data_16770 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of a soluble PrgI mutant from Salmonella Typhimurium ; _BMRB_accession_number 16770 _BMRB_flat_file_name bmr16770.str _Entry_type original _Submission_date 2010-03-09 _Accession_date 2010-03-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR solution structure of a functional full length PrgI mutant of the S. thyphimurium Type Three Secretion System' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schmidt Holger . . 2 Poyraz Oemer . . 3 Seidel Karsten . . 4 Delissen Friedmar . . 5 Ader Christian . . 6 Tenenboim Hezi . . 7 Goosmann Christian . . 8 Laube Britta . . 9 Thuenemann Andreas F. . 10 Zychlinski Arturo . . 11 Baldus Marc . . 12 Lange Adam . . 13 Griesinger Christian . . 14 Kolbe Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 474 "13C chemical shifts" 335 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-27 original author . stop_ _Original_release_date 2010-07-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protein refolding is required for assembly of the type three secretion needle.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20543831 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Poyraz Omer . . 2 Schmidt Holger . . 3 Seidel Karsten . . 4 Delissen Friedmar . . 5 Ader Christian . . 6 Tenenboim Hezi . . 7 Goosmann Christian . . 8 Laube Britta . . 9 Thunemann Andreas F. . 10 Zychlinsky Arturo . . 11 Baldus Marc . . 12 Lange Adam . . 13 Griesinger Christian . . 14 Kolbe Michael . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature structural & molecular biology' _Journal_volume 17 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 788 _Page_last 792 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PrgI mutant' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PrgI $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 PrgI _Molecular_mass 9091.127 _Mol_thiol_state 'not present' loop_ _Biological_function ; assembles to a needle-like structure of the TTSS. Essential for bacterial infectivity. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; GSHMATPWSGYLDDVSAKFD TGVDNLQTQVTEALDKLAAK PSDPALLAAYQSKLSEYNLY RNAQSNTAKAFKDIDAAIIQ NFR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ALA 6 THR 7 PRO 8 TRP 9 SER 10 GLY 11 TYR 12 LEU 13 ASP 14 ASP 15 VAL 16 SER 17 ALA 18 LYS 19 PHE 20 ASP 21 THR 22 GLY 23 VAL 24 ASP 25 ASN 26 LEU 27 GLN 28 THR 29 GLN 30 VAL 31 THR 32 GLU 33 ALA 34 LEU 35 ASP 36 LYS 37 LEU 38 ALA 39 ALA 40 LYS 41 PRO 42 SER 43 ASP 44 PRO 45 ALA 46 LEU 47 LEU 48 ALA 49 ALA 50 TYR 51 GLN 52 SER 53 LYS 54 LEU 55 SER 56 GLU 57 TYR 58 ASN 59 LEU 60 TYR 61 ARG 62 ASN 63 ALA 64 GLN 65 SER 66 ASN 67 THR 68 ALA 69 LYS 70 ALA 71 PHE 72 LYS 73 ASP 74 ILE 75 ASP 76 ALA 77 ALA 78 ILE 79 ILE 80 GLN 81 ASN 82 PHE 83 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18276 PrgI 96.39 80 97.50 97.50 2.55e-48 PDB 2KV7 "Nmr Solution Structure Of A Soluble Prgi Mutant From Salmone Typhimurium" 100.00 83 100.00 100.00 2.56e-52 PDB 2LPZ "Atomic Model Of The Type-Iii Secretion System Needle" 96.39 80 97.50 97.50 2.55e-48 PDB 2MEX "Structure Of The Tetrameric Building Block Of The Salmonella Typhimurium Prgi Type Three Secretion System Needle" 96.39 80 97.50 97.50 2.55e-48 PDB 2X9C "Crystal Structure Of A Soluble Prgi Mutant From Salmonella Typhimurium" 100.00 83 100.00 100.00 2.56e-52 PDB 3ZQB "Prgi-Sipd From Salmonella Typhimurium" 100.00 305 97.59 97.59 3.65e-49 PDB 3ZQE "Prgi-Sipd From Salmonella Typhimurium In Complex With Deoxycholate" 100.00 305 97.59 97.59 3.65e-49 DBJ BAJ37865 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 96.39 80 97.50 97.50 2.55e-48 DBJ BAP08778 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 96.39 80 97.50 97.50 2.55e-48 EMBL CAR34293 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 96.39 80 97.50 97.50 2.55e-48 EMBL CAR38585 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 96.39 80 97.50 97.50 2.55e-48 EMBL CBG25842 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 96.39 80 97.50 97.50 2.55e-48 EMBL CBW18951 "type III secretion system apparatus [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]" 96.39 80 97.50 97.50 2.55e-48 EMBL CCF89508 "needle complex major subunit [Salmonella enterica subsp. enterica serovar Senftenberg str. SS209]" 96.39 80 97.50 97.50 2.55e-48 GB AAB60189 "PrgI protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 96.39 80 97.50 97.50 2.55e-48 GB AAL21753 "cytoplasmic cell invasion protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 96.39 80 97.50 97.50 2.55e-48 GB AAX49613 "PrgI [Salmonella enterica subsp. enterica serovar Gallinarum]" 96.39 80 97.50 97.50 2.55e-48 