data_16964 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solid-state NMR assignment of the globular domain of HET-s(1-227) prion protein in microcrystalline form. ; _BMRB_accession_number 16964 _BMRB_flat_file_name bmr16964.str _Entry_type original _Submission_date 2010-05-29 _Accession_date 2010-05-29 _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 Schuetz Anne . . 2 Wasmer Christian . . 3 Habenstein Birgit . . 4 Verel Rene . . 5 Greenwald Jason . . 6 Riek Roland . . 7 Bockmann Anja . . 8 Meier Beat H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 817 "15N chemical shifts" 205 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-19 update BMRB 'complete entry citation' 2010-06-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16965 'HET-s(1-227) solid state' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20572250 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schuetz Anne . . 2 Wasmer Christian . . 3 Habenstein Birgit . . 4 Verel Rene . . 5 Greenwald Jason . . 6 Riek Roland . . 7 Bockmann Anja . . 8 Meier Beat H. . stop_ _Journal_abbreviation Chembiochem _Journal_name_full 'Chembiochem : a European journal of chemical biology' _Journal_volume 11 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1543 _Page_last 1551 _Year 2010 _Details . loop_ _Keyword 'prion proteins' 'sequence determination' 'solid-state NMR' spectroscopy 'structure determination' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HET-s(1-227) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HET-s(1-227) $HET-s stop_ _System_molecular_weight 25470 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 HET-s(1-227) stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HET-s _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HET-s _Molecular_mass 25470 _Mol_thiol_state 'all free' loop_ _Biological_function 'heterokaryon incompatibility' 'prion protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 229 _Mol_residue_sequence ; GSMSEPFGIVAGALNVAGLF NNCVDCFEYVQLGRPFGRDY ERCQLRLDIAKARLSRWGEA VKINDDPRFHSSAPTDKSVQ LAKSIVEEILLLFESAQKTS KRYELVADQQDLVVFEDKDM KPIGRALHRRLNDLVSRRQK QTSLAKKTAWALYDGKSLEK IVDQVARFVDELEKAFPIEA VCHKLAEIEIEEVEDEASLT ILKDAAGGIDAAMSDAAAQK IDAIVGRNS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 MET 4 2 SER 5 3 GLU 6 4 PRO 7 5 PHE 8 6 GLY 9 7 ILE 10 8 VAL 11 9 ALA 12 10 GLY 13 11 ALA 14 12 LEU 15 13 ASN 16 14 VAL 17 15 ALA 18 16 GLY 19 17 LEU 20 18 PHE 21 19 ASN 22 20 ASN 23 21 CYS 24 22 VAL 25 23 ASP 26 24 CYS 27 25 PHE 28 26 GLU 29 27 TYR 30 28 VAL 31 29 GLN 32 30 LEU 33 31 GLY 34 32 ARG 35 33 PRO 36 34 PHE 37 35 GLY 38 36 ARG 39 37 ASP 40 38 TYR 41 39 GLU 42 40 ARG 43 41 CYS 44 42 GLN 45 43 LEU 46 44 ARG 47 45 LEU 48 46 ASP 49 47 ILE 50 48 ALA 51 49 LYS 52 50 ALA 53 51 ARG 54 52 LEU 55 53 SER 56 54 ARG 57 55 TRP 58 56 GLY 59 57 GLU 60 58 ALA 61 59 VAL 62 60 LYS 63 61 ILE 64 62 ASN 65 63 ASP 66 64 ASP 67 65 PRO 68 66 ARG 69 67 PHE 70 68 HIS 71 69 SER 72 70 SER 73 71 ALA 74 72 PRO 75 73 THR 76 74 ASP 77 75 LYS 78 76 SER 79 77 VAL 80 78 GLN 81 79 LEU 82 80 ALA 83 81 LYS 84 82 SER 85 83 ILE 86 84 VAL 87 85 GLU 88 86 GLU 89 87 ILE 90 88 LEU 91 89 LEU 92 90 LEU 93 91 PHE 94 92 GLU 95 93 SER 96 94 ALA 97 95 GLN 98 96 LYS 99 97 THR 100 98 SER 101 99 LYS 102 100 ARG 103 101 TYR 104 102 GLU 105 103 LEU 106 104 VAL 107 105 ALA 108 106 ASP 109 107 GLN 110 108 GLN 111 109 ASP 112 110 LEU 113 111 VAL 114 112 VAL 115 113 PHE 116 114 GLU 117 115 ASP 118 116 LYS 119 117 ASP 120 118 MET 121 119 LYS 122 120 PRO 123 121 ILE 124 122 GLY 125 123 ARG 126 124 ALA 127 125 LEU 128 126 HIS 129 127 ARG 130 128 ARG 131 129 LEU 132 130 ASN 133 131 ASP 134 132 LEU 135 133 VAL 136 134 SER 137 135 ARG 138 136 ARG 139 137 GLN 140 138 LYS 141 139 GLN 142 140 THR 143 141 SER 144 142 LEU 145 143 ALA 146 144 LYS 147 145 LYS 148 146 THR 149 147 ALA 150 148 TRP 151 149 ALA 152 150 LEU 153 151 TYR 154 152 ASP 155 153 GLY 156 154 LYS 157 155 SER 158 156 LEU 159 157 GLU 160 158 LYS 161 159 ILE 162 160 VAL 163 161 ASP 164 162 GLN 165 163 VAL 166 164 ALA 167 165 ARG 168 166 PHE 169 167 VAL 170 168 ASP 171 169 GLU 172 170 LEU 173 171 GLU 174 172 LYS 175 173 ALA 176 174 PHE 177 175 PRO 178 176 ILE 179 177 GLU 180 178 ALA 181 179 VAL 182 180 CYS 183 181 HIS 184 182 LYS 185 183 LEU 186 184 ALA 187 185 GLU 188 186 ILE 189 187 GLU 190 188 ILE 191 189 GLU 192 190 GLU 193 191 VAL 194 192 GLU 195 193 ASP 196 194 GLU 197 195 ALA 198 196 SER 199 197 LEU 200 198 THR 201 199 ILE 202 200 LEU 203 201 LYS 204 202 ASP 205 203 ALA 206 204 ALA 207 205 GLY 208 206 GLY 209 207 ILE 210 208 ASP 211 209 ALA 212 210 ALA 213 211 MET 214 212 SER 215 213 ASP 216 214 ALA 217 215 ALA 218 216 ALA 219 217 GLN 220 218 LYS 221 219 ILE 222 220 ASP 223 221 ALA 224 222 ILE 225 223 VAL 226 224 GLY 227 225 ARG 228 226 ASN 229 227 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 16965 HET-s 100.00 229 100.00 100.00 1.71e-164 PDB 2WVN "Structure