data_7178 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of Q8ZP25 from Salmonella typhimurium LT2. ; _BMRB_accession_number 7178 _BMRB_flat_file_name bmr7178.str _Entry_type original _Submission_date 2006-06-21 _Accession_date 2006-07-14 _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 Parish D. . . 2 Liu G. . . 3 Shen Y. . . 4 Ho C. . . 5 Cunningham K. . . 6 Xiao R. . . 7 Swapna G. V.T. . 8 Acton T. B. . 9 Montelione G. T. . 10 Szyperski T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 584 "13C chemical shifts" 356 "15N chemical shifts" 100 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-09-12 original author 'original release' 2008-01-14 update author 'addition of new chemical shifts' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR structure of Q8ZP25 from Salmonella typhimurium LT2.' _Citation_status submitted _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 Parish D. . . 2 Liu G. . . 3 Shen Y. . . 4 Ho C. K. . 5 Cunningham K. . . 6 Xiao R. . . 7 Swapna G. V.T. . 8 Acton T. B. . 9 Montelione G. T. . 10 Szyperski T. . . stop_ _Journal_abbreviation . _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 . loop_ _Keyword GFT-NMR NESG 'Northeast Structural Genomics Consortium' 'Protein Structure Initiative' PSI 'Putative thiol-disulfide isomerase' 'Structural Genomics' stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name 'putative chaperone' _Abbreviation_common 'putative chaperone' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'putative chaperone' $chaperone stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_chaperone _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'putative chaperone' _Abbreviation_common 'putative chaperone' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; MANDTPFSALWQRLLTRGWQ PVEASTVDDWIKRVGDGVIL LSSDPRRTPEVSDNPVMIAE LLREFPQFDWQVAVADLEQS EAIGDRFNVRRFPATLVFTD GKLRGALSGIHPWAELLTLM RSIVDTPAAQETVQLEHHHH HH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASN 4 ASP 5 THR 6 PRO 7 PHE 8 SER 9 ALA 10 LEU 11 TRP 12 GLN 13 ARG 14 LEU 15 LEU 16 THR 17 ARG 18 GLY 19 TRP 20 GLN 21 PRO 22 VAL 23 GLU 24 ALA 25 SER 26 THR 27 VAL 28 ASP 29 ASP 30 TRP 31 ILE 32 LYS 33 ARG 34 VAL 35 GLY 36 ASP 37 GLY 38 VAL 39 ILE 40 LEU 41 LEU 42 SER 43 SER 44 ASP 45 PRO 46 ARG 47 ARG 48 THR 49 PRO 50 GLU 51 VAL 52 SER 53 ASP 54 ASN 55 PRO 56 VAL 57 MET 58 ILE 59 ALA 60 GLU 61 LEU 62 LEU 63 ARG 64 GLU 65 PHE 66 PRO 67 GLN 68 PHE 69 ASP 70 TRP 71 GLN 72 VAL 73 ALA 74 VAL 75 ALA 76 ASP 77 LEU 78 GLU 79 GLN 80 SER 81 GLU 82 ALA 83 ILE 84 GLY 85 ASP 86 ARG 87 PHE 88 ASN 89 VAL 90 ARG 91 ARG 92 PHE 93 PRO 94 ALA 95 THR 96 LEU 97 VAL 98 PHE 99 THR 100 ASP 101 GLY 102 LYS 103 LEU 104 ARG 105 GLY 106 ALA 107 LEU 108 SER 109 GLY 110 ILE 111 HIS 112 PRO 113 TRP 114 ALA 115 GLU 116 LEU 117 LEU 118 THR 119 LEU 120 MET 121 ARG 122 SER 123 ILE 124 VAL 125 ASP 126 THR 127 PRO 128 ALA 129 ALA 130 GLN 131 GLU 132 THR 133 VAL 134 GLN 135 LEU 136 GLU 137 HIS 138 HIS 139 HIS 140 HIS 141 HIS 142 HIS 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 2ES7 "Crystal Structure Of Q8zp25 From Salmonella Typhimurium Lt2. Nesg Target Str70" 99.30 142 98.58 98.58 1.75e-94 PDB 2GZP "Solution Nmr Structure Of Q8zp25 From Salmonella Typhimurium Lt2; Northeast Structural Genomics Consortium Target Str70" 100.00 142 100.00 100.00 1.68e-97 PDB 2JZT "Solution Nmr Structure Of Q8zp25_salty From Salmonella Typhimurium. Northeast Structural Genomics Consortium Target Str70" 100.00 142 100.00 100.00 1.68e-97 DBJ BAJ36754 "hydrogenase 1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 94.37 134 100.00 100.00 2.36e-90 DBJ BAP07655 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 94.37 134 100.00 100.00 2.36e-90 EMBL CAD05474 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 94.37 134 97.01 99.25 2.24e-88 EMBL CAR32826 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 94.37 134 98.51 100.00 3.28e-89 EMBL CAR37202 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 94.37 134 98.51 100.00 3.28e-89 EMBL CBG24793 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 94.37 134 100.00 100.00 2.36e-90 EMBL CBW17813 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]" 94.37 134 100.00 100.00 2.36e-90 GB AAL20705 "putative thiol-disulfide isomerase and thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 94.37 134 100.00 100.00 2.36e-90 GB AAO68750 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 94.37 134 97.01 99.25 2.24e-88 GB ABX66837 "hypothetical protein SPAB_01430 [Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]" 94.37 134 98.51 100.00 3.28e-89 GB ACF61159 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Newport