data_15490 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of E coli NusG carboxyterminal domain ; _BMRB_accession_number 15490 _BMRB_flat_file_name bmr15490.str _Entry_type original _Submission_date 2007-09-26 _Accession_date 2007-09-26 _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" 336 "13C chemical shifts" 254 "15N chemical shifts" 54 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-21 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 $NusG 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_NusG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NusG _Molecular_mass . _Mol_thiol_state 'all free' _Details 'Only the carboxyterminal domain (res. 124-181) gave interpretable NMR data for assignment and structure determination' ############################## # Polymer residue sequence # ############################## _Residue_count 181 _Mol_residue_sequence ; MSEAPKKRWYVVQAFSGFEG RVATSLREHIKLHNMEDLFG EVMVPTEEVVEIRGGQRRKS ERKFFPGYVLVQMVMNDASW HLVRSVPRVMGFIGGTSDRP APISDKEVDAIMNRLQQVGD KPRPKTLFEPGEMVRVNDGP FADFNGVVEEVDYEKSRLKV SVSIFGRATPVELDFSQVEK A ; 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 124 PRO 125 LYS 126 THR 127 LEU 128 PHE 129 GLU 130 PRO 131 GLY 132 GLU 133 MET 134 VAL 135 ARG 136 VAL 137 ASN 138 ASP 139 GLY 140 PRO 141 PHE 142 ALA 143 ASP 144 PHE 145 ASN 146 GLY 147 VAL 148 VAL 149 GLU 150 GLU 151 VAL 152 ASP 153 TYR 154 GLU 155 LYS 156 SER 157 ARG 158 LEU 159 LYS 160 VAL 161 SER 162 VAL 163 SER 164 ILE 165 PHE 166 GLY 167 ARG 168 ALA 169 THR 170 PRO 171 VAL 172 GLU 173 LEU 174 ASP 175 PHE 176 SER 177 GLN 178 VAL 179 GLU 180 LYS 181 ALA 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 15642 NusG 67.96 123 100.00 100.00 5.26e-83 PDB 2JVV "Solution Structure Of E. Coli Nusg Carboxyterminal Domain" 100.00 181 100.00 100.00 4.51e-127 PDB 2K06 "Solution Structure Of The Aminoterminal Domain Of E. Coli Nusg" 67.96 123 100.00 100.00 5.26e-83 DBJ BAB38328 "component in transcription antitermination [Escherichia coli O157:H7 str. Sakai]" 100.00 181 100.00 100.00 4.51e-127 DBJ BAE77338 "transcription termination factor [Escherichia coli str. K12 substr. W3110]" 100.00 181 100.00 100.00 4.51e-127 DBJ BAG79793 "transcription antitermination protein [Escherichia coli SE11]" 100.00 181 100.00 100.00 4.51e-127 DBJ BAH61119 "transcription antitermination protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 181 99.45 100.00 2.27e-126 DBJ BAI28242 "transcription termination factor NusG [Escherichia coli O26:H11 str. 11368]" 100.00 181 100.00 100.00 4.51e-127 EMBL CAD09492 "transcription antitermination protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 181 99.45 100.00 2.27e-126 EMBL CAG73137 "transcription antitermination protein [Pectobacterium atrosepticum SCRI1043]" 100.00 181 97.24 98.34 2.60e-123 EMBL CAO95196 "Transcription antitermination protein [Erwinia tasmaniensis Et1/99]" 100.00 181 97.24 98.34 2.43e-123 EMBL CAP78438 "Transcription antitermination protein nusG [Escherichia coli LF82]" 100.00 181 99.45 100.00 2.27e-126 EMBL CAQ34328 "transcription termination factor NusG [Escherichia coli BL21(DE3)]" 100.00 181 100.00 100.00 4.51e-127 GB AAA24622 "NusG protein [Escherichia coli]" 100.00 181 100.00 100.00 4.51e-127 GB AAC43080 "ORF_o181 [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 4.51e-127 GB AAC76956 "transcription termination factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 