data_15514 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of backbone 1H, 13C and 15N resonances of human IgG1 Fc (51.4 kDa) ; _BMRB_accession_number 15514 _BMRB_flat_file_name bmr15514.str _Entry_type original _Submission_date 2007-10-09 _Accession_date 2007-10-09 _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 Cocco Melanie . . 2 Rosenfied Robert . . 3 Lewis Jeff . . 4 Ren Da . . 5 Li Luke . . 6 Remmele Richard L. Jr. 7 Brems David N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 195 "13C chemical shifts" 573 "15N chemical shifts" 195 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-12 update BMRB 'added PubMed ID' 2008-01-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Assignment of backbone (1)H, (13)C and (15)N resonances of human IgG1 Fc (51.4 kDa)' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636873 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Cocco Melanie J. . 3 Rosenfied Robert . . 4 Lewis Jeffery K. . 5 Ren Da . . 6 Li Luke . . 7 Remmele Richard L. Jr. 8 Brems David N. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 233 _Page_last 235 _Year 2007 _Details . loop_ _Keyword assignment Fc IgG1 NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'human IgG1 Fc' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human IgG1 Fc, chain 1' $IgG1_Fc 'human IgG1 Fc, chain 2' $IgG1_Fc stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IgG1_Fc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IgG1_Fc _Molecular_mass 25679 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 228 _Mol_residue_sequence ; MDKTHTCPPCPAPELLGGPS VFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNST YRVVSVLTVLHQDWLNGKEY KCKVSNKALPAPIEKTISKA KGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAV EWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQ GNVFSCSVMHEALHNHYTQK SLSLSPGK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 LYS 4 THR 5 HIS 6 THR 7 CYS 8 PRO 9 PRO 10 CYS 11 PRO 12 ALA 13 PRO 14 GLU 15 LEU 16 LEU 17 GLY 18 GLY 19 PRO 20 SER 21 VAL 22 PHE 23 LEU 24 PHE 25 PRO 26 PRO 27 LYS 28 PRO 29 LYS 30 ASP 31 THR 32 LEU 33 MET 34 ILE 35 SER 36 ARG 37 THR 38 PRO 39 GLU 40 VAL 41 THR 42 CYS 43 VAL 44 VAL 45 VAL 46 ASP 47 VAL 48 SER 49 HIS 50 GLU 51 ASP 52 PRO 53 GLU 54 VAL 55 LYS 56 PHE 57 ASN 58 TRP 59 TYR 60 VAL 61 ASP 62 GLY 63 VAL 64 GLU 65 VAL 66 HIS 67 ASN 68 ALA 69 LYS 70 THR 71 LYS 72 PRO 73 ARG 74 GLU 75 GLU 76 GLN 77 TYR 78 ASN 79 SER 80 THR 81 TYR 82 ARG 83 VAL 84 VAL 85 SER 86 VAL 87 LEU 88 THR 89 VAL 90 LEU 91 HIS 92 GLN 93 ASP 94 TRP 95 LEU 96 ASN 97 GLY 98 LYS 99 GLU 100 TYR 101 LYS 102 CYS 103 LYS 104 VAL 105 SER 106 ASN 107 LYS 108 ALA 109 LEU 110 PRO 111 ALA 112 PRO 113 ILE 114 GLU 115 LYS 116 THR 117 ILE 118 SER 119 LYS 120 ALA 121 LYS 122 GLY 123 GLN 124 PRO 125 ARG 126 GLU 127 PRO 128 GLN 129 VAL 130 TYR 131 THR 132 LEU 133 PRO 134 PRO 135 SER 136 ARG 137 ASP 138 GLU 139 LEU 140 THR 141 LYS 142 ASN 143 GLN 144 VAL 145 SER 146 LEU 147 THR 148 CYS 149 LEU 150 VAL 151 LYS 152 GLY 153 PHE 154 TYR 155 PRO 156 SER 157 ASP 158 ILE 159 ALA 160 VAL 161 GLU 162 TRP 163 GLU 164 SER 165 ASN 166 GLY 167 GLN 168 PRO 169 GLU 170 ASN 171 ASN 172 TYR 173 LYS 174 THR 175 THR 176 PRO 177 PRO 178 VAL 179 LEU 180 ASP 181 SER 182 ASP 183 GLY 184 SER 185 PHE 186 PHE 187 LEU 188 TYR 189 SER 190 LYS 191 LEU 192 THR 193 VAL 194 ASP 195 LYS 196 SER 197 ARG 198 TRP 199 GLN 200 GLN 201 GLY 202 ASN 203 VAL 204 PHE 205 SER 206 CYS 207 SER 208 VAL 209 MET 210 HIS 211 GLU 212 ALA 213 LEU 214 HIS 215 ASN 216 HIS 217 TYR 218 THR 219 GLN 220 LYS 221 SER 222 LEU 223 SER 224 LEU 225 SER 226 PRO 227 GLY 228 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 25224 human_IgG1-Fc 97.37 222 100.00 100.00 1.46e-161 PDB 1DN2 "Fc Fragment Of Human Igg1 In Complex With An Engineered 13 Residue Peptide Dcawhlgelvwct-Nh2" 90.79 207 98.55 100.00 4.18e-148 PDB 1L6X "Fc Fragment Of Rituximab Bound To A Minimized Version Of The B-Domain From Protein A Called Z34c" 90.79 207 100.00 100.00 1.22e-149 PDB 1OQO "Complex Between G0 Version Of An Fc Bound To A Minimized Version Of Protein A Called Mini-Z" 92.98 212 100.00 100.00 1.46e-153 PDB 1OQX "G-2 Glycovariant Of Human Igg Fc Bound To Minimized Version Of Protein A Called Z34c" 92.98 212 100.00 100.00 1.46e-153 PDB 1T83 "Crystal Structure Of A Human Type Iii Fc Gamma Receptor In Complex With An Fc Fragment Of Igg1 (Orthorhombic)" 98.25 224 99.11 100.00 1.72e-162 PDB 1T89 "Crystal Structure Of A Human Type Iii Fc Gamma Receptor In Complex With An Fc Fragment Of Igg1 (Hexagonal)" 98.25 224 99.11 100.00 1.72e-162 PDB 2DTS "Crystal Structure Of The Defucosylated Fc Fragment From Human Immunoglobulin G1" 97.81 223 100.00 100.00 2.83e-162 PDB 2GJ7 "Crystal Structure Of A Ge-GiFC COMPLEX" 99.12 227 98.67 100.00 2.21e-163 PDB 2IWG "Complex Between The Pryspry Domain Of Trim21 And Igg Fc" 90.79 207 100.00 100.00 1.22e-149 PDB 2J6E "Crystal Structure Of An Autoimmune Complex Between A Human Igm Rheumatoid Factor And Igg1 Fc Reveals A Novel Fc Epitope And Evi" 99.56 232 99.56 100.00 7.57e-165 PDB 2QL1 "Structural Characterization Of A Mutated, Adcc-Enhanced Human Fc Fragment" 98.68 225 97.78 98.67 1.99e-160 PDB 2WAH "Crystal Structure Of An Igg1 Fc Glycoform (man9glcnac2)" 91.67 209 99.52 99.52 2.36e-150 PDB 3AGV "Crystal Structure Of A Human Igg-Aptamer Complex" 92.54 211 100.00 100.00 1.55e-152 PDB 3AVE "Crystal Structure Of The Fucosylated Fc Fragment From Human Immunoglobulin G1" 97.81 223 100.00 100.00 2.83e-162 PDB 3AY4 "Crystal Structure Of Nonfucosylated Fc Complexed With Bis-Glycosylated Soluble Form Of Fc Gamma Receptor Iiia" 97.81 223 100.00 100.00 2.83e-162 PDB 3C2S "Structural Characterization Of A Human