data_16401 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Separation of Inhibitor and Substrate Binding Locations in the Globin Dehaloperoxidase ; _BMRB_accession_number 16401 _BMRB_flat_file_name bmr16401.str _Entry_type original _Submission_date 2009-07-09 _Accession_date 2009-07-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone 13C, 15N, and 1H assignments for metcyano DHP at 25 C.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Davis Michael F. . 2 Bobay Benjamin G. . 3 Franzen Stefan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 128 "13C chemical shifts" 388 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-02-17 original author . stop_ _Original_release_date 2010-02-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Determination of separate inhibitor and substrate binding sites in the dehaloperoxidase-hemoglobin from Amphitrite ornata.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20067301 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Davis Michael F. . 2 Bobay Benjamin G. . 3 Franzen Stefan . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 49 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1199 _Page_last 1206 _Year 2010 _Details . loop_ _Keyword bioremediation dehalogenation globin halophenols peroxidase stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DHPCN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DHPCN $DHPCN Heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DHPCN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DHPCN _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 145 _Mol_residue_sequence ; MGHHHHHHGFKQDIATIRGD LRTYAQDIFLAFLNKYPDER RYFKNYVGKSDQELKSMAKF GDHTEKVFNLMMEVADRATD CVPLASDANTLVQMKQHSSL TTGNFEKLFVALVEYMRASG QSFDSQSWDRFGKNLVSALS SAGMK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 GLY 10 PHE 11 LYS 12 GLN 13 ASP 14 ILE 15 ALA 16 THR 17 ILE 18 ARG 19 GLY 20 ASP 21 LEU 22 ARG 23 THR 24 TYR 25 ALA 26 GLN 27 ASP 28 ILE 29 PHE 30 LEU 31 ALA 32 PHE 33 LEU 34 ASN 35 LYS 36 TYR 37 PRO 38 ASP 39 GLU 40 ARG 41 ARG 42 TYR 43 PHE 44 LYS 45 ASN 46 TYR 47 VAL 48 GLY 49 LYS 50 SER 51 ASP 52 GLN 53 GLU 54 LEU 55 LYS 56 SER 57 MET 58 ALA 59 LYS 60 PHE 61 GLY 62 ASP 63 HIS 64 THR 65 GLU 66 LYS 67 VAL 68 PHE 69 ASN 70 LEU 71 MET 72 MET 73 GLU 74 VAL 75 ALA 76 ASP 77 ARG 78 ALA 79 THR 80 ASP 81 CYS 82 VAL 83 PRO 84 LEU 85 ALA 86 SER 87 ASP 88 ALA 89 ASN 90 THR 91 LEU 92 VAL 93 GLN 94 MET 95 LYS 96 GLN 97 HIS 98 SER 99 SER 100 LEU 101 THR 102 THR 103 GLY 104 ASN 105 PHE 106 GLU 107 LYS 108 LEU 109 PHE 110 VAL 111 ALA 112 LEU 113 VAL 114 GLU 115 TYR 116 MET 117 ARG 118 ALA 119 SER 120 GLY 121 GLN 122 SER 123 PHE 124 ASP 125 SER 126 GLN 127 SER 128 TRP 129 ASP 130 ARG 131 PHE 132 GLY 133 LYS 134 ASN 135 LEU 136 VAL 137 SER 138 ALA 139 LEU 140 SER 141 SER 142 ALA 143 GLY 144 MET 145 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1EW6 "The Crystal Structure And Amino Acid Sequence Of Dehaloperoxidase From Amphitrite Ornata Indicate Common Ancestry With Globins" 94.48 137 100.00 100.00 2.31e-96 PDB 1EWA "Dehaloperoxidase And 4-Iodophenol" 94.48 137 100.00 100.00 2.31e-96 PDB 2QFK "X-Ray Crystal Structure Analysis Of The Binding Site In The Ferric And Oxyferrous Forms Of The Recombinant Heme Dehaloperoxidas" 94.48 137 100.00 100.00 2.31e-96 PDB 2QFN "X-Ray Crystal Structure Analysis Of The Binding Site In The Ferric And Oxyferrous Forms Of The Recombinant Heme Dehaloperoxidas" 94.48 138 99.27 99.27 5.86e-95 PDB 3DR9 "Increased Distal Histidine Conformational Flexibility In The Deoxy Form Of Dehaloperoxidase From Amphitrite Ornata" 94.48 137 100.00 100.00 2.31e-96 PDB 3K3U "The V59w Mutation Blocks The Distal Pocket Of The Hemoglobin Dehaloperoxidase From Amphitrite Ornata" 94.48 