data_15642 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the aminoterminal domain of E. coli NusG ; _BMRB_accession_number 15642 _BMRB_flat_file_name bmr15642.str _Entry_type original _Submission_date 2008-01-25 _Accession_date 2008-01-25 _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 Schweimer Kristian . . 2 Scheckenhofer Ulrich . . 3 Roesch Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 662 "13C chemical shifts" 498 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-27 update BMRB 'complete entry citation' 2009-06-10 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19500594 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mooney 'Rachel Anne' . . 2 Schweimer Kristian . . 3 Roesch Paul . . 4 Gottesman Max . . 5 Landick Robert . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 391 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 341 _Page_last 358 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NusG _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NusG $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 NusG _Molecular_mass 14096.366 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; MSEAPKKRWYVVQAFSGFEG RVATSLREHIKLHNMEDLFG EVMVPTEEVVEIRGGQRRKS ERKFFPGYVLVQMVMNDASW HLVRSVPRVMGFIGGTSDRP APISDKEVDAIMNRLQQVGD KPR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLU 4 ALA 5 PRO 6 LYS 7 LYS 8 ARG 9 TRP 10 TYR 11 VAL 12 VAL 13 GLN 14 ALA 15 PHE 16 SER 17 GLY 18 PHE 19 GLU 20 GLY 21 ARG 22 VAL 23 ALA 24 THR 25 SER 26 LEU 27 ARG 28 GLU 29 HIS 30 ILE 31 LYS 32 LEU 33 HIS 34 ASN 35 MET 36 GLU 37 ASP 38 LEU 39 PHE 40 GLY 41 GLU 42 VAL 43 MET 44 VAL 45 PRO 46 THR 47 GLU 48 GLU 49 VAL 50 VAL 51 GLU 52 ILE 53 ARG 54 GLY 55 GLY 56 GLN 57 ARG 58 ARG 59 LYS 60 SER 61 GLU 62 ARG 63 LYS 64 PHE 65 PHE 66 PRO 67 GLY 68 TYR 69 VAL 70 LEU 71 VAL 72 GLN 73 MET 74 VAL 75 MET 76 ASN 77 ASP 78 ALA 79 SER 80 TRP 81 HIS 82 LEU 83 VAL 84 ARG 85 SER 86 VAL 87 PRO 88 ARG 89 VAL 90 MET 91 GLY 92 PHE 93 ILE 94 GLY 95 GLY 96 THR 97 SER 98 ASP 99 ARG 100 PRO 101 ALA 102 PRO 103 ILE 104 SER 105 ASP 106 LYS 107 GLU 108 VAL 109 ASP 110 ALA 111 ILE 112 MET 113 ASN 114 ARG 115 LEU 116 GLN 117 GLN 118 VAL 119 GLY 120 ASP 121 LYS 122 PRO 123 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 15490 NusG 100.00 181 100.00 100.00 3.58e-83 PDB 2JVV "Solution Structure Of E. Coli Nusg Carboxyterminal Domain" 100.00 181 100.00 100.00 3.58e-83 PDB 2K06 "Solution Structure Of The Aminoterminal Domain Of E. Coli Nusg" 100.00 123 100.00 100.00 1.25e-83 DBJ BAB38328 "component in transcription antitermination [Escherichia coli O157:H7 str. Sakai]" 100.00 181 100.00 100.00 3.58e-83 DBJ BAE73404 "transcription antitermination protein [Sodalis glossinidius str. 'morsitans']" 100.00 181 97.56 99.19 1.66e-80 DBJ BAE77338 "transcription termination factor [Escherichia coli str. K12 substr. W3110]" 100.00 181 100.00 100.00 3.58e-83 DBJ BAG79793 "transcription antitermination protein [Escherichia coli SE11]" 100.00 181 100.00 100.00 3.58e-83 DBJ BAH61119 "transcription antitermination protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 181 99.19 100.00 1.74e-82 EMBL CAD09492 "transcription antitermination protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 181 99.19 100.00 1.74e-82 EMBL CAG73137 "transcription antitermination protein [Pectobacterium atrosepticum SCRI1043]" 100.00 181 97.56 98.37 2.15e-80 EMBL CAH19518 "transcription antitermination protein [Yersinia pseudotuberculosis IP 32953]" 100.00 181 97.56 99.19 1.03e-80 EMBL CAL10413 "transcription antitermination protein [Yersinia enterocolitica subsp. enterocolitica 8081]" 100.00 181 97.56 99.19 1.03e-80 EMBL CAL22339 "transcription antitermination protein [Yersinia pestis CO92]" 100.00 181 97.56 99.19 1.03e-80 GB AAA24622 "NusG protein [Escherichia coli]" 100.00 181 100.00 100.00 3.58e-83 GB AAC43080 "ORF_o181 [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 3.58e-83 GB AAC76956 "transcription termination factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 3.58e-83 GB AAF33495 "99% identity over 181 amino acids with E. coli transcription antitermination factor (NUSG) (SW:P16921) [Salmonella enterica sub" 100.00 181 99.19 100.00 1.74e-82 GB AAG59178 "component in transcription antitermination [Escherichia coli O157:H7 str. EDL933]" 100.00 181 100.00 100.00 3.58e-83 PIR AB0934 "transcription antitermination protein STY3737 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 181 99.19 100.00 1.74e-82 REF NP_312932 "transcription antitermination protein NusG [Escherichia coli O157:H7 str. Sakai]" 100.00 181 100.00 100.00 3.58e-83 REF NP_418409 "transcription termination factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 3.58e-83 REF NP_457922 "transcription antitermination protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 181 99.19 100.00 1.74e-82 REF NP_463017 "transcription termination/antitermination protein NusG [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 181 99.19 100.00 1.74e-82 REF NP_709777 "transcription antitermination protein NusG [Shigella flexneri 2a str. 301]" 100.00 181 100.00 100.00 3.58e-83 SP P0AA01 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.19 100.00 1.74e-82 SP P0AA02 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.19 100.00 1.74e-82 SP P0AA03 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.19 100.00 1.74e-82 SP P0AFG0 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 100.00 100.00 3.58e-83 SP P0AFG1 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 100.00 100.00 3.58e-83 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 . 