Fc Fragment Engineered For Lack Of Effector Functions" 98.68 225 97.78 98.67 9.64e-161 PDB 3D6G "Fc Fragment Of Igg1 (herceptin) With Protein-a Mimetic Peptide Dendrimer Ligand" 92.11 210 100.00 100.00 6.76e-152 PDB 3DNK "Enzyme Deglycosylated Human Igg1 Fc Fragment" 92.98 212 98.58 100.00 5.83e-152 PDB 3DO3 "Human 1gg1 Fc Fragment, 2.5 Angstrom Structure" 92.98 212 99.06 100.00 1.21e-152 PDB 3FJT "Crystal Structure Of A Human Fc Fragment Engineered For Extended Serum Half-life" 91.67 209 98.56 99.04 1.21e-148 PDB 3S7G "Aglycosylated Human Igg1 Fc Fragment" 99.56 227 100.00 100.00 1.06e-165 PDB 3SGJ "Unique Carbohydrate-Carbohydrate Interactions Are Required For High Affinity Binding Between Fcgiii And Antibodies Lacking Core" 98.68 225 100.00 100.00 4.86e-164 PDB 3SGK "Unique CarbohydrateCARBOHYDRATE INTERACTIONS ARE REQUIRED FOR HIGH Affinity Binding Of Fcgiii And Antibodies Lacking Core Fucos" 98.68 225 100.00 100.00 4.86e-164 PDB 3V7M "Crystal Structure Of Monoclonal Human Anti-rhesus D Fc Igg1 T125(yb2/0) In The Presence Of Zn2+" 91.67 209 100.00 100.00 4.52e-151 PDB 3V8C "Crystal Structure Of Monoclonal Human Anti-rhesus D Fc Igg1 T125(yb2/0) Double Mutant (h310 And H435 In K)" 92.98 212 99.06 99.06 3.87e-151 PDB 3V95 "Crystal Structure Of Monoclonal Human Anti-rhesus D Fc And Igg1 T125(yb2/0) In The Presence Of Edta" 92.98 212 100.00 100.00 1.46e-153 PDB 3WJJ "Crystal Structure Of Iib Selective Fc Variant, Fc(p238d), In Complex With Fcgriib" 98.68 230 99.56 99.56 6.11e-163 PDB 3WJL "Crystal Structure Of Iib Selective Fc Variant, Fc(v12), In Complex With Fcgriib" 98.68 230 97.33 97.78 4.48e-158 PDB 3WKN "Crystal Structure Of The Artificial Protein Affinger P17 (af.p17) Complexed With Fc Fragment Of Human Igg" 92.98 212 100.00 100.00 1.46e-153 PDB 4ACP "Deactivation Of Human Igg1 Fc By Endoglycosidase Treatment" 99.12 240 99.56 99.56 4.00e-164 PDB 4B7I "Crystal Structure Of Human Igg Fc Bearing Hybrid-Type Glycans" 92.11 218 99.52 99.52 4.84e-151 PDB 4BM7 "Crystal Structure Of Igg Fc F241a Mutant With Native Glycosylation" 98.25 233 98.66 99.55 3.73e-161 PDB 4BYH "Crystal Structure Of Sialylated Igg Fc" 98.25 233 99.11 100.00 2.12e-162 PDB 4CDH "Crystallographic Structure Of The Human Igg1 Alpha 2-6 Sialilated Fc-fragment" 99.56 255 100.00 100.00 1.13e-166 PDB 4DZ8 "Human Igg1 Fc Fragment Heterodimer" 92.54 211 99.05 99.05 1.32e-147 PDB 4J12 "Monomeric Fc" 91.67 210 97.61 99.04 1.71e-147 PDB 4KU1 "Role Of The Hinge And C-gamma-2/c-gamma-3 Interface In Immunoglobin G1 Fc Domain Motions: Implications For Fc Engineering" 91.23 208 100.00 100.00 3.56e-150 PDB 4N0U "Ternary Complex Between Neonatal Fc Receptor, Serum Albumin And Fc" 91.67 209 98.56 99.04 1.21e-148 PDB 4NQS "Knob-into-hole Igg Fc" 93.42 213 98.59 99.53 6.52e-152 PDB 4NQT "Anti-parallel Fc-hole(t366s/l368a/y407v) Homodimer" 93.42 213 97.65 99.06 6.92e-151 PDB 4NQU "Anti-parallel Fc-knob (t366w) Homodimer" 93.42 213 98.59 99.53 6.52e-152 PDB 4Q6Y "Crystal Structure Of A Chemoenzymatic Glycoengineered Disialylated Fc (di-sfc)" 96.93 221 100.00 100.00 5.57e-161 PDB 4Q74 "F241a Fc" 98.68 230 98.67 99.11 1.56e-161 PDB 4Q7D "Wild Type Fc (wtfc)" 96.93 221 100.00 100.00 5.57e-161 PDB 4QGT "The Crystal Structure Of Human Igg Fc Domain With Enhanced Aromatic Sequon" 99.56 233 98.24 99.12 2.89e-162 PDB 4W4N "Crystal Structure Of Human Fc At 1.80 A" 97.81 223 100.00 100.00 1.30e-162 PDB 4W4O "High-resolution Crystal Structure Of Fc Bound To Its Human Receptor Fc-gamma-ri" 98.25 224 99.55 100.00 5.32e-163 PDB 4WI2 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc (wild-type)" 91.23 208 100.00 100.00 3.56e-150 PDB 4WI3 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation I253a" 91.23 208 99.52 99.52 1.82e-149 PDB 4WI4 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation S254a" 90.79 207 99.52 100.00 6.44e-149 PDB 4WI5 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation H310a" 91.23 208 99.52 99.52 6.97e-149 PDB 4WI6 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation N434a" 91.23 208 99.52 99.52 3.58e-149 PDB 4WI7 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation H435a" 91.23 208 99.52 99.52 6.97e-149 PDB 4WI8 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation Y436a" 91.23 208 99.52 99.52 5.13e-149 PDB 4WI9 "Structural Mapping Of The Human Igg1 Binding Site For Fcrn: Hu3s193 Fc Mutation I253a/h310a" 91.23 208 99.04 99.04 3.30e-148 PDB 4X4M "Structure Of Fcgammari In Complex With Fc Reveals The Importance Of Glycan Recognition For High Affinity Igg Binding" 96.05 219 100.00 100.00 7.21e-159 PDB 4X98 "Immunoglobulin Fc Heterodimer Variant" 96.49 220 99.09 99.55 5.72e-158 PDB 4X99 "Immunoglobulin Fc Heterodimers Variant" 97.81 223 98.65 99.10 7.14e-159 PDB 4ZNE "Igg1 Fc-fcgammari Ecd Complex" 99.56 227 100.00 100.00 1.06e-165 PDB 5BW7 "Crystal Structure Of Nonfucosylated Fc Y296w Mutant Complexed With Bis-glycosylated Soluble Form Of Fc Gamma Receptor Iiia" 97.81 223 99.55 100.00 2.10e-161 DBJ BAC86226 "unnamed protein product [Homo sapiens]" 99.56 447 100.00 100.00 7.53e-164 EMBL CAA49866 "IgG1 Fc fragment [synthetic construct]" 99.56 255 100.00 100.00 1.13e-166 EMBL CAE45920 "hypothetical protein [Homo sapiens]" 99.56 473 99.12 100.00 8.78e-163 EMBL CAM91874 "soluble immunoglobulin-like receptor CHIR-AB1 construct [synthetic construct]" 99.56 364 99.56 99.56 2.46e-163 EMBL CAP05188 "murine anti-CD30 ScFv antibody-human IgG1-IL2 chimeric fusion protein [synthetic construct]" 95.18 646 99.54 100.00 7.81e-153 EMBL CAP05190 "human IgG1-IL2-murine anti-CD30 ScFv antibody chimaeric fusion protein [synthetic construct]" 94.30 615 100.00 100.00 5.12e-152 GB AAB37424 "FV/M4 [synthetic