data_6234 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts of PagP in CYFOS-7 detergent ; _BMRB_accession_number 6234 _BMRB_flat_file_name bmr6234.str _Entry_type original _Submission_date 2004-06-11 _Accession_date 2004-06-11 _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 Hwang Peter M. . 2 Bishop Russell E. . 3 Kay Lewis E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 117 "13C chemical shifts" 232 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-23 original author . stop_ _Original_release_date 2004-07-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The integral membrane enzyme PagP alternates between two dynamically distinct states. ; _Citation_status 'in press' _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 Hwang Peter M. . 2 Bishop Russell E. . 3 Kay Lewis E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PagP in CYFOS-7' _Abbreviation_common CYFOS-7 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PagP in CYFOS-7' $PagP 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_PagP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PagP _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 170 _Mol_residue_sequence ; MNADEWMTTFRENIAQTWQQ PEHYDLYIPAITWHARFAYD KEKTDRYNERPWGGGFGLSR WDEKGNWHGLYAMAFKDSWN KWEPIAGYGWESTWRPLADE NFHLGLGFTAGVTARDNWNY IPLPVLLPLASVGYGPVTFQ MTYIPGTYNNGNVYFAWMRF QFLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 ALA 4 ASP 5 GLU 6 TRP 7 MET 8 THR 9 THR 10 PHE 11 ARG 12 GLU 13 ASN 14 ILE 15 ALA 16 GLN 17 THR 18 TRP 19 GLN 20 GLN 21 PRO 22 GLU 23 HIS 24 TYR 25 ASP 26 LEU 27 TYR 28 ILE 29 PRO 30 ALA 31 ILE 32 THR 33 TRP 34 HIS 35 ALA 36 ARG 37 PHE 38 ALA 39 TYR 40 ASP 41 LYS 42 GLU 43 LYS 44 THR 45 ASP 46 ARG 47 TYR 48 ASN 49 GLU 50 ARG 51 PRO 52 TRP 53 GLY 54 GLY 55 GLY 56 PHE 57 GLY 58 LEU 59 SER 60 ARG 61 TRP 62 ASP 63 GLU 64 LYS 65 GLY 66 ASN 67 TRP 68 HIS 69 GLY 70 LEU 71 TYR 72 ALA 73 MET 74 ALA 75 PHE 76 LYS 77 ASP 78 SER 79 TRP 80 ASN 81 LYS 82 TRP 83 GLU 84 PRO 85 ILE 86 ALA 87 GLY 88 TYR 89 GLY 90 TRP 91 GLU 92 SER 93 THR 94 TRP 95 ARG 96 PRO 97 LEU 98 ALA 99 ASP 100 GLU 101 ASN 102 PHE 103 HIS 104 LEU 105 GLY 106 LEU 107 GLY 108 PHE 109 THR 110 ALA 111 GLY 112 VAL 113 THR 114 ALA 115 ARG 116 ASP 117 ASN 118 TRP 119 ASN 120 TYR 121 ILE 122 PRO 123 LEU 124 PRO 125 VAL 126 LEU 127 LEU 128 PRO 129 LEU 130 ALA 131 SER 132 VAL 133 GLY 134 TYR 135 GLY 136 PRO 137 VAL 138 THR 139 PHE 140 GLN 141 MET 142 THR 143 TYR 144 ILE 145 PRO 146 GLY 147 THR 148 TYR 149 ASN 150 ASN 151 GLY 152 ASN 153 VAL 154 TYR 155 PHE 156 ALA 157 TRP 158 MET 