Of The Het-S N-Terminal Domain" 100.00 229 99.56 99.56 1.51e-163 GB AAB19707 "s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]" 99.13 289 99.56 99.56 1.50e-161 GB AAB94631 "small s protein [Podospora anserina]" 99.13 289 99.56 99.56 1.25e-161 PRF 1718317A "vegetative incompatibility gene s" 99.13 289 99.12 99.12 3.81e-160 SP Q03689 "RecName: Full=Heterokaryon incompatibility protein s; AltName: Full=Small s protein; AltName: Full=Vegetative incompatibility p" 99.13 289 99.56 99.56 1.25e-161 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HET-s ascomycetes 5145 Eukaryota Fungi Podospora anserina 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 $HET-s 'recombinant technology' . Escherichia coli BL21 pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HET-s 25 mg '[U-100% 13C; U-100% 15N]' DTT 0.5 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' DSS 1 mg 'natural abundance' TRIS 20 mM 'natural abundance' H2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NCACO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACO' _Sample_label $sample_1 save_ save_3D_NCOCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCA' _Sample_label $sample_1 save_ save_3D_CANCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANCO' _Sample_label $sample_1 save_ save_3D_NCACB-DREAM_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACB-DREAM' _Sample_label $sample_1 save_ save_3D_N(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D N(CO)CACB' _Sample_label $sample_1 save_ save_3D_CAN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CAN(CO)CA' _Sample_label $sample_1 save_ save_3D_CCC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCC' _Sample_label $sample_1 save_ save_3D_NCACX-DARR_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX-DARR' _Sample_label $sample_1 save_ save_3D_N(CA)CBCX_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D N(CA)CBCX' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 5 mM pH 8.5 0.2 pH pressure 1 . atm temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D NCACO' '3D NCOCA' '3D CANCO' '3D NCACB-DREAM' '3D N(CO)CACB' '3D CAN(CO)CA' '3D CCC' '3D NCACX-DARR' '3D N(CA)CBCX' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name HET-s(1-227) _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 13 15 ASN C C 174.4 0.2 1 2 13 15 ASN CA C 50.7 0.2 1 3 14 16 VAL C C 177.1 0.2 1 4 14 16 VAL CA C 68.0 0.2 1 5 14 16 VAL CB C 31.1 0.2 1 6 14 16 VAL CG1 C 21.7 0.2 2 7 14 16 VAL CG2 C 23.1 0.2 2 8 14 16 VAL N N 116.9 0.2 1 9 15 17 ALA C C 177.2 0.2 1 10 15 17 ALA CA C 55.7 0.2 1 11 15 17 ALA CB C 17.7 0.2 1 12 15 17 ALA N N 121.2 0.2 1 13 16 18 GLY CA C 47.2 0.2 1 14 16 18 GLY N N 107.1 0.2 1 15 17 19 LEU C C 178.6 0.2 1 16 17 19 LEU CA C 58.6 0.2 1 17 17 19 LEU CB C 42.9 0.2 1 18 17 19 LEU CD1 C 23.9 0.2 2 19 17 19 LEU CG C 26.4 0.2 1 20 17 19 LEU N N 126.5 0.2 1 21 18 20 PHE C C 176.6 0.2 1 22 18 20 PHE CA C 62.3 0.2 1 23 18 20 PHE CB C 39.3 0.2 1 24 18 20 PHE CG C 137.3 0.2 1 25 18 20 PHE N N 120.5 0.2 1 26 19 21 ASN CA C 56.6 0.2 1 27 19 21 ASN CB C 38.1 0.2 1 28 19 21 ASN N N 118.9 0.2 1 29 20 22 ASN C C 175.8 0.2 1 30 20 22 ASN CA C 57.9 0.2 1 31 20 22 ASN CB C 40.1 0.2 1 32 20 22 ASN N N 117.9 0.2 1 33 21 23 CYS C C 175.9 0.2 1 34 21 23 CYS CA C 63.7 0.2 1 35 21 23 CYS CB C 26.6 0.2 1 36 21 23 CYS N N 122.2 0.2 1 37 22 24 VAL C C 178.7 0.2 1 38 22 24 VAL CA C 66.8 0.2 1 39 22 24 VAL CB C 31.8 0.2 1 40 22 24 VAL CG1 C 22.9 0.2 2 41 22 24 VAL CG2 C 22.0 0.2 2 42 22 24 VAL N N 117.8 0.2 1 43 23 25 ASP C C 178.6 0.2 1 44 23 25 ASP CA C 56.5 0.2 1 45 23 25 ASP CB C 44.1 0.2 1 46 23 25 ASP N N 117.2 0.2 1 47 24 26 CYS C C 178.2 0.2 1 48 24 26 CYS CA C 65.2 0.2 1 49 24 26 CYS CB C 26.0 0.2 1 50 24 26 CYS N N 115.2 0.2 1 51 25 27 PHE C C 177.5 0.2 1 52 25 27 PHE CA C 62.1 0.2 1 53 25 27 PHE CB C 39.9 0.2 1 54 25 27 PHE CD1 C 128.6 0.2 3 55 25 27 PHE CG C 140.6 0.2 1 56 25 27 PHE N N 114.4 0.2 1 57 26 28 GLU C C 176.6 0.2 1 58 26 28 GLU CA C 56.7 0.2 1 59 26 28 GLU CB C 28.5 0.2 1 60 26 28 GLU CD C 183.3 0.2 1 61 26 28 GLU CG C 35.2 0.2 1 62 26 28 GLU N N 116.1 0.2 1 63 27 29 TYR C C 171.9 0.2 1 64 27 29 TYR CA C 58.8 0.2 1 65 27 29 TYR CB C 39.5 0.2 1 66 27 29 TYR CD1 C 132.6 0.2 3 67 27 29 TYR CE1 C 118.2 0.2 3 68 27 29 TYR CG C 131.1 0.2 1 69 27 29 TYR CZ C 157.2 0.2 1 70 27 29 TYR N N 116.3 0.2 1 71 28 30 VAL C C 175.2 0.2 1 72 28 30 VAL CA C 61.5 0.2 1 73 28 30 VAL CB C 32.0 0.2 1 74 28 30 VAL CG1 C 21.3 0.2 2 75 28 30 VAL CG2 C 21.2 0.2 2 76 28 30 VAL N N 117.9 0.2 1 77 29 31 GLN C C 173.6 0.2 1 78 29 31 GLN CA C 53.1 0.2 1 79 29 31 GLN CB C 31.1 0.2 1 80 29 31 GLN CD C 179.2 0.2 1 81 29 31 GLN CG C 33.8 0.2 1 82 29 31 GLN N N 127.9 0.2 1 83 30 32 LEU C C 175.8 0.2 1 84 30 32 LEU CA C 54.5 0.2 1 85 30 32 LEU CB C 41.0 0.2 1 86 30 32 LEU CD1 C 24.4 0.2 2 87 30 32 LEU CD2 C 25.2 0.2 2 88 30 32 LEU CG C 28.5 0.2 1 89 30 32 LEU N N 122.1 0.2 1 90 31 33 