construct]" 99.56 487 99.12 99.12 4.16e-162 GB AAD38158 "immunoglobulin G1 Fc fragment [Homo sapiens]" 97.81 223 99.55 99.55 2.75e-161 GB AAF42993 "10B5 scFv [synthetic construct]" 96.49 604 98.64 99.09 6.53e-156 GB AAG00448 "anti-human melanoma single-chain variable fragment antibody G71-1 immunoconjugate [synthetic construct]" 99.56 501 100.00 100.00 2.61e-164 GB AAG00449 "mutated mouse factor VII molecule immunoconjugate [synthetic construct]" 99.56 681 100.00 100.00 1.05e-159 PIR PT0207 "Ig gamma chain C region - chimpanzee" 96.49 234 98.64 99.09 2.00e-158 PIR S69339 "Ig heavy chain V region precursor - human" 99.56 374 99.12 100.00 2.59e-163 PRF 1605217A "Ig gamma1" 97.81 224 99.10 100.00 8.95e-162 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IgG1_Fc 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 $IgG1_Fc 'recombinant technology' . Escherichia coli . pAM 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 $IgG1_Fc 2.5 mM '[U-13C; U-15N; U-2H]' 'sodium acetate' 10 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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' 0.2 . M pH 5.0 . pH pressure 1 . atm temperature 302 . 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 'methylene protons' ppm 0 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external 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 HNCO' '3D HNCACB' 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 'human IgG1 Fc, chain 1' _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 2 2 ASP C C 175.998 0.05 1 2 2 2 ASP CA C 53.830 0.05 1 3 2 2 ASP CB C 41.040 0.05 1 4 3 3 LYS H H 8.522 0.005 1 5 3 3 LYS C C 176.928 0.05 1 6 3 3 LYS CA C 56.277 0.05 1 7 3 3 LYS CB C 31.860 0.05 1 8 3 3 LYS N N 123.013 0.05 1 9 4 4 THR H H 8.138 0.005 1 10 4 4 THR C C 174.427 0.05 1 11 4 4 THR CA C 61.905 0.05 1 12 4 4 THR CB C 69.183 0.05 1 13 4 4 THR N N 114.456 0.05 1 14 5 5 HIS H H 8.307 0.005 1 15 5 5 HIS C C 174.273 0.05 1 16 5 5 HIS CA C 55.131 0.05 1 17 5 5 HIS CB C 28.671 0.05 1 18 5 5 HIS N N 121.006 0.05 1 19 6 6 THR H H 8.052 0.005 1 20 6 6 THR C C 174.463 0.05 1 21 6 6 THR CA C 61.538 0.05 1 22 6 6 THR CB C 69.449 0.05 1 23 6 6 THR N N 116.427 0.05 1 24 7 7 CYS H H 8.493 0.005 1 25 7 7 CYS CA C 53.219 0.05 1 26 7 7 CYS CB C 39.952 0.05 1 27 7 7 CYS N N 123.245 0.05 1 28 9 9 PRO C C 177.014 0.05 1 29 9 9 PRO CA C 62.270 0.05 1 30 9 9 PRO CB C 31.260 0.05 1 31 10 10 CYS H H 8.650 0.005 1 32 10 10 CYS CA C 52.794 0.05 1 33 10 10 CYS CB C 37.682 0.05 1 34 10 10 CYS N N 121.958 0.05 1 35 11 11 PRO C C 175.889 0.05 1 36 11 11 PRO CA C 62.378 0.05 1 37 11 11 PRO CB C 31.423 0.05 1 38 12 12 ALA H H 8.277 0.005 1 39 12 12 ALA CA C 49.955 0.05 1 40 12 12 ALA CB C 17.366 0.05 1 41 12 12 ALA N N 126.221 0.05 1 42 13 13 PRO CA C 62.975 0.05 1 43 13 13 PRO CB C 31.810 0.05 1 44 14 14 GLU H H 8.510 0.005 1 45 14 14 GLU CA C 56.222 0.05 1 46 14 14 GLU CB C 29.095 0.05 1 47 14 14 GLU N N 120.603 0.05 1 48 15 15 LEU H H 8.160 0.005 1 49 15 15 LEU C C 177.219 0.05 1 50 15 15 LEU CA C 54.592 0.05 1 51 15 15 LEU CB C 41.241 0.05 1 52 15 15 LEU N N 123.247 0.05 1 53 16 16 LEU H H 8.117 0.005 1 54 16 16 LEU C C 177.771 0.05 1 55 16 16 LEU CA C 54.779 0.05 1 56 16 16 LEU CB C 41.412 0.05 1 57 16 16 LEU N N 123.646 0.05 1 58 17 17 GLY H H 8.301 0.005 1 59 17 17 GLY C C 174.111 0.05 1 60 17 17 GLY CA C 44.540 0.05 1 61 17 17 GLY N N 109.961 0.05 1 62 18 18 GLY H H 7.902 0.005 1 63 18 18 GLY CA C 44.217 0.05 1 64 18 18 GLY N N 108.869 0.05 1 65 19 19 PRO C C 177.067 0.05 1 66 20 20 SER H H 8.012 0.005 1 67 20 20 SER C C 171.755 0.05 1 68 20 20 SER CA C 57.270 0.05 1 69 20 20 SER CB C 65.160 0.05 1 70 20 20 SER N N 114.460 0.05 1 71 21 21 VAL H H 8.041 0.005 1 72 21 21 VAL C C 174.028 0.05 1 73 21 21 VAL CA C 60.159 0.05 1 74 21 21 VAL CB C 34.016 0.05 1 75 21 21 VAL N N 122.014 0.05 1 76 22 22 PHE H H 9.413 0.005 1 77 22 22 PHE C C 172.678 0.05 1 78 22 22 PHE CA C 55.667 0.05 1 79 22 22 PHE CB C 42.819 0.05 1 80 22 22 PHE N N 125.736 0.05 1 81 23 23 LEU H H 8.215 0.005 1 82 23 23 LEU C C 174.807 0.05 1 83 23 23 LEU CA C 52.928 0.05 1 84 23 23 LEU CB C 45.037 0.05 1 85 23 23 LEU N N 124.184 0.05 1 86 24 24 PHE H H 9.340 0.005 1 87 24 24 PHE CA C 54.378 0.05 1 88 24 24 PHE CB C 39.535 0.05 1 89 24 24 PHE N N 125.124 0.05 1 90 28 28 PRO C C 179.039 0.05 1 91 28 28 PRO CA C 65.020 0.05 1 92 28 28 PRO CB C 31.690 0.05 1 93 29 29 LYS H H 8.897 0.005 1 94 29 29 LYS C C 177.235 0.05 1 95 29 29 LYS CA C 60.048 0.05 1 96 29 29 LYS CB C 32.092 0.05 1 97 29 29 LYS N N 116.137 0.05 1 98 30 30 ASP H H 6.777 0.005 1 99 30 30 ASP C C 176.129 0.05 1 100 30 30 ASP CA C 56.031 0.05 1 101 30 30 ASP CB C 39.494 0.05 1 102 30 30 ASP N N 114.152 0.05 1 103 31 31 THR H H 7.071 0.005 1 104 31 31 THR C C 175.479 0.05 1 105 31 31 THR CA C 63.200 0.05 1 106 31 31 THR CB C 68.894 0.05 1 107 31 31 THR N N 105.413 0.05 1 108 32 32 LEU H H 7.115 0.005 1 109 32 32 LEU C C 176.925 0.05 1 110 32 32 LEU CA C 54.530 0.05 1 111 32 32 LEU CB C 42.500 0.05 1 112 32 32 LEU N N 117.953 0.05 1 113 33 33 MET H H 7.209 0.005 1 114 33 33 MET C C 176.022 0.05 1 115 33 33 MET CA C 53.932 0.05 1 116 33 33 MET CB C 33.459 0.05 1 117 33 33 MET N N 119.587 0.05 1 118 34 34 ILE H H 8.271 0.005 1 119 34 34 ILE C C 175.070 0.05 1 120 34 34 ILE CA C 61.919 0.05 1 121 34 34 ILE CB C 37.076 0.05 1 122 34 34 ILE N N 123.632 0.05 1 123 35 35 SER H H 7.596 0.005 1 124 35 35 SER C C 174.667 0.05 1 125 35 35 SER CA C 57.998 0.05 1 126 35 35 SER CB C 62.438 0.05 1 127 35 35 SER N N 112.602 0.05 1 128 36 36 ARG H H 7.736 0.005 1 129 36 36 ARG C C 175.480 0.05 1 130 36 36 ARG CA C 54.682 0.05 1 131 36 36 ARG CB C 31.513 0.05 1 132 36 36 ARG N N 123.331 0.05 1 133 37 