4.51e-127 GB AAF33495 "99% identity over 181 amino acids with E. coli transcription antitermination factor (NUSG) (SW:P16921) [Salmonella enterica sub" 100.00 181 99.45 100.00 2.27e-126 GB AAG59178 "component in transcription antitermination [Escherichia coli O157:H7 str. EDL933]" 100.00 181 100.00 100.00 4.51e-127 PIR AB0934 "transcription antitermination protein STY3737 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 181 99.45 100.00 2.27e-126 REF NP_312932 "transcription antitermination protein NusG [Escherichia coli O157:H7 str. Sakai]" 100.00 181 100.00 100.00 4.51e-127 REF NP_418409 "transcription termination factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 181 100.00 100.00 4.51e-127 REF NP_457922 "transcription antitermination protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 181 99.45 100.00 2.27e-126 REF NP_463017 "transcription termination/antitermination protein NusG [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 181 99.45 100.00 2.27e-126 REF NP_709777 "transcription antitermination protein NusG [Shigella flexneri 2a str. 301]" 100.00 181 100.00 100.00 4.51e-127 SP P0AA01 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.45 100.00 2.27e-126 SP P0AA02 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.45 100.00 2.27e-126 SP P0AA03 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 99.45 100.00 2.27e-126 SP P0AFG0 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 100.00 100.00 4.51e-127 SP P0AFG1 "RecName: Full=Transcription termination/antitermination protein NusG" 100.00 181 100.00 100.00 4.51e-127 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NusG 'E. coli' 562 Eubacteria . 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 $NusG 'recombinant technology' . Escherichia coli BL21(DE3) 'pET 11a' 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 $NusG 0.45 mM '[U-95% 13C; U-95% 15N]' 'potassium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' H2O 90 % . D2O 10 % . 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' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 1.2.1 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement '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 900 _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_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_10 _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_ _Software_label $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HCCH-TOCSY' 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 1 124 124 PRO HA H 4.43 0.03 1 2 124 124 PRO HB2 H 1.86 0.03 2 3 124 124 PRO HB3 H 2.31 0.03 2 4 124 124 PRO HD2 H 3.86 0.03 2 5 124 124 PRO HD3 H 3.63 0.03 2 6 124 124 PRO HG2 H 2.04 0.03 2 7 124 124 PRO HG3 H 1.99 0.03 2 8 124 124 PRO C C 176.76 0.2 1 9 124 124 PRO CA C 62.93 0.2 1 10 124 124 PRO CB C 32.21 0.2 1 11 124 124 PRO CD C 50.60 0.2 1 12 124 124 PRO CG C 27.50 0.2 1 13 125 125 LYS H H 8.52 0.03 1 14 125 125 LYS HA H 4.27 0.03 1 15 125 125 LYS HB2 H 1.74 0.03 2 16 125 125 LYS HB3 H 1.83 0.03 2 17 125 125 LYS HD3 H 1.70 0.03 2 18 125 125 LYS HE3 H 2.99 0.03 2 19 125 125 LYS HG2 H 1.43 0.03 2 20 125 125 LYS HG3 H 1.50 0.03 2 21 125 125 LYS C C 176.62 0.2 1 22 125 125 LYS CA C 56.79 0.2 1 23 125 125 LYS CB C 32.66 0.2 1 24 125 125 LYS CD C 29.21 0.2 1 25 125 125 LYS CE C 42.10 0.2 1 26 125 125 LYS CG C 24.91 0.2 1 27 125 125 LYS N N 121.94 0.1 1 28 126 126 THR H H 8.02 0.03 1 29 126 