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity 'recombinant technology' . Escherichia coli BL21(DE3) pET11a 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 0.4 mM '[U-98% 13C; U-98% 15N]' 'potassium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' D2O 10 % '[U-100% 2H]' H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' 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 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_9 _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 . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' 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 NusG _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 MET C C 175.21 . 1 2 2 2 SER H H 7.89 . 1 3 2 2 SER HA H 4.27 . 1 4 2 2 SER C C 173.96 . 1 5 2 2 SER CA C 60.80 . 1 6 2 2 SER N N 111.94 . 1 7 3 3 GLU H H 8.01 . 1 8 3 3 GLU HA H 4.36 . 1 9 3 3 GLU C C 175.71 . 1 10 3 3 GLU CA C 56.31 . 1 11 3 3 GLU N N 121.28 . 1 12 4 4 ALA H H 8.54 . 1 13 4 4 ALA HA H 4.56 . 1 14 4 4 ALA CA C 50.63 . 1 15 4 4 ALA N N 127.84 . 1 16 5 5 PRO HA H 4.42 . 1 17 5 5 PRO C C 174.24 . 1 18 5 5 PRO CA C 62.84 . 1 19 6 6 LYS H H 8.32 . 1 20 6 6 LYS HA H 4.29 . 1 21 6 6 LYS C C 176.10 . 1 22 6 6 LYS CA C 55.54 . 1 23 6 6 LYS N N 121.91 . 1 24 7 7 LYS H H 8.45 . 1 25 7 7 LYS HA H 3.94 . 1 26 7 7 LYS C C 175.70 . 1 27 7 7 LYS CA C 56.44 . 1 28 7 7 LYS N N 122.25 . 1 29 8 8 ARG H H 8.21 . 1 30 8 8 ARG HA H 4.67 . 1 31 8 8 ARG C C 173.76 . 1 32 8 8 ARG CA C 53.42 . 1 33 8 8 ARG N N 122.56 . 1 34 9 9 TRP H H 8.61 . 1 35 9 9 TRP HA H 4.91 . 1 36 9 9 TRP HB2 H 2.67 . 2 37 9 9 TRP HB3 H 3.05 . 2 38 9 9 TRP HD1 H 7.32 . 1 39 9 9 TRP HE1 H 10.17 . 1 40 9 9 TRP HE3 H 7.30 . 1 41 9 9 TRP HH2 H 6.94 . 1 42 9 9 TRP HZ2 H 7.35 . 1 43 9 9 TRP HZ3 H 6.81 . 1 44 9 9 TRP C C 174.61 . 1 45 9 9 TRP CA C 57.63 . 1 46 9 9 TRP CB C 31.02 . 1 47 9 9 TRP CD1 C 127.60 . 1 48 9 9 TRP CE3 C 120.10 . 1 49 9 9 TRP CH2 C 124.90 . 1 50 9 9 TRP CZ2 C 114.40 . 1 51 9 9 TRP CZ3 C 122.20 . 1 52 9 9 TRP N N 120.54 . 1 53 9 9 TRP NE1 N 128.60 . 1 54 10 10 TYR H H 9.26 . 1 55 10 10 TYR HA H 4.82 . 1 56 10 10 TYR HB2 H 2.86 . 2 57 10 10 TYR HB3 H 3.29 . 2 58 10 10 TYR HD1 H 7.06 . 1 59 10 10 TYR HD2 H 7.06 . 1 60 10 10 TYR HE1 H 6.58 . 1 61 10 10 TYR HE2 H 6.58 . 1 62 10 10 TYR C C 174.34 . 1 63 10 10 TYR CA C 57.05 . 1 64 10 10 TYR CB C 41.92 . 1 65 10 10 TYR CD1 C 134.20 . 1 66 10 10 TYR CD2 C 134.20 . 1 67 10 10 TYR CE1 C 117.50 . 1 68 10 10 TYR CE2 C 117.50 . 1 69 10 10 TYR N N 118.99 . 1 70 11 11 VAL H H 9.45 . 1 71 11 11 VAL HA H 4.47 . 1 72 11 11 VAL HB H 2.16 . 1 73 11 11 VAL HG1 H 0.29 . 2 74 11 11 VAL HG2 H 0.81 . 2 75 11 11 VAL C C 175.03 . 1 76 11 11 VAL CA C 62.32 . 1 77 11 11 VAL CB C 32.40 . 1 78 11 11 VAL CG1 C 22.50 . 2 79 11 11 VAL CG2 C 21.17 . 2 80 11 11 VAL N N 120.93 . 1 81 12 12 VAL H H 9.32 . 1 82 12 12 VAL HA H 3.94 . 1 83 12 12 VAL HB H 1.91 . 1 84 12 12 VAL HG1 H 0.45 . 2 85 12 12 VAL HG2 H 0.52 . 2 86 12 12 VAL C C 173.87 . 1 87 12 12 VAL CA C 61.33 . 1 88 12 12 VAL CB C 33.50 . 1 89 12 12 VAL CG1 C 21.90 . 2 90 12 12 VAL CG2 C 23.40 . 2 91 12 12 VAL N N 128.86 . 1 92 13 13 GLN H H 8.83 . 1 93 13 13 GLN HA H 4.71 . 1 94 13 13 GLN HB2 H 1.90 . 2 95 13 13 GLN HB3 H 1.90 . 2 96 13 13 GLN HE21 H 7.57 . 1 97 13 13 GLN HE22 H 6.79 . 1 98 13 13 GLN HG2 H 2.33 . 2 99 13 13 GLN HG3 H 2.33 . 2 100 13 13 GLN C C 174.23 . 1 101 13 13 GLN CA C 54.80 . 1 102 13 13 GLN CB C 29.45 . 1 103 13 13 GLN N N 126.05 . 1 104 13 13 GLN NE2 N 110.60 . 1 105 14 14 ALA H H 9.42 . 1 106 14 14 ALA HA H 5.15 . 1 107 14 14 ALA HB H 1.24 . 1 108 14 14 ALA C C 176.40 . 1 109 14 14 ALA CA C 49.66 . 1 110 14 14 ALA CB C 22.84 . 1 111 14 14 ALA N N 131.62 . 1 112 15 15 PHE H H 8.07 . 1 113 15 15 PHE HA H 4.41 . 1 114 15 15 PHE HB2 H 2.79 . 2 115 15 15 PHE HB3 H 3.19 . 2 116 15 15 PHE HD1 H 7.11 . 1 117 15 15 PHE HD2 H 7.11 . 1 118 15 15 PHE C C 176.13 . 1 119 15 15 PHE CA C 58.55 . 1 120 15 15 PHE CB C 39.78 . 1 121 15 15 PHE CD1 C 131.50 . 1 122 15 15 PHE CD2 C 131.50 . . 123 15 15 PHE N N 119.68 . 1 124 16 16 SER H H 8.37 . 1 125 16 16 SER HA H 4.14 . 1 126 16 16 SER HB2 H 3.85 . 2 127 16 16 SER HB3 H 3.85 . 2 128 16 16 SER C C 175.82 . 1 129 16 16 SER CA C 60.57 . 1 130 16 16 SER CB C 63.03 . 1 131 16 16 SER N N 119.70 . 1 132 17 17 GLY H H 9.13 . 1 133 17 17 GLY HA2 H 3.64 . 2 134 17 17 GLY HA3 H 4.20 . 2 135 17 17 GLY C C 175.52 . 1 136 17 17 GLY CA C 45.26 . 1 137 17 17 GLY N N 115.85 . 1 138 18 18 PHE H H 8.48 . 1 139 18 18 PHE HA H 4.74 . 1 140 18 18 PHE HB2 H 3.03 . 2 141 18 18 PHE HB3 H 3.46 . 2 142 18 18 PHE HD1 H 7.11 . 1 143 18 18 PHE HD2 H 7.11 . 1 144 18 18 PHE C C 175.43 . 1 145 18 18 PHE CA C 58.24 . 1 146 18 18 PHE CB C 39.01 . 1 147 18 18 PHE CD1 C 131.86 . 1 148 18 18 PHE CD2 C 131.86 . 1 149 18 18 PHE N N 118.55 . 1 150 19 19 GLU H H 10.69 . 1 151 19 19 GLU HA H 3.49 . 1 152 19 19 GLU HB2 H 2.06 . 2 153 19 19 GLU HB3 H 2.06 . 2 154 19 19 GLU HG2 H 2.80 . 2 155 19 19 GLU HG3 H 2.80 . 2 156 19 19 GLU C C 177.65 . 1 157 19 19 GLU CA C 62.28 . 1 158 19 19 GLU CB C 28.38 . 1 159 19 19 GLU CG C 36.58 . 1 160 19 19 GLU N N 123.47 . 1 161 20 20 GLY H H 8.74 . 1 162 20 20 GLY HA2 H 3.84 . 2 163 20 20 GLY HA3 H 3.94 . 2 164 20 20 GLY C C 176.86 . 1 165 20 20 GLY CA C 47.14 . 1 166 20 20 GLY N N 105.48 . 1 167 21 21 ARG H H 7.69 . 1 168 21 21 ARG HA H 4.18 . 1 169 21 21 ARG HB2 H 2.05 . 2 170 21 21 ARG HB3 H 2.12 . 