37 THR H H 8.467 0.005 1 134 37 37 THR CA C 58.661 0.05 1 135 37 37 THR CB C 69.743 0.05 1 136 37 37 THR N N 116.250 0.05 1 137 38 38 PRO C C 174.673 0.05 1 138 38 38 PRO CA C 60.790 0.05 1 139 38 38 PRO CB C 30.830 0.05 1 140 39 39 GLU H H 7.759 0.005 1 141 39 39 GLU C C 175.342 0.05 1 142 39 39 GLU CA C 53.620 0.05 1 143 39 39 GLU CB C 29.470 0.05 1 144 39 39 GLU N N 118.193 0.05 1 145 40 40 VAL H H 8.475 0.005 1 146 40 40 VAL C C 174.792 0.05 1 147 40 40 VAL CA C 60.290 0.05 1 148 40 40 VAL CB C 32.428 0.05 1 149 40 40 VAL N N 120.892 0.05 1 150 41 41 THR H H 7.907 0.005 1 151 41 41 THR C C 172.165 0.05 1 152 41 41 THR CA C 61.922 0.05 1 153 41 41 THR CB C 70.211 0.05 1 154 41 41 THR N N 119.859 0.05 1 155 42 42 CYS H H 9.958 0.005 1 156 42 42 CYS C C 171.782 0.05 1 157 42 42 CYS CA C 53.423 0.05 1 158 42 42 CYS CB C 43.433 0.05 1 159 42 42 CYS N N 130.708 0.05 1 160 43 43 VAL H H 9.488 0.005 1 161 43 43 VAL C C 173.749 0.05 1 162 43 43 VAL CA C 61.100 0.05 1 163 43 43 VAL CB C 34.373 0.05 1 164 43 43 VAL N N 127.436 0.05 1 165 44 44 VAL H H 9.306 0.005 1 166 44 44 VAL C C 174.820 0.05 1 167 44 44 VAL CA C 59.511 0.05 1 168 44 44 VAL CB C 32.323 0.05 1 169 44 44 VAL N N 127.672 0.05 1 170 45 45 VAL H H 8.859 0.005 1 171 45 45 VAL N N 119.735 0.05 1 172 46 46 ASP C C 175.000 0.05 1 173 46 46 ASP CA C 50.570 0.05 1 174 46 46 ASP CB C 43.500 0.05 1 175 47 47 VAL H H 8.134 0.005 1 176 47 47 VAL C C 174.343 0.05 1 177 47 47 VAL CA C 60.692 0.05 1 178 47 47 VAL CB C 34.018 0.05 1 179 47 47 VAL N N 122.900 0.05 1 180 48 48 SER H H 8.305 0.005 1 181 48 48 SER CA C 56.412 0.05 1 182 48 48 SER CB C 64.250 0.05 1 183 48 48 SER N N 118.837 0.05 1 184 49 49 HIS H H 8.205 0.005 1 185 49 49 HIS N N 121.706 0.05 1 186 50 50 GLU H H 7.728 0.005 1 187 50 50 GLU N N 119.009 0.05 1 188 51 51 ASP H H 9.055 0.005 1 189 51 51 ASP N N 125.210 0.05 1 190 54 54 VAL C C 174.280 0.05 1 191 54 54 VAL CA C 60.600 0.05 1 192 55 55 LYS H H 8.198 0.005 1 193 55 55 LYS C C 175.618 0.05 1 194 55 55 LYS CA C 54.208 0.05 1 195 55 55 LYS CB C 33.697 0.05 1 196 55 55 LYS N N 126.821 0.05 1 197 56 56 PHE H H 8.681 0.005 1 198 56 56 PHE C C 176.392 0.05 1 199 56 56 PHE CA C 56.619 0.05 1 200 56 56 PHE CB C 41.027 0.05 1 201 56 56 PHE N N 122.037 0.05 1 202 57 57 ASN H H 9.235 0.005 1 203 57 57 ASN C C 171.885 0.05 1 204 57 57 ASN CA C 53.349 0.05 1 205 57 57 ASN CB C 42.719 0.05 1 206 57 57 ASN N N 121.229 0.05 1 207 58 58 TRP H H 8.800 0.005 1 208 58 58 TRP C C 175.452 0.05 1 209 58 58 TRP CA C 55.456 0.05 1 210 58 58 TRP CB C 33.966 0.05 1 211 58 58 TRP N N 123.305 0.05 1 212 59 59 TYR H H 9.207 0.005 1 213 59 59 TYR C C 174.953 0.05 1 214 59 59 TYR CA C 55.258 0.05 1 215 59 59 TYR CB C 40.944 0.05 1 216 59 59 TYR N N 117.253 0.05 1 217 60 60 VAL H H 8.876 0.005 1 218 60 60 VAL C C 177.053 0.05 1 219 60 60 VAL CA C 60.755 0.05 1 220 60 60 VAL CB C 32.307 0.05 1 221 60 60 VAL N N 122.270 0.05 1 222 61 61 ASP H H 9.895 0.005 1 223 61 61 ASP C C 176.133 0.05 1 224 61 61 ASP CA C 55.135 0.05 1 225 61 61 ASP CB C 39.422 0.05 1 226 61 61 ASP N N 132.017 0.05 1 227 62 62 GLY H H 9.066 0.005 1 228 62 62 GLY C C 173.739 0.05 1 229 62 62 GLY CA C 45.169 0.05 1 230 62 62 GLY N N 102.732 0.05 1 231 63 63 VAL H H 7.903 0.005 1 232 63 63 VAL C C 175.599 0.05 1 233 63 63 VAL CA C 61.496 0.05 1 234 63 63 VAL CB C 32.285 0.05 1 235 63 63 VAL N N 124.615 0.05 1 236 64 64 GLU H H 8.927 0.005 1 237 64 64 GLU C C 176.395 0.05 1 238 64 64 GLU CA C 56.696 0.05 1 239 64 64 GLU CB C 28.123 0.05 1 240 64 64 GLU N N 129.884 0.05 1 241 65 65 VAL H H 8.210 0.005 1 242 65 65 VAL C C 176.919 0.05 1 243 65 65 VAL CA C 59.077 0.05 1 244 65 65 VAL CB C 33.749 0.05 1 245 65 65 VAL N N 119.478 0.05 1 246 66 66 HIS H H 8.852 0.005 1 247 66 66 HIS C C 174.814 0.05 1 248 66 66 HIS CA C 55.788 0.05 1 249 66 66 HIS CB C 29.566 0.05 1 250 66 66 HIS N N 118.180 0.05 1 251 67 67 ASN H H 8.156 0.005 1 252 67 67 ASN C C 174.949 0.05 1 253 67 67 ASN CA C 52.673 0.05 1 254 67 67 ASN CB C 36.831 0.05 1 255 67 67 ASN N N 116.137 0.05 1 256 68 68 ALA H H 8.067 0.005 1 257 68 68 ALA CA C 52.364 0.05 1 258 68 68 ALA CB C 19.731 0.05 1 259 68 68 ALA N N 124.428 0.05 1 260 69 69 LYS H H 8.486 0.005 1 261 69 69 LYS C C 174.416 0.05 1 262 69 69 LYS CA C 54.641 0.05 1 263 69 69 LYS CB C 33.827 0.05 1 264 69 69 LYS N N 121.178 0.05 1 265 70 70 THR H H 8.682 0.005 1 266 70 70 THR C C 174.813 0.05 1 267 70 70 THR CA C 61.830 0.05 1 268 70 70 THR CB C 69.000 0.05 1 269 70 70 THR N N 122.304 0.05 1 270 71 71 LYS H H 8.818 0.005 1 271 71 71 LYS CA C 54.556 0.05 1 272 71 71 LYS CB C 30.587 0.05 1 273 71 71 LYS N N 129.554 0.05 1 274 73 73 ARG C C 175.008 0.05 1 275 73 73 ARG CA C 56.000 0.05 1 276 73 73 ARG CB C 33.958 0.05 1 277 74 74 GLU H H 8.769 0.005 1 278 74 74 GLU C C 176.133 0.05 1 279 74 74 GLU CA C 54.170 0.05 1 280 74 74 GLU CB C 31.920 0.05 1 281 74 74 GLU N N 122.343 0.05 1 282 75 75 GLU H H 9.132 0.005 1 283 75 75 GLU C C 176.571 0.05 1 284 75 75 GLU CA C 56.756 0.05 1 285 75 75 GLU CB C 29.451 0.05 1 286 75 75 GLU N N 127.811 0.05 1 287 76 76 GLN H H 8.892 0.005 1 288 76 76 GLN C C 175.922 0.05 1 289 76 76 GLN CA C 54.062 0.05 1 290 76 76 GLN CB C 30.618 0.05 1 291 76 76 GLN N N 124.099 0.05 1 292 77 77 TYR H H 8.439 0.005 1 293 77 77 TYR CA C 59.060 0.05 1 294 77 77 TYR CB C 36.980 0.05 1 295 77 77 TYR N N 120.568 0.05 1 296 78 78 ASN H H 7.454 0.005 1 297 78 78 ASN C C 175.215 0.05 1 298 78 78 ASN CA C 51.881 0.05 1 299 78 78 ASN CB C 36.308 0.05 1 300 78 78 ASN N N 118.103 0.05 1 301 79 79 SER H H 7.994 0.005 1 302 79 79 SER C C 173.351 0.05 1 303 79 79 SER CA C 59.540 0.05 1 304 79 79 SER CB C 61.106 0.05 1 305 79 79 SER N N 111.023 0.05 1 306 80 80 