data_5305 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl-prolyl cis-trans isomerase Pin1 ; _BMRB_accession_number 5305 _BMRB_flat_file_name bmr5305.str _Entry_type original _Submission_date 2002-02-26 _Accession_date 2002-02-26 _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 Jacobs Doris M. . 2 Saxena Krishna . . 3 Grimme Susanne . . 4 Vogtherr Martin . . 5 Pescatore Barbara . . 6 Langer Thomas . . 7 Elshorst Bettina . . 8 Fiebig Klaus M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 313 "13C chemical shifts" 462 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22147550 _PubMed_ID 12153046 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacobs Doris M. . 2 Saxena Krishna . . 3 Grimme Susanne . . 4 Vogtherr Martin . . 5 Pescatore Barbara . . 6 Langer Thomas . . 7 Elshorst Bettina . . 8 Fiebig Klaus M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 163 _Page_last 164 _Year 2002 _Details . loop_ _Keyword Pin1 PPIase 'peptidyl-prolyl cis-trans isomerase' stop_ save_ ################################## # Molecular system description # ################################## save_system_Pin1 _Saveframe_category molecular_system _Mol_system_name 'Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1' _Abbreviation_common Pin1 _Enzyme_commission_number 5.2.1.8 loop_ _Mol_system_component_name _Mol_label Pin1 $Pin1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'peptidyl-prolyl cis-trans isomerase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pin1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Peptidyl-prolyl cis-trans isomerase NIMA-interacting1' _Abbreviation_common Pin1 _Molecular_mass 18243 _Mol_thiol_state 'all free' loop_ _Biological_function ; The WW domain of Pin1 is residues 1-54 (20-73). sequence: madeeklppgwekrmsrssgrvyyfnhitnasqwerpsgnsssggkngqgepar ; ; The catalytic domain of Pin1 is residues 44-163 (63-182). sequence: ggkngqgeparvrcshllvkhsqsrrpsswrqekitrtkeealelingyiqkiksgeedfes lasqfsdcssakargdlgafsrgqmqkpfedasfalrtgemsgpvftdsgihiilrte ; stop_ _Details ; The molecular mass (18243) does not include the his-tag. ; ############################## # Polymer residue sequence # ############################## _Residue_count 183 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MADEEKLPPGWEKRMSRSSG RVYYFNHITNASQWERPSGN SSSGGKNGQGEPARVRCSHL LVKHSQSRRPSSWRQEKITR TKEEALELINGYIQKIKSGE EDFESLASQFSDCSSAKARG DLGAFSRGQMQKPFEDASFA LRTGEMSGPVFTDSGIHIIL RTE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 GLY 3 -17 SER 4 -16 SER 5 -15 HIS 6 -14 HIS 7 -13 HIS 8 -12 HIS 9 -11 HIS 10 -10 HIS 11 -9 SER 12 -8 SER 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PRO 17 -3 ARG 18 -2 GLY 19 -1 SER 20 0 HIS 21 1 MET 22 2 ALA 23 3 ASP 24 4 GLU 25 5 GLU 26 6 LYS 27 7 LEU 28 8 PRO 29 9 PRO 30 10 GLY 31 11 TRP 32 12 GLU 33 13 LYS 34 14 ARG 35 15 MET 36 16 SER 37 17 ARG 38 18 SER 39 19 SER 40 20 GLY 41 21 ARG 42 22 VAL 43 23 TYR 44 24 TYR 45 25 PHE 46 26 ASN 47 27 HIS 48 28 ILE 49 29 THR 50 30 ASN 51 31 ALA 52 32 SER 53 33 GLN 54 34 TRP 55 35 GLU 56 36 ARG 57 37 PRO 58 38 SER 59 39 GLY 60 40 ASN 61 41 SER 62 42 SER 63 43 SER 64 44 GLY 65 45 GLY 66 46 LYS 67 47 ASN 68 48 GLY 69 49 GLN 70 50 GLY 71 51 GLU 72 52 PRO 73 53 ALA 74 54 ARG 75 55 VAL 76 56 ARG 77 57 CYS 78 58 SER 79 59 HIS 80 60 LEU 81 61 LEU 82 62 VAL 83 63 LYS 84 64 HIS 85 65 SER 86 66 GLN 87 67 SER 88 68 ARG 89 69 ARG 90 70 PRO 91 71 SER 92 72 SER 93 73 TRP 94 74 ARG 95 75 GLN 96 76 GLU 97 77 LYS 98 78 ILE 99 79 THR 100 80 ARG 101 81 THR 102 82 LYS 103 83 GLU 104 84 GLU 105 85 ALA 106 86 LEU 107 87 GLU 108 88 LEU 109 89 ILE 110 90 ASN 111 91 GLY 112 92 TYR 113 93 ILE 114 94 GLN 115 95 LYS 116 96 ILE 117 97 LYS 118 98 SER 119 99 GLY 120 100 GLU 121 101 GLU 122 102 ASP 123 103 PHE 124 104 GLU 125 105 SER 126 106 LEU 127 107 ALA 128 108 SER 129 109 GLN 130 110 PHE 131 111 SER 132 112 ASP 133 113 CYS 134 114 SER 135 115 SER 136 116 ALA 137 117 LYS 138 118 ALA 139 119 ARG 140 120 GLY 141 121 ASP 142 122 LEU 143 123 GLY 144 124 ALA 145 125 PHE 146 126 SER 147 127 ARG 148 128 GLY 149 129 GLN 150 130 MET 151 131 GLN 152 132 LYS 153 133 PRO 154 134 PHE 155 135 GLU 156 136 ASP 157 137 ALA 158 138 SER 159 139 PHE 160 140 ALA 161 141 LEU 162 142 ARG 163 143 THR 164 144 GLY 165 145 GLU 166 146 MET 167 147 SER 168 148 GLY 169 149 PRO 170 150 VAL 171 151 PHE 172 152 THR 173 153 ASP 174 154 SER 175 155 GLY 176 156 ILE 177 157 HIS 178 158 ILE 179 159 ILE 180 160 LEU 181 161 ARG 182 162 THR 183 163 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 11559 wild_type_hPin1_PPIase_domain 61.75 117 100.00 100.00 7.97e-75 BMRB 11560 C113D_mutant_hPin1_PPIase_domain 61.75 117 99.12 99.12 5.22e-73 PDB 1F8A "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" 91.26 167 99.40 99.40 8.76e-116 PDB 1NMV "Solution Structure Of Human Pin1" 89.07 163 100.00 100.00 1.89e-115 PDB 1NMW "Solution Structure Of The Ppiase Domain Of Human Pin1" 62.30 114 100.00 100.00 1.01e-75 PDB 1PIN "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" 89.07 163 100.00 100.00 1.89e-115 PDB 1ZCN "Human Pin1 Ng Mutant" 89.07 161 98.16 98.77 7.88e-112 PDB 2F21 "Human Pin1 Fip Mutant" 89.07 162 98.16 98.77 4.67e-112 PDB 2ITK "Human Pin1 Bound To D-Peptide" 91.26 167 98.80 