data_19800 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the PrgK first periplasmic domain ; _BMRB_accession_number 19800 _BMRB_flat_file_name bmr19800.str _Entry_type original _Submission_date 2014-02-14 _Accession_date 2014-02-14 _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 Bergeron Julien . . 2 McIntosh Lawrence . . 3 Strynadka Natalie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 328 "13C chemical shifts" 250 "15N chemical shifts" 57 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-10-27 original author . stop_ _Original_release_date 2014-10-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The structure of PrgK reveals structural rearrangements upon assembly of the type III secretion system basal body.' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bergeron Julien . . 2 Worrall Liam . . 3 De Soumya . . 4 Sgourakis Nikolaos . . 5 Cheung Adrienne . . 6 Lameignere Emilie . . 7 Okon Mark . . 8 Baker David . . 9 McIntosh Lawrence . . 10 Strynadka Natalie . . stop_ _Journal_abbreviation Structure _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PrgK first periplasmic domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PrgK first periplasmic domain' $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 6532.430 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; KDKDLLKGLDQEQANEVIAV LQMHNIEANKIDSGKLGYSI TVAEPDFTAAVYWIKTYQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 19 LYS 2 20 ASP 3 21 LYS 4 22 ASP 5 23 LEU 6 24 LEU 7 25 LYS 8 26 GLY 9 27 LEU 10 28 ASP 11 29 GLN 12 30 GLU 13 31 GLN 14 32 ALA 15 33 ASN 16 34 GLU 17 35 VAL 18 36 ILE 19 37 ALA 20 38 VAL 21 39 LEU 22 40 GLN 23 41 MET 24 42 HIS 25 43 ASN 26 44 ILE 27 45 GLU 28 46 ALA 29 47 ASN 30 48 LYS 31 49 ILE 32 50 ASP 33 51 SER 34 52 GLY 35 53 LYS 36 54 LEU 37 55 GLY 38 56 TYR 39 57 SER 40 58 ILE 41 59 THR 42 60 VAL 43 61 ALA 44 62 GLU 45 63 PRO 46 64 ASP 47 65 PHE 48 66 THR 49 67 ALA 50 68 ALA 51 69 VAL 52 70 TYR 53 71 TRP 54 72 ILE 55 73 LYS 56 74 THR 57 75 TYR 58 76 GLN 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 2MKY "Structure Of The Prgk First Periplasmic Domain" 100.00 58 100.00 100.00 3.98e-33 PDB 2Y9J "Three-Dimensional Model Of Salmonella's Needle Complex At Subnanometer Resolution" 96.55 170 100.00 100.00 2.14e-31 PDB 3J6D "Model Of The Prgh-prgk Periplasmic Rings" 100.00 252 100.00 100.00 7.29e-32 PDB 4W4M "Crystal Structure Of Prgk 19-92" 100.00 78 100.00 100.00 3.33e-33 DBJ BAJ37863 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 100.00 252 100.00 100.00 7.29e-32 DBJ BAP08776 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 100.00 252 100.00 100.00 7.29e-32 EMBL CAD05978 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 252 100.00 100.00 7.21e-32 EMBL CAR34291 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 100.00 252 100.00 100.00 7.29e-32 EMBL CAR38583 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 100.00 252 100.00 100.00 7.29e-32 EMBL CAR60779 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" 100.00 252 100.00 100.00 7.29e-32 EMBL CBG25840 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 100.00 252 100.00 100.00 7.29e-32 GB AAB60191 "PrgK protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 252 100.00 100.00 7.29e-32 GB AAL21751 "cell invasion protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 252 100.00 100.00 7.29e-32 GB AAO70334 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 100.00 252 100.00 100.00 7.21e-32 GB AAV78586 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]" 100.00 252 100.00 100.00 7.29e-32 GB AAX66709 "cell invasion protein; lipoprotein, may link inner and outer membranes [Salmonella enterica subsp. enterica serovar Choleraesui" 100.00 252 100.00 100.00 7.29e-32 PIR AC0849 "pathogenicity 1 island effector protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 252 100.00 100.00 7.21e-32 REF NP_457265 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 252 100.00 100.00 7.21e-32 REF NP_461792 "secretion system lipoprotein PrgK [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 252 100.00 100.00 7.29e-32 REF WP_000001630 "hypothetical protein, partial [Salmonella enterica]" 98.28 233 100.00 100.00 2.40e-31 REF WP_000621236 "hypothetical protein [Salmonella enterica]" 100.00 252 100.00 100.00 8.92e-32 REF WP_000621237 "hypothetical protein [Salmonella enterica]" 100.00 252 100.00 100.00 7.77e-32 SP P41786 "RecName: Full=Lipoprotein PrgK; Flags: Precursor" 100.00 252 100.00 100.00 7.29e-32 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'Salmonella typhimurium' 90371 Bacteria . Salmonella typhimurium 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 $entity 'recombinant technology' . Escherichia coli . pET28a 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 $entity 1 mM '[U-100% 13C; U-100% 15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' HEPES 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'G??ntert P.' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '25 mM HEPES pH 6.8, 10 % D2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 6.8 . pH pressure 1 . atm temperature 273 . 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 TSP C 13 'methyl protons' ppm . internal direct . . . 1 TSP H 1 'methyl protons' ppm . internal direct . . . 1 TSP N 15 'methyl protons' ppm . internal direct . . . 1 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 '3D 1H-13C NOESY aliphatic' '3D 1H-15N NOESY' '3D 1H-13C NOESY' 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 'PrgK first periplasmic domain' _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 LYS H H 8.508 0.003 . 2 19 1 LYS HA H 4.318 0.003 . 3 19 1 LYS HB2 H 1.773 0.032 . 4 19 1 LYS HB3 H 1.773 0.032 . 5 19 1 LYS HG2 H 1.477 0 . 6 19 1 LYS HG3 H 1.409 0.008 . 7 19 1 LYS HD2 H 1.668 0.011 . 8 19 1 LYS HD3 H 1.668 0.011 . 9 19 1 LYS HE2 H 2.98 0.01 . 10 19 1 LYS HE3 H 2.98 0.01 . 11 19 1 LYS C C 176.021 0 . 12 19 1 LYS CA C 55.918 0.052 . 13 19 1 LYS CB C 32.527 0.064 . 14 19 1 LYS CG C 24.735 0.031 . 15 19 1 LYS CD C 29.039 0.051 . 16 19 1 LYS CE C 42.052 0.037 . 17 19 1 LYS N N 122.797 0.028 . 18 20 2 ASP H H 8.066 0.005 . 19 20 2 ASP HA H 4.824 0.005 . 20 20 2 ASP HB2 H 2.428 0.003 . 21 20 2 ASP HB3 H 2.576 0.002 . 22 20 2 ASP C C 176.378 0 . 23 20 2 ASP CA C 54.063 0.009 . 24 20 2 ASP CB C 41.753 0.005 . 25 20 2 ASP N N 121.855 0.045 . 26 21 3 LYS H H 9.136 0.003 . 27 21 3 LYS HA H 4.493 0.004 . 28 21 3 LYS HB2 H 1.51 0.004 . 29 21 3 LYS HB3 H 1.51 0.004 . 30 21 3 LYS HG2 H 1.154 0.003 . 31 21 3 LYS HG3 H 1.184 0.006 . 32 21 3 LYS HD2 H 1.139 0 . 33 21 3 LYS HD3 H 1.355 0.001 . 