GLY C C 172.3 0.2 1 91 31 33 GLY CA C 43.6 0.2 1 92 31 33 GLY N N 107.1 0.2 1 93 32 34 ARG C C 175.1 0.2 1 94 32 34 ARG CA C 59.5 0.2 1 95 32 34 ARG CB C 29.3 0.2 1 96 32 34 ARG CD C 42.7 0.2 1 97 32 34 ARG CG C 27.1 0.2 1 98 32 34 ARG N N 120.0 0.2 1 99 33 35 PRO C C 177.7 0.2 1 100 33 35 PRO CA C 65.5 0.2 1 101 33 35 PRO CB C 31.2 0.2 1 102 33 35 PRO CD C 51.2 0.2 1 103 33 35 PRO CG C 28.6 0.2 1 104 33 35 PRO N N 136.1 0.2 1 105 34 36 PHE C C 177.9 0.2 1 106 34 36 PHE CA C 62.8 0.2 1 107 34 36 PHE CB C 39.0 0.2 1 108 34 36 PHE CD1 C 130.9 0.2 3 109 34 36 PHE CG C 140.8 0.2 1 110 34 36 PHE N N 113.6 0.2 1 111 35 37 GLY C C 175.4 0.2 1 112 35 37 GLY CA C 47.2 0.2 1 113 35 37 GLY N N 107.2 0.2 1 114 36 38 ARG C C 177.4 0.2 1 115 36 38 ARG CA C 57.4 0.2 1 116 36 38 ARG CB C 29.5 0.2 1 117 36 38 ARG CD C 43.2 0.2 1 118 36 38 ARG CG C 27.0 0.2 1 119 36 38 ARG N N 125.0 0.2 1 120 37 39 ASP C C 174.8 0.2 1 121 37 39 ASP CA C 55.1 0.2 1 122 37 39 ASP CB C 41.5 0.2 1 123 37 39 ASP CG C 180.3 0.2 1 124 37 39 ASP N N 120.3 0.2 1 125 38 40 TYR C C 174.5 0.2 1 126 38 40 TYR CA C 61.0 0.2 1 127 38 40 TYR CB C 36.7 0.2 1 128 38 40 TYR CD1 C 133.0 0.2 . 129 38 40 TYR CD2 C 133.0 0.2 . 130 38 40 TYR CE1 C 117.9 0.2 3 131 38 40 TYR CG C 128.3 0.2 1 132 38 40 TYR CZ C 158.2 0.2 1 133 38 40 TYR N N 120.5 0.2 1 134 39 41 GLU C C 176.6 0.2 1 135 39 41 GLU CA C 60.4 0.2 1 136 39 41 GLU CB C 30.5 0.2 1 137 39 41 GLU CG C 35.8 0.2 1 138 39 41 GLU N N 119.1 0.2 1 139 40 42 ARG C C 177.4 0.2 1 140 40 42 ARG CA C 59.3 0.2 1 141 40 42 ARG CB C 29.7 0.2 1 142 40 42 ARG CD C 44.0 0.2 1 143 40 42 ARG CG C 26.0 0.2 1 144 40 42 ARG CZ C 159.6 0.2 1 145 40 42 ARG N N 117.1 0.2 1 146 41 43 CYS C C 175.8 0.2 1 147 41 43 CYS CA C 65.4 0.2 1 148 41 43 CYS CB C 27.1 0.2 1 149 41 43 CYS N N 115.6 0.2 1 150 42 44 GLN CA C 57.6 0.2 1 151 42 44 GLN CB C 28.1 0.2 1 152 42 44 GLN CG C 34.1 0.2 1 153 42 44 GLN N N 119.5 0.2 1 154 43 45 LEU C C 178.9 0.2 1 155 43 45 LEU CA C 57.5 0.2 1 156 43 45 LEU CB C 40.7 0.2 1 157 43 45 LEU CD1 C 22.4 0.2 2 158 43 45 LEU CD2 C 25.9 0.2 2 159 43 45 LEU CG C 26.9 0.2 1 160 43 45 LEU N N 119.1 0.2 1 161 44 46 ARG C C 178.3 0.2 1 162 44 46 ARG CA C 60.7 0.2 1 163 44 46 ARG CB C 29.5 0.2 1 164 44 46 ARG CD C 43.8 0.2 1 165 44 46 ARG CZ C 160.7 0.2 1 166 44 46 ARG N N 118.6 0.2 1 167 45 47 LEU CA C 58.5 0.2 1 168 45 47 LEU CB C 41.9 0.2 1 169 45 47 LEU CD1 C 23.4 0.2 2 170 45 47 LEU CD2 C 23.4 0.2 2 171 45 47 LEU CG C 26.4 0.2 1 172 45 47 LEU N N 120.1 0.2 1 173 46 48 ASP C C 178.7 0.2 1 174 46 48 ASP CA C 56.6 0.2 1 175 46 48 ASP CB C 41.9 0.2 1 176 46 48 ASP N N 117.7 0.2 1 177 47 49 ILE C C 177.1 0.2 1 178 47 49 ILE CA C 64.9 0.2 1 179 47 49 ILE CB C 38.3 0.2 1 180 47 49 ILE CD1 C 14.3 0.2 1 181 47 49 ILE CG1 C 30.1 0.2 1 182 47 49 ILE CG2 C 18.1 0.2 1 183 47 49 ILE N N 122.7 0.2 1 184 48 50 ALA C C 178.2 0.2 1 185 48 50 ALA CA C 55.8 0.2 1 186 48 50 ALA CB C 17.0 0.2 1 187 48 50 ALA N N 124.1 0.2 1 188 49 51 LYS C C 178.2 0.2 1 189 49 51 LYS CA C 59.3 0.2 1 190 49 51 LYS CB C 31.6 0.2 1 191 49 51 LYS CD C 30.2 0.2 1 192 49 51 LYS CE C 40.4 0.2 1 193 49 51 LYS CG C 24.0 0.2 1 194 49 51 LYS N N 117.7 0.2 1 195 50 52 ALA C C 179.2 0.2 1 196 50 52 ALA CA C 55.2 0.2 1 197 50 52 ALA CB C 16.7 0.2 1 198 50 52 ALA N N 123.5 0.2 1 199 51 53 ARG C C 179.6 0.2 1 200 51 53 ARG CA C 61.1 0.2 1 201 51 53 ARG CB C 29.4 0.2 1 202 51 53 ARG N N 121.3 0.2 1 203 53 55 SER C C 176.8 0.2 1 204 53 55 SER CA C 61.4 0.2 1 205 53 55 SER CB C 62.9 0.2 1 206 53 55 SER N N 113.9 0.2 1 207 54 56 ARG C C 177.3 0.2 1 208 54 56 ARG CA C 59.6 0.2 1 209 54 56 ARG CB C 30.7 0.2 1 210 54 56 ARG CG C 27.3 0.2 1 211 54 56 ARG N N 126.9 0.2 1 212 55 57 TRP C C 176.6 0.2 1 213 55 57 TRP CA C 63.0 0.2 1 214 55 57 TRP CB C 26.1 0.2 1 215 55 57 TRP CD1 C 123.2 0.2 1 216 55 57 TRP CD2 C 124.7 0.2 1 217 55 57 TRP CE2 C 138.4 0.2 1 218 55 57 TRP CG C 113.8 0.2 1 219 55 57 TRP N N 120.2 0.2 1 220 56 58 GLY C C 175.1 0.2 1 221 56 58 GLY CA C 46.4 0.2 1 222 56 58 GLY N N 102.6 0.2 1 223 57 59 GLU CA C 58.2 0.2 1 224 57 59 GLU CB C 28.8 0.2 1 225 57 59 GLU N N 121.3 0.2 1 226 58 60 ALA C C 178.8 0.2 1 227 58 60 ALA CA C 55.0 0.2 1 228 58 60 ALA CB C 20.3 0.2 1 229 58 60 ALA N N 123.8 0.2 1 230 59 61 VAL C C 174.2 0.2 1 231 59 61 VAL CA C 60.4 0.2 1 232 59 61 VAL CB C 31.3 0.2 1 233 59 61 VAL CG1 C 17.6 0.2 2 234 59 61 VAL CG2 C 20.3 0.2 2 235 59 61 VAL N N 108.1 0.2 1 236 60 62 LYS C C 176.2 0.2 1 237 60 62 LYS CA C 55.9 0.2 1 238 60 62 LYS CB C 28.6 0.2 1 239 60 62 LYS CG C 24.2 0.2 1 240 60 62 LYS N N 118.1 0.2 1 241 61 63 ILE C C 174.6 0.2 1 242 61 63 ILE CA C 62.8 0.2 1 243 61 63 ILE CB C 38.2 0.2 1 244 61 63 ILE CD1 C 14.2 0.2 1 245 61 63 ILE CG1 C 28.1 0.2 1 246 61 63 ILE CG2 C 16.3 0.2 1 247 61 63 ILE N N 119.5 0.2 1 248 62 64 ASN C C 175.1 0.2 1 249 62 64 ASN CA C 55.0 0.2 1 250 62 64 ASN CB C 39.1 0.2 1 251 62 64 ASN CG C 176.7 0.2 1 252 62 64 ASN N N 