98.80 6.83e-115 PDB 2Q5A "Human Pin1 Bound To L-Peptide" 91.26 167 98.80 98.80 6.83e-115 PDB 2RUC "Solution Structure Of The Peptidyl Prolyl Cis-trans Isomerase Domain Of Human Pin1 With Sulfate Ion" 61.75 117 100.00 100.00 7.97e-75 PDB 2RUD "Solution Structure Of The Peptidyl Prolyl Cis-trans Isomerase Domain Of C113d Mutant Human Pin1 With Sulfate Ion" 61.75 117 99.12 99.12 5.22e-73 PDB 2XP3 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XP4 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XP5 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XP6 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.20 98.20 4.68e-114 PDB 2XP7 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XP8 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XP9 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XPA "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2XPB "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 2ZQS "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 3.42e-114 PDB 2ZQT "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 1.52e-114 PDB 2ZQU "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 4.45e-114 PDB 2ZQV "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 3.07e-114 PDB 2ZR4 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 100.00 3.89e-115 PDB 2ZR5 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 1.02e-114 PDB 2ZR6 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 89.07 163 99.39 99.39 1.59e-114 PDB 3I6C "Structure-Based Design Of Novel Pin1 Inhibitors (Ii)" 65.03 123 98.32 100.00 1.20e-78 PDB 3IK8 "Structure-Based Design Of Novel Pin1 Inhibitors (I)" 65.03 123 98.32 100.00 1.20e-78 PDB 3IKD "Structure-Based Design Of Novel Pin1 Inhibitors (I)" 65.03 123 98.32 100.00 1.20e-78 PDB 3IKG "Structure-Based Design Of Novel Pin1 Inhibitors (I)" 65.03 123 98.32 100.00 1.20e-78 PDB 3JYJ "Structure-Based Design Of Novel Pin1 Inhibitors (Ii)" 65.03 123 98.32 100.00 1.20e-78 PDB 3KAB "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.80 98.80 6.83e-115 PDB 3KAC "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 66.67 123 97.54 99.18 1.54e-79 PDB 3KAD "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.20 98.20 4.68e-114 PDB 3KAF "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.20 98.20 4.68e-114 PDB 3KAG "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.80 98.80 6.83e-115 PDB 3KAH "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.80 98.80 6.83e-115 PDB 3KAI "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.80 98.80 6.83e-115 PDB 3KCE "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 91.26 167 98.80 98.80 6.83e-115 PDB 3NTP "Human Pin1 Complexed With Reduced Amide Inhibitor" 91.26 167 98.80 98.80 6.83e-115 PDB 3ODK "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 91.26 167 98.80 98.80 6.83e-115 PDB 3OOB "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" 89.07 163 99.39 99.39 1.59e-114 PDB 3TC5 "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" 90.71 166 99.40 99.40 8.91e-117 PDB 3TCZ "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" 86.34 158 99.37 99.37 1.48e-110 PDB 3TDB "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" 86.34 158 99.37 99.37 1.48e-110 PDB 3WH0 "Structure Of Pin1 Complex With 18-crown-6" 89.07 163 99.39 99.39 1.59e-114 PDB 4TYO "Ppiase In Complex With A Non-phosphate Small Molecule Inhibitor" 65.03 123 98.32 100.00 1.20e-78 DBJ BAE02434 "unnamed protein product [Macaca fascicularis]" 89.07 163 99.39 99.39 1.65e-114 DBJ BAF83763 "unnamed protein product [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 DBJ BAG11415 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [synthetic construct]" 89.07 163 100.00 100.00 1.89e-115 DBJ BAG53486 "unnamed protein product [Homo sapiens]" 69.95 145 98.44 99.22 4.06e-85 EMBL CAG28582 "UBL5 [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 GB AAC50492 "Pin1 [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 GB AAH02899 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 GB AAI12584 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Bos taurus]" 89.07 163 98.16 98.16 3.11e-113 GB AAV38138 "protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 GB AAX31371 "protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Bos taurus]" 89.07 163 98.16 98.16 3.11e-113 PRF 2209428A "peptidyl-Pro isomerase" 89.07 163 100.00 100.00 1.89e-115 REF NP_001029804 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 89.07 163 98.16 98.16 3.11e-113 REF NP_001231300 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" 89.07 163 97.55 98.16 8.98e-113 REF NP_001270625 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" 89.07 163 99.39 99.39 1.65e-114 REF NP_006212 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Homo sapiens]" 89.07 163 100.00 100.00 1.89e-115 REF XP_001099116 "PREDICTED: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca mulatta]" 69.95 145 100.00 100.00 1.06e-86 SP Q13526 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 89.07 163 100.00 100.00 1.89e-115 SP Q4R383 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 89.07 163 99.39 99.39 1.65e-114 SP Q5BIN5 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 89.07 163 