34 21 3 LYS HE2 H 2.15 0 . 35 21 3 LYS HE3 H 2.284 0 . 36 21 3 LYS C C 175.887 0 . 37 21 3 LYS CA C 54.395 0.027 . 38 21 3 LYS CB C 35.006 0.029 . 39 21 3 LYS CG C 24.414 0.068 . 40 21 3 LYS CD C 28.662 0.037 . 41 21 3 LYS N N 121.556 0.011 . 42 22 4 ASP H H 8.429 0.003 . 43 22 4 ASP HA H 4.558 0.003 . 44 22 4 ASP HB2 H 2.354 0.001 . 45 22 4 ASP HB3 H 2.543 0.027 . 46 22 4 ASP C C 175.402 0 . 47 22 4 ASP CA C 55.514 0.152 . 48 22 4 ASP CB C 40.854 0.094 . 49 22 4 ASP N N 123.097 0.023 . 50 23 5 LEU H H 9.313 0.003 . 51 23 5 LEU HA H 4.68 0.003 . 52 23 5 LEU HB2 H 1.716 0.001 . 53 23 5 LEU HB3 H 1.31 0.002 . 54 23 5 LEU HG H 1.475 0 . 55 23 5 LEU HD1 H 0.659 0.002 . 56 23 5 LEU HD2 H 0.712 0.002 . 57 23 5 LEU C C 176.338 0 . 58 23 5 LEU CA C 56.204 0.059 . 59 23 5 LEU CB C 45.211 0.023 . 60 23 5 LEU CD1 C 24.805 0.057 . 61 23 5 LEU CD2 C 27.408 0.077 . 62 23 5 LEU N N 126.265 0.013 . 63 24 6 LEU H H 7.346 0.002 . 64 24 6 LEU HA H 4.789 0 . 65 24 6 LEU HB2 H 1.406 0.002 . 66 24 6 LEU HB3 H 1.551 0.007 . 67 24 6 LEU HD1 H 0.902 0.008 . 68 24 6 LEU HD2 H 1.034 0.007 . 69 24 6 LEU C C 174.976 0 . 70 24 6 LEU CA C 53.674 0.035 . 71 24 6 LEU CB C 49.345 0.018 . 72 24 6 LEU CG C 23.722 0 . 73 24 6 LEU CD1 C 27.484 0.068 . 74 24 6 LEU CD2 C 23.674 0.094 . 75 24 6 LEU N N 114.484 0.013 . 76 25 7 LYS H H 8.516 0.003 . 77 25 7 LYS HA H 4.994 0.002 . 78 25 7 LYS HB2 H 1.883 0.002 . 79 25 7 LYS HB3 H 1.664 0.013 . 80 25 7 LYS HG2 H 1.32 0.004 . 81 25 7 LYS HG3 H 1.416 0.004 . 82 25 7 LYS HE2 H 2.913 0.001 . 83 25 7 LYS HE3 H 2.913 0.001 . 84 25 7 LYS C C 176.242 0 . 85 25 7 LYS CA C 55.21 0.048 . 86 25 7 LYS CB C 35.992 0.021 . 87 25 7 LYS CG C 23.95 0.029 . 88 25 7 LYS CD C 29.048 0 . 89 25 7 LYS CE C 41.943 0.026 . 90 25 7 LYS N N 118.529 0.008 . 91 26 8 GLY H H 8.265 0.002 . 92 26 8 GLY HA2 H 3.957 0.002 . 93 26 8 GLY HA3 H 4.188 0.002 . 94 26 8 GLY C C 176.034 0 . 95 26 8 GLY CA C 46.394 0.02 . 96 26 8 GLY N N 107.756 0.014 . 97 27 9 LEU H H 8.884 0.004 . 98 27 9 LEU HA H 4.601 0.003 . 99 27 9 LEU HB2 H 1.754 0 . 100 27 9 LEU HB3 H 1.738 0.004 . 101 27 9 LEU HG H 1.535 0.005 . 102 27 9 LEU HD1 H 0.737 0.003 . 103 27 9 LEU HD2 H 0.657 0.003 . 104 27 9 LEU C C 179.874 0 . 105 27 9 LEU CA C 54.325 0.006 . 106 27 9 LEU CB C 43.622 0.014 . 107 27 9 LEU CG C 26.485 0 . 108 27 9 LEU CD1 C 21.913 0.137 . 109 27 9 LEU CD2 C 26.366 0.082 . 110 27 9 LEU N N 120.147 0.018 . 111 28 10 ASP H H 8.555 0.004 . 112 28 10 ASP HA H 5.096 0.003 . 113 28 10 ASP HB2 H 2.75 0.006 . 114 28 10 ASP HB3 H 3.185 0.002 . 115 28 10 ASP C C 177.406 0 . 116 28 10 ASP CA C 52.835 0.17 . 117 28 10 ASP CB C 41.18 0.01 . 118 28 10 ASP N N 119.966 0.01 . 119 29 11 GLN H H 8.705 0.002 . 120 29 11 GLN HA H 2.969 0.002 . 121 29 11 GLN HB2 H 1.962 0.005 . 122 29 11 GLN HB3 H 1.962 0.005 . 123 29 11 GLN HG2 H 2.137 0.002 . 124 29 11 GLN HG3 H 1.81 0.003 . 125 29 11 GLN C C 178.379 0 . 126 29 11 GLN CA C 59.978 0.008 . 127 29 11 GLN CB C 28.897 0.084 . 128 29 11 GLN CG C 34.174 0.136 . 129 29 11 GLN N N 118.219 0.021 . 130 30 12 GLU H H 8.135 0.005 . 131 30 12 GLU HA H 3.986 0.002 . 132 30 12 GLU HB2 H 2.054 0.013 . 133 30 12 GLU HB3 H 2.054 0.013 . 134 30 12 GLU HG2 H 2.303 0.003 . 135 30 12 GLU HG3 H 2.303 0.003 . 136 30 12 GLU C C 182.812 0 . 137 30 12 GLU CA C 59.73 0.05 . 