2 171 21 21 ARG HD2 H 3.23 . 2 172 21 21 ARG HD3 H 3.30 . 2 173 21 21 ARG HG2 H 1.82 . 2 174 21 21 ARG HG3 H 1.93 . 2 175 21 21 ARG C C 179.49 . 1 176 21 21 ARG CA C 58.66 . 1 177 21 21 ARG CB C 30.10 . 1 178 21 21 ARG CD C 43.29 . 1 179 21 21 ARG CG C 27.39 . 1 180 21 21 ARG N N 123.12 . 1 181 22 22 VAL H H 8.98 . 1 182 22 22 VAL HA H 3.56 . 1 183 22 22 VAL HB H 2.15 . 1 184 22 22 VAL HG1 H 0.65 . 2 185 22 22 VAL HG2 H 1.13 . 2 186 22 22 VAL C C 177.32 . 1 187 22 22 VAL CA C 66.96 . 1 188 22 22 VAL CB C 31.05 . 1 189 22 22 VAL CG1 C 21.68 . 2 190 22 22 VAL CG2 C 25.03 . 2 191 22 22 VAL N N 122.76 . 1 192 23 23 ALA H H 8.28 . 1 193 23 23 ALA HA H 3.85 . 1 194 23 23 ALA HB H 1.46 . 1 195 23 23 ALA C C 179.34 . 1 196 23 23 ALA CA C 56.26 . 1 197 23 23 ALA CB C 18.26 . 1 198 23 23 ALA N N 122.12 . 1 199 24 24 THR H H 8.02 . 1 200 24 24 THR HA H 3.92 . 1 201 24 24 THR HB H 4.26 . 1 202 24 24 THR HG2 H 1.29 . 1 203 24 24 THR C C 176.94 . 1 204 24 24 THR CA C 66.82 . 1 205 24 24 THR CB C 68.93 . 1 206 24 24 THR CG2 C 22.06 . 1 207 24 24 THR N N 113.41 . 1 208 25 25 SER H H 8.57 . 1 209 25 25 SER HA H 4.40 . 1 210 25 25 SER HB2 H 3.82 . 2 211 25 25 SER HB3 H 3.98 . 2 212 25 25 SER C C 177.61 . 1 213 25 25 SER CA C 61.92 . 1 214 25 25 SER CB C 63.54 . 1 215 25 25 SER N N 118.26 . 1 216 26 26 LEU H H 9.43 . 1 217 26 26 LEU HA H 3.90 . 1 218 26 26 LEU HB2 H 1.81 . 2 219 26 26 LEU HB3 H 1.61 . 2 220 26 26 LEU HD1 H 0.80 . 2 221 26 26 LEU HD2 H 0.67 . 2 222 26 26 LEU HG H 1.46 . 1 223 26 26 LEU C C 177.71 . 1 224 26 26 LEU CA C 58.91 . 1 225 26 26 LEU CB C 41.30 . 1 226 26 26 LEU CD1 C 26.50 . 2 227 26 26 LEU CD2 C 25.00 . 2 228 26 26 LEU CG C 27.50 . 1 229 26 26 LEU N N 124.12 . 1 230 27 27 ARG H H 7.79 . 1 231 27 27 ARG HA H 3.88 . 1 232 27 27 ARG HB2 H 1.99 . 2 233 27 27 ARG HB3 H 2.10 . 2 234 27 27 ARG HD2 H 3.21 . 2 235 27 27 ARG HD3 H 3.28 . 2 236 27 27 ARG HG2 H 1.67 . 2 237 27 27 ARG HG3 H 1.97 . 2 238 27 27 ARG C C 179.38 . 1 239 27 27 ARG CA C 60.51 . 1 240 27 27 ARG CB C 29.67 . 1 241 27 27 ARG CD C 43.63 . 1 242 27 27 ARG CG C 28.49 . 1 243 27 27 ARG N N 116.71 . 1 244 28 28 GLU H H 7.90 . 1 245 28 28 GLU HA H 4.07 . 1 246 28 28 GLU HB2 H 2.14 . 2 247 28 28 GLU HB3 H 2.37 . 2 248 28 28 GLU HG2 H 2.23 . 2 249 28 28 GLU HG3 H 2.50 . 2 250 28 28 GLU C C 179.45 . 1 251 28 28 GLU CA C 59.45 . 1 252 28 28 GLU CB C 29.61 . 1 253 28 28 GLU CG C 36.23 . 1 254 28 28 GLU N N 118.34 . 1 255 29 29 HIS H H 8.94 . 1 256 29 29 HIS HA H 4.16 . 1 257 29 29 HIS HB2 H 2.93 . 2 258 29 29 HIS HB3 H 3.19 . 2 259 29 29 HIS HD2 H 7.05 . 1 260 29 29 HIS HE1 H 7.79 . 1 261 29 29 HIS C C 177.75 . 1 262 29 29 HIS CA C 61.26 . 1 263 29 29 HIS CB C 29.87 . 1 264 29 29 HIS CD2 C 122.60 . 1 265 29 29 HIS N N 120.44 . 1 266 30 30 ILE H H 8.58 . 1 267 30 30 ILE HA H 3.16 . 1 268 30 30 ILE HB H 1.61 . 1 269 30 30 ILE HD1 H 0.19 . 1 270 30 30 ILE HG12 H -0.49 . 2 271 30 30 ILE HG13 H 1.20 . 2 272 30 30 ILE HG2 H 0.65 . 1 273 30 30 ILE C C 177.23 . 1 274 30 30 ILE CA C 66.46 . 1 275 30 30 ILE CB C 38.63 . 1 276 30 30 ILE CD1 C 14.81 . 1 277 30 30 ILE CG1 C 28.97 . 1 278 30 30 ILE CG2 C 17.40 . 1 279 30 30 ILE N N 121.01 . 1 280 31 31 LYS H H 7.02 . 1 281 31 31 LYS HA H 4.17 . 1 282 31 31 LYS HB2 H 1.92 . 2 283 31 31 LYS HB3 H 1.92 . 2 284 31 31 LYS HD2 H 1.69 . 2 285 31 31 LYS HD3 H 1.69 . 2 286 31 31 LYS HE2 H 3.00 . 2 287 31 31 LYS HE3 H 3.00 . 2 288 31 31 LYS HG2 H 1.57 . 2 289 31 31 LYS HG3 H 1.57 . 2 290 31 31 LYS C C 180.57 . 1 291 31 31 LYS CA C 58.92 . 1 292 31 31 LYS CB C 32.49 . 1 293 31 31 LYS CD C 29.20 . 1 294 31 31 LYS CE C 42.20 . 1 295 31 31 LYS CG C 24.80 . 1 296 31 31 LYS N N 117.40 . 1 297 32 32 LEU H H 8.40 . 1 298 32 32 LEU HA H 3.99 . 1 299 32 32 LEU HB2 H 1.41 . 2 300 32 32 LEU HB3 H 1.59 . 2 301 32 32 LEU HD1 H 0.70 . 2 302 32 32 LEU HD2 H 0.70 . 2 303 32 32 LEU HG H 1.25 . 1 304 32 32 LEU C C 178.23 . 1 305 32 32 LEU CA C 57.70 . 1 306 32 32 LEU CB C 42.54 . 1 307 32 32 LEU CD1 C 23.79 . 2 308 32 32 LEU CD2 C 25.30 . 2 309 32 32 LEU CG C 26.65 . 1 310 32 32 LEU N N 121.18 . 1 311 33 33 HIS H H 7.62 . 1 312 33 33 HIS HA H 4.60 . 1 313 33 33 HIS HB2 H 2.82 . 2 314 33 33 HIS HB3 H 3.54 . 2 315 33 33 HIS HD2 H 7.15 . 1 316 33 33 HIS HE1 H 8.08 . 1 317 33 33 HIS C C 177.09 . 1 318 33 33 HIS CA C 55.84 . 1 319 33 33 HIS CB C 29.33 . 1 320 33 33 HIS CD2 C 120.80 . 1 321 33 33 HIS N N 112.22 . 1 322 34 34 ASN H H 8.03 . 1 323 34 34 ASN HA H 4.89 . 1 324 34 34 ASN HB2 H 2.85 . 2 325 34 34 ASN HB3 H 3.18 . 2 326 34 34 ASN HD21 H 7.85 . 1 327 34 34 ASN HD22 H 6.82 . 1 328 34 34 ASN C C 175.91 . 1 329 34 34 ASN CA C 54.53 . 1 330 34 34 ASN CB C 37.38 . 1 331 34 34 ASN N N 117.60 . 1 332 34 34 ASN ND2 N 112.72 . 1 333 35 35 MET H H 8.33 . 1 334 35 35 MET HA H 4.94 . 1 335 35 35 MET HB2 H 1.70 . 2 336 35 35 MET HB3 H 1.80 . 2 337 35 35 MET HE H 2.17 . 1 338 35 35 MET HG2 H 2.73 . 2 339 35 35 MET HG3 H 2.77 . 2 340 35 35 MET C C 176.88 . 1 341 35 35 MET CA C 55.60 . 1 342 35 35 MET CB C 33.79 . 1 343 35 35 MET CE C 18.26 . 1 344 35 35 MET CG C 33.82 . 1 345 35 35 MET N N 116.19 . 1 346 36 36 GLU H H 9.73 . 1 347 36 36 GLU HA H 3.85 . 1 348 36 36 GLU HB2 H 2.04 . 2 349 36 36 GLU HB3 H 2.10 . 2 350 36 36 GLU HG2 H 2.26 . 2 351 36 36 GLU HG3 H 2.47 . 2 352 36 36 GLU C C 178.29 . 1 353 36 36 GLU CA C 61.28 . 1 354 36 36 GLU CB C 29.27 . 1 355 36 36 GLU CG C 37.66 . 1 356 36 36 GLU N N 121.63 . 1 357 37 37 ASP H H 8.85 . 1 358 37 37 ASP HA H 4.47 . 1 359 37 37 ASP HB2 H 2.61 . 2 360 37 37 ASP HB3 H 2.67 . 