137 99.27 99.27 5.20e-95 PDB 3KUN "X-Ray Structure Of The Metcyano Form Of Dehaloperoxidase From Amphitrite Ornata: Evidence For Photoreductive Lysis Of Iron-Cyan" 94.48 137 100.00 100.00 2.31e-96 PDB 3KUO "X-Ray Structure Of The Metcyano Form Of Dehaloperoxidase From Amphitrite Ornata: Evidence For Photoreductive Lysis Of Iron-Cyan" 94.48 137 99.27 99.27 5.49e-95 PDB 3LB1 "Two-Site Competitive Inhibition In Dehaloperoxidase-Hemoglobin" 94.48 137 100.00 100.00 2.31e-96 PDB 3LB2 "Two-Site Competitive Inhibition In Dehaloperoxidase-Hemoglobin" 94.48 137 100.00 100.00 2.31e-96 PDB 3LB3 "Two-Site Competitive Inhibition In Dehaloperoxidase-Hemoglobin" 94.48 137 100.00 100.00 2.31e-96 PDB 3LB4 "Two-Site Competitive Inhibition In Dehaloperoxidase-Hemoglobin" 94.48 137 100.00 100.00 2.31e-96 PDB 3MOU "Characterization Of The Inhibitor Binding Site Of The Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure X" 94.48 137 100.00 100.00 2.31e-96 PDB 3MYM "Mutation Of Methionine-86 In Dehaloperoxidase-Hemoglobin: Effects Of The Asp-His-Fe Triad In A 33 GLOBIN" 94.48 137 99.27 99.27 3.79e-95 PDB 3MYN "Mutation Of Methionine-86 In Dehaloperoxidase-Hemoglobin: Effects Of The Asp-His-Fe Triad In A 33 GLOBIN" 94.48 137 99.27 99.27 8.49e-95 PDB 3O7N "The V59w Mutation Blocks The Distal Pocket Of The Hemoglobin - Dehaloperoxidase From Amphitrite Ornata" 94.48 137 99.27 99.27 5.20e-95 PDB 3OJ1 "Structure Of The H55d Mutant Of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata" 94.48 137 99.27 99.27 2.82e-95 PDB 3OK5 "Structure Of The H55d Mutant Of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata With 4-Bromophenol Inhibitor" 94.48 137 99.27 99.27 2.82e-95 PDB 3ORD "Structural Evidence For Stabilization Of Inhibitor Binding By A Protein Cavity In The Dehaloperoxidase-hemoglobin From Amphitri" 94.48 137 100.00 100.00 2.31e-96 PDB 4DWT "Carbonmonoxy Dehaloperoxidase-hemoglobin A Structure At 2.05 Angstrom Resolution" 94.48 137 100.00 100.00 2.31e-96 PDB 4DWU "Carbonmonoxy Dehaloperoxidase-hemoglobin A Structure At 1.44 Angstrom Resolution" 94.48 137 100.00 100.00 2.31e-96 PDB 4FH6 "Structure Of Dhp A In Complex With 2,4,6-tribromophenol In 10% Dmso" 94.48 137 100.00 100.00 2.31e-96 PDB 4FH7 "Structure Of Dhp A In Complex With 2,4,6-tribromophenol In 20% Methanol" 94.48 137 100.00 100.00 2.31e-96 PDB 4GZG "Crystal Structures Of Dhpa-co Complex" 94.48 137 100.00 100.00 2.31e-96 PDB 4HSW "Structure Of The L100f Mutant Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata" 94.48 137 99.27 99.27 1.55e-95 PDB 4HSX "Structure Of The L100f Mutant Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata With 4-bromophenol" 94.48 137 99.27 99.27 1.55e-95 PDB 4ILZ "Structural And Kinetic Study Of An Internal Substrate Binding Site Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata" 94.48 137 100.00 100.00 2.31e-96 PDB 4JAC "Dehaloperoxidase-hemoglobin T56s" 94.48 138 99.27 100.00 7.28e-96 PDB 4JYQ "Dhp-co Crystal Structure" 94.48 137 100.00 100.00 2.31e-96 PDB 4KJT "Structure Of The L100f Mutant Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata With Oxygen" 94.48 137 99.27 99.27 1.55e-95 PDB 4KMV "Structure Of The L100f Mutant Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata With 2,4,6-trichlorophenol" 94.48 137 99.27 99.27 1.55e-95 PDB 4KMW "Structure Of The Y34n Mutant Of Dehaloperoxidase-hemoglobin A From Amphitrite Ornata With 2,4,6-trichlorophenol" 94.48 137 99.27 99.27 4.27e-95 PDB 4KN3 "Structure Of The Y34ns91g Double Mutant Of Dehaloperoxidase From Amphitrite Ornata With 2,4,6-trichlorophenol" 94.48 137 98.54 98.54 3.15e-94 GB AAF97245 "dehaloperoxidase A [Amphitrite ornata]" 94.48 138 100.00 100.00 2.24e-96 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic yes _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 14:29:58 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? SING CHD C4C ? ? DOUB CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? DOUB NB C1B ? ? SING NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? DOUB C3C C4C ? ? SING C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING ND C1D ? ? DOUB ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DHPCN 'Segmented worm' 129555 Eukaryota Metazoa Amphitrite ornata 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 $DHPCN 'recombinant technology' 'Segmented worm' Amphitrite ornata . pET-16b 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 $DHPCN 1.6 mM '[U-99% 13C; U-99% 15N]' 'potassium phosphate' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.1 . M pH 7.0 . pH pressure 1 . atm temperature 298 . 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 TMS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 TMS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 TMS N 15 'methyl protons' ppm 0.0 . 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 HNCO' '3D HN(CO)CA' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DHPCN _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 1 9 GLY H H 9.489 0.02 1 2 1 9 GLY C C 173.903 0.05 1 3 1 9 GLY CA C 46.725 0.05 1 4 1 9 GLY N N 112.414 0.05 1 5 2 10 PHE H H 8.585 0.02 1 6 2 10 PHE C C 176.745 0.05 1 7 2 10 PHE CA C 61.81 0.05 1 8 2 10 PHE CB C 40.895 0.05 1 9 2 10 PHE N N 123.341 0.05 1 10 3 11 LYS H H 8.52 0.02 1 11 3 11 LYS C C 180.619 0.05 1 12 3 11 LYS CA C 58.988 0.05 1 13 3 11 LYS CB C 32.316 0.05 1 14 3 11 LYS N N 114.221 0.05 1 15 4 12 GLN H H 8.279 0.02 1 16 4 12 GLN C C 178.401 0.05 1 17 4 12 GLN CA C 58.966 0.05 1 18 4 12 GLN CB C 28.097 0.05 1 19 4 12 GLN N N 121.42 0.05 1 20 5 13 ASP H H 8.799 0.02 1 21 5 13 ASP C C 178.281 0.05 1 22 5 13 ASP CA C 57.743 0.05 1 23 5 13 ASP CB C 41.415 0.05 1 24 5 13 ASP N N 122.484 0.05 1 25 6 14 ILE H H 7.9 0.02 1 26 6 14 ILE C C 178.3 0.05 1 27 6 14 ILE CA C 65.786 0.05 1 28 6 14 ILE CB C 39.349 0.05 1 29 6 14 ILE N N 120.087 0.05 1 30 7 15 ALA H H 7.365 0.02 1 31 7 15 ALA C C 181.713 0.05 1 32 7 15 ALA CA C 55.591 0.05 1 33 7 15 ALA CB C 18.037 0.05 1 34 7 15 ALA N N 121.115 0.05 1 35 8 16 THR H H 9.228 0.02 1 36 8 16 THR C C 177.397 0.05 1 37 8 16 THR CA C 66.652 0.05 1 38 8 16 THR CB C 68.739 0.05 1 39 8 16 THR N N 120.229 0.05 1 40 9 17 ILE H H 8.787 0.02 1 41 9 17 ILE C C 179.252 0.05 1 42 9 17 ILE CA C 65.083 0.05 1 43 9 17 ILE CB C 37.073 0.05 1 44 9 17 ILE N N 123.28 0.05 1 45 10 18 ARG H H 8.798 0.02 1 46 10 18 ARG C C 178.847 0.05 1 47 10 18 ARG CA C 60.715 0.05 1 48 10 18 ARG CB C 31.05 0.05 1 49 10 18 ARG N N 116.457 0.05 1 50 11 19 GLY H H 8.238 0.02 1 51 11 19 GLY C C 174.166 0.05 1 52 11 19 GLY CA C 46.546 0.05 1 53 11 19 GLY N N 106.031 0.05 1 54 12 20 ASP H H 7.869 0.02 1 55 12 20 ASP C C 178.892 0.05 1 56 12 20 ASP CA C 53.584 0.05 1 57 12 20 ASP CB C 40.289 0.05 1 58 12 20 ASP N N 121.792 0.05 1 59 13 21 LEU H H 7.566 0.02 1 60 13 21 LEU C C 178.715 0.05 1 61 13 21 LEU CA C 60.321 0.05 1 62 13 21 LEU CB C 43.334 0.05 1 63 13 21 LEU N N 124.41 0.05 1 64 14 22 ARG H H 8.851 0.02 1 65 14 22 ARG C C 178.901 0.05 1 66 14 22 ARG CA C 60.761 0.05 1 67 14 22 ARG CB C 30.735 0.05 1 68 14 22 ARG N N 116.592 0.05 1 69 15 23 THR H H 7.612 0.02 1 70 15 23 THR C C 178.55 0.05 1 71 15 23 THR CA C 66.477 0.05 1 72 15 23 THR CB C 68.196 0.05 1 73 15 23 THR N N 115.715 0.05 1 74 16 24 TYR H H 7.984 0.02 1 75 16 24 TYR C C 179.493 0.05 1 76 16 24 TYR CA C 63.376 0.05 1 77 16 24 TYR CB C 39 0.05 1 78 16 24 TYR N N 118.445 0.05 1 79 17 25 ALA H H 9.084 0.02 1 80 17 25 ALA C C 179.616 0.05 1 81 17 25 ALA CA C 54.862 0.05 1 82 17 25 ALA