126 THR HA H 4.14 0.03 1 30 126 126 THR HB H 4.00 0.03 1 31 126 126 THR HG2 H 0.91 0.03 1 32 126 126 THR C C 172.84 0.2 1 33 126 126 THR CA C 61.89 0.2 1 34 126 126 THR CB C 69.84 0.2 1 35 126 126 THR CG2 C 22.20 0.2 1 36 126 126 THR N N 116.37 0.1 1 37 127 127 LEU H H 7.93 0.03 1 38 127 127 LEU HA H 4.55 0.03 1 39 127 127 LEU HB2 H 1.38 0.03 2 40 127 127 LEU HB3 H 1.49 0.03 2 41 127 127 LEU HD1 H 0.85 0.03 2 42 127 127 LEU HD2 H 0.78 0.03 2 43 127 127 LEU HG H 1.46 0.03 1 44 127 127 LEU C C 175.75 0.2 1 45 127 127 LEU CA C 54.56 0.2 1 46 127 127 LEU CB C 43.48 0.2 1 47 127 127 LEU CD1 C 25.11 0.2 2 48 127 127 LEU CD2 C 23.76 0.2 2 49 127 127 LEU CG C 27.00 0.2 1 50 127 127 LEU N N 124.51 0.1 1 51 128 128 PHE H H 7.62 0.03 1 52 128 128 PHE HA H 4.97 0.03 1 53 128 128 PHE HB2 H 2.19 0.03 2 54 128 128 PHE HB3 H 2.60 0.03 2 55 128 128 PHE HD1 H 6.38 0.03 1 56 128 128 PHE HD2 H 6.38 0.03 1 57 128 128 PHE HE1 H 6.49 0.03 1 58 128 128 PHE HE2 H 6.49 0.03 1 59 128 128 PHE HZ H 6.97 0.03 1 60 128 128 PHE C C 174.32 0.2 1 61 128 128 PHE CA C 56.63 0.2 1 62 128 128 PHE CB C 44.08 0.2 1 63 128 128 PHE CD1 C 131.50 0.2 1 64 128 128 PHE CD2 C 131.50 0.2 1 65 128 128 PHE CE1 C 130.70 0.2 1 66 128 128 PHE CE2 C 130.70 0.2 1 67 128 128 PHE CZ C 129.70 0.2 1 68 128 128 PHE N N 117.32 0.1 1 69 129 129 GLU H H 9.02 0.03 1 70 129 129 GLU HA H 4.94 0.03 1 71 129 129 GLU HB2 H 1.78 0.03 2 72 129 129 GLU HB3 H 2.02 0.03 2 73 129 129 GLU HG2 H 2.22 0.03 1 74 129 129 GLU HG3 H 2.22 0.03 1 75 129 129 GLU CA C 52.80 0.2 1 76 129 129 GLU CB C 32.00 0.2 1 77 129 129 GLU CG C 35.78 0.2 1 78 129 129 GLU N N 120.56 0.1 1 79 130 130 PRO HA H 3.93 0.03 1 80 130 130 PRO HB2 H 1.93 0.03 2 81 130 130 PRO HB3 H 2.23 0.03 2 82 130 130 PRO HD2 H 3.75 0.03 2 83 130 130 PRO HD3 H 3.83 0.03 2 84 130 130 PRO HG2 H 1.74 0.03 2 85 130 130 PRO HG3 H 2.33 0.03 2 86 130 130 PRO C C 177.35 0.2 1 87 130 130 PRO CA C 63.78 0.2 1 88 130 130 PRO CB C 31.45 0.2 1 89 130 130 PRO CD C 50.83 0.2 1 90 130 130 PRO CG C 28.77 0.2 1 91 131 131 GLY H H 9.36 0.03 1 92 131 131 GLY HA2 H 3.48 0.03 2 93 131 131 GLY HA3 H 4.45 0.03 2 94 131 131 GLY C C 174.25 0.2 1 95 131 131 GLY CA C 44.89 0.2 1 96 131 131 GLY N N 112.98 0.1 1 97 132 132 GLU H H 7.84 0.03 1 98 132 132 GLU HA H 4.40 0.03 1 99 132 132 GLU HB2 H 2.06 0.03 1 100 132 132 GLU HB3 H 2.06 0.03 1 101 132 132 GLU HG2 H 2.39 0.03 1 102 132 132 GLU HG3 H 2.39 0.03 1 103 132 132 GLU C C 175.03 0.2 1 104 132 132 GLU CA C 56.69 0.2 1 105 132 132 GLU CB C 31.60 0.2 1 106 132 132 GLU CG C 36.70 0.2 1 107 132 132 GLU N N 120.83 0.1 1 108 133 133 MET H H 8.68 0.03 1 109 133 133 MET HA H 5.28 0.03 1 110 133 133 MET HB2 H 2.10 0.03 1 111 133 133 MET HB3 H 2.10 0.03 1 112 133 133 MET HE H 2.04 0.03 1 113 133 133 MET HG2 H 2.55 0.03 2 114 133 133 MET HG3 H 2.65 0.03 2 115 133 133 MET C C 176.67 0.2 1 116 133 133 MET CA C 54.60 0.2 1 117 133 133 MET CB C 33.03 0.2 1 118 133 133 MET CE C 16.60 0.2 1 119 133 133 MET CG C 32.16 0.2 1 120 133 133 MET N N 121.97 0.1 1 121 134 134 VAL H H 9.08 0.03 1 122 134 134 VAL HA H 5.06 0.03 1 123 134 134 VAL HB H 2.05 0.03 1 124 134 134 VAL HG1 H 0.43 0.03 2 125 134 134 VAL HG2 H 0.67 0.03 2 126 134 134 VAL C C 173.77 0.2 1 127 134 134 VAL CA C 58.65 0.2 1 128 134 134 VAL CB C 36.09 0.2 1 129 134 134 VAL CG1 C 17.96 0.2 2 130 134 134 VAL CG2 C 22.35 0.2 2 131 134 134 VAL N N 116.28 0.1 1 132 135 135 ARG H H 9.03 0.03 1 133 135 135 ARG HA