2 361 37 37 ASP C C 177.19 . 1 362 37 37 ASP CA C 56.14 . 1 363 37 37 ASP CB C 40.05 . 1 364 37 37 ASP N N 114.39 . 1 365 38 38 LEU H H 7.88 . 1 366 38 38 LEU HA H 4.29 . 1 367 38 38 LEU HB2 H 1.53 . 2 368 38 38 LEU HB3 H 1.92 . 2 369 38 38 LEU HD1 H 0.76 . 2 370 38 38 LEU HD2 H 1.09 . 2 371 38 38 LEU HG H 1.75 . 1 372 38 38 LEU C C 175.09 . 1 373 38 38 LEU CA C 54.67 . 1 374 38 38 LEU CB C 42.94 . 1 375 38 38 LEU CD1 C 22.37 . 2 376 38 38 LEU CD2 C 26.40 . 2 377 38 38 LEU CG C 26.73 . 1 378 38 38 LEU N N 116.55 . 1 379 39 39 PHE H H 7.50 . 1 380 39 39 PHE HA H 4.97 . 1 381 39 39 PHE HB2 H 2.77 . 2 382 39 39 PHE HB3 H 3.09 . 2 383 39 39 PHE HD1 H 7.42 . 1 384 39 39 PHE HD2 H 7.42 . 1 385 39 39 PHE HE1 H 7.20 . 1 386 39 39 PHE HE2 H 7.20 . 1 387 39 39 PHE HZ H 7.33 . 1 388 39 39 PHE C C 175.38 . 1 389 39 39 PHE CA C 57.58 . 1 390 39 39 PHE CB C 44.99 . 1 391 39 39 PHE CD1 C 133.20 . 1 392 39 39 PHE CD2 C 133.20 . 1 393 39 39 PHE CE1 C 130.70 . 1 394 39 39 PHE CE2 C 139.70 . 1 395 39 39 PHE CZ C 129.50 . 1 396 39 39 PHE N N 115.37 . 1 397 40 40 GLY H H 8.68 . 1 398 40 40 GLY HA2 H 3.37 . 2 399 40 40 GLY HA3 H 4.55 . 2 400 40 40 GLY C C 173.09 . 1 401 40 40 GLY CA C 44.18 . 1 402 40 40 GLY N N 110.93 . 1 403 41 41 GLU H H 8.32 . 1 404 41 41 GLU HA H 4.28 . 1 405 41 41 GLU HB2 H 2.01 . 2 406 41 41 GLU HB3 H 2.17 . 2 407 41 41 GLU HG2 H 2.36 . 2 408 41 41 GLU HG3 H 2.48 . 2 409 41 41 GLU C C 173.90 . 1 410 41 41 GLU CA C 56.90 . 1 411 41 41 GLU CB C 32.11 . 1 412 41 41 GLU CG C 36.67 . 1 413 41 41 GLU N N 126.73 . 1 414 42 42 VAL H H 8.10 . 1 415 42 42 VAL HA H 5.16 . 1 416 42 42 VAL HB H 1.98 . 1 417 42 42 VAL HG1 H 1.02 . 2 418 42 42 VAL HG2 H 0.97 . 2 419 42 42 VAL C C 176.34 . 1 420 42 42 VAL CA C 61.20 . 1 421 42 42 VAL CB C 34.77 . 1 422 42 42 VAL CG1 C 21.05 . 2 423 42 42 VAL CG2 C 21.67 . 2 424 42 42 VAL N N 119.36 . 1 425 43 43 MET H H 9.87 . 1 426 43 43 MET HA H 5.07 . 1 427 43 43 MET HB2 H 2.02 . 2 428 43 43 MET HB3 H 2.10 . 2 429 43 43 MET HE H 1.79 . 1 430 43 43 MET HG2 H 2.52 . 2 431 43 43 MET HG3 H 2.57 . 2 432 43 43 MET C C 173.89 . 1 433 43 43 MET CA C 54.74 . 1 434 43 43 MET CB C 37.50 . 1 435 43 43 MET CE C 17.70 . 1 436 43 43 MET CG C 31.78 . 1 437 43 43 MET N N 125.72 . 1 438 44 44 VAL H H 8.80 . 1 439 44 44 VAL HA H 4.72 . 1 440 44 44 VAL HB H 2.12 . 1 441 44 44 VAL HG1 H 1.00 . 2 442 44 44 VAL HG2 H 0.94 . 2 443 44 44 VAL CA C 59.09 . 1 444 44 44 VAL CB C 33.71 . 1 445 44 44 VAL CG1 C 22.00 . 2 446 44 44 VAL CG2 C 21.20 . 2 447 44 44 VAL N N 122.34 . 1 448 45 45 PRO HA H 4.48 . 1 449 45 45 PRO HB2 H 1.87 . 2 450 45 45 PRO HB3 H 2.29 . 2 451 45 45 PRO HD2 H 3.63 . 2 452 45 45 PRO HD3 H 3.81 . 2 453 45 45 PRO HG2 H 2.02 . 2 454 45 45 PRO HG3 H 2.02 . 2 455 45 45 PRO C C 177.08 . 1 456 45 45 PRO CA C 63.24 . 1 457 45 45 PRO CB C 32.17 . 1 458 45 45 PRO CD C 50.69 . 1 459 45 45 PRO CG C 27.58 . 1 460 46 46 THR H H 8.20 . 1 461 46 46 THR HA H 4.29 . 1 462 46 46 THR HB H 4.30 . 1 463 46 46 THR HG2 H 1.24 . 1 464 46 46 THR C C 174.60 . 1 465 46 46 THR CA C 62.10 . 1 466 46 46 THR CB C 69.99 . 1 467 46 46 THR CG2 C 21.79 . 1 468 46 46 THR N N 113.41 . 1 469 47 47 GLU H H 8.38 . 1 470 47 47 GLU HA H 4.40 . 1 471 47 47 GLU HB2 H 1.90 . 2 472 47 47 GLU HB3 H 1.90 . 2 473 47 47 GLU C C 175.97 . 1 474 47 47 GLU CA C 55.20 . 1 475 47 47 GLU CB C 32.30 . 1 476 47 47 GLU N N 122.83 . 1 477 48 48 GLU H H 8.40 . 1 478 48 48 GLU HA H 4.28 . 1 479 48 48 GLU HB2 H 2.00 . 2 480 48 48 GLU HB3 H 2.17 . 2 481 48 48 GLU HG2 H 2.36 . 2 482 48 48 GLU HG3 H 2.48 . 2 483 48 48 GLU C C 175.75 . 1 484 48 48 GLU CA C 55.19 . 1 485 48 48 GLU CB C 31.98 . 1 486 48 48 GLU CG C 36.67 . 1 487 48 48 GLU N N 121.95 . 1 488 49 49 VAL H H 8.24 . 1 489 49 49 VAL HA H 4.17 . 1 490 49 49 VAL HB H 2.04 . 1 491 49 49 VAL HG1 H 0.90 . 2 492 49 49 VAL C C 174.61 . 1 493 49 49 VAL CA C 62.28 . 1 494 49 49 VAL CB C 32.93 . 1 495 49 49 VAL CG1 C 21.00 . 2 496 49 49 VAL N N 123.99 . 1 497 50 50 VAL H H 8.23 . 1 498 50 50 VAL HA H 4.22 . 1 499 50 50 VAL HB H 2.01 . 1 500 50 50 VAL HG1 H 0.90 . 2 501 50 50 VAL C C 175.77 . 1 502 50 50 VAL CA C 62.17 . 1 503 50 50 VAL CB C 33.11 . 1 504 50 50 VAL CG1 C 21.00 . 2 505 50 50 VAL N N 123.96 . 1 506 51 51 GLU H H 8.57 . 1 507 51 51 GLU HA H 4.38 . 1 508 51 51 GLU HB2 H 1.90 . 2 509 51 51 GLU HB3 H 1.98 . 2 510 51 51 GLU HG2 H 2.17 . 2 511 51 51 GLU HG3 H 2.24 . 2 512 51 51 GLU C C 175.92 . 1 513 51 51 GLU CA C 56.05 . 1 514 51 51 GLU CB C 31.08 . 1 515 51 51 GLU CG C 36.40 . 1 516 51 51 GLU N N 125.07 . 1 517 52 52 ILE H H 8.32 . 1 518 52 52 ILE HA H 4.29 . 1 519 52 52 ILE HB H 1.84 . 1 520 52 52 ILE HD1 H 0.80 . 1 521 52 52 ILE HG12 H 1.12 . 2 522 52 52 ILE HG13 H 1.45 . 2 523 52 52 ILE HG2 H 0.82 . 1 524 52 52 ILE C C 176.33 . 1 525 52 52 ILE CA C 60.94 . 1 526 52 52 ILE CB C 38.51 . 1 527 52 52 ILE CD1 C 12.83 . 1 528 52 52 ILE CG1 C 27.45 . 1 529 52 52 ILE CG2 C 17.48 . 1 530 52 52 ILE N N 122.76 . 1 531 53 53 ARG H H 8.50 . 1 532 53 53 ARG HA H 4.43 . 1 533 53 53 ARG HB2 H 1.75 . 2 534 53 53 ARG HB3 H 1.75 . 2 535 53 53 ARG HD2 H 3.20 . 2 536 53 53 ARG HD3 H 3.20 . 2 537 53 53 ARG HG2 H 1.62 . 2 538 53 53 ARG HG3 H 1.62 . 2 539 53 53 ARG C C 176.95 . 1 540 53 53 ARG CA C 56.15 . 1 541 53 53 ARG CB C 30.20 . 1 542 53 53 ARG CD C 43.30 . 1 543 53 53 ARG CG C 27.20 . 1 544 53 53 ARG N N 125.25 . 1 545 54 54 GLY H H 8.76 . 1 546 54 54 GLY HA2 H 3.92 . 2 547 54 54 GLY HA3 H 4.01 . 2 548 54 54 GLY C C 175.11 . 1 549 54 54 GLY CA C 46.03 . 