138 30 12 GLU CB C 28.936 0.047 . 139 30 12 GLU CG C 36.681 0.041 . 140 30 12 GLU N N 118.429 0.008 . 141 31 13 GLN H H 8.742 0.003 . 142 31 13 GLN HA H 4.068 0.003 . 143 31 13 GLN HB2 H 1.894 0.003 . 144 31 13 GLN HB3 H 2.321 0.002 . 145 31 13 GLN HG2 H 2.403 0.001 . 146 31 13 GLN HG3 H 2.799 0 . 147 31 13 GLN C C 180.864 0 . 148 31 13 GLN CA C 58.612 0.023 . 149 31 13 GLN CB C 29.844 0.083 . 150 31 13 GLN CG C 34.424 0.01 . 151 31 13 GLN N N 120.672 0.005 . 152 32 14 ALA H H 8.408 0.003 . 153 32 14 ALA HA H 3.771 0.002 . 154 32 14 ALA HB H 1.033 0.004 . 155 32 14 ALA C C 180.339 0 . 156 32 14 ALA CA C 55.122 0.04 . 157 32 14 ALA CB C 17.289 0.077 . 158 32 14 ALA N N 120.2 0.011 . 159 33 15 ASN H H 8.077 0.003 . 160 33 15 ASN HA H 4.292 0.002 . 161 33 15 ASN HB2 H 2.705 0.002 . 162 33 15 ASN HB3 H 2.854 0.016 . 163 33 15 ASN C C 180.713 0 . 164 33 15 ASN CA C 55.479 0.015 . 165 33 15 ASN CB C 37.104 0.038 . 166 33 15 ASN N N 115.507 0.017 . 167 34 16 GLU H H 7.973 0.003 . 168 34 16 GLU HA H 4.083 0.002 . 169 34 16 GLU HB2 H 2.188 0.015 . 170 34 16 GLU HB3 H 2.188 0.015 . 171 34 16 GLU HG2 H 2.386 0.001 . 172 34 16 GLU HG3 H 2.386 0.001 . 173 34 16 GLU C C 180.367 0 . 174 34 16 GLU CA C 59.486 0.035 . 175 34 16 GLU CB C 29.37 0.031 . 176 34 16 GLU CG C 36.07 0.014 . 177 34 16 GLU N N 122.826 0.01 . 178 35 17 VAL H H 8.025 0.002 . 179 35 17 VAL HA H 3.373 0.002 . 180 35 17 VAL HB H 1.969 0.002 . 181 35 17 VAL HG1 H 0.742 0.01 . 182 35 17 VAL HG2 H 0.745 0.006 . 183 35 17 VAL C C 179.502 0 . 184 35 17 VAL CA C 66.809 0.041 . 185 35 17 VAL CB C 31 0 . 186 35 17 VAL CG1 C 22.474 0.029 . 187 35 17 VAL CG2 C 22.183 0.013 . 188 35 17 VAL N N 119.909 0.007 . 189 36 18 ILE H H 8.031 0.004 . 190 36 18 ILE HA H 3.514 0.002 . 191 36 18 ILE HB H 2.011 0.001 . 192 36 18 ILE HG12 H 1.524 0.001 . 193 36 18 ILE HG13 H 1.352 0.002 . 194 36 18 ILE HG2 H 0.902 0.002 . 195 36 18 ILE HD1 H 0.695 0.003 . 196 36 18 ILE C C 180.436 0 . 197 36 18 ILE CA C 64.355 0.039 . 198 36 18 ILE CB C 36.534 0.023 . 199 36 18 ILE CG1 C 28.463 0.063 . 200 36 18 ILE CG2 C 16.82 0.094 . 201 36 18 ILE CD1 C 11.96 0.104 . 202 36 18 ILE N N 118.626 0.017 . 203 37 19 ALA H H 7.69 0.003 . 204 37 19 ALA HA H 4.145 0.001 . 205 37 19 ALA HB H 1.482 0.002 . 206 37 19 ALA C C 183.902 0 . 207 37 19 ALA CA C 55.433 0 . 208 37 19 ALA CB C 17.807 0.09 . 209 37 19 ALA N N 122.361 0.007 . 210 38 20 VAL H H 8.177 0.001 . 211 38 20 VAL HA H 3.63 0.002 . 212 38 20 VAL HB H 2.113 0.001 . 213 38 20 VAL HG1 H 0.988 0.016 . 214 38 20 VAL HG2 H 0.911 0.01 . 215 38 20 VAL C C 180.529 0 . 216 38 20 VAL CA C 66.453 0.045 . 217 38 20 VAL CB C 31.763 0.039 . 218 38 20 VAL CG1 C 22.658 0.079 . 219 38 20 VAL CG2 C 20.969 0.075 . 220 38 20 VAL N N 120.987 0.006 . 221 39 21 LEU H H 8.197 0.002 . 222 39 21 LEU HA H 3.929 0.007 . 223 39 21 LEU HB2 H 1.488 0.001 . 224 39 21 LEU HB3 H 1.833 0.01 . 225 39 21 LEU HG H 0.576 0.003 . 226 39 21 LEU HD1 H 0.907 0.002 . 227 39 21 LEU C C 183.063 0 . 228 39 21 LEU CA C 58.544 0.038 . 229 39 21 LEU CB C 39.409 0.019 . 230 39 21 LEU CG C 26.616 0.077 . 231 39 21 LEU CD1 C 22.814 0.063 . 232 39 21 LEU N N 119.408 0.012 . 233 40 22 GLN H H 8.615 0.003 . 234 40 22 GLN HA H 3.928 0.006 . 235 40 22 GLN HB2 H 2.088 0.003 . 236 40 22 GLN HB3 H 2.274 0.003 . 237 40 22 GLN HG2 H 2.509 0 . 