H 4.98 0.03 1 134 135 135 ARG HB2 H 1.61 0.03 2 135 135 135 ARG HB3 H 1.70 0.03 2 136 135 135 ARG HD2 H 3.19 0.03 2 137 135 135 ARG HD3 H 3.24 0.03 2 138 135 135 ARG HG2 H 1.42 0.03 2 139 135 135 ARG HG3 H 1.46 0.03 2 140 135 135 ARG C C 175.54 0.2 1 141 135 135 ARG CA C 54.62 0.2 1 142 135 135 ARG CB C 33.24 0.2 1 143 135 135 ARG CD C 43.50 0.2 1 144 135 135 ARG CG C 27.67 0.2 1 145 135 135 ARG N N 121.68 0.1 1 146 136 136 VAL H H 8.75 0.03 1 147 136 136 VAL HA H 4.24 0.03 1 148 136 136 VAL HB H 2.56 0.03 1 149 136 136 VAL HG1 H 1.08 0.03 2 150 136 136 VAL HG2 H 0.72 0.03 2 151 136 136 VAL C C 177.25 0.2 1 152 136 136 VAL CA C 63.22 0.2 1 153 136 136 VAL CB C 31.02 0.2 1 154 136 136 VAL CG1 C 22.90 0.2 2 155 136 136 VAL CG2 C 21.06 0.2 2 156 136 136 VAL N N 127.25 0.1 1 157 137 137 ASN H H 9.16 0.03 1 158 137 137 ASN HA H 5.14 0.03 1 159 137 137 ASN HB2 H 2.93 0.03 2 160 137 137 ASN HB3 H 2.52 0.03 2 161 137 137 ASN C C 175.26 0.2 1 162 137 137 ASN CA C 52.56 0.2 1 163 137 137 ASN CB C 40.72 0.2 1 164 137 137 ASN N N 125.31 0.1 1 165 138 138 ASP H H 7.31 0.03 1 166 138 138 ASP HA H 4.99 0.03 1 167 138 138 ASP HB2 H 2.39 0.03 2 168 138 138 ASP HB3 H 2.99 0.03 2 169 138 138 ASP C C 174.63 0.2 1 170 138 138 ASP CA C 54.03 0.2 1 171 138 138 ASP CB C 45.99 0.2 1 172 138 138 ASP N N 117.20 0.1 1 173 139 139 GLY H H 8.27 0.03 1 174 139 139 GLY HA2 H 3.85 0.03 2 175 139 139 GLY HA3 H 4.37 0.03 2 176 139 139 GLY CA C 45.27 0.2 1 177 139 139 GLY N N 108.68 0.1 1 178 140 140 PRO HA H 4.19 0.03 1 179 140 140 PRO HB2 H 1.14 0.03 2 180 140 140 PRO HB3 H 2.06 0.03 2 181 140 140 PRO HD2 H 3.50 0.03 2 182 140 140 PRO HD3 H 3.80 0.03 2 183 140 140 PRO HG2 H 1.78 0.03 2 184 140 140 PRO HG3 H 1.87 0.03 2 185 140 140 PRO C C 177.81 0.2 1 186 140 140 PRO CA C 64.49 0.2 1 187 140 140 PRO CB C 31.61 0.2 1 188 140 140 PRO CD C 49.56 0.2 1 189 140 140 PRO CG C 27.15 0.2 1 190 141 141 PHE H H 8.96 0.03 1 191 141 141 PHE HA H 4.58 0.03 1 192 141 141 PHE HB2 H 2.94 0.03 2 193 141 141 PHE HB3 H 3.23 0.03 2 194 141 141 PHE HD1 H 6.76 0.03 1 195 141 141 PHE HD2 H 6.76 0.03 1 196 141 141 PHE HE1 H 7.10 0.03 1 197 141 141 PHE HE2 H 7.10 0.03 1 198 141 141 PHE HZ H 7.33 0.03 1 199 141 141 PHE C C 173.30 0.2 1 200 141 141 PHE CA C 56.74 0.2 1 201 141 141 PHE CB C 37.00 0.2 1 202 141 141 PHE CD1 C 131.20 0.2 1 203 141 141 PHE CD2 C 131.20 0.2 1 204 141 141 PHE CE1 C 131.20 0.2 1 205 141 141 PHE CE2 C 131.20 0.2 1 206 141 141 PHE N N 116.14 0.1 1 207 142 142 ALA H H 7.40 0.03 1 208 142 142 ALA HA H 3.52 0.03 1 209 142 142 ALA HB H 1.23 0.03 1 210 142 142 ALA C C 178.01 0.2 1 211 142 142 ALA CA C 54.09 0.2 1 212 142 142 ALA CB C 17.99 0.2 1 213 142 142 ALA N N 121.25 0.1 1 214 143 143 ASP H H 8.93 0.03 1 215 143 143 ASP HA H 4.19 0.03 1 216 143 143 ASP HB2 H 2.81 0.03 2 217 143 143 ASP HB3 H 3.00 0.03 2 218 143 143 ASP C C 176.18 0.2 1 219 143 143 ASP CA C 57.21 0.2 1 220 143 143 ASP CB C 39.67 0.2 1 221 143 143 ASP N N 113.70 0.1 1 222 144 144 PHE H H 8.28 0.03 1 223 144 144 PHE HA H 4.72 0.03 1 224 144 144 PHE HB2 H 3.08 0.03 2 225 144 144 PHE HB3 H 3.38 0.03 2 226 144 144 PHE HD1 H 7.37 0.03 1 227 144 144 PHE HD2 H 7.37 0.03 1 228 144 144 PHE HE1 H 7.13 0.03 1 229 144 144 PHE HE2 H 7.13 0.03 1 230 144 144 PHE C C 174.94 0.2 1 231 144 144 PHE CA C 58.38 0.2 1 232 144 144 PHE CB C 39.69 0.2 1 233 144 144 PHE N N 119.10 0.1 1 234 145 145 ASN H H 8.85 0.03 1 235 145 145 ASN HA H 5.74 0.03 