GB AAX66711 "cell invasion protein; cytoplasmic [Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67]" 96.39 80 97.50 97.50 2.55e-48 GB ACF64232 "type III secretion apparatus needle protein [Salmonella enterica subsp. enterica serovar Newport str. SL254]" 96.39 80 97.50 97.50 2.55e-48 REF NP_461794 "secretion system protein PrgI [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 96.39 80 97.50 97.50 2.55e-48 REF WP_000235228 "protein PrgI [Salmonella enterica]" 96.39 80 97.50 97.50 2.55e-48 REF YP_009073587 "PrgI protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 96.39 80 97.50 97.50 2.55e-48 SP P41784 "RecName: Full=Protein PrgI" 96.39 80 97.50 97.50 2.55e-48 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Variant _Gene_mnemonic $entity 'Salmonella enterica' 28901 Bacteria . Salmonella typhimurium SL1344 'enterica serovar' prgI 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 'BL21 (DE3) RIL' pET28a(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_15N _Saveframe_category sample _Sample_type solution _Details ; 0.3 mM PrgI* 20 mM MES 20 mM NaCl pH 5.5 ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.3 mM '[U-100% 15N]' MES 20 mM 'natural abundance' NaCl 20 mM 'natural abundance' stop_ save_ save_sample_15N13C _Saveframe_category sample _Sample_type solution _Details ; 0.3 mM PrgI* 20 mM MES 20 mM NaCl pH 5.5 ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.3 mM '[U-100% 13C; U-100% 15N]' MES 20 mM 'natural abundance' NaCl 20 mM 'natural abundance' stop_ save_ save_sample_15Naniso _Saveframe_category sample _Sample_type solution _Details ; 0.3 mM PrgI* 20 mM MES 20 mM NaCl pH 5.5 18mg/ml pf1 phages ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.3 mM '[U-100% 15N]' MES 20 mM 'natural abundance' NaCl 20 mM '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_AtnosCandid _Saveframe_category software _Name ATHNOS-CANDID _Version . loop_ _Vendor _Address _Electronic_address 'Herrmann, Guntert and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details 'refinement with RDCs' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_900cryo _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_800cryo _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_600cryo _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_600 _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_15N save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_15N13C save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_15N13C save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_15N13C save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_15N13C save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_15N13C save_ save_3D_HCCH-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_15N13C save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_15N13C save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_15N save_ save_3D_1H-13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_15N13C save_ save_2D_1H-15N_TROSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_15N save_ save_2D_1H-15N_COCAINE_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N COCAINE' _Sample_label $sample_15N save_ save_2D_1H-15N_TROSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_15Naniso save_ save_2D_1H-15N_COCAINE_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N COCAINE' _Sample_label $sample_15Naniso save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; 0.3 mM PrgI* 20 mM MES 20 mM NaCl pH 5.5 ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 5.5 . pH pressure 1 . atm temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCACB' '3D HNCA' '3D CBCA(CO)NH' '3D HNCO' '3D HCCH-COSY' '3D HCCH-TOCSY' '3D 1H-15N NOESY' '3D 1H-13C NOESY' stop_ loop_ _Sample_label $sample_15N $sample_15N13C stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PrgI _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 1 GLY H H 8.669 0.02 1 2 1 1 GLY HA2 H 3.789 0.02 2 3 1 1 GLY HA3 H 3.789 0.02 2 4 1 1 GLY C C 181.535 0.3 1 5 1 1 GLY CA C 43.105 0.3 1 6 2 2 SER H H 8.68 0.02 1 7 2 2 SER HA H 4.377 0.02 1 8 2 2 SER HB2 H 3.726 0.02 2 9 2 2 SER HB3 H 3.726 0.02 2 10 2 2 SER C C 174.144 0.3 1 11 2 2 SER CA C 58.074 0.3 1 12 2 2 SER CB C 63.785 0.3 1 13 2 2 SER N N 115.681 0.3 1 14 3 3 HIS H H 8.72 0.02 1 15 3 3 HIS HA H 4.625 0.02 1 16 3 3 HIS HB2 H 3.054 0.02 2 17 3 3 HIS HB3 H 3.159 0.02 2 18 3 3 HIS HD2 H 7.139 0.02 1 19 3 3 HIS HE1 H 8.391 0.02 1 20 3 3 HIS C C 174.133 0.3 1 21 3 3 HIS CA C 55.289 0.3 1 22 3 3 HIS CB C 29.032 0.3 1 23 3 3 HIS CD2 C 119.909 0.3 1 24 3 3 HIS CE1 C 136.391 0.3 1 25 3 3 HIS N N 120.87 0.3 1 26 4 4 MET H H 8.447 0.02 1 27 