238 40 22 GLN HG3 H 2.358 0 . 239 40 22 GLN C C 183.366 0 . 240 40 22 GLN CA C 59.324 0.041 . 241 40 22 GLN CB C 28.254 0.03 . 242 40 22 GLN CG C 34.149 0 . 243 40 22 GLN N N 121.514 0.043 . 244 41 23 MET H H 7.706 0.003 . 245 41 23 MET HA H 4.032 0.004 . 246 41 23 MET HB2 H 1.764 0.002 . 247 41 23 MET HB3 H 2.35 0.019 . 248 41 23 MET HG2 H 2.026 0.001 . 249 41 23 MET HG3 H 2.353 0 . 250 41 23 MET C C 177.125 0 . 251 41 23 MET CA C 57.763 0.035 . 252 41 23 MET CB C 31.579 0.166 . 253 41 23 MET CG C 31.48 0.013 . 254 41 23 MET N N 119.672 0.011 . 255 42 24 HIS H H 7.218 0.003 . 256 42 24 HIS HA H 4.371 0.001 . 257 42 24 HIS HB2 H 2.178 0.001 . 258 42 24 HIS HB3 H 3 0.002 . 259 42 24 HIS HD2 H 6.729 0.003 . 260 42 24 HIS HE1 H 6.724 0 . 261 42 24 HIS C C 171.216 0 . 262 42 24 HIS CA C 54.601 0.007 . 263 42 24 HIS CB C 27.399 0.052 . 264 42 24 HIS CD2 C 119.787 0.156 . 265 42 24 HIS N N 115.329 0.011 . 266 43 25 ASN H H 7.855 0.003 . 267 43 25 ASN HA H 4.293 0.002 . 268 43 25 ASN HB2 H 2.821 0.001 . 269 43 25 ASN HB3 H 3.106 0.002 . 270 43 25 ASN C C 173.011 0 . 271 43 25 ASN CA C 54.571 0.023 . 272 43 25 ASN CB C 36.981 0.02 . 273 43 25 ASN N N 112.995 0.008 . 274 44 26 ILE H H 7.978 0.002 . 275 44 26 ILE HA H 4.225 0.003 . 276 44 26 ILE HB H 1.592 0.002 . 277 44 26 ILE HG12 H 1.654 0.002 . 278 44 26 ILE HG13 H 1.654 0.002 . 279 44 26 ILE HG2 H 0.855 0.004 . 280 44 26 ILE HD1 H 0.996 0.002 . 281 44 26 ILE C C 174.63 0 . 282 44 26 ILE CA C 60.469 0.038 . 283 44 26 ILE CB C 39.933 0.019 . 284 44 26 ILE CG1 C 27.408 0 . 285 44 26 ILE CG2 C 17.382 0.079 . 286 44 26 ILE CD1 C 14.477 0.086 . 287 44 26 ILE N N 120.077 0.011 . 288 45 27 GLU H H 8.866 0.003 . 289 45 27 GLU HA H 4.144 0.002 . 290 45 27 GLU HB2 H 2.007 0.004 . 291 45 27 GLU HB3 H 1.921 0.009 . 292 45 27 GLU HG2 H 2.146 0.002 . 293 45 27 GLU HG3 H 2.286 0.009 . 294 45 27 GLU C C 174.368 0 . 295 45 27 GLU CA C 56.121 0.01 . 296 45 27 GLU CB C 29.979 0 . 297 45 27 GLU CG C 36.22 0.028 . 298 45 27 GLU N N 129.083 0.017 . 299 46 28 ALA H H 7.897 0.003 . 300 46 28 ALA HA H 5.087 0.003 . 301 46 28 ALA HB H 1.247 0.003 . 302 46 28 ALA C C 175.515 0 . 303 46 28 ALA CA C 50.426 0.009 . 304 46 28 ALA CB C 23.581 0.044 . 305 46 28 ALA N N 127.014 0.009 . 306 47 29 ASN H H 8.712 0.002 . 307 47 29 ASN HA H 5.059 0.001 . 308 47 29 ASN HB2 H 2.54 0.003 . 309 47 29 ASN HB3 H 2.784 0.002 . 310 47 29 ASN C C 172.618 0 . 311 47 29 ASN CA C 51.733 0.034 . 312 47 29 ASN CB C 41.163 0 . 313 47 29 ASN N N 117.293 0.008 . 314 48 30 LYS H H 8.607 0.003 . 315 48 30 LYS HA H 5.302 0.003 . 316 48 30 LYS HB2 H 1.572 0.003 . 317 48 30 LYS HB3 H 1.784 0.003 . 318 48 30 LYS HG2 H 1.332 0 . 319 48 30 LYS HG3 H 1.332 0 . 320 48 30 LYS HD2 H 1.349 0.025 . 321 48 30 LYS HD3 H 1.301 0.007 . 322 48 30 LYS HE2 H 2.722 0.004 . 323 48 30 LYS HE3 H 2.796 0.006 . 324 48 30 LYS C C 175.186 0 . 325 48 30 LYS CA C 54.377 0.006 . 326 48 30 LYS CB C 34.817 0.039 . 327 48 30 LYS CG C 24.702 0.082 . 328 48 30 LYS CD C 29.546 0.07 . 329 48 30 LYS CE C 41.376 0 . 330 48 30 LYS N N 121.209 0.023 . 331 49 31 ILE H H 9.231 0.003 . 332 49 31 ILE HA H 4.335 0.001 . 333 49 31 ILE HB H 1.871 0.002 . 334 49 31 ILE HG12 H 1.311 0.001 . 335 49 31 ILE HG13 H 1.11 0.005 . 336 49 31 ILE HG2 H 0.747 0.003 . 337 49 31 ILE HD1 H 0.737 0.001 . 