1 236 145 145 ASN HB2 H 2.75 0.03 2 237 145 145 ASN HB3 H 2.81 0.03 2 238 145 145 ASN C C 175.29 0.2 1 239 145 145 ASN CA C 52.01 0.2 1 240 145 145 ASN CB C 41.20 0.2 1 241 145 145 ASN N N 117.59 0.1 1 242 146 146 GLY H H 8.95 0.03 1 243 146 146 GLY HA2 H 3.48 0.03 2 244 146 146 GLY HA3 H 4.72 0.03 2 245 146 146 GLY C C 170.78 0.2 1 246 146 146 GLY CA C 45.76 0.2 1 247 146 146 GLY N N 105.84 0.1 1 248 147 147 VAL H H 8.01 0.03 1 249 147 147 VAL HA H 4.90 0.03 1 250 147 147 VAL HB H 1.88 0.03 1 251 147 147 VAL HG1 H 0.94 0.03 2 252 147 147 VAL HG2 H 0.87 0.03 2 253 147 147 VAL C C 176.20 0.2 1 254 147 147 VAL CA C 59.90 0.2 1 255 147 147 VAL CB C 34.81 0.2 1 256 147 147 VAL CG1 C 21.53 0.2 2 257 147 147 VAL CG2 C 20.82 0.2 2 258 147 147 VAL N N 118.32 0.1 1 259 148 148 VAL H H 9.05 0.03 1 260 148 148 VAL HA H 3.67 0.03 1 261 148 148 VAL HB H 2.34 0.03 1 262 148 148 VAL HG1 H 0.89 0.03 2 263 148 148 VAL HG2 H 0.57 0.03 2 264 148 148 VAL C C 176.28 0.2 1 265 148 148 VAL CA C 64.99 0.2 1 266 148 148 VAL CB C 32.05 0.2 1 267 148 148 VAL CG1 C 23.70 0.2 2 268 148 148 VAL CG2 C 22.94 0.2 2 269 148 148 VAL N N 126.69 0.1 1 270 149 149 GLU H H 9.57 0.03 1 271 149 149 GLU HA H 4.66 0.03 1 272 149 149 GLU HB2 H 1.68 0.03 2 273 149 149 GLU HB3 H 2.03 0.03 2 274 149 149 GLU HG2 H 2.13 0.03 2 275 149 149 GLU HG3 H 2.23 0.03 2 276 149 149 GLU C C 176.01 0.2 1 277 149 149 GLU CA C 57.46 0.2 1 278 149 149 GLU CB C 31.91 0.2 1 279 149 149 GLU CG C 36.01 0.2 1 280 149 149 GLU N N 129.00 0.1 1 281 150 150 GLU H H 7.66 0.03 1 282 150 150 GLU HA H 4.62 0.03 1 283 150 150 GLU HB2 H 1.88 0.03 2 284 150 150 GLU HB3 H 2.01 0.03 2 285 150 150 GLU HG2 H 2.18 0.03 2 286 150 150 GLU HG3 H 2.27 0.03 2 287 150 150 GLU C C 173.74 0.2 1 288 150 150 GLU CA C 55.39 0.2 1 289 150 150 GLU CB C 34.58 0.2 1 290 150 150 GLU CG C 36.43 0.2 1 291 150 150 GLU N N 115.69 0.1 1 292 151 151 VAL H H 8.89 0.03 1 293 151 151 VAL HA H 4.24 0.03 1 294 151 151 VAL HB H 1.80 0.03 1 295 151 151 VAL HG1 H 0.58 0.03 1 296 151 151 VAL HG2 H 0.58 0.03 1 297 151 151 VAL C C 173.46 0.2 1 298 151 151 VAL CA C 61.78 0.2 1 299 151 151 VAL CB C 34.94 0.2 1 300 151 151 VAL CG1 C 21.17 0.2 2 301 151 151 VAL CG2 C 21.17 0.2 2 302 151 151 VAL N N 122.37 0.1 1 303 152 152 ASP H H 8.77 0.03 1 304 152 152 ASP HA H 5.00 0.03 1 305 152 152 ASP HB2 H 2.44 0.03 2 306 152 152 ASP HB3 H 2.91 0.03 2 307 152 152 ASP C C 176.92 0.2 1 308 152 152 ASP CA C 52.01 0.2 1 309 152 152 ASP CB C 41.68 0.2 1 310 152 152 ASP N N 126.68 0.1 1 311 153 153 TYR H H 8.96 0.03 1 312 153 153 TYR HA H 4.32 0.03 1 313 153 153 TYR HB2 H 3.01 0.03 2 314 153 153 TYR HB3 H 3.29 0.03 2 315 153 153 TYR HD1 H 7.46 0.03 1 316 153 153 TYR HD2 H 7.46 0.03 1 317 153 153 TYR HE1 H 7.16 0.03 1 318 153 153 TYR HE2 H 7.16 0.03 1 319 153 153 TYR C C 178.19 0.2 1 320 153 153 TYR CA C 61.91 0.2 1 321 153 153 TYR CB C 38.52 0.2 1 322 153 153 TYR CD1 C 133.30 0.2 1 323 153 153 TYR CD2 C 133.30 0.2 1 324 153 153 TYR CE1 C 118.80 0.2 1 325 153 153 TYR CE2 C 118.80 0.2 1 326 153 153 TYR N N 122.73 0.1 1 327 154 154 GLU H H 8.47 0.03 1 328 154 154 GLU HA H 4.17 0.03 1 329 154 154 GLU HB2 H 2.19 0.03 2 330 154 154 GLU HB3 H 2.28 0.03 2 331 154 154 GLU HG2 H 2.31 0.03 2 332 154 154 GLU HG3 H 2.41 0.03 2 333 154 154 GLU C C 175.96 0.2 1 334 154 154 GLU CA C 59.38 0.2 1 335 154 154 GLU CB C 29.40 0.2 1 336 154 154 GLU CG C 36.68 0.2 1 337 154 154 GLU N N 120.47 0.1 1 338 155 