data_19787 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human FKBP51-FK506 binding domain 1 ; _BMRB_accession_number 19787 _BMRB_flat_file_name bmr19787.str _Entry_type original _Submission_date 2014-02-11 _Accession_date 2014-02-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Human FKBP51-FK506 binding domain 1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mustafi Sourajit Mitra . 2 LeMaster David M. . 3 Hernandez Griselda . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 250 "13C chemical shifts" 351 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-06 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19788 FKBP52 stop_ _Original_release_date 2014-08-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24749623 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mustafi Sourajit Mitra . 2 LeMaster David M. . 3 Hernandez Griselda . . stop_ _Journal_abbreviation 'Biochem J.' _Journal_volume 461 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 115 _Page_last 123 _Year 2014 _Details . loop_ _Keyword 'conformational dynamics' 'FKBP51 and FKBP52' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FKBP51 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FKBP51 $FKBP51 stop_ _System_molecular_weight 13537.59 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Hsp 90 binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FKBP51 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FKBP51 _Molecular_mass 13537.59 _Mol_thiol_state 'all free' loop_ _Biological_function 'Hsp90 binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MEQGEDITSKKDRGVLKIVK RVGNGEETPMIGDKVYVHYK GKLSNGKKFDSSHDRNEPFV FSLGKGQVIKAWDIGVATMK KGEICHLLCKPEYAYGSAGS LPKIPSNATLFFEIELLDFK GE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 19 MET 2 20 GLU 3 21 GLN 4 22 GLY 5 23 GLU 6 24 ASP 7 25 ILE 8 26 THR 9 27 SER 10 28 LYS 11 29 LYS 12 30 ASP 13 31 ARG 14 32 GLY 15 33 VAL 16 34 LEU 17 35 LYS 18 36 ILE 19 37 VAL 20 38 LYS 21 39 ARG 22 40 VAL 23 41 GLY 24 42 ASN 25 43 GLY 26 44 GLU 27 45 GLU 28 46 THR 29 47 PRO 30 48 MET 31 49 ILE 32 50 GLY 33 51 ASP 34 52 LYS 35 53 VAL 36 54 TYR 37 55 VAL 38 56 HIS 39 57 TYR 40 58 LYS 41 59 GLY 42 60 LYS 43 61 LEU 44 62 SER 45 63 ASN 46 64 GLY 47 65 LYS 48 66 LYS 49 67 PHE 50 68 ASP 51 69 SER 52 70 SER 53 71 HIS 54 72 ASP 55 73 ARG 56 74 ASN 57 75 GLU 58 76 PRO 59 77 PHE 60 78 VAL 61 79 PHE 62 80 SER 63 81 LEU 64 82 GLY 65 83 LYS 66 84 GLY 67 85 GLN 68 86 VAL 69 87 ILE 70 88 LYS 71 89 ALA 72 90 TRP 73 91 ASP 74 92 ILE 75 93 GLY 76 94 VAL 77 95 ALA 78 96 THR 79 97 MET 80 98 LYS 81 99 LYS 82 100 GLY 83 101 GLU 84 102 ILE 85 103 CYS 86 104 HIS 87 105 LEU 88 106 LEU 89 107 CYS 90 108 LYS 91 109 PRO 92 110 GLU 93 111 TYR 94 112 ALA 95 113 TYR 96 114 GLY 97 115 SER 98 116 ALA 99 117 GLY 100 118 SER 101 119 LEU 102 120 PRO 103 121 LYS 104 122 ILE 105 123 PRO 106 124 SER 107 125 ASN 108 126 ALA 109 127 THR 110 128 LEU 111 129 PHE 112 130 PHE 113 131 GLU 114 132 ILE 115 133 GLU 116 134 LEU 117 135 LEU 118 136 ASP 119 137 PHE 120 138 LYS 121 139 GLY 122 140 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 PDB 3O5E "Fk1 Domain Of Fkbp51, Crystal Form Vi" 99.18 144 100.00 100.00 1.46e-82 PDB 3O5F "Fk1 Domain Of Fkbp51, Crystal Form Vii" 99.18 144 100.00 100.00 1.46e-82 PDB 3O5G "Fk1 Domain Of Fkbp51, Crystal Form I" 99.18 128 100.00 100.00 6.20e-82 PDB 3O5I "Fk1 Domain Of Fkbp51, Crystal Form Ii" 99.18 128 100.00 100.00 6.20e-82 PDB 3O5J "Fk1 Domain Of Fkbp51, Crystal Form Iii" 99.18 128 100.00 100.00 6.20e-82 PDB 3O5K "Fk1 Domain Of Fkbp51, Crystal Form Viii" 99.18 128 100.00 100.00 6.20e-82 PDB 3O5L "Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form I" 99.18 128 100.00 100.00 6.61e-82 PDB 3O5M "Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Ii" 99.18 128 100.00 100.00 6.61e-82 PDB 3O5O "Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iii" 99.18 128 100.00 100.00 6.61e-82 PDB 3O5P "Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iv" 99.18 128 100.00 100.00 6.61e-82 PDB 3O5Q "Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iv, In Presence Of Dmso" 99.18 128 100.00 100.00 6.61e-82 PDB 3O5R "Complex Of Fk506 With The Fk1 Domain Mutant A19t Of Fkbp51" 99.18 128 100.00 100.00 6.61e-82 PDB 4DRH "Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor At Low Ph" 99.18 144 100.00 100.00 2.64e-82 PDB 4DRI "Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor" 99.18 144 100.00 100.00 2.64e-82 PDB 4DRK "Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With {3-[(1r)-3-(3,4-Dimethoxyphenyl)" 99.18 128 100.00 100.00 6.61e-82 PDB 4DRM "Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With {3-[(1r)-3-(3,4-Dimethoxyphenyl)" 99.18 128 100.00 100.00 6.61e-82 PDB 4DRN "Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With {3-[(1r)-3-(3,4-Dimethoxyphenyl)" 99.18 128 100.00 100.00 6.61e-82 PDB 4DRO "Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With (1r)-3-(3,4-Dimethoxyphenyl)-1- " 99.18 128 100.00 100.00 6.61e-82 PDB 4DRP "Evaluation Of Synthetic Fk506 Analogs As Ligands For The Fk506-Binding Proteins 51 And 52: Complex Of Fkbp51 With 2-(3-((R)-3-(" 99.18 128 100.00 100.00 6.61e-82 PDB 4DRQ "Exploration Of Pipecolate Sulfonamides As Binders Of The Fk506-Binding Proteins 51 And 52: Complex Of Fkbp51 With 2-(3-((R)-1-(" 99.18 128 100.00 100.00 6.61e-82 PDB 4JFI "Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W" 98.36 127 100.00 100.00 2.89e-81 PDB 4JFJ "Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W" 99.18 128 100.00 100.00 6.61e-82 PDB 4JFK "Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W" 99.18 128 100.00 100.00 6.61e-82 PDB 4JFL "Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W" 99.18 128 100.00 100.00 6.61e-82 PDB 4JFM "Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W" 99.18 128 100.00 100.00 6.61e-82 PDB 4R0X "Allosteric Coupling Of Conformational Transitions In The Fk1 Domain Of Fkbp51 Near The Site Of Steroid Receptor Interaction" 100.00 122 99.18 99.18 8.90e-82 PDB 4TW6 "The Fk1 Domain Of Fkbp51 In Complex With Ifit1" 99.18 128 100.00 100.00 6.61e-82 PDB 4TW7 "The Fk1 Domain Of Fkbp51 In Complex With Ifit4" 99.18 128 100.00 100.00 6.61e-82 PDB 4TX0 "The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3" 99.18 128 100.00 100.00 6.61e-82 PDB 4W9O "The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-[(1r)-1,2-dihydroxyethyl]-3-[2-(3,4- D" 99.18 128 100.00 100.00 6.61e-82 PDB 4W9P "The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-[(1s)-1,2-dihydroxyethyl]-3-[2-(3,4- D" 99.18 128 100.00 100.00 6.61e-82 PDB 4W9Q "The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-5-ethy" 99.18 128 100.00 100.00 6.61e-82 PDB 5DIT "The Fk1 Domain Of Fkbp51 In Complex With The New Synthetic Ligand (1r)-3-(3,4-dimethoxyphenyl)-1-f3-[2-(morpholin-4-yl) Ethoxy]" 99.18 128 100.00 100.00 6.61e-82 DBJ BAD93130 "FK506 binding protein 5 variant [Homo sapiens]" 95.08 267 97.41 98.28 1.14e-73 GB AAI18470 "FKBP5 protein [Bos taurus]" 99.18 158 98.35 98.35 1.40e-80 REF NP_001139249 "peptidyl-prolyl cis-trans isomerase FKBP5 isoform 2 [Homo sapiens]" 99.18 268 100.00 100.00 1.26e-79 REF XP_003897552 "PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5-like [Papio anubis]" 99.18 172 99.17 99.17 3.07e-81 REF XP_012387759 "PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X2 [Orcinus orca]" 99.18 257 99.17 99.17 4.17e-79 REF XP_013833287 "PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X6 [Sus scrofa]" 