data_18204 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for human PEBP1 ; _BMRB_accession_number 18204 _BMRB_flat_file_name bmr18204.str _Entry_type original _Submission_date 2012-01-20 _Accession_date 2012-01-20 _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 Karsisiotis Andreas I. Sr. 2 Tavel Laurette . . 3 Damblon Christian . Sr. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 167 "13C chemical shifts" 531 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-12 update BMRB 'update entry citation' 2012-03-02 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16992 'NMR complete assignment of the same protein in different condition: sodium acetate pH4' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ligand binding study of human PEBP1/RKIP: interaction with nucleotides and Raf-1 peptides evidenced by NMR and mass spectrometry.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22558375 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tavel Laurette . . 2 Jaquillard Lucie . . 3 Karsisiotis Andreas I. . 4 Saab Fabienne . . 5 Jouvensal Laurence . . 6 Brans Alain . . 7 Delmas Agnes F. . 8 Schoentgen Francoise . . 9 Cadene Martine . . 10 Damblon Christian . . stop_ _Journal_abbreviation 'PLoS ONE' _Journal_name_full 'PloS one' _Journal_volume 7 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hPEBP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hPEBP1 $hPEBP1 stop_ _System_molecular_weight 20924 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hPEBP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hPEBP1 _Molecular_mass 20924 _Mol_thiol_state 'all free' loop_ _Biological_function 'Raf-1 Kinase Inhibitory Protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 187 _Mol_residue_sequence ; MPVDLSKWSGPLSLQEVDEQ PQHPLHVTYAGAAVDELGKV LTPTQVKNRPTSISWDGLDS GKLYTLVLTDPDAPSRKDPK YREWHHFLVVNMKGNDISSG TVLSDYVGSGPPKGTGLHRY VWLVYEQDRPLKCDEPILSN RSGDHRGKFKVASFRKKYEL RAPVAGTCYQAEWDDYVPKL YEQLSGK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 VAL 4 ASP 5 LEU 6 SER 7 LYS 8 TRP 9 SER 10 GLY 11 PRO 12 LEU 13 SER 14 LEU 15 GLN 16 GLU 17 VAL 18 ASP 19 GLU 20 GLN 21 PRO 22 GLN 23 HIS 24 PRO 25 LEU 26 HIS 27 VAL 28 THR 29 TYR 30 ALA 31 GLY 32 ALA 33 ALA 34 VAL 35 ASP 36 GLU 37 LEU 38 GLY 39 LYS 40 VAL 41 LEU 42 THR 43 PRO 44 THR 45 GLN 46 VAL 47 LYS 48 ASN 49 ARG 50 PRO 51 THR 52 SER 53 ILE 54 SER 55 TRP 56 ASP 57 GLY 58 LEU 59 ASP 60 SER 61 GLY 62 LYS 63 LEU 64 TYR 65 THR 66 LEU 67 VAL 68 LEU 69 THR 70 ASP 71 PRO 72 ASP 73 ALA 74 PRO 75 SER 76 ARG 77 LYS 78 ASP 79 PRO 80 LYS 81 TYR 82 ARG 83 GLU 84 TRP 85 HIS 86 HIS 87 PHE 88 LEU 89 VAL 90 VAL 91 ASN 92 MET 93 LYS 94 GLY 95 ASN 96 ASP 97 ILE 98 SER 99 SER 100 GLY 101 THR 102 VAL 103 LEU 104 SER 105 ASP 106 TYR 107 VAL 108 GLY 109 SER 110 GLY 111 PRO 112 PRO 113 LYS 114 GLY 115 THR 116 GLY 117 LEU 118 HIS 119 ARG 120 TYR 121 VAL 122 TRP 123 LEU 124 VAL 125 TYR 126 GLU 127 GLN 128 ASP 129 ARG 130 PRO 131 LEU 132 LYS 133 CYS 134 ASP 135 GLU 136 PRO 137 ILE 138 LEU 139 SER 140 ASN 141 ARG 142 SER 143 GLY 144 ASP 145 HIS 146 ARG 147 GLY 148 LYS 149 PHE 150 LYS 151 VAL 152 ALA 153 SER 154 PHE 155 ARG 156 LYS 157 LYS 158 TYR 159 GLU 160 LEU 161 ARG 162 ALA 163 PRO 164 VAL 165 ALA 166 GLY 167 THR 168 CYS 169 TYR 170 GLN 171 ALA 172 GLU 173 TRP 174 ASP 175 ASP 176 TYR 177 VAL 178 PRO 179 LYS 180 LEU 181 TYR 182 GLU 183 GLN 184 LEU 185 SER 186 GLY 187 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 16992 RKIP 100.00 202 100.00 100.00 1.57e-133 BMRB 17382 Raf-1_kinase_inhibitor_protein 100.00 187 100.00 100.00 1.19e-133 PDB 1BD9 "Human Phosphatidylethanolamine Binding Protein" 100.00 187 100.00 100.00 1.19e-133 PDB 1BEH "Human Phosphatidylethanolamine Binding Protein In Complex With Cacodylate" 100.00 187 100.00 100.00 1.19e-133 PDB 2L7W "Solution Structure Of The Human Raf-1 Kinase Inhibitor Protein" 100.00 187 100.00 100.00 1.19e-133 PDB 2QYQ "Human Raf Kinase Inhibitor Protein (Rkip) In Complex With O- Phosphotyrosine" 100.00 187 100.00 100.00 1.19e-133 DBJ BAA03684 "rat phosphatidylethanolamine binding protein homologue [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 DBJ BAE88027 "unnamed protein product [Macaca fascicularis]" 100.00 187 97.33 97.86 1.07e-129 DBJ BAE88359 "unnamed protein product [Macaca fascicularis]" 75.40 165 98.58 99.29 4.60e-95 DBJ BAG34868 "unnamed protein product [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 DBJ BAG61396 "unnamed protein product [Homo sapiens]" 71.66 155 100.00 100.00 2.73e-91 EMBL CAA51652 "phosphatidylethanolamine-binding protein [Macaca fascicularis]" 100.00 187 97.86 98.40 2.44e-130 EMBL CAA53031 "phosphatidylethanolamine binding protein [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 EMBL CAA59404 "phosphatidylethanolamine binding protein [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 EMBL CAH93256 "hypothetical protein [Pongo abelii]" 100.00 187 98.93 100.00 2.22e-132 GB AAB32876 "neuropolypeptide h3 [human, brain, Peptide, 186 aa]" 99.47 186 100.00 100.00 1.49e-132 GB AAD14234 "neuropolypeptide h3, partial [Homo sapiens]" 74.87 140 100.00 100.00 1.80e-97 GB AAH08714 "Phosphatidylethanolamine binding protein 1 [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAH17396 "Phosphatidylethanolamine binding protein 1 [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAH31102 "Phosphatidylethanolamine binding protein 1 [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 PRF 2117380B "hippocampal cholinergic neurostimulating peptide" 100.00 187 100.00 100.00 1.19e-133 REF NP_001126915 "phosphatidylethanolamine-binding protein 1 [Pongo abelii]" 100.00 187 98.93 100.00 2.22e-132 REF NP_001233128 "phosphatidylethanolamine-binding protein 1 [Macaca mulatta]" 100.00 187 97.86 98.40 2.44e-130 REF NP_002558 "phosphatidylethanolamine-binding protein 1 [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 REF XP_002753109 "PREDICTED: phosphatidylethanolamine-binding protein 1 [Callithrix jacchus]" 100.00 187 98.93 99.47 2.19e-132 REF XP_004054017 "PREDICTED: phosphatidylethanolamine-binding protein 1 [Gorilla gorilla gorilla]" 100.00 187 99.47 99.47 5.90e-133 SP P30086 "RecName: Full=Phosphatidylethanolamine-binding protein 1; Short=PEBP-1; AltName: Full=HCNPpp; AltName: Full=Neuropolypeptide h3" 100.00 187 100.00 100.00 1.19e-133 SP P48737 "RecName: Full=Phosphatidylethanolamine-binding protein 1; Short=PEBP-1; AltName: Full=HCNPpp; Contains: RecName: Full=Hippocamp" 100.00 187 97.86 98.40 2.44e-130 SP Q5R4R0 "RecName: Full=Phosphatidylethanolamine-binding protein 1; Short=PEBP-1; AltName: Full=HCNPpp; Contains: RecName: Full=Hippocamp" 100.00 187 98.93 100.00 2.22e-132 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hPEBP1 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 _Variant _Vector_name $hPEBP1 'recombinant technology' . Escherichia coli BL21 DE3 pET31B 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 $hPEBP1 0.5 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' MES 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'Cryo-probe TXI' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.01 0.0005 M pH 6.5 0.1 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '3D HN(CO)CA' '3D HNCO' '3D HN(CA)CO' 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 hPEBP1 _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 3 3 VAL C C 174.068 0.002 1 2 3 3 VAL CA C 63.969 0.008 1 3 3 3 VAL CB C 31.727 0.003 1 4 4 4 ASP H H 8.561 0.007 1 5 4 4 ASP C C 176.688 0.008 1 6 4 4 ASP CA C 52.210 0.021 1 7 4 4 ASP CB C 40.969 0.005 1 8 4 4 ASP N N 128.114 0.006 1 9 5 5 LEU H H 9.030 0.007 1 10 5 5 LEU C C 178.125 0.007 1 11 5 5 LEU CA C 56.547 0.004 1 12 5 5 LEU CB C 41.573 0.059 1 13 5 5 LEU N N 122.936 0.003 1 14 6 6 SER H H 8.619 0.007 1 15 6 6 SER C C 176.572 0.007 1 16 6 6 SER CA C 61.635 0.085 1 17 6 6 SER CB C 62.465 0.122 1 18 6 6 SER N N 115.522 0.011 1 19 7 7 LYS H H 7.511 0.006 1 20 7 7 LYS C C 177.269 0.012 1 21 7 7 LYS CA C 55.238 0.002 1 22 7 7 LYS CB C 31.575 0.019 1 23 7 7 LYS N N 119.772 0.007 1 24 8 8 TRP H H 8.340 0.006 1 25 8 8 TRP C C 174.408 0.004 1 26 8 8 TRP CA C 62.417 0.021 1 27 8 8 TRP CB C 29.661 0.006 1 28 8 8 TRP N N 125.727 0.004 1 29 9 9 SER H H 8.003 0.007 1 30 9 9 SER C C 176.256 0.010 1 31 9 9 SER CA C 56.802 0.026 1 32 9 9 SER CB C 63.273 0.007 1 33 9 9 SER N N 106.001 0.009 1 34 10 10 GLY H H 7.298 0.006 1 35 10 10 GLY C C 172.910 0.000 1 36 10 10 GLY CA C 44.053 0.000 1 37 10 10 GLY N N 109.104 0.003 1 38 11 11 PRO C C 178.796 0.004 1 39 11 11 PRO CA C 65.251 0.009 1 40 11 11 PRO CB C 32.005 0.011 1 41 12 12 LEU H H 9.245 0.007 1 42 12 12 LEU C C 175.946 0.013 1 43 12 12 LEU CA C 57.144 0.071 1 44 12 12 LEU CB C 42.376 0.010 1 45 12 12 LEU N N 117.782 0.004 1 46 13 13 SER H H 8.596 0.007 1 47 13 13 SER C C 175.692 0.004 1 48 13 13 SER CA C 57.594 0.048 1 49 13 13 SER CB C 62.649 0.012 1 50 13 13 SER N N 111.523 0.005 1 51 14 14 LEU H H 8.169 0.007 1 52 14 14 LEU C C 178.682 0.009 1 53 14 14 LEU CA C 56.978 0.003 1 54 14 14 LEU CB C 37.315 0.002 1 55 14 14 LEU N N 116.604 0.004 1 56 15 15 GLN H H 9.515 0.007 1 57 15 15 GLN C C 177.581 0.009 1 58 15 15 GLN CA C 57.257 0.025 1 59 15 15 GLN CB C 25.285 0.005 1 60 15 15 GLN N N 121.970 0.005 1 61 16 16 GLU H H 7.722 0.007 1 62 16 16 GLU C C 176.570 