1 550 54 54 GLY N N 112.51 . 1 551 55 55 GLY H H 8.35 . 1 552 55 55 GLY HA2 H 3.98 . 2 553 55 55 GLY HA3 H 3.98 . 2 554 55 55 GLY C C 173.92 . 1 555 55 55 GLY CA C 45.20 . 1 556 55 55 GLY N N 107.94 . 1 557 56 56 GLN H H 8.10 . 1 558 56 56 GLN HA H 4.42 . 1 559 56 56 GLN HB2 H 1.98 . 2 560 56 56 GLN HB3 H 2.01 . 2 561 56 56 GLN HG2 H 2.36 . 2 562 56 56 GLN HG3 H 2.39 . 2 563 56 56 GLN C C 175.57 . 1 564 56 56 GLN CA C 55.42 . 1 565 56 56 GLN CB C 30.10 . 1 566 56 56 GLN CG C 33.90 . 1 567 56 56 GLN N N 119.35 . 1 568 57 57 ARG H H 8.52 . 1 569 57 57 ARG HA H 4.40 . 1 570 57 57 ARG HB2 H 1.77 . 2 571 57 57 ARG HB3 H 1.77 . 2 572 57 57 ARG HD2 H 3.20 . 2 573 57 57 ARG HD3 H 3.20 . 2 574 57 57 ARG HG2 H 1.60 . 2 575 57 57 ARG HG3 H 1.60 . 2 576 57 57 ARG C C 176.21 . 1 577 57 57 ARG CA C 56.44 . 1 578 57 57 ARG CB C 30.93 . 1 579 57 57 ARG CD C 43.40 . 1 580 57 57 ARG CG C 27.10 . 1 581 57 57 ARG N N 122.61 . 1 582 58 58 ARG H H 8.63 . 1 583 58 58 ARG HA H 4.43 . 1 584 58 58 ARG HB2 H 1.75 . 2 585 58 58 ARG HB3 H 1.86 . 2 586 58 58 ARG HD2 H 3.18 . 2 587 58 58 ARG HD3 H 3.18 . 2 588 58 58 ARG HG2 H 1.63 . 2 589 58 58 ARG HG3 H 1.67 . 2 590 58 58 ARG C C 175.95 . 1 591 58 58 ARG CA C 55.45 . 1 592 58 58 ARG CB C 31.30 . 1 593 58 58 ARG CD C 43.42 . 1 594 58 58 ARG CG C 27.20 . 1 595 58 58 ARG N N 123.32 . 1 596 59 59 LYS H H 8.56 . 1 597 59 59 LYS HA H 4.41 . 1 598 59 59 LYS HB2 H 1.77 . 2 599 59 59 LYS HB3 H 1.84 . 2 600 59 59 LYS HD2 H 1.68 . 2 601 59 59 LYS HD3 H 1.73 . 2 602 59 59 LYS HE2 H 3.00 . 2 603 59 59 LYS HE3 H 3.00 . 2 604 59 59 LYS HG2 H 1.41 . 2 605 59 59 LYS HG3 H 1.47 . 2 606 59 59 LYS C C 176.59 . 1 607 59 59 LYS CA C 56.72 . 1 608 59 59 LYS CB C 33.15 . 1 609 59 59 LYS CD C 29.00 . 1 610 59 59 LYS CE C 42.10 . 1 611 59 59 LYS CG C 24.73 . 1 612 59 59 LYS N N 123.38 . 1 613 60 60 SER H H 8.45 . 1 614 60 60 SER HA H 4.48 . 1 615 60 60 SER HB2 H 3.81 . 2 616 60 60 SER HB3 H 3.86 . 2 617 60 60 SER C C 174.28 . 1 618 60 60 SER CA C 58.14 . 1 619 60 60 SER CB C 64.16 . 1 620 60 60 SER N N 117.32 . 1 621 61 61 GLU H H 8.55 . 1 622 61 61 GLU HA H 4.40 . 1 623 61 61 GLU HB2 H 1.92 . 2 624 61 61 GLU HB3 H 2.05 . 2 625 61 61 GLU HG2 H 2.18 . 2 626 61 61 GLU HG3 H 2.25 . 2 627 61 61 GLU C C 176.15 . 1 628 61 61 GLU CA C 56.30 . 1 629 61 61 GLU CB C 30.79 . 1 630 61 61 GLU CG C 36.35 . 1 631 61 61 GLU N N 122.81 . 1 632 62 62 ARG H H 8.31 . 1 633 62 62 ARG HA H 4.34 . 1 634 62 62 ARG HB2 H 1.92 . 2 635 62 62 ARG HB3 H 1.99 . 2 636 62 62 ARG C C 176.14 . 1 637 62 62 ARG CA C 56.23 . 1 638 62 62 ARG CB C 30.78 . 1 639 62 62 ARG N N 122.08 . 1 640 63 63 LYS H H 8.47 . 1 641 63 63 LYS HA H 4.30 . 1 642 63 63 LYS HB2 H 1.78 . 2 643 63 63 LYS HB3 H 1.78 . 2 644 63 63 LYS C C 175.49 . 1 645 63 63 LYS CA C 56.20 . 1 646 63 63 LYS CB C 30.73 . 1 647 63 63 LYS N N 123.45 . 1 648 64 64 PHE H H 8.20 . 1 649 64 64 PHE HA H 4.45 . 1 650 64 64 PHE HB2 H 2.75 . 2 651 64 64 PHE HB3 H 2.75 . 2 652 64 64 PHE HD1 H 7.08 . 1 653 64 64 PHE HD2 H 7.08 . 1 654 64 64 PHE C C 174.25 . 1 655 64 64 PHE CA C 57.43 . 1 656 64 64 PHE CB C 40.33 . 1 657 64 64 PHE CD1 C 131.50 . 1 658 64 64 PHE CD2 C 131.50 . 1 659 64 64 PHE N N 121.74 . 1 660 65 65 PHE H H 8.13 . 1 661 65 65 PHE HA H 4.44 . 1 662 65 65 PHE HB2 H 2.53 . 2 663 65 65 PHE HB3 H 2.53 . 2 664 65 65 PHE HD1 H 6.92 . 1 665 65 65 PHE HD2 H 6.92 . 1 666 65 65 PHE HE1 H 7.24 . 1 667 65 65 PHE HE2 H 7.24 . 1 668 65 65 PHE HZ H 7.19 . 1 669 65 65 PHE CA C 55.65 . 1 670 65 65 PHE CB C 38.90 . 1 671 65 65 PHE CD1 C 132.20 . 1 672 65 65 PHE CD2 C 132.20 . 1 673 65 65 PHE CE1 C 131.20 . 1 674 65 65 PHE CE2 C 131.20 . 1 675 65 65 PHE N N 120.91 . 1 676 66 66 PRO C C 176.78 . 1 677 67 67 GLY H H 9.97 . 1 678 67 67 GLY HA2 H 3.82 . 2 679 67 67 GLY HA3 H 4.40 . 2 680 67 67 GLY C C 173.67 . 1 681 67 67 GLY CA C 45.90 . 1 682 67 67 GLY N N 111.55 . 1 683 68 68 TYR H H 7.65 . 1 684 68 68 TYR HA H 5.00 . 1 685 68 68 TYR HB2 H 2.68 . 2 686 68 68 TYR HB3 H 3.27 . 2 687 68 68 TYR HD1 H 6.81 . 1 688 68 68 TYR HD2 H 6.81 . 1 689 68 68 TYR HE1 H 6.73 . 1 690 68 68 TYR HE2 H 6.73 . 1 691 68 68 TYR C C 175.22 . 1 692 68 68 TYR CA C 57.94 . 1 693 68 68 TYR CD1 C 131.95 . 1 694 68 68 TYR CD2 C 131.95 . 1 695 68 68 TYR CE1 C 118.30 . 1 696 68 68 TYR CE2 C 118.30 . 1 697 68 68 TYR N N 118.80 . 1 698 69 69 VAL H H 9.09 . 1 699 69 69 VAL HA H 4.33 . 1 700 69 69 VAL HB H 1.92 . 1 701 69 69 VAL HG1 H 0.89 . 2 702 69 69 VAL HG2 H 0.79 . 2 703 69 69 VAL C C 174.25 . 1 704 69 69 VAL CA C 62.12 . 1 705 69 69 VAL CB C 35.24 . 1 706 69 69 VAL CG1 C 21.65 . 2 707 69 69 VAL CG2 C 21.63 . 2 708 69 69 VAL N N 119.30 . 1 709 70 70 LEU H H 9.19 . 1 710 70 70 LEU HA H 5.46 . 1 711 70 70 LEU HB2 H 1.76 . 2 712 70 70 LEU HB3 H 1.99 . 2 713 70 70 LEU HD1 H 0.82 . 2 714 70 70 LEU HD2 H 0.74 . 2 715 70 70 LEU HG H 1.69 . 1 716 70 70 LEU C C 176.13 . 1 717 70 70 LEU CA C 54.12 . 1 718 70 70 LEU CB C 43.33 . 1 719 70 70 LEU CD1 C 25.35 . 2 720 70 70 LEU CD2 C 26.11 . 2 721 70 70 LEU CG C 28.48 . 1 722 70 70 LEU N N 126.71 . 1 723 71 71 VAL H H 9.35 . 1 724 71 71 VAL HA H 5.04 . 1 725 71 71 VAL HB H 2.10 . 1 726 71 71 VAL HG1 H 1.18 . 2 727 71 71 VAL HG2 H 1.02 . 2 728 71 71 VAL C C 173.67 . 1 729 71 71 VAL CA C 61.09 . 1 730 71 71 VAL CB C 35.80 . 1 731 71 71 VAL CG1 C 22.13 . 2 732 71 71 VAL CG2 C 22.80 . 2 733 71 71 VAL N N 121.92 . 1 734 72 72 GLN H H 8.39 . 1 735 72 72 GLN HA H 4.61 . 1 736 72 72 GLN HB2 H 0.08 . 2 737 72 72 GLN HB3 H 1.53 . 2 738 72 72 GLN HE21 H 6.82 . 1 739 72 72 GLN HE22 H 6.89 . 