98.16 98.16 3.11e-113 TPG DAA28013 "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 89.07 163 98.16 98.16 3.11e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pin1 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 $Pin1 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pin1 1.5 mM '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.14 _Details ; ETH Zuerich Institueof Molecularbiology and Biophysics ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HCC(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _Sample_label . save_ save_15N-edited_NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.2 na temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; The histidine-tag was not assigned. Pin1 was assigned using 3 different constructs, namely full-length Pin1, Pin1_WW and Pin1_cat. Some resonances were not visible in spectra recorded on full-lenght Pin1, but in spectra recorded on either Pin1_WW or Pin1_cat. The resonances of Arg 17 (37), Ser 18 (38), His 27 (47), Ile 28 (48), Trp 34 (54) were assigned from spectra recorded on Pin_WW. The resonances of Glu 104 (124), Ser 105 (125) were taken form spectra recorded on Pin1_cat. Resonances originating form residues Ser 38 (58) to Gly 44 (64) of the linker sequence are broadended in full-lenght Pin1-spectra. These residues could be assigned using the spectra of Pin1_WW. ; loop_ _Experiment_label '1H-15N HSQC' CBCA(CO)NH HNCACB HNCO HN(CA)CO HCC(CO)NH '15N-edited NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Pin1 _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 . 21 MET CA C 54.104 0.05 1 2 . 21 MET HA H 4.236 0.02 1 3 . 21 MET CB C 31.234 0.05 1 4 . 21 MET C C 173.487 0.05 1 5 . 22 ALA N N 124.151 0.05 1 6 . 22 ALA H H 8.248 0.02 1 7 . 22 ALA CA C 50.858 0.05 1 8 . 22 ALA HA H 4.174 0.02 1 9 . 22 ALA CB C 17.810 0.05 1 10 . 22 ALA C C 175.259 0.05 1 11 . 23 ASP N N 118.856 0.05 1 12 . 23 ASP H H 8.185 0.02 1 13 . 23 ASP CA C 52.770 0.05 1 14 . 23 ASP HA H 4.441 0.02 1 15 . 23 ASP CB C 39.510 0.05 1 16 . 23 ASP C C 174.212 0.05 1 17 . 24 GLU N N 120.001 0.05 1 18 . 24 GLU H H 8.230 0.02 1 19 . 24 GLU CA C 54.748 0.05 1 20 . 24 GLU HA H 4.138 0.02 1 21 . 24 GLU CB C 28.757 0.05 1 22 . 24 GLU C C 174.184 0.05 1 23 . 25 GLU N N 121.023 0.05 1 24 . 25 GLU H H 8.247 0.02 1 25 . 25 GLU CA C 54.550 0.05 1 26 . 25 GLU HA H 4.111 0.02 1 27 . 25 GLU CB C 28.757 0.05 1 28 . 25 GLU C C 173.820 0.05 1 29 . 26 LYS N N 122.648 0.05 1 30 . 26 LYS H H 8.180 0.02 1 31 . 26 LYS CA C 54.155 0.05 1 32 . 26 LYS HA H 4.156 0.02 1 33 . 26 LYS CB C 31.103 0.05 1 34 . 26 LYS C C 173.896 0.05 1 35 . 27 LEU N N 124.121 0.05 1 36 . 27 LEU H H 8.422 0.02 1 37 . 27 LEU CA C 50.792 0.05 1 38 . 27 LEU HA H 4.312 0.02 1 39 . 27 LEU CB C 40.617 0.05 1 40 . 27 LEU C C 171.900 0.05 1 41 . 29 PRO CA C 62.258 0.05 1 42 . 29 PRO HA H 4.236 0.02 1 43 . 29 PRO CB C 29.862 0.05 1 44 . 29 PRO C C 174.888 0.05 1 45 . 30 GLY N N 111.090 0.05 1 46 . 30 GLY H H 8.664 0.02 1 47 . 30 GLY CA C 43.077 0.05 1 48 . 30 GLY HA2 H 3.924 0.02 1 49 . 30 GLY HA3 H 3.130 0.02 1 50 . 30 GLY C C 170.488 0.05 1 51 . 31 TRP N N 116.744 0.05 1 52 . 31 TRP H H 7.337 0.02 1 53 . 31 TRP CA C 55.276 0.05 1 54 . 31 TRP HA H 5.110 0.02 1 55 . 31 TRP CB C 30.647 0.05 1 56 . 31 TRP NE1 N 129.001 0.05 1 57 . 31 TRP HE1 H 10.400 0.02 1 58 . 31 TRP C C 174.139 0.05 1 59 . 32 GLU N N 119.730 0.05 1 60 . 32 GLU H H 9.670 0.02 1 61 . 32 GLU CA C 52.770 0.05 1 62 . 32 GLU HA H 4.735 0.02 1 63 . 32 GLU CB C 32.993 0.05 1 64 . 32 GLU C C 171.715 0.05 1 65 . 33 LYS N N 124.287 0.05 1 66 . 33 LYS H H 8.790 0.02 1 67 . 33 LYS CA C 53.693 0.05 1 68 . 33 LYS HA H 4.299 0.02 1 69 . 33 LYS CB C 32.667 0.05 1 70 . 33 LYS C C 173.078 0.05 1 71 . 34 ARG N N 125.895 0.05 1 72 . 34 ARG H H 8.696 0.02 1 73 . 34 ARG CA C 52.572 0.05 1 74 . 34 ARG HA H 4.307 0.02 1 75 . 34 ARG CB C 32.733 0.05 1 76 . 34 ARG C C 170.821 0.05 1 77 . 35 MET N N 116.735 0.05 1 78 . 35 MET H H 8.090 0.02 1 79 . 35 MET CA C 52.045 0.05 1 80 . 35 MET HA H 4.789 0.02 1 81 . 35 MET CB C 32.993 0.05 1 82 . 35 MET C C 174.214 0.05 1 83 . 36 SER N N 120.196 0.05 1 84 . 36 SER H H 8.882 0.02 1 85 . 36 SER CA C 55.473 0.05 1 86 . 36 SER HA H 4.574 0.02 1 87 . 36 SER CB C 61.600 0.05 1 88 . 36 SER C C 174.180 0.05 1 89 . 37 ARG N N 129.981 0.05 1 90 . 37 ARG H H 9.458 0.02 1 91 . 37 ARG CA C 55.892 0.05 1 92 . 37 ARG HA H 4.031 0.02 1 93 . 37 ARG CB C 27.582 0.05 1 94 . 38 SER N N 112.983 0.05 1 95 . 38 SER H H 8.489 0.02 1 96 . 38 SER CA C 57.186 0.05 1 97 . 38 SER CB C 60.259 0.05 1 98 . 39 SER CA C 55.662 0.05 1 99 . 39 SER HA H 4.277 0.02 1 100 . 39 SER CB C 62.997 0.05 1 101 . 39 SER C C 173.460 0.05 1 102 . 40 GLY N N 111.400 0.05 1 103 . 40 GLY H H 7.998 0.02 1 104 . 40 GLY CA C 44.264 0.05 1 105 . 40 GLY HA2 H 3.977 0.02 1 106 . 40 GLY HA3 H 3.808 0.02 1 107 . 40 GLY C C 171.140 0.05 1 108 . 41 ARG N N 118.279 0.05 1 109 . 41 ARG H H 7.562 0.02 1 110 . 41 ARG CA C 53.759 0.05 1 111 . 41 ARG HA H 4.370 0.02 1 112 . 41 ARG CB C 31.103 0.05 1 113 . 41 ARG C C 173.593 0.05 1 114 . 42 VAL N N 123.475 0.05 1 115 . 42 VAL H H 8.362 0.02 1 116 . 42 VAL CA C 59.891 0.05 1 117 . 42 VAL HA H 4.593 0.02 1 118 . 42 VAL CB C 31.494 0.05 1 119 . 42 VAL C C 172.938 0.05 1 120 . 