99.18 272 99.17 99.17 7.58e-79 REF XP_013833288 "PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X7 [Sus scrofa]" 99.18 271 99.17 99.17 6.59e-79 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FKBP51 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 $FKBP51 'recombinant technology' . Escherichia coli BL21 pET11a 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 $FKBP51 1.0 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FKBP51 1.0 mM '[U-98% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 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' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ save_sample_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . 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_ _Software_label $Felix stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HCCH-TOCSY' '3D HNCO' '3D HCACO' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FKBP51 _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 19 1 MET HA H 3.880 . 1 2 19 1 MET CA C 55.304 . 1 3 19 1 MET CB C 33.680 . 1 4 20 2 GLU HA H 4.233 . 1 5 20 2 GLU C C 175.673 . 1 6 20 2 GLU CA C 56.676 . 1 7 20 2 GLU CB C 30.205 . 1 8 21 3 GLN H H 8.408 . 1 9 21 3 GLN HA H 4.328 . 1 10 21 3 GLN C C 174.987 . 1 11 21 3 GLN CA C 55.744 . 1 12 21 3 GLN CB C 30.175 . 1 13 21 3 GLN N N 120.647 . 1 14 22 4 GLY H H 8.186 . 1 15 22 4 GLY HA2 H 3.784 . 1 16 22 4 GLY HA3 H 3.784 . 1 17 22 4 GLY C C 172.326 . 1 18 22 4 GLY CA C 44.618 . 1 19 22 4 GLY N N 107.248 . 1 20 23 5 GLU H H 8.639 . 1 21 23 5 GLU HA H 4.348 . 1 22 23 5 GLU C C 176.055 . 1 23 23 5 GLU CA C 54.917 . 1 24 23 5 GLU CB C 31.377 . 1 25 23 5 GLU N N 121.388 . 1 26 24 6 ASP H H 8.811 . 1 27 24 6 ASP HA H 4.875 . 1 28 24 6 ASP C C 177.460 . 1 29 24 6 ASP CA C 53.588 . 1 30 24 6 ASP CB C 39.671 . 1 31 24 6 ASP N N 125.041 . 1 32 25 7 ILE H H 7.666 . 1 33 25 7 ILE HA H 4.523 . 1 34 25 7 ILE C C 176.043 . 1 35 25 7 ILE CA C 60.886 . 1 36 25 7 ILE CB C 37.464 . 1 37 25 7 ILE N N 120.078 . 1 38 26 8 THR H H 8.471 . 1 39 26 8 THR HA H 4.064 . 1 40 26 8 THR C C 175.678 . 1 41 26 8 THR CA C 62.476 . 1 42 26 8 THR CB C 70.453 . 1 43 26 8 THR N N 114.201 . 1 44 27 9 SER H H 8.743 . 1 45 27 9 SER HA H 4.238 . 1 46 27 9 SER C C 177.502 . 1 47 27 9 SER CA C 60.532 . 1 48 27 9 SER CB C 62.658 . 1 49 27 9 SER N N 118.292 . 1 50 28 10 LYS H H 8.037 . 1 51 28 10 LYS HA H 4.008 . 1 52 28 10 LYS C C 175.676 . 1 53 28 10 LYS CA C 56.782 . 1 54 28 10 LYS CB C 32.619 . 1 55 28 10 LYS N N 119.185 . 1 56 29 11 LYS H H 7.693 . 1 57 29 11 LYS HA H 4.039 . 1 58 29 11 LYS C C 176.295 . 1 59 29 11 LYS CA C 55.037 . 1 60 29 11 LYS CB C 28.296 . 1 61 29 11 LYS N N 116.844 . 1 62 30 12 ASP H H 7.663 . 1 63 30 12 ASP HA H 4.508 . 1 64 30 12 ASP C C 177.246 . 1 65 30 12 ASP CA C 51.997 . 1 66 30 12 ASP CB C 41.188 . 1 67 30 12 ASP N N 117.397 . 1 68 31 13 ARG H H 9.439 . 1 69 31 13 ARG HA H 3.116 . 1 70 31 13 ARG C C 176.659 . 1 71 31 13 ARG CA C 57.416 . 1 72 31 13 ARG CB C 28.055 . 1 73 31 13 ARG N N 115.267 . 1 74 32 14 GLY H H 8.784 . 1 75 32 14 GLY HA2 H 3.623 . 1 76 32 14 GLY HA3 H 3.623 . 1 77 32 14 GLY C C 172.297 . 1 78 32 14 GLY CA C 46.894 . 1 79 32 14 GLY N N 105.069 . 1 80 33 15 VAL H H 6.157 . 1 81 33 15 VAL HA H 4.537 . 1 82 33 15 VAL C C 173.557 . 1 83 33 15 VAL CA C 61.882 . 1 84 33 15 VAL CB C 34.635 . 1 85 33 15 VAL N N 115.645 . 1 86 34 16 LEU H H 8.422 . 1 87 34 16 LEU HA H 5.180 . 1 88 34 16 LEU C C 176.466 . 1 89 34 16 LEU CA C 51.990 . 1 90 34 16 LEU CB C 44.494 . 1 91 34 16 LEU N N 124.693 . 1 92 35 17 LYS H H 9.378 . 1 93 35 17 LYS HA H 5.484 . 1 94 35 17 LYS C C 176.014 . 1 95 35 17 LYS CA C 54.903 . 1 96 35 17 LYS CB C 38.067 . 1 97 35 17 LYS N N 123.784 . 1 98 36 18 ILE H H 9.005 . 