4 4 MET HA H 4.355 0.02 1 28 4 4 MET HB2 H 1.861 0.02 2 29 4 4 MET HB3 H 1.961 0.02 2 30 4 4 MET HE H 1.982 0.02 1 31 4 4 MET HG2 H 2.4 0.02 2 32 4 4 MET HG3 H 2.456 0.02 2 33 4 4 MET C C 175.507 0.3 1 34 4 4 MET CA C 55.142 0.3 1 35 4 4 MET CB C 32.941 0.3 1 36 4 4 MET CE C 16.715 0.3 1 37 4 4 MET CG C 31.633 0.3 1 38 4 4 MET N N 122.574 0.3 1 39 5 5 ALA H H 8.494 0.02 1 40 5 5 ALA HA H 4.253 0.02 1 41 5 5 ALA HB H 1.289 0.02 1 42 5 5 ALA C C 177.357 0.3 1 43 5 5 ALA CA C 52.402 0.3 1 44 5 5 ALA CB C 19.075 0.3 1 45 5 5 ALA N N 126.111 0.3 1 46 6 6 THR H H 8.182 0.02 1 47 6 6 THR HA H 4.42 0.02 1 48 6 6 THR HB H 3.883 0.02 1 49 6 6 THR HG2 H 1.095 0.02 1 50 6 6 THR CA C 59.209 0.3 1 51 6 6 THR CB C 69.568 0.3 1 52 6 6 THR CG2 C 21.29 0.3 1 53 6 6 THR N N 115.244 0.3 1 54 7 7 PRO HA H 4.262 0.02 1 55 7 7 PRO HB2 H 1.624 0.02 2 56 7 7 PRO HB3 H 2.112 0.02 2 57 7 7 PRO HD2 H 3.385 0.02 2 58 7 7 PRO HD3 H 3.637 0.02 2 59 7 7 PRO HG2 H 1.788 0.02 2 60 7 7 PRO HG3 H 1.788 0.02 2 61 7 7 PRO C C 176.417 0.3 1 62 7 7 PRO CA C 63.428 0.3 1 63 7 7 PRO CB C 31.741 0.3 1 64 7 7 PRO CD C 50.757 0.3 1 65 7 7 PRO CG C 27.277 0.3 1 66 8 8 TRP H H 7.992 0.02 1 67 8 8 TRP HA H 4.597 0.02 1 68 8 8 TRP HB2 H 3.202 0.02 2 69 8 8 TRP HB3 H 3.202 0.02 2 70 8 8 TRP HD1 H 7.148 0.02 1 71 8 8 TRP HE1 H 10.194 0.02 1 72 8 8 TRP HE3 H 7.448 0.02 1 73 8 8 TRP HH2 H 7.042 0.02 1 74 8 8 TRP HZ2 H 7.3 0.02 1 75 8 8 TRP HZ3 H 6.97 0.02 1 76 8 8 TRP C C 176.293 0.3 1 77 8 8 TRP CA C 57.268 0.3 1 78 8 8 TRP CB C 29.092 0.3 1 79 8 8 TRP CD1 C 127.201 0.3 1 80 8 8 TRP CE3 C 120.694 0.3 1 81 8 8 TRP CH2 C 124.554 0.3 1 82 8 8 TRP CZ2 C 114.442 0.3 1 83 8 8 TRP CZ3 C 122.024 0.3 1 84 8 8 TRP N N 120.143 0.3 1 85 8 8 TRP NE1 N 130.28 0.3 1 86 9 9 SER H H 8.043 0.02 1 87 9 9 SER HA H 4.181 0.02 1 88 9 9 SER HB2 H 3.62 0.02 2 89 9 9 SER HB3 H 3.71 0.02 2 90 9 9 SER C C 174.421 0.3 1 91 9 9 SER CA C 58.546 0.3 1 92 9 9 SER CB C 63.63 0.3 1 93 9 9 SER N N 118.779 0.3 1 94 10 10 GLY H H 7.349 0.02 1 95 10 10 GLY HA2 H 3.62 0.02 1 96 10 10 GLY HA3 H 3.462 0.02 1 97 10 10 GLY C C 173.48 0.3 1 98 10 10 GLY CA C 45.028 0.3 1 99 10 10 GLY N N 109.947 0.3 1 100 11 11 TYR H H 7.835 0.02 1 101 11 11 TYR HA H 4.393 0.02 1 102 11 11 TYR HB2 H 2.804 0.02 2 103 11 11 TYR HB3 H 2.906 0.02 2 104 11 11 TYR HD1 H 6.964 0.02 3 105 11 11 TYR HD2 H 6.964 0.02 3 106 11 11 TYR HE1 H 6.715 0.02 3 107 11 11 TYR HE2 H 6.715 0.02 3 108 11 11 TYR C C 175.662 0.3 1 109 11 11 TYR CA C 58.11 0.3 1 110 11 11 TYR CB C 38.592 0.3 1 111 11 11 TYR CD1 C 132.982 0.3 3 112 11 11 TYR CE1 C 118.051 0.3 3 113 11 11 TYR N N 119.888 0.3 1 114 12 12 LEU H H 8.133 0.02 1 115 12 12 LEU HA H 4.173 0.02 1 116 12 12 LEU HB2 H 1.416 0.02 2 117 12 12 LEU HB3 H 1.487 0.02 2 118 12 12 LEU HD1 H 0.775 0.02 2 119 12 12 LEU HD2 H 0.725 0.02 2 120 12 12 LEU HG H 1.359 0.02 1 121 12 12 LEU C C 176.637 0.3 1 122 12 12 LEU CA C 54.954 0.3 1 123 12 12 LEU CB C 42.237 0.3 1 124 12 12 LEU CD1 C 24.894 0.3 2 125 12 12 LEU CD2 C 23.389 0.3 2 126 12 12 LEU CG C 26.63 0.3 1 127 12 12 LEU N N 123.68 0.3 1 128 13 13 ASP H H 8.099 0.02 1 129 13 13 ASP HA H 4.45 0.02 1 130 13 13 ASP HB2 H 2.542 0.02 2 131 13 13 ASP HB3 H 2.563 0.02 2 132 13 13 ASP C C 175.728 0.3 1 133 13 13 ASP CA C 54.235 0.3 1 134 13 13 ASP CB C 40.872 0.3 1 135 13 13 ASP N N 120.604 0.3 1 136 14 14 ASP H H 8.186 0.02 1 137 14 14 ASP HA H 4.518 0.02 1 138 14 14 ASP HB2 H 2.579 0.02 2 139 14 14 ASP HB3 H 2.648 0.02 2 140 14 14 ASP C C 176.759 0.3 1 141 14 14 ASP CA C 54.291 0.3 1 142 14 14 ASP CB C 40.896 0.3 1 143 14 14 ASP N N 120.504 0.3 1 144 15 15 VAL H H 8.126 0.02 1 145 15 15 VAL HA H 3.999 0.02 1 146 15 15 VAL HB H 2.11 0.02 1 147 15 15 VAL HG1 H 0.858 0.02 2 148 15 15 VAL HG2 H 0.858 0.02 2 149 15 15 VAL C C 176.825 0.3 1 150 15 15 VAL CA C 63.029 0.3 1 151 15 15 VAL CB C 32.042 0.3 1 152 15 15 VAL CG1 C 21.071 0.3 2 153 15 15 VAL CG2 C 20.337 0.3 2 154 15 15 VAL N N 120.391 0.3 1 155 16 16 SER H H 8.337 0.02 1 156 16 16 SER HA H 4.254 0.02 1 157 16 16 SER HB2 H 3.81 0.02 2 158 16 16 SER HB3 H 3.81 0.02 2 159 16 16 SER C C 174.61 0.3 1 160 16 16 SER CA C 59.126 0.3 1 161 16 16 SER CB C 63.386 0.3 1 162 16 16 SER N N 118.364 0.3 1 163 17 17 ALA H H 8.09 0.02 1 164 17 17 ALA HA H 4.16 0.02 1 165 17 17 ALA HB H 1.28 0.02 1 166 17 17 ALA C C 177.645 0.3 1 167 17 17 ALA CA C 52.35 0.3 1 168 17 17 ALA CB C 18.905 0.3 1 169 17 17 ALA N N 125.365 0.3 1 170 18 18 LYS H H 7.996 0.02 1 171 18 18 LYS HA H 4.132 0.02 1 172 18 18 LYS HB2 H 1.612 0.02 2 173 18 18 LYS HB3 H 1.612 0.02 2 174 18 18 LYS HD2 H 1.531 0.02 2 175 18 18 LYS HD3 H 1.531 0.02 2 176 18 18 LYS HE2 H 2.851 0.02 2 177 18 18 LYS HE3 H 2.851 0.02 2 