data_5022 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Converting a DNA Damage Checkpoint Effector (UmuD2C) into a Lesion Bypass Polymerase (UmuD'2C) ; _BMRB_accession_number 5022 _BMRB_flat_file_name bmr5022.str _Entry_type original _Submission_date 2001-05-21 _Accession_date 2001-05-21 _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 Ferentz A. E. . 2 Walker G. C. . 3 Wagner G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 447 "13C chemical shifts" 290 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-07 original author . stop_ _Original_release_date 2003-01-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Converting a DNA Damage Checkpoint Effector (UmuD2C) into a Lesion Bypass Polymerase (UmuD'2C) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21376075 _PubMed_ID 11483531 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ferentz A. E. . 2 Walker G. C. . 3 Wagner G. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 20 _Journal_issue 15 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4287 _Page_last 4298 _Year 2001 _Details . loop_ _Keyword 'SOS response' 'SOS mutagenesis' 'DNA repair' 'DNA polymerase V' 'DNA polymerase accessory protein' 'LexA repressor' 'lambda CI' 'signal peptidase' 'serine-lysine dyad' 'autocatalytic cleavage' 'serine protease' stop_ save_ ################################## # Molecular system description # ################################## save_system_UMUD _Saveframe_category molecular_system _Mol_system_name 'UMUD PROTEIN' _Abbreviation_common UMUD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UMUD PROTEIN, chain A' $UMUD 'UMUD PROTEIN, chain B' $UMUD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'UMUD PROTEIN, chain A' 1 'UMUD PROTEIN, chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UMUD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'UMUD PROTEIN' _Abbreviation_common UMUD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 115 _Mol_residue_sequence ; AFPSPAADYVEQRIDLNQLL IQHPSATYFVKASGDSMIDG GISDGDLLIVDSAITASHGD IVIAAVDGEFTVKKLQLRPT VQLIPMNSAYSPITISSEDT LDVFGVVIHVVKAMR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 25 ALA 2 26 PHE 3 27 PRO 4 28 SER 5 29 PRO 6 30 ALA 7 31 ALA 8 32 ASP 9 33 TYR 10 34 VAL 11 35 GLU 12 36 GLN 13 37 ARG 14 38 ILE 15 39 ASP 16 40 LEU 17 41 ASN 18 42 GLN 19 43 LEU 20 44 LEU 21 45 ILE 22 46 GLN 23 47 HIS 24 48 PRO 25 49 SER 26 50 ALA 27 51 THR 28 52 TYR 29 53 PHE 30 54 VAL 31 55 LYS 32 56 ALA 33 57 SER 34 58 GLY 35 59 ASP 36 60 SER 37 61 MET 38 62 ILE 39 63 ASP 40 64 GLY 41 65 GLY 42 66 ILE 43 67 SER 44 68 ASP 45 69 GLY 46 70 ASP 47 71 LEU 48 72 LEU 49 73 ILE 50 74 VAL 51 75 ASP 52 76 SER 53 77 ALA 54 78 ILE 55 79 THR 56 80 ALA 57 81 SER 58 82 HIS 59 83 GLY 60 84 ASP 61 85 ILE 62 86 VAL 63 87 ILE 64 88 ALA 65 89 ALA 66 90 VAL 67 91 ASP 68 92 GLY 69 93 GLU 70 94 PHE 71 95 THR 72 96 VAL 73 97 LYS 74 98 LYS 75 99 LEU 76 100 GLN 77 101 LEU 78 102 ARG 79 103 PRO 80 104 THR 81 105 VAL 82 106 GLN 83 107 LEU 84 108 ILE 85 109 PRO 86 110 MET 87 111 ASN 88 112 SER 89 113 ALA 90 114 TYR 91 115 SER 92 116 PRO 93 117 ILE 94 118 THR 95 119 ILE 96 120 SER 97 121 SER 98 122 GLU 99 123 ASP 100 124 THR 101 125 LEU 102 126 ASP 103 127 VAL 104 128 PHE 105 129 GLY 106 130 VAL 107 131 VAL 108 132 ILE 109 133 HIS 110 134 VAL 111 135 VAL 112 136 LYS 113 137 ALA 114 138 MET 115 139 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1AY9 "Wild-Type Umud' From E. Coli" 93.91 108 100.00 100.00 1.54e-69 PDB 1I4V "Solution Structure Of The Umud' Homodimer" 100.00 115 100.00 100.00 3.96e-75 PDB 1UMU "Structure Determination Of Umud' By Mad Phasing Of The Selenomethionyl Protein" 98.26 116 97.35 97.35 2.21e-70 DBJ BAA36030 "DNA polymerase V, subunit D [Escherichia coli str. K-12 substr. W3110]" 100.00 139 99.13 99.13 4.58e-74 DBJ BAB35101 "UmuD protein [Escherichia coli O157:H7 str. Sakai]" 100.00 139 99.13 99.13 4.58e-74 DBJ BAG76755 "mutagenesis and repair protein UmuD [Escherichia coli SE11]" 100.00 139 99.13 99.13 4.58e-74 DBJ BAI24995 "DNA polymerase V subunit D [Escherichia coli O26:H11 str. 11368]" 100.00 139 99.13 99.13 4.58e-74 DBJ BAI30119 "DNA polymerase V subunit D [Escherichia coli O103:H2 str. 12009]" 100.00 139 99.13 99.13 4.58e-74 EMBL CAP75718 "Protein umuD [Escherichia coli LF82]" 100.00 139 98.26 98.26 2.32e-73 EMBL CAQ31685 "SOS mutagenesis; error-prone repair; processed to UmuD'; forms complex with UmuC, subunit of DNA polymerase V [Escherichia coli" 100.00 139 99.13 99.13 4.58e-74 EMBL CAQ98062 "DNA polymerase V, subunit D [Escherichia coli IAI1]" 100.00 139 99.13 99.13 4.58e-74 EMBL CAR02572 "DNA polymerase V, subunit D [Escherichia coli S88]" 100.00 139 98.26 98.26 2.32e-73 EMBL CAR07525 "DNA polymerase V, subunit D [Escherichia coli ED1a]" 100.00 139 98.26 99.13 7.23e-74 GB AAA24728 "UmuD protein [Escherichia coli]" 100.00 139 99.13 99.13 4.58e-74 GB AAA98073 "umuD [Escherichia coli]" 100.00 139 99.13 99.13 4.58e-74 GB AAC74267 "translesion error-prone DNA polymerase V subunit; RecA-activated auto-protease [Escherichia coli str. K-12 substr. MG1655]" 100.00 139 99.13 99.13 4.58e-74 GB AAG56034 "SOS mutagenesis; error-prone repair; processed to UmuD'; forms complex with UmuC [Escherichia coli O157:H7 str. EDL933]" 100.00 139 99.13 99.13 4.58e-74 GB AAN42787 "mutagenesis and repair protein [Shigella flexneri 2a str. 301]" 100.00 139 99.13 99.13 4.58e-74 REF NP_287422 "DNA polymerase V subunit UmuD [Escherichia coli O157:H7 str. EDL933]" 100.00 139 99.13 99.13 4.58e-74 REF NP_309705 "DNA polymerase V subunit UmuD [Escherichia coli O157:H7 str. Sakai]" 100.00 139 99.13 99.13 4.58e-74 REF NP_415701 "translesion error-prone DNA polymerase V subunit; RecA-activated auto-protease [Escherichia coli str. K-12 substr. MG1655]" 100.00 139 99.13 99.13 4.58e-74 REF NP_707080 "DNA polymerase V subunit UmuD [Shigella flexneri 2a str. 301]" 100.00 139 99.13 99.13 4.58e-74 REF NP_753536 "DNA polymerase V subunit UmuD [Escherichia coli CFT073]" 100.00 139 98.26 98.26 2.32e-73 SP P0AG11 "RecName: Full=Protein UmuD; Contains: RecName: Full=Protein UmuD' [Escherichia coli K-12]" 100.00 139 99.13 99.13 4.58e-74 SP P0AG12 "RecName: Full=Protein UmuD; Contains: RecName: Full=Protein UmuD' [Escherichia coli O157:H7]" 100.00 139 99.13 99.13 4.58e-74 SP P0AG13 "RecName: Full=Protein UmuD; Contains: RecName: Full=Protein UmuD' [Shigella flexneri]" 100.00 139 99.13 99.13 4.58e-74 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $UMUD 'E. coli' 562 Bacteria . Escherichia coli 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 $UMUD 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UMUD 0.9 mM [U-15N] NaCl 150 mM . phosphate 10 mM . DTT 1 mM . EDTA 0.1 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UMUD 1.3 mM '[U-15N; U-13C]' NaCl 150 mM . phosphate 20 mM . DTT 1 mM . EDTA 0.1 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UMUD 1.5 mM . NaCl 150 mM . phosphate 10 mM . DTT 1 mM . EDTA 0.1 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UMUD 1.4 mM . NaCl 150 mM . phosphate 10 mM . DTT 1 mM . EDTA 0.1 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.9 loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXR _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNHA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 303 . K 'ionic strength' 160 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis TSP H 1 'methyl protons' ppm . . . . . . TSP N 15 'methyl protons' ppm . . . . . . TSP C 13 'methyl protons' ppm . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'UMUD PROTEIN, chain A' _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 PRO CA C 62.882 0.2 . 2 . 3 PRO HA H 4.512 0.02 . 3 . 3 PRO CB C 31.314 0.2 . 4 . 3 PRO HB2 H 1.875 0.02 . 5 . 3 PRO HB3 H 2.199 0.02 . 6 . 4 SER N N 117.868 0.2 . 7 . 4 SER H H 8.301 0.02 . 8 . 4 SER HA H 4.790 0.02 . 9 . 4 SER HB2 H 3.926 0.02 . 10 . 5 PRO HA H 4.421 0.02 . 11 . 6 ALA N N 123.083 0.2 . 12 . 6 ALA H H 8.050 0.02 . 13 . 6 ALA CA C 52.256 0.2 . 14 . 6 ALA HA H 4.248 0.02 . 15 . 6 ALA HB H 1.315 0.02 . 16 . 6 ALA CB C 18.937 0.2 . 17 . 7 ALA N N 122.579 0.2 . 18 . 7 ALA H H 8.045 0.02 . 19 . 7 ALA CA C 52.764 0.2 . 20 . 7 ALA HA H 4.260 0.02 . 21 . 7 ALA HB H 1.375 0.02 . 22 . 7 ALA CB C 18.949 0.2 . 23 . 8 ASP N N 118.073 0.2 . 24 . 8 ASP H H 8.166 0.02 . 25 . 8 ASP CA C 54.507 0.2 . 26 . 8 ASP HA H 4.574 0.02 . 27 . 8 ASP CB C 40.477 0.2 . 28 . 8 ASP HB2 H 2.613 0.02 . 29 . 9 TYR N N 119.589 0.2 . 30 . 9 TYR H H 7.877 0.02 . 31 . 