1 99 36 18 ILE HA H 4.367 . 1 100 36 18 ILE C C 175.664 . 1 101 36 18 ILE CA C 60.302 . 1 102 36 18 ILE CB C 42.597 . 1 103 36 18 ILE N N 127.977 . 1 104 37 19 VAL H H 9.140 . 1 105 37 19 VAL HA H 3.683 . 1 106 37 19 VAL C C 174.974 . 1 107 37 19 VAL CA C 64.766 . 1 108 37 19 VAL CB C 31.622 . 1 109 37 19 VAL N N 128.878 . 1 110 38 20 LYS H H 8.669 . 1 111 38 20 LYS HA H 4.284 . 1 112 38 20 LYS C C 176.012 . 1 113 38 20 LYS CA C 54.886 . 1 114 38 20 LYS CB C 32.333 . 1 115 38 20 LYS N N 128.410 . 1 116 39 21 ARG H H 8.088 . 1 117 39 21 ARG HA H 4.475 . 1 118 39 21 ARG C C 174.292 . 1 119 39 21 ARG CA C 55.629 . 1 120 39 21 ARG CB C 34.172 . 1 121 39 21 ARG N N 121.679 . 1 122 40 22 VAL H H 8.439 . 1 123 40 22 VAL HA H 3.930 . 1 124 40 22 VAL C C 177.078 . 1 125 40 22 VAL CA C 62.875 . 1 126 40 22 VAL CB C 32.131 . 1 127 40 22 VAL N N 126.367 . 1 128 41 23 GLY H H 9.646 . 1 129 41 23 GLY HA2 H 4.062 . 1 130 41 23 GLY HA3 H 3.299 . 1 131 41 23 GLY C C 172.713 . 1 132 41 23 GLY CA C 43.950 . 1 133 41 23 GLY N N 112.734 . 1 134 42 24 ASN H H 8.744 . 1 135 42 24 ASN HA H 4.814 . 1 136 42 24 ASN C C 175.105 . 1 137 42 24 ASN CA C 53.041 . 1 138 42 24 ASN CB C 40.860 . 1 139 42 24 ASN N N 117.167 . 1 140 43 25 GLY H H 8.307 . 1 141 43 25 GLY HA2 H 4.177 . 1 142 43 25 GLY HA3 H 3.900 . 1 143 43 25 GLY C C 173.216 . 1 144 43 25 GLY CA C 44.924 . 1 145 43 25 GLY N N 108.888 . 1 146 44 26 GLU H H 8.314 . 1 147 44 26 GLU HA H 4.325 . 1 148 44 26 GLU C C 176.888 . 1 149 44 26 GLU CA C 56.400 . 1 150 44 26 GLU CB C 31.720 . 1 151 44 26 GLU N N 116.634 . 1 152 45 27 GLU H H 8.160 . 1 153 45 27 GLU HA H 4.411 . 1 154 45 27 GLU C C 175.257 . 1 155 45 27 GLU CA C 57.184 . 1 156 45 27 GLU CB C 31.029 . 1 157 45 27 GLU N N 118.971 . 1 158 46 28 THR H H 7.771 . 1 159 46 28 THR HA H 4.799 . 1 160 46 28 THR C C 171.938 . 1 161 46 28 THR CA C 58.220 . 1 162 46 28 THR CB C 69.109 . 1 163 46 28 THR N N 112.448 . 1 164 47 29 PRO HA H 3.480 . 1 165 47 29 PRO C C 175.056 . 1 166 47 29 PRO CA C 62.115 . 1 167 47 29 PRO CB C 31.444 . 1 168 48 30 MET H H 8.671 . 1 169 48 30 MET HA H 4.428 . 1 170 48 30 MET C C 176.112 . 1 171 48 30 MET CA C 52.825 . 1 172 48 30 MET CB C 34.809 . 1 173 48 30 MET N N 121.060 . 1 174 49 31 ILE H H 8.040 . 1 175 49 31 ILE HA H 3.323 . 1 176 49 31 ILE C C 177.299 . 1 177 49 31 ILE CA C 63.403 . 1 178 49 31 ILE CB C 36.794 . 1 179 49 31 ILE N N 120.249 . 1 180 50 32 GLY H H 9.218 . 1 181 50 32 GLY HA2 H 4.410 . 1 182 50 32 GLY HA3 H 3.227 . 1 183 50 32 GLY C C 174.265 . 1 184 50 32 GLY CA C 44.713 . 1 185 50 32 GLY N N 116.578 . 1 186 51 33 ASP H H 8.374 . 1 187 51 33 ASP HA H 4.489 . 1 188 51 33 ASP C C 175.694 . 1 189 51 33 ASP CA C 55.409 . 1 190 51 33 ASP CB C 40.313 . 1 191 51 33 ASP N N 123.101 . 1 192 52 34 LYS H H 8.556 . 1 193 52 34 LYS HA H 4.310 . 1 194 52 34 LYS C C 175.473 . 1 195 52 34 LYS CA C 55.530 . 1 196 52 34 LYS CB C 32.590 . 1 197 52 34 LYS N N 121.310 . 1 198 53 35 VAL H H 8.622 . 1 199 53 35 VAL HA H 4.627 . 1 200 53 35 VAL C C 172.259 . 1 201 53 35 VAL CA C 59.381 . 1 202 53 35 VAL CB C 32.940 . 1 203 53 35 VAL N N 119.803 . 1 204 54 36 TYR H H 7.993 . 1 205 54 36 TYR HA H 4.928 . 1 206 54 36 TYR C C 175.758 . 1 207 54 36 TYR CA C 55.635 . 1 208 54 36 TYR CB C 39.824 . 1 209 54 36 TYR N N 120.645 . 1 210 55 37 VAL H H 9.481 . 1 211 55 37 VAL HA H 5.706 . 1 212 55 37 VAL C C 175.624 . 1 213 55 37 VAL CA C 58.147 . 1 214 55 37 VAL CB C 35.235 . 1 215 55 37 VAL N N 114.829 . 1 216 56 38 HIS H H 8.629 . 1 217 56 38 HIS HA H 5.502 . 1 218 56 38 HIS C C 175.728 . 1 219 56 38 HIS CA C 54.626 . 1 220 56 38 HIS CB C 35.160 . 1 221 56 38 HIS N N 119.257 . 1 222 57 39 TYR H H 9.575 . 1 223 57 39 TYR HA H 6.083 . 1 224 57 39 TYR C C 173.579 . 