str. SL254]" 94.37 134 98.51 100.00 3.28e-89 GB ACF68193 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Heidelberg str. SL476]" 94.37 134 100.00 100.00 2.36e-90 PIR AH0721 "hydrogenase-1 operon protein HyaE [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 94.37 134 97.01 99.25 2.24e-88 REF NP_456299 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 94.37 134 97.01 99.25 2.24e-88 REF NP_460746 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 94.37 134 100.00 100.00 2.36e-90 REF NP_804901 "hydrogenase-1 operon protein HyaE [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 94.37 134 97.01 99.25 2.24e-88 REF WP_000245855 "hydrogenase-1 operon protein HyaE [Salmonella enterica]" 94.37 134 97.76 99.25 1.86e-88 REF WP_001262570 "hydrogenase-1 operon protein HyaE [Salmonella enterica]" 94.37 134 97.01 98.51 1.60e-87 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $chaperone 'Salmonella typhimurium' 602 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 $chaperone '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 $chaperone 1 mM '[U-13C; U-15N]' H20 95 % . D20 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $chaperone 1 mM '[U-5% 13C; U-15N]' H20 95 % . D20 5 % . stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task refinement stop_ _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details Guntert save_ save_CYANA1 _Saveframe_category software _Name CYANA _Version 1.05 loop_ _Task 'structure solution' stop_ _Details Guntert save_ save_CYANA2 _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Task 'structure solution' stop_ _Details Guntert save_ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1c loop_ _Task collection stop_ _Details Varian save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task processing stop_ _Details 'Delaglio, Bax.' save_ save_xeasy _Saveframe_category software _Name XEASY _Version 1.3.1.3 loop_ _Task 'data analysis' stop_ _Details Glaser save_ save_autostructure _Saveframe_category software _Name AutoStruct _Version 2.0.0 loop_ _Task 'data analysis' stop_ _Details 'Huang, Tejero, Power, Montelione.' save_ save_autoassign _Saveframe_category software _Name AutoAssign _Version . loop_ _Task 'data analysis' stop_ _Details 'Zimmerman, Moseley, Kiriyeva, Kulikowski, Montelione' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Brunger,_Adams,_Clore,_DeLano,_Gros,_Grosse-Kunstleve,_Jiang,_Kuszewski,_Nilges,_Pannu,_Read,_Rice,_Simonson,_Warren._1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Brunger, Adams, Clore, DeLano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warren.' _Sample_label . save_ save_Guntert_2 _Saveframe_category NMR_applied_experiment _Experiment_name Guntert _Sample_label . save_ save_Varian_3 _Saveframe_category NMR_applied_experiment _Experiment_name Varian _Sample_label . save_ save_Delaglio,_Bax_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'Delaglio, Bax' _Sample_label . save_ save_Glaser_5 _Saveframe_category NMR_applied_experiment _Experiment_name Glaser _Sample_label . save_ save_Huang,_Tejero,_Power,_Montelione_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'Huang, Tejero, Power, Montelione' _Sample_label . save_ save_Zimmerman,_Moseley,_Kiriyeva,_Kulikowski,_Montelione_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'Zimmerman, Moseley, Kiriyeva, Kulikowski, Montelione' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 300 . K 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 _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'putative chaperone' _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 . 11 TRP N N 120.1 . 1 2 . 11 TRP H H 8.74 . 1 3 . 11 TRP CA C 59.7 . 1 4 . 11 TRP HA H 4.04 . 1 5 . 11 TRP CB C 29.9 . 1 6 . 11 TRP HB2 H 3.09 . 2 7 . 11 TRP HB3 H 2.71 . 2 8 . 11 TRP CD1 C 126.0 . 1 9 . 11 TRP CE3 C 120.3 . 1 10 . 11 TRP NE1 N 129.3 . 1 11 . 11 TRP HD1 H 7.15 . 1 12 . 11 TRP HE3 H 7.34 . 1 13 . 11 TRP CZ3 C 120.2 . 1 14 . 11 TRP CZ2 C 114.0 . 1 15 . 11 TRP HE1 H 10.25 . 1 16 . 11 TRP HZ3 H 6.68 . 1 17 . 11 TRP CH2 C 124.3 . 1 18 . 11 TRP HZ2 H 7.49 . 1 19 . 11 TRP HH2 H 7.17 . 1 20 . 12 GLN N N 113.7 . 1 21 . 12 GLN H H 7.69 . 1 22 . 12 GLN CA C 58.7 . 1 23 . 12 GLN HA H 3.81 . 1 24 . 12 GLN CB C 28.1 . 1 25 . 12 GLN HB2 H 2.12 . 2 26 . 12 GLN HB3 H 2.11 . 2 27 . 12 GLN CG C 33.6 . 1 28 . 12 GLN HG2 H 2.47 . 2 29 . 12 GLN HG3 H 2.46 . 2 30 . 12 GLN HE21 H 7.19 . 2 31 . 12 GLN HE22 H 7.11 . 2 32 . 13 ARG N N 119.2 . 1 33 . 13 ARG H H 7.54 . 1 34 . 13 ARG CA C 59.4 . 1 35 . 13 ARG HA H 3.90 . 1 36 . 13 ARG CB C 30.0 . 1 37 . 13 ARG HB2 H 2.02 . 2 38 . 