THR H H 6.874 0.005 1 307 80 80 THR N N 108.388 0.05 1 308 81 81 TYR H H 9.285 0.005 1 309 81 81 TYR C C 174.800 0.05 1 310 81 81 TYR N N 116.488 0.05 1 311 82 82 ARG H H 9.045 0.005 1 312 82 82 ARG C C 175.464 0.05 1 313 82 82 ARG N N 123.762 0.05 1 314 83 83 VAL H H 9.350 0.005 1 315 83 83 VAL C C 173.654 0.05 1 316 83 83 VAL N N 126.787 0.05 1 317 84 84 VAL H H 8.339 0.005 1 318 84 84 VAL C C 173.744 0.05 1 319 84 84 VAL CA C 60.752 0.05 1 320 84 84 VAL CB C 34.330 0.05 1 321 84 84 VAL N N 127.533 0.05 1 322 85 85 SER H H 8.897 0.005 1 323 85 85 SER C C 173.731 0.05 1 324 85 85 SER CA C 55.700 0.05 1 325 85 85 SER CB C 62.189 0.05 1 326 85 85 SER N N 121.169 0.05 1 327 86 86 VAL H H 8.639 0.005 1 328 86 86 VAL C C 174.009 0.05 1 329 86 86 VAL CA C 60.076 0.05 1 330 86 86 VAL CB C 34.037 0.05 1 331 86 86 VAL N N 126.360 0.05 1 332 87 87 LEU H H 8.508 0.005 1 333 87 87 LEU C C 175.479 0.05 1 334 87 87 LEU CA C 52.286 0.05 1 335 87 87 LEU CB C 42.282 0.05 1 336 87 87 LEU N N 130.692 0.05 1 337 88 88 THR H H 7.932 0.005 1 338 88 88 THR C C 174.014 0.05 1 339 88 88 THR CA C 62.965 0.05 1 340 88 88 THR CB C 68.285 0.05 1 341 88 88 THR N N 123.132 0.05 1 342 89 89 VAL H H 7.847 0.005 1 343 89 89 VAL C C 174.863 0.05 1 344 89 89 VAL CA C 58.463 0.05 1 345 89 89 VAL CB C 33.012 0.05 1 346 89 89 VAL N N 121.198 0.05 1 347 90 90 LEU H H 8.441 0.005 1 348 90 90 LEU C C 178.643 0.05 1 349 90 90 LEU CA C 54.179 0.05 1 350 90 90 LEU CB C 39.979 0.05 1 351 90 90 LEU N N 122.824 0.05 1 352 91 91 HIS H H 8.933 0.005 1 353 91 91 HIS C C 177.185 0.05 1 354 91 91 HIS CA C 61.337 0.05 1 355 91 91 HIS CB C 29.326 0.05 1 356 91 91 HIS N N 123.921 0.05 1 357 92 92 GLN H H 9.176 0.005 1 358 92 92 GLN C C 177.720 0.05 1 359 92 92 GLN CA C 57.628 0.05 1 360 92 92 GLN CB C 27.673 0.05 1 361 92 92 GLN N N 113.916 0.05 1 362 93 93 ASP H H 6.916 0.005 1 363 93 93 ASP C C 177.586 0.05 1 364 93 93 ASP CA C 56.973 0.05 1 365 93 93 ASP CB C 40.063 0.05 1 366 93 93 ASP N N 120.066 0.05 1 367 94 94 TRP H H 7.636 0.005 1 368 94 94 TRP C C 180.044 0.05 1 369 94 94 TRP CA C 51.417 0.05 1 370 94 94 TRP CB C 28.08 0.05 1 371 94 94 TRP N N 119.176 0.05 1 372 95 95 LEU H H 8.208 0.005 1 373 95 95 LEU C C 178.151 0.05 1 374 95 95 LEU CA C 57.126 0.05 1 375 95 95 LEU CB C 40.077 0.05 1 376 95 95 LEU N N 116.322 0.05 1 377 96 96 ASN H H 7.950 0.005 1 378 96 96 ASN C C 176.504 0.05 1 379 96 96 ASN CA C 52.816 0.05 1 380 96 96 ASN CB C 37.709 0.05 1 381 96 96 ASN N N 116.299 0.05 1 382 97 97 GLY H H 7.674 0.005 1 383 97 97 GLY C C 175.323 0.05 1 384 97 97 GLY CA C 46.433 0.05 1 385 97 97 GLY N N 107.750 0.05 1 386 98 98 LYS H H 7.404 0.005 1 387 98 98 LYS C C 174.816 0.05 1 388 98 98 LYS CA C 58.021 0.05 1 389 98 98 LYS CB C 31.342 0.05 1 390 98 98 LYS N N 118.977 0.05 1 391 99 99 GLU H H 8.453 0.005 1 392 99 99 GLU C C 175.610 0.05 1 393 99 99 GLU CA C 55.018 0.05 1 394 99 99 GLU CB C 31.338 0.05 1 395 99 99 GLU N N 119.707 0.05 1 396 100 100 TYR H H 9.093 0.005 1 397 100 100 TYR C C 174.147 0.05 1 398 100 100 TYR CA C 57.821 0.05 1 399 100 100 TYR CB C 39.889 0.05 1 400 100 100 TYR N N 127.435 0.05 1 401 101 101 LYS H H 9.388 0.005 1 402 101 101 LYS C C 173.780 0.05 1 403 101 101 LYS CA C 53.656 0.05 1 404 101 101 LYS CB C 35.696 0.05 1 405 101 101 LYS N N 124.281 0.05 1 406 102 102 CYS H H 8.663 0.005 1 407 102 102 CYS C C 171.216 0.05 1 408 102 102 CYS CA C 60.658 0.05 1 409 102 102 CYS CB C 33.961 0.05 1 410 102 102 CYS N N 125.723 0.05 1 411 103 103 LYS H H 9.072 0.005 1 412 103 103 LYS C C 174.513 0.05 1 413 103 103 LYS CA C 53.750 0.05 1 414 103 103 LYS CB C 33.960 0.05 1 415 103 103 LYS N N 128.890 0.05 1 416 104 104 VAL H H 9.175 0.005 1 417 104 104 VAL C C 174.294 0.05 1 418 104 104 VAL CA C 61.369 0.05 1 419 104 104 VAL CB C 34.020 0.05 1 420 104 104 VAL N N 128.902 0.05 1 421 105 105 SER H H 8.306 0.005 1 422 105 105 SER C C 174.481 0.05 1 423 105 105 SER N N 118.582 0.05 1 424 106 106 ASN C C 174.481 0.05 1 425 107 107 LYS H H 8.679 0.005 1 426 107 107 LYS C C 175.036 0.05 1 427 107 107 LYS N N 122.037 0.05 1 428 108 108 ALA H H 8.444 0.005 1 429 108 108 ALA CA C 50.169 0.05 1 430 108 108 ALA CB C 17.318 0.05 1 431 108 108 ALA N N 124.628 0.05 1 432 111 111 ALA H H 7.235 0.005 1 433 111 111 ALA CA C 49.232 0.05 1 434 111 111 ALA CB C 19.036 0.05 1 435 111 111 ALA N N 118.652 0.05 1 436 112 112 PRO C C 176.392 0.05 1 437 112 112 PRO CA C 62.570 0.05 1 438 112 112 PRO CB C 31.450 0.05 1 439 113 113 ILE H H 8.355 0.005 1 440 113 113 ILE C C 174.523 0.05 1 441 113 113 ILE CA C 59.897 0.05 1 442 113 113 ILE CB C 39.696 0.05 1 443 113 113 ILE N N 122.958 0.05 1 444 114 114 GLU H H 8.478 0.005 1 445 114 114 GLU C C 175.506 0.05 1 446 114 114 GLU CA C 53.753 0.05 1 447 114 114 GLU CB C 32.337 0.05 1 448 114 114 GLU N N 124.302 0.05 1 449 115 115 LYS H H 8.613 0.005 1 450 115 115 LYS C C 174.302 0.05 1 451 115 115 LYS CA C 53.497 0.05 1 452 115 115 LYS CB C 35.972 0.05 1 453 115 115 LYS N N 122.746 0.05 1 454 116 116 THR H H 8.236 0.005 1 455 116 116 THR C C 174.285 0.05 1 456 116 116 THR CA C 59.829 0.05 1 457 116 116 THR CB C 71.321 0.05 1 458 116 116 THR N N 113.699 0.05 1 459 117 117 ILE H H 9.359 0.005 1 460 117 117 ILE C C 171.904 0.05 1 461 117 117 ILE CA C 59.797 0.05 1 462 117 117 ILE CB C 41.927 0.05 1 463 117 117 ILE N N 122.184 0.05 1 464 118 118 SER H H 7.677 0.005 1 465 118 118 SER C C 172.942 0.05 1 466 118 118 SER CA C 57.024 0.05 1 467 118 118 SER CB C 65.529 0.05 1 468 118 118 SER N N 115.224 0.05 1 469 119 119 LYS H H 8.688 0.005 1 470 119 119 LYS CA C 56.115 0.05 1 471 119 119 LYS CB C 30.601 0.05 1 472 119 119 LYS N N 125.498 0.05 1 473 120 120 ALA H H 8.624 0.005 1 474 120 120 ALA C C 177.710 