43 TYR N N 121.174 0.05 1 121 . 43 TYR H H 8.623 0.02 1 122 . 43 TYR CA C 53.429 0.05 1 123 . 43 TYR HA H 4.753 0.02 1 124 . 43 TYR CB C 38.272 0.05 1 125 . 43 TYR C C 168.368 0.05 1 126 . 44 TYR N N 116.313 0.05 1 127 . 44 TYR H H 8.891 0.02 1 128 . 44 TYR CA C 55.210 0.05 1 129 . 44 TYR HA H 5.146 0.02 1 130 . 44 TYR CB C 39.705 0.05 1 131 . 44 TYR C C 171.942 0.05 1 132 . 45 PHE N N 123.805 0.05 1 133 . 45 PHE H H 9.312 0.02 1 134 . 45 PHE CA C 54.089 0.05 1 135 . 45 PHE HA H 5.458 0.02 1 136 . 45 PHE CB C 42.768 0.05 1 137 . 45 PHE C C 170.670 0.05 1 138 . 46 ASN N N 128.097 0.05 1 139 . 46 ASN H H 8.032 0.02 1 140 . 46 ASN CA C 48.868 0.05 1 141 . 46 ASN HA H 6.233 0.02 1 142 . 46 ASN CB C 36.642 0.05 1 143 . 46 ASN C C 178.710 0.05 1 144 . 47 HIS N N 120.240 0.05 1 145 . 47 HIS H H 8.062 0.02 1 146 . 47 HIS CA C 54.719 0.05 1 147 . 47 HIS CB C 26.590 0.05 1 148 . 48 ILE N N 121.383 0.05 1 149 . 48 ILE H H 8.203 0.02 1 150 . 48 ILE CA C 60.836 0.05 1 151 . 48 ILE HA H 3.728 0.02 1 152 . 48 ILE CB C 34.311 0.05 1 153 . 48 ILE C C 175.438 0.05 1 154 . 49 THR N N 107.028 0.05 1 155 . 49 THR H H 7.311 0.02 1 156 . 49 THR CA C 59.364 0.05 1 157 . 49 THR HA H 4.102 0.02 1 158 . 49 THR CB C 68.247 0.05 1 159 . 49 THR C C 173.323 0.05 1 160 . 50 ASN N N 116.827 0.05 1 161 . 50 ASN H H 7.893 0.02 1 162 . 50 ASN CA C 53.034 0.05 1 163 . 50 ASN HA H 4.204 0.02 1 164 . 50 ASN CB C 35.469 0.05 1 165 . 50 ASN C C 170.958 0.05 1 166 . 51 ALA N N 120.828 0.05 1 167 . 51 ALA H H 7.056 0.02 1 168 . 51 ALA CA C 50.198 0.05 1 169 . 51 ALA HA H 4.334 0.02 1 170 . 51 ALA CB C 19.309 0.05 1 171 . 51 ALA C C 173.184 0.05 1 172 . 52 SER N N 111.464 0.05 1 173 . 52 SER H H 8.135 0.02 1 174 . 52 SER CA C 55.012 0.05 1 175 . 52 SER HA H 5.850 0.02 1 176 . 52 SER CB C 64.859 0.05 1 177 . 52 SER C C 171.624 0.05 1 178 . 53 GLN N N 115.918 0.05 1 179 . 53 GLN H H 9.274 0.02 1 180 . 53 GLN CA C 53.298 0.05 1 181 . 53 GLN HA H 4.700 0.02 1 182 . 53 GLN CB C 31.494 0.05 1 183 . 53 GLN C C 172.411 0.05 1 184 . 54 TRP N N 120.167 0.05 1 185 . 54 TRP H H 8.439 0.02 1 186 . 54 TRP CA C 56.246 0.05 1 187 . 54 TRP HA H 4.834 0.02 1 188 . 54 TRP CB C 28.219 0.05 1 189 . 54 TRP NE1 N 128.450 0.05 1 190 . 54 TRP HE1 H 9.997 0.02 1 191 . 54 TRP C C 174.610 0.05 1 192 . 55 GLU N N 116.560 0.05 1 193 . 55 GLU H H 7.941 0.02 1 194 . 55 GLU CA C 53.693 0.05 1 195 . 55 GLU HA H 4.281 0.02 1 196 . 55 GLU CB C 28.888 0.05 1 197 . 55 GLU C C 173.318 0.05 1 198 . 56 ARG N N 124.181 0.05 1 199 . 56 ARG H H 8.351 0.02 1 200 . 56 ARG CA C 52.243 0.05 1 201 . 56 ARG HA H 4.404 0.02 1 202 . 56 ARG CB C 28.658 0.05 1 203 . 56 ARG C C 172.322 0.05 1 204 . 57 PRO CA C 61.316 0.05 1 205 . 57 PRO HA H 3.746 0.02 1 206 . 57 PRO CB C 29.871 0.05 1 207 . 57 PRO C C 174.729 0.05 1 208 . 58 SER N N 114.922 0.05 1 209 . 58 SER H H 7.999 0.02 1 210 . 58 SER CA C 55.854 0.05 1 211 . 58 SER HA H 4.612 0.02 1 212 . 58 SER CB C 62.694 0.05 1 213 . 58 SER C C 172.751 0.05 1 214 . 59 GLY N N 109.750 0.05 1 215 . 59 GLY H H 8.313 0.02 1 216 . 59 GLY CA C 43.671 0.05 1 217 . 59 GLY HA2 H 3.844 0.02 1 218 . 59 GLY C C 170.397 0.05 1 219 . 60 ASN N N 118.312 0.05 1 220 . 60 ASN H H 8.329 0.02 1 221 . 60 ASN CA C 51.319 0.05 1 222 . 60 ASN CB C 37.555 0.05 1 223 . 60 ASN C C 177.068 0.05 1 224 . 61 SER N N 116.236 0.05 1 225 . 61 SER H H 8.314 0.02 1 226 . 61 SER CA C 56.508 0.05 1 227 . 61 SER CB C 62.448 0.05 1 228 . 62 SER N N 117.430 0.05 1 229 . 62 SER H H 8.308 0.02 1 230 . 62 SER CA C 55.966 0.05 1 231 . 62 SER CB C 61.468 0.05 1 232 . 63 SER N N 117.669 0.05 1 233 . 63 SER H H 8.397 0.02 1 234 . 63 SER CA C 55.966 0.05 1 235 . 63 SER CB C 61.404 0.05 1 236 . 64 GLY N N 110.376 0.05 1 237 . 64 GLY H H 8.344 0.02 1 238 . 64 GLY CA C 42.881 0.05 1 239 . 64 GLY HA2 H 3.897 0.02 1 240 . 64 GLY C C 172.351 0.05 1 241 . 65 GLY N N 107.853 0.05 1 242 . 65 GLY H H 8.176 0.02 1 243 . 65 GLY CA C 43.818 0.05 1 244 . 65 GLY HA2 H 3.862 0.02 1 245 . 65 GLY C C 171.670 0.05 1 246 . 66 LYS N N 120.001 0.05 1 247 . 66 LYS H H 8.075 0.02 1 248 . 66 LYS CA C 54.155 0.05 1 249 . 66 LYS HA H 4.254 0.02 1 250 . 66 LYS CB C 31.625 0.05 1 251 . 66 LYS C C 173.245 0.05 1 252 . 67 ASN N N 124.512 0.05 1 253 . 67 ASN H H 7.987 0.02 1 254 . 67 ASN CA C 53.232 0.05 1 255 . 67 ASN HA H 4.361 0.02 1 256 . 67 ASN CB C 39.184 0.05 1 257 . 67 ASN C C 174.107 0.05 1 258 . 68 GLY N N 113.358 0.05 1 259 . 68 GLY H H 8.222 0.02 1 260 . 68 GLY CA C 43.991 0.05 1 261 . 68 GLY HA2 H 3.875 0.02 1 262 . 68 GLY C C 172.352 0.05 1 263 . 69 GLN N N 118.870 0.05 1 264 . 69 GLN H H 8.333 0.02 1 265 . 69 GLN CA C 53.825 0.05 1 266 . 69 GLN HA H 4.267 0.02 1 267 . 69 GLN CB C 27.910 0.05 1 268 . 69 GLN C C 174.271 0.05 1 269 . 70 GLY N N 109.193 0.05 1 270 . 70 GLY H H 8.320 0.02 1 271 . 70 GLY CA C 43.143 0.05 1 272 . 70 GLY HA2 H 3.826 0.02 1 273 . 70 GLY C C 171.408 0.05 1 274 . 71 GLU N N 121.218 0.05 1 275 . 71 GLU H H 8.150 0.02 1 276 . 71 GLU CA C 52.506 0.05 1 277 . 71 GLU CB C 30.647 0.05 1 278 . 71 GLU C C 172.068 0.05 1 279 . 72 PRO CA C 60.707 0.05 1 280 . 72 PRO HA H 4.303 0.02 1 281 . 72 PRO CB C 30.328 0.05 1 282 . 72 PRO C C 173.983 0.05 1 283 . 73 ALA N N 121.850 0.05 1 284 . 73 ALA H H 8.499 0.02 1 285 . 