338 49 31 ILE C C 175.247 0 . 339 49 31 ILE CA C 59.683 0.023 . 340 49 31 ILE CB C 39.941 0.014 . 341 49 31 ILE CG1 C 27.175 0.023 . 342 49 31 ILE CG2 C 17.077 0.088 . 343 49 31 ILE CD1 C 12.604 0.085 . 344 49 31 ILE N N 127.508 0.015 . 345 50 32 ASP H H 8.821 0.004 . 346 50 32 ASP HA H 3.854 0.002 . 347 50 32 ASP HB2 H 2.44 0.002 . 348 50 32 ASP HB3 H 2.791 0.002 . 349 50 32 ASP C C 177.327 0 . 350 50 32 ASP CA C 53.639 0.046 . 351 50 32 ASP CB C 40.857 0.026 . 352 50 32 ASP N N 127.775 0.004 . 353 51 33 SER H H 8.035 0.003 . 354 51 33 SER HA H 4.66 0.004 . 355 51 33 SER HB2 H 3.728 0.002 . 356 51 33 SER HB3 H 4.032 0.002 . 357 51 33 SER C C 177.258 0 . 358 51 33 SER CA C 57.111 0.07 . 359 51 33 SER CB C 63.271 0.023 . 360 51 33 SER N N 123.948 0.005 . 361 52 34 GLY H H 8.643 0.002 . 362 52 34 GLY HA2 H 3.945 0.003 . 363 52 34 GLY HA3 H 3.632 0.002 . 364 52 34 GLY C C 178.261 0 . 365 52 34 GLY CA C 46.45 0.02 . 366 52 34 GLY N N 112.626 0.015 . 367 53 35 LYS HA H 4.119 0.002 . 368 53 35 LYS HB2 H 1.851 0.003 . 369 53 35 LYS HB3 H 1.851 0.003 . 370 53 35 LYS HG2 H 1.477 0.005 . 371 53 35 LYS HG3 H 1.477 0.005 . 372 53 35 LYS HD2 H 1.687 0.003 . 373 53 35 LYS HD3 H 1.687 0.003 . 374 53 35 LYS HE2 H 2.986 0.001 . 375 53 35 LYS HE3 H 2.986 0.001 . 376 53 35 LYS C C 178.526 0 . 377 53 35 LYS CA C 58.349 0.018 . 378 53 35 LYS CB C 32.038 0.052 . 379 53 35 LYS CG C 24.747 0.037 . 380 53 35 LYS CD C 28.946 0.076 . 381 53 35 LYS CE C 42.001 0.019 . 382 54 36 LEU H H 7.453 0.003 . 383 54 36 LEU HA H 4.309 0.014 . 384 54 36 LEU HB2 H 1.67 0.012 . 385 54 36 LEU HB3 H 1.67 0.012 . 386 54 36 LEU HG H 1.612 0.006 . 387 54 36 LEU HD1 H 0.919 0.003 . 388 54 36 LEU HD2 H 0.836 0.006 . 389 54 36 LEU C C 178.832 0 . 390 54 36 LEU CA C 54.958 0.085 . 391 54 36 LEU CB C 41.155 0.019 . 392 54 36 LEU CG C 27.183 0.04 . 393 54 36 LEU CD1 C 24.926 0.043 . 394 54 36 LEU CD2 C 22.477 0.132 . 395 54 36 LEU N N 117.133 0.01 . 396 55 37 GLY H H 7.727 0.002 . 397 55 37 GLY HA2 H 3.759 0.002 . 398 55 37 GLY HA3 H 4.016 0.003 . 399 55 37 GLY C C 172.511 0 . 400 55 37 GLY CA C 44.519 0.027 . 401 55 37 GLY N N 106.946 0.019 . 402 56 38 TYR H H 9.77 0.004 . 403 56 38 TYR HA H 5.267 0.003 . 404 56 38 TYR HB2 H 2.452 0.002 . 405 56 38 TYR HB3 H 2.611 0.002 . 406 56 38 TYR HD1 H 6.922 0.004 . 407 56 38 TYR HD2 H 6.922 0.004 . 408 56 38 TYR HE1 H 6.764 0.009 . 409 56 38 TYR HE2 H 6.764 0.009 . 410 56 38 TYR C C 177.412 0 . 411 56 38 TYR CA C 57.986 0.073 . 412 56 38 TYR CB C 40.838 0.011 . 413 56 38 TYR CD1 C 132.549 0.039 . 414 56 38 TYR CE1 C 117.815 0.105 . 415 56 38 TYR N N 119.5 0.006 . 416 57 39 SER H H 9.13 0.003 . 417 57 39 SER HA H 5.386 0.002 . 418 57 39 SER HB2 H 3.833 0.004 . 419 57 39 SER HB3 H 3.905 0.006 . 420 57 39 SER C C 171.818 0 . 421 57 39 SER CA C 55.817 0.037 . 422 57 39 SER CB C 65.566 0.02 . 423 57 39 SER N N 114.46 0.005 . 424 58 40 ILE H H 8.604 0.004 . 425 58 40 ILE HA H 5.538 0.002 . 426 58 40 ILE HB H 1.837 0.003 . 427 58 40 ILE HG12 H 1.242 0.011 . 428 58 40 ILE HG13 H 1.453 0.006 . 429 58 40 ILE HG2 H 0.808 0.002 . 430 58 40 ILE HD1 H 0.808 0.001 . 431 58 40 ILE C C 176.822 0 . 432 58 40 ILE CA C 57.04 0.043 . 433 58 40 ILE CB C 39.157 0.134 . 434 58 40 ILE CG1 C 27.019 0.142 . 435 58 40 ILE CG2 C 17.784 0.068 . 436 58 40 ILE CD1 C 10.554 0.096 . 