155 LYS H H 7.51 0.03 1 339 155 155 LYS HA H 4.31 0.03 1 340 155 155 LYS HB2 H 1.29 0.03 2 341 155 155 LYS HB3 H 1.83 0.03 2 342 155 155 LYS HD2 H 1.57 0.03 1 343 155 155 LYS HD3 H 1.57 0.03 1 344 155 155 LYS HE2 H 2.94 0.03 2 345 155 155 LYS HE3 H 3.03 0.03 2 346 155 155 LYS HG2 H 1.29 0.03 2 347 155 155 LYS HG3 H 1.45 0.03 2 348 155 155 LYS C C 175.60 0.2 1 349 155 155 LYS CA C 55.12 0.2 1 350 155 155 LYS CB C 33.00 0.2 1 351 155 155 LYS CD C 29.45 0.2 1 352 155 155 LYS CE C 42.24 0.2 1 353 155 155 LYS CG C 25.45 0.2 1 354 155 155 LYS N N 115.61 0.1 1 355 156 156 SER H H 7.42 0.03 1 356 156 156 SER HA H 2.46 0.03 1 357 156 156 SER HB2 H 3.22 0.03 2 358 156 156 SER HB3 H 3.92 0.03 2 359 156 156 SER C C 173.97 0.2 1 360 156 156 SER CA C 58.28 0.2 1 361 156 156 SER CB C 61.03 0.2 1 362 156 156 SER N N 114.11 0.1 1 363 157 157 ARG H H 7.76 0.03 1 364 157 157 ARG HA H 5.18 0.03 1 365 157 157 ARG HB2 H 1.45 0.03 2 366 157 157 ARG HB3 H 1.73 0.03 2 367 157 157 ARG HD2 H 3.04 0.03 2 368 157 157 ARG HD3 H 3.15 0.03 2 369 157 157 ARG HG2 H 1.53 0.03 2 370 157 157 ARG HG3 H 1.58 0.03 2 371 157 157 ARG C C 174.09 0.2 1 372 157 157 ARG CA C 53.33 0.2 1 373 157 157 ARG CB C 35.10 0.2 1 374 157 157 ARG CD C 43.22 0.2 1 375 157 157 ARG CG C 26.57 0.2 1 376 157 157 ARG N N 117.59 0.1 1 377 158 158 LEU H H 9.45 0.03 1 378 158 158 LEU HA H 5.01 0.03 1 379 158 158 LEU HB2 H 1.52 0.03 2 380 158 158 LEU HB3 H 1.27 0.03 2 381 158 158 LEU HD1 H 0.04 0.03 2 382 158 158 LEU HD2 H 0.39 0.03 2 383 158 158 LEU HG H 1.34 0.03 1 384 158 158 LEU C C 175.11 0.2 1 385 158 158 LEU CA C 53.39 0.2 1 386 158 158 LEU CB C 46.43 0.2 1 387 158 158 LEU CD1 C 26.69 0.2 2 388 158 158 LEU CD2 C 25.77 0.2 2 389 158 158 LEU CG C 26.49 0.2 1 390 158 158 LEU N N 121.51 0.1 1 391 159 159 LYS H H 8.46 0.03 1 392 159 159 LYS HA H 5.02 0.03 1 393 159 159 LYS HB2 H 1.67 0.03 2 394 159 159 LYS HB3 H 1.73 0.03 2 395 159 159 LYS HD2 H 1.53 0.03 2 396 159 159 LYS HD3 H 1.60 0.03 2 397 159 159 LYS HE2 H 2.85 0.03 1 398 159 159 LYS HE3 H 2.85 0.03 1 399 159 159 LYS HG2 H 1.16 0.03 2 400 159 159 LYS HG3 H 1.30 0.03 2 401 159 159 LYS C C 175.51 0.2 1 402 159 159 LYS CA C 55.60 0.2 1 403 159 159 LYS CB C 34.38 0.2 1 404 159 159 LYS CD C 29.45 0.2 1 405 159 159 LYS CE C 41.95 0.2 1 406 159 159 LYS CG C 25.29 0.2 1 407 159 159 LYS N N 121.37 0.1 1 408 160 160 VAL H H 9.19 0.03 1 409 160 160 VAL HA H 4.69 0.03 1 410 160 160 VAL HB H 1.61 0.03 1 411 160 160 VAL HG1 H 0.41 0.03 2 412 160 160 VAL HG2 H 0.58 0.03 2 413 160 160 VAL C C 174.11 0.2 1 414 160 160 VAL CA C 59.51 0.2 1 415 160 160 VAL CB C 35.23 0.2 1 416 160 160 VAL CG1 C 21.35 0.2 2 417 160 160 VAL CG2 C 22.54 0.2 2 418 160 160 VAL N N 125.89 0.1 1 419 161 161 SER H H 9.00 0.03 1 420 161 161 SER HA H 4.72 0.03 1 421 161 161 SER HB2 H 3.68 0.03 2 422 161 161 SER HB3 H 3.68 0.03 2 423 161 161 SER C C 175.06 0.2 1 424 161 161 SER CA C 56.95 0.2 1 425 161 161 SER CB C 62.93 0.2 1 426 161 161 SER N N 120.52 0.1 1 427 162 162 VAL H H 8.76 0.03 1 428 162 162 VAL HA H 4.37 0.03 1 429 162 162 VAL HB H 1.75 0.03 1 430 162 162 VAL HG1 H 0.65 0.03 2 431 162 162 VAL HG2 H 0.47 0.03 2 432 162 162 VAL C C 174.96 0.2 1 433 162 162 VAL CA C 60.91 0.2 1 434 162 162 VAL CB C 33.63 0.2 1 435 162 162 VAL CG1 C 21.92 0.2 2 436 162 162 VAL CG2 C 20.91 0.2 2 437 162 162 VAL N N 127.97 0.1 1 438 163 163 SER H H 8.80 0.03 1 439 163 163 SER HA H 4.61 0.03 1 440 163 163 SER HB2 H 