159 ARG 160 PHE 161 GLN 162 PHE 163 LEU 164 GLU 165 HIS 166 HIS 167 HIS 168 HIS 169 HIS 170 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 BMRB 5557 PagP 100.00 170 100.00 100.00 2.37e-122 PDB 1MM4 "Solution Nmr Structure Of The Outer Membrane Enzyme Pagp In Dpc Micelles" 100.00 170 100.00 100.00 2.37e-122 PDB 1MM5 "Solution Nmr Structure Of The Outer Membrane Enzyme Pagp In Og Micelles" 100.00 170 100.00 100.00 2.37e-122 PDB 1THQ "Crystal Structure Of Outer Membrane Enzyme Pagp" 100.00 170 100.00 100.00 2.37e-122 PDB 3GP6 "Crystal Structure Of Pagp In SdsMPD" 95.88 163 100.00 100.00 4.15e-116 DBJ BAA35265 "palmitoyl transferase for Lipid A [Escherichia coli str. K-12 substr. W3110]" 94.71 186 100.00 100.00 1.67e-115 DBJ BAB34084 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 94.71 186 99.38 99.38 5.68e-115 DBJ BAG76214 "conserved hypothetical protein [Escherichia coli SE11]" 94.71 186 99.38 99.38 1.91e-114 DBJ BAI24026 "palmitoyl transferase CrcA for Lipid A [Escherichia coli O26:H11 str. 11368]" 94.71 186 100.00 100.00 1.67e-115 DBJ BAI29493 "palmitoyl transferase CrcA for Lipid A [Escherichia coli O103:H2 str. 12009]" 94.71 186 100.00 100.00 1.67e-115 EMBL CAP75122 "Protein crcA [Escherichia coli LF82]" 94.71 186 98.76 98.76 9.84e-114 EMBL CAQ31098 "PagP monomer, subunit of palmitoyl transferase for Lipid A [Escherichia coli BL21(DE3)]" 94.71 186 100.00 100.00 1.67e-115 EMBL CAQ97476 "palmitoyl transferase for Lipid A [Escherichia coli IAI1]" 94.71 186 100.00 100.00 1.67e-115 EMBL CAR02004 "palmitoyl transferase for Lipid A [Escherichia coli S88]" 94.71 186 98.14 98.14 1.70e-112 EMBL CAR06827 "palmitoyl transferase for Lipid A [Escherichia coli ED1a]" 94.71 186 98.14 98.14 8.11e-113 GB AAA67555 "putative [Escherichia coli str. K-12 substr. W3110]" 94.71 186 100.00 100.00 1.67e-115 GB AAB40822 "hypothetical protein [Escherichia coli]" 94.71 186 100.00 100.00 1.67e-115 GB AAC73723 "phospholipid:lipid A palmitoyltransferase [Escherichia coli str. K-12 substr. MG1655]" 94.71 186 100.00 100.00 1.67e-115 GB AAG54957 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 94.71 186 99.38 99.38 5.68e-115 GB AAN42294 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 94.71 186 99.38 99.38 4.15e-114 REF NP_286349 "palmitoyl transferase [Escherichia coli O157:H7 str. EDL933]" 94.71 186 99.38 99.38 5.68e-115 REF NP_308688 "palmitoyl transferase [Escherichia coli O157:H7 str. Sakai]" 94.71 186 99.38 99.38 5.68e-115 REF NP_415155 "phospholipid:lipid A palmitoyltransferase [Escherichia coli str. K-12 