0.05 1 475 120 120 ALA CA C 52.936 0.05 1 476 120 120 ALA CB C 18.416 0.05 1 477 120 120 ALA N N 129.602 0.05 1 478 121 121 LYS H H 8.400 0.005 1 479 121 121 LYS C C 177.647 0.05 1 480 121 121 LYS CA C 55.638 0.05 1 481 121 121 LYS CB C 32.990 0.05 1 482 121 121 LYS N N 121.184 0.05 1 483 122 122 GLY H H 8.532 0.005 1 484 122 122 GLY C C 173.111 0.05 1 485 122 122 GLY CA C 43.586 0.05 1 486 122 122 GLY N N 111.997 0.05 1 487 123 123 GLN H H 8.187 0.005 1 488 123 123 GLN CA C 53.507 0.05 1 489 123 123 GLN CB C 28.535 0.05 1 490 123 123 GLN N N 122.755 0.05 1 491 124 124 PRO C C 176.785 0.05 1 492 124 124 PRO CA C 62.820 0.05 1 493 124 124 PRO CB C 32.160 0.05 1 494 125 125 ARG H H 9.417 0.005 1 495 125 125 ARG C C 174.946 0.05 1 496 125 125 ARG CA C 54.804 0.05 1 497 125 125 ARG CB C 33.637 0.05 1 498 125 125 ARG N N 122.913 0.05 1 499 126 126 GLU H H 8.588 0.005 1 500 126 126 GLU CA C 53.482 0.05 1 501 126 126 GLU CB C 33.620 0.05 1 502 126 126 GLU N N 124.363 0.05 1 503 127 127 PRO C C 175.505 0.05 1 504 127 127 PRO CA C 61.970 0.05 1 505 127 127 PRO CB C 31.320 0.05 1 506 128 128 GLN H H 8.978 0.005 1 507 128 128 GLN C C 174.157 0.05 1 508 128 128 GLN CA C 53.816 0.05 1 509 128 128 GLN CB C 29.467 0.05 1 510 128 128 GLN N N 121.050 0.05 1 511 129 129 VAL H H 7.810 0.005 1 512 129 129 VAL C C 173.367 0.05 1 513 129 129 VAL CA C 60.762 0.05 1 514 129 129 VAL CB C 32.411 0.05 1 515 129 129 VAL N N 122.684 0.05 1 516 130 130 TYR H H 9.319 0.005 1 517 130 130 TYR C C 174.682 0.05 1 518 130 130 TYR CA C 55.042 0.05 1 519 130 130 TYR CB C 40.916 0.05 1 520 130 130 TYR N N 125.292 0.05 1 521 131 131 THR H H 8.626 0.005 1 522 131 131 THR C C 174.222 0.05 1 523 131 131 THR CA C 58.222 0.05 1 524 131 131 THR CB C 69.162 0.05 1 525 131 131 THR N N 112.709 0.05 1 526 132 132 LEU H H 9.437 0.005 1 527 132 132 LEU CA C 50.886 0.05 1 528 132 132 LEU CB C 42.059 0.05 1 529 132 132 LEU N N 124.579 0.05 1 530 134 134 PRO C C 177.583 0.05 1 531 134 134 PRO CA C 61.770 0.05 1 532 134 134 PRO CB C 30.100 0.05 1 533 135 135 SER H H 8.885 0.005 1 534 135 135 SER C C 176.953 0.05 1 535 135 135 SER CA C 56.998 0.05 1 536 135 135 SER CB C 62.872 0.05 1 537 135 135 SER N N 118.302 0.05 1 538 136 136 ARG H H 9.029 0.005 1 539 136 136 ARG C C 179.018 0.05 1 540 136 136 ARG CA C 58.951 0.05 1 541 136 136 ARG CB C 28.853 0.05 1 542 136 136 ARG N N 128.822 0.05 1 543 137 137 ASP H H 8.337 0.005 1 544 137 137 ASP C C 177.221 0.05 1 545 137 137 ASP CA C 56.048 0.05 1 546 137 137 ASP CB C 40.237 0.05 1 547 137 137 ASP N N 118.130 0.05 1 548 138 138 GLU H H 7.656 0.005 1 549 138 138 GLU C C 177.051 0.05 1 550 138 138 GLU CA C 55.573 0.05 1 551 138 138 GLU CB C 30.115 0.05 1 552 138 138 GLU N N 122.350 0.05 1 553 139 139 LEU H H 7.148 0.005 1 554 139 139 LEU C C 176.201 0.05 1 555 139 139 LEU CA C 56.050 0.05 1 556 139 139 LEU CB C 39.902 0.05 1 557 139 139 LEU N N 114.720 0.05 1 558 140 140 THR H H 6.952 0.005 1 559 140 140 THR C C 175.445 0.05 1 560 140 140 THR CA C 61.961 0.05 1 561 140 140 THR CB C 68.416 0.05 1 562 140 140 THR N N 107.254 0.05 1 563 141 141 LYS H H 7.855 0.005 1 564 141 141 LYS C C 176.060 0.05 1 565 141 141 LYS CA C 53.730 0.05 1 566 141 141 LYS CB C 31.902 0.05 1 567 141 141 LYS N N 122.865 0.05 1 568 142 142 ASN H H 8.387 0.005 1 569 142 142 ASN C C 176.061 0.05 1 570 142 142 ASN CA C 54.282 0.05 1 571 142 142 ASN CB C 38.027 0.05 1 572 142 142 ASN N N 114.598 0.05 1 573 143 143 GLN H H 7.397 0.005 1 574 143 143 GLN C C 173.884 0.05 1 575 143 143 GLN CA C 54.340 0.05 1 576 143 143 GLN CB C 31.134 0.05 1 577 143 143 GLN N N 118.491 0.05 1 578 144 144 VAL H H 8.628 0.005 1 579 144 144 VAL C C 173.333 0.05 1 580 144 144 VAL CA C 57.591 0.05 1 581 144 144 VAL CB C 33.822 0.05 1 582 144 144 VAL N N 111.286 0.05 1 583 145 145 SER H H 8.803 0.005 1 584 145 145 SER C C 172.771 0.05 1 585 145 145 SER CA C 57.135 0.05 1 586 145 145 SER CB C 61.201 0.05 1 587 145 145 SER N N 115.066 0.05 1 588 146 146 LEU H H 9.273 0.005 1 589 146 146 LEU C C 175.336 0.05 1 590 146 146 LEU CA C 53.175 0.05 1 591 146 146 LEU CB C 40.205 0.05 1 592 146 146 LEU N N 129.302 0.05 1 593 147 147 THR H H 7.906 0.005 1 594 147 147 THR C C 172.578 0.05 1 595 147 147 THR CA C 62.441 0.05 1 596 147 147 THR CB C 70.222 0.05 1 597 147 147 THR N N 118.250 0.05 1 598 148 148 CYS H H 9.742 0.005 1 599 148 148 CYS CA C 53.409 0.05 1 600 148 148 CYS CB C 41.728 0.05 1 601 148 148 CYS N N 129.213 0.05 1 602 149 149 LEU H H 9.397 0.005 1 603 149 149 LEU C C 172.489 0.05 1 604 149 149 LEU CA C 53.365 0.05 1 605 149 149 LEU CB C 41.431 0.05 1 606 149 149 LEU N N 131.760 0.05 1 607 150 150 VAL H H 8.257 0.005 1 608 150 150 VAL C C 175.099 0.05 1 609 150 150 VAL CA C 59.929 0.05 1 610 150 150 VAL CB C 31.348 0.05 1 611 150 150 VAL N N 127.570 0.05 1 612 151 151 LYS H H 9.252 0.005 1 613 151 151 LYS C C 174.818 0.05 1 614 151 151 LYS CA C 54.092 0.05 1 615 151 151 LYS CB C 35.394 0.05 1 616 151 151 LYS N N 122.768 0.05 1 617 152 152 GLY H H 8.252 0.005 1 618 152 152 GLY C C 174.287 0.05 1 619 152 152 GLY CA C 45.345 0.05 1 620 152 152 GLY N N 111.447 0.05 1 621 153 153 PHE H H 7.751 0.005 1 622 153 153 PHE C C 174.618 0.05 1 623 153 153 PHE CA C 53.898 0.05 1 624 153 153 PHE CB C 40.976 0.05 1 625 153 153 PHE N N 111.860 0.05 1 626 154 154 TYR H H 8.276 0.005 1 627 154 154 TYR CA C 58.694 0.05 1 628 154 154 TYR CB C 41.984 0.05 1 629 154 154 TYR N N 120.309 0.05 1 630 155 155 PRO C C 176.037 0.05 1 631 155 155 PRO CA C 62.240 0.05 1 632 155 155 PRO CB C 33.830 0.05 1 633 156 156 SER H H 8.301 0.005 1 634 156 156 SER C C 173.044 0.05 1 635 156 156 SER CA C 59.763 0.05 1 636 156 156 SER CB C 60.864 0.05 1 637 156 156 SER N N 112.486 0.05 