114.4 0.2 1 253 63 65 ASP C C 175.3 0.2 1 254 63 65 ASP CA C 58.6 0.2 1 255 63 65 ASP CB C 40.3 0.2 1 256 63 65 ASP CG C 180.5 0.2 1 257 63 65 ASP N N 117.0 0.2 1 258 64 66 ASP C C 175.2 0.2 1 259 64 66 ASP CA C 51.5 0.2 1 260 64 66 ASP CB C 41.6 0.2 1 261 64 66 ASP CG C 179.6 0.2 1 262 64 66 ASP N N 122.8 0.2 1 263 65 67 PRO C C 179.4 0.2 1 264 65 67 PRO CA C 63.9 0.2 1 265 65 67 PRO CB C 32.2 0.2 1 266 65 67 PRO CD C 51.5 0.2 1 267 65 67 PRO CG C 27.0 0.2 1 268 65 67 PRO N N 137.6 0.2 1 269 66 68 ARG C C 178.4 0.2 1 270 66 68 ARG CA C 58.6 0.2 1 271 66 68 ARG CB C 30.7 0.2 1 272 66 68 ARG CZ C 160.0 0.2 1 273 66 68 ARG N N 120.4 0.2 1 274 67 69 PHE C C 175.5 0.2 1 275 67 69 PHE CA C 58.7 0.2 1 276 67 69 PHE CB C 39.2 0.2 1 277 67 69 PHE CD1 C 129.6 0.2 3 278 67 69 PHE CD2 C 131.2 0.2 3 279 67 69 PHE CG C 139.7 0.2 1 280 67 69 PHE N N 113.5 0.2 1 281 68 70 HIS CA C 55.3 0.2 1 282 68 70 HIS CB C 30.8 0.2 1 283 68 70 HIS CG C 131.0 0.2 1 284 68 70 HIS N N 120.4 0.2 1 285 69 71 SER C C 175.1 0.2 1 286 69 71 SER CA C 56.1 0.2 1 287 69 71 SER CB C 65.3 0.2 1 288 69 71 SER N N 112.9 0.2 1 289 70 72 SER CA C 59.0 0.2 1 290 70 72 SER CB C 63.6 0.2 1 291 70 72 SER N N 120.3 0.2 1 292 71 73 ALA CA C 49.7 0.2 1 293 71 73 ALA CB C 18.9 0.2 1 294 71 73 ALA N N 126.0 0.2 1 295 72 74 PRO C C 177.2 0.2 1 296 72 74 PRO CA C 62.7 0.2 1 297 72 74 PRO CB C 32.4 0.2 1 298 72 74 PRO CD C 49.7 0.2 1 299 72 74 PRO CG C 27.7 0.2 1 300 72 74 PRO N N 135.4 0.2 1 301 73 75 THR C C 175.1 0.2 1 302 73 75 THR CA C 61.9 0.2 1 303 73 75 THR CB C 69.4 0.2 1 304 73 75 THR N N 111.4 0.2 1 305 74 76 ASP C C 177.1 0.2 1 306 74 76 ASP CA C 54.0 0.2 1 307 74 76 ASP CB C 42.6 0.2 1 308 74 76 ASP CG C 179.1 0.2 1 309 74 76 ASP N N 124.6 0.2 1 310 75 77 LYS C C 178.3 0.2 1 311 75 77 LYS CA C 60.4 0.2 1 312 75 77 LYS CB C 32.4 0.2 1 313 75 77 LYS CD C 29.5 0.2 1 314 75 77 LYS CE C 42.5 0.2 1 315 75 77 LYS CG C 25.1 0.2 1 316 75 77 LYS N N 128.3 0.2 1 317 76 78 SER C C 175.8 0.2 1 318 76 78 SER CA C 62.4 0.2 1 319 76 78 SER CB C 61.4 0.2 1 320 76 78 SER N N 115.9 0.2 1 321 77 79 VAL C C 178.0 0.2 1 322 77 79 VAL CA C 66.6 0.2 1 323 77 79 VAL CB C 31.3 0.2 1 324 77 79 VAL CG1 C 22.1 0.2 2 325 77 79 VAL CG2 C 22.8 0.2 2 326 77 79 VAL N N 123.3 0.2 1 327 78 80 GLN CA C 60.2 0.2 1 328 78 80 GLN CB C 28.8 0.2 1 329 78 80 GLN CD C 180.1 0.2 1 330 78 80 GLN N N 119.9 0.2 1 331 79 81 LEU C C 174.6 0.2 1 332 79 81 LEU CA C 58.9 0.2 1 333 79 81 LEU CB C 41.4 0.2 1 334 79 81 LEU CD1 C 22.4 0.2 2 335 79 81 LEU CD2 C 24.3 0.2 2 336 79 81 LEU CG C 26.7 0.2 1 337 79 81 LEU N N 122.5 0.2 1 338 80 82 ALA C C 180.1 0.2 1 339 80 82 ALA CA C 55.2 0.2 1 340 80 82 ALA CB C 18.4 0.2 1 341 80 82 ALA N N 120.4 0.2 1 342 81 83 LYS C C 176.3 0.2 1 343 81 83 LYS CA C 60.0 0.2 1 344 81 83 LYS CB C 33.0 0.2 1 345 81 83 LYS CD C 29.8 0.2 1 346 81 83 LYS CE C 42.0 0.2 1 347 81 83 LYS CG C 25.2 0.2 1 348 81 83 LYS N N 117.2 0.2 1 349 82 84 SER C C 176.6 0.2 1 350 82 84 SER CA C 60.5 0.2 1 351 82 84 SER CB C 63.1 0.2 1 352 82 84 SER N N 109.9 0.2 1 353 83 85 ILE C C 177.5 0.2 1 354 83 85 ILE CA C 65.6 0.2 1 355 83 85 ILE CB C 37.2 0.2 1 356 83 85 ILE CD1 C 13.6 0.2 1 357 83 85 ILE CG1 C 29.5 0.2 1 358 83 85 ILE CG2 C 17.2 0.2 1 359 83 85 ILE N N 118.8 0.2 1 360 84 86 VAL C C 178.5 0.2 1 361 84 86 VAL CA C 66.4 0.2 1 362 84 86 VAL CB C 30.8 0.2 1 363 84 86 VAL N N 116.1 0.2 1 364 85 87 GLU C C 179.2 0.2 1 365 85 87 GLU CA C 58.2 0.2 1 366 85 87 GLU CB C 28.0 0.2 1 367 85 87 GLU CD C 183.2 0.2 1 368 85 87 GLU CG C 31.2 0.2 1 369 85 87 GLU N N 121.9 0.2 1 370 86 88 GLU C C 178.8 0.2 1 371 86 88 GLU CA C 60.7 0.2 1 372 86 88 GLU CB C 29.5 0.2 1 373 86 88 GLU N N 116.7 0.2 1 374 87 89 ILE CA C 66.2 0.2 1 375 87 89 ILE CB C 38.2 0.2 1 376 87 89 ILE CD1 C 13.4 0.2 1 377 87 89 ILE CG1 C 31.3 0.2 1 378 87 89 ILE CG2 C 17.5 0.2 1 379 87 89 ILE N N 120.8 0.2 1 380 88 90 LEU CA C 59.0 0.2 1 381 88 90 LEU CB C 40.9 0.2 1 382 88 90 LEU CD1 C 23.5 0.2 2 383 88 90 LEU CG C 26.7 0.2 1 384 88 90 LEU N N 120.5 0.2 1 385 89 91 LEU C C 178.7 0.2 1 386 89 91 LEU CA C 57.8 0.2 1 387 89 91 LEU CB C 41.7 0.2 1 388 89 91 LEU CD1 C 22.4 0.2 2 389 89 91 LEU CG C 26.8 0.2 1 390 89 91 LEU N N 119.3 0.2 1 391 90 92 LEU C C 180.2 0.2 1 392 90 92 LEU CA C 58.0 0.2 1 393 90 92 LEU CB C 41.9 0.2 1 394 90 92 LEU CD1 C 26.5 0.2 2 395 90 92 LEU CD2 C 24.4 0.2 2 396 90 92 LEU CG C 28.1 0.2 1 397 90 92 LEU N N 124.4 0.2 1 398 91 93 PHE C C 177.8 0.2 1 399 91 93 PHE CA C 62.2 0.2 1 400 91 93 PHE CB C 38.7 0.2 1 401 91 93 PHE CD1 C 130.3 0.2 3 402 91 93 PHE CG C 140.0 0.2 1 403 91 93 PHE N N 118.4 0.2 1 404 92 94 GLU C C 178.9 0.2 1 405 92 94 GLU CA C 59.8 0.2 1 406 92 94 GLU CB C 28.3 0.2 1 407 92 94 GLU CG C 34.5 0.2 1 408 92 94 GLU N N 120.5 0.2 1 409 93 95 SER C C 175.7 0.2 1 410 93 95 SER CA C 62.6 0.2 1 411 93 95 SER CB C 62.7 0.2 1 412 93 95 SER N N 115.1 0.2 1 413 94 96 ALA CA C 54.8 0.2 1 414 94 96 ALA CB C 18.9 