437 58 40 ILE N N 121.24 0.032 . 438 59 41 THR H H 8.969 0.003 . 439 59 41 THR HA H 5.435 0.002 . 440 59 41 THR HB H 4.039 0.001 . 441 59 41 THR HG2 H 1.109 0.003 . 442 59 41 THR C C 172.703 0 . 443 59 41 THR CA C 58.889 0.136 . 444 59 41 THR CB C 71.574 0.018 . 445 59 41 THR CG2 C 21.524 0.064 . 446 59 41 THR N N 118.505 0.009 . 447 60 42 VAL H H 8.602 0.003 . 448 60 42 VAL HA H 4.787 0.001 . 449 60 42 VAL HB H 2.402 0.007 . 450 60 42 VAL HG1 H 0.935 0.003 . 451 60 42 VAL HG2 H 0.871 0.005 . 452 60 42 VAL C C 173.802 0 . 453 60 42 VAL CA C 58.594 0.066 . 454 60 42 VAL CB C 36.56 0.091 . 455 60 42 VAL CG1 C 22.942 0.068 . 456 60 42 VAL CG2 C 18.868 0.093 . 457 60 42 VAL N N 111.299 0.007 . 458 61 43 ALA H H 9.41 0.004 . 459 61 43 ALA HA H 4.678 0.003 . 460 61 43 ALA HB H 1.482 0.004 . 461 61 43 ALA C C 182.244 0 . 462 61 43 ALA CA C 52.304 0.004 . 463 61 43 ALA CB C 19.742 0.112 . 464 61 43 ALA N N 125.688 0.008 . 465 62 44 GLU H H 9.047 0.004 . 466 62 44 GLU HA H 3.97 0.001 . 467 62 44 GLU HB2 H 2.134 0.009 . 468 62 44 GLU HB3 H 2.134 0.009 . 469 62 44 GLU HG2 H 2.213 0.002 . 470 62 44 GLU HG3 H 2.284 0 . 471 62 44 GLU C C 175.922 0 . 472 62 44 GLU CA C 62.328 0.03 . 473 62 44 GLU CB C 27.421 0.035 . 474 62 44 GLU N N 122.612 0.013 . 475 63 45 PRO HA H 4.486 0.002 . 476 63 45 PRO HB2 H 1.844 0.006 . 477 63 45 PRO HB3 H 2.396 0.001 . 478 63 45 PRO HG2 H 1.947 0.001 . 479 63 45 PRO HG3 H 1.947 0.001 . 480 63 45 PRO HD2 H 3.83 0.002 . 481 63 45 PRO HD3 H 3.61 0.002 . 482 63 45 PRO C C 178.721 0 . 483 63 45 PRO CA C 65.517 0.004 . 484 63 45 PRO CB C 31.124 0.043 . 485 63 45 PRO CG C 27.985 0.082 . 486 63 45 PRO CD C 50.389 0.02 . 487 64 46 ASP H H 7.812 0.002 . 488 64 46 ASP HA H 4.994 0.002 . 489 64 46 ASP HB2 H 3.001 0.002 . 490 64 46 ASP HB3 H 2.807 0.002 . 491 64 46 ASP C C 176.565 0 . 492 64 46 ASP CA C 54.701 0.013 . 493 64 46 ASP CB C 43.082 0.008 . 494 64 46 ASP N N 115.002 0.005 . 495 65 47 PHE H H 7.902 0.003 . 496 65 47 PHE HA H 3.926 0.003 . 497 65 47 PHE HB2 H 3.002 0.001 . 498 65 47 PHE HB3 H 3.285 0.002 . 499 65 47 PHE HD1 H 6.982 0.004 . 500 65 47 PHE HD2 H 6.982 0.004 . 501 65 47 PHE HE1 H 7.347 0.004 . 502 65 47 PHE HE2 H 7.347 0.004 . 503 65 47 PHE C C 175.918 0 . 504 65 47 PHE CA C 63.611 0.029 . 505 65 47 PHE CB C 40.354 0.044 . 506 65 47 PHE CD1 C 131.561 0.027 . 507 65 47 PHE CE1 C 132.029 0 . 508 65 47 PHE N N 122.01 0.022 . 509 66 48 THR H H 8.648 0.003 . 510 66 48 THR HA H 3.66 0.002 . 511 66 48 THR HB H 4.167 0.002 . 512 66 48 THR HG2 H 1.27 0.002 . 513 66 48 THR C C 178.106 0 . 514 66 48 THR CA C 66.742 0.031 . 515 66 48 THR CB C 68.412 0.189 . 516 66 48 THR CG2 C 22.183 0.111 . 517 66 48 THR N N 112.195 0.023 . 518 67 49 ALA H H 8.198 0.002 . 519 67 49 ALA HA H 4.044 0.002 . 520 67 49 ALA HB H 1.528 0.001 . 521 67 49 ALA C C 180.268 0 . 522 67 49 ALA CA C 54.618 0.009 . 523 67 49 ALA CB C 18.408 0.076 . 524 67 49 ALA N N 124.955 0.019 . 525 68 50 ALA H H 8.469 0.003 . 526 68 50 ALA HA H 3.966 0.003 . 527 68 50 ALA HB H 1.473 0.002 . 528 68 50 ALA C C 181.033 0 . 529 68 50 ALA CA C 55.623 0 . 530 68 50 ALA CB C 19.802 0.063 . 531 68 50 ALA N N 119.593 0.025 . 532 69 51 VAL H H 8.034 0.002 . 533 69 51 VAL HA H 3.257 0.002 . 534 69 51 VAL HB H 1.744 0.004 . 535 69 51 VAL HG1 H 0.698 0.002 . 536 69 51 VAL HG2 H 0.413 0.003 . 