178 18 18 LYS HG2 H 1.208 0.02 2 179 18 18 LYS HG3 H 1.208 0.02 2 180 18 18 LYS C C 176.438 0.3 1 181 18 18 LYS CA C 56.318 0.3 1 182 18 18 LYS CB C 32.808 0.3 1 183 18 18 LYS CD C 28.939 0.3 1 184 18 18 LYS CE C 41.95 0.3 1 185 18 18 LYS CG C 24.578 0.3 1 186 18 18 LYS N N 119.638 0.3 1 187 19 19 PHE H H 8.159 0.02 1 188 19 19 PHE HA H 4.551 0.02 1 189 19 19 PHE HB2 H 2.933 0.02 2 190 19 19 PHE HB3 H 3.081 0.02 2 191 19 19 PHE HD1 H 7.158 0.02 3 192 19 19 PHE HD2 H 7.158 0.02 3 193 19 19 PHE C C 175.374 0.3 1 194 19 19 PHE CA C 57.754 0.3 1 195 19 19 PHE CB C 39.469 0.3 1 196 19 19 PHE N N 121.077 0.3 1 197 20 20 ASP H H 8.33 0.02 1 198 20 20 ASP HA H 4.581 0.02 1 199 20 20 ASP HB2 H 2.571 0.02 2 200 20 20 ASP HB3 H 2.65 0.02 2 201 20 20 ASP C C 176.426 0.3 1 202 20 20 ASP CA C 54.194 0.3 1 203 20 20 ASP CB C 41.086 0.3 1 204 20 20 ASP N N 122.284 0.3 1 205 21 21 THR H H 8.236 0.02 1 206 21 21 THR HA H 4.166 0.02 1 207 21 21 THR HB H 4.238 0.02 1 208 21 21 THR HG2 H 1.172 0.02 1 209 21 21 THR C C 175.507 0.3 1 210 21 21 THR CA C 62.783 0.3 1 211 21 21 THR CB C 69.378 0.3 1 212 21 21 THR CG2 C 21.628 0.3 1 213 21 21 THR N N 115.228 0.3 1 214 22 22 GLY H H 8.422 0.02 1 215 22 22 GLY HA2 H 3.905 0.02 1 216 22 22 GLY HA3 H 3.839 0.02 1 217 22 22 GLY C C 174.964 0.3 1 218 22 22 GLY CA C 45.75 0.3 1 219 22 22 GLY N N 111.104 0.3 1 220 23 23 VAL H H 8.036 0.02 1 221 23 23 VAL HA H 3.778 0.02 1 222 23 23 VAL HB H 2 0.02 1 223 23 23 VAL HG1 H 0.88 0.02 2 224 23 23 VAL HG2 H 0.868 0.02 2 225 23 23 VAL C C 176.293 0.3 1 226 23 23 VAL CA C 64.001 0.3 1 227 23 23 VAL CB C 32.187 0.3 1 228 23 23 VAL CG1 C 21.166 0.3 2 229 23 23 VAL CG2 C 21.415 0.3 2 230 23 23 VAL N N 120.374 0.3 1 231 24 24 ASP H H 8.242 0.02 1 232 24 24 ASP HA H 4.464 0.02 1 233 24 24 ASP HB2 H 2.669 0.02 2 234 24 24 ASP HB3 H 2.669 0.02 2 235 24 24 ASP C C 177.047 0.3 1 236 24 24 ASP CA C 55.533 0.3 1 237 24 24 ASP CB C 40.888 0.3 1 238 24 24 ASP N N 122.266 0.3 1 239 25 25 ASN H H 8.274 0.02 1 240 25 25 ASN HA H 4.467 0.02 1 241 25 25 ASN HB2 H 2.725 0.02 2 242 25 25 ASN HB3 H 2.725 0.02 2 243 25 25 ASN HD21 H 6.921 0.02 2 244 25 25 ASN HD22 H 7.654 0.02 2 245 25 25 ASN C C 176.918 0.3 1 246 25 25 ASN CA C 54.679 0.3 1 247 25 25 ASN CB C 38.523 0.3 1 248 25 25 ASN N N 119.267 0.3 1 249 25 25 ASN ND2 N 113.21 0.3 1 250 26 26 LEU H H 8.065 0.02 1 251 26 26 LEU HA H 3.954 0.02 1 252 26 26 LEU HB2 H 1.371 0.02 2 253 26 26 LEU HB3 H 1.802 0.02 2 254 26 26 LEU HD1 H 0.662 0.02 2 255 26 26 LEU HD2 H 0.73 0.02 2 256 26 26 LEU HG H 1.525 0.02 1 257 26 26 LEU C C 178.472 0.3 1 258 26 26 LEU CA C 57.85 0.3 1 259 26 26 LEU CB C 42.512 0.3 1 260 26 26 LEU CD1 C 25.478 0.3 2 261 26 26 LEU CD2 C 23.653 0.3 2 262 26 26 LEU CG C 27.393 0.3 1 263 26 26 LEU N N 121.054 0.3 1 264 27 27 GLN H H 8.542 0.02 1 265 27 27 GLN HA H 3.321 0.02 1 266 27 27 GLN HB2 H 2.085 0.02 2 267 27 27 GLN HB3 H 2.122 0.02 2 268 27 27 GLN HE21 H 6.947 0.02 2 269 27 27 GLN HE22 H 7.299 0.02 2 270 27 27 GLN HG2 H 2.11 0.02 2 271 27 27 GLN HG3 H 2.11 0.02 2 272 27 27 GLN C C 178.487 0.3 1 273 27 27 GLN CA C 59.171 0.3 1 274 27 27 GLN CB C 28.078 0.3 1 275 27 27 GLN CG C 34.008 0.3 1 276 27 27 GLN N N 120.069 0.3 1 277 27 27 GLN NE2 N 111.156 0.3 1 278 28 28 THR H H 8.048 0.02 1 279 28 28 THR HA H 3.893 0.02 1 280 28 28 THR HB H 4.239 0.02 1 281 28 28 THR HG2 H 1.17 0.02 1 282 28 28 THR C C 176.223 0.3 1 283 28 28 THR CA C 66.171 0.3 1 284 28 28 THR CB C 68.355 0.3 1 285 28 28 THR CG2 C 21.915 0.3 1 286 28 28 THR N N 116.384 0.3 1 287 29 29 GLN H H 7.827 0.02 1 288 29 29 GLN HA H 4.064 0.02 1 289 29 29 GLN HB2 H 1.938 0.02 2 290 29 29 GLN HB3 H 1.938 0.02 2 291 29 29 GLN HE21 H 6.778 0.02 2 292 29 29 GLN HE22 H 7.228 0.02 2 293 29 29 GLN HG2 H 2.12 0.02 2 294 29 29 GLN HG3 H 2.12 0.02 2 295 29 29 GLN C C 179.906 0.3 1 296 29 29 GLN CA C 59.067 0.3 1 297 29 29 GLN CB C 28.728 0.3 1 298 29 29 GLN CG C 34.012 0.3 1 299 29 29 GLN N N 120.243 0.3 1 300 29 29 GLN NE2 N 111.812 0.3 1 301 30 30 VAL H H 8.238 0.02 1 302 30 30 VAL HA H 3.418 0.02 1 303 30 30 VAL HB H 2.077 0.02 1 304 30 30 VAL HG1 H 0.74 0.02 2 305 30 30 VAL HG2 H 0.824 0.02 2 306 30 30 VAL C C 177.003 0.3 1 307 30 30 VAL CA C 67.322 0.3 1 308 30 30 VAL CB C 31.509 0.3 1 309 30 30 VAL CG1 C 23.516 0.3 2 310 30 30 VAL CG2 C 22.309 0.3 2 311 30 30 VAL N N 122.828 0.3 1 312 31 31 THR H H 8.055 0.02 1 313 31 31 THR HA H 3.791 0.02 1 314 31 31 THR HB H 4.224 0.02 1 315 31 31 THR HG2 H 1.174 0.02 1 316 31 31 THR C C 175.994 0.3 1 317 31 31 THR CA C 66.562 0.3 1 318 31 31 THR CB C 68.538 0.3 1 319 31 31 THR CG2 C 22.03 0.3 1 320 31 31 THR N N 117.042 0.3 1 321 32 32 GLU H H 8.389 0.02 1 322 32 32 GLU HA H 