CB C 19.852 0.05 1 83 17 25 ALA N N 119.957 0.05 1 84 18 26 GLN H H 7.869 0.02 1 85 18 26 GLN C C 178.341 0.05 1 86 18 26 GLN CA C 60.309 0.05 1 87 18 26 GLN CB C 31.057 0.05 1 88 18 26 GLN N N 113.993 0.05 1 89 19 27 ASP H H 8.339 0.02 1 90 19 27 ASP C C 180.75 0.05 1 91 19 27 ASP CA C 58.15 0.05 1 92 19 27 ASP CB C 36.844 0.05 1 93 19 27 ASP N N 118.641 0.05 1 94 20 28 ILE H H 9.059 0.02 1 95 20 28 ILE C C 177.794 0.05 1 96 20 28 ILE CA C 66.048 0.05 1 97 20 28 ILE CB C 36.844 0.05 1 98 20 28 ILE N N 120.847 0.05 1 99 21 29 PHE H H 9.01 0.02 1 100 21 29 PHE C C 180.178 0.05 1 101 21 29 PHE CA C 64.54 0.05 1 102 21 29 PHE CB C 41.828 0.05 1 103 21 29 PHE N N 122.414 0.05 1 104 22 30 LEU H H 9.56 0.02 1 105 22 30 LEU C C 179.814 0.05 1 106 22 30 LEU CA C 59.202 0.05 1 107 22 30 LEU CB C 41.946 0.05 1 108 22 30 LEU N N 117.372 0.05 1 109 23 31 ALA H H 8.504 0.02 1 110 23 31 ALA C C 181.579 0.05 1 111 23 31 ALA CA C 56.219 0.05 1 112 23 31 ALA CB C 17.748 0.05 1 113 23 31 ALA N N 123.597 0.05 1 114 24 32 PHE H H 8.95 0.02 1 115 24 32 PHE C C 176.028 0.05 1 116 24 32 PHE CA C 60.812 0.05 1 117 24 32 PHE CB C 39.415 0.05 1 118 24 32 PHE N N 120.153 0.05 1 119 25 33 LEU H H 9.239 0.02 1 120 25 33 LEU C C 179.688 0.05 1 121 25 33 LEU CA C 57.579 0.05 1 122 25 33 LEU CB C 42.023 0.05 1 123 25 33 LEU N N 117.133 0.05 1 124 26 34 ASN H H 8.969 0.02 1 125 26 34 ASN C C 177.164 0.05 1 126 26 34 ASN CA C 55.978 0.05 1 127 26 34 ASN CB C 40.332 0.05 1 128 26 34 ASN N N 115.685 0.05 1 129 27 35 LYS H H 8.606 0.02 1 130 27 35 LYS C C 179.391 0.05 1 131 27 35 LYS CA C 59.301 0.05 1 132 27 35 LYS CB C 34.059 0.05 1 133 27 35 LYS N N 122.411 0.05 1 134 28 36 TYR H H 8.333 0.02 1 135 28 36 TYR C C 173.615 0.05 1 136 28 36 TYR CA C 55.364 0.05 1 137 28 36 TYR CB C 39.022 0.05 1 138 28 36 TYR N N 116.178 0.05 1 139 29 37 PRO C C 181.021 0.05 1 140 29 37 PRO CA C 65.459 0.05 1 141 29 37 PRO CB C 32.38 0.05 1 142 30 38 ASP H H 9.523 0.02 1 143 30 38 ASP C C 179.491 0.05 1 144 30 38 ASP CA C 57.416 0.05 1 145 30 38 ASP CB C 40.538 0.05 1 146 30 38 ASP N N 118.918 0.05 1 147 31 39 GLU H H 9.074 0.02 1 148 31 39 GLU C C 179.584 0.05 1 149 31 39 GLU CA C 58.169 0.05 1 150 31 39 GLU CB C 30.649 0.05 1 151 31 39 GLU N N 119.815 0.05 1 152 32 40 ARG H H 8.412 0.02 1 153 32 40 ARG C C 178.194 0.05 1 154 32 40 ARG CA C 60.02 0.05 1 155 32 40 ARG CB C 31.637 0.05 1 156 32 40 ARG N N 116.014 0.05 1 157 33 41 ARG H H 7.894 0.02 1 158 33 41 ARG C C 177.155 0.05 1 159 33 41 ARG CA C 58.458 0.05 1 160 33 41 ARG CB C 29.698 0.05 1 161 33 41 ARG N N 114.289 0.05 1 162 34 42 TYR H H 7.507 0.02 1 163 34 42 TYR C C 174.832 0.05 1 164 34 42 TYR CA C 60.232 0.05 1 165 34 42 TYR CB C 38.215 0.05 1 166 34 42 TYR N N 116.41 0.05 1 167 35 43 PHE H H 9.162 0.02 1 168 35 43 PHE N N 118.687 0.05 1 169 36 44 LYS CA C 59.931 0.05 1 170 36 44 LYS CB C 32.598 0.05 1 171 37 45 ASN H H 8.789 0.02 1 172 37 45 ASN C C 176.283 0.05 1 173 37 45 ASN CA C 55.253 0.05 1 174 37 45 ASN CB C 37.95 0.05 1 175 37 45 ASN N N 119.094 0.05 1 176 38 46 TYR H H 8.921 0.02 1 177 38 46 TYR C C 178.227 0.05 1 178 38 46 TYR CA C 54.947 0.05 1 179 38 46 TYR CB C 38.802 0.05 1 180 38 46 TYR N N 116.85 0.05 1 181 39 47 VAL H H 8.049 0.02 1 182 39 47 VAL C C 177.716 0.05 1 183 39 47 VAL CA C 65.662 0.05 1 184 39 47 VAL CB C 32.872 0.05 1 185 39 47 VAL N N 124.143 0.05 1 186 40 48 GLY H H 9.849 0.02 1 187 40 48 GLY C C 174.535 0.05 1 188 40 48 GLY CA C 46.431 0.05 1 189 40 48 GLY N N 116.272 0.05 1 190 41 49 LYS H H 7.512 0.02 1 191 41 49 LYS C C 177.618 0.05 1 192 41 49 LYS CA C 54.358 0.05 1 193 41 49 LYS CB C 35.085 0.05 1 194 41 49 LYS N N 117.627 0.05 1 195 42 50 SER H H 10.117 0.02 1 196 42 50 SER C C 174.663 0.05 1 197 42 50 SER CA C 57.845 