9 TYR CA C 58.258 0.2 . 32 . 9 TYR HA H 4.583 0.02 . 33 . 9 TYR CB C 38.633 0.2 . 34 . 9 TYR HB2 H 3.000 0.02 . 35 . 9 TYR HD1 H 7.040 0.02 . 36 . 10 VAL N N 119.533 0.2 . 37 . 10 VAL H H 7.717 0.02 . 38 . 10 VAL CA C 61.976 0.2 . 39 . 10 VAL HA H 4.238 0.02 . 40 . 10 VAL CB C 32.529 0.2 . 41 . 10 VAL HB H 2.080 0.02 . 42 . 10 VAL CG1 C 21.065 0.2 . 43 . 10 VAL HG1 H 0.829 0.02 . 44 . 11 GLU N N 123.924 0.2 . 45 . 11 GLU H H 8.556 0.02 . 46 . 11 GLU CA C 55.902 0.2 . 47 . 11 GLU HA H 4.569 0.02 . 48 . 11 GLU CB C 30.704 0.2 . 49 . 11 GLU HB2 H 2.216 0.02 . 50 . 12 GLN N N 120.793 0.2 . 51 . 12 GLN H H 8.443 0.02 . 52 . 12 GLN CA C 55.861 0.2 . 53 . 12 GLN HA H 4.529 0.02 . 54 . 12 GLN CB C 30.727 0.2 . 55 . 12 GLN HB2 H 2.049 0.02 . 56 . 12 GLN HB3 H 2.211 0.02 . 57 . 12 GLN CG C 34.587 0.2 . 58 . 12 GLN HG2 H 2.403 0.02 . 59 . 13 ARG N N 121.403 0.2 . 60 . 13 ARG H H 8.550 0.02 . 61 . 13 ARG CA C 56.015 0.2 . 62 . 13 ARG HA H 4.562 0.02 . 63 . 13 ARG CB C 29.184 0.2 . 64 . 13 ARG HB2 H 1.816 0.02 . 65 . 13 ARG HG2 H 1.607 0.02 . 66 . 13 ARG CD C 43.105 0.2 . 67 . 13 ARG HD2 H 3.195 0.02 . 68 . 14 ILE N N 122.447 0.2 . 69 . 14 ILE H H 7.284 0.02 . 70 . 14 ILE CA C 59.789 0.2 . 71 . 14 ILE HA H 4.194 0.02 . 72 . 14 ILE CB C 39.249 0.2 . 73 . 14 ILE HG2 H 0.513 0.02 . 74 . 14 ILE CG2 C 17.099 0.2 . 75 . 14 ILE HG12 H 1.216 0.02 . 76 . 14 ILE HD1 H 0.789 0.02 . 77 . 15 ASP N N 125.241 0.2 . 78 . 15 ASP H H 8.296 0.02 . 79 . 15 ASP CA C 52.390 0.2 . 80 . 15 ASP HA H 4.754 0.02 . 81 . 15 ASP CB C 40.677 0.2 . 82 . 15 ASP HB2 H 2.923 0.02 . 83 . 15 ASP HB3 H 2.688 0.02 . 84 . 16 LEU N N 128.278 0.2 . 85 . 16 LEU H H 9.382 0.02 . 86 . 16 LEU CA C 53.143 0.2 . 87 . 16 LEU HA H 3.776 0.02 . 88 . 16 LEU CB C 42.842 0.2 . 89 . 16 LEU HB2 H 1.571 0.02 . 90 . 16 LEU CG C 26.860 0.2 . 91 . 16 LEU HG H 1.678 0.02 . 92 . 16 LEU HD1 H 0.562 0.02 . 93 . 16 LEU HD2 H 0.827 0.02 . 94 . 16 LEU CD1 C 22.738 0.2 . 95 . 16 LEU CD2 C 26.646 0.2 . 96 . 17 ASN N N 115.506 0.2 . 97 . 17 ASN H H 8.255 0.02 . 98 . 17 ASN CA C 56.170 0.2 . 99 . 17 ASN HA H 4.426 0.02 . 100 . 17 ASN CB C 38.109 0.2 . 101 . 17 ASN HB2 H 2.805 0.02 . 102 . 17 ASN HB3 H 3.072 0.02 . 103 . 18 GLN N N 117.561 0.2 . 104 . 18 GLN H H 7.097 0.02 . 105 . 18 GLN CA C 57.097 0.2 . 106 . 18 GLN HA H 4.179 0.02 . 107 . 18 GLN CB C 28.928 0.2 . 108 . 18 GLN HB2 H 2.211 0.02 . 109 . 18 GLN HB3 H 2.040 0.02 . 110 . 18 GLN CG C 34.436 0.2 . 111 . 18 GLN HG2 H 2.461 0.02 . 112 . 19 LEU N N 118.387 0.2 . 113 . 19 LEU H H 7.743 0.02 . 114 . 19 LEU CA C 57.307 0.2 . 115 . 19 LEU HA H 4.103 0.02 . 116 . 19 LEU CB C 43.657 0.2 . 117 . 19 LEU HB2 H 2.015 0.02 . 118 . 19 LEU CG C 27.203 0.2 . 119 . 19 LEU HG H 1.486 0.02 . 120 . 19 LEU HD1 H 0.670 0.02 . 121 . 19 LEU HD2 H 0.850 0.02 . 122 . 19 LEU CD1 C 24.700 0.2 . 123 . 19 LEU CD2 C 22.861 0.2 . 124 . 20 LEU N N 113.317 0.2 . 125 . 20 LEU H H 7.508 0.02 . 126 . 20 LEU CA C 55.358 0.2 . 127 . 20 LEU HA H 4.257 0.02 . 128 . 20 LEU CB C 42.775 0.2 . 129 . 20 LEU HB2 H 1.168 0.02 . 130 . 20 LEU CG C 26.256 0.2 . 131 . 20 LEU HG H 1.501 0.02 . 132 . 20 LEU HD1 H 0.530 0.02 . 133 . 20 LEU HD2 H 0.041 0.02 . 134 . 20 LEU CD1 C 25.638 0.2 . 135 . 20 LEU CD2 C 20.781 0.2 . 136 . 21 ILE N N 116.851 0.2 . 137 . 21 ILE H H 7.298 0.02 . 138 . 21 ILE CA C 60.236 0.2 . 139 . 21 ILE HA H 4.206 0.02 . 140 . 21 ILE CB C 37.144 0.2 . 141 . 21 ILE HB H 2.368 0.02 . 142 . 21 ILE HG2 H 0.781 0.02 . 143 . 21 ILE CG2 C 16.789 0.2 . 144 . 21 ILE CG1 C 26.849 0.2 . 145 . 21 ILE HG12 H 1.708 0.02 . 146 . 21 ILE HD1 H 1.090 0.02 . 147 . 21 ILE CD1 C 12.990 0.2 . 148 . 22 GLN N N 126.714 0.2 . 149 . 22 GLN H H 8.209 0.02 . 150 . 22 GLN CA C 56.646 0.2 . 151 . 22 GLN HA H 4.284 0.02 . 152 . 22 GLN CB C 30.204 0.2 . 153 . 22 GLN HB2 H 1.605 0.02 . 154 . 22 GLN CG C 34.007 0.2 . 155 . 22 GLN HG2 H 2.196 0.02 . 156 . 23 HIS N N 117.256 0.2 . 157 . 23 HIS H H 8.825 0.02 . 158 . 23 HIS CA C 52.205 0.2 . 159 . 23 HIS HA H 5.363 0.02 . 160 . 23 HIS HB2 H 3.302 0.02 . 161 . 25 SER CA C 60.319 0.2 . 162 . 25 SER HA H 4.472 0.02 . 163 . 25 SER CB C 62.731 0.2 . 164 . 25 SER HB2 H 4.074 0.02 . 165 . 26 ALA N N 124.844 0.2 . 166 . 26 ALA H H 7.701 0.02 . 167 . 26 ALA CA C 50.326 0.2 . 168 . 26 ALA HA H 4.732 0.02 . 169 . 