1 740 72 72 GLN HG2 H 0.79 . 2 741 72 72 GLN HG3 H 0.52 . 2 742 72 72 GLN C C 175.92 . 1 743 72 72 GLN CA C 53.81 . 1 744 72 72 GLN CB C 28.85 . 1 745 72 72 GLN CG C 33.28 . 1 746 72 72 GLN N N 130.76 . 1 747 72 72 GLN NE2 N 112.15 . 1 748 73 73 MET H H 9.75 . 1 749 73 73 MET HA H 5.06 . 1 750 73 73 MET HB2 H 1.35 . 2 751 73 73 MET HB3 H 1.88 . 2 752 73 73 MET HE H 1.80 . 1 753 73 73 MET HG2 H 2.55 . 2 754 73 73 MET HG3 H 2.55 . 2 755 73 73 MET C C 175.50 . 1 756 73 73 MET CA C 55.52 . 1 757 73 73 MET CB C 35.35 . 1 758 73 73 MET CE C 17.80 . 1 759 73 73 MET CG C 31.12 . 1 760 73 73 MET N N 121.07 . 1 761 74 74 VAL H H 8.53 . 1 762 74 74 VAL HA H 3.97 . 1 763 74 74 VAL HB H 1.96 . 1 764 74 74 VAL HG1 H 0.79 . 2 765 74 74 VAL HG2 H 0.78 . 2 766 74 74 VAL C C 174.90 . 1 767 74 74 VAL CA C 62.15 . 1 768 74 74 VAL CB C 32.48 . 1 769 74 74 VAL CG1 C 21.63 . 2 770 74 74 VAL CG2 C 21.60 . 2 771 74 74 VAL N N 124.12 . 1 772 75 75 MET H H 8.60 . 1 773 75 75 MET HA H 4.36 . 1 774 75 75 MET HB2 H 1.92 . 2 775 75 75 MET HB3 H 1.92 . 2 776 75 75 MET HE H 0.68 . 1 777 75 75 MET HG2 H 2.34 . 2 778 75 75 MET HG3 H 2.34 . 2 779 75 75 MET C C 173.48 . 1 780 75 75 MET CA C 53.83 . 1 781 75 75 MET CB C 29.96 . 1 782 75 75 MET CE C 15.30 . 1 783 75 75 MET CG C 31.96 . 1 784 75 75 MET N N 128.25 . 1 785 76 76 ASN H H 8.41 . 1 786 76 76 ASN HA H 4.54 . 1 787 76 76 ASN HB2 H 2.99 . 2 788 76 76 ASN HB3 H 3.18 . 2 789 76 76 ASN HD21 H 7.49 . 1 790 76 76 ASN HD22 H 5.88 . 1 791 76 76 ASN C C 173.95 . 1 792 76 76 ASN CA C 51.72 . 1 793 76 76 ASN CB C 38.43 . 1 794 76 76 ASN N N 127.50 . 1 795 76 76 ASN ND2 N 108.57 . 1 796 77 77 ASP H H 8.47 . 1 797 77 77 ASP HA H 4.41 . 1 798 77 77 ASP HB2 H 2.67 . 2 799 77 77 ASP HB3 H 2.71 . 2 800 77 77 ASP C C 178.53 . 1 801 77 77 ASP CA C 58.73 . 1 802 77 77 ASP CB C 40.94 . 1 803 77 77 ASP N N 117.09 . 1 804 78 78 ALA H H 8.16 . 1 805 78 78 ALA HA H 4.35 . 1 806 78 78 ALA HB H 1.52 . 1 807 78 78 ALA C C 181.25 . 1 808 78 78 ALA CA C 55.19 . 1 809 78 78 ALA CB C 18.26 . 1 810 78 78 ALA N N 122.50 . 1 811 79 79 SER H H 9.32 . 1 812 79 79 SER HA H 4.29 . 1 813 79 79 SER HB2 H 3.77 . 2 814 79 79 SER HB3 H 3.94 . 2 815 79 79 SER C C 176.57 . 1 816 79 79 SER CA C 61.08 . 1 817 79 79 SER CB C 62.20 . 1 818 79 79 SER N N 119.28 . 1 819 80 80 TRP H H 8.90 . 1 820 80 80 TRP HA H 4.02 . 1 821 80 80 TRP HB2 H 3.40 . 2 822 80 80 TRP HB3 H 3.40 . 2 823 80 80 TRP HD1 H 6.71 . 1 824 80 80 TRP HE1 H 9.95 . 1 825 80 80 TRP HE3 H 6.82 . 1 826 80 80 TRP HH2 H 7.14 . 1 827 80 80 TRP HZ2 H 7.46 . 1 828 80 80 TRP HZ3 H 6.73 . 1 829 80 80 TRP C C 178.21 . 1 830 80 80 TRP CA C 62.49 . 1 831 80 80 TRP CB C 29.80 . 1 832 80 80 TRP CD1 C 126.80 . . 833 80 80 TRP CE3 C 131.40 . 1 834 80 80 TRP CH2 C 124.80 . 1 835 80 80 TRP CZ2 C 114.50 . 1 836 80 80 TRP CZ3 C 121.90 . 1 837 80 80 TRP N N 125.87 . 1 838 80 80 TRP NE1 N 127.31 . 1 839 81 81 HIS H H 8.19 . 1 840 81 81 HIS HA H 3.93 . 1 841 81 81 HIS HB2 H 3.31 . 2 842 81 81 HIS HB3 H 3.42 . 2 843 81 81 HIS HD2 H 7.42 . 1 844 81 81 HIS HE1 H 8.09 . 1 845 81 81 HIS C C 177.74 . 1 846 81 81 HIS CA C 61.02 . 1 847 81 81 HIS CB C 28.91 . 1 848 81 81 HIS CD2 C 121.08 . 1 849 81 81 HIS N N 114.08 . 1 850 82 82 LEU H H 8.08 . 1 851 82 82 LEU HA H 3.90 . 1 852 82 82 LEU HB2 H 1.60 . 2 853 82 82 LEU HB3 H 1.81 . 2 854 82 82 LEU HD1 H 0.80 . 2 855 82 82 LEU HD2 H 0.68 . 2 856 82 82 LEU HG H 1.44 . 1 857 82 82 LEU C C 180.33 . 1 858 82 82 LEU CA C 58.59 . 1 859 82 82 LEU CB C 41.35 . 1 860 82 82 LEU CD1 C 26.68 . 2 861 82 82 LEU CD2 C 25.27 . 2 862 82 82 LEU CG C 27.22 . 1 863 82 82 LEU N N 121.32 . 1 864 83 83 VAL H H 8.00 . 1 865 83 83 VAL HA H 3.21 . 1 866 83 83 VAL HB H 2.05 . 1 867 83 83 VAL HG1 H 0.47 . 2 868 83 83 VAL HG2 H 1.33 . 2 869 83 83 VAL C C 177.06 . 1 870 83 83 VAL CA C 67.43 . 1 871 83 83 VAL CB C 31.68 . 1 872 83 83 VAL CG1 C 22.92 . 2 873 83 83 VAL CG2 C 23.53 . 2 874 83 83 VAL N N 118.85 . 1 875 84 84 ARG H H 7.54 . 1 876 84 84 ARG HA H 3.59 . 1 877 84 84 ARG HB2 H 1.21 . 2 878 84 84 ARG HB3 H 1.52 . 2 879 84 84 ARG HD2 H 2.26 . 2 880 84 84 ARG HD3 H 2.39 . 2 881 84 84 ARG HG2 H 0.50 . 2 882 84 84 ARG HG3 H 0.76 . 2 883 84 84 ARG C C 177.24 . 1 884 84 84 ARG CA C 56.05 . 1 885 84 84 ARG CB C 28.19 . 1 886 84 84 ARG CD C 40.59 . 1 887 84 84 ARG CG C 25.49 . 1 888 84 84 ARG N N 111.46 . 1 889 85 85 SER H H 7.53 . 1 890 85 85 SER HA H 4.28 . 1 891 85 85 SER HB2 H 3.88 . 2 892 85 85 SER HB3 H 4.00 . 2 893 85 85 SER C C 173.93 . 1 894 85 85 SER CA C 59.22 . 1 895 85 85 SER CB C 63.83 . 1 896 85 85 SER N N 113.66 . 1 897 86 86 VAL H H 7.23 . 1 898 86 86 VAL HA H 3.48 . 1 899 86 86 VAL HB H 2.12 . 1 900 86 86 VAL HG1 H 0.82 . 2 901 86 86 VAL HG2 H 0.55 . 2 902 86 86 VAL CA C 61.30 . 1 903 86 86 VAL CB C 31.78 . 1 904 86 86 VAL CG1 C 20.90 . 2 905 86 86 VAL CG2 C 22.79 . 2 906 86 86 VAL N N 128.12 . 1 907 87 87 PRO HA H 4.14 . 1 908 87 87 PRO HB2 H 1.75 . 2 909 87 87 PRO HB3 H 2.23 . 2 910 87 87 PRO HD2 H 3.44 . 2 911 87 87 PRO HD3 H 3.97 . 2 912 87 87 PRO HG2 H 2.00 . 2 913 87 87 PRO HG3 H 2.12 . 2 914 87 87 PRO C C 176.40 . 1 915 87 87 PRO CA C 64.10 . 1 916 87 87 PRO CB C 31.71 . 1 917 87 87 PRO CD C 51.28 . 1 918 87 87 PRO CG C 28.01 . 1 919 88 88 ARG H H 8.32 . 1 920 88 88 ARG HA H 3.03 . 1 921 88 88 ARG HB2 H 0.91 . 2 922 88 88 ARG HB3 H 1.02 . 2 923 88 88 ARG HD2 H 2.02 . 2 924 88 88 ARG HD3 H 2.21 . 2 925 88 88 ARG HG2 H 1.33 . 2 926 88 88 ARG HG3 H 1.33 . 2 927 88 88 ARG C C 174.63 . 1 928 88 88 ARG CA C 57.62 . 1 929 88 88 ARG CB C 26.96 . 