0.2 1 415 94 96 ALA N N 123.8 0.2 1 416 95 97 GLN CA C 58.8 0.2 1 417 95 97 GLN CB C 27.7 0.2 1 418 95 97 GLN N N 119.7 0.2 1 419 96 98 LYS C C 178.9 0.2 1 420 96 98 LYS CA C 58.7 0.2 1 421 96 98 LYS CB C 29.9 0.2 1 422 96 98 LYS CD C 27.8 0.2 1 423 96 98 LYS CE C 42.9 0.2 1 424 96 98 LYS CG C 24.9 0.2 1 425 96 98 LYS N N 120.1 0.2 1 426 97 99 THR C C 177.5 0.2 1 427 97 99 THR CA C 67.5 0.2 1 428 97 99 THR CB C 69.1 0.2 1 429 97 99 THR CG2 C 22.1 0.2 1 430 97 99 THR N N 117.8 0.2 1 431 98 100 SER CA C 62.6 0.2 1 432 98 100 SER CB C 63.6 0.2 1 433 98 100 SER N N 119.0 0.2 1 434 99 101 LYS CA C 58.2 0.2 1 435 99 101 LYS CB C 31.3 0.2 1 436 99 101 LYS CD C 28.0 0.2 1 437 99 101 LYS CE C 42.0 0.2 1 438 99 101 LYS CG C 24.0 0.2 1 439 99 101 LYS N N 121.6 0.2 1 440 100 102 ARG C C 178.6 0.2 1 441 100 102 ARG CA C 59.8 0.2 1 442 100 102 ARG CB C 29.7 0.2 1 443 100 102 ARG CD C 42.6 0.2 1 444 100 102 ARG CG C 28.3 0.2 1 445 100 102 ARG N N 117.2 0.2 1 446 101 103 TYR C C 178.1 0.2 1 447 101 103 TYR CA C 61.4 0.2 1 448 101 103 TYR CB C 37.8 0.2 1 449 101 103 TYR CD1 C 133.0 0.2 3 450 101 103 TYR CE1 C 117.6 0.2 3 451 101 103 TYR CG C 129.4 0.2 1 452 101 103 TYR N N 121.1 0.2 1 453 102 104 GLU CA C 59.0 0.2 1 454 102 104 GLU CB C 29.8 0.2 1 455 102 104 GLU CD C 183.3 0.2 1 456 102 104 GLU CG C 37.6 0.2 1 457 102 104 GLU N N 117.8 0.2 1 458 103 105 LEU C C 177.9 0.2 1 459 103 105 LEU CA C 57.2 0.2 1 460 103 105 LEU CB C 43.2 0.2 1 461 103 105 LEU CD1 C 25.7 0.2 2 462 103 105 LEU CD2 C 26.8 0.2 2 463 103 105 LEU N N 116.6 0.2 1 464 104 106 VAL C C 175.7 0.2 1 465 104 106 VAL CA C 60.1 0.2 1 466 104 106 VAL CB C 32.8 0.2 1 467 104 106 VAL CG1 C 21.2 0.2 2 468 104 106 VAL CG2 C 18.1 0.2 2 469 104 106 VAL N N 107.7 0.2 1 470 105 107 ALA C C 177.7 0.2 1 471 105 107 ALA CA C 51.9 0.2 1 472 105 107 ALA CB C 20.5 0.2 1 473 105 107 ALA N N 125.3 0.2 1 474 106 108 ASP C C 177.6 0.2 1 475 106 108 ASP CA C 54.1 0.2 1 476 106 108 ASP CB C 42.1 0.2 1 477 106 108 ASP CG C 180.0 0.2 1 478 106 108 ASP N N 121.0 0.2 1 479 107 109 GLN CA C 59.0 0.2 1 480 107 109 GLN CB C 28.5 0.2 1 481 107 109 GLN N N 123.7 0.2 1 482 108 110 GLN CA C 57.6 0.2 1 483 108 110 GLN CB C 27.8 0.2 1 484 108 110 GLN N N 117.6 0.2 1 485 109 111 ASP CA C 55.5 0.2 1 486 109 111 ASP CB C 41.6 0.2 1 487 109 111 ASP CG C 180.0 0.2 1 488 109 111 ASP N N 119.8 0.2 1 489 110 112 LEU CA C 54.4 0.2 1 490 110 112 LEU CB C 40.5 0.2 1 491 110 112 LEU CD1 C 25.5 0.2 2 492 110 112 LEU CD2 C 22.9 0.2 2 493 110 112 LEU CG C 27.2 0.2 1 494 110 112 LEU N N 115.7 0.2 1 495 111 113 VAL C C 176.2 0.2 1 496 111 113 VAL CA C 62.2 0.2 1 497 111 113 VAL CB C 33.0 0.2 1 498 111 113 VAL CG1 C 21.0 0.2 2 499 111 113 VAL N N 119.1 0.2 1 500 112 114 VAL CA C 59.2 0.2 1 501 112 114 VAL CB C 33.7 0.2 1 502 112 114 VAL CG1 C 17.8 0.2 2 503 112 114 VAL CG2 C 21.3 0.2 2 504 112 114 VAL N N 118.9 0.2 1 505 113 115 PHE C C 175.1 0.2 1 506 113 115 PHE CA C 58.7 0.2 1 507 113 115 PHE CB C 39.3 0.2 1 508 113 115 PHE CD1 C 133.0 0.2 3 509 113 115 PHE CE1 C 129.0 0.2 3 510 113 115 PHE CG C 141.3 0.2 1 511 113 115 PHE CZ C 128.2 0.2 1 512 113 115 PHE N N 120.3 0.2 1 513 114 116 GLU C C 176.7 0.2 1 514 114 116 GLU CA C 54.2 0.2 1 515 114 116 GLU CB C 34.2 0.2 1 516 114 116 GLU CD C 183.9 0.2 1 517 114 116 GLU CG C 36.3 0.2 1 518 114 116 GLU N N 119.6 0.2 1 519 115 117 ASP CA C 57.5 0.2 1 520 115 117 ASP CB C 39.3 0.2 1 521 115 117 ASP N N 119.7 0.2 1 522 116 118 LYS C C 174.2 0.2 1 523 116 118 LYS CA C 57.9 0.2 1 524 116 118 LYS CB C 30.9 0.2 1 525 116 118 LYS CD C 29.0 0.2 1 526 116 118 LYS CE C 42.1 0.2 1 527 116 118 LYS CG C 27.3 0.2 1 528 116 118 LYS N N 119.9 0.2 1 529 117 119 ASP CA C 55.6 0.2 1 530 117 119 ASP CB C 41.4 0.2 1 531 117 119 ASP N N 117.8 0.2 1 532 118 120 MET CA C 56.2 0.2 1 533 118 120 MET CB C 34.9 0.2 1 534 118 120 MET N N 118.3 0.2 1 535 119 121 LYS C C 175.4 0.2 1 536 119 121 LYS CA C 55.7 0.2 1 537 119 121 LYS CB C 30.0 0.2 1 538 119 121 LYS CD C 28.6 0.2 1 539 119 121 LYS CG C 25.2 0.2 1 540 119 121 LYS N N 123.5 0.2 1 541 120 122 PRO C C 179.4 0.2 1 542 120 122 PRO CA C 66.8 0.2 1 543 120 122 PRO CB C 32.2 0.2 1 544 120 122 PRO CD C 49.7 0.2 1 545 120 122 PRO CG C 27.7 0.2 1 546 120 122 PRO N N 134.1 0.2 1 547 121 123 ILE C C 178.4 0.2 1 548 121 123 ILE CA C 64.5 0.2 1 549 121 123 ILE CB C 37.0 0.2 1 550 121 123 ILE CD1 C 13.3 0.2 1 551 121 123 ILE CG1 C 29.0 0.2 1 552 121 123 ILE CG2 C 17.3 0.2 1 553 121 123 ILE N N 117.7 0.2 1 554 122 124 GLY C C 175.1 0.2 1 555 122 124 GLY CA C 46.9 0.2 1 556 122 124 GLY N N 111.4 0.2 1 557 123 125 ARG C C 175.2 0.2 1 558 123 125 ARG CA C 59.6 0.2 1 559 123 125 ARG CB C 29.7 0.2 1 560 123 125 ARG CZ C 159.5 0.2 1 561 123 125 ARG N N 123.6 0.2 1 562 124 126 ALA CA C 54.8 0.2 1 563 124 126 ALA CB C 18.0 0.2 1 564 124 126 ALA N N 119.9 0.2 1 565 125 127 LEU CA C 57.7 0.2 1 566 125 127 LEU CB C 43.0 0.2 1 567 125 127 LEU CD1 C 24.6 0.2 2 