1 225 57 39 TYR CA C 55.965 . 1 226 57 39 TYR CB C 44.005 . 1 227 57 39 TYR N N 116.956 . 1 228 58 40 LYS H H 8.868 . 1 229 58 40 LYS HA H 4.675 . 1 230 58 40 LYS C C 174.989 . 1 231 58 40 LYS CA C 56.144 . 1 232 58 40 LYS CB C 36.553 . 1 233 58 40 LYS N N 118.999 . 1 234 59 41 GLY H H 8.897 . 1 235 59 41 GLY HA2 H 3.614 . 1 236 59 41 GLY HA3 H 3.614 . 1 237 59 41 GLY C C 172.111 . 1 238 59 41 GLY CA C 45.311 . 1 239 59 41 GLY N N 111.802 . 1 240 60 42 LYS H H 9.349 . 1 241 60 42 LYS HA H 5.256 . 1 242 60 42 LYS C C 175.975 . 1 243 60 42 LYS CA C 54.838 . 1 244 60 42 LYS CB C 37.360 . 1 245 60 42 LYS N N 124.561 . 1 246 61 43 LEU H H 8.590 . 1 247 61 43 LEU HA H 4.658 . 1 248 61 43 LEU C C 179.883 . 1 249 61 43 LEU CA C 53.747 . 1 250 61 43 LEU CB C 42.235 . 1 251 61 43 LEU N N 119.829 . 1 252 62 44 SER H H 9.366 . 1 253 62 44 SER HA H 3.929 . 1 254 62 44 SER C C 174.696 . 1 255 62 44 SER CA C 61.433 . 1 256 62 44 SER CB C 62.387 . 1 257 62 44 SER N N 117.483 . 1 258 63 45 ASN H H 7.419 . 1 259 63 45 ASN HA H 4.512 . 1 260 63 45 ASN C C 176.269 . 1 261 63 45 ASN CA C 52.439 . 1 262 63 45 ASN CB C 37.218 . 1 263 63 45 ASN N N 117.258 . 1 264 64 46 GLY H H 8.120 . 1 265 64 46 GLY HA2 H 3.443 . 1 266 64 46 GLY HA3 H 4.177 . 1 267 64 46 GLY C C 173.868 . 1 268 64 46 GLY CA C 44.905 . 1 269 64 46 GLY N N 107.879 . 1 270 65 47 LYS H H 7.705 . 1 271 65 47 LYS HA H 4.137 . 1 272 65 47 LYS C C 176.243 . 1 273 65 47 LYS CA C 56.451 . 1 274 65 47 LYS CB C 32.847 . 1 275 65 47 LYS N N 121.044 . 1 276 66 48 LYS H H 8.684 . 1 277 66 48 LYS HA H 4.570 . 1 278 66 48 LYS C C 176.607 . 1 279 66 48 LYS CA C 56.602 . 1 280 66 48 LYS CB C 32.547 . 1 281 66 48 LYS N N 126.732 . 1 282 67 49 PHE H H 8.382 . 1 283 67 49 PHE HA H 5.086 . 1 284 67 49 PHE C C 174.112 . 1 285 67 49 PHE CA C 56.398 . 1 286 67 49 PHE CB C 41.072 . 1 287 67 49 PHE N N 121.786 . 1 288 68 50 ASP H H 6.841 . 1 289 68 50 ASP HA H 4.822 . 1 290 68 50 ASP C C 174.466 . 1 291 68 50 ASP CA C 54.524 . 1 292 68 50 ASP CB C 44.418 . 1 293 68 50 ASP N N 118.637 . 1 294 69 51 SER H H 8.222 . 1 295 69 51 SER HA H 4.613 . 1 296 69 51 SER C C 174.563 . 1 297 69 51 SER CA C 56.151 . 1 298 69 51 SER CB C 65.188 . 1 299 69 51 SER N N 117.004 . 1 300 70 52 SER H H 8.033 . 1 301 70 52 SER HA H 4.168 . 1 302 70 52 SER C C 177.213 . 1 303 70 52 SER CA C 60.808 . 1 304 70 52 SER CB C 60.810 . 1 305 70 52 SER N N 122.580 . 1 306 71 53 HIS H H 7.733 . 1 307 71 53 HIS HA H 4.047 . 1 308 71 53 HIS C C 177.442 . 1 309 71 53 HIS CA C 58.121 . 1 310 71 53 HIS CB C 29.084 . 1 311 71 53 HIS N N 121.704 . 1 312 72 54 ASP H H 7.452 . 1 313 72 54 ASP HA H 4.366 . 1 314 72 54 ASP C C 176.665 . 1 315 72 54 ASP CA C 56.217 . 1 316 72 54 ASP CB C 40.108 . 1 317 72 54 ASP N N 118.705 . 1 318 73 55 ARG H H 7.331 . 1 319 73 55 ARG HA H 4.393 . 1 320 73 55 ARG C C 175.564 . 1 321 73 55 ARG CA C 55.901 . 1 322 73 55 ARG CB C 30.938 . 1 323 73 55 ARG N N 116.452 . 1 324 74 56 ASN H H 7.897 . 1 325 74 56 ASN HA H 4.416 . 1 326 74 56 ASN C C 173.905 . 1 327 74 56 ASN CA C 54.173 . 1 328 74 56 ASN CB C 37.766 . 1 329 74 56 ASN N N 115.470 . 1 330 75 57 GLU H H 7.380 . 1 331 75 57 GLU HA H 4.889 . 1 332 75 57 GLU C C 172.427 . 1 333 75 57 GLU CA C 53.519 . 1 334 75 57 GLU CB C 32.081 . 1 335 75 57 GLU N N 115.249 . 1 336 76 58 PRO HA H 3.846 . 1 337 76 58 PRO C C 174.506 . 1 338 76 58 PRO CA C 62.658 . 1 339 76 58 PRO CB C 32.108 . 1 340 77 59 PHE H H 9.264 . 1 341 77 59 PHE HA H 4.761 . 1 342 77 59 PHE C C 173.430 . 1 343 77 59 PHE CA C 57.665 . 1 344 77 59 PHE CB C 41.539 . 1 345 77 59 PHE N N 124.850 . 1 346 78 60 VAL H H 7.311 . 1 347 78 60 VAL HA H 5.169 . 1 348 78 60 VAL C C 174.765 . 1 349 78 60 VAL CA C 59.179 . 1 350 78 60 VAL CB C 33.941 . 