0.05 1 198 42 50 SER CB C 65.925 0.05 1 199 42 50 SER N N 122.657 0.05 1 200 43 51 ASP H H 9.707 0.02 1 201 43 51 ASP C C 178.503 0.05 1 202 43 51 ASP CA C 58.431 0.05 1 203 43 51 ASP CB C 40.363 0.05 1 204 43 51 ASP N N 123.009 0.05 1 205 44 52 GLN H H 8.803 0.02 1 206 44 52 GLN C C 178.618 0.05 1 207 44 52 GLN CA C 59.576 0.05 1 208 44 52 GLN CB C 28.783 0.05 1 209 44 52 GLN N N 117.162 0.05 1 210 45 53 GLU H H 8.305 0.02 1 211 45 53 GLU C C 180.576 0.05 1 212 45 53 GLU CA C 59.817 0.05 1 213 45 53 GLU CB C 30.785 0.05 1 214 45 53 GLU N N 120.918 0.05 1 215 46 54 LEU C C 179.368 0.05 1 216 46 54 LEU CA C 58.936 0.05 1 217 46 54 LEU CB C 39.519 0.05 1 218 47 55 LYS H H 8.614 0.02 1 219 47 55 LYS C C 178.586 0.05 1 220 47 55 LYS CA C 60.354 0.05 1 221 47 55 LYS CB C 32.944 0.05 1 222 47 55 LYS N N 115.906 0.05 1 223 48 56 SER H H 7.912 0.02 1 224 48 56 SER C C 173.922 0.05 1 225 48 56 SER CA C 59.376 0.05 1 226 48 56 SER CB C 64.663 0.05 1 227 48 56 SER N N 112.375 0.05 1 228 49 57 MET H H 8.396 0.02 1 229 49 57 MET C C 177.29 0.05 1 230 49 57 MET CA C 55.757 0.05 1 231 49 57 MET CB C 35.216 0.05 1 232 49 57 MET N N 124.846 0.05 1 233 51 59 LYS C C 179.458 0.05 1 234 51 59 LYS CA C 59.714 0.05 1 235 51 59 LYS CB C 33.713 0.05 1 236 52 60 PHE H H 8.026 0.02 1 237 52 60 PHE C C 179.329 0.05 1 238 52 60 PHE CA C 61.63 0.05 1 239 52 60 PHE CB C 40.696 0.05 1 240 52 60 PHE N N 120.12 0.05 1 241 53 61 GLY H H 8.535 0.02 1 242 53 61 GLY C C 175.869 0.05 1 243 53 61 GLY CA C 47.923 0.05 1 244 53 61 GLY N N 109.808 0.05 1 245 54 62 ASP H H 9.029 0.02 1 246 54 62 ASP C C 178.658 0.05 1 247 54 62 ASP CA C 58.072 0.05 1 248 54 62 ASP CB C 41.303 0.05 1 249 54 62 ASP N N 121.678 0.05 1 250 55 63 HIS H H 8.891 0.02 1 251 55 63 HIS HE2 H 11.239 0.02 1 252 55 63 HIS C C 177.955 0.05 1 253 55 63 HIS CA C 60.357 0.05 1 254 55 63 HIS CB C 33.103 0.05 1 255 55 63 HIS N N 120.754 0.05 1 256 55 63 HIS NE2 N 118.520 0.05 1 257 56 64 THR H H 8.922 0.02 1 258 56 64 THR C C 175.874 0.05 1 259 56 64 THR CA C 67.209 0.05 1 260 56 64 THR CB C 68.877 0.05 1 261 56 64 THR N N 108.896 0.05 1 262 57 65 GLU H H 8.408 0.02 1 263 57 65 GLU C C 177.866 0.05 1 264 57 65 GLU CA C 60.719 0.05 1 265 57 65 GLU CB C 30.376 0.05 1 266 57 65 GLU N N 123.285 0.05 1 267 58 66 LYS H H 7.675 0.02 1 268 58 66 LYS C C 179.796 0.05 1 269 58 66 LYS CA C 60.053 0.05 1 270 58 66 LYS CB C 32.848 0.05 1 271 58 66 LYS N N 119.407 0.05 1 272 59 67 VAL H H 7.579 0.02 1 273 59 67 VAL C C 176.23 0.05 1 274 59 67 VAL CA C 63.577 0.05 1 275 59 67 VAL CB C 30.557 0.05 1 276 59 67 VAL N N 119.779 0.05 1 277 60 68 PHE H H 7.897 0.02 1 278 60 68 PHE C C 177.548 0.05 1 279 60 68 PHE CA C 61.993 0.05 1 280 60 68 PHE CB C 38.416 0.05 1 281 60 68 PHE N N 116.24 0.05 1 282 61 69 ASN H H 8.727 0.02 1 283 61 69 ASN C C 177.796 0.05 1 284 61 69 ASN CA C 57.07 0.05 1 285 61 69 ASN CB C 38.829 0.05 1 286 61 69 ASN N N 121.019 0.05 1 287 62 70 LEU H H 6.795 0.02 1 288 62 70 LEU C C 177.903 0.05 1 289 62 70 LEU CA C 57.3 0.05 1 290 62 70 LEU CB C 40.287 0.05 1 291 62 70 LEU N N 119.073 0.05 1 292 63 71 MET H H 7.757 0.02 1 293 63 71 MET C C 177.65 0.05 1 294 63 71 MET CA C 59.497 0.05 1 295 63 71 MET CB C 33.266 0.05 1 296 63 71 MET N N 117.638 0.05 1 297 64 72 MET H H 8.239 0.02 1 298 64 72 MET C C 178.55 0.05 1 299 64 72 MET CA C 56.475 0.05 1 300 64 72 MET CB C 33.481 0.05 1 301 64 72 MET N N 114.637 0.05 1 302 65 73 GLU H H 7.707 0.02 1 303 65 73 GLU C C 178.349 0.05 1 304 65 73 GLU CA C 60.393 0.05 1 305 65 73 GLU CB C 29.72 0.05 1 306 65 73 GLU N N 121.305 0.05 1 307 66 74 VAL H H 8.349 0.02 1 308 66 74 VAL C C 180.761 0.05 1 309 66 74 VAL CA C 65.963 0.05 1 310 66 74 VAL CB C 31.957 0.05 1 311 66 74 VAL N N 118.814 0.05 1 312 67 75 ALA H H 