26 ALA HB H 1.456 0.02 . 170 . 26 ALA CB C 21.473 0.2 . 171 . 27 THR N N 116.465 0.2 . 172 . 27 THR H H 7.020 0.02 . 173 . 27 THR CA C 61.980 0.2 . 174 . 27 THR HA H 5.650 0.02 . 175 . 27 THR CB C 69.708 0.2 . 176 . 27 THR HB H 3.830 0.02 . 177 . 27 THR HG2 H 1.014 0.02 . 178 . 27 THR CG2 C 21.319 0.2 . 179 . 28 TYR N N 126.411 0.2 . 180 . 28 TYR H H 9.423 0.02 . 181 . 28 TYR CA C 56.188 0.2 . 182 . 28 TYR HA H 4.754 0.02 . 183 . 28 TYR CB C 41.705 0.2 . 184 . 28 TYR HB2 H 2.553 0.02 . 185 . 28 TYR HE1 H 6.753 0.02 . 186 . 29 PHE N N 120.361 0.2 . 187 . 29 PHE H H 8.871 0.02 . 188 . 29 PHE CA C 54.923 0.2 . 189 . 29 PHE HA H 5.781 0.02 . 190 . 29 PHE CB C 40.547 0.2 . 191 . 29 PHE HB2 H 3.008 0.02 . 192 . 29 PHE HD1 H 7.272 0.02 . 193 . 29 PHE HE1 H 6.989 0.02 . 194 . 30 VAL N N 122.952 0.2 . 195 . 30 VAL H H 8.905 0.02 . 196 . 30 VAL CA C 60.104 0.2 . 197 . 30 VAL HA H 4.619 0.02 . 198 . 30 VAL CB C 36.702 0.2 . 199 . 30 VAL HB H 1.905 0.02 . 200 . 30 VAL HG1 H 0.831 0.02 . 201 . 30 VAL CG1 C 20.930 0.2 . 202 . 31 LYS N N 127.633 0.2 . 203 . 31 LYS H H 8.816 0.02 . 204 . 31 LYS CA C 54.928 0.2 . 205 . 31 LYS HA H 5.014 0.02 . 206 . 31 LYS CB C 32.778 0.2 . 207 . 31 LYS HB2 H 1.745 0.02 . 208 . 31 LYS CG C 24.641 0.2 . 209 . 31 LYS HG2 H 1.485 0.02 . 210 . 31 LYS CD C 29.305 0.2 . 211 . 31 LYS HD2 H 1.737 0.02 . 212 . 31 LYS CE C 41.218 0.2 . 213 . 31 LYS HE2 H 3.035 0.02 . 214 . 32 ALA N N 129.416 0.2 . 215 . 32 ALA H H 9.229 0.02 . 216 . 32 ALA CA C 52.233 0.2 . 217 . 32 ALA HA H 4.245 0.02 . 218 . 32 ALA HB H 1.399 0.02 . 219 . 32 ALA CB C 19.102 0.2 . 220 . 33 SER N N 118.624 0.2 . 221 . 33 SER H H 8.887 0.02 . 222 . 33 SER CA C 56.183 0.2 . 223 . 33 SER HA H 5.245 0.02 . 224 . 33 SER CB C 65.017 0.2 . 225 . 33 SER HB2 H 3.848 0.02 . 226 . 34 GLY N N 117.477 0.2 . 227 . 34 GLY H H 10.120 0.02 . 228 . 34 GLY CA C 44.973 0.2 . 229 . 34 GLY HA2 H 4.045 0.02 . 230 . 34 GLY HA3 H 4.395 0.02 . 231 . 35 ASP N N 115.826 0.2 . 232 . 35 ASP H H 8.130 0.02 . 233 . 35 ASP CA C 53.434 0.2 . 234 . 35 ASP HA H 5.037 0.02 . 235 . 35 ASP CB C 41.171 0.2 . 236 . 35 ASP HB2 H 2.874 0.02 . 237 . 35 ASP HB3 H 3.073 0.02 . 238 . 36 SER N N 117.548 0.2 . 239 . 36 SER H H 8.679 0.02 . 240 . 36 SER CA C 63.187 0.2 . 241 . 36 SER HA H 4.056 0.02 . 242 . 36 SER HB2 H 3.532 0.02 . 243 . 36 SER HB3 H 3.654 0.02 . 244 . 37 MET N N 117.992 0.2 . 245 . 37 MET H H 8.477 0.02 . 246 . 37 MET CA C 52.620 0.2 . 247 . 37 MET HA H 5.145 0.02 . 248 . 37 MET HB2 H 2.554 0.02 . 249 . 37 MET HG2 H 2.504 0.02 . 250 . 38 ILE N N 121.008 0.2 . 251 . 38 ILE H H 7.375 0.02 . 252 . 38 ILE CA C 64.907 0.2 . 253 . 38 ILE HA H 4.228 0.02 . 254 . 38 ILE CB C 38.661 0.2 . 255 . 38 ILE HB H 2.048 0.02 . 256 . 38 ILE HG2 H 1.279 0.02 . 257 . 38 ILE CG2 C 17.943 0.2 . 258 . 38 ILE CG1 C 27.094 0.2 . 259 . 38 ILE HG12 H 1.685 0.02 . 260 . 38 ILE HD1 H 1.064 0.02 . 261 . 38 ILE CD1 C 13.748 0.2 . 262 . 39 ASP N N 122.883 0.2 . 263 . 39 ASP H H 9.021 0.02 . 264 . 39 ASP CA C 56.441 0.2 . 265 . 39 ASP HA H 4.730 0.02 . 266 . 39 ASP CB C 38.818 0.2 . 267 . 39 ASP HB2 H 2.570 0.02 . 268 . 39 ASP HB3 H 2.830 0.02 . 269 . 40 GLY N N 107.793 0.2 . 270 . 40 GLY H H 8.282 0.02 . 271 . 40 GLY CA C 44.001 0.2 . 272 . 40 GLY HA2 H 3.919 0.02 . 273 . 40 GLY HA3 H 4.564 0.02 . 274 . 41 GLY N N 105.863 0.2 . 275 . 41 GLY H H 7.772 0.02 . 276 . 41 GLY CA C 44.733 0.2 . 277 . 41 GLY HA2 H 3.777 0.02 . 278 . 41 GLY HA3 H 4.229 0.02 . 279 . 42 ILE N N 119.976 0.2 . 280 . 42 ILE H H 6.927 0.02 . 281 . 42 ILE CA C 60.754 0.2 . 282 . 42 ILE HA H 4.301 0.02 . 283 . 42 ILE CB C 32.834 0.2 . 284 . 42 ILE HB H 2.017 0.02 . 285 . 42 ILE HG2 H 0.824 0.02 . 286 . 42 ILE CG2 C 17.099 0.2 . 287 . 42 ILE CG1 C 26.981 0.2 . 288 . 42 ILE HG12 H 1.560 0.02 . 289 . 42 ILE HD1 H 0.798 0.02 . 290 . 42 ILE CD1 C 12.283 0.2 . 291 . 43 SER N N 127.131 0.2 . 292 . 43 SER H H 9.459 0.02 . 293 . 43 SER CA C 56.032 0.2 . 294 . 43 SER HA H 4.750 0.02 . 295 . 43 SER CB C 64.677 0.2 . 296 . 43 SER HB2 H 3.723 0.02 . 297 . 43 SER HB3 H 3.935 0.02 . 298 . 44 ASP N N 123.180 0.2 . 299 . 44 ASP H H 8.498 0.02 . 300 . 44 ASP CA C 56.806 0.2 . 301 . 44 ASP HA H 4.043 0.02 . 302 . 44 ASP CB C 42.462 0.2 . 303 . 44 ASP HB2 H 2.580 0.02 . 304 . 45 GLY N N 115.717 0.2 . 