0.006 1 63 16 16 GLU CA C 58.333 0.012 1 64 16 16 GLU CB C 30.586 0.002 1 65 16 16 GLU N N 120.090 0.009 1 66 17 17 VAL H H 8.397 0.007 1 67 17 17 VAL C C 175.093 0.013 1 68 17 17 VAL CA C 65.072 0.013 1 69 17 17 VAL CB C 32.074 0.021 1 70 17 17 VAL N N 119.901 0.003 1 71 18 18 ASP H H 8.131 0.007 1 72 18 18 ASP C C 173.787 0.002 1 73 18 18 ASP CA C 53.315 0.007 1 74 18 18 ASP CB C 42.955 0.013 1 75 18 18 ASP N N 111.149 0.009 1 76 19 19 GLU H H 8.931 0.006 1 77 19 19 GLU C C 172.465 0.005 1 78 19 19 GLU CA C 55.826 0.012 1 79 19 19 GLU CB C 31.909 0.007 1 80 19 19 GLU N N 118.055 0.005 1 81 20 20 GLN H H 7.773 0.007 1 82 20 20 GLN C C 174.186 0.000 1 83 20 20 GLN CA C 53.220 0.000 1 84 20 20 GLN CB C 30.287 0.000 1 85 20 20 GLN N N 117.338 0.005 1 86 21 21 PRO C C 176.483 0.000 1 87 21 21 PRO CA C 68.622 0.105 1 88 22 22 GLN H H 7.706 0.007 1 89 22 22 GLN C C 178.466 0.010 1 90 22 22 GLN CA C 58.663 0.043 1 91 22 22 GLN CB C 29.394 0.028 1 92 22 22 GLN N N 119.327 0.009 1 93 23 23 HIS H H 6.871 0.006 1 94 23 23 HIS C C 174.925 0.000 1 95 23 23 HIS CA C 59.141 0.000 1 96 23 23 HIS CB C 30.127 0.000 1 97 23 23 HIS N N 108.583 0.006 1 98 24 24 PRO C C 175.594 0.002 1 99 24 24 PRO CA C 62.660 0.007 1 100 24 24 PRO CB C 32.177 0.004 1 101 25 25 LEU H H 7.578 0.007 1 102 25 25 LEU C C 174.629 0.011 1 103 25 25 LEU CA C 53.110 0.015 1 104 25 25 LEU CB C 43.745 0.010 1 105 25 25 LEU N N 123.600 0.008 1 106 26 26 HIS H H 9.315 0.006 1 107 26 26 HIS C C 174.962 0.006 1 108 26 26 HIS CA C 56.381 0.024 1 109 26 26 HIS CB C 29.680 0.004 1 110 26 26 HIS N N 127.845 0.006 1 111 27 27 VAL H H 7.355 0.008 1 112 27 27 VAL C C 173.927 0.008 1 113 27 27 VAL CA C 61.683 0.033 1 114 27 27 VAL CB C 34.720 0.002 1 115 27 27 VAL N N 124.696 0.002 1 116 28 28 THR H H 8.268 0.006 1 117 28 28 THR C C 172.123 0.005 1 118 28 28 THR CA C 61.276 0.042 1 119 28 28 THR CB C 70.991 0.012 1 120 28 28 THR N N 121.087 0.009 1 121 29 29 TYR H H 9.010 0.007 1 122 29 29 TYR C C 175.097 0.010 1 123 29 29 TYR CA C 56.823 0.014 1 124 29 29 TYR CB C 40.377 0.022 1 125 29 29 TYR N N 122.471 0.005 1 126 30 30 ALA H H 8.430 0.007 1 127 30 30 ALA C C 178.033 0.004 1 128 30 30 ALA CA C 54.727 0.003 1 129 30 30 ALA CB C 17.761 0.011 1 130 30 30 ALA N N 123.703 0.008 1 131 31 31 GLY H H 8.666 0.007 1 132 31 31 GLY C C 173.955 0.009 1 133 31 31 GLY CA C 45.308 0.016 1 134 31 31 GLY N N 106.333 0.005 1 135 32 32 ALA H H 7.312 0.006 1 136 32 32 ALA C C 174.592 0.005 1 137 32 32 ALA CA C 51.793 0.055 1 138 32 32 ALA CB C 22.285 0.071 1 139 32 32 ALA N N 120.410 0.005 1 140 33 33 ALA H H 8.746 0.007 1 141 33 33 ALA C C 176.676 0.004 1 142 33 33 ALA CA C 51.298 0.043 1 143 33 33 ALA CB C 22.134 0.002 1 144 33 33 ALA N N 121.258 0.004 1 145 34 34 VAL H H 8.326 0.006 1 146 34 34 VAL C C 175.692 0.000 1 147 34 34 VAL CA C 62.567 0.000 1 148 34 34 VAL CB C 29.622 0.000 1 149 34 34 VAL N N 119.356 0.006 1 150 35 35 ASP C C 173.394 0.006 1 151 35 35 ASP CA C 53.220 0.015 1 152 35 35 ASP CB C 39.851 0.011 1 153 36 36 GLU H H 7.252 0.006 1 154 36 36 GLU C C 175.688 0.004 1 155 36 36 GLU CA C 55.254 0.005 1 156 36 36 GLU CB C 34.005 0.009 1 157 36 36 GLU N N 114.240 0.001 1 158 37 37 LEU H H 9.552 0.007 1 159 37 37 LEU C C 177.592 0.006 1 160 37 37 LEU CA C 56.908 0.013 1 161 37 37 LEU CB C 41.380 0.006 1 162 37 37 LEU N N 126.469 0.003 1 163 38 38 GLY H H 9.269 0.007 1 164 38 38 GLY C C 172.828 0.014 1 165 38 38 GLY CA C 45.823 0.012 1 166 38 38 GLY N N 116.480 0.005 1 167 39 39 LYS H H 7.576 0.006 1 168 39 39 LYS C C 175.035 0.002 1 169 39 39 LYS CA C 57.163 0.008 1 170 39 39 LYS CB C 35.651 0.003 1 171 39 39 LYS N N 121.507 0.004 1 172 40 40 VAL H H 8.764 0.007 1 173 40 40 VAL C C 176.102 0.010 1 174 40 40 VAL CA C 63.309 0.011 1 175 40 40 VAL CB C 31.623 0.019 1 176 40 40 VAL N N 128.133 0.006 1 177 41 41 LEU H H 9.232 0.007 1 178 41 41 LEU C C 176.428 0.007 1 179 41 41 LEU CA C 52.928 0.005 1 180 41 41 LEU CB C 45.821 0.008 1 181 41 41 LEU N N 130.211 0.004 1 182 42 42 THR H H 8.626 0.007 1 183 42 42 THR C C 174.602 0.000 1 184 42 42 THR CA C 58.492 0.000 1 185 42 42 THR CB C 68.731 0.000 1 186 42 42 THR N N 110.207 0.007 1 187 43 43 PRO C C 179.489 0.000 1 188 43 43 PRO CA C 65.275 0.006 1 189 43 43 PRO CB C 29.550 0.009 1 190 44 44 THR H H 8.606 0.006 1 191 44 44 THR C C 176.465 0.000 1 192 44 44 THR CA C 68.650 0.000 1 193 44 44 THR N N 115.057 0.007 1 194 45 45 GLN C C 174.670 0.004 1 195 45 45 GLN CA C 58.449 0.000 1 196 45 45 GLN CB C 29.693 0.000 1 197 46 46 VAL H H 6.681 0.007 1 198 46 46 VAL C C 176.053 0.000 1 199 46 46 VAL CA C 60.670 0.000 1 200 46 46 VAL CB C 32.292 0.000 1 201 46 46 VAL N N 115.984 