1 351 78 60 VAL N N 127.100 . 1 352 79 61 PHE H H 8.101 . 1 353 79 61 PHE HA H 4.731 . 1 354 79 61 PHE C C 172.150 . 1 355 79 61 PHE CA C 55.537 . 1 356 79 61 PHE CB C 40.581 . 1 357 79 61 PHE N N 120.754 . 1 358 80 62 SER H H 8.287 . 1 359 80 62 SER HA H 4.917 . 1 360 80 62 SER C C 174.291 . 1 361 80 62 SER CA C 56.804 . 1 362 80 62 SER CB C 62.942 . 1 363 80 62 SER N N 115.277 . 1 364 81 63 LEU H H 8.852 . 1 365 81 63 LEU HA H 3.981 . 1 366 81 63 LEU C C 177.637 . 1 367 81 63 LEU CA C 56.455 . 1 368 81 63 LEU CB C 42.216 . 1 369 81 63 LEU N N 129.621 . 1 370 82 64 GLY H H 9.125 . 1 371 82 64 GLY HA2 H 3.556 . 1 372 82 64 GLY HA3 H 3.556 . 1 373 82 64 GLY C C 174.211 . 1 374 82 64 GLY CA C 46.729 . 1 375 82 64 GLY N N 114.976 . 1 376 83 65 LYS H H 7.697 . 1 377 83 65 LYS HA H 4.525 . 1 378 83 65 LYS C C 176.653 . 1 379 83 65 LYS CA C 53.923 . 1 380 83 65 LYS CB C 32.757 . 1 381 83 65 LYS N N 117.063 . 1 382 84 66 GLY H H 8.803 . 1 383 84 66 GLY HA2 H 3.943 . 1 384 84 66 GLY HA3 H 3.943 . 1 385 84 66 GLY C C 175.667 . 1 386 84 66 GLY CA C 46.573 . 1 387 84 66 GLY N N 111.802 . 1 388 85 67 GLN H H 9.206 . 1 389 85 67 GLN HA H 4.088 . 1 390 85 67 GLN C C 174.704 . 1 391 85 67 GLN CA C 56.747 . 1 392 85 67 GLN CB C 34.176 . 1 393 85 67 GLN N N 118.561 . 1 394 86 68 VAL H H 6.749 . 1 395 86 68 VAL HA H 4.089 . 1 396 86 68 VAL C C 175.167 . 1 397 86 68 VAL CA C 57.289 . 1 398 86 68 VAL CB C 35.743 . 1 399 86 68 VAL N N 108.827 . 1 400 87 69 ILE H H 7.031 . 1 401 87 69 ILE HA H 3.729 . 1 402 87 69 ILE C C 177.165 . 1 403 87 69 ILE CA C 61.654 . 1 404 87 69 ILE CB C 38.255 . 1 405 87 69 ILE N N 111.872 . 1 406 88 70 LYS H H 8.821 . 1 407 88 70 LYS HA H 4.144 . 1 408 88 70 LYS C C 179.268 . 1 409 88 70 LYS CA C 59.507 . 1 410 88 70 LYS CB C 32.847 . 1 411 88 70 LYS N N 124.388 . 1 412 89 71 ALA H H 8.809 . 1 413 89 71 ALA HA H 3.954 . 1 414 89 71 ALA C C 179.465 . 1 415 89 71 ALA CA C 55.147 . 1 416 89 71 ALA CB C 20.738 . 1 417 89 71 ALA N N 114.144 . 1 418 90 72 TRP H H 7.530 . 1 419 90 72 TRP HA H 4.115 . 1 420 90 72 TRP C C 177.493 . 1 421 90 72 TRP CA C 59.488 . 1 422 90 72 TRP CB C 28.912 . 1 423 90 72 TRP N N 115.010 . 1 424 91 73 ASP H H 6.996 . 1 425 91 73 ASP HA H 4.814 . 1 426 91 73 ASP C C 179.046 . 1 427 91 73 ASP CA C 57.687 . 1 428 91 73 ASP CB C 40.343 . 1 429 91 73 ASP N N 121.698 . 1 430 92 74 ILE H H 8.073 . 1 431 92 74 ILE HA H 3.814 . 1 432 92 74 ILE C C 178.694 . 1 433 92 74 ILE CA C 63.872 . 1 434 92 74 ILE CB C 39.294 . 1 435 92 74 ILE N N 115.065 . 1 436 93 75 GLY H H 8.406 . 1 437 93 75 GLY HA2 H 3.601 . 1 438 93 75 GLY HA3 H 3.415 . 1 439 93 75 GLY C C 177.280 . 1 440 93 75 GLY CA C 46.955 . 1 441 93 75 GLY N N 105.690 . 1 442 94 76 VAL H H 9.324 . 1 443 94 76 VAL HA H 3.405 . 1 444 94 76 VAL C C 175.843 . 1 445 94 76 VAL CA C 66.390 . 1 446 94 76 VAL CB C 29.971 . 1 447 94 76 VAL N N 124.557 . 1 448 95 77 ALA H H 6.286 . 1 449 95 77 ALA HA H 3.809 . 1 450 95 77 ALA C C 176.935 . 1 451 95 77 ALA CA C 53.881 . 1 452 95 77 ALA CB C 18.783 . 1 453 95 77 ALA N N 116.201 . 1 454 96 78 THR H H 7.054 . 1 455 96 78 THR HA H 4.405 . 1 456 96 78 THR C C 174.850 . 1 457 96 78 THR CA C 61.489 . 1 458 96 78 THR CB C 71.145 . 1 459 96 78 THR N N 103.452 . 1 460 97 79 MET H H 7.287 . 1 461 97 79 MET HA H 4.317 . 1 462 97 79 MET C C 172.574 . 1 463 97 79 MET CA C 56.360 . 1 464 97 79 MET CB C 36.080 . 1 465 97 79 MET N N 123.516 . 1 466 98 80 LYS H H 7.124 . 1 467 98 80 LYS HA H 4.680 . 1 468 98 80 LYS C C 177.665 . 1 469 98 80 LYS CA C 53.715 . 1 470 98 80 LYS CB C 34.752 . 1 471 98 80 LYS N N 115.600 . 1 472 99 81 LYS H H 9.207 . 1 473 99 81 LYS HA H 3.596 . 1 474 99 81 LYS C C 176.794 . 1 475 99 81 LYS CA C 60.335 . 1 476 99 81 LYS CB C 32.569 . 