3.68 0.03 2 441 163 163 SER HB3 H 3.83 0.03 2 442 163 163 SER C C 173.93 0.2 1 443 163 163 SER CA C 57.37 0.2 1 444 163 163 SER CB C 63.03 0.2 1 445 163 163 SER N N 120.41 0.1 1 446 164 164 ILE H H 8.27 0.03 1 447 164 164 ILE HA H 4.06 0.03 1 448 164 164 ILE HB H 1.69 0.03 1 449 164 164 ILE HD1 H 0.46 0.03 1 450 164 164 ILE HG12 H 0.55 0.03 2 451 164 164 ILE HG13 H 1.16 0.03 2 452 164 164 ILE HG2 H 0.69 0.03 1 453 164 164 ILE C C 175.87 0.2 1 454 164 164 ILE CA C 60.23 0.2 1 455 164 164 ILE CB C 38.24 0.2 1 456 164 164 ILE CD1 C 13.17 0.2 1 457 164 164 ILE CG1 C 26.80 0.2 1 458 164 164 ILE CG2 C 17.01 0.2 1 459 164 164 ILE N N 127.59 0.1 1 460 165 165 PHE H H 8.94 0.03 1 461 165 165 PHE HA H 4.34 0.03 1 462 165 165 PHE HB2 H 3.12 0.03 2 463 165 165 PHE HB3 H 3.42 0.03 2 464 165 165 PHE HD1 H 7.28 0.03 1 465 165 165 PHE HD2 H 7.28 0.03 1 466 165 165 PHE C C 176.27 0.2 1 467 165 165 PHE CA C 58.52 0.2 1 468 165 165 PHE CB C 36.99 0.2 1 469 165 165 PHE CD1 C 131.80 0.2 1 470 165 165 PHE CD2 C 131.80 0.2 1 471 165 165 PHE N N 126.14 0.1 1 472 166 166 GLY H H 8.18 0.03 1 473 166 166 GLY HA2 H 3.55 0.03 2 474 166 166 GLY HA3 H 4.22 0.03 2 475 166 166 GLY C C 173.80 0.2 1 476 166 166 GLY CA C 45.42 0.2 1 477 166 166 GLY N N 103.47 0.1 1 478 167 167 ARG H H 7.80 0.03 1 479 167 167 ARG HA H 4.59 0.03 1 480 167 167 ARG HB2 H 1.81 0.03 2 481 167 167 ARG HB3 H 1.89 0.03 2 482 167 167 ARG HD2 H 3.20 0.03 2 483 167 167 ARG HD3 H 3.25 0.03 2 484 167 167 ARG HG2 H 1.64 0.03 2 485 167 167 ARG HG3 H 1.54 0.03 2 486 167 167 ARG C C 175.62 0.2 1 487 167 167 ARG CA C 54.75 0.2 1 488 167 167 ARG CB C 31.72 0.2 1 489 167 167 ARG CD C 43.60 0.2 1 490 167 167 ARG CG C 27.20 0.2 1 491 167 167 ARG N N 120.96 0.1 1 492 168 168 ALA H H 8.72 0.03 1 493 168 168 ALA HA H 4.52 0.03 1 494 168 168 ALA HB H 1.25 0.03 1 495 168 168 ALA C C 177.69 0.2 1 496 168 168 ALA CA C 52.83 0.2 1 497 168 168 ALA CB C 18.73 0.2 1 498 168 168 ALA N N 130.96 0.1 1 499 169 169 THR H H 9.06 0.03 1 500 169 169 THR HA H 4.74 0.03 1 501 169 169 THR HB H 3.88 0.03 1 502 169 169 THR HG2 H 1.03 0.03 1 503 169 169 THR CA C 59.87 0.2 1 504 169 169 THR CB C 72.27 0.2 1 505 169 169 THR CG2 C 19.60 0.2 1 506 169 169 THR N N 122.74 0.1 1 507 170 170 PRO HA H 4.96 0.03 1 508 170 170 PRO HB2 H 1.76 0.03 2 509 170 170 PRO HB3 H 2.06 0.03 2 510 170 170 PRO HD2 H 3.83 0.03 2 511 170 170 PRO HD3 H 3.62 0.03 2 512 170 170 PRO HG2 H 2.03 0.03 2 513 170 170 PRO HG3 H 2.20 0.03 2 514 170 170 PRO C C 177.05 0.2 1 515 170 170 PRO CA C 62.15 0.2 1 516 170 170 PRO CB C 31.63 0.2 1 517 170 170 PRO CD C 50.64 0.2 1 518 170 170 PRO CG C 27.16 0.2 1 519 171 171 VAL H H 9.08 0.03 1 520 171 171 VAL HA H 4.26 0.03 1 521 171 171 VAL HB H 1.72 0.03 1 522 171 171 VAL HG1 H 0.42 0.03 2 523 171 171 VAL HG2 H 0.61 0.03 2 524 171 171 VAL C C 173.82 0.2 1 525 171 171 VAL CA C 60.91 0.2 1 526 171 171 VAL CB C 35.40 0.2 1 527 171 171 VAL CG1 C 20.40 0.2 2 528 171 171 VAL CG2 C 21.17 0.2 2 529 171 171 VAL N N 122.94 0.1 1 530 172 172 GLU H H 8.44 0.03 1 531 172 172 GLU HA H 5.26 0.03 1 532 172 172 GLU HB2 H 1.83 0.03 2 533 172 172 GLU HB3 H 1.88 0.03 2 534 172 172 GLU HG2 H 2.01 0.03 2 535 172 172 GLU HG3 H 2.17 0.03 2 536 172 172 GLU C C 175.52 0.2 1 537 172 172 GLU CA C 55.23 0.2 1 538 172 172 GLU CB C 31.50 0.2 1 539 172 172 GLU CG C 37.30 0.2 1 540 172 172 GLU N N 126.17 0.1 1 541 173 173 LEU H H 8.89 0.03 1 542 173 173 LEU HA H 4.83 0.03 1 543 