8.658 0.02 1 313 67 75 ALA C C 176.943 0.05 1 314 67 75 ALA CA C 55.436 0.05 1 315 67 75 ALA CB C 18.038 0.05 1 316 67 75 ALA N N 122.368 0.05 1 317 68 76 ASP H H 8.798 0.02 1 318 68 76 ASP C C 178.029 0.05 1 319 68 76 ASP CA C 56.82 0.05 1 320 68 76 ASP CB C 41.912 0.05 1 321 68 76 ASP N N 119.287 0.05 1 322 69 77 ARG H H 7.828 0.02 1 323 69 77 ARG C C 178.818 0.05 1 324 69 77 ARG CA C 57.814 0.05 1 325 69 77 ARG CB C 33.202 0.05 1 326 69 77 ARG N N 114.605 0.05 1 327 70 78 ALA H H 7.537 0.02 1 328 70 78 ALA C C 177.244 0.05 1 329 70 78 ALA CA C 52.24 0.05 1 330 70 78 ALA CB C 18.582 0.05 1 331 70 78 ALA N N 121.602 0.05 1 332 71 79 THR H H 8.212 0.02 1 333 71 79 THR CA C 62.985 0.05 1 334 71 79 THR CB C 69.992 0.05 1 335 71 79 THR N N 118.65 0.05 1 336 72 80 ASP C C 175.079 0.05 1 337 72 80 ASP CA C 56.615 0.05 1 338 73 81 CYS H H 8.974 0.02 1 339 73 81 CYS C C 173.649 0.05 1 340 73 81 CYS CA C 61.069 0.05 1 341 73 81 CYS CB C 25.506 0.05 1 342 73 81 CYS N N 103.497 0.05 1 343 74 82 VAL H H 8.281 0.02 1 344 74 82 VAL C C 175.18 0.05 1 345 74 82 VAL CA C 60.731 0.05 1 346 74 82 VAL N N 123.227 0.05 1 347 75 83 PRO C C 175.457 0.05 1 348 75 83 PRO CA C 62.323 0.05 1 349 75 83 PRO CB C 32.913 0.05 1 350 76 84 LEU H H 9.805 0.02 1 351 76 84 LEU C C 179.655 0.05 1 352 76 84 LEU CA C 55.189 0.05 1 353 76 84 LEU CB C 43.371 0.05 1 354 76 84 LEU N N 121.109 0.05 1 355 77 85 ALA H H 9.342 0.02 1 356 77 85 ALA C C 180.996 0.05 1 357 77 85 ALA CA C 55.704 0.05 1 358 77 85 ALA CB C 18.504 0.05 1 359 77 85 ALA N N 127.716 0.05 1 360 78 86 SER C C 178.051 0.05 1 361 78 86 SER CA C 61.533 0.05 1 362 79 87 ASP H H 7.518 0.02 1 363 79 87 ASP C C 178.745 0.05 1 364 79 87 ASP CA C 58.146 0.05 1 365 79 87 ASP CB C 42.399 0.05 1 366 79 87 ASP N N 122.92 0.05 1 367 80 88 ALA H H 8.218 0.02 1 368 80 88 ALA C C 179.629 0.05 1 369 80 88 ALA CA C 56.437 0.05 1 370 80 88 ALA CB C 19.098 0.05 1 371 80 88 ALA N N 122.824 0.05 1 372 81 89 ASN H H 9.286 0.02 1 373 81 89 ASN C C 178.486 0.05 1 374 81 89 ASN CA C 58.118 0.05 1 375 81 89 ASN CB C 39.366 0.05 1 376 81 89 ASN N N 115.981 0.05 1 377 82 90 THR H H 9.066 0.02 1 378 82 90 THR C C 178.546 0.05 1 379 82 90 THR CA C 68.276 0.05 1 380 82 90 THR CB C 70.048 0.05 1 381 82 90 THR N N 117.845 0.05 1 382 83 91 LEU H H 9.302 0.02 1 383 83 91 LEU C C 182.6 0.05 1 384 83 91 LEU CA C 61.949 0.05 1 385 83 91 LEU CB C 45.694 0.05 1 386 83 91 LEU N N 120.411 0.05 1 387 84 92 VAL H H 9.85 0.02 1 388 84 92 VAL C C 179.239 0.05 1 389 84 92 VAL CA C 67.18 0.05 1 390 84 92 VAL CB C 33.978 0.05 1 391 84 92 VAL N N 118.619 0.05 1 392 85 93 GLN H H 9.893 0.02 1 393 85 93 GLN C C 178.526 0.05 1 394 85 93 GLN CA C 58.087 0.05 1 395 85 93 GLN CB C 29.894 0.05 1 396 85 93 GLN N N 117.241 0.05 1 397 86 94 MET H H 10.085 0.02 1 398 86 94 MET C C 180.559 0.05 1 399 86 94 MET CA C 59.224 0.05 1 400 86 94 MET CB C 38.776 0.05 1 401 86 94 MET N N 122.192 0.05 1 402 87 95 LYS C C 179.233 0.05 1 403 87 95 LYS CA C 60.05 0.05 1 404 87 95 LYS CB C 32.066 0.05 1 405 88 96 GLN H H 9.39 0.02 1 406 88 96 GLN C C 174.196 0.05 1 407 88 96 GLN CA C 57.534 0.05 1 408 88 96 GLN CB C 25.39 0.05 1 409 88 96 GLN N N 117.357 0.05 1 410 89 97 HIS H H 9.405 0.02 1 411 89 97 HIS C C 177.28 0.05 1 412 89 97 HIS CA C 54.256 0.05 1 413 89 97 HIS CB C 28.027 0.05 1 414 89 97 HIS N N 114.321 0.05 1 415 90 98 SER H H 7.913 0.02 1 416 90 98 SER C C 175.79 0.05 1 417 90 98 SER CA C 62.243 0.05 1 418 90 98 SER CB C 63.915 0.05 1 419 90 98 SER N N 117.916 0.05 1 420 91 99 SER C C 173.952 0.05 1 421 91 99 SER CA C 58.698 0.05 1 422 91 99 SER CB C 63.404 0.05 1 423 92 100 LEU H H 7.279 0.02 1 424 92 100 LEU C C 175.87 0.05 1 425 92 100 LEU CA C 54.121 0.05 1 426 92 100 LEU CB C 43.303 0.05 1 427 92 100 LEU