568 125 127 LEU CD2 C 26.0 0.2 2 569 125 127 LEU CG C 27.3 0.2 1 570 125 127 LEU N N 120.2 0.2 1 571 126 128 HIS CA C 58.5 0.2 1 572 126 128 HIS CB C 29.3 0.2 1 573 126 128 HIS CD2 C 120.5 0.2 1 574 126 128 HIS CE1 C 137.4 0.2 1 575 126 128 HIS CG C 130.9 0.2 1 576 126 128 HIS N N 120.0 0.2 1 577 127 129 ARG CA C 59.3 0.2 1 578 127 129 ARG CB C 29.2 0.2 1 579 127 129 ARG N N 117.9 0.2 1 580 128 130 ARG CA C 59.3 0.2 1 581 128 130 ARG CB C 29.8 0.2 1 582 128 130 ARG CD C 42.9 0.2 1 583 128 130 ARG CG C 27.3 0.2 1 584 128 130 ARG CZ C 159.4 0.2 1 585 128 130 ARG N N 120.7 0.2 1 586 129 131 LEU CA C 57.8 0.2 1 587 129 131 LEU CB C 41.2 0.2 1 588 129 131 LEU CD1 C 22.3 0.2 2 589 129 131 LEU CD2 C 23.7 0.2 2 590 129 131 LEU CG C 29.1 0.2 1 591 129 131 LEU N N 119.5 0.2 1 592 130 132 ASN C C 178.5 0.2 1 593 130 132 ASN CA C 56.1 0.2 1 594 130 132 ASN CB C 37.5 0.2 1 595 130 132 ASN N N 117.7 0.2 1 596 131 133 ASP C C 178.2 0.2 1 597 131 133 ASP CA C 57.3 0.2 1 598 131 133 ASP CB C 40.6 0.2 1 599 131 133 ASP N N 123.1 0.2 1 600 132 134 LEU CA C 58.0 0.2 1 601 132 134 LEU CB C 41.2 0.2 1 602 132 134 LEU N N 120.5 0.2 1 603 133 135 VAL C C 178.2 0.2 1 604 133 135 VAL CA C 66.4 0.2 1 605 133 135 VAL CB C 31.4 0.2 1 606 133 135 VAL CG1 C 21.6 0.2 2 607 133 135 VAL N N 119.3 0.2 1 608 134 136 SER C C 177.3 0.2 1 609 134 136 SER CA C 61.7 0.2 1 610 134 136 SER CB C 62.5 0.2 1 611 134 136 SER N N 116.9 0.2 1 612 135 137 ARG CA C 58.5 0.2 1 613 135 137 ARG CB C 27.9 0.2 1 614 135 137 ARG CD C 43.4 0.2 1 615 135 137 ARG CG C 30.0 0.2 1 616 135 137 ARG CZ C 159.3 0.2 1 617 135 137 ARG N N 118.5 0.2 1 618 136 138 ARG CA C 57.3 0.2 1 619 136 138 ARG CB C 31.8 0.2 1 620 136 138 ARG CD C 40.9 0.2 1 621 136 138 ARG CG C 29.7 0.2 1 622 136 138 ARG N N 117.5 0.2 1 623 137 139 GLN CA C 56.0 0.2 1 624 137 139 GLN CB C 28.7 0.2 1 625 137 139 GLN N N 118.1 0.2 1 626 138 140 LYS N N 119.3 0.2 1 627 140 142 THR CA C 61.7 0.2 1 628 140 142 THR CB C 69.5 0.2 1 629 140 142 THR CG2 C 21.8 0.2 1 630 143 145 ALA C C 179.9 0.2 1 631 143 145 ALA CA C 51.5 0.2 1 632 143 145 ALA N N 122.8 0.2 1 633 144 146 LYS CA C 57.3 0.2 1 634 144 146 LYS CB C 32.1 0.2 1 635 144 146 LYS CD C 28.3 0.2 1 636 144 146 LYS CE C 39.8 0.2 1 637 144 146 LYS CG C 24.6 0.2 1 638 144 146 LYS N N 125.9 0.2 1 639 145 147 LYS CA C 55.6 0.2 1 640 145 147 LYS CB C 32.5 0.2 1 641 145 147 LYS N N 124.1 0.2 1 642 146 148 THR C C 173.8 0.2 1 643 146 148 THR CA C 60.6 0.2 1 644 146 148 THR CB C 71.1 0.2 1 645 146 148 THR CG2 C 21.7 0.2 1 646 146 148 THR N N 112.9 0.2 1 647 147 149 ALA C C 176.8 0.2 1 648 147 149 ALA CA C 52.4 0.2 1 649 147 149 ALA CB C 19.3 0.2 1 650 147 149 ALA N N 128.2 0.2 1 651 148 150 TRP C C 172.2 0.2 1 652 148 150 TRP CA C 55.4 0.2 1 653 148 150 TRP CB C 30.3 0.2 1 654 148 150 TRP CD1 C 128.3 0.2 1 655 148 150 TRP CD2 C 130.8 0.2 1 656 148 150 TRP CE2 C 137.9 0.2 1 657 148 150 TRP CG C 109.5 0.2 1 658 148 150 TRP N N 121.9 0.2 1 659 149 151 ALA C C 175.9 0.2 1 660 149 151 ALA CA C 49.6 0.2 1 661 149 151 ALA CB C 21.5 0.2 1 662 149 151 ALA N N 120.5 0.2 1 663 150 152 LEU C C 177.0 0.2 1 664 150 152 LEU CA C 53.4 0.2 1 665 150 152 LEU CB C 46.0 0.2 1 666 150 152 LEU CD1 C 26.3 0.2 2 667 150 152 LEU CD2 C 25.4 0.2 2 668 150 152 LEU CG C 26.2 0.2 1 669 150 152 LEU N N 119.3 0.2 1 670 151 153 TYR C C 173.0 0.2 1 671 151 153 TYR CA C 58.3 0.2 1 672 151 153 TYR CB C 40.2 0.2 1 673 151 153 TYR CD1 C 133.2 0.2 3 674 151 153 TYR CE1 C 118.4 0.2 3 675 151 153 TYR CZ C 157.3 0.2 1 676 151 153 TYR N N 116.8 0.2 1 677 152 154 ASP C C 175.2 0.2 1 678 152 154 ASP CA C 52.1 0.2 1 679 152 154 ASP CB C 44.8 0.2 1 680 152 154 ASP CG C 180.6 0.2 1 681 152 154 ASP N N 115.2 0.2 1 682 153 155 GLY C C 176.1 0.2 1 683 153 155 GLY CA C 47.1 0.2 1 684 153 155 GLY N N 111.5 0.2 1 685 154 156 LYS CA C 59.4 0.2 1 686 154 156 LYS CB C 31.3 0.2 1 687 154 156 LYS CE C 39.2 0.2 1 688 154 156 LYS CG C 24.9 0.2 1 689 154 156 LYS N N 123.0 0.2 1 690 155 157 SER C C 176.3 0.2 1 691 155 157 SER CA C 62.0 0.2 1 692 155 157 SER CB C 62.9 0.2 1 693 155 157 SER N N 117.9 0.2 1 694 156 158 LEU CA C 58.1 0.2 1 695 156 158 LEU CB C 41.2 0.2 1 696 156 158 LEU CD1 C 24.9 0.2 2 697 156 158 LEU CD2 C 22.8 0.2 2 698 156 158 LEU N N 122.0 0.2 1 699 157 159 GLU CA C 58.3 0.2 1 700 157 159 GLU CB C 29.4 0.2 1 701 157 159 GLU N N 120.4 0.2 1 702 158 160 LYS C C 178.6 0.2 1 703 158 160 LYS CA C 59.3 0.2 1 704 158 160 LYS CB C 32.0 0.2 1 705 158 160 LYS CG C 24.2 0.2 1 706 158 160 LYS N N 117.7 0.2 1 707 159 161 ILE C C 177.3 0.2 1 708 159 161 ILE CA C 65.5 0.2 1 709 159 161 ILE CB C 38.3 0.2 1 710 159 161 ILE CD1 C 13.6 0.2 1 711 159 161 ILE CG1 C 29.2 0.2 1 712 159 161 ILE CG2 C 16.3 0.2 1 713 159 161 ILE N N 117.3 0.2 1 714 160 162 VAL C C 177.2 0.2 1 715 160 162 VAL CA C 67.1 0.2 1 716 160 162 VAL CB C 31.4 0.2 1 717 160 162 VAL N N 115.3 0.2 1 718 161 163 ASP C C 178.4 0.2 1 719 161 163 ASP CA C 57.5 0.2 