1 638 157 157 ASP H H 6.753 0.005 1 639 157 157 ASP C C 173.076 0.05 1 640 157 157 ASP CA C 54.440 0.05 1 641 157 157 ASP CB C 40.427 0.05 1 642 157 157 ASP N N 120.875 0.05 1 643 158 158 ILE H H 7.943 0.005 1 644 158 158 ILE CA C 59.997 0.05 1 645 158 158 ILE CB C 40.431 0.05 1 646 158 158 ILE N N 124.184 0.05 1 647 159 159 ALA H H 8.097 0.005 1 648 159 159 ALA C C 173.731 0.05 1 649 159 159 ALA CA C 50.569 0.05 1 650 159 159 ALA CB C 21.403 0.05 1 651 159 159 ALA N N 126.686 0.05 1 652 160 160 VAL H H 8.128 0.005 1 653 160 160 VAL C C 174.690 0.05 1 654 160 160 VAL CA C 60.629 0.05 1 655 160 160 VAL CB C 33.935 0.05 1 656 160 160 VAL N N 122.469 0.05 1 657 161 161 GLU H H 8.826 0.005 1 658 161 161 GLU C C 172.815 0.05 1 659 161 161 GLU CA C 54.236 0.05 1 660 161 161 GLU CB C 33.248 0.05 1 661 161 161 GLU N N 126.174 0.05 1 662 162 162 TRP H H 7.651 0.005 1 663 162 162 TRP C C 176.523 0.05 1 664 162 162 TRP CA C 55.285 0.05 1 665 162 162 TRP CB C 33.321 0.05 1 666 162 162 TRP N N 121.275 0.05 1 667 163 163 GLU H H 9.074 0.005 1 668 163 163 GLU C C 175.060 0.05 1 669 163 163 GLU CA C 54.775 0.05 1 670 163 163 GLU CB C 33.653 0.05 1 671 163 163 GLU N N 118.614 0.05 1 672 164 164 SER H H 8.889 0.005 1 673 164 164 SER C C 175.568 0.05 1 674 164 164 SER CA C 57.628 0.05 1 675 164 164 SER CB C 63.996 0.05 1 676 164 164 SER N N 113.376 0.05 1 677 165 165 ASN H H 9.453 0.005 1 678 165 165 ASN C C 175.360 0.05 1 679 165 165 ASN CA C 53.834 0.05 1 680 165 165 ASN CB C 36.922 0.05 1 681 165 165 ASN N N 127.151 0.05 1 682 166 166 GLY H H 8.722 0.005 1 683 166 166 GLY C C 173.752 0.05 1 684 166 166 GLY CA C 45.063 0.05 1 685 166 166 GLY N N 104.168 0.05 1 686 167 167 GLN H H 7.900 0.005 1 687 167 167 GLN CA C 51.784 0.05 1 688 167 167 GLN CB C 29.238 0.05 1 689 167 167 GLN N N 120.352 0.05 1 690 168 168 PRO C C 177.321 0.05 1 691 168 168 PRO CA C 63.380 0.05 1 692 169 169 GLU H H 8.062 0.005 1 693 169 169 GLU CA C 54.573 0.05 1 694 169 169 GLU CB C 31.233 0.05 1 695 169 169 GLU N N 123.913 0.05 1 696 171 171 ASN C C 173.196 0.05 1 697 172 172 TYR H H 7.549 0.005 1 698 172 172 TYR C C 174.028 0.05 1 699 172 172 TYR CA C 54.222 0.05 1 700 172 172 TYR CB C 42.397 0.05 1 701 172 172 TYR N N 115.911 0.05 1 702 173 173 LYS H H 8.415 0.005 1 703 173 173 LYS C C 174.932 0.05 1 704 173 173 LYS CA C 53.824 0.05 1 705 173 173 LYS CB C 37.996 0.05 1 706 173 173 LYS N N 119.446 0.05 1 707 174 174 THR H H 9.141 0.005 1 708 174 174 THR C C 174.282 0.05 1 709 174 174 THR CA C 60.445 0.05 1 710 174 174 THR CB C 70.182 0.05 1 711 174 174 THR N N 121.589 0.05 1 712 175 175 THR H H 9.544 0.005 1 713 175 175 THR CA C 61.257 0.05 1 714 175 175 THR CB C 68.026 0.05 1 715 175 175 THR N N 118.677 0.05 1 716 177 177 PRO C C 176.685 0.05 1 717 177 177 PRO CA C 61.980 0.05 1 718 177 177 PRO CB C 31.100 0.05 1 719 178 178 VAL H H 9.269 0.005 1 720 178 178 VAL C C 174.291 0.05 1 721 178 178 VAL CA C 60.357 0.05 1 722 178 178 VAL CB C 32.853 0.05 1 723 178 178 VAL N N 127.094 0.05 1 724 179 179 LEU H H 8.361 0.005 1 725 179 179 LEU C C 175.435 0.05 1 726 179 179 LEU CA C 55.380 0.05 1 727 179 179 LEU CB C 41.297 0.05 1 728 179 179 LEU N N 128.322 0.05 1 729 180 180 ASP H H 9.542 0.005 1 730 180 180 ASP C C 178.351 0.05 1 731 180 180 ASP CA C 51.036 0.05 1 732 180 180 ASP CB C 43.011 0.05 1 733 180 180 ASP N N 129.330 0.05 1 734 181 181 SER H H 9.775 0.005 1 735 181 181 SER C C 174.311 0.05 1 736 181 181 SER CA C 59.985 0.05 1 737 181 181 SER CB C 62.480 0.05 1 738 181 181 SER N N 116.798 0.05 1 739 182 182 ASP H H 7.543 0.005 1 740 182 182 ASP C C 177.574 0.05 1 741 182 182 ASP CA C 52.154 0.05 1 742 182 182 ASP CB C 39.795 0.05 1 743 182 182 ASP N N 118.031 0.05 1 744 183 183 GLY H H 7.639 0.005 1 745 183 183 GLY C C 172.865 0.05 1 746 183 183 GLY CA C 45.189 0.05 1 747 183 183 GLY N N 108.215 0.05 1 748 184 184 SER H H 7.503 0.005 1 749 184 184 SER C C 170.549 0.05 1 750 184 184 SER CA C 56.641 0.05 1 751 184 184 SER CB C 64.268 0.05 1 752 184 184 SER N N 115.427 0.05 1 753 185 185 PHE H H 8.701 0.005 1 754 185 185 PHE C C 174.343 0.05 1 755 185 185 PHE CA C 56.932 0.05 1 756 185 185 PHE CB C 42.100 0.05 1 757 185 185 PHE N N 115.903 0.05 1 758 186 186 PHE H H 8.678 0.005 1 759 186 186 PHE C C 172.498 0.05 1 760 186 186 PHE CA C 55.310 0.05 1 761 186 186 PHE CB C 42.308 0.05 1 762 186 186 PHE N N 112.001 0.05 1 763 187 187 LEU H H 9.540 0.005 1 764 187 187 LEU C C 174.394 0.05 1 765 187 187 LEU CA C 54.419 0.05 1 766 187 187 LEU CB C 43.806 0.05 1 767 187 187 LEU N N 115.031 0.05 1 768 188 188 TYR H H 8.019 0.005 1 769 188 188 TYR C C 175.088 0.05 1 770 188 188 TYR CA C 56.334 0.05 1 771 188 188 TYR CB C 44.440 0.05 1 772 188 188 TYR N N 115.899 0.05 1 773 189 189 SER H H 9.343 0.005 1 774 189 189 SER C C 173.237 0.05 1 775 189 189 SER CA C 56.641 0.05 1 776 189 189 SER CB C 64.445 0.05 1 777 189 189 SER N N 114.951 0.05 1 778 190 190 LYS H H 9.508 0.005 1 779 190 190 LYS C C 175.193 0.05 1 780 190 190 LYS CA C 54.897 0.05 1 781 190 190 LYS CB C 33.363 0.05 1 782 190 190 LYS N N 131.772 0.05 1 783 191 191 LEU H H 9.224 0.005 1 784 191 191 LEU C C 174.693 0.05 1 785 191 191 LEU CA C 53.126 0.05 1 786 191 191 LEU CB C 39.600 0.05 1 787 191 191 LEU N N 134.990 0.05 1 788 192 192 THR H H 8.192 0.005 1 789 192 192 THR C C 173.751 0.05 1 790 192 192 THR CA C 61.719 0.05 1 791 192 192 THR CB C 68.469 0.05 1 792 192 192 THR N N 125.749 0.05 1 793 193 193 VAL H H 8.365 0.005 1 794 193 193 VAL C C 174.650 0.05 1 795 193 193 VAL CA C 57.680 0.05 1 796 193 193 VAL CB C 35.435 0.05 1 797 193 193 VAL N N 119.934 0.05 1 798 194 194 ASP H H 8.470 0.005 1 799 194 194 ASP C C 177.436 0.05 1 800 194 194 ASP CA C 55.063 0.05 1 801 