1 477 99 81 LYS N N 121.694 . 1 478 100 82 GLY H H 9.018 . 1 479 100 82 GLY HA2 H 4.339 . 1 480 100 82 GLY HA3 H 3.875 . 1 481 100 82 GLY C C 174.206 . 1 482 100 82 GLY CA C 44.979 . 1 483 100 82 GLY N N 114.573 . 1 484 101 83 GLU H H 8.389 . 1 485 101 83 GLU HA H 4.310 . 1 486 101 83 GLU C C 175.666 . 1 487 101 83 GLU CA C 55.530 . 1 488 101 83 GLU CB C 33.613 . 1 489 101 83 GLU N N 124.654 . 1 490 102 84 ILE H H 8.505 . 1 491 102 84 ILE HA H 5.280 . 1 492 102 84 ILE C C 176.649 . 1 493 102 84 ILE CA C 60.173 . 1 494 102 84 ILE CB C 40.156 . 1 495 102 84 ILE N N 120.959 . 1 496 103 85 CYS H H 9.623 . 1 497 103 85 CYS HA H 5.516 . 1 498 103 85 CYS C C 171.027 . 1 499 103 85 CYS CA C 54.622 . 1 500 103 85 CYS CB C 32.501 . 1 501 103 85 CYS N N 123.541 . 1 502 104 86 HIS H H 9.341 . 1 503 104 86 HIS HA H 5.748 . 1 504 104 86 HIS C C 174.833 . 1 505 104 86 HIS CA C 52.808 . 1 506 104 86 HIS CB C 33.977 . 1 507 104 86 HIS N N 120.416 . 1 508 105 87 LEU H H 9.141 . 1 509 105 87 LEU HA H 5.427 . 1 510 105 87 LEU C C 174.711 . 1 511 105 87 LEU CA C 52.637 . 1 512 105 87 LEU CB C 46.440 . 1 513 105 87 LEU N N 121.607 . 1 514 106 88 LEU H H 9.040 . 1 515 106 88 LEU HA H 5.140 . 1 516 106 88 LEU C C 177.562 . 1 517 106 88 LEU CA C 54.278 . 1 518 106 88 LEU CB C 43.975 . 1 519 106 88 LEU N N 127.189 . 1 520 107 89 CYS H H 9.362 . 1 521 107 89 CYS HA H 5.318 . 1 522 107 89 CYS C C 173.269 . 1 523 107 89 CYS CA C 56.073 . 1 524 107 89 CYS CB C 30.745 . 1 525 107 89 CYS N N 123.836 . 1 526 108 90 LYS H H 9.129 . 1 527 108 90 LYS HA H 4.489 . 1 528 108 90 LYS C C 175.645 . 1 529 108 90 LYS CA C 55.409 . 1 530 108 90 LYS CB C 30.830 . 1 531 108 90 LYS N N 124.563 . 1 532 109 91 PRO HA H 4.350 . 1 533 109 91 PRO C C 179.772 . 1 534 109 91 PRO CA C 65.593 . 1 535 109 91 PRO CB C 30.790 . 1 536 110 92 GLU H H 9.534 . 1 537 110 92 GLU HA H 3.930 . 1 538 110 92 GLU C C 176.936 . 1 539 110 92 GLU CA C 59.525 . 1 540 110 92 GLU CB C 28.192 . 1 541 110 92 GLU N N 118.722 . 1 542 111 93 TYR H H 7.988 . 1 543 111 93 TYR HA H 4.260 . 1 544 111 93 TYR C C 172.585 . 1 545 111 93 TYR CA C 58.070 . 1 546 111 93 TYR CB C 39.316 . 1 547 111 93 TYR N N 116.936 . 1 548 112 94 ALA H H 7.823 . 1 549 112 94 ALA HA H 4.328 . 1 550 112 94 ALA C C 175.690 . 1 551 112 94 ALA CA C 51.443 . 1 552 112 94 ALA CB C 19.111 . 1 553 112 94 ALA N N 125.186 . 1 554 113 95 TYR H H 9.141 . 1 555 113 95 TYR HA H 4.415 . 1 556 113 95 TYR C C 176.401 . 1 557 113 95 TYR CA C 59.075 . 1 558 113 95 TYR CB C 37.706 . 1 559 113 95 TYR N N 121.607 . 1 560 114 96 GLY H H 8.344 . 1 561 114 96 GLY HA2 H 3.555 . 1 562 114 96 GLY HA3 H 4.004 . 1 563 114 96 GLY C C 175.161 . 1 564 114 96 GLY CA C 46.613 . 1 565 114 96 GLY N N 107.249 . 1 566 115 97 SER HA H 4.112 . 1 567 115 97 SER C C 176.319 . 1 568 115 97 SER CA C 59.930 . 1 569 115 97 SER CB C 62.667 . 1 570 116 98 ALA H H 8.611 . 1 571 116 98 ALA HA H 4.149 . 1 572 116 98 ALA C C 180.548 . 1 573 116 98 ALA CA C 54.198 . 1 574 116 98 ALA CB C 19.004 . 1 575 116 98 ALA N N 124.702 . 1 576 117 99 GLY H H 7.176 . 1 577 117 99 GLY HA2 H 3.569 . 1 578 117 99 GLY HA3 H 3.267 . 1 579 117 99 GLY C C 171.726 . 1 580 117 99 GLY CA C 44.188 . 1 581 117 99 GLY N N 101.728 . 1 582 118 100 SER H H 8.534 . 1 583 118 100 SER HA H 4.225 . 1 584 118 100 SER C C 173.985 . 1 585 118 100 SER CA C 56.193 . 1 586 118 100 SER CB C 61.316 . 1 587 118 100 SER N N 115.618 . 1 588 119 101 LEU H H 8.813 . 1 589 119 101 LEU HA H 3.699 . 1 590 119 101 LEU C C 176.635 . 1 591 119 101 LEU CA C 54.879 . 1 592 119 101 LEU CB C 40.237 . 1 593 119 101 LEU N N 129.012 . 1 594 120 102 PRO HA H 4.289 . 1 595 120 102 PRO C C 176.884 . 1 596 120 102 PRO CA C 63.401 . 1 597 120 102 PRO CB C 34.773 . 