4.054 0.02 1 323 32 32 GLU HB2 H 1.936 0.02 2 324 32 32 GLU HB3 H 2.044 0.02 2 325 32 32 GLU HG2 H 2.171 0.02 2 326 32 32 GLU HG3 H 2.428 0.02 2 327 32 32 GLU C C 178.045 0.3 1 328 32 32 GLU CA C 59.106 0.3 1 329 32 32 GLU CB C 29.428 0.3 1 330 32 32 GLU CG C 36.152 0.3 1 331 32 32 GLU N N 121.083 0.3 1 332 33 33 ALA H H 7.854 0.02 1 333 33 33 ALA HA H 4.148 0.02 1 334 33 33 ALA HB H 1.452 0.02 1 335 33 33 ALA C C 180.798 0.3 1 336 33 33 ALA CA C 54.854 0.3 1 337 33 33 ALA CB C 17.706 0.3 1 338 33 33 ALA N N 121.243 0.3 1 339 34 34 LEU H H 8.696 0.02 1 340 34 34 LEU HA H 3.558 0.02 1 341 34 34 LEU HB2 H 1.536 0.02 2 342 34 34 LEU HB3 H 1.839 0.02 2 343 34 34 LEU HD1 H 0.636 0.02 2 344 34 34 LEU HD2 H 0.343 0.02 2 345 34 34 LEU HG H 1.356 0.02 1 346 34 34 LEU C C 178.221 0.3 1 347 34 34 LEU CA C 57.375 0.3 1 348 34 34 LEU CB C 40.939 0.3 1 349 34 34 LEU CD1 C 25.201 0.3 2 350 34 34 LEU CD2 C 22.342 0.3 2 351 34 34 LEU CG C 26.408 0.3 1 352 34 34 LEU N N 123.911 0.3 1 353 35 35 ASP H H 8.453 0.02 1 354 35 35 ASP HA H 4.257 0.02 1 355 35 35 ASP HB2 H 2.542 0.02 2 356 35 35 ASP HB3 H 2.739 0.02 2 357 35 35 ASP C C 179.595 0.3 1 358 35 35 ASP CA C 56.95 0.3 1 359 35 35 ASP CB C 39.855 0.3 1 360 35 35 ASP N N 120.457 0.3 1 361 36 36 LYS H H 7.773 0.02 1 362 36 36 LYS HA H 3.967 0.02 1 363 36 36 LYS HB2 H 1.812 0.02 2 364 36 36 LYS HB3 H 1.812 0.02 2 365 36 36 LYS HD2 H 1.595 0.02 2 366 36 36 LYS HD3 H 1.595 0.02 2 367 36 36 LYS HE2 H 2.901 0.02 2 368 36 36 LYS HE3 H 2.901 0.02 2 369 36 36 LYS HG2 H 1.399 0.02 2 370 36 36 LYS HG3 H 1.67 0.02 2 371 36 36 LYS C C 179.096 0.3 1 372 36 36 LYS CA C 59.284 0.3 1 373 36 36 LYS CB C 32.748 0.3 1 374 36 36 LYS CD C 29.043 0.3 1 375 36 36 LYS CE C 41.436 0.3 1 376 36 36 LYS CG C 25.656 0.3 1 377 36 36 LYS N N 119.286 0.3 1 378 37 37 LEU H H 7.575 0.02 1 379 37 37 LEU HA H 3.9 0.02 1 380 37 37 LEU HB2 H 1.128 0.02 2 381 37 37 LEU HB3 H 1.823 0.02 2 382 37 37 LEU HD1 H 0.639 0.02 2 383 37 37 LEU HD2 H 0.791 0.02 2 384 37 37 LEU HG H 1.322 0.02 1 385 37 37 LEU CA C 57.015 0.3 1 386 37 37 LEU CB C 42.132 0.3 1 387 37 37 LEU CD1 C 26.452 0.3 2 388 37 37 LEU CD2 C 23.498 0.3 2 389 37 37 LEU CG C 26.561 0.3 1 390 37 37 LEU N N 121.039 0.3 1 391 38 38 ALA H H 8.239 0.02 1 392 38 38 ALA HA H 3.813 0.02 1 393 38 38 ALA HB H 1.338 0.02 1 394 38 38 ALA C C 178.007 0.3 1 395 38 38 ALA CA C 53.981 0.3 1 396 38 38 ALA CB C 18.09 0.3 1 397 39 39 ALA H H 6.989 0.02 1 398 39 39 ALA HA H 4.206 0.02 1 399 39 39 ALA HB H 1.41 0.02 1 400 39 39 ALA C C 178.084 0.3 1 401 39 39 ALA CA C 52.791 0.3 1 402 39 39 ALA CB C 19.077 0.3 1 403 39 39 ALA N N 116.436 0.3 1 404 40 40 LYS H H 7.398 0.02 1 405 40 40 LYS HA H 4.529 0.02 1 406 40 40 LYS HB2 H 1.53 0.02 2 407 40 40 LYS HB3 H 1.891 0.02 2 408 40 40 LYS HD2 H 1.658 0.02 2 409 40 40 LYS HD3 H 1.682 0.02 2 410 40 40 LYS HE2 H 2.947 0.02 2 411 40 40 LYS HE3 H 2.947 0.02 2 412 40 40 LYS HG2 H 1.317 0.02 2 413 40 40 LYS HG3 H 1.317 0.02 2 414 40 40 LYS CA C 54.422 0.3 1 415 40 40 LYS CB C 33.323 0.3 1 416 40 40 LYS CD C 29.536 0.3 1 417 40 40 LYS CE C 42.096 0.3 1 418 40 40 LYS CG C 25.388 0.3 1 419 40 40 LYS N N 119.688 0.3 1 420 41 41 PRO HA H 4.489 0.02 1 421 41 41 PRO HB2 H 1.865 0.02 2 422 41 41 PRO HB3 H 1.88 0.02 2 423 41 41 PRO HD2 H 3.39 0.02 2 424 41 41 PRO HD3 H 3.505 0.02 2 425 41 41 PRO HG2 H 1.838 0.02 2 426 41 41 PRO HG3 H 1.894 0.02 2 427 41 41 PRO C C 177.735 0.3 1 428 41 41 PRO CA C 64.774 0.3 1 429 41 41 PRO CB C 31.824 0.3 1 430 41 41 PRO CD C 49.401 0.3 1 431 41 41 PRO CG C 27.045 0.3 1 432 42 42 SER H H 8.081 0.02 1 433 42 42 SER HA H 4.393 0.02 1 434 42 42 SER HB2 H 3.976 0.02 2 435 42 42 SER HB3 H 3.976 0.02 2 436 42 42 SER C C 174.362 0.3 1 437 42 42 SER CA C 57.845 0.3 1 438 42 42 SER CB C 63.372 0.3 1 439 42 42 SER N N 112.524 0.3 1 440 43 43 ASP H H 7.795 0.02 1 441 43 43 ASP HA H 4.455 0.02 1 442 43 43 ASP HB2 H 2.469 0.02 2 443 43 43 ASP HB3 H 3.043 0.02 2 444 43 43 ASP CA C 54.561 0.3 1 445 43 43 ASP CB C 42.733 0.3 1 446 43 43 ASP N N 125.224 0.3 1 447 44 44 PRO HA H 4.258 0.02 1 448 44 44 PRO HB2 H 1.99 0.02 2 449 44 44 PRO HB3 H 2.339 0.02 2 450 44 44 PRO HD2 H 3.852 0.02 2 451 44 44 PRO HD3 H 4.328 0.02 2 452 44 44 PRO HG2 H 2.035 0.02 2 453 44 44 PRO HG3 H 2.106 0.02 2 454 44 44 PRO C C 179.519 0.3 1 455 44 44 PRO CA C 64.798 0.3 1 456 44 44 PRO CB C 32.048 0.3 1 457 44 44 PRO CD C 51.239 0.3 1 458 44 44 PRO CG C 27.186 0.3 1 459 45 45 ALA H H 8.188 0.02 1 460 45 45 ALA HA H 4.262 0.02 1 461 45 45 ALA HB H 1.453 0.02 1 462 45 45 ALA CA C 54.831 0.3 1 463 45 45 ALA CB C 17.898 0.3 1 464 45 45 ALA N N 122.911 0.3 1 465 46 46 LEU H H 8.065 0.02 1 466 46 46 LEU HA H 4.144 0.02 1 467 