13 ARG HB3 H 1.79 . 2 39 . 13 ARG CG C 27.8 . 1 40 . 13 ARG HG2 H 1.53 . 2 41 . 13 ARG HG3 H 1.83 . 2 42 . 13 ARG CD C 43.5 . 1 43 . 13 ARG HD2 H 3.17 . 2 44 . 13 ARG HD3 H 3.17 . 2 45 . 14 LEU N N 120.2 . 1 46 . 14 LEU H H 8.11 . 1 47 . 14 LEU CA C 57.5 . 1 48 . 14 LEU HA H 3.64 . 1 49 . 14 LEU CB C 40.4 . 1 50 . 14 LEU HB2 H 1.79 . 2 51 . 14 LEU HB3 H 1.17 . 2 52 . 14 LEU CG C 26.2 . 1 53 . 14 LEU HG H 1.02 . 1 54 . 14 LEU HD1 H 0.75 . 2 55 . 14 LEU HD2 H 0.88 . 2 56 . 14 LEU CD1 C 22.3 . 1 57 . 14 LEU CD2 C 24.2 . 1 58 . 15 LEU N N 117.5 . 1 59 . 15 LEU H H 7.78 . 1 60 . 15 LEU CA C 57.4 . 1 61 . 15 LEU HA H 3.92 . 1 62 . 15 LEU CB C 40.4 . 1 63 . 15 LEU HB2 H 1.50 . 2 64 . 15 LEU HB3 H 1.32 . 2 65 . 15 LEU CG C 27.0 . 1 66 . 15 LEU HG H 1.10 . 1 67 . 15 LEU HD1 H 0.32 . 2 68 . 15 LEU HD2 H 0.28 . 2 69 . 15 LEU CD1 C 24.0 . 1 70 . 15 LEU CD2 C 21.8 . 1 71 . 16 THR N N 115.3 . 1 72 . 16 THR H H 7.96 . 1 73 . 16 THR CA C 65.2 . 1 74 . 16 THR HA H 3.95 . 1 75 . 16 THR CB C 68.7 . 1 76 . 16 THR HB H 4.17 . 1 77 . 16 THR HG2 H 1.20 . 1 78 . 16 THR CG2 C 21.8 . 1 79 . 17 ARG N N 119.0 . 1 80 . 17 ARG H H 6.98 . 1 81 . 17 ARG CA C 56.3 . 1 82 . 17 ARG HA H 3.95 . 1 83 . 17 ARG CB C 27.1 . 1 84 . 17 ARG HB2 H 1.08 . 2 85 . 17 ARG HB3 H 1.04 . 2 86 . 17 ARG CG C 26.9 . 1 87 . 17 ARG HG2 H 1.50 . 2 88 . 17 ARG HG3 H 1.37 . 2 89 . 17 ARG CD C 43.1 . 1 90 . 17 ARG HD2 H 3.08 . 2 91 . 17 ARG HD3 H 3.07 . 2 92 . 18 GLY N N 105.7 . 1 93 . 18 GLY H H 7.80 . 1 94 . 18 GLY CA C 44.7 . 1 95 . 18 GLY HA2 H 4.21 . 2 96 . 18 GLY HA3 H 3.74 . 2 97 . 19 TRP N N 118.5 . 1 98 . 19 TRP H H 7.12 . 1 99 . 19 TRP CA C 54.9 . 1 100 . 19 TRP HA H 4.94 . 1 101 . 19 TRP CB C 29.3 . 1 102 . 19 TRP HB2 H 2.87 . 2 103 . 19 TRP HB3 H 2.66 . 2 104 . 19 TRP CD1 C 124.5 . 1 105 . 19 TRP CE3 C 120.6 . 1 106 . 19 TRP NE1 N 127.9 . 1 107 . 19 TRP HD1 H 6.90 . 1 108 . 19 TRP HE3 H 7.11 . 1 109 . 19 TRP CZ3 C 120.6 . 1 110 . 19 TRP CZ2 C 113.6 . 1 111 . 19 TRP HE1 H 10.10 . 1 112 . 19 TRP HZ3 H 6.69 . 1 113 . 19 TRP CH2 C 122.7 . 1 114 . 19 TRP HZ2 H 7.34 . 1 115 . 19 TRP HH2 H 7.12 . 1 116 . 20 GLN N N 122.3 . 1 117 . 20 GLN H H 8.18 . 1 118 . 20 GLN CA C 53.5 . 1 119 . 20 GLN HA H 4.57 . 1 120 . 20 GLN CB C 31.2 . 1 121 . 20 GLN HB2 H 1.95 . 2 122 . 20 GLN HB3 H 2.17 . 2 123 . 20 GLN CG C 33.4 . 1 124 . 20 GLN HG2 H 2.38 . 2 125 . 20 GLN HG3 H 2.26 . 2 126 . 20 GLN HE21 H 7.83 . 2 127 . 20 GLN HE22 H 7.11 . 2 128 . 21 PRO CD C 50.5 . 1 129 . 21 PRO CA C 62.2 . 1 130 . 21 PRO HA H 5.25 . 1 131 . 21 PRO CB C 32.1 . 1 132 . 21 PRO HB2 H 2.08 . 2 133 . 21 PRO HB3 H 2.39 . 2 134 . 21 PRO CG C 28.0 . 1 135 . 21 PRO HG2 H 1.83 . 2 136 . 21 PRO HG3 H 2.21 . 2 137 . 21 PRO HD2 H 3.73 . 2 138 . 21 PRO HD3 H 3.90 . 2 139 . 22 VAL N N 117.6 . 1 140 . 22 VAL H H 8.51 . 1 141 . 22 VAL CA C 59.3 . 1 142 . 22 VAL HA H 4.43 . 1 143 . 22 VAL CB C 35.7 . 1 144 . 22 VAL HB H 1.60 . 1 145 . 22 VAL HG1 H 0.24 . 2 146 . 22 VAL HG2 H 0.42 . 2 147 . 22 VAL CG1 C 21.0 . 1 148 . 22 VAL CG2 C 18.8 . 1 149 . 23 GLU N N 117.5 . 1 150 . 23 GLU H H 7.53 . 1 151 . 23 GLU CA C 53.5 . 1 152 . 23 GLU HA H 4.63 . 1 153 . 23 GLU CB C 32.7 . 1 154 . 23 GLU HB2 H 2.12 . 2 155 . 23 GLU HB3 H 1.97 . 2 156 . 23 GLU CG C 36.3 . 1 157 . 23 GLU HG2 H 2.11 . 2 158 . 23 GLU HG3 H 2.21 . 2 159 . 24 ALA N N 124.9 . 1 160 . 24 ALA H H 9.30 . 1 161 . 24 ALA CA C 56.2 . 1 162 . 24 ALA HA H 3.94 . 1 163 . 24 ALA HB H 1.50 . 1 164 . 24 ALA CB C 17.8 . 1 165 . 25 SER CA C 60.0 . 1 166 . 25 SER HA H 4.36 . 1 167 . 25 SER CB C 63.0 . 1 168 . 25 SER HB2 H 4.06 . 2 169 . 25 SER HB3 H 3.92 . 2 170 . 26 THR N N 110.1 . 1 171 . 26 THR H H 7.58 . 1 172 . 26 THR CA C 61.1 . 1 173 . 26 THR HA H 4.90 . 1 174 . 26 THR CB C 70.1 . 1 175 . 26 THR HB H 4.69 . 1 176 . 26 THR HG2 H 1.18 . 1 177 . 26 THR CG2 C 22.2 . 1 178 . 27 VAL N N 123.3 . 1 179 . 27 VAL H H 7.57 . 1 180 . 27 VAL CA C 65.8 . 1 181 . 27 VAL HA H 3.83 . 1 182 . 27 VAL CB C 31.7 . 1 183 . 27 VAL HB H 2.10 . 1 184 . 27 VAL HG1 H 1.06 . 2 185 . 27 VAL HG2 H 1.00 . 2 186 . 27 VAL CG1 C 20.2 . 1 187 . 27 VAL CG2 C 23.6 . 1 188 . 28 ASP N N 121.1 . 1 189 . 28 ASP H H 8.54 . 1 190 . 28 ASP CA C 58.2 . 1 191 . 28 ASP HA H 4.37 . 1 192 . 28 ASP CB C 39.8 . 1 193 . 28 ASP HB2 H 2.56 . 2 194 . 28 ASP HB3 H 2.67 . 2 195 . 29 ASP N N 119.9 . 1 196 . 29 ASP H H 8.19 . 1 197 . 29 ASP CA C 57.0 . 1 198 . 29 ASP HA H 4.33 . 1 199 . 29 ASP CB C 40.8 . 1 200 . 29 ASP HB2 H 2.64 . 2 201 . 29 ASP HB3 H 2.72 . 2 202 . 30 TRP N N 122.2 . 1 203 . 30 TRP H H 7.88 . 1 204 . 30 TRP CA C 63.3 . 1 205 . 30 TRP HA H 3.95 . 1 206 . 30 TRP CB C 28.2 . 1 207 . 30 TRP HB2 H 3.21 . 2 208 . 30 TRP HB3 H 3.36 . 2 209 . 