305 . 45 GLY H H 8.771 0.02 . 306 . 45 GLY CA C 44.972 0.2 . 307 . 45 GLY HA2 H 3.662 0.02 . 308 . 45 GLY HA3 H 4.545 0.02 . 309 . 46 ASP N N 122.661 0.2 . 310 . 46 ASP H H 8.198 0.02 . 311 . 46 ASP CA C 55.419 0.2 . 312 . 46 ASP HA H 4.768 0.02 . 313 . 46 ASP CB C 41.018 0.2 . 314 . 46 ASP HB2 H 2.595 0.02 . 315 . 46 ASP HB3 H 2.745 0.02 . 316 . 47 LEU N N 122.255 0.2 . 317 . 47 LEU H H 8.251 0.02 . 318 . 47 LEU CA C 54.480 0.2 . 319 . 47 LEU HA H 4.722 0.02 . 320 . 47 LEU CB C 43.657 0.2 . 321 . 47 LEU HB2 H 1.568 0.02 . 322 . 47 LEU CG C 26.534 0.2 . 323 . 47 LEU HG H 2.359 0.02 . 324 . 47 LEU HD1 H 0.693 0.02 . 325 . 47 LEU HD2 H 0.869 0.02 . 326 . 47 LEU CD1 C 25.116 0.2 . 327 . 47 LEU CD2 C 23.384 0.2 . 328 . 48 LEU N N 127.022 0.2 . 329 . 48 LEU H H 9.687 0.02 . 330 . 48 LEU CA C 53.002 0.2 . 331 . 48 LEU HA H 5.032 0.02 . 332 . 48 LEU CB C 41.784 0.2 . 333 . 48 LEU HB2 H 2.171 0.02 . 334 . 48 LEU CG C 26.612 0.2 . 335 . 48 LEU HG H 1.965 0.02 . 336 . 48 LEU HD1 H 0.828 0.02 . 337 . 48 LEU HD2 H 0.925 0.02 . 338 . 48 LEU CD1 C 26.168 0.2 . 339 . 48 LEU CD2 C 24.662 0.2 . 340 . 49 ILE N N 123.388 0.2 . 341 . 49 ILE H H 8.629 0.02 . 342 . 49 ILE CA C 61.491 0.2 . 343 . 49 ILE HA H 4.408 0.02 . 344 . 49 ILE CB C 40.078 0.2 . 345 . 49 ILE HB H 1.950 0.02 . 346 . 49 ILE CG1 C 27.006 0.2 . 347 . 49 ILE HG12 H 1.685 0.02 . 348 . 49 ILE HD1 H 0.953 0.02 . 349 . 49 ILE CD1 C 13.934 0.2 . 350 . 50 VAL N N 129.525 0.2 . 351 . 50 VAL H H 9.111 0.02 . 352 . 50 VAL CA C 61.189 0.2 . 353 . 50 VAL HA H 4.490 0.02 . 354 . 50 VAL CB C 34.005 0.2 . 355 . 50 VAL HB H 1.744 0.02 . 356 . 50 VAL HG1 H 0.539 0.02 . 357 . 50 VAL HG2 H 0.831 0.02 . 358 . 51 ASP N N 128.281 0.2 . 359 . 51 ASP H H 9.465 0.02 . 360 . 51 ASP CA C 52.183 0.2 . 361 . 51 ASP HA H 5.408 0.02 . 362 . 51 ASP CB C 43.998 0.2 . 363 . 51 ASP HB2 H 2.435 0.02 . 364 . 51 ASP HB3 H 3.181 0.02 . 365 . 52 SER N N 122.351 0.2 . 366 . 52 SER H H 9.232 0.02 . 367 . 52 SER CA C 59.236 0.2 . 368 . 52 SER HA H 4.924 0.02 . 369 . 52 SER CB C 64.791 0.2 . 370 . 52 SER HB2 H 4.241 0.02 . 371 . 53 ALA N N 126.805 0.2 . 372 . 53 ALA H H 9.451 0.02 . 373 . 53 ALA CA C 52.124 0.2 . 374 . 53 ALA HA H 4.370 0.02 . 375 . 53 ALA HB H 0.945 0.02 . 376 . 53 ALA CB C 17.952 0.2 . 377 . 54 ILE N N 116.443 0.2 . 378 . 54 ILE H H 6.661 0.02 . 379 . 54 ILE CA C 60.049 0.2 . 380 . 54 ILE HA H 4.191 0.02 . 381 . 54 ILE CB C 39.507 0.2 . 382 . 54 ILE HB H 1.753 0.02 . 383 . 54 ILE HG2 H 0.875 0.02 . 384 . 54 ILE CG2 C 17.567 0.2 . 385 . 54 ILE CG1 C 25.746 0.2 . 386 . 54 ILE HG12 H 1.378 0.02 . 387 . 54 ILE HD1 H 0.873 0.02 . 388 . 54 ILE CD1 C 12.764 0.2 . 389 . 55 THR N N 121.619 0.2 . 390 . 55 THR H H 8.351 0.02 . 391 . 55 THR CA C 62.119 0.2 . 392 . 55 THR HA H 4.210 0.02 . 393 . 55 THR CB C 69.033 0.2 . 394 . 55 THR HB H 4.000 0.02 . 395 . 55 THR HG2 H 1.272 0.02 . 396 . 55 THR CG2 C 21.673 0.2 . 397 . 56 ALA N N 131.815 0.2 . 398 . 56 ALA H H 8.889 0.02 . 399 . 56 ALA CA C 52.243 0.2 . 400 . 56 ALA HA H 4.274 0.02 . 401 . 56 ALA HB H 1.285 0.02 . 402 . 56 ALA CB C 19.960 0.2 . 403 . 57 SER N N 119.966 0.2 . 404 . 57 SER H H 9.658 0.02 . 405 . 57 SER CA C 56.023 0.2 . 406 . 57 SER HA H 4.704 0.02 . 407 . 57 SER CB C 65.136 0.2 . 408 . 57 SER HB2 H 3.771 0.02 . 409 . 57 SER HB3 H 3.922 0.02 . 410 . 58 HIS N N 122.138 0.2 . 411 . 58 HIS H H 8.514 0.02 . 412 . 58 HIS CA C 59.561 0.2 . 413 . 58 HIS HA H 4.737 0.02 . 414 . 58 HIS CB C 31.802 0.2 . 415 . 58 HIS HB2 H 1.802 0.02 . 416 . 58 HIS HD2 H 7.125 0.02 . 417 . 58 HIS HE1 H 8.253 0.02 . 418 . 59 GLY N N 118.602 0.2 . 419 . 59 GLY H H 8.899 0.02 . 420 . 59 GLY CA C 44.679 0.2 . 421 . 59 GLY HA2 H 3.269 0.02 . 422 . 59 GLY HA3 H 4.456 0.02 . 423 . 60 ASP N N 121.431 0.2 . 424 . 60 ASP H H 8.109 0.02 . 425 . 60 ASP CA C 55.029 0.2 . 426 . 60 ASP HA H 4.717 0.02 . 427 . 60 ASP CB C 41.213 0.2 . 428 . 60 ASP HB2 H 2.644 0.02 . 429 . 60 ASP HB3 H 2.823 0.02 . 430 . 61 ILE N N 122.049 0.2 . 431 . 61 ILE H H 9.479 0.02 . 432 . 61 ILE CA C 60.322 0.2 . 433 . 61 ILE HA H 4.602 0.02 . 434 . 61 ILE CB C 36.257 0.2 . 435 . 61 ILE HB H 1.985 0.02 . 436 . 61 ILE HG2 H 0.696 0.02 . 437 . 61 ILE CG2 C 18.145 0.2 . 438 . 61 ILE CG1 C 28.325 0.2 . 439 . 61 ILE HG12 H 1.309 0.02 . 440 . 