46 46 LEU HB2 H 1.298 0.02 2 468 46 46 LEU HB3 H 1.954 0.02 2 469 46 46 LEU HD1 H 0.97 0.02 2 470 46 46 LEU HD2 H 0.782 0.02 2 471 46 46 LEU HG H 1.674 0.02 1 472 46 46 LEU CA C 56.61 0.3 1 473 46 46 LEU CB C 41.336 0.3 1 474 46 46 LEU CD1 C 26.622 0.3 2 475 46 46 LEU CD2 C 21.873 0.3 2 476 46 46 LEU CG C 26.674 0.3 1 477 47 47 LEU H H 7.833 0.02 1 478 47 47 LEU HA H 4.199 0.02 1 479 47 47 LEU HB2 H 1.722 0.02 2 480 47 47 LEU HB3 H 1.722 0.02 2 481 47 47 LEU HD1 H 0.93 0.02 2 482 47 47 LEU HD2 H 0.984 0.02 2 483 47 47 LEU HG H 1.511 0.02 1 484 47 47 LEU C C 178.763 0.3 1 485 47 47 LEU CA C 58.413 0.3 1 486 47 47 LEU CB C 41.305 0.3 1 487 47 47 LEU CD1 C 25.302 0.3 2 488 47 47 LEU CD2 C 23.614 0.3 2 489 47 47 LEU CG C 26.963 0.3 1 490 48 48 ALA H H 7.847 0.02 1 491 48 48 ALA HA H 4.129 0.02 1 492 48 48 ALA HB H 1.621 0.02 1 493 48 48 ALA C C 180.566 0.3 1 494 48 48 ALA CA C 54.699 0.3 1 495 48 48 ALA CB C 17.752 0.3 1 496 48 48 ALA N N 121.006 0.3 1 497 49 49 ALA H H 8.055 0.02 1 498 49 49 ALA HA H 4.161 0.02 1 499 49 49 ALA HB H 1.49 0.02 1 500 49 49 ALA C C 180.16 0.3 1 501 49 49 ALA CA C 54.824 0.3 1 502 49 49 ALA CB C 18.304 0.3 1 503 49 49 ALA N N 120.764 0.3 1 504 50 50 TYR H H 7.771 0.02 1 505 50 50 TYR HA H 4.127 0.02 1 506 50 50 TYR HB2 H 2.969 0.02 2 507 50 50 TYR HB3 H 3.04 0.02 2 508 50 50 TYR HD1 H 6.871 0.02 3 509 50 50 TYR HD2 H 6.871 0.02 3 510 50 50 TYR HE1 H 6.603 0.02 3 511 50 50 TYR HE2 H 6.603 0.02 3 512 50 50 TYR C C 175.773 0.3 1 513 50 50 TYR CA C 61.051 0.3 1 514 50 50 TYR CB C 38.329 0.3 1 515 50 50 TYR CD1 C 132.286 0.3 3 516 50 50 TYR CE1 C 118.214 0.3 3 517 50 50 TYR N N 118.686 0.3 1 518 51 51 GLN H H 8.534 0.02 1 519 51 51 GLN HA H 3.471 0.02 1 520 51 51 GLN HB2 H 1.933 0.02 2 521 51 51 GLN HB3 H 2.125 0.02 2 522 51 51 GLN HE21 H 6.892 0.02 2 523 51 51 GLN HE22 H 7.313 0.02 2 524 51 51 GLN HG2 H 2.322 0.02 2 525 51 51 GLN HG3 H 2.562 0.02 2 526 51 51 GLN C C 179.384 0.3 1 527 51 51 GLN CA C 59.036 0.3 1 528 51 51 GLN CB C 27.773 0.3 1 529 51 51 GLN CG C 34.025 0.3 1 530 51 51 GLN N N 117.208 0.3 1 531 51 51 GLN NE2 N 112.503 0.3 1 532 52 52 SER H H 8.319 0.02 1 533 52 52 SER HA H 4.185 0.02 1 534 52 52 SER HB2 H 3.935 0.02 2 535 52 52 SER HB3 H 3.935 0.02 2 536 52 52 SER C C 177.08 0.3 1 537 52 52 SER CA C 61.395 0.3 1 538 52 52 SER CB C 62.583 0.3 1 539 52 52 SER N N 114.777 0.3 1 540 53 53 LYS H H 7.894 0.02 1 541 53 53 LYS HA H 4.156 0.02 1 542 53 53 LYS HB2 H 1.644 0.02 2 543 53 53 LYS HB3 H 1.892 0.02 2 544 53 53 LYS HD2 H 1.816 0.02 2 545 53 53 LYS HD3 H 1.816 0.02 2 546 53 53 LYS HE2 H 2.841 0.02 2 547 53 53 LYS HE3 H 2.841 0.02 2 548 53 53 LYS HG2 H 1.435 0.02 2 549 53 53 LYS HG3 H 1.435 0.02 2 550 53 53 LYS C C 178.188 0.3 1 551 53 53 LYS CA C 56.817 0.3 1 552 53 53 LYS CB C 30.181 0.3 1 553 53 53 LYS CD C 26.873 0.3 1 554 53 53 LYS CE C 41.439 0.3 1 555 53 53 LYS CG C 23.847 0.3 1 556 53 53 LYS N N 122.725 0.3 1 557 54 54 LEU H H 8.663 0.02 1 558 54 54 LEU HA H 3.918 0.02 1 559 54 54 LEU HB2 H 0.887 0.02 2 560 54 54 LEU HB3 H 1.458 0.02 2 561 54 54 LEU HD1 H 0.748 0.02 2 562 54 54 LEU HD2 H 0.84 0.02 2 563 54 54 LEU HG H 1.392 0.02 1 564 54 54 LEU C C 178.52 0.3 1 565 54 54 LEU CA C 57.845 0.3 1 566 54 54 LEU CB C 41.523 0.3 1 567 54 54 LEU CD1 C 25.03 0.3 2 568 54 54 LEU CD2 C 23.247 0.3 2 569 54 54 LEU CG C 26.47 0.3 1 570 54 54 LEU N N 121.381 0.3 1 571 55 55 SER H H 7.927 0.02 1 572 55 55 SER HA H 4.186 0.02 1 573 55 55 SER HB2 H 3.964 0.02 2 574 55 55 SER HB3 H 3.964 0.02 2 575 55 55 SER C C 176.87 0.3 1 576 55 55 SER CA C 61.586 0.3 1 577 55 55 SER CB C 62.406 0.3 1 578 55 55 SER N N 113.618 0.3 1 579 56 56 GLU H H 7.875 0.02 1 580 56 56 GLU HA H 3.957 0.02 1 581 56 56 GLU HB2 H 2.164 0.02 2 582 56 56 GLU HB3 H 2.164 0.02 2 583 56 56 GLU HG2 H 2.164 0.02 2 584 56 56 GLU HG3 H 2.448 0.02 2 585 56 56 GLU C C 178.952 0.3 1 586 56 56 GLU CA C 59.491 0.3 1 587 56 56 GLU CB C 29.855 0.3 1 588 56 56 GLU CG C 35.916 0.3 1 589 56 56 GLU N N 122.107 0.3 1 590 57 57 TYR H H 8.504 0.02 1 591 57 57 TYR HA H 4.205 0.02 1 592 57 57 TYR HB2 H 2.884 0.02 2 593 57 57 TYR HB3 H 3.15 0.02 2 594 57 57 TYR HD1 H 6.948 0.02 3 595 57 57 TYR HD2 H 6.948 0.02 3 596 57 57 TYR HE1 H 6.778 0.02 3 597 57 57 TYR HE2 H 6.778 0.02 3 598 57 57 TYR C C 176.493 0.3 1 599 57 57 TYR CA C 61.138 0.3 1 600 57 57 TYR CB C 38.527 0.3 1 601 57 57 TYR CD1 C 132.78 0.3 3 602 57 57 TYR CE1 C 118.048 0.3 3 603 57 57 TYR N N 120.845 0.3 1 604 58 58 ASN H H 8.767 0.02 1 605 58 58 ASN HA H 4.193 0.02 1 606 58 58 ASN HB2 H 2.698 0.02 2 607 58 58 ASN HB3 H 2.82 0.02 2 608 58 58 ASN HD21 H 6.853 0.02 2 609 58 58 ASN HD22 H 7.554 0.02 2 610 58 58 ASN C C 177.723 0.3 1 611 58 