73 ALA CA C 51.715 0.05 1 286 . 73 ALA HA H 4.178 0.02 1 287 . 73 ALA CB C 17.810 0.05 1 288 . 73 ALA C C 175.820 0.05 1 289 . 74 ARG N N 114.614 0.05 1 290 . 74 ARG H H 7.623 0.02 1 291 . 74 ARG CA C 52.243 0.05 1 292 . 74 ARG HA H 4.927 0.02 1 293 . 74 ARG CB C 32.602 0.05 1 294 . 74 ARG C C 172.079 0.05 1 295 . 75 VAL N N 113.065 0.05 1 296 . 75 VAL H H 7.771 0.02 1 297 . 75 VAL CA C 56.792 0.05 1 298 . 75 VAL HA H 3.901 0.02 1 299 . 75 VAL CB C 33.339 0.05 1 300 . 75 VAL C C 169.869 0.05 1 301 . 76 ARG N N 120.001 0.05 1 302 . 76 ARG H H 8.128 0.02 1 303 . 76 ARG CA C 53.166 0.05 1 304 . 76 ARG HA H 4.749 0.02 1 305 . 76 ARG CB C 32.301 0.05 1 306 . 76 ARG C C 173.593 0.05 1 307 . 77 CYS N N 116.925 0.05 1 308 . 77 CYS H H 7.163 0.02 1 309 . 77 CYS CA C 53.759 0.05 1 310 . 77 CYS HA H 5.658 0.02 1 311 . 77 CYS CB C 31.846 0.05 1 312 . 77 CYS C C 171.018 0.05 1 313 . 78 SER N N 115.724 0.05 1 314 . 78 SER H H 9.267 0.02 1 315 . 78 SER CA C 54.221 0.05 1 316 . 78 SER HA H 5.596 0.02 1 317 . 78 SER CB C 64.170 0.05 1 318 . 78 SER C C 170.867 0.05 1 319 . 79 HIS N N 119.313 0.05 1 320 . 79 HIS H H 9.726 0.02 1 321 . 79 HIS CA C 52.374 0.05 1 322 . 79 HIS HA H 6.202 0.02 1 323 . 79 HIS CB C 35.481 0.05 1 324 . 79 HIS C C 169.458 0.05 1 325 . 80 LEU N N 124.437 0.05 1 326 . 80 LEU H H 8.845 0.02 1 327 . 80 LEU CA C 53.166 0.05 1 328 . 80 LEU HA H 4.606 0.02 1 329 . 80 LEU CB C 43.724 0.05 1 330 . 80 LEU C C 171.140 0.05 1 331 . 81 LEU N N 126.604 0.05 1 332 . 81 LEU H H 8.027 0.02 1 333 . 81 LEU CA C 50.792 0.05 1 334 . 81 LEU HA H 4.633 0.02 1 335 . 81 LEU CB C 43.789 0.05 1 336 . 81 LEU C C 171.670 0.05 1 337 . 82 VAL N N 127.505 0.05 1 338 . 82 VAL H H 9.436 0.02 1 339 . 82 VAL CA C 59.569 0.05 1 340 . 82 VAL HA H 4.579 0.02 1 341 . 82 VAL CB C 31.652 0.05 1 342 . 82 VAL C C 174.068 0.05 1 343 . 83 LYS N N 124.798 0.05 1 344 . 83 LYS H H 9.078 0.02 1 345 . 83 LYS CA C 54.880 0.05 1 346 . 83 LYS HA H 4.419 0.02 1 347 . 83 LYS CB C 35.092 0.05 1 348 . 83 LYS C C 171.867 0.05 1 349 . 84 HIS N N 113.375 0.05 1 350 . 84 HIS H H 8.249 0.02 1 351 . 84 HIS CA C 52.857 0.05 1 352 . 84 HIS HA H 4.624 0.02 1 353 . 84 HIS CB C 32.171 0.05 1 354 . 84 HIS C C 174.260 0.05 1 355 . 85 SER N N 113.039 0.05 1 356 . 85 SER H H 9.410 0.02 1 357 . 85 SER CA C 59.234 0.05 1 358 . 85 SER HA H 4.089 0.02 1 359 . 85 SER CB C 61.314 0.05 1 360 . 85 SER C C 173.245 0.05 1 361 . 86 GLN N N 119.683 0.05 1 362 . 86 GLN H H 9.096 0.02 1 363 . 86 GLN CA C 53.166 0.05 1 364 . 86 GLN HA H 4.383 0.02 1 365 . 86 GLN CB C 27.757 0.05 1 366 . 86 GLN C C 174.033 0.05 1 367 . 87 SER N N 120.682 0.05 1 368 . 87 SER H H 7.767 0.02 1 369 . 87 SER CA C 59.693 0.05 1 370 . 87 SER HA H 4.517 0.02 1 371 . 87 SER CB C 62.223 0.05 1 372 . 87 SER C C 172.972 0.05 1 373 . 88 ARG N N 121.179 0.05 1 374 . 88 ARG H H 8.176 0.02 1 375 . 88 ARG CA C 57.144 0.05 1 376 . 88 ARG HA H 4.035 0.02 1 377 . 88 ARG CB C 27.822 0.05 1 378 . 88 ARG C C 174.351 0.05 1 379 . 89 ARG N N 117.561 0.05 1 380 . 89 ARG H H 8.267 0.02 1 381 . 89 ARG CA C 51.254 0.05 1 382 . 89 ARG HA H 3.944 0.02 1 383 . 89 ARG CB C 30.354 0.05 1 384 . 89 ARG C C 173.401 0.05 1 385 . 90 PRO CA C 60.673 0.05 1 386 . 90 PRO HA H 4.374 0.02 1 387 . 90 PRO CB C 25.483 0.05 1 388 . 90 PRO C C 171.555 0.05 1 389 . 91 SER N N 120.332 0.05 1 390 . 91 SER H H 9.039 0.02 1 391 . 91 SER CA C 56.133 0.05 1 392 . 91 SER HA H 4.338 0.02 1 393 . 91 SER CB C 64.040 0.05 1 394 . 91 SER C C 170.011 0.05 1 395 . 92 SER N N 118.140 0.05 1 396 . 92 SER H H 8.882 0.02 1 397 . 92 SER CA C 55.144 0.05 1 398 . 92 SER HA H 4.434 0.02 1 399 . 92 SER CB C 67.091 0.05 1 400 . 92 SER C C 172.276 0.05 1 401 . 93 TRP N N 118.081 0.05 1 402 . 93 TRP H H 8.480 0.02 1 403 . 93 TRP CA C 56.109 0.05 1 404 . 93 TRP HA H 4.312 0.02 1 405 . 93 TRP CB C 25.486 0.05 1 406 . 93 TRP NE1 N 131.936 0.05 1 407 . 93 TRP HE1 H 9.929 0.02 1 408 . 93 TRP C C 174.023 0.05 1 409 . 94 ARG N N 117.036 0.05 1 410 . 94 ARG H H 6.945 0.02 1 411 . 94 ARG CA C 55.210 0.05 1 412 . 94 ARG HA H 4.267 0.02 1 413 . 94 ARG CB C 28.536 0.05 1 414 . 94 ARG C C 174.209 0.05 1 415 . 96 GLU CA C 56.671 0.05 1 416 . 96 GLU HA H 3.991 0.02 1 417 . 96 GLU CB C 28.466 0.05 1 418 . 96 GLU C C 174.307 0.05 1 419 . 97 LYS N N 117.166 0.05 1 420 . 97 LYS H H 7.910 0.02 1 421 . 97 LYS CA C 53.297 0.05 1 422 . 97 LYS HA H 4.597 0.02 1 423 . 97 LYS CB C 32.391 0.05 1 424 . 97 LYS C C 172.170 0.05 1 425 . 98 ILE N N 125.348 0.05 1 426 . 98 ILE H H 7.742 0.02 1 427 . 98 ILE CA C 58.902 0.05 1 428 . 98 ILE HA H 4.169 0.02 1 429 . 98 ILE CB C 35.947 0.05 1 430 . 98 ILE C C 173.287 0.05 1 431 . 99 THR N N 115.610 0.05 1 432 . 99 THR H H 8.107 0.02 1 433 . 99 THR CA C 58.704 0.05 1 434 . 99 THR HA H 4.285 0.02 1 435 . 99 THR CB C 68.336 0.05 1 436 . 99 THR C C 172.862 0.05 1 437 . 100 ARG N N 123.039 0.05 1 438 . 100 ARG H H 7.453 0.02 1 439 . 100 ARG CA C 53.693 0.05 1 440 . 100 ARG HA H 4.535 0.02 1 441 . 100 ARG CB C 29.288 0.05 1 442 . 100 ARG C C 172.276 0.05 1 443 . 101 THR N N 112.833 0.05 1 444 . 101 THR H H 8.899 0.02 1 445 . 101 THR CA C 59.034 0.05 1 446 . 101 THR HA H 4.535 0.02 1 447 . 101 THR CB C 70.017 0.05 1 448 . 101 THR C C 174.110 0.05 1 449 . 102 LYS N N 121.775 0.05 1 450 . 