1 720 161 163 ASP CB C 42.1 0.2 1 721 161 163 ASP N N 119.4 0.2 1 722 162 164 GLN C C 178.9 0.2 1 723 162 164 GLN CA C 58.7 0.2 1 724 162 164 GLN CB C 29.7 0.2 1 725 162 164 GLN CG C 31.9 0.2 1 726 162 164 GLN N N 116.4 0.2 1 727 163 165 VAL C C 177.1 0.2 1 728 163 165 VAL CA C 68.4 0.2 1 729 163 165 VAL CB C 31.1 0.2 1 730 163 165 VAL CG1 C 21.9 0.2 2 731 163 165 VAL CG2 C 24.6 0.2 2 732 163 165 VAL N N 119.6 0.2 1 733 164 166 ALA C C 179.3 0.2 1 734 164 166 ALA CA C 55.9 0.2 1 735 164 166 ALA CB C 18.6 0.2 1 736 164 166 ALA N N 122.1 0.2 1 737 165 167 ARG CA C 59.1 0.2 1 738 165 167 ARG CB C 30.0 0.2 1 739 165 167 ARG CG C 28.1 0.2 1 740 165 167 ARG CZ C 159.2 0.2 1 741 165 167 ARG N N 117.4 0.2 1 742 166 168 PHE C C 178.9 0.2 1 743 166 168 PHE CA C 59.1 0.2 1 744 166 168 PHE CB C 37.8 0.2 1 745 166 168 PHE CD1 C 130.4 0.2 3 746 166 168 PHE CG C 137.7 0.2 1 747 166 168 PHE N N 121.1 0.2 1 748 167 169 VAL C C 177.9 0.2 1 749 167 169 VAL CA C 66.5 0.2 1 750 167 169 VAL CB C 30.4 0.2 1 751 167 169 VAL CG1 C 24.0 0.2 2 752 167 169 VAL N N 121.4 0.2 1 753 168 170 ASP CA C 57.9 0.2 1 754 168 170 ASP CB C 39.8 0.2 1 755 168 170 ASP CG C 182.6 0.2 1 756 168 170 ASP N N 121.8 0.2 1 757 169 171 GLU CA C 60.2 0.2 1 758 169 171 GLU CB C 29.6 0.2 1 759 169 171 GLU CD C 182.0 0.2 1 760 169 171 GLU CG C 35.7 0.2 1 761 169 171 GLU N N 118.9 0.2 1 762 170 172 LEU CA C 58.2 0.2 1 763 170 172 LEU CB C 38.9 0.2 1 764 170 172 LEU CD1 C 22.7 0.2 2 765 170 172 LEU CD2 C 23.4 0.2 2 766 170 172 LEU CG C 24.8 0.2 1 767 170 172 LEU N N 121.9 0.2 1 768 171 173 GLU C C 177.4 0.2 1 769 171 173 GLU CA C 59.2 0.2 1 770 171 173 GLU CB C 29.5 0.2 1 771 171 173 GLU CD C 182.8 0.2 1 772 171 173 GLU CG C 36.4 0.2 1 773 171 173 GLU N N 117.9 0.2 1 774 172 174 LYS C C 178.0 0.2 1 775 172 174 LYS CA C 57.4 0.2 1 776 172 174 LYS CB C 33.0 0.2 1 777 172 174 LYS CD C 29.0 0.2 1 778 172 174 LYS CG C 25.2 0.2 1 779 172 174 LYS N N 115.1 0.2 1 780 173 175 ALA C C 175.6 0.2 1 781 173 175 ALA CA C 53.0 0.2 1 782 173 175 ALA CB C 19.1 0.2 1 783 173 175 ALA N N 119.8 0.2 1 784 174 176 PHE C C 175.7 0.2 1 785 174 176 PHE CA C 54.9 0.2 1 786 174 176 PHE CB C 42.2 0.2 1 787 174 176 PHE CD1 C 132.7 0.2 3 788 174 176 PHE CE1 C 131.4 0.2 3 789 174 176 PHE CG C 140.4 0.2 1 790 174 176 PHE CZ C 129.4 0.2 1 791 174 176 PHE N N 115.9 0.2 1 792 175 177 PRO CA C 62.9 0.2 1 793 175 177 PRO CB C 32.9 0.2 1 794 175 177 PRO CD C 49.6 0.2 1 795 175 177 PRO CG C 27.7 0.2 1 796 175 177 PRO N N 135.7 0.2 1 797 176 178 ILE N N 114.9 0.2 1 798 177 179 GLU C C 178.4 0.2 1 799 177 179 GLU CA C 61.4 0.2 1 800 177 179 GLU CB C 29.5 0.2 1 801 177 179 GLU CD C 178.3 0.2 1 802 177 179 GLU CG C 36.3 0.2 1 803 177 179 GLU N N 126.5 0.2 1 804 178 180 ALA CA C 55.1 0.2 1 805 178 180 ALA CB C 16.7 0.2 1 806 178 180 ALA N N 120.9 0.2 1 807 179 181 VAL C C 178.2 0.2 1 808 179 181 VAL CA C 65.7 0.2 1 809 179 181 VAL CB C 32.0 0.2 1 810 179 181 VAL CG1 C 22.1 0.2 2 811 179 181 VAL CG2 C 21.2 0.2 2 812 179 181 VAL N N 120.0 0.2 1 813 180 182 CYS C C 176.4 0.2 1 814 180 182 CYS CA C 65.4 0.2 1 815 180 182 CYS CB C 26.2 0.2 1 816 180 182 CYS N N 118.5 0.2 1 817 181 183 HIS CA C 60.6 0.2 1 818 181 183 HIS CB C 29.5 0.2 1 819 181 183 HIS CG C 133.8 0.2 1 820 181 183 HIS N N 118.3 0.2 1 821 182 184 LYS CA C 58.6 0.2 1 822 182 184 LYS CB C 31.7 0.2 1 823 182 184 LYS CD C 29.4 0.2 1 824 182 184 LYS CG C 25.6 0.2 1 825 182 184 LYS N N 120.0 0.2 1 826 183 185 LEU C C 175.1 0.2 1 827 183 185 LEU CA C 54.8 0.2 1 828 183 185 LEU CB C 44.5 0.2 1 829 183 185 LEU N N 118.0 0.2 1 830 184 186 ALA CA C 55.1 0.2 1 831 184 186 ALA CB C 17.8 0.2 1 832 184 186 ALA N N 123.0 0.2 1 833 185 187 GLU C C 179.7 0.2 1 834 185 187 GLU CA C 59.4 0.2 1 835 185 187 GLU CB C 29.4 0.2 1 836 185 187 GLU CD C 183.7 0.2 1 837 185 187 GLU CG C 37.4 0.2 1 838 185 187 GLU N N 115.4 0.2 1 839 186 188 ILE C C 177.9 0.2 1 840 186 188 ILE CA C 66.1 0.2 1 841 186 188 ILE CB C 37.3 0.2 1 842 186 188 ILE CD1 C 13.6 0.2 1 843 186 188 ILE CG1 C 30.6 0.2 1 844 186 188 ILE CG2 C 18.6 0.2 1 845 186 188 ILE N N 122.7 0.2 1 846 187 189 GLU C C 178.3 0.2 1 847 187 189 GLU CA C 59.1 0.2 1 848 187 189 GLU CB C 29.5 0.2 1 849 187 189 GLU CD C 180.7 0.2 1 850 187 189 GLU CG C 37.2 0.2 1 851 187 189 GLU N N 120.4 0.2 1 852 188 190 ILE C C 177.0 0.2 1 853 188 190 ILE CA C 59.8 0.2 1 854 188 190 ILE CB C 38.4 0.2 1 855 188 190 ILE CD1 C 14.4 0.2 1 856 188 190 ILE CG1 C 25.4 0.2 1 857 188 190 ILE CG2 C 17.4 0.2 1 858 188 190 ILE N N 106.4 0.2 1 859 189 191 GLU C C 177.4 0.2 1 860 189 191 GLU CA C 59.5 0.2 1 861 189 191 GLU CB C 27.2 0.2 1 862 189 191 GLU N N 123.2 0.2 1 863 190 192 GLU C C 175.5 0.2 1 864 190 192 GLU CA C 56.1 0.2 1 865 190 192 GLU CB C 29.5 0.2 1 866 190 192 GLU CD C 184.1 0.2 1 867 190 192 GLU CG C 36.8 0.2 1 868 190 192 GLU N N 113.2 0.2 1 869 191 193 VAL C C 175.5 0.2 1 870 191 193 VAL CA C 62.7 0.2 1 871 191 193 VAL CB C 30.6 