1 930 88 88 ARG CD C 43.12 . 1 931 88 88 ARG CG C 26.25 . 1 932 88 88 ARG N N 111.36 . 1 933 89 89 VAL H H 7.39 . 1 934 89 89 VAL HA H 3.91 . 1 935 89 89 VAL HB H 2.11 . 1 936 89 89 VAL HG1 H 0.73 . 2 937 89 89 VAL HG2 H 0.52 . 2 938 89 89 VAL C C 177.37 . 1 939 89 89 VAL CA C 64.17 . 1 940 89 89 VAL CB C 32.07 . 1 941 89 89 VAL CG1 C 24.19 . 2 942 89 89 VAL CG2 C 21.34 . 2 943 89 89 VAL N N 117.90 . 1 944 90 90 MET H H 9.29 . 1 945 90 90 MET HA H 4.34 . 1 946 90 90 MET HB2 H 2.05 . 2 947 90 90 MET HB3 H 1.42 . 2 948 90 90 MET HE H 1.84 . 1 949 90 90 MET HG2 H 2.12 . 2 950 90 90 MET HG3 H 2.16 . 2 951 90 90 MET C C 175.80 . 1 952 90 90 MET CA C 56.44 . 1 953 90 90 MET CB C 34.16 . 1 954 90 90 MET CE C 16.50 . 1 955 90 90 MET CG C 31.79 . 1 956 90 90 MET N N 128.20 . 1 957 91 91 GLY H H 7.13 . 1 958 91 91 GLY HA2 H 3.34 . 2 959 91 91 GLY HA3 H 4.41 . 2 960 91 91 GLY C C 170.92 . 1 961 91 91 GLY CA C 44.44 . 1 962 91 91 GLY N N 104.32 . 1 963 92 92 PHE H H 8.79 . 1 964 92 92 PHE HA H 5.27 . 1 965 92 92 PHE HB2 H 3.04 . 2 966 92 92 PHE HB3 H 3.20 . 2 967 92 92 PHE HD1 H 7.32 . 1 968 92 92 PHE HD2 H 7.32 . 1 969 92 92 PHE HE1 H 6.82 . 1 970 92 92 PHE HE2 H 6.82 . 1 971 92 92 PHE HZ H 6.76 . 1 972 92 92 PHE C C 176.23 . 1 973 92 92 PHE CA C 57.48 . 1 974 92 92 PHE CB C 42.19 . 1 975 92 92 PHE CD1 C 132.40 . 1 976 92 92 PHE CD2 C 132.40 . 1 977 92 92 PHE CE1 C 131.20 . 1 978 92 92 PHE CE2 C 131.20 . 1 979 92 92 PHE N N 118.77 . 1 980 93 93 ILE H H 8.80 . 1 981 93 93 ILE HA H 4.31 . 1 982 93 93 ILE HB H 1.61 . 1 983 93 93 ILE HD1 H 0.63 . 1 984 93 93 ILE HG12 H 1.03 . 2 985 93 93 ILE HG13 H 1.20 . 2 986 93 93 ILE HG2 H 0.89 . 1 987 93 93 ILE C C 176.38 . 1 988 93 93 ILE CA C 60.48 . 1 989 93 93 ILE CB C 38.01 . 1 990 93 93 ILE CD1 C 11.49 . 1 991 93 93 ILE CG1 C 27.36 . 1 992 93 93 ILE CG2 C 16.80 . 1 993 93 93 ILE N N 122.30 . 1 994 94 94 GLY H H 8.64 . 1 995 94 94 GLY HA2 H 3.83 . 2 996 94 94 GLY HA3 H 4.60 . 2 997 94 94 GLY C C 175.08 . 1 998 94 94 GLY CA C 44.53 . 1 999 94 94 GLY N N 116.55 . 1 1000 95 95 GLY H H 8.90 . 1 1001 95 95 GLY HA2 H 3.97 . 2 1002 95 95 GLY HA3 H 4.37 . 2 1003 95 95 GLY C C 174.56 . 1 1004 95 95 GLY CA C 45.64 . 1 1005 95 95 GLY N N 112.96 . 1 1006 96 96 THR H H 7.83 . 1 1007 96 96 THR HA H 4.72 . 1 1008 96 96 THR HB H 4.54 . 1 1009 96 96 THR HG2 H 1.21 . 1 1010 96 96 THR C C 176.26 . 1 1011 96 96 THR CA C 60.36 . 1 1012 96 96 THR CB C 70.96 . 1 1013 96 96 THR CG2 C 21.60 . 1 1014 96 96 THR N N 113.35 . 1 1015 97 97 SER H H 8.85 . 1 1016 97 97 SER HA H 4.31 . 1 1017 97 97 SER HB2 H 4.05 . 2 1018 97 97 SER HB3 H 4.05 . 2 1019 97 97 SER C C 175.57 . 1 1020 97 97 SER CA C 60.85 . 1 1021 97 97 SER CB C 63.00 . 1 1022 97 97 SER N N 116.42 . 1 1023 98 98 ASP H H 8.36 . 1 1024 98 98 ASP HA H 4.31 . 1 1025 98 98 ASP HB2 H 2.38 . 2 1026 98 98 ASP HB3 H 2.43 . 2 1027 98 98 ASP C C 175.38 . 1 1028 98 98 ASP CA C 54.19 . 1 1029 98 98 ASP CB C 40.74 . 1 1030 98 98 ASP N N 116.32 . 1 1031 99 99 ARG H H 7.45 . 1 1032 99 99 ARG HA H 4.35 . 1 1033 99 99 ARG HB2 H 1.56 . 2 1034 99 99 ARG HB3 H 1.61 . 2 1035 99 99 ARG HD2 H 2.97 . 2 1036 99 99 ARG HD3 H 3.00 . 2 1037 99 99 ARG HG2 H 1.30 . 2 1038 99 99 ARG HG3 H 1.35 . 2 1039 99 99 ARG CA C 52.92 . 1 1040 99 99 ARG CB C 30.34 . 1 1041 99 99 ARG CD C 43.26 . 1 1042 99 99 ARG CG C 26.63 . 1 1043 99 99 ARG N N 119.96 . 1 1044 100 100 PRO HA H 4.75 . 1 1045 100 100 PRO HB2 H 1.57 . 2 1046 100 100 PRO HB3 H 2.11 . 2 1047 100 100 PRO HD2 H 3.07 . 2 1048 100 100 PRO HD3 H 3.23 . 2 1049 100 100 PRO HG2 H 1.34 . 2 1050 100 100 PRO HG3 H 0.96 . 2 1051 100 100 PRO C C 175.22 . 1 1052 100 100 PRO CA C 62.68 . 1 1053 100 100 PRO CB C 32.82 . 1 1054 100 100 PRO CD C 49.84 . 1 1055 100 100 PRO CG C 27.51 . 1 1056 101 101 ALA H H 7.21 . 1 1057 101 101 ALA HA H 5.03 . 1 1058 101 101 ALA HB H 1.37 . 1 1059 101 101 ALA CA C 48.57 . 1 1060 101 101 ALA CB C 19.66 . 1 1061 101 101 ALA N N 124.49 . 1 1062 102 102 PRO HA H 4.44 . 1 1063 102 102 PRO HB2 H 1.82 . 2 1064 102 102 PRO HB3 H 2.28 . 2 1065 102 102 PRO HD2 H 3.62 . 2 1066 102 102 PRO HD3 H 3.81 . 2 1067 102 102 PRO HG2 H 2.01 . 2 1068 102 102 PRO HG3 H 2.01 . 2 1069 102 102 PRO C C 177.20 . 1 1070 102 102 PRO CA C 62.19 . 1 1071 102 102 PRO CB C 32.31 . 1 1072 102 102 PRO CD C 50.50 . 1 1073 102 102 PRO CG C 27.44 . 1 1074 103 103 ILE H H 8.55 . 1 1075 103 103 ILE HA H 4.63 . 1 1076 103 103 ILE HB H 1.79 . 1 1077 103 103 ILE HD1 H 0.55 . 1 1078 103 103 ILE HG12 H 0.82 . 2 1079 103 103 ILE HG13 H 1.34 . 2 1080 103 103 ILE HG2 H 0.83 . 1 1081 103 103 ILE C C 175.46 . 1 1082 103 103 ILE CA C 59.73 . 1 1083 103 103 ILE CB C 40.14 . 1 1084 103 103 ILE CD1 C 14.47 . 1 1085 103 103 ILE CG1 C 26.06 . 1 1086 103 103 ILE CG2 C 17.85 . 1 1087 103 103 ILE N N 115.67 . 1 1088 104 104 SER H H 8.73 . 1 1089 104 104 SER HA H 4.50 . 1 1090 104 104 SER HB2 H 4.04 . 2 1091 104 104 SER HB3 H 4.34 . 2 1092 104 104 SER C C 174.84 . 1 1093 104 104 SER CA C 58.01 . 1 1094 104 104 SER CB C 65.47 . 1 1095 104 104 SER N N 119.17 . 1 1096 105 105 ASP H H 8.83 . 1 1097 105 105 ASP HA H 4.20 . 1 1098 105 105 ASP HB2 H 2.68 . 2 1099 105 105 ASP HB3 H 2.81 . 2 1100 105 105 ASP C C 178.52 . 1 1101 105 105 ASP CA C 57.87 . 1 1102 105 105 ASP CB C 40.04 . 1 1103 105 105 ASP N N 121.64 . 1 1104 106 106 LYS H H 8.13 . 1 1105 106 106 LYS HA H 4.10 . 1 1106 106 106 LYS HB2 H 1.77 . 2 1107 106 106 LYS HB3 H 1.77 . 2 1108 106 106 LYS HD2 H 1.68 . 2 1109 106 106 LYS HD3 H 1.72 . 2 1110 106 106 LYS HE2 H 3.01 . 