30 TRP CD1 C 125.7 . 1 210 . 30 TRP CE3 C 118.8 . 1 211 . 30 TRP NE1 N 129.0 . 1 212 . 30 TRP HD1 H 7.12 . 1 213 . 30 TRP HE3 H 6.98 . 1 214 . 30 TRP CZ3 C 120.5 . 1 215 . 30 TRP CZ2 C 114.2 . 1 216 . 30 TRP HE1 H 10.10 . 1 217 . 30 TRP HZ3 H 6.16 . 1 218 . 30 TRP CH2 C 124.0 . 1 219 . 30 TRP HZ2 H 6.94 . 1 220 . 30 TRP HH2 H 6.89 . 1 221 . 31 ILE N N 117.2 . 1 222 . 31 ILE H H 8.44 . 1 223 . 31 ILE CA C 64.2 . 1 224 . 31 ILE HA H 2.81 . 1 225 . 31 ILE CB C 38.2 . 1 226 . 31 ILE HB H 1.53 . 1 227 . 31 ILE HG2 H 0.38 . 1 228 . 31 ILE CG2 C 17.6 . 1 229 . 31 ILE CG1 C 27.9 . 1 230 . 31 ILE HG12 H 1.44 . 2 231 . 31 ILE HG13 H 0.00 . 2 232 . 31 ILE HD1 H 0.41 . 1 233 . 31 ILE CD1 C 15.5 . 1 234 . 32 LYS N N 116.3 . 1 235 . 32 LYS H H 7.42 . 1 236 . 32 LYS CA C 58.5 . 1 237 . 32 LYS HA H 3.83 . 1 238 . 32 LYS CB C 32.4 . 1 239 . 32 LYS HB2 H 1.79 . 2 240 . 32 LYS HB3 H 1.79 . 2 241 . 32 LYS CG C 24.9 . 1 242 . 32 LYS HG2 H 1.38 . 2 243 . 32 LYS HG3 H 1.46 . 2 244 . 32 LYS CD C 29.1 . 1 245 . 32 LYS HD2 H 1.64 . 2 246 . 32 LYS HD3 H 1.64 . 2 247 . 32 LYS CE C 42.0 . 1 248 . 32 LYS HE2 H 2.94 . 2 249 . 32 LYS HE3 H 2.94 . 2 250 . 33 ARG N N 117.6 . 1 251 . 33 ARG H H 7.50 . 1 252 . 33 ARG CA C 58.6 . 1 253 . 33 ARG HA H 3.94 . 1 254 . 33 ARG CB C 30.5 . 1 255 . 33 ARG HB2 H 1.78 . 2 256 . 33 ARG HB3 H 1.71 . 2 257 . 33 ARG CG C 27.5 . 1 258 . 33 ARG HG2 H 1.40 . 2 259 . 33 ARG HG3 H 1.54 . 2 260 . 33 ARG CD C 43.5 . 1 261 . 33 ARG HD2 H 3.16 . 2 262 . 33 ARG HD3 H 3.17 . 2 263 . 34 VAL N N 112.4 . 1 264 . 34 VAL H H 7.90 . 1 265 . 34 VAL CA C 62.7 . 1 266 . 34 VAL HA H 3.86 . 1 267 . 34 VAL CB C 31.5 . 1 268 . 34 VAL HB H 1.51 . 1 269 . 34 VAL HG1 H 0.01 . 2 270 . 34 VAL HG2 H -0.53 . 2 271 . 34 VAL CG1 C 19.9 . 1 272 . 34 VAL CG2 C 16.2 . 1 273 . 35 GLY N N 113.3 . 1 274 . 35 GLY H H 8.01 . 1 275 . 35 GLY CA C 47.2 . 1 276 . 35 GLY HA2 H 4.22 . 2 277 . 35 GLY HA3 H 3.16 . 2 278 . 36 ASP N N 126.0 . 1 279 . 36 ASP H H 8.08 . 1 280 . 36 ASP CA C 51.4 . 1 281 . 36 ASP HA H 5.31 . 1 282 . 36 ASP CB C 41.6 . 1 283 . 36 ASP HB2 H 1.72 . 2 284 . 36 ASP HB3 H 2.25 . 2 285 . 37 GLY N N 109.1 . 1 286 . 37 GLY H H 9.15 . 1 287 . 37 GLY CA C 47.0 . 1 288 . 37 GLY HA2 H 3.94 . 2 289 . 37 GLY HA3 H 5.42 . 2 290 . 38 VAL N N 111.4 . 1 291 . 38 VAL H H 8.56 . 1 292 . 38 VAL CA C 57.8 . 1 293 . 38 VAL HA H 5.91 . 1 294 . 38 VAL CB C 34.8 . 1 295 . 38 VAL HB H 1.80 . 1 296 . 38 VAL HG1 H 0.51 . 2 297 . 38 VAL HG2 H 0.54 . 2 298 . 38 VAL CG1 C 22.5 . 1 299 . 38 VAL CG2 C 20.5 . 1 300 . 39 ILE N N 118.1 . 1 301 . 39 ILE H H 8.54 . 1 302 . 39 ILE CA C 59.4 . 1 303 . 39 ILE HA H 4.60 . 1 304 . 39 ILE CB C 41.0 . 1 305 . 39 ILE HB H 1.54 . 1 306 . 39 ILE HG2 H 0.40 . 1 307 . 39 ILE CG2 C 16.7 . 1 308 . 39 ILE CG1 C 26.9 . 1 309 . 39 ILE HG12 H 1.48 . 2 310 . 39 ILE HG13 H 1.56 . 2 311 . 39 ILE HD1 H 0.58 . 1 312 . 39 ILE CD1 C 14.5 . 1 313 . 40 LEU N N 128.1 . 1 314 . 40 LEU H H 8.76 . 1 315 . 40 LEU CA C 55.7 . 1 316 . 40 LEU HA H 4.78 . 1 317 . 40 LEU CB C 41.6 . 1 318 . 40 LEU HB2 H 1.79 . 2 319 . 40 LEU HB3 H 1.64 . 2 320 . 40 LEU CG C 28.4 . 1 321 . 40 LEU HG H 1.58 . 1 322 . 40 LEU HD1 H 0.74 . 2 323 . 40 LEU HD2 H 0.59 . 2 324 . 40 LEU CD1 C 25.8 . 1 325 . 40 LEU CD2 C 25.7 . 1 326 . 41 LEU N N 124.8 . 1 327 . 41 LEU H H 9.31 . 1 328 . 41 LEU CA C 53.5 . 1 329 . 41 LEU HA H 4.88 . 1 330 . 41 LEU CB C 42.2 . 1 331 . 41 LEU HB2 H 1.14 . 2 332 . 41 LEU HB3 H 1.92 . 2 333 . 41 LEU CG C 26.8 . 1 334 . 41 LEU HG H 1.68 . 1 335 . 41 LEU HD1 H 0.87 . 2 336 . 41 LEU HD2 H 0.79 . 2 337 . 41 LEU CD1 C 25.9 . 1 338 . 41 LEU CD2 C 23.2 . 1 339 . 42 SER N N 119.0 . 1 340 . 42 SER H H 8.70 . 1 341 . 42 SER CA C 57.8 . 1 342 . 42 SER HA H 4.61 . 1 343 . 42 SER CB C 66.5 . 1 344 . 42 SER HB2 H 3.50 . 2 345 . 42 SER HB3 H 3.90 . 2 346 . 55 PRO CD C 50.3 . 1 347 . 55 PRO CA C 37.6 . 1 348 . 55 PRO HA H 4.21 . 1 349 . 55 PRO CB C 31.6 . 1 350 . 55 PRO HB2 H 2.24 . 2 351 . 55 PRO HB3 H 1.81 . 2 352 . 55 PRO CG C 28.9 . 1 353 . 55 PRO HG2 H 2.05 . 2 354 . 55 PRO HG3 H 1.95 . 2 355 . 55 PRO HD2 H 3.78 . 2 356 . 55 PRO HD3 H 3.78 . 2 357 . 56 VAL N N 114.7 . 1 358 . 56 VAL H H 7.09 . 1 359 . 56 VAL CA C 65.4 . 1 360 . 56 VAL HA H 3.72 . 1 361 . 56 VAL CB C 31.9 . 1 362 . 56 VAL HB H 2.14 . 1 363 . 56 VAL HG1 H 1.00 . 2 364 . 56 VAL HG2 H 0.94 . 2 365 . 56 VAL CG1 C 22.2 . 1 366 . 56 VAL CG2 C 21.0 . 1 367 . 57 MET N N 118.1 . 1 368 . 57 MET H H 7.57 . 1 369 . 57 MET CA C 56.5 . 1 370 . 57 MET HA H 4.39 . 1 371 . 57 MET CB C 31.6 . 1 372 . 57 MET HB2 H 1.99 . 2 373 . 57 MET HB3 H 1.87 . 2 374 . 57 MET CG C 43.2 . 1 375 . 57 MET HG2 H 3.18 . 2 376 . 57 MET HG3 H 3.15 . 2 377 . 58 ILE N N 117.9 . 