substr. MG1655]" 94.71 186 100.00 100.00 1.67e-115 REF NP_706587 "phospholipid:lipid A palmitoyltransferase [Shigella flexneri 2a str. 301]" 94.71 186 99.38 99.38 4.15e-114 REF NP_752642 "palmitoyl transferase [Escherichia coli CFT073]" 94.71 186 98.76 98.76 9.84e-114 SP D2AA19 "RecName: Full=Lipid A palmitoyltransferase PagP; AltName: Full=Lipid A acylation protein; Flags: Precursor [Shigella flexneri 2" 94.71 186 99.38 99.38 4.15e-114 SP E0J1Q4 "RecName: Full=Lipid A palmitoyltransferase PagP; AltName: Full=Lipid A acylation protein; Flags: Precursor [Escherichia coli W]" 94.71 186 99.38 99.38 4.15e-114 SP E8Y6Y6 "RecName: Full=Lipid A palmitoyltransferase PagP; AltName: Full=Lipid A acylation protein; Flags: Precursor [Escherichia coli KO" 94.71 186 99.38 99.38 4.15e-114 SP P37001 "RecName: Full=Lipid A palmitoyltransferase PagP; AltName: Full=Antimicrobial peptide resistance; AltName: Full=Lipid A acylatio" 94.71 186 100.00 100.00 1.67e-115 SP Q0T6N3 "RecName: Full=Lipid A palmitoyltransferase PagP; AltName: Full=Lipid A acylation protein; Flags: Precursor [Shigella flexneri 5" 94.71 186 99.38 99.38 4.15e-114 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PagP 'E. coli' 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 $PagP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PagP 1.0 mM '[U-13C; U-15N; U-2H]' CYFOS-7 . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . pH temperature 318 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details '1H: water(shift value 4.5819 at 45 degrees)' 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_citation_label _Correction_value_citation_label water H 1 protons ppm 4.5819 internal direct . . . $entry_citation $entry_citation urea N 15 nitrogen ppm 78.98 external indirect . . . $entry_citation $entry_citation acetate C 13 'methyl carbon' ppm 25.85 external indirect . . . $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_PagPin_CYFOS-7 _Saveframe_category assigned_chemical_shifts _Details ; The protein was uniformly deuterated (except at exchangeable sites). Deuteration will change the chemical shift values. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PagP in CYFOS-7' _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 . 2 ASN CA C 52.021 0.1 1 2 . 2 ASN CB C 38.482 0.1 1 3 . 3 ALA N N 125.845 0.1 1 4 . 3 ALA H H 8.874 0.01 1 5 . 3 ALA CA C 54.956 0.1 1 6 . 3 ALA CB C 17.903 0.1 1 7 . 4 ASP N N 117.487 0.1 1 8 . 4 ASP H H 8.241 0.01 1 9 . 4 ASP CA C 56.884 0.1 1 10 . 4 ASP CB C 39.736 0.1 1 11 . 5 GLU N N 120.872 0.1 1 12 . 