2 1111 106 106 LYS HE3 H 3.01 . 2 1112 106 106 LYS HG2 H 1.45 . 2 1113 106 106 LYS HG3 H 1.57 . 2 1114 106 106 LYS C C 179.40 . 1 1115 106 106 LYS CA C 58.98 . 1 1116 106 106 LYS CB C 32.33 . 1 1117 106 106 LYS CD C 29.10 . 1 1118 106 106 LYS CE C 42.22 . 1 1119 106 106 LYS CG C 24.99 . 1 1120 106 106 LYS N N 118.30 . 1 1121 107 107 GLU H H 7.67 . 1 1122 107 107 GLU HA H 4.02 . 1 1123 107 107 GLU HB2 H 1.97 . 2 1124 107 107 GLU HB3 H 2.26 . 2 1125 107 107 GLU HG2 H 2.24 . 2 1126 107 107 GLU HG3 H 2.24 . 2 1127 107 107 GLU C C 178.75 . 1 1128 107 107 GLU CA C 59.21 . 1 1129 107 107 GLU CB C 29.78 . 1 1130 107 107 GLU CG C 37.65 . 1 1131 107 107 GLU N N 121.27 . 1 1132 108 108 VAL H H 7.79 . 1 1133 108 108 VAL HA H 3.05 . 1 1134 108 108 VAL HB H 1.67 . 1 1135 108 108 VAL HG1 H -0.06 . 2 1136 108 108 VAL HG2 H 0.19 . 2 1137 108 108 VAL C C 177.55 . 1 1138 108 108 VAL CA C 67.08 . 1 1139 108 108 VAL CB C 31.22 . 1 1140 108 108 VAL CG1 C 20.46 . 2 1141 108 108 VAL CG2 C 22.66 . 2 1142 108 108 VAL N N 120.94 . 1 1143 109 109 ASP H H 7.84 . 1 1144 109 109 ASP HA H 4.11 . 1 1145 109 109 ASP HB2 H 2.69 . 2 1146 109 109 ASP HB3 H 2.53 . 2 1147 109 109 ASP C C 178.19 . 1 1148 109 109 ASP CA C 57.47 . 1 1149 109 109 ASP CB C 40.48 . 1 1150 109 109 ASP N N 118.78 . 1 1151 110 110 ALA H H 7.52 . 1 1152 110 110 ALA HA H 4.11 . 1 1153 110 110 ALA HB H 1.46 . 1 1154 110 110 ALA C C 180.55 . 1 1155 110 110 ALA CA C 54.88 . 1 1156 110 110 ALA CB C 18.44 . 1 1157 110 110 ALA N N 120.64 . 1 1158 111 111 ILE H H 7.84 . 1 1159 111 111 ILE HA H 3.58 . 1 1160 111 111 ILE HB H 1.62 . 1 1161 111 111 ILE HD1 H 0.61 . 1 1162 111 111 ILE HG2 H 0.55 . 1 1163 111 111 ILE C C 177.47 . 1 1164 111 111 ILE CA C 64.62 . 1 1165 111 111 ILE CB C 38.60 . 1 1166 111 111 ILE CD1 C 13.88 . 1 1167 111 111 ILE CG2 C 17.29 . 1 1168 111 111 ILE N N 119.84 . 1 1169 112 112 MET H H 8.10 . 1 1170 112 112 MET HA H 4.40 . 1 1171 112 112 MET HB2 H 1.92 . 2 1172 112 112 MET HB3 H 2.06 . 2 1173 112 112 MET HE H 1.90 . 1 1174 112 112 MET HG2 H 2.25 . 2 1175 112 112 MET HG3 H 2.25 . 2 1176 112 112 MET C C 177.71 . 1 1177 112 112 MET CA C 55.30 . 1 1178 112 112 MET CB C 30.51 . 1 1179 112 112 MET CE C 16.10 . 1 1180 112 112 MET CG C 36.27 . 1 1181 112 112 MET N N 115.18 . 1 1182 113 113 ASN H H 8.07 . 1 1183 113 113 ASN HA H 4.57 . 1 1184 113 113 ASN HB2 H 2.71 . 2 1185 113 113 ASN HB3 H 2.96 . 2 1186 113 113 ASN HD21 H 7.59 . 1 1187 113 113 ASN HD22 H 6.88 . 1 1188 113 113 ASN C C 175.53 . 1 1189 113 113 ASN CA C 54.42 . 1 1190 113 113 ASN CB C 38.35 . 1 1191 113 113 ASN N N 117.19 . 1 1192 113 113 ASN ND2 N 112.90 . 1 1193 114 114 ARG H H 8.07 . 1 1194 114 114 ARG HA H 4.28 . 1 1195 114 114 ARG HB2 H 1.83 . 2 1196 114 114 ARG HB3 H 1.83 . 2 1197 114 114 ARG HD2 H 3.10 . 2 1198 114 114 ARG HD3 H 3.10 . 2 1199 114 114 ARG HG2 H 1.58 . 2 1200 114 114 ARG HG3 H 1.58 . 2 1201 114 114 ARG C C 176.62 . 1 1202 114 114 ARG CA C 56.91 . 1 1203 114 114 ARG CB C 30.37 . 1 1204 114 114 ARG CD C 43.48 . 1 1205 114 114 ARG CG C 27.20 . 1 1206 114 114 ARG N N 118.36 . 1 1207 115 115 LEU H H 8.10 . 1 1208 115 115 LEU HA H 4.31 . 1 1209 115 115 LEU HB2 H 1.56 . 2 1210 115 115 LEU HB3 H 1.66 . 2 1211 115 115 LEU HD1 H 0.89 . 2 1212 115 115 LEU HD2 H 0.83 . 2 1213 115 115 LEU HG H 1.61 . 1 1214 115 115 LEU C C 177.44 . 1 1215 115 115 LEU CA C 55.44 . 1 1216 115 115 LEU CB C 42.25 . 1 1217 115 115 LEU CD1 C 25.28 . 2 1218 115 115 LEU CD2 C 23.51 . 2 1219 115 115 LEU CG C 26.96 . 1 1220 115 115 LEU N N 120.58 . 1 1221 116 116 GLN H H 8.18 . 1 1222 116 116 GLN HA H 4.36 . 1 1223 116 116 GLN HB2 H 1.99 . 2 1224 116 116 GLN HB3 H 2.09 . 2 1225 116 116 GLN HE21 H 6.80 . 1 1226 116 116 GLN HE22 H 7.50 . 1 1227 116 116 GLN HG2 H 2.34 . 2 1228 116 116 GLN HG3 H 2.36 . 2 1229 116 116 GLN C C 175.89 . 1 1230 116 116 GLN CA C 55.81 . 1 1231 116 116 GLN CB C 29.50 . 1 1232 116 116 GLN CG C 33.85 . 1 1233 116 116 GLN N N 119.77 . 1 1234 117 117 GLN H H 8.35 . 1 1235 117 117 GLN HA H 4.38 . 1 1236 117 117 GLN HB2 H 2.00 . 2 1237 117 117 GLN HB3 H 2.11 . 2 1238 117 117 GLN HE21 H 6.80 . 1 1239 117 117 GLN HE22 H 7.50 . 1 1240 117 117 GLN HG2 H 2.36 . 2 1241 117 117 GLN HG3 H 2.36 . 2 1242 117 117 GLN C C 176.13 . 1 1243 117 117 GLN CA C 55.81 . 1 1244 117 117 GLN CB C 29.50 . 1 1245 117 117 GLN CG C 33.85 . 1 1246 117 117 GLN N N 121.44 . 1 1247 118 118 VAL H H 8.24 . 1 1248 118 118 VAL HA H 4.12 . 1 1249 118 118 VAL HB H 2.08 . 1 1250 118 118 VAL HG1 H 0.90 . 2 1251 118 118 VAL HG2 H 0.90 . 2 1252 118 118 VAL C C 176.65 . 1 1253 118 118 VAL CA C 62.72 . 1 1254 118 118 VAL CB C 32.73 . 1 1255 118 118 VAL CG1 C 20.90 . 2 1256 118 118 VAL CG2 C 20.90 . 2 1257 118 118 VAL N N 121.25 . 1 1258 119 119 GLY H H 8.46 . 1 1259 119 119 GLY HA2 H 3.99 . 2 1260 119 119 GLY HA3 H 3.99 . 2 1261 119 119 GLY C C 173.77 . 1 1262 119 119 GLY CA C 45.26 . 1 1263 119 119 GLY N N 112.30 . 1 1264 120 120 ASP H H 8.23 . 1 1265 120 120 ASP HA H 4.58 . 1 1266 120 120 ASP HB2 H 2.61 . 2 1267 120 120 ASP HB3 H 2.65 . 2 1268 120 120 ASP C C 175.18 . 1 1269 120 120 ASP CA C 54.34 . 1 1270 120 120 ASP CB C 41.39 . 1 1271 120 120 ASP N N 120.42 . 1 1272 121 121 LYS H H 7.95 . 1 1273 121 121 LYS HA H 4.24 . 1 1274 121 121 LYS CA C 53.62 . 1 1275 121 121 LYS N N 119.11 . 1 1276 122 122 PRO HA H 4.41 . 1 1277 122 122 PRO C C 176.56 . 1 1278 122 122 PRO CA C 63.13 . 1 1279 123 123 ARG H H 8.40 . 1 1280 123 123 ARG HA H 4.62 . 1 1281 123 123 ARG CA C 53.83 . 1 1282 123 123 ARG N N 122.91 . 1 stop_ save_