0.003 1 202 47 47 LYS C C 175.967 0.002 1 203 47 47 LYS CA C 58.314 0.017 1 204 47 47 LYS CB C 31.377 0.008 1 205 48 48 ASN H H 8.114 0.007 1 206 48 48 ASN C C 172.278 0.008 1 207 48 48 ASN CA C 50.977 0.013 1 208 48 48 ASN CB C 41.624 0.000 1 209 48 48 ASN N N 118.686 0.006 1 210 49 49 ARG H H 7.568 0.007 1 211 49 49 ARG C C 174.041 0.000 1 212 49 49 ARG CA C 54.331 0.000 1 213 49 49 ARG CB C 29.527 0.000 1 214 49 49 ARG N N 113.624 0.002 1 215 50 50 PRO C C 175.577 0.006 1 216 50 50 PRO CA C 63.511 0.007 1 217 50 50 PRO CB C 31.795 0.006 1 218 51 51 THR H H 8.651 0.006 1 219 51 51 THR C C 176.381 0.012 1 220 51 51 THR CA C 62.281 0.018 1 221 51 51 THR CB C 68.656 0.018 1 222 51 51 THR N N 112.507 0.002 1 223 52 52 SER H H 7.254 0.006 1 224 52 52 SER C C 172.276 0.004 1 225 52 52 SER CA C 58.333 0.012 1 226 52 52 SER CB C 65.000 0.015 1 227 52 52 SER N N 113.374 0.008 1 228 53 53 ILE H H 8.341 0.007 1 229 53 53 ILE C C 174.541 0.007 1 230 53 53 ILE CA C 59.231 0.063 1 231 53 53 ILE CB C 41.876 0.014 1 232 53 53 ILE N N 116.763 0.006 1 233 54 54 SER H H 8.497 0.006 1 234 54 54 SER C C 171.329 0.004 1 235 54 54 SER CA C 59.068 0.020 1 236 54 54 SER CB C 63.973 0.015 1 237 54 54 SER N N 112.502 0.002 1 238 55 55 TRP H H 6.594 0.005 1 239 55 55 TRP C C 174.348 0.004 1 240 55 55 TRP CA C 56.873 0.011 1 241 55 55 TRP CB C 33.086 0.010 1 242 55 55 TRP N N 119.040 0.004 1 243 56 56 ASP H H 9.557 0.007 1 244 56 56 ASP C C 175.327 0.007 1 245 56 56 ASP CA C 55.250 0.006 1 246 56 56 ASP CB C 40.303 0.011 1 247 56 56 ASP N N 124.021 0.005 1 248 57 57 GLY H H 8.102 0.008 1 249 57 57 GLY C C 174.928 0.013 1 250 57 57 GLY CA C 44.677 0.011 1 251 57 57 GLY N N 107.599 0.009 1 252 58 58 LEU H H 6.397 0.007 1 253 58 58 LEU C C 174.552 0.006 1 254 58 58 LEU CA C 56.719 0.007 1 255 58 58 LEU CB C 41.421 0.003 1 256 58 58 LEU N N 123.022 0.009 1 257 59 59 ASP H H 7.972 0.007 1 258 59 59 ASP C C 176.711 0.007 1 259 59 59 ASP CA C 52.133 0.015 1 260 59 59 ASP CB C 43.215 0.015 1 261 59 59 ASP N N 127.249 0.006 1 262 60 60 SER H H 8.869 0.007 1 263 60 60 SER C C 174.380 0.025 1 264 60 60 SER CA C 60.937 0.031 1 265 60 60 SER CB C 62.911 0.004 1 266 60 60 SER N N 121.872 0.006 1 267 61 61 GLY H H 9.253 0.007 1 268 61 61 GLY CA C 44.830 0.027 1 269 61 61 GLY N N 109.190 0.005 1 270 62 62 LYS H H 7.681 0.007 1 271 62 62 LYS C C 174.032 0.008 1 272 62 62 LYS CA C 55.421 0.009 1 273 62 62 LYS CB C 35.485 0.002 1 274 62 62 LYS N N 122.142 0.004 1 275 63 63 LEU H H 8.168 0.007 1 276 63 63 LEU C C 175.809 0.008 1 277 63 63 LEU CA C 52.240 0.021 1 278 63 63 LEU CB C 45.853 0.031 1 279 63 63 LEU N N 119.349 0.007 1 280 64 64 TYR H H 9.478 0.006 1 281 64 64 TYR C C 174.835 0.009 1 282 64 64 TYR CA C 57.289 0.023 1 283 64 64 TYR CB C 43.329 0.103 1 284 64 64 TYR N N 116.893 0.004 1 285 65 65 THR H H 9.360 0.007 1 286 65 65 THR C C 172.467 0.004 1 287 65 65 THR CA C 62.388 0.022 1 288 65 65 THR CB C 72.840 0.012 1 289 65 65 THR N N 118.121 0.014 1 290 66 66 LEU H H 9.574 0.007 1 291 66 66 LEU C C 174.320 0.004 1 292 66 66 LEU CA C 53.433 0.011 1 293 66 66 LEU CB C 47.591 0.007 1 294 66 66 LEU N N 129.861 0.004 1 295 67 67 VAL H H 9.430 0.007 1 296 67 67 VAL C C 173.767 0.004 1 297 67 67 VAL CA C 60.190 0.010 1 298 67 67 VAL CB C 36.829 0.001 1 299 67 67 VAL N N 124.628 0.005 1 300 68 68 LEU H H 8.386 0.007 1 301 68 68 LEU C C 176.441 0.008 1 302 68 68 LEU CA C 53.752 0.010 1 303 68 68 LEU CB C 44.562 0.033 1 304 68 68 LEU N N 125.508 0.003 1 305 69 69 THR H H 9.225 0.007 1 306 69 69 THR C C 169.322 0.003 1 307 69 69 THR CA C 60.332 0.011 1 308 69 69 THR CB C 72.389 0.010 1 309 69 69 THR N N 124.025 0.005 1 310 70 70 ASP H H 8.399 0.007 1 311 70 70 ASP C C 175.984 0.000 1 312 70 70 ASP CA C 49.719 0.000 1 313 70 70 ASP CB C 43.040 0.000 1 314 70 70 ASP N N 126.287 0.010 1 315 71 71 PRO C C 176.163 0.007 1 316 71 71 PRO CA C 63.226 0.020 1 317 71 71 PRO CB C 32.144 0.045 1 318 72 72 ASP H H 9.307 0.007 1 319 72 72 ASP C C 170.425 0.003 1 320 72 72 ASP CA C 54.456 0.016 1 321 72 72 ASP CB C 40.792 0.033 1 322 72 72 ASP N N 130.276 0.012 1 323 73 73 ALA H H 5.629 0.008 1 324 73 73 ALA C C 176.071 0.000 1 325 73 73 ALA CA C 47.358 0.000 1 326 73 73 ALA CB C 22.349 0.000 1 327 73 73 ALA N N 116.245 0.007 1 328 74 74 PRO C C 174.702 0.004 1 329 74 74 PRO CA C 64.689 0.015 1 330 74 74 PRO CB C 34.409 0.022 1 331 75 75 SER H H 6.589 0.006 1 332 75 75 SER C C 173.258 0.005 1 333 75 75 SER CA C 56.744 0.016 1 334 75 75 SER CB C 66.984 0.005 1 335 75 75 SER N N 110.261 0.003 1 336 76 76 ARG H H 8.982 0.007 1 337 76 76 ARG C C 177.685 0.006 1 338 76 76 ARG CA C 58.661 0.019 1 339 76 76 ARG CB