0.2 1 872 191 193 VAL CG1 C 19.7 0.2 2 873 191 193 VAL CG2 C 22.6 0.2 2 874 191 193 VAL N N 122.6 0.2 1 875 192 194 GLU C C 175.2 0.2 1 876 192 194 GLU CA C 55.9 0.2 1 877 192 194 GLU CB C 32.1 0.2 1 878 192 194 GLU CD C 184.0 0.2 1 879 192 194 GLU CG C 35.9 0.2 1 880 192 194 GLU N N 124.2 0.2 1 881 193 195 ASP C C 175.0 0.2 1 882 193 195 ASP CA C 51.9 0.2 1 883 193 195 ASP CB C 42.2 0.2 1 884 193 195 ASP CG C 181.3 0.2 1 885 193 195 ASP N N 115.8 0.2 1 886 194 196 GLU C C 178.3 0.2 1 887 194 196 GLU CA C 60.1 0.2 1 888 194 196 GLU CB C 29.8 0.2 1 889 194 196 GLU CD C 181.3 0.2 1 890 194 196 GLU CG C 35.9 0.2 1 891 194 196 GLU N N 123.9 0.2 1 892 195 197 ALA C C 180.7 0.2 1 893 195 197 ALA CA C 55.9 0.2 1 894 195 197 ALA CB C 18.0 0.2 1 895 195 197 ALA N N 123.6 0.2 1 896 196 198 SER C C 175.7 0.2 1 897 196 198 SER CA C 62.7 0.2 1 898 196 198 SER CB C 62.6 0.2 1 899 196 198 SER N N 116.7 0.2 1 900 197 199 LEU C C 178.4 0.2 1 901 197 199 LEU CA C 57.7 0.2 1 902 197 199 LEU CB C 42.8 0.2 1 903 197 199 LEU CD1 C 23.8 0.2 2 904 197 199 LEU CD2 C 23.0 0.2 2 905 197 199 LEU CG C 27.3 0.2 1 906 197 199 LEU N N 121.1 0.2 1 907 198 200 THR C C 176.0 0.2 1 908 198 200 THR CA C 67.2 0.2 1 909 198 200 THR CB C 68.6 0.2 1 910 198 200 THR CG2 C 21.1 0.2 1 911 198 200 THR N N 117.3 0.2 1 912 199 201 ILE C C 178.7 0.2 1 913 199 201 ILE CA C 64.8 0.2 1 914 199 201 ILE CB C 37.5 0.2 1 915 199 201 ILE CD1 C 13.5 0.2 1 916 199 201 ILE CG1 C 29.1 0.2 1 917 199 201 ILE CG2 C 17.6 0.2 1 918 199 201 ILE N N 122.2 0.2 1 919 200 202 LEU CA C 58.0 0.2 1 920 200 202 LEU CB C 42.0 0.2 1 921 200 202 LEU CD1 C 26.3 0.2 2 922 200 202 LEU CD2 C 25.2 0.2 2 923 200 202 LEU CG C 29.6 0.2 1 924 200 202 LEU N N 119.4 0.2 1 925 201 203 LYS CA C 60.0 0.2 1 926 201 203 LYS CB C 32.5 0.2 1 927 201 203 LYS CD C 29.5 0.2 1 928 201 203 LYS CE C 41.5 0.2 1 929 201 203 LYS CG C 24.1 0.2 1 930 201 203 LYS N N 118.1 0.2 1 931 202 204 ASP CA C 56.9 0.2 1 932 202 204 ASP CB C 41.3 0.2 1 933 202 204 ASP N N 117.7 0.2 1 934 203 205 ALA C C 177.3 0.2 1 935 203 205 ALA CA C 54.8 0.2 1 936 203 205 ALA CB C 17.9 0.2 1 937 203 205 ALA N N 123.1 0.2 1 938 204 206 ALA C C 178.9 0.2 1 939 204 206 ALA CA C 52.5 0.2 1 940 204 206 ALA CB C 18.6 0.2 1 941 204 206 ALA N N 115.9 0.2 1 942 205 207 GLY C C 175.2 0.2 1 943 205 207 GLY CA C 47.6 0.2 1 944 205 207 GLY N N 108.0 0.2 1 945 206 208 GLY C C 174.0 0.2 1 946 206 208 GLY CA C 45.8 0.2 1 947 206 208 GLY N N 116.7 0.2 1 948 207 209 ILE C C 174.5 0.2 1 949 207 209 ILE CA C 61.4 0.2 1 950 207 209 ILE CB C 41.3 0.2 1 951 207 209 ILE CD1 C 15.1 0.2 1 952 207 209 ILE CG2 C 17.7 0.2 1 953 207 209 ILE N N 114.8 0.2 1 954 208 210 ASP C C 174.5 0.2 1 955 208 210 ASP CA C 52.7 0.2 1 956 208 210 ASP CB C 41.8 0.2 1 957 208 210 ASP CG C 178.8 0.2 1 958 208 210 ASP N N 120.5 0.2 1 959 209 211 ALA C C 179.2 0.2 1 960 209 211 ALA CA C 54.8 0.2 1 961 209 211 ALA CB C 18.4 0.2 1 962 209 211 ALA N N 129.2 0.2 1 963 210 212 ALA C C 174.9 0.2 1 964 210 212 ALA CA C 54.9 0.2 1 965 210 212 ALA CB C 18.1 0.2 1 966 210 212 ALA N N 120.1 0.2 1 967 211 213 MET C C 177.8 0.2 1 968 211 213 MET CA C 58.4 0.2 1 969 211 213 MET CB C 33.9 0.2 1 970 211 213 MET CG C 30.7 0.2 1 971 211 213 MET N N 120.9 0.2 1 972 212 214 SER C C 176.5 0.2 1 973 212 214 SER CA C 62.7 0.2 1 974 212 214 SER N N 113.2 0.2 1 975 213 215 ASP C C 178.7 0.2 1 976 213 215 ASP CA C 56.8 0.2 1 977 213 215 ASP CB C 40.4 0.2 1 978 213 215 ASP N N 119.3 0.2 1 979 214 216 ALA CA C 55.0 0.2 1 980 214 216 ALA CB C 17.4 0.2 1 981 214 216 ALA N N 123.1 0.2 1 982 215 217 ALA CA C 55.4 0.2 1 983 215 217 ALA CB C 17.5 0.2 1 984 215 217 ALA N N 122.2 0.2 1 985 216 218 ALA CA C 55.6 0.2 1 986 216 218 ALA CB C 17.9 0.2 1 987 216 218 ALA N N 121.8 0.2 1 988 217 219 GLN CA C 58.2 0.2 1 989 217 219 GLN CB C 28.5 0.2 1 990 217 219 GLN CD C 178.8 0.2 1 991 217 219 GLN CG C 32.8 0.2 1 992 217 219 GLN N N 116.6 0.2 1 993 218 220 LYS C C 178.7 0.2 1 994 218 220 LYS CA C 59.8 0.2 1 995 218 220 LYS CB C 32.5 0.2 1 996 218 220 LYS CD C 29.5 0.2 1 997 218 220 LYS CE C 42.8 0.2 1 998 218 220 LYS CG C 26.1 0.2 1 999 218 220 LYS N N 121.5 0.2 1 1000 219 221 ILE C C 178.9 0.2 1 1001 219 221 ILE CA C 66.2 0.2 1 1002 219 221 ILE CB C 38.2 0.2 1 1003 219 221 ILE CD1 C 13.5 0.2 1 1004 219 221 ILE CG1 C 29.0 0.2 1 1005 219 221 ILE CG2 C 17.5 0.2 1 1006 219 221 ILE N N 120.9 0.2 1 1007 220 222 ASP CA C 57.3 0.2 1 1008 220 222 ASP CB C 40.2 0.2 1 1009 220 222 ASP N N 118.5 0.2 1 1010 221 223 ALA C C 179.8 0.2 1 1011 221 223 ALA CA C 54.2 0.2 1 1012 221 223 ALA CB C 18.4 0.2 1 1013 221 223 ALA N N 121.4 0.2 1 1014 222 224 ILE C C 179.3 0.2 1 1015 222 224 ILE CA C 64.3 0.2 1 1016 222 224 ILE CB C 38.3 0.2 1 1017 222 224 ILE CG1 C 29.1 0.2 1 1018 222 224 ILE CG2 C 17.3 0.2 1 1019 222 224 ILE N N 120.7 0.2 1 1020 223 225 VAL CA C 62.9 0.2 1 1021 223 225 VAL CB C 29.9 0.2 1 1022 223 225 VAL N N 120.3 0.2 1 stop_ save_