1 378 . 58 ILE H H 8.32 . 1 379 . 58 ILE CA C 61.6 . 1 380 . 58 ILE HA H 3.78 . 1 381 . 58 ILE CB C 35.4 . 1 382 . 58 ILE HB H 2.02 . 1 383 . 58 ILE HG2 H 0.61 . 1 384 . 58 ILE CG2 C 17.5 . 1 385 . 58 ILE CG1 C 26.7 . 1 386 . 58 ILE HG12 H 1.60 . 2 387 . 58 ILE HG13 H 1.28 . 2 388 . 58 ILE HD1 H 0.58 . 1 389 . 58 ILE CD1 C 9.7 . 1 390 . 59 ALA N N 121.0 . 1 391 . 59 ALA H H 8.15 . 1 392 . 59 ALA CA C 55.6 . 1 393 . 59 ALA HA H 4.05 . 1 394 . 59 ALA HB H 1.67 . 1 395 . 59 ALA CB C 18.0 . 1 396 . 60 GLU N N 116.0 . 1 397 . 60 GLU H H 7.82 . 1 398 . 60 GLU CA C 59.1 . 1 399 . 60 GLU HA H 4.09 . 1 400 . 60 GLU CB C 29.3 . 1 401 . 60 GLU HB2 H 2.04 . 2 402 . 60 GLU HB3 H 2.18 . 2 403 . 60 GLU CG C 36.5 . 1 404 . 60 GLU HG2 H 2.24 . 2 405 . 60 GLU HG3 H 2.34 . 2 406 . 61 LEU N N 123.1 . 1 407 . 61 LEU H H 8.66 . 1 408 . 61 LEU CA C 58.2 . 1 409 . 61 LEU HA H 4.28 . 1 410 . 61 LEU CB C 42.8 . 1 411 . 61 LEU HB2 H 2.15 . 2 412 . 61 LEU HB3 H 1.73 . 2 413 . 61 LEU CG C 26.9 . 1 414 . 61 LEU HG H 1.44 . 1 415 . 61 LEU HD1 H 0.61 . 2 416 . 61 LEU HD2 H 0.61 . 2 417 . 61 LEU CD1 C 24.0 . 1 418 . 61 LEU CD2 C 23.9 . 1 419 . 62 LEU N N 114.8 . 1 420 . 62 LEU H H 8.18 . 1 421 . 62 LEU CA C 57.6 . 1 422 . 62 LEU HA H 3.75 . 1 423 . 62 LEU CB C 39.8 . 1 424 . 62 LEU HB2 H 1.64 . 2 425 . 62 LEU HB3 H 1.19 . 2 426 . 62 LEU CG C 24.9 . 1 427 . 62 LEU HG H 1.74 . 1 428 . 62 LEU HD1 H 0.32 . 2 429 . 62 LEU HD2 H 0.33 . 2 430 . 62 LEU CD1 C 24.7 . 1 431 . 62 LEU CD2 C 24.7 . 1 432 . 63 ARG N N 117.4 . 1 433 . 63 ARG H H 7.41 . 1 434 . 63 ARG CA C 58.4 . 1 435 . 63 ARG HA H 4.16 . 1 436 . 63 ARG CB C 30.2 . 1 437 . 63 ARG HB3 H 2.10 . 2 438 . 63 ARG CG C 27.8 . 1 439 . 63 ARG HG2 H 2.02 . 2 440 . 63 ARG HG3 H 1.77 . 2 441 . 63 ARG CD C 43.5 . 1 442 . 63 ARG HD2 H 3.30 . 2 443 . 63 ARG HD3 H 3.30 . 2 444 . 64 GLU N N 115.3 . 1 445 . 64 GLU H H 7.81 . 1 446 . 64 GLU CA C 56.0 . 1 447 . 64 GLU HA H 4.13 . 1 448 . 64 GLU CB C 29.2 . 1 449 . 64 GLU HB2 H 1.90 . 2 450 . 64 GLU HB3 H 2.10 . 2 451 . 64 GLU CG C 35.8 . 1 452 . 64 GLU HG2 H 2.45 . 2 453 . 64 GLU HG3 H 2.45 . 2 454 . 65 PHE N N 116.1 . 1 455 . 65 PHE H H 7.64 . 1 456 . 65 PHE CA C 56.1 . 1 457 . 65 PHE HA H 5.21 . 1 458 . 65 PHE CB C 40.8 . 1 459 . 65 PHE HB2 H 3.67 . 2 460 . 65 PHE HB3 H 3.25 . 2 461 . 65 PHE CD1 C 132.0 . 1 462 . 65 PHE HD1 H 7.47 . 1 463 . 65 PHE CE1 C 129.6 . 1 464 . 65 PHE HE1 H 7.32 . 1 465 . 65 PHE CZ C 130.5 . 1 466 . 65 PHE HZ H 7.13 . 1 467 . 65 PHE HE2 H 7.32 . 1 468 . 65 PHE CD2 C 132.0 . 1 469 . 65 PHE HD2 H 7.52 . 1 470 . 66 PRO CD C 22.0 . 1 471 . 66 PRO CA C 64.3 . 1 472 . 66 PRO HA H 4.47 . 1 473 . 66 PRO CB C 32.1 . 1 474 . 66 PRO HB2 H 2.42 . 2 475 . 66 PRO HB3 H 1.95 . 2 476 . 66 PRO CG C 27.2 . 1 477 . 66 PRO HG2 H 2.02 . 2 478 . 66 PRO HG3 H 2.03 . 2 479 . 66 PRO HD2 H 3.42 . 2 480 . 66 PRO HD3 H 3.65 . 2 481 . 67 GLN N N 121.3 . 1 482 . 67 GLN H H 9.67 . 1 483 . 67 GLN CA C 57.2 . 1 484 . 67 GLN HA H 4.02 . 1 485 . 67 GLN CB C 26.9 . 1 486 . 67 GLN HB2 H 1.74 . 2 487 . 67 GLN HB3 H 1.62 . 2 488 . 67 GLN CG C 29.9 . 1 489 . 67 GLN HG2 H 2.06 . 2 490 . 67 GLN HG3 H 2.05 . 2 491 . 67 GLN NE2 N 112.0 . 1 492 . 67 GLN HE21 H 7.62 . 2 493 . 67 GLN HE22 H 7.16 . 2 494 . 68 PHE N N 118.3 . 1 495 . 68 PHE H H 7.02 . 1 496 . 68 PHE CA C 55.9 . 1 497 . 68 PHE HA H 4.29 . 1 498 . 68 PHE CB C 39.4 . 1 499 . 68 PHE HB2 H 1.43 . 2 500 . 68 PHE HB3 H 0.98 . 2 501 . 68 PHE CD1 C 131.6 . 1 502 . 68 PHE HD1 H 6.99 . 1 503 . 68 PHE CE1 C 131.8 . 1 504 . 68 PHE HE1 H 6.77 . 1 505 . 68 PHE CZ C 130.4 . 1 506 . 68 PHE HZ H 7.25 . 1 507 . 68 PHE HE2 H 6.78 . 1 508 . 68 PHE CD2 C 131.6 . 1 509 . 68 PHE HD2 H 7.00 . 1 510 . 69 ASP N N 125.5 . 1 511 . 69 ASP H H 9.44 . 1 512 . 69 ASP CA C 52.0 . 1 513 . 69 ASP HA H 4.86 . 1 514 . 69 ASP CB C 39.2 . 1 515 . 69 ASP HB2 H 2.84 . 2 516 . 69 ASP HB3 H 2.42 . 2 517 . 70 TRP N N 117.6 . 1 518 . 70 TRP H H 6.94 . 1 519 . 70 TRP CA C 58.1 . 1 520 . 70 TRP HA H 4.14 . 1 521 . 70 TRP CB C 31.4 . 1 522 . 70 TRP HB2 H 2.99 . 2 523 . 70 TRP HB3 H 2.89 . 2 524 . 70 TRP CD1 C 128.8 . 1 525 . 70 TRP CE3 C 118.8 . 1 526 . 70 TRP NE1 N 128.9 . 1 527 . 70 TRP HD1 H 7.40 . 1 528 . 70 TRP HE3 H 6.96 . 1 529 . 70 TRP CZ3 C 122.3 . 1 530 . 70 TRP CZ2 C 113.8 . 1 531 . 70 TRP HE1 H 10.63 . 1 532 . 70 TRP HZ3 H 6.93 . 1 533 . 70 TRP CH2 C 123.2 . 1 534 . 70 TRP HZ2 H 6.77 . 1 535 . 70 TRP HH2 H 6.05 . 1 536 . 71 GLN N N 121.3 . 1 537 . 71 GLN H H 8.23 . 1 538 . 71 GLN CA C 54.9 . 1 539 . 71 GLN HA H 4.91 . 1 540 . 71 GLN CB C 31.4 . 1 541 . 71 GLN HB2 H 2.56 . 2 542 . 71 GLN HB3 H 1.73 . 2 543 . 71 GLN CG C 34.5 . 1 544 . 71 GLN HG2 H 2.57 . 2 545 . 71 GLN HG3 H 2.53 . 