C 30.579 0.004 1 340 76 76 ARG N N 120.621 0.004 1 341 77 77 LYS H H 7.483 0.006 1 342 77 77 LYS C C 176.603 0.007 1 343 77 77 LYS CA C 57.475 0.003 1 344 77 77 LYS CB C 32.789 0.003 1 345 77 77 LYS N N 115.346 0.007 1 346 78 78 ASP H H 7.284 0.007 1 347 78 78 ASP C C 173.147 0.000 1 348 78 78 ASP CA C 51.440 0.000 1 349 78 78 ASP CB C 40.717 0.000 1 350 78 78 ASP N N 116.601 0.004 1 351 79 79 PRO C C 178.679 0.000 1 352 79 79 PRO CA C 63.341 0.028 1 353 79 79 PRO CB C 28.740 0.003 1 354 80 80 LYS H H 8.407 0.007 1 355 80 80 LYS C C 177.600 0.008 1 356 80 80 LYS CA C 58.977 0.010 1 357 80 80 LYS CB C 33.022 0.018 1 358 80 80 LYS N N 123.820 0.008 1 359 81 81 TYR H H 9.001 0.007 1 360 81 81 TYR C C 174.595 0.005 1 361 81 81 TYR CA C 54.268 0.017 1 362 81 81 TYR CB C 37.540 0.011 1 363 81 81 TYR N N 117.285 0.006 1 364 82 82 ARG H H 7.605 0.006 1 365 82 82 ARG C C 177.670 0.009 1 366 82 82 ARG CA C 51.978 0.023 1 367 82 82 ARG CB C 31.922 0.004 1 368 82 82 ARG N N 121.252 0.009 1 369 83 83 GLU H H 9.714 0.009 1 370 83 83 GLU C C 174.895 0.006 1 371 83 83 GLU CA C 58.201 0.027 1 372 83 83 GLU CB C 30.299 0.013 1 373 83 83 GLU N N 128.517 0.017 1 374 84 84 TRP H H 9.144 0.007 1 375 84 84 TRP C C 176.407 0.008 1 376 84 84 TRP CA C 58.114 0.021 1 377 84 84 TRP CB C 32.131 0.026 1 378 84 84 TRP N N 124.605 0.005 1 379 85 85 HIS H H 7.871 0.006 1 380 85 85 HIS C C 171.870 0.007 1 381 85 85 HIS CA C 55.470 0.013 1 382 85 85 HIS CB C 30.751 0.116 1 383 85 85 HIS N N 124.732 0.008 1 384 86 86 HIS H H 8.707 0.006 1 385 86 86 HIS C C 175.328 0.007 1 386 86 86 HIS CA C 59.408 0.012 1 387 86 86 HIS CB C 31.249 0.079 1 388 86 86 HIS N N 122.734 0.009 1 389 87 87 PHE H H 7.742 0.006 1 390 87 87 PHE C C 173.048 0.002 1 391 87 87 PHE CA C 54.153 0.017 1 392 87 87 PHE CB C 43.089 0.010 1 393 87 87 PHE N N 118.670 0.007 1 394 88 88 LEU H H 8.416 0.007 1 395 88 88 LEU C C 173.537 0.003 1 396 88 88 LEU CA C 55.566 0.002 1 397 88 88 LEU CB C 45.666 0.008 1 398 88 88 LEU N N 129.028 0.002 1 399 89 89 VAL H H 9.266 0.007 1 400 89 89 VAL C C 174.203 0.007 1 401 89 89 VAL CA C 60.606 0.015 1 402 89 89 VAL CB C 35.813 0.026 1 403 89 89 VAL N N 130.476 0.008 1 404 90 90 VAL H H 8.688 0.006 1 405 90 90 VAL C C 175.455 0.011 1 406 90 90 VAL CA C 58.601 0.006 1 407 90 90 VAL CB C 35.820 0.020 1 408 90 90 VAL N N 116.100 0.006 1 409 91 91 ASN H H 9.391 0.006 1 410 91 91 ASN C C 173.417 0.005 1 411 91 91 ASN CA C 54.363 0.011 1 412 91 91 ASN CB C 36.207 0.062 1 413 91 91 ASN N N 115.573 0.004 1 414 92 92 MET H H 9.363 0.007 1 415 92 92 MET C C 175.017 0.010 1 416 92 92 MET CA C 56.420 0.036 1 417 92 92 MET CB C 34.176 0.018 1 418 92 92 MET N N 120.005 0.003 1 419 93 93 LYS H H 8.555 0.007 1 420 93 93 LYS C C 177.828 0.008 1 421 93 93 LYS CA C 55.705 0.020 1 422 93 93 LYS CB C 31.600 0.026 1 423 93 93 LYS N N 127.099 0.006 1 424 94 94 GLY H H 8.965 0.006 1 425 94 94 GLY C C 169.868 0.007 1 426 94 94 GLY CA C 48.125 0.010 1 427 94 94 GLY N N 118.169 0.008 1 428 95 95 ASN H H 7.725 0.006 1 429 95 95 ASN C C 175.512 0.008 1 430 95 95 ASN CA C 50.612 0.018 1 431 95 95 ASN CB C 37.631 0.017 1 432 95 95 ASN N N 118.946 0.004 1 433 96 96 ASP H H 7.843 0.006 1 434 96 96 ASP C C 177.178 0.013 1 435 96 96 ASP CA C 52.221 0.029 1 436 96 96 ASP CB C 39.346 0.008 1 437 96 96 ASP N N 116.729 0.005 1 438 97 97 ILE H H 8.289 0.007 1 439 97 97 ILE C C 177.491 0.007 1 440 97 97 ILE CA C 65.893 0.009 1 441 97 97 ILE CB C 38.269 0.003 1 442 97 97 ILE N N 129.549 0.009 1 443 98 98 SER H H 8.073 0.007 1 444 98 98 SER C C 174.691 0.006 1 445 98 98 SER CA C 60.702 0.014 1 446 98 98 SER CB C 63.401 0.007 1 447 98 98 SER N N 113.210 0.005 1 448 99 99 SER H H 7.860 0.006 1 449 99 99 SER C C 175.547 0.011 1 450 99 99 SER CA C 59.484 0.023 1 451 99 99 SER CB C 65.337 0.020 1 452 99 99 SER N N 117.440 0.006 1 453 100 100 GLY H H 7.723 0.006 1 454 100 100 GLY C C 172.877 0.006 1 455 100 100 GLY CA C 44.240 0.014 1 456 100 100 GLY N N 107.360 0.004 1 457 101 101 THR H H 9.354 0.006 1 458 101 101 THR C C 173.192 0.011 1 459 101 101 THR CA C 62.365 0.031 1 460 101 101 THR CB C 69.834 0.006 1 461 101 101 THR N N 118.052 0.004 1 462 102 102 VAL H H 9.009 0.007 1 463 102 102 VAL C C 175.696 0.004 1 464 102 102 VAL CA C 63.024 0.021 1 465 102 102 VAL CB C 30.889 0.008 1 466 102 102 VAL N N 129.556 0.006 1 467 103 103 LEU H H 8.409 0.007 1 468 103 103 LEU C C 176.368 0.014 1 469 103 103 LEU CA C 56.628 0.026 1 470 103 103 LEU CB C 41.392 0.017 1 471 103 103 LEU N N 131.991 0.006 1 472 104 104 SER H H 7.745 0.006 1 473 104 104 SER C C 173.689 0.004 1 474 104 104 SER CA C 55.736 0.015 1 475 104 104 SER CB C 62.739 0.004 