6.72 . 1 1093 . 107 TYR CD1 C 132.9 . 1 1094 . 107 TYR CE1 C 117.7 . 1 1095 . 108 TYR N N 118.2 . 1 1096 . 108 TYR H H 7.93 . 1 1097 . 108 TYR CA C 58.7 . 1 1098 . 108 TYR HA H 4.36 . 1 1099 . 108 TYR CB C 38.0 . 1 1100 . 108 TYR HB2 H 3.11 . 2 1101 . 108 TYR HB3 H 2.91 . 2 1102 . 108 TYR HD1 H 7.17 . 1 1103 . 108 TYR HD2 H 7.17 . 1 1104 . 108 TYR HE1 H 6.83 . 1 1105 . 108 TYR HE2 H 6.83 . 1 1106 . 108 TYR CD1 C 133.1 . 1 1107 . 108 TYR CE1 C 117.9 . 1 1108 . 109 GLN N N 119.6 . 1 1109 . 109 GLN H H 7.86 . 1 1110 . 109 GLN CA C 55.9 . 1 1111 . 109 GLN HA H 4.21 . 1 1112 . 109 GLN CB C 28.6 . 1 1113 . 109 GLN HB2 H 2.01 . 1 1114 . 109 GLN HB3 H 2.10 . 1 1115 . 109 GLN CG C 33.6 . 1 1116 . 109 GLN HG2 H 2.33 . 1 1117 . 109 GLN HG3 H 2.33 . 1 1118 . 109 GLN NE2 N 111.8 . 1 1119 . 109 GLN HE21 H 7.46 . 1 1120 . 109 GLN HE22 H 6.81 . 1 1121 . 110 ARG N N 120.8 . 1 1122 . 110 ARG H H 7.95 . 1 1123 . 110 ARG CA C 56.5 . 1 1124 . 110 ARG HA H 4.26 . 1 1125 . 110 ARG CB C 30.5 . 1 1126 . 110 ARG HB2 H 1.79 . 2 1127 . 110 ARG HB3 H 1.84 . 2 1128 . 110 ARG CG C 26.8 . 1 1129 . 110 ARG HG2 H 1.65 . 2 1130 . 110 ARG HG3 H 1.62 . 2 1131 . 110 ARG CD C 43.1 . 1 1132 . 110 ARG HD2 H 3.13 . 1 1133 . 110 ARG HD3 H 3.13 . 1 1134 . 110 ARG NE N 84.5 . 1 1135 . 110 ARG HE H 7.14 . 1 1136 . 111 GLY N N 109.4 . 1 1137 . 111 GLY H H 8.28 . 1 1138 . 111 GLY CA C 45.0 . 1 1139 . 111 GLY HA2 H 3.95 . 1 1140 . 111 GLY HA3 H 3.95 . 1 1141 . 112 SER N N 120.7 . 1 1142 . 112 SER H H 7.84 . 1 1143 . 112 SER CA C 58.3 . 1 1144 . 112 SER HA H 4.50 . 1 1145 . 112 SER CB C 63.5 . 1 1146 . 112 SER HB2 H 3.88 . 1 1147 . 112 SER HB3 H 3.88 . 1 stop_ save_