102 LYS H H 8.743 0.02 1 451 . 102 LYS CA C 58.638 0.05 1 452 . 102 LYS HA H 3.821 0.02 1 453 . 102 LYS CB C 30.322 0.05 1 454 . 102 LYS C C 175.472 0.05 1 455 . 103 GLU N N 117.475 0.05 1 456 . 103 GLU H H 8.441 0.02 1 457 . 103 GLU CA C 58.507 0.05 1 458 . 103 GLU HA H 3.839 0.02 1 459 . 103 GLU CB C 27.025 0.05 1 460 . 103 GLU C C 177.515 0.05 1 461 . 104 GLU N N 120.858 0.05 1 462 . 104 GLU H H 7.825 0.02 1 463 . 104 GLU CA C 56.990 0.05 1 464 . 104 GLU HA H 3.901 0.02 1 465 . 104 GLU CB C 28.835 0.05 1 466 . 104 GLU C C 177.628 0.05 1 467 . 105 ALA N N 121.189 0.05 1 468 . 105 ALA H H 8.556 0.02 1 469 . 105 ALA CA C 52.902 0.05 1 470 . 105 ALA HA H 3.884 0.02 1 471 . 105 ALA CB C 17.263 0.05 1 472 . 105 ALA C C 175.774 0.05 1 473 . 106 LEU N N 119.309 0.05 1 474 . 106 LEU H H 8.110 0.02 1 475 . 106 LEU CA C 55.276 0.05 1 476 . 106 LEU HA H 3.830 0.02 1 477 . 106 LEU CB C 39.696 0.05 1 478 . 106 LEU C C 175.411 0.05 1 479 . 107 GLU N N 118.599 0.05 1 480 . 107 GLU H H 7.613 0.02 1 481 . 107 GLU CA C 57.386 0.05 1 482 . 107 GLU HA H 3.964 0.02 1 483 . 107 GLU CB C 27.672 0.05 1 484 . 107 GLU C C 178.088 0.05 1 485 . 108 LEU N N 120.407 0.05 1 486 . 108 LEU H H 7.687 0.02 1 487 . 108 LEU CA C 55.803 0.05 1 488 . 108 LEU HA H 3.572 0.02 1 489 . 108 LEU CB C 39.890 0.05 1 490 . 108 LEU C C 176.305 0.05 1 491 . 109 ILE N N 119.414 0.05 1 492 . 109 ILE H H 7.971 0.02 1 493 . 109 ILE CA C 60.809 0.05 1 494 . 109 ILE HA H 3.598 0.02 1 495 . 109 ILE CB C 33.943 0.05 1 496 . 109 ILE C C 175.261 0.05 1 497 . 110 ASN N N 118.186 0.05 1 498 . 110 ASN H H 8.632 0.02 1 499 . 110 ASN CA C 53.957 0.05 1 500 . 110 ASN HA H 4.445 0.02 1 501 . 110 ASN CB C 36.011 0.05 1 502 . 110 ASN C C 176.880 0.05 1 503 . 111 GLY N N 109.308 0.05 1 504 . 111 GLY H H 7.868 0.02 1 505 . 111 GLY CA C 44.726 0.05 1 506 . 111 GLY HA2 H 3.794 0.02 1 507 . 111 GLY C C 174.548 0.05 1 508 . 112 TYR N N 122.347 0.05 1 509 . 112 TYR H H 8.024 0.02 1 510 . 112 TYR CA C 57.056 0.05 1 511 . 112 TYR HA H 4.356 0.02 1 512 . 112 TYR CB C 34.524 0.05 1 513 . 112 TYR C C 175.922 0.05 1 514 . 113 ILE N N 118.158 0.05 1 515 . 113 ILE H H 8.552 0.02 1 516 . 113 ILE CA C 64.968 0.05 1 517 . 113 ILE HA H 3.456 0.02 1 518 . 113 ILE CB C 36.787 0.05 1 519 . 113 ILE C C 175.641 0.05 1 520 . 114 GLN N N 116.818 0.05 1 521 . 114 GLN H H 7.731 0.02 1 522 . 114 GLN CA C 57.056 0.05 1 523 . 114 GLN HA H 3.991 0.02 1 524 . 114 GLN CB C 26.443 0.05 1 525 . 114 GLN C C 176.977 0.05 1 526 . 115 LYS N N 119.354 0.05 1 527 . 115 LYS H H 7.972 0.02 1 528 . 115 LYS CA C 57.590 0.05 1 529 . 115 LYS HA H 4.267 0.02 1 530 . 115 LYS CB C 32.068 0.05 1 531 . 115 LYS C C 176.175 0.05 1 532 . 116 ILE N N 119.353 0.05 1 533 . 116 ILE H H 8.075 0.02 1 534 . 116 ILE CA C 61.788 0.05 1 535 . 116 ILE HA H 4.240 0.02 1 536 . 116 ILE CB C 37.498 0.05 1 537 . 116 ILE C C 178.960 0.05 1 538 . 117 LYS N N 120.383 0.05 1 539 . 117 LYS H H 8.961 0.02 1 540 . 117 LYS CA C 58.527 0.05 1 541 . 117 LYS HA H 4.044 0.02 1 542 . 117 LYS CB C 31.033 0.05 1 543 . 117 LYS C C 176.696 0.05 1 544 . 118 SER N N 110.741 0.05 1 545 . 118 SER H H 8.087 0.02 1 546 . 118 SER CA C 57.517 0.05 1 547 . 118 SER HA H 4.035 0.02 1 548 . 118 SER CB C 62.424 0.05 1 549 . 118 SER C C 173.433 0.05 1 550 . 119 GLY N N 109.515 0.05 1 551 . 119 GLY H H 7.734 0.02 1 552 . 119 GLY CA C 43.671 0.05 1 553 . 119 GLY HA2 H 3.108 0.02 1 554 . 119 GLY HA3 H 3.019 0.02 1 555 . 119 GLY C C 172.167 0.05 1 556 . 120 GLU N N 120.937 0.05 1 557 . 120 GLU H H 8.175 0.02 1 558 . 120 GLU CA C 57.109 0.05 1 559 . 120 GLU HA H 3.964 0.02 1 560 . 120 GLU CB C 28.940 0.05 1 561 . 120 GLU C C 174.417 0.05 1 562 . 121 GLU N N 113.439 0.05 1 563 . 121 GLU H H 7.297 0.02 1 564 . 121 GLU CA C 52.111 0.05 1 565 . 121 GLU HA H 4.588 0.02 1 566 . 121 GLU CB C 32.675 0.05 1 567 . 121 GLU C C 172.026 0.05 1 568 . 122 ASP N N 117.719 0.05 1 569 . 122 ASP H H 8.259 0.02 1 570 . 122 ASP CA C 51.077 0.05 1 571 . 122 ASP HA H 4.829 0.02 1 572 . 122 ASP CB C 41.497 0.05 1 573 . 122 ASP C C 173.336 0.05 1 574 . 123 PHE N N 121.294 0.05 1 575 . 123 PHE H H 8.994 0.02 1 576 . 123 PHE CA C 60.688 0.05 1 577 . 123 PHE HA H 3.572 0.02 1 578 . 123 PHE CB C 41.773 0.05 1 579 . 123 PHE C C 174.305 0.05 1 580 . 124 GLU N N 115.769 0.05 1 581 . 124 GLU H H 8.951 0.02 1 582 . 124 GLU CA C 58.411 0.05 1 583 . 124 GLU HA H 3.777 0.02 1 584 . 124 GLU CB C 26.945 0.05 1 585 . 124 GLU C C 173.065 0.05 1 586 . 125 SER N N 115.087 0.05 1 587 . 125 SER H H 7.964 0.02 1 588 . 125 SER CA C 58.920 0.05 1 589 . 125 SER HA H 3.946 0.02 1 590 . 125 SER CB C 60.576 0.05 1 591 . 125 SER C C 175.724 0.05 1 592 . 126 LEU N N 119.956 0.05 1 593 . 126 LEU H H 7.592 0.02 1 594 . 126 LEU CA C 55.342 0.05 1 595 . 126 LEU HA H 3.937 0.02 1 596 . 126 LEU CB C 40.015 0.05 1 597 . 126 LEU C C 176.517 0.05 1 598 . 127 ALA N N 121.790 0.05 1 599 . 127 ALA H H 8.688 0.02 1 600 . 127 ALA CA C 53.627 0.05 1 601 . 127 ALA HA H 3.589 0.02 1 602 . 127 ALA CB C 15.482 0.05 1 603 . 127 ALA C C 176.577 0.05 1 604 . 128 SER N N 107.638 0.05 1 605 . 128 SER H H 7.611 0.02 1 606 . 128 SER CA C 59.100 0.05 1 607 . 128 SER HA H 3.884 0.02 1 608 . 128 SER CB C 61.909 0.05 1 609 . 128 SER C C 172.545 0.05 1 610 . 