1 476 104 104 SER N N 110.953 0.005 1 477 105 105 ASP H H 8.065 0.006 1 478 105 105 ASP C C 176.333 0.005 1 479 105 105 ASP CA C 54.076 0.011 1 480 105 105 ASP CB C 40.425 0.025 1 481 105 105 ASP N N 123.296 0.005 1 482 106 106 TYR H H 8.977 0.007 1 483 106 106 TYR C C 174.332 0.004 1 484 106 106 TYR CA C 61.251 0.004 1 485 106 106 TYR CB C 38.787 0.007 1 486 106 106 TYR N N 122.814 0.005 1 487 107 107 VAL H H 7.670 0.006 1 488 107 107 VAL C C 175.329 0.007 1 489 107 107 VAL CA C 61.405 0.028 1 490 107 107 VAL CB C 35.842 0.004 1 491 107 107 VAL N N 130.913 0.004 1 492 108 108 GLY H H 7.995 0.006 1 493 108 108 GLY C C 173.254 0.006 1 494 108 108 GLY CA C 44.353 0.008 1 495 108 108 GLY N N 112.672 0.011 1 496 109 109 SER H H 6.134 0.006 1 497 109 109 SER C C 172.183 0.015 1 498 109 109 SER CA C 61.248 0.019 1 499 109 109 SER CB C 64.895 0.030 1 500 109 109 SER N N 110.439 0.006 1 501 110 110 GLY H H 7.647 0.008 1 502 110 110 GLY C C 170.035 0.000 1 503 110 110 GLY CA C 47.267 0.000 1 504 110 110 GLY N N 109.438 0.012 1 505 112 112 PRO C C 178.774 0.003 1 506 112 112 PRO CA C 62.572 0.005 1 507 112 112 PRO CB C 32.089 0.000 1 508 113 113 LYS H H 9.095 0.006 1 509 113 113 LYS C C 177.569 0.007 1 510 113 113 LYS CA C 58.780 0.013 1 511 113 113 LYS CB C 31.790 0.039 1 512 113 113 LYS N N 130.075 0.004 1 513 114 114 GLY H H 9.114 0.007 1 514 114 114 GLY C C 175.661 0.016 1 515 114 114 GLY CA C 45.585 0.012 1 516 114 114 GLY N N 113.930 0.008 1 517 115 115 THR H H 7.537 0.006 1 518 115 115 THR C C 174.587 0.009 1 519 115 115 THR CA C 62.003 0.016 1 520 115 115 THR CB C 71.112 0.010 1 521 115 115 THR N N 106.952 0.007 1 522 116 116 GLY H H 8.516 0.006 1 523 116 116 GLY C C 173.782 0.008 1 524 116 116 GLY CA C 44.916 0.010 1 525 116 116 GLY N N 111.580 0.006 1 526 117 117 LEU H H 8.577 0.007 1 527 117 117 LEU C C 179.841 0.005 1 528 117 117 LEU CA C 55.299 0.003 1 529 117 117 LEU CB C 43.111 0.018 1 530 117 117 LEU N N 118.539 0.006 1 531 118 118 HIS H H 9.194 0.006 1 532 118 118 HIS C C 174.066 0.008 1 533 118 118 HIS CA C 53.554 0.017 1 534 118 118 HIS CB C 29.926 0.018 1 535 118 118 HIS N N 126.251 0.007 1 536 119 119 ARG H H 9.255 0.007 1 537 119 119 ARG C C 171.434 0.004 1 538 119 119 ARG CA C 55.918 0.024 1 539 119 119 ARG CB C 30.777 0.025 1 540 119 119 ARG N N 122.292 0.009 1 541 120 120 TYR H H 8.534 0.006 1 542 120 120 TYR C C 174.591 0.005 1 543 120 120 TYR CA C 57.476 0.006 1 544 120 120 TYR CB C 38.047 0.018 1 545 120 120 TYR N N 117.633 0.003 1 546 121 121 VAL H H 8.919 0.006 1 547 121 121 VAL C C 175.332 0.004 1 548 121 121 VAL CA C 62.236 0.008 1 549 121 121 VAL CB C 33.432 0.013 1 550 121 121 VAL N N 124.246 0.002 1 551 122 122 TRP H H 8.422 0.007 1 552 122 122 TRP C C 176.597 0.005 1 553 122 122 TRP CA C 55.323 0.008 1 554 122 122 TRP CB C 34.473 0.003 1 555 122 122 TRP N N 127.607 0.003 1 556 123 123 LEU H H 9.662 0.007 1 557 123 123 LEU C C 174.251 0.005 1 558 123 123 LEU CA C 54.270 0.010 1 559 123 123 LEU CB C 48.781 0.016 1 560 123 123 LEU N N 121.530 0.004 1 561 124 124 VAL H H 8.135 0.007 1 562 124 124 VAL C C 175.033 0.005 1 563 124 124 VAL CA C 59.707 0.008 1 564 124 124 VAL CB C 34.263 0.010 1 565 124 124 VAL N N 118.434 0.005 1 566 125 125 TYR H H 9.597 0.007 1 567 125 125 TYR C C 175.548 0.009 1 568 125 125 TYR CA C 56.921 0.051 1 569 125 125 TYR CB C 42.812 0.002 1 570 125 125 TYR N N 124.953 0.004 1 571 126 126 GLU H H 9.009 0.007 1 572 126 126 GLU C C 175.042 0.004 1 573 126 126 GLU CA C 56.394 0.058 1 574 126 126 GLU CB C 32.235 0.004 1 575 126 126 GLU N N 123.989 0.001 1 576 127 127 GLN H H 8.509 0.006 1 577 127 127 GLN C C 176.478 0.009 1 578 127 127 GLN CA C 54.332 0.046 1 579 127 127 GLN CB C 30.418 0.004 1 580 127 127 GLN N N 122.305 0.007 1 581 128 128 ASP H H 8.921 0.007 1 582 128 128 ASP C C 175.187 0.010 1 583 128 128 ASP CA C 54.791 0.033 1 584 128 128 ASP CB C 41.924 0.016 1 585 128 128 ASP N N 120.679 0.004 1 586 129 129 ARG H H 7.886 0.007 1 587 129 129 ARG C C 172.762 0.000 1 588 129 129 ARG CA C 53.668 0.000 1 589 129 129 ARG CB C 29.321 0.000 1 590 129 129 ARG N N 116.508 0.004 1 591 130 130 PRO C C 176.136 0.002 1 592 130 130 PRO CA C 63.058 0.007 1 593 130 130 PRO CB C 31.427 0.014 1 594 131 131 LEU H H 9.552 0.007 1 595 131 131 LEU C C 177.418 0.007 1 596 131 131 LEU CA C 53.956 0.009 1 597 131 131 LEU CB C 44.322 0.007 1 598 131 131 LEU N N 124.646 0.007 1 599 132 132 LYS H H 8.596 0.007 1 600 132 132 LYS C C 175.313 0.005 1 601 132 132 LYS CA C 55.355 0.007 1 602 132 132 LYS CB C 32.520 0.020 1 603 132 132 LYS N N 125.846 0.004 1 604 133 133 CYS H H 8.763 0.008 1 605 133 133 CYS C C 176.202 0.011 1 606 