2 546 . 71 GLN NE2 N 114.8 . 1 547 . 71 GLN HE21 H 6.87 . 2 548 . 71 GLN HE22 H 7.75 . 2 549 . 72 VAL N N 119.9 . 1 550 . 72 VAL H H 8.36 . 1 551 . 72 VAL CA C 62.1 . 1 552 . 72 VAL HA H 4.61 . 1 553 . 72 VAL CB C 33.3 . 1 554 . 72 VAL HB H 0.55 . 1 555 . 72 VAL HG1 H -0.62 . 2 556 . 72 VAL HG2 H 0.20 . 2 557 . 72 VAL CG1 C 21.1 . 1 558 . 72 VAL CG2 C 19.9 . 1 559 . 73 ALA N N 130.5 . 1 560 . 73 ALA H H 8.80 . 1 561 . 73 ALA CA C 49.1 . 1 562 . 73 ALA HA H 5.25 . 1 563 . 73 ALA HB H 0.08 . 1 564 . 73 ALA CB C 21.9 . 1 565 . 74 VAL N N 110.8 . 1 566 . 74 VAL H H 8.21 . 1 567 . 74 VAL CA C 58.2 . 1 568 . 74 VAL HA H 4.88 . 1 569 . 74 VAL CB C 35.3 . 1 570 . 74 VAL HB H 2.21 . 1 571 . 74 VAL HG1 H 0.92 . 2 572 . 74 VAL HG2 H 0.34 . 2 573 . 74 VAL CG1 C 24.3 . 1 574 . 74 VAL CG2 C 18.3 . 1 575 . 75 ALA N N 122.2 . 1 576 . 75 ALA H H 7.35 . 1 577 . 75 ALA CA C 49.4 . 1 578 . 75 ALA HA H 5.46 . 1 579 . 75 ALA HB H 1.22 . 1 580 . 75 ALA CB C 22.9 . 1 581 . 76 ASP N N 124.6 . 1 582 . 76 ASP H H 9.30 . 1 583 . 76 ASP CA C 53.1 . 1 584 . 76 ASP HA H 4.02 . 1 585 . 76 ASP CB C 37.8 . 1 586 . 76 ASP HB2 H 2.61 . 2 587 . 76 ASP HB3 H 2.83 . 2 588 . 77 LEU N N 116.8 . 1 589 . 77 LEU H H 7.55 . 1 590 . 77 LEU CA C 59.1 . 1 591 . 77 LEU HA H 3.54 . 1 592 . 77 LEU CB C 40.1 . 1 593 . 77 LEU HB2 H 1.36 . 2 594 . 77 LEU HB3 H 1.07 . 2 595 . 77 LEU CG C 25.6 . 1 596 . 77 LEU HG H 0.42 . 1 597 . 77 LEU HD1 H 0.52 . 2 598 . 77 LEU HD2 H 0.00 . 2 599 . 77 LEU CD1 C 25.3 . 1 600 . 77 LEU CD2 C 22.4 . 1 601 . 78 GLU N N 120.1 . 1 602 . 78 GLU H H 7.83 . 1 603 . 78 GLU CA C 59.5 . 1 604 . 78 GLU HA H 4.03 . 1 605 . 78 GLU CB C 29.6 . 1 606 . 78 GLU HB2 H 1.94 . 2 607 . 78 GLU HB3 H 2.10 . 2 608 . 78 GLU CG C 36.6 . 1 609 . 78 GLU HG2 H 2.34 . 2 610 . 78 GLU HG3 H 2.18 . 2 611 . 79 GLN N N 119.4 . 1 612 . 79 GLN H H 9.62 . 1 613 . 79 GLN CA C 56.8 . 1 614 . 79 GLN HA H 4.17 . 1 615 . 79 GLN CB C 27.2 . 1 616 . 79 GLN HB2 H 2.17 . 2 617 . 79 GLN HB3 H 2.02 . 2 618 . 79 GLN CG C 33.3 . 1 619 . 79 GLN HG2 H 3.12 . 2 620 . 79 GLN HG3 H 2.69 . 2 621 . 79 GLN NE2 N 115.7 . 1 622 . 79 GLN HE21 H 6.97 . 2 623 . 79 GLN HE22 H 8.12 . 2 624 . 80 SER N N 117.3 . 1 625 . 80 SER H H 8.94 . 1 626 . 80 SER CA C 63.6 . 1 627 . 80 SER HA H 4.11 . 1 628 . 80 SER CB C 63.6 . 1 629 . 80 SER HB2 H 3.40 . 2 630 . 80 SER HB3 H 3.40 . 2 631 . 81 GLU N N 120.6 . 1 632 . 81 GLU H H 6.96 . 1 633 . 81 GLU CA C 59.6 . 1 634 . 81 GLU HA H 4.03 . 1 635 . 81 GLU CB C 29.4 . 1 636 . 81 GLU HB2 H 2.03 . 2 637 . 81 GLU HB3 H 2.02 . 2 638 . 81 GLU CG C 36.2 . 1 639 . 81 GLU HG2 H 2.08 . 2 640 . 81 GLU HG3 H 2.35 . 2 641 . 82 ALA N N 120.8 . 1 642 . 82 ALA H H 7.29 . 1 643 . 82 ALA CA C 55.1 . 1 644 . 82 ALA HA H 4.24 . 1 645 . 82 ALA HB H 1.49 . 1 646 . 82 ALA CB C 19.0 . 1 647 . 83 ILE N N 120.3 . 1 648 . 83 ILE H H 9.13 . 1 649 . 83 ILE CA C 65.6 . 1 650 . 83 ILE HA H 3.64 . 1 651 . 83 ILE CB C 38.3 . 1 652 . 83 ILE HB H 1.78 . 1 653 . 83 ILE HG2 H 1.02 . 1 654 . 83 ILE CG2 C 18.7 . 1 655 . 83 ILE CG1 C 30.0 . 1 656 . 83 ILE HG12 H 1.99 . 2 657 . 83 ILE HG13 H 0.83 . 2 658 . 83 ILE HD1 H 0.48 . 1 659 . 83 ILE CD1 C 13.7 . 1 660 . 84 GLY N N 108.4 . 1 661 . 84 GLY H H 8.81 . 1 662 . 84 GLY CA C 48.1 . 1 663 . 84 GLY HA2 H 4.10 . 2 664 . 84 GLY HA3 H 3.69 . 2 665 . 85 ASP N N 120.7 . 1 666 . 85 ASP H H 8.22 . 1 667 . 85 ASP CA C 57.5 . 1 668 . 85 ASP HA H 4.38 . 1 669 . 85 ASP CB C 41.2 . 1 670 . 85 ASP HB2 H 2.86 . 2 671 . 85 ASP HB3 H 2.65 . 2 672 . 86 ARG N N 119.3 . 1 673 . 86 ARG H H 7.36 . 1 674 . 86 ARG CA C 58.6 . 1 675 . 86 ARG HA H 3.90 . 1 676 . 86 ARG CB C 29.4 . 1 677 . 86 ARG HB2 H 1.75 . 2 678 . 86 ARG HB3 H 1.81 . 2 679 . 86 ARG CG C 26.5 . 1 680 . 86 ARG HG2 H 1.27 . 2 681 . 86 ARG HG3 H 0.58 . 2 682 . 86 ARG CD C 43.6 . 1 683 . 86 ARG HD2 H 2.92 . 2 684 . 86 ARG HD3 H 2.56 . 2 685 . 87 PHE N N 114.1 . 1 686 . 87 PHE H H 7.61 . 1 687 . 87 PHE CA C 58.1 . 1 688 . 87 PHE HA H 4.63 . 1 689 . 87 PHE CB C 39.0 . 1 690 . 87 PHE HB2 H 3.48 . 2 691 . 87 PHE HB3 H 2.47 . 2 692 . 87 PHE CD1 C 131.9 . 1 693 . 87 PHE HD1 H 7.51 . 1 694 . 87 PHE HE1 H 7.31 . 1 695 . 87 PHE CZ C 130.0 . 1 696 . 87 PHE HZ H 7.24 . 1 697 . 87 PHE CE2 C 129.6 . 1 698 . 87 PHE HE2 H 7.32 . 1 699 . 87 PHE CD2 C 131.8 . 1 700 . 87 PHE HD2 H 7.45 . 1 701 . 88 ASN N N 116.2 . 1 702 . 88 ASN H H 7.83 . 1 703 . 88 ASN CA C 54.4 . 1 704 . 88 ASN HA H 4.25 . 1 705 . 88 ASN CB C 37.1 . 1 706 . 88 ASN HB2 H 2.71 . 2 707 . 88 ASN HB3 H 3.12 . 2 708 . 88 ASN ND2 N 32.2 . 1 709 . 88 ASN HD21 H 7.81 . 2 710 . 88 ASN HD22 H 7.19 . 2 711 . 89 VAL N N 119.6 . 1 712 . 89 VAL H H 8.73 . 1 713 . 89 VAL CA C 62.6 . 1 714 . 