129 GLN N N 114.270 0.05 1 611 . 129 GLN H H 6.787 0.02 1 612 . 129 GLN CA C 55.473 0.05 1 613 . 129 GLN HA H 4.080 0.02 1 614 . 129 GLN CB C 29.648 0.05 1 615 . 129 GLN C C 175.381 0.05 1 616 . 130 PHE N N 111.877 0.05 1 617 . 130 PHE H H 8.048 0.02 1 618 . 130 PHE CA C 55.342 0.05 1 619 . 130 PHE HA H 4.677 0.02 1 620 . 130 PHE CB C 39.694 0.05 1 621 . 130 PHE C C 172.685 0.05 1 622 . 131 SER N N 110.522 0.05 1 623 . 131 SER H H 7.745 0.02 1 624 . 131 SER CA C 55.276 0.05 1 625 . 131 SER HA H 4.557 0.02 1 626 . 131 SER CB C 64.098 0.05 1 627 . 131 SER C C 173.548 0.05 1 628 . 132 ASP N N 124.016 0.05 1 629 . 132 ASP H H 9.841 0.02 1 630 . 132 ASP CA C 54.353 0.05 1 631 . 132 ASP HA H 4.725 0.02 1 632 . 132 ASP CB C 41.947 0.05 1 633 . 132 ASP C C 172.594 0.05 1 634 . 133 CYS N N 122.744 0.05 1 635 . 133 CYS H H 8.038 0.02 1 636 . 133 CYS CA C 57.887 0.05 1 637 . 133 CYS HA H 4.499 0.02 1 638 . 133 CYS CB C 27.717 0.05 1 639 . 133 CYS C C 174.553 0.05 1 640 . 134 SER N N 126.573 0.05 1 641 . 134 SER H H 8.802 0.02 1 642 . 134 SER CA C 60.353 0.05 1 643 . 134 SER HA H 3.982 0.02 1 644 . 134 SER CB C 60.353 0.05 1 645 . 134 SER C C 173.980 0.05 1 646 . 135 SER N N 122.798 0.05 1 647 . 135 SER H H 9.803 0.02 1 648 . 135 SER CA C 59.364 0.05 1 649 . 135 SER HA H 3.928 0.02 1 650 . 135 SER CB C 61.265 0.05 1 651 . 135 SER C C 174.915 0.05 1 652 . 136 ALA N N 131.461 0.05 1 653 . 136 ALA H H 8.506 0.02 1 654 . 136 ALA CA C 54.677 0.05 1 655 . 136 ALA HA H 3.723 0.02 1 656 . 136 ALA CB C 18.637 0.05 1 657 . 136 ALA C C 177.789 0.05 1 658 . 137 LYS N N 113.246 0.05 1 659 . 137 LYS H H 6.982 0.02 1 660 . 137 LYS CA C 55.539 0.05 1 661 . 137 LYS HA H 3.928 0.02 1 662 . 137 LYS CB C 29.970 0.05 1 663 . 137 LYS C C 174.275 0.05 1 664 . 138 ALA N N 123.460 0.05 1 665 . 138 ALA H H 7.671 0.02 1 666 . 138 ALA CA C 48.814 0.05 1 667 . 138 ALA HA H 4.651 0.02 1 668 . 138 ALA CB C 16.963 0.05 1 669 . 138 ALA C C 175.032 0.05 1 670 . 139 ARG N N 114.459 0.05 1 671 . 139 ARG H H 7.978 0.02 1 672 . 139 ARG CA C 55.605 0.05 1 673 . 139 ARG HA H 4.327 0.02 1 674 . 139 ARG CB C 25.270 0.05 1 675 . 139 ARG C C 172.503 0.05 1 676 . 140 GLY N N 102.634 0.05 1 677 . 140 GLY H H 8.257 0.02 1 678 . 140 GLY CA C 42.945 0.05 1 679 . 140 GLY HA2 H 4.365 0.02 1 680 . 140 GLY HA3 H 3.750 0.02 1 681 . 140 GLY C C 171.503 0.05 1 682 . 141 ASP N N 117.829 0.05 1 683 . 141 ASP H H 7.079 0.02 1 684 . 141 ASP CA C 53.759 0.05 1 685 . 141 ASP HA H 4.713 0.02 1 686 . 141 ASP CB C 40.466 0.05 1 687 . 141 ASP C C 173.230 0.05 1 688 . 142 LEU N N 125.105 0.05 1 689 . 142 LEU H H 8.730 0.02 1 690 . 142 LEU CA C 52.704 0.05 1 691 . 142 LEU CB C 42.462 0.05 1 692 . 142 LEU C C 174.563 0.05 1 693 . 143 GLY N N 108.051 0.05 1 694 . 143 GLY H H 8.211 0.02 1 695 . 143 GLY CA C 43.473 0.05 1 696 . 143 GLY HA2 H 4.187 0.02 1 697 . 143 GLY HA3 H 4.545 0.02 1 698 . 143 GLY C C 168.686 0.05 1 699 . 144 ALA N N 118.582 0.05 1 700 . 144 ALA H H 7.997 0.02 1 701 . 144 ALA CA C 48.524 0.05 1 702 . 144 ALA HA H 5.221 0.02 1 703 . 144 ALA CB C 18.573 0.05 1 704 . 144 ALA C C 176.714 0.05 1 705 . 145 PHE N N 116.983 0.05 1 706 . 145 PHE H H 8.823 0.02 1 707 . 145 PHE CA C 54.023 0.05 1 708 . 145 PHE HA H 5.016 0.02 1 709 . 145 PHE CB C 39.178 0.05 1 710 . 145 PHE C C 170.503 0.05 1 711 . 146 SER N N 113.091 0.05 1 712 . 146 SER H H 8.353 0.02 1 713 . 146 SER CA C 54.418 0.05 1 714 . 146 SER HA H 4.035 0.02 1 715 . 146 SER CB C 64.731 0.05 1 716 . 146 SER C C 172.821 0.05 1 717 . 147 ARG N N 120.560 0.05 1 718 . 147 ARG H H 8.801 0.02 1 719 . 147 ARG CA C 56.726 0.05 1 720 . 147 ARG HA H 3.901 0.02 1 721 . 147 ARG CB C 28.576 0.05 1 722 . 147 ARG C C 175.572 0.05 1 723 . 148 GLY N N 111.852 0.05 1 724 . 148 GLY H H 10.215 0.02 1 725 . 148 GLY CA C 43.473 0.05 1 726 . 148 GLY HA2 H 4.285 0.02 1 727 . 148 GLY HA3 H 3.750 0.02 1 728 . 148 GLY C C 172.260 0.05 1 729 . 149 GLN N N 118.204 0.05 1 730 . 149 GLN H H 7.800 0.02 1 731 . 149 GLN CA C 55.803 0.05 1 732 . 149 GLN HA H 4.374 0.02 1 733 . 149 GLN CB C 30.301 0.05 1 734 . 149 GLN C C 173.820 0.05 1 735 . 150 MET N N 117.433 0.05 1 736 . 150 MET H H 8.993 0.02 1 737 . 150 MET CA C 50.396 0.05 1 738 . 150 MET HA H 4.526 0.02 1 739 . 150 MET CB C 32.154 0.05 1 740 . 150 MET C C 173.290 0.05 1 741 . 151 GLN N N 117.551 0.05 1 742 . 151 GLN H H 8.372 0.02 1 743 . 151 GLN CA C 55.645 0.05 1 744 . 151 GLN HA H 4.160 0.02 1 745 . 151 GLN CB C 28.576 0.05 1 746 . 151 GLN C C 176.395 0.05 1 747 . 152 LYS N N 125.469 0.05 1 748 . 152 LYS H H 9.087 0.02 1 749 . 152 LYS CA C 59.367 0.05 1 750 . 152 LYS HA H 4.204 0.02 1 751 . 152 LYS CB C 28.640 0.05 1 752 . 152 LYS C C 171.673 0.05 1 753 . 153 PRO CA C 63.721 0.05 1 754 . 153 PRO HA H 4.490 0.02 1 755 . 153 PRO CB C 29.172 0.05 1 756 . 153 PRO C C 177.842 0.05 1 757 . 154 PHE N N 115.363 0.05 1 758 . 154 PHE H H 6.858 0.02 1 759 . 154 PHE CA C 58.662 0.05 1 760 . 154 PHE HA H 3.598 0.02 1 761 . 154 PHE CB C 38.797 0.05 1 762 . 154 PHE C C 176.044 0.05 1 763 . 155 GLU N N 122.257 0.05 1 764 . 155 GLU H H 8.672 0.02 1 765 . 155 GLU CA C 58.726 0.05 1 766 . 155 GLU HA H 4.026 0.02 1 767 . 155 GLU CB C 29.087 0.05 1 768 . 155 GLU C C 175.143 0.05 1 769 . 156 ASP N N 117.938 0.05 1 770 . 