N N 119.797 0.05 1 428 93 101 THR H H 9.026 0.02 1 429 93 101 THR C C 177.117 0.05 1 430 93 101 THR CA C 60.088 0.05 1 431 93 101 THR CB C 73.092 0.05 1 432 93 101 THR N N 109.13 0.05 1 433 94 102 THR H H 10.404 0.02 1 434 94 102 THR C C 177.916 0.05 1 435 94 102 THR CA C 66.841 0.05 1 436 94 102 THR CB C 68.832 0.05 1 437 94 102 THR N N 112.531 0.05 1 438 95 103 GLY H H 8.394 0.02 1 439 95 103 GLY C C 176.56 0.05 1 440 95 103 GLY CA C 47.309 0.05 1 441 95 103 GLY N N 108.798 0.05 1 442 96 104 ASN H H 7.873 0.02 1 443 96 104 ASN C C 177.52 0.05 1 444 96 104 ASN CA C 58.485 0.05 1 445 96 104 ASN CB C 42.02 0.05 1 446 96 104 ASN N N 118.588 0.05 1 447 97 105 PHE H H 6.796 0.02 1 448 97 105 PHE C C 176.968 0.05 1 449 97 105 PHE CA C 61.074 0.05 1 450 97 105 PHE CB C 39.468 0.05 1 451 97 105 PHE N N 115.147 0.05 1 452 98 106 GLU H H 8.621 0.02 1 453 98 106 GLU C C 178.949 0.05 1 454 98 106 GLU CA C 60.079 0.05 1 455 98 106 GLU CB C 30.527 0.05 1 456 98 106 GLU N N 120.054 0.05 1 457 99 107 LYS H H 7.392 0.02 1 458 99 107 LYS C C 177.588 0.05 1 459 99 107 LYS CA C 60.249 0.05 1 460 99 107 LYS CB C 33.592 0.05 1 461 99 107 LYS N N 117.329 0.05 1 462 100 108 LEU H H 6.727 0.02 1 463 100 108 LEU C C 177.6 0.05 1 464 100 108 LEU CA C 58.516 0.05 1 465 100 108 LEU CB C 40.143 0.05 1 466 100 108 LEU N N 119.504 0.05 1 467 101 109 PHE H H 7.625 0.02 1 468 101 109 PHE C C 178.654 0.05 1 469 101 109 PHE CA C 63.934 0.05 1 470 101 109 PHE CB C 38.747 0.05 1 471 101 109 PHE N N 115 0.05 1 472 102 110 VAL H H 8.76 0.02 1 473 102 110 VAL C C 179.504 0.05 1 474 102 110 VAL CA C 67.804 0.05 1 475 102 110 VAL CB C 31.811 0.05 1 476 102 110 VAL N N 123.439 0.05 1 477 103 111 ALA H H 8.47 0.02 1 478 103 111 ALA C C 174.838 0.05 1 479 103 111 ALA CA C 55.728 0.05 1 480 103 111 ALA CB C 18.541 0.05 1 481 103 111 ALA N N 120.978 0.05 1 482 104 112 LEU H H 8.765 0.02 1 483 104 112 LEU C C 176.319 0.05 1 484 104 112 LEU CA C 56.646 0.05 1 485 104 112 LEU CB C 41.204 0.05 1 486 104 112 LEU N N 120.375 0.05 1 487 105 113 VAL H H 8.602 0.02 1 488 105 113 VAL C C 175.444 0.05 1 489 105 113 VAL CA C 59.996 0.05 1 490 105 113 VAL CB C 32.578 0.05 1 491 105 113 VAL N N 121.433 0.05 1 492 106 114 GLU H H 8.757 0.02 1 493 106 114 GLU C C 179.913 0.05 1 494 106 114 GLU CA C 60.575 0.05 1 495 106 114 GLU CB C 29.932 0.05 1 496 106 114 GLU N N 120.671 0.05 1 497 107 115 TYR H H 8.911 0.02 1 498 107 115 TYR C C 178.9 0.05 1 499 107 115 TYR CA C 61.858 0.05 1 500 107 115 TYR CB C 37.96 0.05 1 501 107 115 TYR N N 121.848 0.05 1 502 108 116 MET H H 8.676 0.02 1 503 108 116 MET C C 180.152 0.05 1 504 108 116 MET CA C 61.085 0.05 1 505 108 116 MET CB C 32.657 0.05 1 506 108 116 MET N N 120.38 0.05 1 507 109 117 ARG H H 8.979 0.02 1 508 109 117 ARG C C 178.262 0.05 1 509 109 117 ARG CA C 60.154 0.05 1 510 109 117 ARG CB C 31.027 0.05 1 511 109 117 ARG N N 120.128 0.05 1 512 110 118 ALA H H 8.084 0.02 1 513 110 118 ALA C C 178.98 0.05 1 514 110 118 ALA CA C 53.238 0.05 1 515 110 118 ALA CB C 19.459 0.05 1 516 110 118 ALA N N 120.473 0.05 1 517 111 119 SER H H 7.853 0.02 1 518 111 119 SER C C 176.117 0.05 1 519 111 119 SER CA C 60.653 0.05 1 520 111 119 SER CB C 64.311 0.05 1 521 111 119 SER N N 113.827 0.05 1 522 112 120 GLY H H 8.623 0.02 1 523 112 120 GLY C C 175.013 0.05 1 524 112 120 GLY CA C 46.447 0.05 1 525 112 120 GLY N N 111.742 0.05 1 526 113 121 GLN H H 8.594 0.02 1 527 113 121 GLN CA C 54.933 0.05 1 528 113 121 GLN CB C 29.786 0.05 1 529 113 121 GLN N N 120.119 0.05 1 530 114 122 SER C C 174.523 0.05 1 531 114 122 SER CA C 58.515 0.05 1 532 114 122 SER CB C 62.763 0.05 1 533 115 123 PHE H H 7.936 0.02 1 534 115 123 PHE C C 177.491 0.05 1 535 115 123 PHE CA C 58.029 0.05 1 536 115 123 PHE CB C 43.457 