89 VAL HA H 3.82 . 1 715 . 89 VAL CB C 32.7 . 1 716 . 89 VAL HB H 1.66 . 1 717 . 89 VAL HG1 H 0.68 . 2 718 . 89 VAL HG2 H 0.47 . 2 719 . 89 VAL CG1 C 21.1 . 1 720 . 89 VAL CG2 C 21.8 . 1 721 . 93 PRO CD C 50.4 . 1 722 . 93 PRO CB C 35.7 . 1 723 . 93 PRO HB2 H 2.37 . 2 724 . 93 PRO HB3 H 2.52 . 2 725 . 93 PRO CG C 24.5 . 1 726 . 93 PRO HG2 H 1.73 . 2 727 . 93 PRO HG3 H 1.73 . 2 728 . 93 PRO HD2 H 3.29 . 2 729 . 93 PRO HD3 H 3.65 . 2 730 . 94 ALA N N 121.2 . 1 731 . 94 ALA H H 8.51 . 1 732 . 94 ALA CA C 51.2 . 1 733 . 94 ALA HA H 5.32 . 1 734 . 94 ALA HB H 1.38 . 1 735 . 94 ALA CB C 24.2 . 1 736 . 95 THR N N 117.4 . 1 737 . 95 THR H H 8.80 . 1 738 . 95 THR CA C 61.4 . 1 739 . 95 THR HA H 5.11 . 1 740 . 95 THR CB C 70.7 . 1 741 . 95 THR HB H 3.71 . 1 742 . 95 THR HG2 H 0.78 . 1 743 . 95 THR CG2 C 21.2 . 1 744 . 96 LEU N N 126.8 . 1 745 . 96 LEU H H 9.14 . 1 746 . 96 LEU CA C 53.9 . 1 747 . 96 LEU HA H 4.47 . 1 748 . 96 LEU CB C 43.8 . 1 749 . 96 LEU HB2 H 1.71 . 2 750 . 96 LEU HB3 H 1.06 . 2 751 . 96 LEU CG C 40.6 . 1 752 . 96 LEU HG H 1.52 . 1 753 . 96 LEU HD1 H 0.56 . 2 754 . 96 LEU HD2 H 0.56 . 2 755 . 96 LEU CD1 C 23.1 . 1 756 . 96 LEU CD2 C 23.2 . 1 757 . 97 VAL N N 120.8 . 1 758 . 97 VAL H H 8.05 . 1 759 . 97 VAL CA C 62.3 . 1 760 . 97 VAL HA H 4.32 . 1 761 . 97 VAL CB C 33.4 . 1 762 . 97 VAL HB H 1.58 . 1 763 . 97 VAL HG1 H 0.60 . 2 764 . 97 VAL HG2 H 0.49 . 2 765 . 97 VAL CG1 C 21.0 . 1 766 . 97 VAL CG2 C 19.5 . 1 767 . 98 PHE N N 127.2 . 1 768 . 98 PHE H H 9.45 . 1 769 . 98 PHE CA C 56.1 . 1 770 . 98 PHE HA H 5.41 . 1 771 . 98 PHE CB C 41.2 . 1 772 . 98 PHE HB2 H 2.89 . 2 773 . 98 PHE HB3 H 2.45 . 2 774 . 98 PHE CD1 C 131.0 . 1 775 . 98 PHE HD1 H 6.84 . 1 776 . 98 PHE CE1 C 130.8 . 1 777 . 98 PHE HE1 H 6.94 . 1 778 . 98 PHE CZ C 128.5 . 1 779 . 98 PHE HZ H 6.35 . 1 780 . 98 PHE CE2 C 130.8 . 1 781 . 98 PHE HE2 H 6.82 . 1 782 . 98 PHE HD2 H 6.82 . 1 783 . 99 THR N N 109.8 . 1 784 . 99 THR H H 8.35 . 1 785 . 99 THR CA C 60.1 . 1 786 . 99 THR HA H 5.20 . 1 787 . 99 THR CB C 71.4 . 1 788 . 99 THR HB H 3.98 . 1 789 . 99 THR HG2 H 0.39 . 1 790 . 99 THR CG2 C 22.2 . 1 791 . 100 ASP N N 123.1 . 1 792 . 100 ASP H H 8.92 . 1 793 . 100 ASP CA C 55.1 . 1 794 . 100 ASP HA H 4.29 . 1 795 . 100 ASP CB C 41.0 . 1 796 . 100 ASP HB2 H 2.93 . 2 797 . 100 ASP HB3 H 2.58 . 2 798 . 101 GLY N N 103.7 . 1 799 . 101 GLY H H 9.69 . 1 800 . 101 GLY CA C 45.4 . 1 801 . 101 GLY HA2 H 4.03 . 2 802 . 101 GLY HA3 H 3.42 . 2 803 . 102 LYS N N 119.9 . 1 804 . 102 LYS H H 8.03 . 1 805 . 102 LYS CA C 54.6 . 1 806 . 102 LYS HA H 4.71 . 1 807 . 102 LYS CB C 35.1 . 1 808 . 102 LYS HB2 H 1.78 . 2 809 . 102 LYS HB3 H 1.72 . 2 810 . 102 LYS CG C 24.4 . 1 811 . 102 LYS HG2 H 1.41 . 2 812 . 102 LYS HG3 H 1.41 . 2 813 . 102 LYS CD C 29.1 . 1 814 . 102 LYS HD2 H 1.69 . 2 815 . 102 LYS HD3 H 1.63 . 2 816 . 102 LYS CE C 42.4 . 1 817 . 102 LYS HE2 H 3.03 . 2 818 . 102 LYS HE3 H 2.93 . 2 819 . 103 LEU N N 123.6 . 1 820 . 103 LEU H H 8.76 . 1 821 . 103 LEU CA C 55.8 . 1 822 . 103 LEU HA H 3.54 . 1 823 . 103 LEU CB C 40.9 . 1 824 . 103 LEU HB2 H 1.73 . 2 825 . 103 LEU HB3 H 1.23 . 2 826 . 103 LEU CG C 26.9 . 1 827 . 103 LEU HG H 1.04 . 1 828 . 103 LEU HD1 H 0.09 . 2 829 . 103 LEU HD2 H 0.82 . 2 830 . 103 LEU CD1 C 22.7 . 1 831 . 103 LEU CD2 C 26.6 . 1 832 . 104 ARG N N 126.6 . 1 833 . 104 ARG H H 9.45 . 1 834 . 104 ARG CA C 53.5 . 1 835 . 104 ARG HA H 4.46 . 1 836 . 104 ARG CB C 30.6 . 1 837 . 104 ARG HB2 H 1.92 . 2 838 . 104 ARG HB3 H 1.28 . 2 839 . 104 ARG CG C 25.5 . 1 840 . 104 ARG HG2 H 1.72 . 2 841 . 104 ARG HG3 H 1.72 . 2 842 . 104 ARG CD C 41.6 . 1 843 . 104 ARG HD2 H 3.00 . 2 844 . 104 ARG HD3 H 3.00 . 2 845 . 105 GLY N N 103.9 . 1 846 . 105 GLY H H 7.16 . 1 847 . 105 GLY CA C 44.6 . 1 848 . 105 GLY HA2 H 3.92 . 2 849 . 105 GLY HA3 H 3.79 . 2 850 . 106 ALA N N 119.8 . 1 851 . 106 ALA H H 8.32 . 1 852 . 106 ALA CA C 50.2 . 1 853 . 106 ALA HA H 5.19 . 1 854 . 106 ALA HB H 1.07 . 1 855 . 106 ALA CB C 22.0 . 1 856 . 107 LEU N N 123.1 . 1 857 . 107 LEU H H 8.89 . 1 858 . 107 LEU CA C 53.0 . 1 859 . 107 LEU HA H 4.50 . 1 860 . 107 LEU CB C 42.5 . 1 861 . 107 LEU HB2 H 1.25 . 2 862 . 107 LEU HB3 H 1.63 . 2 863 . 107 LEU CG C 26.9 . 1 864 . 107 LEU HG H 1.59 . 1 865 . 107 LEU HD1 H 0.55 . 2 866 . 107 LEU HD2 H 0.55 . 2 867 . 107 LEU CD1 C 24.5 . 1 868 . 107 LEU CD2 C 24.5 . 1 869 . 110 ILE N N 124.7 . 1 870 . 110 ILE H H 8.03 . 1 871 . 110 ILE CA C 30.9 . 1 872 . 110 ILE HA H 4.14 . 1 873 . 110 ILE CB C 38.1 . 1 874 . 110 ILE HB H 1.67 . 1 875 . 110 ILE HG2 H 0.76 . 1 876 . 110 ILE CG2 C 46.1 . 1 877 . 110 ILE CG1 C 26.9 . 1 878 . 110 ILE HG12 H 1.10 . 2 879 . 110 ILE HG13 H 1.30 . 2 880 . 