537 69 51 VAL C C 179 0 . 538 69 51 VAL CA C 66.077 0.034 . 539 69 51 VAL CB C 31.684 0.102 . 540 69 51 VAL CG1 C 21.184 0.12 . 541 69 51 VAL CG2 C 22.941 0.127 . 542 69 51 VAL N N 115.582 0.011 . 543 70 52 TYR H H 7.179 0.005 . 544 70 52 TYR HA H 3.805 0.002 . 545 70 52 TYR HB2 H 2.708 0.006 . 546 70 52 TYR HB3 H 2.708 0.006 . 547 70 52 TYR HD1 H 5.898 0.003 . 548 70 52 TYR HD2 H 5.898 0.003 . 549 70 52 TYR HE1 H 6.001 0.003 . 550 70 52 TYR HE2 H 6.001 0.003 . 551 70 52 TYR C C 180.084 0 . 552 70 52 TYR CA C 61.459 0.032 . 553 70 52 TYR CB C 37.712 0.059 . 554 70 52 TYR CD1 C 132.675 0.025 . 555 70 52 TYR CE1 C 117.778 0.05 . 556 70 52 TYR N N 118.722 0.01 . 557 71 53 TRP H H 7.924 0.002 . 558 71 53 TRP HA H 4.482 0.015 . 559 71 53 TRP HB2 H 2.929 0.03 . 560 71 53 TRP HB3 H 3.079 0.043 . 561 71 53 TRP HD1 H 6.925 0.003 . 562 71 53 TRP HE1 H 10.291 0 . 563 71 53 TRP HE3 H 7.397 0.006 . 564 71 53 TRP HZ2 H 7.41 0.001 . 565 71 53 TRP HZ3 H 7.101 0.002 . 566 71 53 TRP HH2 H 7.267 0.002 . 567 71 53 TRP C C 180.643 0 . 568 71 53 TRP CA C 58.833 0.028 . 569 71 53 TRP CB C 30.133 0.097 . 570 71 53 TRP CD1 C 127.675 0.052 . 571 71 53 TRP CE3 C 120.961 0.042 . 572 71 53 TRP CZ2 C 114.61 0.114 . 573 71 53 TRP CZ3 C 122.001 0.06 . 574 71 53 TRP CH2 C 124.639 0.019 . 575 71 53 TRP N N 117.18 0.022 . 576 71 53 TRP NE1 N 127.809 0 . 577 72 54 ILE H H 7.978 0.003 . 578 72 54 ILE HA H 4.452 0.002 . 579 72 54 ILE HB H 2.224 0.003 . 580 72 54 ILE HG12 H 1.462 0 . 581 72 54 ILE HG13 H 1.512 0.001 . 582 72 54 ILE HG2 H 0.924 0.003 . 583 72 54 ILE HD1 H 0.79 0.002 . 584 72 54 ILE C C 178.49 0 . 585 72 54 ILE CA C 61.563 0.011 . 586 72 54 ILE CB C 37.491 0.014 . 587 72 54 ILE CG1 C 27.431 0.042 . 588 72 54 ILE CG2 C 18.936 0.045 . 589 72 54 ILE CD1 C 13.745 0.028 . 590 72 54 ILE N N 113.422 0.048 . 591 73 55 LYS H H 7.677 0.006 . 592 73 55 LYS HA H 4.177 0.003 . 593 73 55 LYS HB2 H 1.768 0.003 . 594 73 55 LYS HB3 H 1.768 0.003 . 595 73 55 LYS HG2 H 1.363 0.001 . 596 73 55 LYS HG3 H 1.401 0.005 . 597 73 55 LYS HD2 H 1.552 0.002 . 598 73 55 LYS HD3 H 1.552 0.002 . 599 73 55 LYS HE2 H 2.834 0.001 . 600 73 55 LYS HE3 H 2.834 0.001 . 601 73 55 LYS C C 179.46 0 . 602 73 55 LYS CA C 58.31 0.021 . 603 73 55 LYS CB C 32.247 0.036 . 604 73 55 LYS CG C 24.707 0.046 . 605 73 55 LYS CD C 28.962 0.054 . 606 73 55 LYS CE C 42.022 0.018 . 607 73 55 LYS N N 120.911 0.033 . 608 74 56 THR H H 7.647 0.003 . 609 74 56 THR HA H 4.14 0.016 . 610 74 56 THR HB H 4.066 0.002 . 611 74 56 THR HG2 H 0.978 0.01 . 612 74 56 THR C C 174.574 0 . 613 74 56 THR CA C 63.019 0.157 . 614 74 56 THR CB C 69.394 0.034 . 615 74 56 THR CG2 C 21.249 0.051 . 616 74 56 THR N N 110.017 0.05 . 617 75 57 TYR H H 7.915 0.008 . 618 75 57 TYR HA H 4.468 0 . 619 75 57 TYR HB2 H 3.132 0 . 620 75 57 TYR HB3 H 2.969 0 . 621 75 57 TYR HD1 H 7.116 0.004 . 622 75 57 TYR HD2 H 7.116 0.004 . 623 75 57 TYR HE1 H 6.76 0.011 . 624 75 57 TYR HE2 H 6.76 0.011 . 625 75 57 TYR C C 174.634 0 . 626 75 57 TYR CA C 58.964 0 . 627 75 57 TYR CB C 38.945 0.068 . 628 75 57 TYR CD1 C 133.363 0.096 . 629 75 57 TYR CE1 C 117.608 0 . 630 75 57 TYR N N 122.005 0.012 . 631 76 58 GLN H H 7.467 0.008 . 632 76 58 GLN C C 183.049 0 . 633 76 58 GLN CA C 57.5 0 . 634 76 58 GLN CB C 30.632 0 . 635 76 58 GLN N N 125.769 0.003 . stop_ save_