5 GLU H H 7.890 0.01 1 13 . 5 GLU CA C 58.305 0.1 1 14 . 5 GLU CB C 28.740 0.1 1 15 . 6 TRP N N 122.222 0.1 1 16 . 6 TRP H H 7.826 0.01 1 17 . 6 TRP CA C 60.441 0.1 1 18 . 6 TRP CB C 28.452 0.1 1 19 . 7 MET N N 118.993 0.1 1 20 . 7 MET H H 8.334 0.01 1 21 . 7 MET CA C 58.700 0.1 1 22 . 7 MET CB C 31.515 0.1 1 23 . 8 THR N N 116.875 0.1 1 24 . 8 THR H H 8.033 0.01 1 25 . 8 THR CA C 66.508 0.1 1 26 . 8 THR CB C 68.102 0.1 1 27 . 9 THR N N 119.988 0.1 1 28 . 9 THR H H 7.781 0.01 1 29 . 9 THR CA C 66.521 0.1 1 30 . 9 THR CB C 67.844 0.1 1 31 . 10 PHE N N 122.188 0.1 1 32 . 10 PHE H H 8.100 0.01 1 33 . 10 PHE CA C 60.591 0.1 1 34 . 10 PHE CB C 38.540 0.1 1 35 . 11 ARG N N 118.356 0.1 1 36 . 11 ARG H H 8.177 0.01 1 37 . 11 ARG CA C 59.762 0.1 1 38 . 11 ARG CB C 29.219 0.1 1 39 . 12 GLU N N 119.028 0.1 1 40 . 12 GLU H H 8.283 0.01 1 41 . 12 GLU CA C 58.564 0.1 1 42 . 12 GLU CB C 28.055 0.1 1 43 . 13 ASN N N 120.009 0.1 1 44 . 13 ASN H H 8.254 0.01 1 45 . 13 ASN CA C 55.171 0.1 1 46 . 13 ASN CB C 37.286 0.1 1 47 . 14 ILE N N 124.971 0.1 1 48 . 14 ILE H H 7.838 0.01 1 49 . 14 ILE CA C 65.829 0.1 1 50 . 14 ILE CB C 37.000 0.1 1 51 . 15 ALA N N 123.172 0.1 1 52 . 15 ALA H H 8.201 0.01 1 53 . 15 ALA CA C 55.439 0.1 1 54 . 15 ALA CB C 17.479 0.1 1 55 . 16 GLN N N 115.822 0.1 1 56 . 16 GLN H H 8.425 0.01 1 57 . 16 GLN CA C 58.298 0.1 1 58 . 16 GLN CB C 27.744 0.1 1 59 . 17 THR N N 116.541 0.1 1 60 . 17 THR H H 7.271 0.01 1 61 . 17 THR CA C 66.849 0.1 1 62 . 17 THR CB C 67.536 0.1 1 63 . 18 TRP N N 117.814 0.1 1 64 . 18 TRP H H 7.209 0.01 1 65 . 18 TRP CA C 58.201 0.1 1 66 . 18 TRP CB C 29.903 0.1 1 67 . 19 GLN N N 112.658 0.1 1 68 . 19 GLN H H 8.226 0.01 1 69 . 19 GLN CA C 57.587 0.1 1 70 . 19 GLN CB C 28.832 0.1 1 71 . 20 GLN N N 116.844 0.1 1 72 . 20 GLN H H 7.740 0.01 1 73 . 20 GLN CA C 52.562 0.1 1 74 . 20 GLN CB C 28.608 0.1 1 75 . 21 PRO CA C 63.286 0.1 1 76 . 21 PRO CB C 31.078 0.1 1 77 . 22 GLU N N 118.798 0.1 1 78 . 22 GLU H H 8.236 0.01 1 79 . 22 GLU CA C 55.825 0.1 1 80 . 22 GLU CB C 32.456 0.1 1 81 . 23 HIS N N 114.613 0.1 1 82 . 23 HIS H H 8.007 0.01 1 83 . 23 HIS CA C 53.584 0.1 1 84 . 23 HIS CB C 32.259 0.1 1 85 . 24 TYR N N 119.725 0.1 1 86 . 24 TYR H H 8.325 0.01 1 87 . 24 TYR CA C 55.379 0.1 1 88 . 24 TYR CB C 39.896 0.1 1 89 . 25 ASP N N 120.594 0.1 1 90 . 25 ASP H H 8.811 0.01 1 91 . 25 ASP CA C 55.437 0.1 1 92 . 25 ASP CB C 39.802 0.1 1 93 . 26 LEU N N 122.202 0.1 1 94 . 26 LEU H H 9.082 0.01 1 95 . 26 LEU CA C 53.237 0.1 1 96 . 26 LEU CB C 45.495 0.1 1 97 . 27 TYR N N 125.410 0.1 1 98 . 27 TYR H H 8.615 0.01 1 99 . 