110 ILE HD1 H 0.72 . 1 881 . 110 ILE CD1 C 41.0 . 1 882 . 113 TRP CA C 60.9 . 1 883 . 113 TRP HA H 4.35 . 1 884 . 113 TRP CB C 1.6 . 1 885 . 113 TRP HB2 H 3.44 . 2 886 . 113 TRP HB3 H 3.12 . 2 887 . 113 TRP CD1 C 126.5 . 1 888 . 113 TRP CE3 C 120.4 . 1 889 . 113 TRP NE1 N 129.0 . 1 890 . 113 TRP HD1 H 7.16 . 1 891 . 113 TRP HE3 H 7.57 . 1 892 . 113 TRP CZ3 C 120.3 . 1 893 . 113 TRP CZ2 C 114.2 . 1 894 . 113 TRP HE1 H 10.16 . 1 895 . 113 TRP HZ3 H 7.12 . 1 896 . 113 TRP CH2 C 123.4 . 1 897 . 113 TRP HZ2 H 7.42 . 1 898 . 113 TRP HH2 H 6.99 . 1 899 . 114 ALA N N 116.3 . 1 900 . 114 ALA H H 8.88 . 1 901 . 114 ALA CA C 55.4 . 1 902 . 114 ALA HA H 3.75 . 1 903 . 114 ALA HB H 1.44 . 1 904 . 114 ALA CB C 18.2 . 1 905 . 115 GLU N N 116.1 . 1 906 . 115 GLU H H 7.28 . 1 907 . 115 GLU CA C 58.3 . 1 908 . 115 GLU HA H 4.06 . 1 909 . 115 GLU CB C 29.9 . 1 910 . 115 GLU HB2 H 2.03 . 2 911 . 115 GLU HB3 H 2.03 . 2 912 . 115 GLU CG C 36.2 . 1 913 . 115 GLU HG2 H 2.31 . 2 914 . 115 GLU HG3 H 2.26 . 2 915 . 116 LEU N N 122.2 . 1 916 . 116 LEU H H 8.31 . 1 917 . 116 LEU CA C 58.0 . 1 918 . 116 LEU HA H 3.64 . 1 919 . 116 LEU CB C 41.9 . 1 920 . 116 LEU HB2 H 1.64 . 2 921 . 116 LEU HB3 H 1.46 . 2 922 . 116 LEU CG C 26.2 . 1 923 . 116 LEU HG H 1.44 . 1 924 . 116 LEU HD1 H 0.87 . 2 925 . 116 LEU HD2 H 0.60 . 2 926 . 116 LEU CD1 C 24.4 . 1 927 . 116 LEU CD2 C 23.9 . 1 928 . 117 LEU N N 117.3 . 1 929 . 117 LEU H H 7.95 . 1 930 . 117 LEU CA C 58.1 . 1 931 . 117 LEU HA H 3.63 . 1 932 . 117 LEU CB C 41.4 . 1 933 . 117 LEU HB2 H 1.30 . 2 934 . 117 LEU HB3 H 0.97 . 2 935 . 117 LEU CG C 26.7 . 1 936 . 117 LEU HG H 1.02 . 1 937 . 117 LEU HD1 H 0.87 . 2 938 . 117 LEU HD2 H 0.61 . 2 939 . 117 LEU CD1 C 24.5 . 1 940 . 117 LEU CD2 C 24.1 . 1 941 . 118 THR N N 114.8 . 1 942 . 118 THR H H 7.31 . 1 943 . 118 THR CA C 66.5 . 1 944 . 118 THR HA H 3.76 . 1 945 . 118 THR CB C 68.6 . 1 946 . 118 THR HB H 4.18 . 1 947 . 118 THR HG2 H 1.19 . 1 948 . 118 THR CG2 C 22.0 . 1 949 . 119 LEU N N 123.5 . 1 950 . 119 LEU H H 8.23 . 1 951 . 119 LEU CA C 57.7 . 1 952 . 119 LEU HA H 3.93 . 1 953 . 119 LEU CB C 41.8 . 1 954 . 119 LEU HB2 H 1.63 . 2 955 . 119 LEU HB3 H 1.21 . 2 956 . 119 LEU CG C 26.5 . 1 957 . 119 LEU HG H 1.47 . 1 958 . 119 LEU HD1 H 0.32 . 2 959 . 119 LEU HD2 H 0.66 . 2 960 . 119 LEU CD1 C 23.8 . 1 961 . 119 LEU CD2 C 23.0 . 1 962 . 120 MET N N 119.6 . 1 963 . 120 MET H H 8.52 . 1 964 . 120 MET CA C 57.5 . 1 965 . 120 MET HA H 3.79 . 1 966 . 120 MET CB C 32.5 . 1 967 . 120 MET HB2 H 1.73 . 2 968 . 120 MET HB3 H 1.72 . 2 969 . 120 MET CG C 31.9 . 1 970 . 120 MET HG2 H 2.08 . 2 971 . 120 MET HG3 H 1.99 . 2 972 . 121 ARG N N 118.6 . 1 973 . 121 ARG H H 8.47 . 1 974 . 121 ARG CA C 60.2 . 1 975 . 121 ARG HA H 3.93 . 1 976 . 121 ARG CB C 29.8 . 1 977 . 121 ARG HB2 H 2.00 . 2 978 . 121 ARG HB3 H 2.00 . 2 979 . 121 ARG CG C 28.3 . 1 980 . 121 ARG HG2 H 1.86 . 2 981 . 121 ARG HG3 H 2.02 . 2 982 . 121 ARG CD C 43.6 . 1 983 . 121 ARG HD2 H 3.27 . 2 984 . 121 ARG HD3 H 3.17 . 2 985 . 122 SER N N 112.1 . 1 986 . 122 SER H H 7.61 . 1 987 . 122 SER CA C 61.0 . 1 988 . 122 SER HA H 4.26 . 1 989 . 122 SER CB C 63.0 . 1 990 . 122 SER HB2 H 3.95 . 2 991 . 122 SER HB3 H 3.95 . 2 992 . 123 ILE N N 120.2 . 1 993 . 123 ILE H H 7.47 . 1 994 . 123 ILE CA C 64.3 . 1 995 . 123 ILE HA H 3.83 . 1 996 . 123 ILE CB C 38.3 . 1 997 . 123 ILE HB H 1.82 . 1 998 . 123 ILE HG2 H 0.49 . 1 999 . 123 ILE CG2 C 17.6 . 1 1000 . 123 ILE CG1 C 28.5 . 1 1001 . 123 ILE HG12 H 1.67 . 2 1002 . 123 ILE HG13 H 0.87 . 2 1003 . 123 ILE HD1 H 0.44 . 1 1004 . 123 ILE CD1 C 13.5 . 1 1005 . 124 VAL N N 111.9 . 1 1006 . 124 VAL H H 7.81 . 1 1007 . 124 VAL CA C 63.1 . 1 1008 . 124 VAL HA H 4.03 . 1 1009 . 124 VAL CB C 32.2 . 1 1010 . 124 VAL HB H 2.19 . 1 1011 . 124 VAL HG1 H 0.76 . 2 1012 . 124 VAL HG2 H 0.76 . 2 1013 . 124 VAL CG1 C 22.2 . 1 1014 . 124 VAL CG2 C 20.2 . 1 1015 . 125 ASP N N 121.3 . 1 1016 . 125 ASP H H 8.05 . 1 1017 . 125 ASP CA C 54.3 . 1 1018 . 125 ASP HA H 4.49 . 1 1019 . 125 ASP CB C 40.9 . 1 1020 . 125 ASP HB2 H 2.80 . 2 1021 . 125 ASP HB3 H 2.72 . 2 1022 . 126 THR N N 116.3 . 1 1023 . 126 THR H H 7.84 . 1 1024 . 126 THR CA C 60.2 . 1 1025 . 126 THR HA H 4.55 . 1 1026 . 126 THR CB C 70.0 . 1 1027 . 126 THR HB H 4.15 . 1 1028 . 126 THR HG2 H 1.25 . 1 1029 . 126 THR CG2 C 21.1 . 1 1030 . 127 PRO CD C 50.9 . 1 1031 . 127 PRO CA C 63.0 . 1 1032 . 127 PRO HA H 4.39 . 1 1033 . 127 PRO CB C 32.2 . 1 1034 . 127 PRO HB2 H 2.29 . 2 1035 . 127 PRO HB3 H 1.88 . 2 1036 . 127 PRO CG C 27.3 . 1 1037 . 127 PRO HG2 H 2.02 . 2 1038 . 127 PRO HG3 H 1.97 . 2 1039 . 127 PRO HD2 H 3.67 . 2 1040 . 127 PRO HD3 H 3.84 . 2 stop_ save_