61 ILE HD1 H 0.885 0.02 . 441 . 61 ILE CD1 C 11.848 0.2 . 442 . 62 VAL N N 119.144 0.2 . 443 . 62 VAL H H 9.237 0.02 . 444 . 62 VAL CA C 58.247 0.2 . 445 . 62 VAL HA H 5.362 0.02 . 446 . 62 VAL CB C 35.197 0.2 . 447 . 62 VAL HB H 2.411 0.02 . 448 . 62 VAL HG1 H 0.759 0.02 . 449 . 62 VAL HG2 H 0.950 0.02 . 450 . 62 VAL CG1 C 17.872 0.2 . 451 . 62 VAL CG2 C 22.597 0.2 . 452 . 63 ILE N N 117.472 0.2 . 453 . 63 ILE H H 8.024 0.02 . 454 . 63 ILE CA C 58.505 0.2 . 455 . 63 ILE HA H 5.147 0.02 . 456 . 63 ILE CB C 36.910 0.2 . 457 . 63 ILE HB H 1.914 0.02 . 458 . 63 ILE HG2 H 0.913 0.02 . 459 . 63 ILE CG2 C 17.058 0.2 . 460 . 63 ILE CG1 C 28.057 0.2 . 461 . 63 ILE HG12 H 1.313 0.02 . 462 . 63 ILE HD1 H 0.742 0.02 . 463 . 63 ILE CD1 C 12.237 0.2 . 464 . 64 ALA N N 130.545 0.2 . 465 . 64 ALA H H 9.138 0.02 . 466 . 64 ALA CA C 49.719 0.2 . 467 . 64 ALA HA H 5.381 0.02 . 468 . 64 ALA HB H 1.238 0.02 . 469 . 64 ALA CB C 23.133 0.2 . 470 . 65 ALA N N 124.201 0.2 . 471 . 65 ALA H H 8.681 0.02 . 472 . 65 ALA CA C 50.595 0.2 . 473 . 65 ALA HA H 4.935 0.02 . 474 . 65 ALA HB H 1.016 0.02 . 475 . 65 ALA CB C 19.946 0.2 . 476 . 66 VAL N N 123.520 0.2 . 477 . 66 VAL H H 8.592 0.02 . 478 . 66 VAL CA C 60.931 0.2 . 479 . 66 VAL HA H 5.059 0.02 . 480 . 66 VAL CB C 33.473 0.2 . 481 . 66 VAL HB H 1.678 0.02 . 482 . 66 VAL HG1 H 0.901 0.02 . 483 . 66 VAL CG1 C 19.938 0.2 . 484 . 67 ASP N N 129.313 0.2 . 485 . 67 ASP H H 9.422 0.02 . 486 . 67 ASP CA C 55.306 0.2 . 487 . 67 ASP HA H 4.359 0.02 . 488 . 67 ASP CB C 39.362 0.2 . 489 . 67 ASP HB2 H 2.678 0.02 . 490 . 67 ASP HB3 H 3.027 0.02 . 491 . 68 GLY N N 103.847 0.2 . 492 . 68 GLY H H 8.552 0.02 . 493 . 68 GLY CA C 44.993 0.2 . 494 . 68 GLY HA2 H 3.514 0.02 . 495 . 68 GLY HA3 H 4.169 0.02 . 496 . 69 GLU N N 120.688 0.2 . 497 . 69 GLU H H 7.691 0.02 . 498 . 69 GLU CA C 54.121 0.2 . 499 . 69 GLU HA H 4.641 0.02 . 500 . 69 GLU CB C 31.856 0.2 . 501 . 69 GLU HB2 H 1.989 0.02 . 502 . 69 GLU HB3 H 2.067 0.02 . 503 . 70 PHE N N 124.434 0.2 . 504 . 70 PHE H H 8.687 0.02 . 505 . 70 PHE CA C 57.247 0.2 . 506 . 70 PHE HA H 5.120 0.02 . 507 . 70 PHE CB C 38.932 0.2 . 508 . 70 PHE HB2 H 2.680 0.02 . 509 . 70 PHE HB3 H 2.795 0.02 . 510 . 70 PHE HD1 H 6.959 0.02 . 511 . 71 THR N N 118.714 0.2 . 512 . 71 THR H H 9.087 0.02 . 513 . 71 THR CA C 59.866 0.2 . 514 . 71 THR HA H 4.743 0.02 . 515 . 71 THR CB C 30.156 0.2 . 516 . 71 THR HB H 4.100 0.02 . 517 . 71 THR HG2 H 1.070 0.02 . 518 . 71 THR CG2 C 19.209 0.2 . 519 . 72 VAL N N 126.615 0.2 . 520 . 72 VAL H H 7.979 0.02 . 521 . 72 VAL CA C 60.171 0.2 . 522 . 72 VAL HA H 5.275 0.02 . 523 . 72 VAL CB C 31.889 0.2 . 524 . 72 VAL HB H 2.045 0.02 . 525 . 72 VAL CG1 C 20.864 0.2 . 526 . 72 VAL HG1 H 0.874 0.02 . 527 . 73 LYS N N 126.072 0.2 . 528 . 73 LYS H H 8.748 0.02 . 529 . 73 LYS CA C 52.384 0.2 . 530 . 73 LYS HA H 5.266 0.02 . 531 . 73 LYS CB C 40.178 0.2 . 532 . 73 LYS HG2 H 0.854 0.02 . 533 . 73 LYS HE2 H 2.990 0.02 . 534 . 74 LYS N N 122.015 0.2 . 535 . 74 LYS H H 8.844 0.02 . 536 . 74 LYS CA C 55.512 0.2 . 537 . 74 LYS HA H 4.990 0.02 . 538 . 74 LYS CB C 32.866 0.2 . 539 . 75 LEU N N 129.951 0.2 . 540 . 75 LEU H H 9.428 0.02 . 541 . 75 LEU CA C 54.504 0.2 . 542 . 75 LEU HA H 4.686 0.02 . 543 . 75 LEU CB C 43.493 0.2 . 544 . 75 LEU HB2 H 2.203 0.02 . 545 . 75 LEU CG C 27.479 0.2 . 546 . 75 LEU HG H 1.244 0.02 . 547 . 75 LEU CD1 C 26.157 0.2 . 548 . 75 LEU HD1 H 0.809 0.02 . 549 . 76 GLN N N 130.513 0.2 . 550 . 76 GLN H H 9.183 0.02 . 551 . 76 GLN CA C 53.930 0.2 . 552 . 76 GLN HA H 4.961 0.02 . 553 . 76 GLN CB C 32.148 0.2 . 554 . 76 GLN HG2 H 2.192 0.02 . 555 . 77 LEU N N 125.549 0.2 . 556 . 77 LEU H H 11.110 0.02 . 557 . 77 LEU CA C 54.989 0.2 . 558 . 77 LEU HA H 4.866 0.02 . 559 . 77 LEU CB C 44.797 0.2 . 560 . 77 LEU HB2 H 1.785 0.02 . 561 . 77 LEU CG C 28.175 0.2 . 562 . 77 LEU HG H 1.556 0.02 . 563 . 77 LEU HD1 H 1.089 0.02 . 564 . 77 LEU CD1 C 25.596 0.2 . 565 . 78 ARG N N 116.446 0.2 . 566 . 78 ARG H H 7.398 0.02 . 567 . 78 ARG CA C 52.386 0.2 . 568 . 78 ARG HA H 4.510 0.02 . 569 . 78 ARG CB C 30.944 0.2 . 570 . 78 ARG HB2 H 1.738 0.02 . 571 . 78 ARG CG C 31.294 0.2 . 572 . 78 ARG HG2 H 1.453 0.02 . 573 . 78 ARG CD C 41.414 0.2 . 574 . 78 ARG HD2 H 3.033 0.02 . 575 . 79 PRO HB2 H 2.124 0.02 . 576 . 