1 598 121 103 LYS H H 7.984 . 1 599 121 103 LYS HA H 4.091 . 1 600 121 103 LYS C C 175.841 . 1 601 121 103 LYS CA C 59.489 . 1 602 121 103 LYS CB C 33.715 . 1 603 121 103 LYS N N 122.094 . 1 604 122 104 ILE H H 7.474 . 1 605 122 104 ILE HA H 4.230 . 1 606 122 104 ILE C C 173.883 . 1 607 122 104 ILE CA C 56.980 . 1 608 122 104 ILE CB C 39.131 . 1 609 122 104 ILE N N 116.532 . 1 610 123 105 PRO HA H 4.333 . 1 611 123 105 PRO C C 175.542 . 1 612 123 105 PRO CA C 61.584 . 1 613 123 105 PRO CB C 32.833 . 1 614 124 106 SER H H 8.322 . 1 615 124 106 SER HA H 4.325 . 1 616 124 106 SER C C 174.343 . 1 617 124 106 SER CA C 59.133 . 1 618 124 106 SER CB C 63.852 . 1 619 124 106 SER N N 113.173 . 1 620 125 107 ASN H H 8.091 . 1 621 125 107 ASN HA H 3.871 . 1 622 125 107 ASN C C 173.424 . 1 623 125 107 ASN CA C 54.333 . 1 624 125 107 ASN CB C 37.042 . 1 625 125 107 ASN N N 120.348 . 1 626 126 108 ALA H H 7.877 . 1 627 126 108 ALA HA H 4.313 . 1 628 126 108 ALA C C 176.942 . 1 629 126 108 ALA CA C 52.392 . 1 630 126 108 ALA CB C 20.366 . 1 631 126 108 ALA N N 121.533 . 1 632 127 109 THR H H 8.508 . 1 633 127 109 THR HA H 4.705 . 1 634 127 109 THR C C 174.286 . 1 635 127 109 THR CA C 62.930 . 1 636 127 109 THR CB C 69.196 . 1 637 127 109 THR N N 122.146 . 1 638 128 110 LEU H H 8.725 . 1 639 128 110 LEU HA H 4.897 . 1 640 128 110 LEU C C 174.147 . 1 641 128 110 LEU CA C 52.917 . 1 642 128 110 LEU CB C 46.335 . 1 643 128 110 LEU N N 125.431 . 1 644 129 111 PHE H H 8.586 . 1 645 129 111 PHE HA H 5.445 . 1 646 129 111 PHE C C 174.564 . 1 647 129 111 PHE CA C 55.580 . 1 648 129 111 PHE CB C 41.934 . 1 649 129 111 PHE N N 122.205 . 1 650 130 112 PHE H H 8.860 . 1 651 130 112 PHE HA H 5.723 . 1 652 130 112 PHE C C 174.139 . 1 653 130 112 PHE CA C 56.048 . 1 654 130 112 PHE CB C 43.470 . 1 655 130 112 PHE N N 120.597 . 1 656 131 113 GLU H H 8.710 . 1 657 131 113 GLU HA H 5.256 . 1 658 131 113 GLU C C 175.603 . 1 659 131 113 GLU CA C 54.838 . 1 660 131 113 GLU CB C 32.070 . 1 661 131 113 GLU N N 121.834 . 1 662 132 114 ILE H H 9.057 . 1 663 132 114 ILE HA H 4.839 . 1 664 132 114 ILE C C 172.506 . 1 665 132 114 ILE CA C 60.059 . 1 666 132 114 ILE CB C 41.178 . 1 667 132 114 ILE N N 125.927 . 1 668 133 115 GLU H H 9.258 . 1 669 133 115 GLU HA H 5.324 . 1 670 133 115 GLU C C 175.543 . 1 671 133 115 GLU CA C 53.188 . 1 672 133 115 GLU CB C 33.430 . 1 673 133 115 GLU N N 128.600 . 1 674 134 116 LEU H H 8.363 . 1 675 134 116 LEU HA H 4.686 . 1 676 134 116 LEU C C 174.915 . 1 677 134 116 LEU CA C 54.477 . 1 678 134 116 LEU CB C 40.661 . 1 679 134 116 LEU N N 127.713 . 1 680 135 117 LEU H H 9.065 . 1 681 135 117 LEU HA H 4.208 . 1 682 135 117 LEU C C 177.565 . 1 683 135 117 LEU CA C 56.835 . 1 684 135 117 LEU CB C 42.327 . 1 685 135 117 LEU N N 129.531 . 1 686 136 118 ASP H H 7.830 . 1 687 136 118 ASP HA H 4.472 . 1 688 136 118 ASP C C 173.715 . 1 689 136 118 ASP CA C 52.872 . 1 690 136 118 ASP CB C 42.715 . 1 691 136 118 ASP N N 110.983 . 1 692 137 119 PHE H H 8.308 . 1 693 137 119 PHE HA H 5.688 . 1 694 137 119 PHE C C 172.957 . 1 695 137 119 PHE CA C 56.362 . 1 696 137 119 PHE CB C 41.987 . 1 697 137 119 PHE N N 114.573 . 1 698 138 120 LYS H H 9.131 . 1 699 138 120 LYS HA H 4.566 . 1 700 138 120 LYS C C 174.894 . 1 701 138 120 LYS CA C 55.018 . 1 702 138 120 LYS CB C 36.089 . 1 703 138 120 LYS N N 118.881 . 1 704 139 121 GLY H H 8.534 . 1 705 139 121 GLY HA2 H 4.440 . 1 706 139 121 GLY HA3 H 3.620 . 1 707 139 121 GLY C C 173.525 . 1 708 139 121 GLY CA C 45.309 . 1 709 139 121 GLY N N 110.940 . 1 710 140 122 GLU H H 8.006 . 1 711 140 122 GLU HA H 4.037 . 1 712 140 122 GLU C C 181.002 . 1 713 140 122 GLU CA C 57.964 . 1 714 140 122 GLU CB C 31.255 . 1 715 140 122 GLU N N 125.871 . 1 stop_ save_