58 ASN CA C 55.773 0.3 1 612 58 58 ASN CB C 37.595 0.3 1 613 58 58 ASN N N 118.473 0.3 1 614 58 58 ASN ND2 N 111.51 0.3 1 615 59 59 LEU H H 8.138 0.02 1 616 59 59 LEU HA H 3.993 0.02 1 617 59 59 LEU HB2 H 1.513 0.02 2 618 59 59 LEU HB3 H 1.754 0.02 2 619 59 59 LEU HD1 H 0.811 0.02 2 620 59 59 LEU HD2 H 0.787 0.02 2 621 59 59 LEU HG H 1.625 0.02 1 622 59 59 LEU C C 179.384 0.3 1 623 59 59 LEU CA C 57.925 0.3 1 624 59 59 LEU CB C 41.744 0.3 1 625 59 59 LEU CD1 C 24.74 0.3 2 626 59 59 LEU CD2 C 23.602 0.3 2 627 59 59 LEU CG C 26.815 0.3 1 628 59 59 LEU N N 121.279 0.3 1 629 60 60 TYR H H 7.781 0.02 1 630 60 60 TYR HA H 4.135 0.02 1 631 60 60 TYR HB2 H 2.983 0.02 2 632 60 60 TYR HB3 H 2.983 0.02 2 633 60 60 TYR HD1 H 6.926 0.02 3 634 60 60 TYR HD2 H 6.926 0.02 3 635 60 60 TYR HE1 H 6.733 0.02 3 636 60 60 TYR HE2 H 6.733 0.02 3 637 60 60 TYR C C 177.867 0.3 1 638 60 60 TYR CA C 60.847 0.3 1 639 60 60 TYR CB C 38.538 0.3 1 640 60 60 TYR CD1 C 132.958 0.3 3 641 60 60 TYR CE1 C 118.054 0.3 3 642 60 60 TYR N N 120.448 0.3 1 643 61 61 ARG H H 8.345 0.02 1 644 61 61 ARG HA H 3.77 0.02 1 645 61 61 ARG HB2 H 1.531 0.02 2 646 61 61 ARG HB3 H 1.531 0.02 2 647 61 61 ARG HD2 H 2.778 0.02 2 648 61 61 ARG HD3 H 2.879 0.02 2 649 61 61 ARG HE H 6.889 0.02 1 650 61 61 ARG HG2 H 1.287 0.02 2 651 61 61 ARG HG3 H 1.318 0.02 2 652 61 61 ARG C C 178.265 0.3 1 653 61 61 ARG CA C 58.025 0.3 1 654 61 61 ARG CB C 29.438 0.3 1 655 61 61 ARG CD C 42.828 0.3 1 656 61 61 ARG CG C 26.576 0.3 1 657 61 61 ARG N N 118.929 0.3 1 658 61 61 ARG NE N 83.713 0.3 1 659 62 62 ASN H H 8.046 0.02 1 660 62 62 ASN HA H 4.464 0.02 1 661 62 62 ASN HB2 H 2.733 0.02 2 662 62 62 ASN HB3 H 2.733 0.02 2 663 62 62 ASN HD21 H 6.886 0.02 2 664 62 62 ASN HD22 H 7.539 0.02 2 665 62 62 ASN C C 176.072 0.3 1 666 62 62 ASN CA C 54.521 0.3 1 667 62 62 ASN CB C 38.305 0.3 1 668 62 62 ASN N N 117.751 0.3 1 669 62 62 ASN ND2 N 112.64 0.3 1 670 63 63 ALA H H 7.733 0.02 1 671 63 63 ALA HA H 4.143 0.02 1 672 63 63 ALA HB H 1.338 0.02 1 673 63 63 ALA C C 178.709 0.3 1 674 63 63 ALA CA C 53.631 0.3 1 675 63 63 ALA CB C 18.325 0.3 1 676 63 63 ALA N N 122.793 0.3 1 677 64 64 GLN H H 7.89 0.02 1 678 64 64 GLN HA H 4.049 0.02 1 679 64 64 GLN HB2 H 1.846 0.02 2 680 64 64 GLN HB3 H 2.017 0.02 2 681 64 64 GLN HE21 H 6.773 0.02 2 682 64 64 GLN HE22 H 7.249 0.02 2 683 64 64 GLN HG2 H 2.119 0.02 2 684 64 64 GLN HG3 H 2.119 0.02 2 685 64 64 GLN C C 176.792 0.3 1 686 64 64 GLN CA C 56.403 0.3 1 687 64 64 GLN CB C 28.863 0.3 1 688 64 64 GLN CG C 33.507 0.3 1 689 64 64 GLN N N 117.622 0.3 1 690 64 64 GLN NE2 N 113.142 0.3 1 691 65 65 SER H H 8.016 0.02 1 692 65 65 SER HA H 4.268 0.02 1 693 65 65 SER HB2 H 3.848 0.02 2 694 65 65 SER HB3 H 3.848 0.02 2 695 65 65 SER C C 174.709 0.3 1 696 65 65 SER CA C 58.995 0.3 1 697 65 65 SER CB C 63.396 0.3 1 698 65 65 SER N N 115.458 0.3 1 699 66 66 ASN H H 8.295 0.02 1 700 66 66 ASN HA H 4.644 0.02 1 701 66 66 ASN HB2 H 2.721 0.02 2 702 66 66 ASN HB3 H 2.778 0.02 2 703 66 66 ASN HD21 H 6.88 0.02 2 704 66 66 ASN HD22 H 7.584 0.02 2 705 66 66 ASN C C 175.839 0.3 1 706 66 66 ASN CA C 53.748 0.3 1 707 66 66 ASN CB C 38.474 0.3 1 708 66 66 ASN N N 120.605 0.3 1 709 66 66 ASN ND2 N 112.999 0.3 1 710 67 67 THR H H 8.028 0.02 1 711 67 67 THR HA H 4.144 0.02 1 712 67 67 THR HB H 4.161 0.02 1 713 67 67 THR HG2 H 1.132 0.02 1 714 67 67 THR C C 174.565 0.3 1 715 67 67 THR CA C 62.679 0.3 1 716 67 67 THR CB C 69.448 0.3 1 717 67 67 THR CG2 C 21.541 0.3 1 718 67 67 THR N N 114.682 0.3 1 719 68 68 ALA H H 8.164 0.02 1 720 68 68 ALA HA H 4.159 0.02 1 721 68 68 ALA HB H 1.327 0.02 1 722 68 68 ALA C C 177.977 0.3 1 723 68 68 ALA CA C 52.835 0.3 1 724 68 68 ALA CB C 18.838 0.3 1 725 68 68 ALA N N 125.92 0.3 1 726 69 69 LYS H H 8.112 0.02 1 727 69 69 LYS HA H 4.12 0.02 1 728 69 69 LYS HB2 H 1.693 0.02 2 729 69 69 LYS HB3 H 1.693 0.02 2 730 69 69 LYS HD2 H 1.667 0.02 2 731 69 69 LYS HD3 H 1.684 0.02 2 732 69 69 LYS HE2 H 2.885 0.02 2 733 69 69 LYS HE3 H 2.885 0.02 2 734 69 69 LYS HG2 H 1.315 0.02 2 735 69 69 LYS HG3 H 1.362 0.02 2 736 69 69 LYS C C 176.238 0.3 1 737 69 69 LYS CA C 56.362 0.3 1 738 69 69 LYS CB C 32.962 0.3 1 739 69 69 LYS CD C 29.594 0.3 1 740 69 69 LYS CE C 41.938 0.3 1 741 69 69 LYS CG C 24.683 0.3 1 742 69 69 LYS N N 120.283 0.3 1 743 70 70 ALA H H 8.132 0.02 1 744 70 70 ALA HA H 4.158 0.02 1 745 70 70 ALA HB H 1.238 0.02 1 746 70 70 ALA C C 177.49 0.3 1 747 70 70 ALA CA C 52.665 0.3 1 748 70 70 ALA CB C 19.017 0.3 1 749 70 70 ALA N N 124.348 0.3 1 750 71 71 PHE H H 8.134 0.02 1 751 71 71 PHE HA H 4.453 0.02 1 752 71 71 PHE HB2 H 2.961 0.02 2 753 71 71 PHE HB3 H 3.036 0.02 2 754 71 71 PHE HD1 H 7.138 0.02 3 755 71 71 