194 194 ASP CB C 40.581 0.05 1 802 194 194 ASP N N 123.657 0.05 1 803 195 195 LYS H H 8.664 0.005 1 804 195 195 LYS C C 178.080 0.05 1 805 195 195 LYS CA C 60.200 0.05 1 806 195 195 LYS CB C 30.510 0.05 1 807 195 195 LYS N N 127.313 0.05 1 808 196 196 SER H H 8.769 0.005 1 809 196 196 SER C C 176.337 0.05 1 810 196 196 SER CA C 60.767 0.05 1 811 196 196 SER N N 113.926 0.05 1 812 197 197 ARG H H 7.340 0.005 1 813 197 197 ARG C C 179.280 0.05 1 814 197 197 ARG CA C 58.750 0.05 1 815 197 197 ARG CB C 30.425 0.05 1 816 197 197 ARG N N 120.767 0.05 1 817 198 198 TRP H H 9.016 0.005 1 818 198 198 TRP C C 177.719 0.05 1 819 198 198 TRP CA C 58.829 0.05 1 820 198 198 TRP CB C 30.425 0.05 1 821 198 198 TRP N N 124.836 0.05 1 822 199 199 GLN H H 8.542 0.005 1 823 199 199 GLN C C 176.782 0.05 1 824 199 199 GLN CA C 57.611 0.05 1 825 199 199 GLN CB C 28.316 0.05 1 826 199 199 GLN N N 115.700 0.05 1 827 200 200 GLN H H 7.640 0.005 1 828 200 200 GLN C C 176.851 0.05 1 829 200 200 GLN CA C 55.971 0.05 1 830 200 200 GLN CB C 28.154 0.05 1 831 200 200 GLN N N 115.958 0.05 1 832 201 201 GLY H H 7.477 0.005 1 833 201 201 GLY C C 174.946 0.05 1 834 201 201 GLY CA C 45.712 0.05 1 835 201 201 GLY N N 105.413 0.05 1 836 202 202 ASN H H 6.778 0.005 1 837 202 202 ASN C C 173.086 0.05 1 838 202 202 ASN CA C 54.130 0.05 1 839 202 202 ASN CB C 39.369 0.05 1 840 202 202 ASN N N 116.562 0.05 1 841 203 203 VAL H H 8.321 0.005 1 842 203 203 VAL C C 175.745 0.05 1 843 203 203 VAL CA C 61.596 0.05 1 844 203 203 VAL CB C 31.680 0.05 1 845 203 203 VAL N N 121.569 0.05 1 846 204 204 PHE H H 9.041 0.005 1 847 204 204 PHE C C 174.942 0.05 1 848 204 204 PHE CA C 56.880 0.05 1 849 204 204 PHE CB C 41.932 0.05 1 850 204 204 PHE N N 129.207 0.05 1 851 205 205 SER H H 9.471 0.005 1 852 205 205 SER C C 171.370 0.05 1 853 205 205 SER CA C 56.996 0.05 1 854 205 205 SER CB C 64.344 0.05 1 855 205 205 SER N N 115.639 0.05 1 856 206 206 CYS H H 8.664 0.005 1 857 206 206 CYS C C 172.189 0.05 1 858 206 206 CYS CA C 52.283 0.05 1 859 206 206 CYS CB C 40.495 0.05 1 860 206 206 CYS N N 126.356 0.05 1 861 207 207 SER H H 8.783 0.005 1 862 207 207 SER C C 172.300 0.05 1 863 207 207 SER CA C 56.516 0.05 1 864 207 207 SER CB C 63.671 0.05 1 865 207 207 SER N N 124.071 0.05 1 866 208 208 VAL H H 8.357 0.005 1 867 208 208 VAL C C 173.627 0.05 1 868 208 208 VAL CA C 60.001 0.05 1 869 208 208 VAL CB C 34.537 0.05 1 870 208 208 VAL N N 123.875 0.05 1 871 209 209 MET H H 8.694 0.005 1 872 209 209 MET C C 173.621 0.05 1 873 209 209 MET CA C 53.936 0.05 1 874 209 209 MET CB C 35.962 0.05 1 875 209 209 MET N N 123.531 0.05 1 876 210 210 HIS H H 6.978 0.005 1 877 210 210 HIS C C 175.179 0.05 1 878 210 210 HIS CA C 57.335 0.05 1 879 210 210 HIS CB C 35.845 0.05 1 880 210 210 HIS N N 120.389 0.05 1 881 211 211 GLU H H 8.621 0.005 1 882 211 211 GLU C C 175.184 0.05 1 883 211 211 GLU CA C 58.475 0.05 1 884 211 211 GLU CB C 29.165 0.05 1 885 211 211 GLU N N 127.143 0.05 1 886 212 212 ALA H H 10.465 0.005 1 887 212 212 ALA C C 177.980 0.05 1 888 212 212 ALA CA C 51.739 0.05 1 889 212 212 ALA CB C 18.150 0.05 1 890 212 212 ALA N N 124.577 0.05 1 891 213 213 LEU H H 7.146 0.005 1 892 213 213 LEU C C 179.038 0.05 1 893 213 213 LEU CA C 53.381 0.05 1 894 213 213 LEU CB C 43.480 0.05 1 895 213 213 LEU N N 116.957 0.05 1 896 214 214 HIS H H 9.370 0.005 1 897 214 214 HIS CA C 57.253 0.05 1 898 214 214 HIS CB C 27.244 0.05 1 899 214 214 HIS N N 126.029 0.05 1 900 215 215 ASN H H 9.067 0.005 1 901 215 215 ASN C C 173.376 0.05 1 902 215 215 ASN CA C 54.380 0.05 1 903 215 215 ASN N N 122.583 0.05 1 904 216 216 HIS H H 8.443 0.005 1 905 216 216 HIS C C 173.226 0.05 1 906 216 216 HIS CA C 54.401 0.05 1 907 216 216 HIS CB C 27.072 0.05 1 908 216 216 HIS N N 108.935 0.05 1 909 217 217 TYR H H 7.306 0.005 1 910 217 217 TYR C C 174.026 0.05 1 911 217 217 TYR CA C 57.842 0.05 1 912 217 217 TYR CB C 42.228 0.05 1 913 217 217 TYR N N 119.149 0.05 1 914 218 218 THR H H 8.247 0.005 1 915 218 218 THR C C 169.405 0.05 1 916 218 218 THR CA C 60.681 0.05 1 917 218 218 THR CB C 68.993 0.05 1 918 218 218 THR N N 122.264 0.05 1 919 219 219 GLN H H 7.638 0.005 1 920 219 219 GLN C C 174.283 0.05 1 921 219 219 GLN CA C 53.665 0.05 1 922 219 219 GLN CB C 32.180 0.05 1 923 219 219 GLN N N 120.537 0.05 1 924 220 220 LYS H H 8.443 0.005 1 925 220 220 LYS C C 175.163 0.05 1 926 220 220 LYS CA C 53.390 0.05 1 927 220 220 LYS CB C 35.790 0.05 1 928 220 220 LYS N N 123.831 0.05 1 929 221 221 SER H H 8.636 0.005 1 930 221 221 SER C C 174.026 0.05 1 931 221 221 SER CA C 57.693 0.05 1 932 221 221 SER CB C 65.399 0.05 1 933 221 221 SER N N 118.944 0.05 1 934 222 222 LEU H H 9.457 0.005 1 935 222 222 LEU C C 173.892 0.05 1 936 222 222 LEU CA C 55.212 0.05 1 937 222 222 LEU CB C 44.339 0.05 1 938 222 222 LEU N N 124.868 0.05 1 939 223 223 SER H H 8.278 0.005 1 940 223 223 SER C C 173.100 0.05 1 941 223 223 SER CA C 57.450 0.05 1 942 223 223 SER CB C 65.593 0.05 1 943 223 223 SER N N 116.180 0.05 1 944 224 224 LEU H H 8.700 0.005 1 945 224 224 LEU C C 177.067 0.05 1 946 224 224 LEU CA C 55.268 0.05 1 947 224 224 LEU CB C 40.916 0.05 1 948 224 224 LEU N N 125.147 0.05 1 949 225 225 SER H H 8.189 0.005 1 950 225 225 SER CA C 59.077 0.05 1 951 225 225 SER CB C 59.077 0.05 1 952 225 225 SER N N 119.676 0.05 1 953 226 226 PRO C C 177.586 0.05 1 954 226 226 PRO CA C 63.070 0.05 1 955 226 226 PRO CB C 31.360 0.05 1 956 227 227 GLY H H 8.342 0.005 1 957 227 227 GLY C C 173.226 0.05 1 958 227 227 GLY CA C 44.955 0.05 1 959 227 227 GLY N N 110.166 0.05 1 960 228 228 LYS H H 7.740 0.005 1 961 228 228 LYS CA C 56.988 0.05 1 962 228 228 LYS CB C 32.787 0.05 1 963 228 228 LYS N N 126.121 0.05 1 stop_ save_