133 133 CYS CA C 59.145 0.015 1 607 133 133 CYS CB C 29.689 0.018 1 608 133 133 CYS N N 125.055 0.004 1 609 134 134 ASP H H 8.260 0.006 1 610 134 134 ASP C C 175.664 0.010 1 611 134 134 ASP CA C 53.068 0.023 1 612 134 134 ASP CB C 40.119 0.013 1 613 134 134 ASP N N 121.912 0.009 1 614 135 135 GLU H H 8.855 0.007 1 615 135 135 GLU C C 172.771 0.000 1 616 135 135 GLU CA C 57.514 0.000 1 617 135 135 GLU CB C 28.445 0.000 1 618 135 135 GLU N N 125.994 0.005 1 619 136 136 PRO C C 174.224 0.003 1 620 136 136 PRO CA C 61.840 0.014 1 621 136 136 PRO CB C 31.747 0.001 1 622 137 137 ILE H H 7.967 0.007 1 623 137 137 ILE C C 177.607 0.022 1 624 137 137 ILE CA C 58.937 0.010 1 625 137 137 ILE CB C 35.774 0.010 1 626 137 137 ILE N N 118.795 0.006 1 627 138 138 LEU H H 9.501 0.007 1 628 138 138 LEU C C 177.834 0.010 1 629 138 138 LEU CA C 53.575 0.023 1 630 138 138 LEU CB C 41.767 0.024 1 631 138 138 LEU N N 129.672 0.008 1 632 139 139 SER H H 8.882 0.007 1 633 139 139 SER C C 174.244 0.014 1 634 139 139 SER CA C 57.014 0.016 1 635 139 139 SER CB C 65.126 0.006 1 636 139 139 SER N N 122.476 0.007 1 637 140 140 ASN H H 8.623 0.007 1 638 140 140 ASN C C 174.308 0.000 1 639 140 140 ASN CA C 50.941 0.011 1 640 140 140 ASN CB C 37.616 0.019 1 641 140 140 ASN N N 116.142 0.002 1 642 141 141 ARG H H 8.018 0.007 1 643 141 141 ARG C C 174.310 0.008 1 644 141 141 ARG CA C 54.624 0.012 1 645 141 141 ARG CB C 30.336 0.008 1 646 141 141 ARG N N 114.378 0.002 1 647 142 142 SER H H 6.982 0.007 1 648 142 142 SER C C 175.121 0.006 1 649 142 142 SER CA C 56.636 0.007 1 650 142 142 SER CB C 65.105 0.004 1 651 142 142 SER N N 109.898 0.004 1 652 143 143 GLY H H 8.947 0.007 1 653 143 143 GLY C C 174.140 0.010 1 654 143 143 GLY CA C 44.797 0.029 1 655 143 143 GLY N N 114.859 0.005 1 656 144 144 ASP H H 8.272 0.007 1 657 144 144 ASP C C 176.329 0.011 1 658 144 144 ASP CA C 55.627 0.010 1 659 144 144 ASP CB C 40.419 0.036 1 660 144 144 ASP N N 121.991 0.009 1 661 145 145 HIS H H 8.719 0.009 1 662 145 145 HIS C C 174.939 0.008 1 663 145 145 HIS CA C 57.001 0.021 1 664 145 145 HIS CB C 27.008 0.018 1 665 145 145 HIS N N 112.280 0.003 1 666 146 146 ARG H H 7.162 0.007 1 667 146 146 ARG C C 178.867 0.010 1 668 146 146 ARG CA C 56.446 0.028 1 669 146 146 ARG CB C 30.524 0.034 1 670 146 146 ARG N N 117.790 0.004 1 671 147 147 GLY H H 8.312 0.007 1 672 147 147 GLY C C 173.725 0.013 1 673 147 147 GLY CA C 44.310 0.016 1 674 147 147 GLY N N 107.292 0.009 1 675 148 148 LYS H H 8.183 0.006 1 676 148 148 LYS C C 175.818 0.013 1 677 148 148 LYS CA C 57.448 0.082 1 678 148 148 LYS CB C 28.785 0.013 1 679 148 148 LYS N N 114.469 0.005 1 680 149 149 PHE H H 9.820 0.006 1 681 149 149 PHE C C 174.324 0.006 1 682 149 149 PHE CA C 57.263 0.018 1 683 149 149 PHE CB C 41.127 0.004 1 684 149 149 PHE N N 123.281 0.005 1 685 150 150 LYS H H 7.327 0.007 1 686 150 150 LYS C C 176.440 0.004 1 687 150 150 LYS CA C 53.579 0.029 1 688 150 150 LYS CB C 34.282 0.008 1 689 150 150 LYS N N 123.946 0.005 1 690 151 151 VAL H H 10.160 0.007 1 691 151 151 VAL C C 175.503 0.006 1 692 151 151 VAL CA C 65.886 0.011 1 693 151 151 VAL CB C 31.115 0.019 1 694 151 151 VAL N N 131.678 0.006 1 695 152 152 ALA H H 9.759 0.007 1 696 152 152 ALA C C 180.275 0.008 1 697 152 152 ALA CA C 54.954 0.018 1 698 152 152 ALA CB C 18.393 0.010 1 699 152 152 ALA N N 124.108 0.005 1 700 153 153 SER H H 6.775 0.007 1 701 153 153 SER C C 176.362 0.174 1 702 153 153 SER CA C 61.044 0.054 1 703 153 153 SER CB C 62.426 0.119 1 704 153 153 SER N N 110.754 0.007 1 705 154 154 PHE H H 8.136 0.008 1 706 154 154 PHE C C 176.123 0.000 1 707 154 154 PHE CA C 61.867 0.011 1 708 154 154 PHE CB C 39.448 0.030 1 709 154 154 PHE N N 125.926 0.014 1 710 155 155 ARG H H 9.052 0.007 1 711 155 155 ARG C C 178.338 0.007 1 712 155 155 ARG CA C 58.521 0.009 1 713 155 155 ARG CB C 26.844 0.009 1 714 155 155 ARG N N 117.918 0.003 1 715 156 156 LYS H H 7.547 0.006 1 716 156 156 LYS C C 180.372 0.012 1 717 156 156 LYS CA C 60.286 0.005 1 718 156 156 LYS CB C 32.433 0.025 1 719 156 156 LYS N N 120.469 0.005 1 720 157 157 LYS H H 7.993 0.007 1 721 157 157 LYS C C 177.574 0.005 1 722 157 157 LYS CA C 59.197 0.023 1 723 157 157 LYS CB C 31.545 0.010 1 724 157 157 LYS N N 125.875 0.006 1 725 158 158 TYR H H 6.493 0.006 1 726 158 158 TYR C C 172.676 0.010 1 727 158 158 TYR CA C 59.204 0.019 1 728 158 158 TYR CB C 37.631 0.019 1 729 158 158 TYR N N 114.617 0.002 1 730 159 159 GLU H H 7.721 0.007 1 731 159 159 GLU C C 175.243 0.006 1 732 159 159 GLU CA C 57.194 0.006 1 733 159 159 GLU CB C 26.515 0.022 1 734 159 159 GLU N N 113.044 0.003 1 735 160 160 LEU H H 8.424 0.007 1 736 160 