79 PRO HD2 H 3.588 0.02 . 577 . 79 PRO HD3 H 3.848 0.02 . 578 . 80 THR N N 113.008 0.2 . 579 . 80 THR H H 7.089 0.02 . 580 . 80 THR CA C 59.127 0.2 . 581 . 80 THR HA H 4.538 0.02 . 582 . 80 THR CB C 71.009 0.2 . 583 . 80 THR HB H 4.193 0.02 . 584 . 80 THR HG2 H 1.190 0.02 . 585 . 80 THR CG2 C 21.845 0.2 . 586 . 81 VAL N N 123.482 0.2 . 587 . 81 VAL H H 8.538 0.02 . 588 . 81 VAL CA C 62.199 0.2 . 589 . 81 VAL HA H 4.569 0.02 . 590 . 81 VAL HB H 2.229 0.02 . 591 . 82 GLN N N 125.452 0.2 . 592 . 82 GLN H H 9.155 0.02 . 593 . 82 GLN CA C 53.639 0.2 . 594 . 82 GLN HA H 4.875 0.02 . 595 . 82 GLN CB C 35.580 0.2 . 596 . 82 GLN HB2 H 2.233 0.02 . 597 . 82 GLN CG C 33.149 0.2 . 598 . 83 LEU N N 120.369 0.2 . 599 . 83 LEU H H 8.744 0.02 . 600 . 83 LEU CA C 52.574 0.2 . 601 . 83 LEU HA H 5.089 0.02 . 602 . 83 LEU CB C 42.354 0.2 . 603 . 83 LEU HB2 H 1.849 0.02 . 604 . 83 LEU CG C 25.904 0.2 . 605 . 83 LEU HG H 1.504 0.02 . 606 . 83 LEU HD1 H 0.686 0.02 . 607 . 83 LEU HD2 H 0.945 0.02 . 608 . 83 LEU CD1 C 26.526 0.2 . 609 . 84 ILE N N 125.460 0.2 . 610 . 84 ILE H H 9.922 0.02 . 611 . 84 ILE CA C 58.034 0.2 . 612 . 84 ILE HA H 4.711 0.02 . 613 . 84 ILE CB C 32.361 0.2 . 614 . 84 ILE HB H 2.001 0.02 . 615 . 84 ILE HG2 H 0.953 0.02 . 616 . 84 ILE CG2 C 16.701 0.2 . 617 . 84 ILE CG1 C 27.021 0.2 . 618 . 84 ILE HG12 H 1.148 0.02 . 619 . 84 ILE HD1 H 0.808 0.02 . 620 . 84 ILE CD1 C 12.563 0.2 . 621 . 85 PRO CA C 61.483 0.2 . 622 . 85 PRO CB C 31.692 0.2 . 623 . 86 MET N N 125.887 0.2 . 624 . 86 MET H H 8.604 0.02 . 625 . 86 MET CA C 54.427 0.2 . 626 . 86 MET HA H 4.991 0.02 . 627 . 86 MET CB C 33.062 0.2 . 628 . 86 MET HB2 H 1.781 0.02 . 629 . 86 MET CG C 31.914 0.2 . 630 . 86 MET HG2 H 2.415 0.02 . 631 . 86 MET HE H 2.021 0.02 . 632 . 86 MET CE C 17.714 0.2 . 633 . 87 ASN N N 117.469 0.2 . 634 . 87 ASN H H 6.999 0.02 . 635 . 87 ASN CA C 53.961 0.2 . 636 . 87 ASN HA H 4.716 0.02 . 637 . 87 ASN CB C 38.696 0.2 . 638 . 87 ASN HB2 H 3.310 0.02 . 639 . 87 ASN HB3 H 2.804 0.02 . 640 . 88 SER N N 123.701 0.2 . 641 . 88 SER H H 9.272 0.02 . 642 . 88 SER CA C 60.688 0.2 . 643 . 88 SER HA H 4.670 0.02 . 644 . 88 SER CB C 62.795 0.2 . 645 . 88 SER HB2 H 4.127 0.02 . 646 . 89 ALA N N 124.184 0.2 . 647 . 89 ALA H H 8.691 0.02 . 648 . 89 ALA CA C 52.688 0.2 . 649 . 89 ALA HA H 4.298 0.02 . 650 . 89 ALA HB H 1.182 0.02 . 651 . 89 ALA CB C 18.245 0.2 . 652 . 90 TYR N N 118.929 0.2 . 653 . 90 TYR H H 8.021 0.02 . 654 . 90 TYR CA C 56.212 0.2 . 655 . 90 TYR HA H 4.850 0.02 . 656 . 90 TYR CB C 40.781 0.2 . 657 . 90 TYR HB2 H 3.311 0.02 . 658 . 90 TYR HB3 H 2.881 0.02 . 659 . 90 TYR HD1 H 7.178 0.02 . 660 . 90 TYR HE1 H 6.889 0.02 . 661 . 91 SER N N 117.256 0.2 . 662 . 91 SER H H 8.693 0.02 . 663 . 91 SER CA C 56.280 0.2 . 664 . 91 SER HA H 5.120 0.02 . 665 . 91 SER CB C 63.808 0.2 . 666 . 91 SER HB2 H 3.849 0.02 . 667 . 91 SER HB3 H 4.038 0.02 . 668 . 92 PRO CA C 62.807 0.2 . 669 . 92 PRO HA H 4.470 0.02 . 670 . 92 PRO CB C 32.756 0.2 . 671 . 93 ILE N N 123.791 0.2 . 672 . 93 ILE H H 8.765 0.02 . 673 . 93 ILE CA C 60.148 0.2 . 674 . 93 ILE HA H 4.786 0.02 . 675 . 93 ILE CB C 40.161 0.2 . 676 . 93 ILE HB H 1.886 0.02 . 677 . 93 ILE HG2 H 0.940 0.02 . 678 . 93 ILE CG2 C 17.123 0.2 . 679 . 93 ILE CG1 C 27.188 0.2 . 680 . 93 ILE HG12 H 1.690 0.02 . 681 . 93 ILE HD1 H 1.204 0.02 . 682 . 93 ILE CD1 C 14.209 0.2 . 683 . 94 THR N N 124.731 0.2 . 684 . 94 THR H H 8.847 0.02 . 685 . 94 THR CA C 63.140 0.2 . 686 . 94 THR HA H 4.464 0.02 . 687 . 94 THR CB C 69.059 0.2 . 688 . 94 THR HB H 4.151 0.02 . 689 . 94 THR HG2 H 1.234 0.02 . 690 . 94 THR CG2 C 21.747 0.2 . 691 . 95 ILE N N 129.306 0.2 . 692 . 95 ILE H H 8.126 0.02 . 693 . 95 ILE CA C 58.144 0.2 . 694 . 95 ILE HA H 4.426 0.02 . 695 . 95 ILE CB C 37.012 0.2 . 696 . 95 ILE HB H 1.913 0.02 . 697 . 95 ILE HG2 H 0.878 0.02 . 698 . 95 ILE CG2 C 17.099 0.2 . 699 . 95 ILE CG1 C 26.781 0.2 . 700 . 95 ILE HG12 H 1.225 0.02 . 701 . 95 ILE HD1 H 0.724 0.02 . 702 . 95 ILE CD1 C 9.868 0.2 . 703 . 96 SER N N 124.635 0.2 . 704 . 96 SER H H 9.123 0.02 . 705 . 96 SER CA C 59.607 0.2 . 706 . 96 SER HA H 4.573 0.02 . 707 . 96 SER CB C 63.387 0.2 . 708 . 96 SER HB2 H 4.084 0.02 . 709 . 97 SER N N 115.500 0.2 . 710 . 97 SER H H 8.183 0.02 . 711 . 97 SER CA C 59.319 0.2 . 