156 ASP H H 9.078 0.02 1 771 . 156 ASP CA C 55.596 0.05 1 772 . 156 ASP HA H 4.374 0.02 1 773 . 156 ASP CB C 38.030 0.05 1 774 . 156 ASP C C 176.895 0.05 1 775 . 157 ALA N N 117.816 0.05 1 776 . 157 ALA H H 7.026 0.02 1 777 . 157 ALA CA C 52.638 0.05 1 778 . 157 ALA HA H 4.080 0.02 1 779 . 157 ALA CB C 18.315 0.05 1 780 . 157 ALA C C 176.744 0.05 1 781 . 158 SER N N 112.742 0.05 1 782 . 158 SER H H 7.834 0.02 1 783 . 158 SER CA C 61.276 0.05 1 784 . 158 SER HA H 4.214 0.02 1 785 . 158 SER CB C 61.276 0.05 1 786 . 158 SER C C 172.378 0.05 1 787 . 159 PHE N N 113.749 0.05 1 788 . 159 PHE H H 8.084 0.02 1 789 . 159 PHE CA C 59.298 0.05 1 790 . 159 PHE HA H 3.803 0.02 1 791 . 159 PHE CB C 37.592 0.05 1 792 . 159 PHE C C 173.617 0.05 1 793 . 160 ALA N N 118.718 0.05 1 794 . 160 ALA H H 6.980 0.02 1 795 . 160 ALA CA C 50.001 0.05 1 796 . 160 ALA HA H 4.365 0.02 1 797 . 160 ALA CB C 18.252 0.05 1 798 . 160 ALA C C 175.729 0.05 1 799 . 161 LEU N N 119.745 0.05 1 800 . 161 LEU H H 6.874 0.02 1 801 . 161 LEU CA C 52.770 0.05 1 802 . 161 LEU HA H 4.187 0.02 1 803 . 161 LEU CB C 41.536 0.05 1 804 . 161 LEU C C 175.365 0.05 1 805 . 162 ARG N N 121.234 0.05 1 806 . 162 ARG H H 8.815 0.02 1 807 . 162 ARG CA C 52.902 0.05 1 808 . 162 ARG HA H 4.312 0.02 1 809 . 162 ARG CB C 29.194 0.05 1 810 . 162 ARG C C 174.699 0.05 1 811 . 163 THR N N 115.918 0.05 1 812 . 163 THR H H 8.415 0.02 1 813 . 163 THR CA C 63.913 0.05 1 814 . 163 THR HA H 3.803 0.02 1 815 . 163 THR CB C 65.902 0.05 1 816 . 163 THR C C 173.428 0.05 1 817 . 164 GLY N N 114.575 0.05 1 818 . 164 GLY H H 8.858 0.02 1 819 . 164 GLY CA C 43.526 0.05 1 820 . 164 GLY HA2 H 3.668 0.02 1 821 . 164 GLY C C 170.982 0.05 1 822 . 165 GLU CA C 53.578 0.05 1 823 . 165 GLU HA H 4.276 0.02 1 824 . 165 GLU CB C 30.341 0.05 1 825 . 165 GLU C C 171.124 0.05 1 826 . 166 MET N N 121.850 0.05 1 827 . 166 MET H H 8.135 0.02 1 828 . 166 MET CA C 50.990 0.05 1 829 . 166 MET HA H 5.587 0.02 1 830 . 166 MET CB C 36.129 0.05 1 831 . 166 MET C C 174.017 0.05 1 832 . 167 SER N N 122.392 0.05 1 833 . 167 SER H H 9.593 0.02 1 834 . 167 SER CA C 57.320 0.05 1 835 . 167 SER HA H 4.329 0.02 1 836 . 167 SER CB C 63.294 0.05 1 837 . 167 SER C C 172.447 0.05 1 838 . 168 GLY N N 102.423 0.05 1 839 . 168 GLY H H 7.661 0.02 1 840 . 168 GLY CA C 42.616 0.05 1 841 . 168 GLY HA2 H 3.898 0.02 1 842 . 168 GLY C C 172.504 0.05 1 843 . 169 PRO CA C 61.512 0.05 1 844 . 169 PRO HA H 4.294 0.02 1 845 . 169 PRO CB C 29.5640 0.05 1 846 . 169 PRO C C 174.479 0.05 1 847 . 170 VAL N N 126.387 0.05 1 848 . 170 VAL H H 9.135 0.02 1 849 . 170 VAL CA C 59.693 0.05 1 850 . 170 VAL HA H 4.267 0.02 1 851 . 170 VAL CB C 33.775 0.05 1 852 . 170 VAL C C 172.723 0.05 1 853 . 171 PHE N N 127.144 0.05 1 854 . 171 PHE H H 9.013 0.02 1 855 . 171 PHE CA C 55.824 0.05 1 856 . 171 PHE HA H 5.043 0.02 1 857 . 171 PHE CB C 38.101 0.05 1 858 . 171 PHE C C 173.714 0.05 1 859 . 172 THR N N 111.929 0.05 1 860 . 172 THR H H 8.992 0.02 1 861 . 172 THR CA C 58.375 0.05 1 862 . 172 THR HA H 4.927 0.02 1 863 . 172 THR CB C 70.356 0.05 1 864 . 172 THR C C 173.276 0.05 1 865 . 173 ASP N N 117.084 0.05 1 866 . 173 ASP H H 8.878 0.02 1 867 . 173 ASP CA C 54.353 0.05 1 868 . 173 ASP HA H 4.615 0.02 1 869 . 173 ASP CB C 39.055 0.05 1 870 . 173 ASP C C 176.244 0.05 1 871 . 174 SER N N 113.956 0.05 1 872 . 174 SER H H 8.996 0.02 1 873 . 174 SER CA C 59.298 0.05 1 874 . 174 SER HA H 3.857 0.02 1 875 . 174 SER CB C 61.806 0.05 1 876 . 174 SER C C 173.450 0.05 1 877 . 175 GLY N N 109.228 0.05 1 878 . 175 GLY H H 7.586 0.02 1 879 . 175 GLY CA C 43.341 0.05 1 880 . 175 GLY HA2 H 3.893 0.02 1 881 . 175 GLY HA3 H 3.420 0.02 1 882 . 175 GLY C C 180.470 0.05 1 883 . 176 ILE N N 122.467 0.05 1 884 . 176 ILE H H 8.239 0.02 1 885 . 176 ILE CA C 58.177 0.05 1 886 . 176 ILE HA H 4.989 0.02 1 887 . 176 ILE CB C 37.792 0.05 1 888 . 176 ILE C C 171.572 0.05 1 889 . 177 HIS N N 123.775 0.05 1 890 . 177 HIS H H 9.831 0.02 1 891 . 177 HIS CA C 51.913 0.05 1 892 . 177 HIS HA H 5.961 0.02 1 893 . 177 HIS CB C 30.442 0.05 1 894 . 177 HIS C C 174.699 0.05 1 895 . 178 ILE N N 115.040 0.05 1 896 . 178 ILE H H 8.463 0.02 1 897 . 178 ILE CA C 60.419 0.05 1 898 . 178 ILE HA H 4.115 0.02 1 899 . 178 ILE CB C 39.946 0.05 1 900 . 178 ILE C C 173.175 0.05 1 901 . 179 ILE N N 125.095 0.05 1 902 . 179 ILE H H 8.750 0.02 1 903 . 179 ILE CA C 59.232 0.05 1 904 . 179 ILE HA H 4.642 0.02 1 905 . 179 ILE CB C 40.199 0.05 1 906 . 179 ILE C C 170.476 0.05 1 907 . 180 LEU N N 127.926 0.05 1 908 . 180 LEU H H 8.735 0.02 1 909 . 180 LEU CA C 51.008 0.05 1 910 . 180 LEU HA H 4.775 0.02 1 911 . 180 LEU CB C 43.748 0.05 1 912 . 180 LEU C C 173.154 0.05 1 913 . 181 ARG N N 126.559 0.05 1 914 . 181 ARG H H 8.012 0.02 1 915 . 181 ARG CA C 54.686 0.05 1 916 . 181 ARG HA H 5.052 0.02 1 917 . 181 ARG CB C 28.414 0.05 1 918 . 181 ARG C C 173.972 0.05 1 919 . 182 THR N N 120.382 0.05 1 920 . 182 THR H H 9.001 0.02 1 921 . 182 THR CA C 60.347 0.05 1 922 . 182 THR HA H 4.312 0.02 1 923 . 182 THR CB C 67.572 0.05 1 924 . 182 THR C C 173.011 0.05 1 925 . 183 GLU N N 125.446 0.05 1 926 . 183 GLU H H 7.898 0.02 1 927 . 183 GLU CA C 56.265 0.05 1 928 . 183 GLU CB C 32.152 0.05 1 929 . 183 GLU C C 178.890 0.05 1 stop_ save_