0.05 1 537 115 123 PHE N N 121.339 0.05 1 538 116 124 ASP H H 12.348 0.02 1 539 116 124 ASP C C 178.007 0.05 1 540 116 124 ASP CA C 52.311 0.05 1 541 116 124 ASP CB C 43.474 0.05 1 542 116 124 ASP N N 128.264 0.05 1 543 117 125 SER H H 8.321 0.02 1 544 117 125 SER C C 176.348 0.05 1 545 117 125 SER CA C 63.318 0.05 1 546 117 125 SER N N 119.126 0.05 1 547 118 126 GLN H H 9.184 0.02 1 548 118 126 GLN C C 179.827 0.05 1 549 118 126 GLN CA C 59.606 0.05 1 550 118 126 GLN CB C 28.866 0.05 1 551 118 126 GLN N N 120.982 0.05 1 552 119 127 SER H H 7.966 0.02 1 553 119 127 SER C C 175.929 0.05 1 554 119 127 SER CA C 62.258 0.05 1 555 119 127 SER N N 117.951 0.05 1 556 120 128 TRP H H 7.841 0.02 1 557 120 128 TRP HE1 H 11.809 0.02 1 558 120 128 TRP C C 178.035 0.05 1 559 120 128 TRP CA C 62.105 0.05 1 560 120 128 TRP CB C 29.18 0.05 1 561 120 128 TRP N N 123.706 0.05 1 562 120 128 TRP NE1 N 132.966 0.05 1 563 121 129 ASP H H 8.52 0.02 1 564 121 129 ASP C C 178.65 0.05 1 565 121 129 ASP CA C 57.43 0.05 1 566 121 129 ASP CB C 42.371 0.05 1 567 121 129 ASP N N 120.696 0.05 1 568 122 130 ARG H H 8.081 0.02 1 569 122 130 ARG CA C 60.052 0.05 1 570 122 130 ARG CB C 30.946 0.05 1 571 122 130 ARG N N 119.321 0.05 1 572 123 131 PHE H H 8.876 0.02 1 573 123 131 PHE C C 176.743 0.05 1 574 123 131 PHE CA C 60.292 0.05 1 575 123 131 PHE CB C 40.073 0.05 1 576 123 131 PHE N N 119.045 0.05 1 577 124 132 GLY H H 8.75 0.02 1 578 124 132 GLY C C 176.131 0.05 1 579 124 132 GLY CA C 46.333 0.05 1 580 124 132 GLY N N 107.244 0.05 1 581 125 133 LYS H H 8.126 0.02 1 582 125 133 LYS C C 180.258 0.05 1 583 125 133 LYS CA C 59.964 0.05 1 584 125 133 LYS CB C 32.692 0.05 1 585 125 133 LYS N N 122.098 0.05 1 586 126 134 ASN H H 8.87 0.02 1 587 126 134 ASN C C 179.077 0.05 1 588 126 134 ASN CA C 55.276 0.05 1 589 126 134 ASN CB C 38 0.05 1 590 126 134 ASN N N 119.49 0.05 1 591 127 135 LEU H H 9.262 0.02 1 592 127 135 LEU C C 177.718 0.05 1 593 127 135 LEU CA C 58.242 0.05 1 594 127 135 LEU CB C 40.151 0.05 1 595 127 135 LEU N N 125.314 0.05 1 596 128 136 VAL H H 8.323 0.02 1 597 128 136 VAL C C 178 0.05 1 598 128 136 VAL CA C 68.466 0.05 1 599 128 136 VAL CB C 31.467 0.05 1 600 128 136 VAL N N 120.483 0.05 1 601 129 137 SER H H 8.081 0.02 1 602 129 137 SER C C 177.386 0.05 1 603 129 137 SER CA C 62.035 0.05 1 604 129 137 SER CB C 63.047 0.05 1 605 129 137 SER N N 113.995 0.05 1 606 130 138 ALA H H 8.356 0.02 1 607 130 138 ALA C C 181.239 0.05 1 608 130 138 ALA CA C 55.241 0.05 1 609 130 138 ALA CB C 18.816 0.05 1 610 130 138 ALA N N 124.914 0.05 1 611 131 139 LEU H H 9.306 0.02 1 612 131 139 LEU C C 179.612 0.05 1 613 131 139 LEU CA C 58.734 0.05 1 614 131 139 LEU CB C 40.579 0.05 1 615 131 139 LEU N N 121.878 0.05 1 616 132 140 SER H H 8.367 0.02 1 617 132 140 SER C C 180.509 0.05 1 618 132 140 SER CA C 61.405 0.05 1 619 132 140 SER CB C 63.13 0.05 1 620 132 140 SER N N 115.026 0.05 1 621 133 141 SER H H 8.785 0.02 1 622 133 141 SER C C 175.653 0.05 1 623 133 141 SER CA C 62.363 0.05 1 624 133 141 SER CB C 63.261 0.05 1 625 133 141 SER N N 118.97 0.05 1 626 134 142 ALA H H 8.263 0.02 1 627 134 142 ALA C C 177.334 0.05 1 628 134 142 ALA CA C 52.97 0.05 1 629 134 142 ALA CB C 19.522 0.05 1 630 134 142 ALA N N 122.443 0.05 1 631 135 143 GLY H H 8.243 0.02 1 632 135 143 GLY C C 175.034 0.05 1 633 135 143 GLY CA C 45.712 0.05 1 634 135 143 GLY N N 105.714 0.05 1 635 136 144 MET H H 8.811 0.02 1 636 136 144 MET C C 176.063 0.05 1 637 136 144 MET CA C 57.611 0.05 1 638 136 144 MET CB C 35.82 0.05 1 639 136 144 MET N N 124.607 0.05 1 640 137 145 LYS H H 9.009 0.02 1 641 137 145 LYS C C 180.27 0.05 1 642 137 145 LYS CA C 58.487 0.05 1 643 137 145 LYS CB C 33.177 0.05 1 644 137 145 LYS N N 133.734 0.05 1 stop_ save_