160 LEU C C 178.364 0.012 1 737 160 160 LEU CA C 53.755 0.015 1 738 160 160 LEU CB C 40.996 0.021 1 739 160 160 LEU N N 118.409 0.008 1 740 161 161 ARG H H 9.138 0.007 1 741 161 161 ARG C C 173.091 0.010 1 742 161 161 ARG CA C 55.607 0.007 1 743 161 161 ARG CB C 31.148 0.022 1 744 161 161 ARG N N 124.015 0.005 1 745 162 162 ALA H H 7.614 0.007 1 746 162 162 ALA C C 175.051 0.000 1 747 162 162 ALA CA C 51.516 0.000 1 748 162 162 ALA CB C 16.857 0.000 1 749 162 162 ALA N N 117.652 0.003 1 750 163 163 PRO C C 177.524 0.007 1 751 163 163 PRO CA C 64.276 0.016 1 752 163 163 PRO CB C 30.935 0.008 1 753 164 164 VAL H H 8.479 0.007 1 754 164 164 VAL C C 174.864 0.008 1 755 164 164 VAL CA C 62.651 0.013 1 756 164 164 VAL CB C 32.282 0.016 1 757 164 164 VAL N N 121.192 0.004 1 758 165 165 ALA H H 7.396 0.006 1 759 165 165 ALA C C 175.591 0.004 1 760 165 165 ALA CA C 50.020 0.011 1 761 165 165 ALA CB C 21.796 0.006 1 762 165 165 ALA N N 119.319 0.004 1 763 166 166 GLY H H 7.342 0.006 1 764 166 166 GLY CA C 46.951 0.005 1 765 166 166 GLY N N 103.888 0.008 1 766 167 167 THR H H 9.690 0.007 1 767 167 167 THR C C 171.478 0.004 1 768 167 167 THR CA C 60.550 0.025 1 769 167 167 THR CB C 68.015 0.008 1 770 167 167 THR N N 112.310 0.007 1 771 168 168 CYS H H 8.822 0.006 1 772 168 168 CYS C C 173.792 0.004 1 773 168 168 CYS CA C 56.218 0.010 1 774 168 168 CYS CB C 31.004 0.004 1 775 168 168 CYS N N 121.405 0.004 1 776 169 169 TYR H H 9.306 0.006 1 777 169 169 TYR C C 172.184 0.005 1 778 169 169 TYR CA C 55.907 0.038 1 779 169 169 TYR CB C 41.774 0.023 1 780 169 169 TYR N N 127.562 0.008 1 781 170 170 GLN H H 9.321 0.007 1 782 170 170 GLN C C 174.552 0.009 1 783 170 170 GLN CA C 53.607 0.017 1 784 170 170 GLN CB C 36.607 0.016 1 785 170 170 GLN N N 119.751 0.004 1 786 171 171 ALA H H 8.481 0.007 1 787 171 171 ALA C C 175.387 0.004 1 788 171 171 ALA CA C 52.624 0.029 1 789 171 171 ALA CB C 22.435 0.014 1 790 171 171 ALA N N 117.989 0.003 1 791 172 172 GLU H H 9.002 0.007 1 792 172 172 GLU C C 174.238 0.006 1 793 172 172 GLU CA C 53.391 0.011 1 794 172 172 GLU CB C 33.882 0.005 1 795 172 172 GLU N N 119.940 0.005 1 796 173 173 TRP H H 8.256 0.007 1 797 173 173 TRP C C 176.662 0.003 1 798 173 173 TRP CA C 61.795 0.014 1 799 173 173 TRP CB C 30.279 0.015 1 800 173 173 TRP N N 118.252 0.006 1 801 174 174 ASP H H 6.421 0.007 1 802 174 174 ASP C C 174.134 0.005 1 803 174 174 ASP CA C 52.906 0.008 1 804 174 174 ASP CB C 42.095 0.010 1 805 174 174 ASP N N 124.291 0.008 1 806 175 175 ASP H H 7.392 0.007 1 807 175 175 ASP C C 177.246 0.008 1 808 175 175 ASP CA C 55.743 0.028 1 809 175 175 ASP CB C 40.050 0.032 1 810 175 175 ASP N N 110.716 0.006 1 811 176 176 TYR H H 8.287 0.007 1 812 176 176 TYR C C 176.782 0.008 1 813 176 176 TYR CA C 59.505 0.009 1 814 176 176 TYR CB C 39.157 0.019 1 815 176 176 TYR N N 121.767 0.006 1 816 177 177 VAL H H 7.361 0.006 1 817 177 177 VAL C C 174.095 0.000 1 818 177 177 VAL CA C 68.778 0.000 1 819 177 177 VAL CB C 28.234 0.000 1 820 177 177 VAL N N 118.947 0.005 1 821 178 178 PRO C C 179.696 0.000 1 822 178 178 PRO CA C 66.309 0.012 1 823 178 178 PRO CB C 31.602 0.036 1 824 179 179 LYS H H 7.129 0.007 1 825 179 179 LYS C C 179.660 0.005 1 826 179 179 LYS CA C 57.886 0.010 1 827 179 179 LYS CB C 30.585 0.005 1 828 179 179 LYS N N 116.354 0.002 1 829 180 180 LEU H H 7.294 0.007 1 830 180 180 LEU C C 179.029 0.005 1 831 180 180 LEU CA C 57.380 0.039 1 832 180 180 LEU CB C 41.106 0.002 1 833 180 180 LEU N N 124.443 0.003 1 834 181 181 TYR H H 8.137 0.006 1 835 181 181 TYR CA C 60.849 0.010 1 836 181 181 TYR CB C 36.471 0.027 1 837 181 181 TYR N N 117.042 0.012 1 838 182 182 GLU H H 7.612 0.007 1 839 182 182 GLU C C 179.413 0.005 1 840 182 182 GLU CA C 59.691 0.009 1 841 182 182 GLU CB C 29.304 0.015 1 842 182 182 GLU N N 119.972 0.005 1 843 183 183 GLN H H 7.911 0.007 1 844 183 183 GLN C C 178.566 0.009 1 845 183 183 GLN CA C 59.009 0.018 1 846 183 183 GLN CB C 29.173 0.075 1 847 183 183 GLN N N 122.670 0.008 1 848 184 184 LEU H H 7.897 0.007 1 849 184 184 LEU C C 176.504 0.003 1 850 184 184 LEU CA C 55.597 0.004 1 851 184 184 LEU CB C 41.755 0.059 1 852 184 184 LEU N N 116.760 0.011 1 853 185 185 SER H H 7.579 0.008 1 854 185 185 SER C C 175.155 0.006 1 855 185 185 SER CA C 58.812 0.012 1 856 185 185 SER CB C 64.078 0.010 1 857 185 185 SER N N 113.510 0.025 1 858 186 186 GLY H H 8.013 0.006 1 859 186 186 GLY C C 173.704 0.007 1 860 186 186 GLY CA C 46.062 0.009 1 861 186 186 GLY N N 110.631 0.004 1 862 187 187 LYS H H 7.681 0.007 1 863 187 187 LYS CA C 57.377 0.000 1 864 187 187 LYS CB C 33.685 0.000 1 865 187 187 LYS N N 125.526 0.003 1 stop_ save_