PHE HD2 H 7.138 0.02 3 756 71 71 PHE C C 175.64 0.3 1 757 71 71 PHE CA C 57.889 0.3 1 758 71 71 PHE CB C 39.407 0.3 1 759 71 71 PHE N N 119.557 0.3 1 760 72 72 LYS H H 8.117 0.02 1 761 72 72 LYS HA H 4.156 0.02 1 762 72 72 LYS HB2 H 1.645 0.02 2 763 72 72 LYS HB3 H 1.645 0.02 2 764 72 72 LYS HD2 H 1.573 0.02 2 765 72 72 LYS HD3 H 1.573 0.02 2 766 72 72 LYS HE2 H 2.892 0.02 2 767 72 72 LYS HE3 H 2.892 0.02 2 768 72 72 LYS HG2 H 1.294 0.02 2 769 72 72 LYS HG3 H 1.294 0.02 2 770 72 72 LYS C C 175.795 0.3 1 771 72 72 LYS CA C 56.228 0.3 1 772 72 72 LYS CB C 32.916 0.3 1 773 72 72 LYS CD C 28.986 0.3 1 774 72 72 LYS CE C 42.002 0.3 1 775 72 72 LYS CG C 24.497 0.3 1 776 72 72 LYS N N 122.71 0.3 1 777 73 73 ASP H H 8.268 0.02 1 778 73 73 ASP HA H 4.473 0.02 1 779 73 73 ASP HB2 H 2.514 0.02 2 780 73 73 ASP HB3 H 2.653 0.02 2 781 73 73 ASP C C 176.426 0.3 1 782 73 73 ASP CA C 54.359 0.3 1 783 73 73 ASP CB C 40.81 0.3 1 784 73 73 ASP N N 121.793 0.3 1 785 74 74 ILE H H 8.062 0.02 1 786 74 74 ILE HA H 3.984 0.02 1 787 74 74 ILE HB H 1.789 0.02 1 788 74 74 ILE HD1 H 0.771 0.02 1 789 74 74 ILE HG12 H 1.095 0.02 2 790 74 74 ILE HG13 H 1.397 0.02 2 791 74 74 ILE HG2 H 0.818 0.02 1 792 74 74 ILE C C 176.017 0.3 1 793 74 74 ILE CA C 61.565 0.3 1 794 74 74 ILE CB C 38.561 0.3 1 795 74 74 ILE CD1 C 13.175 0.3 1 796 74 74 ILE CG1 C 27.271 0.3 1 797 74 74 ILE CG2 C 17.381 0.3 1 798 74 74 ILE N N 120.977 0.3 1 799 75 75 ASP H H 8.274 0.02 1 800 75 75 ASP HA H 4.47 0.02 1 801 75 75 ASP HB2 H 2.522 0.02 2 802 75 75 ASP HB3 H 2.658 0.02 2 803 75 75 ASP C C 176.194 0.3 1 804 75 75 ASP CA C 54.511 0.3 1 805 75 75 ASP CB C 40.859 0.3 1 806 75 75 ASP N N 123.802 0.3 1 807 76 76 ALA H H 8.133 0.02 1 808 76 76 ALA HA H 4.167 0.02 1 809 76 76 ALA HB H 1.285 0.02 1 810 76 76 ALA C C 177.645 0.3 1 811 76 76 ALA CA C 52.788 0.3 1 812 76 76 ALA CB C 18.946 0.3 1 813 76 76 ALA N N 124.65 0.3 1 814 77 77 ALA H H 8.18 0.02 1 815 77 77 ALA HA H 4.122 0.02 1 816 77 77 ALA HB H 1.301 0.02 1 817 77 77 ALA C C 177.955 0.3 1 818 77 77 ALA CA C 52.792 0.3 1 819 77 77 ALA CB C 18.844 0.3 1 820 77 77 ALA N N 122.113 0.3 1 821 78 78 ILE H H 7.918 0.02 1 822 78 78 ILE HA H 3.981 0.02 1 823 78 78 ILE HB H 1.796 0.02 1 824 78 78 ILE HD1 H 0.785 0.02 1 825 78 78 ILE HG12 H 1.108 0.02 2 826 78 78 ILE HG13 H 1.428 0.02 2 827 78 78 ILE HG2 H 0.789 0.02 1 828 78 78 ILE C C 176.482 0.3 1 829 78 78 ILE CA C 61.292 0.3 1 830 78 78 ILE CB C 38.326 0.3 1 831 78 78 ILE CD1 C 12.68 0.3 1 832 78 78 ILE CG1 C 27.365 0.3 1 833 78 78 ILE CG2 C 17.251 0.3 1 834 78 78 ILE N N 119.694 0.3 1 835 79 79 ILE H H 8.096 0.02 1 836 79 79 ILE HA H 3.977 0.02 1 837 79 79 ILE HB H 1.758 0.02 1 838 79 79 ILE HD1 H 0.756 0.02 1 839 79 79 ILE HG12 H 1.115 0.02 2 840 79 79 ILE HG13 H 1.415 0.02 2 841 79 79 ILE HG2 H 0.786 0.02 1 842 79 79 ILE C C 176.205 0.3 1 843 79 79 ILE CA C 61.14 0.3 1 844 79 79 ILE CB C 38.145 0.3 1 845 79 79 ILE CD1 C 12.523 0.3 1 846 79 79 ILE CG1 C 27.384 0.3 1 847 79 79 ILE CG2 C 17.331 0.3 1 848 79 79 ILE N N 125.127 0.3 1 849 80 80 GLN H H 8.372 0.02 1 850 80 80 GLN HA H 4.156 0.02 1 851 80 80 GLN HB2 H 1.806 0.02 2 852 80 80 GLN HB3 H 1.854 0.02 2 853 80 80 GLN HE21 H 6.871 0.02 2 854 80 80 GLN HE22 H 7.509 0.02 2 855 80 80 GLN HG2 H 2.182 0.02 2 856 80 80 GLN HG3 H 2.182 0.02 2 857 80 80 GLN C C 175.186 0.3 1 858 80 80 GLN CA C 55.627 0.3 1 859 80 80 GLN CB C 29.253 0.3 1 860 80 80 GLN CG C 33.501 0.3 1 861 80 80 GLN N N 124.295 0.3 1 862 80 80 GLN NE2 N 112.777 0.3 1 863 81 81 ASN H H 8.293 0.02 1 864 81 81 ASN HA H 4.571 0.02 1 865 81 81 ASN HB2 H 2.574 0.02 2 866 81 81 ASN HB3 H 2.631 0.02 2 867 81 81 ASN HD21 H 6.866 0.02 2 868 81 81 ASN HD22 H 7.531 0.02 2 869 81 81 ASN C C 174.488 0.3 1 870 81 81 ASN CA C 52.995 0.3 1 871 81 81 ASN CB C 38.858 0.3 1 872 81 81 ASN N N 119.759 0.3 1 873 81 81 ASN ND2 N 112.978 0.3 1 874 82 82 PHE H H 8.157 0.02 1 875 82 82 PHE HA H 4.544 0.02 1 876 82 82 PHE HB2 H 2.937 0.02 2 877 82 82 PHE HB3 H 3.102 0.02 2 878 82 82 PHE HD1 H 7.128 0.02 3 879 82 82 PHE HD2 H 7.128 0.02 3 880 82 82 PHE C C 174.587 0.3 1 881 82 82 PHE CA C 57.685 0.3 1 882 82 82 PHE CB C 39.289 0.3 1 883 82 82 PHE N N 120.717 0.3 1 884 83 83 ARG H H 7.779 0.02 1 885 83 83 ARG HA H 4.054 0.02 1 886 83 83 ARG HB2 H 1.61 0.02 2 887 83 83 ARG HB3 H 1.737 0.02 2 888 83 83 ARG HD2 H 3.079 0.02 2 889 83 83 ARG HD3 H 3.079 0.02 2 890 83 83 ARG HE H 7.139 0.02 1 891 83 83 ARG HG2 H 1.452 0.02 2 892 83 83 ARG HG3 H 1.452 0.02 2 893 83 83 ARG CA C 57.278 0.3 1 894 83 83 ARG CB C 31.45 0.3 1 895 83 83 ARG CD C 43.279 0.3 1 896 83 83 ARG CG C 26.96 0.3 1 897 83 83 ARG N N 127.261 0.3 1 898 83 83 ARG NE N 84.951 0.3 1 stop_ save_