173 173 LEU HB2 H 1.21 0.03 2 544 173 173 LEU HB3 H 1.66 0.03 2 545 173 173 LEU HD1 H 0.61 0.03 2 546 173 173 LEU HD2 H 0.90 0.03 2 547 173 173 LEU HG H 1.36 0.03 1 548 173 173 LEU C C 175.73 0.2 1 549 173 173 LEU CA C 53.40 0.2 1 550 173 173 LEU CB C 47.16 0.2 1 551 173 173 LEU CD1 C 27.99 0.2 2 552 173 173 LEU CD2 C 23.95 0.2 2 553 173 173 LEU CG C 26.90 0.2 1 554 173 173 LEU N N 125.38 0.1 1 555 174 174 ASP H H 9.03 0.03 1 556 174 174 ASP HA H 5.20 0.03 1 557 174 174 ASP HB2 H 2.63 0.03 2 558 174 174 ASP HB3 H 2.94 0.03 2 559 174 174 ASP C C 178.15 0.2 1 560 174 174 ASP CA C 54.33 0.2 1 561 174 174 ASP CB C 42.87 0.2 1 562 174 174 ASP N N 120.39 0.1 1 563 175 175 PHE H H 8.15 0.03 1 564 175 175 PHE HA H 4.14 0.03 1 565 175 175 PHE HB2 H 3.42 0.03 2 566 175 175 PHE HB3 H 3.42 0.03 2 567 175 175 PHE HD1 H 7.07 0.03 1 568 175 175 PHE HD2 H 7.07 0.03 1 569 175 175 PHE HE1 H 7.33 0.03 1 570 175 175 PHE HE2 H 7.33 0.03 1 571 175 175 PHE HZ H 6.75 0.03 1 572 175 175 PHE C C 177.71 0.2 1 573 175 175 PHE CA C 58.80 0.2 1 574 175 175 PHE CB C 37.96 0.2 1 575 175 175 PHE CD1 C 129.60 0.2 1 576 175 175 PHE CD2 C 129.60 0.2 1 577 175 175 PHE CE1 C 131.80 0.2 1 578 175 175 PHE CE2 C 131.80 0.2 1 579 175 175 PHE CZ C 128.60 0.2 1 580 175 175 PHE N N 121.89 0.1 1 581 176 176 SER H H 8.58 0.03 1 582 176 176 SER HA H 4.42 0.03 1 583 176 176 SER HB2 H 4.17 0.03 2 584 176 176 SER HB3 H 4.01 0.03 2 585 176 176 SER C C 175.79 0.2 1 586 176 176 SER CA C 60.29 0.2 1 587 176 176 SER CB C 63.21 0.2 1 588 176 176 SER N N 109.76 0.1 1 589 177 177 GLN H H 7.93 0.03 1 590 177 177 GLN HA H 4.72 0.03 1 591 177 177 GLN HB2 H 2.36 0.03 2 592 177 177 GLN HB3 H 2.36 0.03 2 593 177 177 GLN HG2 H 2.52 0.03 2 594 177 177 GLN HG3 H 2.52 0.03 2 595 177 177 GLN C C 174.53 0.2 1 596 177 177 GLN CA C 56.64 0.2 1 597 177 177 GLN CB C 31.63 0.2 1 598 177 177 GLN CG C 36.25 0.2 1 599 177 177 GLN N N 119.20 0.1 1 600 178 178 VAL H H 7.39 0.03 1 601 178 178 VAL HA H 5.32 0.03 1 602 178 178 VAL HB H 1.80 0.03 1 603 178 178 VAL HG1 H 0.66 0.03 2 604 178 178 VAL HG2 H 0.51 0.03 2 605 178 178 VAL C C 173.95 0.2 1 606 178 178 VAL CA C 58.57 0.2 1 607 178 178 VAL CB C 36.09 0.2 1 608 178 178 VAL CG1 C 23.08 0.2 2 609 178 178 VAL CG2 C 19.93 0.2 2 610 178 178 VAL N N 109.92 0.1 1 611 179 179 GLU H H 8.76 0.03 1 612 179 179 GLU HA H 4.86 0.03 1 613 179 179 GLU HB2 H 2.12 0.03 2 614 179 179 GLU HB3 H 2.03 0.03 2 615 179 179 GLU HG2 H 2.34 0.03 2 616 179 179 GLU HG3 H 2.22 0.03 2 617 179 179 GLU C C 175.39 0.2 1 618 179 179 GLU CA C 53.97 0.2 1 619 179 179 GLU CB C 33.82 0.2 1 620 179 179 GLU CG C 35.78 0.2 1 621 179 179 GLU N N 117.55 0.1 1 622 180 180 LYS H H 8.87 0.03 1 623 180 180 LYS HA H 4.37 0.03 1 624 180 180 LYS HB2 H 1.78 0.03 2 625 180 180 LYS HB3 H 1.83 0.03 2 626 180 180 LYS HD2 H 1.64 0.03 1 627 180 180 LYS HD3 H 1.64 0.03 1 628 180 180 LYS HE2 H 2.69 0.03 2 629 180 180 LYS HE3 H 2.77 0.03 2 630 180 180 LYS HG2 H 1.59 0.03 1 631 180 180 LYS HG3 H 1.59 0.03 1 632 180 180 LYS C C 175.84 0.2 1 633 180 180 LYS CA C 58.04 0.2 1 634 180 180 LYS CB C 33.09 0.2 1 635 180 180 LYS CD C 28.99 0.2 1 636 180 180 LYS CE C 42.11 0.2 1 637 180 180 LYS CG C 26.06 0.2 1 638 180 180 LYS N N 122.53 0.1 1 639 181 181 ALA H H 7.98 0.03 1 640 181 181 ALA HA H 4.19 0.03 1 641 181 181 ALA HB H 1.21 0.03 1 642 181 181 ALA CA C 53.58 0.2 1 643 181 181 ALA CB C 20.36 0.2 1 644 181 181 ALA N N 131.73 0.1 1 stop_ save_