712 . 97 SER HA H 4.500 0.02 . 713 . 97 SER CB C 63.643 0.2 . 714 . 97 SER HB2 H 4.068 0.02 . 715 . 98 GLU N N 122.011 0.2 . 716 . 98 GLU H H 8.839 0.02 . 717 . 98 GLU CA C 57.778 0.2 . 718 . 98 GLU HA H 4.224 0.02 . 719 . 98 GLU CB C 29.386 0.2 . 720 . 98 GLU HB2 H 2.005 0.02 . 721 . 98 GLU HB3 H 2.246 0.02 . 722 . 98 GLU CG C 36.456 0.2 . 723 . 98 GLU HG2 H 2.343 0.02 . 724 . 99 ASP N N 119.855 0.2 . 725 . 99 ASP H H 8.004 0.02 . 726 . 99 ASP CA C 54.404 0.2 . 727 . 99 ASP HA H 4.793 0.02 . 728 . 99 ASP CB C 41.790 0.2 . 729 . 99 ASP HB2 H 2.782 0.02 . 730 . 100 THR N N 112.801 0.2 . 731 . 100 THR H H 8.078 0.02 . 732 . 100 THR CA C 61.394 0.2 . 733 . 100 THR HA H 4.451 0.02 . 734 . 100 THR CB C 69.521 0.2 . 735 . 100 THR HB H 4.276 0.02 . 736 . 100 THR HG2 H 1.233 0.02 . 737 . 100 THR CG2 C 21.634 0.2 . 738 . 101 LEU N N 126.618 0.2 . 739 . 101 LEU H H 7.975 0.02 . 740 . 101 LEU CA C 54.389 0.2 . 741 . 101 LEU HA H 4.475 0.02 . 742 . 101 LEU CB C 42.900 0.2 . 743 . 101 LEU HB2 H 1.911 0.02 . 744 . 101 LEU CG C 26.376 0.2 . 745 . 101 LEU HG H 1.423 0.02 . 746 . 101 LEU CD1 C 23.670 0.2 . 747 . 101 LEU HD1 H 0.811 0.02 . 748 . 102 ASP N N 130.455 0.2 . 749 . 102 ASP H H 9.179 0.02 . 750 . 102 ASP CA C 52.828 0.2 . 751 . 102 ASP HA H 4.949 0.02 . 752 . 102 ASP CB C 41.320 0.2 . 753 . 102 ASP HB2 H 2.902 0.02 . 754 . 102 ASP HB3 H 2.520 0.02 . 755 . 103 VAL N N 124.192 0.2 . 756 . 103 VAL H H 8.421 0.02 . 757 . 103 VAL CA C 62.221 0.2 . 758 . 103 VAL HA H 4.241 0.02 . 759 . 103 VAL CB C 32.779 0.2 . 760 . 103 VAL HB H 2.103 0.02 . 761 . 103 VAL CG1 C 20.950 0.2 . 762 . 103 VAL HG1 H 0.909 0.02 . 763 . 104 PHE N N 129.704 0.2 . 764 . 104 PHE H H 9.225 0.02 . 765 . 104 PHE CA C 58.602 0.2 . 766 . 104 PHE HA H 4.606 0.02 . 767 . 104 PHE CB C 39.772 0.2 . 768 . 104 PHE HB2 H 2.836 0.02 . 769 . 104 PHE HD1 H 6.925 0.02 . 770 . 105 GLY N N 103.554 0.2 . 771 . 105 GLY H H 7.399 0.02 . 772 . 105 GLY CA C 44.795 0.2 . 773 . 105 GLY HA2 H 3.616 0.02 . 774 . 105 GLY HA3 H 4.421 0.02 . 775 . 106 VAL N N 120.604 0.2 . 776 . 106 VAL H H 7.882 0.02 . 777 . 106 VAL CA C 61.172 0.2 . 778 . 106 VAL HA H 4.318 0.02 . 779 . 106 VAL CB C 33.980 0.2 . 780 . 106 VAL HB H 1.942 0.02 . 781 . 106 VAL CG1 C 20.805 0.2 . 782 . 106 VAL HG1 H 0.903 0.02 . 783 . 107 VAL N N 128.884 0.2 . 784 . 107 VAL H H 9.250 0.02 . 785 . 107 VAL CA C 63.154 0.2 . 786 . 107 VAL HA H 5.381 0.02 . 787 . 107 VAL HB H 1.973 0.02 . 788 . 107 VAL CG1 C 18.062 0.2 . 789 . 107 VAL HG1 H 0.739 0.02 . 790 . 108 ILE N N 121.306 0.2 . 791 . 108 ILE H H 8.886 0.02 . 792 . 108 ILE CA C 62.439 0.2 . 793 . 108 ILE HA H 4.167 0.02 . 794 . 108 ILE CB C 39.276 0.2 . 795 . 108 ILE HB H 1.687 0.02 . 796 . 108 ILE HG2 H 0.843 0.02 . 797 . 108 ILE CG2 C 17.580 0.2 . 798 . 108 ILE HG12 H 1.182 0.02 . 799 . 108 ILE HD1 H 0.861 0.02 . 800 . 108 ILE CD1 C 13.287 0.2 . 801 . 109 HIS N N 119.021 0.2 . 802 . 109 HIS H H 7.692 0.02 . 803 . 109 HIS CA C 55.522 0.2 . 804 . 109 HIS HA H 5.740 0.02 . 805 . 109 HIS HB2 H 3.025 0.02 . 806 . 109 HIS HD1 H 6.866 0.02 . 807 . 109 HIS HE1 H 7.924 0.02 . 808 . 110 VAL N N 120.694 0.2 . 809 . 110 VAL H H 8.571 0.02 . 810 . 111 VAL N N 128.281 0.2 . 811 . 111 VAL H H 9.883 0.02 . 812 . 111 VAL CA C 60.595 0.2 . 813 . 111 VAL HA H 5.048 0.02 . 814 . 111 VAL CB C 36.302 0.2 . 815 . 111 VAL HB H 1.971 0.02 . 816 . 111 VAL HG1 H 0.886 0.02 . 817 . 111 VAL HG2 H 1.030 0.02 . 818 . 111 VAL CG1 C 22.213 0.2 . 819 . 111 VAL CG2 C 20.912 0.2 . 820 . 112 LYS N N 129.317 0.2 . 821 . 112 LYS H H 9.590 0.02 . 822 . 112 LYS CA C 54.296 0.2 . 823 . 112 LYS CB C 34.385 0.2 . 824 . 113 ALA N N 128.993 0.2 . 825 . 113 ALA H H 8.988 0.02 . 826 . 113 ALA CA C 52.037 0.2 . 827 . 113 ALA HA H 5.200 0.02 . 828 . 113 ALA HB H 1.676 0.02 . 829 . 113 ALA CB C 19.087 0.2 . 830 . 114 MET N N 120.910 0.2 . 831 . 114 MET H H 7.892 0.02 . 832 . 114 MET CA C 53.602 0.2 . 833 . 114 MET CB C 32.832 0.2 . 834 . 115 ARG N N 126.591 0.2 . 835 . 115 ARG H H 7.746 0.02 . 836 . 115 ARG CA C 57.145 0.2 . 837 . 115 ARG HA H 4.279 0.02 . 838 . 115 ARG CB C 32.991 0.2 . 839 . 115 ARG HB2 H 1.925 0.02 . 840 . 115 ARG CG C 27.643 0.2 . 841 . 115 ARG HG2 H 1.642 0.02 . 842 . 115 ARG CD C 43.105 0.2 . 843 . 115 ARG HD2 H 3.204 0.02 . stop_ save_