27 TYR CA C 56.984 0.1 1 100 . 27 TYR CB C 39.879 0.1 1 101 . 28 ILE N N 120.609 0.1 1 102 . 28 ILE H H 9.091 0.01 1 103 . 28 ILE CA C 56.831 0.1 1 104 . 28 ILE CB C 40.276 0.1 1 105 . 29 PRO CA C 56.959 0.1 1 106 . 37 PHE N N 120.818 0.1 1 107 . 37 PHE H H 7.982 0.01 1 108 . 37 PHE CA C 57.428 0.1 1 109 . 37 PHE CB C 38.118 0.1 1 110 . 38 ALA N N 124.581 0.1 1 111 . 38 ALA H H 7.747 0.01 1 112 . 38 ALA CA C 51.860 0.1 1 113 . 38 ALA CB C 18.916 0.1 1 114 . 39 TYR N N 119.375 0.1 1 115 . 39 TYR H H 7.680 0.01 1 116 . 39 TYR CA C 57.669 0.1 1 117 . 39 TYR CB C 37.917 0.1 1 118 . 40 ASP N N 122.214 0.1 1 119 . 40 ASP H H 8.000 0.01 1 120 . 40 ASP CA C 53.712 0.1 1 121 . 40 ASP CB C 40.563 0.1 1 122 . 41 LYS N N 122.225 0.1 1 123 . 41 LYS H H 7.901 0.01 1 124 . 41 LYS CA C 56.525 0.1 1 125 . 41 LYS CB C 31.889 0.1 1 126 . 42 GLU N N 120.238 0.1 1 127 . 42 GLU H H 8.192 0.01 1 128 . 42 GLU CA C 56.438 0.1 1 129 . 42 GLU CB C 29.186 0.1 1 130 . 43 LYS N N 121.623 0.1 1 131 . 43 LYS H H 7.926 0.01 1 132 . 43 LYS CA C 56.061 0.1 1 133 . 43 LYS CB C 31.957 0.1 1 134 . 44 THR N N 115.214 0.1 1 135 . 44 THR H H 7.895 0.01 1 136 . 44 THR CA C 61.516 0.1 1 137 . 44 THR CB C 69.327 0.1 1 138 . 45 ASP N N 123.004 0.1 1 139 . 45 ASP H H 8.107 0.01 1 140 . 45 ASP CA C 53.967 0.1 1 141 . 45 ASP CB C 40.678 0.1 1 142 . 46 ARG N N 121.036 0.1 1 143 . 46 ARG H H 7.997 0.01 1 144 . 46 ARG CA C 55.949 0.1 1 145 . 46 ARG CB C 29.948 0.1 1 146 . 47 TYR N N 120.818 0.1 1 147 . 47 TYR H H 7.982 0.01 1 148 . 47 TYR CA C 57.428 0.1 1 149 . 47 TYR CB C 38.118 0.1 1 150 . 48 ASN N N 120.625 0.1 1 151 . 48 ASN H H 8.178 0.01 1 152 . 48 ASN CA C 52.752 0.1 1 153 . 48 ASN CB C 38.989 0.1 1 154 . 49 GLU N N 121.411 0.1 1 155 . 49 GLU H H 8.171 0.01 1 156 . 49 GLU CA C 55.560 0.1 1 157 . 49 GLU CB C 30.136 0.1 1 158 . 54 GLY N N 104.066 0.1 1 159 . 54 GLY H H 8.040 0.01 1 160 . 54 GLY CA C 44.819 0.1 1 161 . 55 GLY N N 105.682 0.1 1 162 . 55 GLY H H 8.413 0.01 1 163 . 55 GLY CA C 46.368 0.1 1 164 . 56 PHE N N 119.118 0.1 1 165 . 56 PHE H H 8.808 0.01 1 166 . 56 PHE CA C 55.369 0.1 1 167 . 56 PHE CB C 44.028 0.1 1 168 . 57 GLY N N 107.807 0.1 1 169 . 57 GLY H H 8.930 0.01 1 170 . 57 GLY CA C 46.623 0.1 1 171 . 58 LEU N N 118.158 0.1 1 172 . 58 LEU H H 8.928 0.01 1 173 . 58 LEU CA C 52.967 0.1 1 174 . 58 LEU CB C 45.087 0.1 1 175 . 59 SER N N 114.628 0.1 1 176 . 59 SER H H 8.662 0.01 1 177 . 59 SER CA C 57.408 0.1 1 178 . 59 SER CB C 65.505 0.1 1 179 . 60 ARG N N 116.817 0.1 1 180 . 60 ARG H H 8.731 0.01 1 181 . 60 ARG CA C 54.667 0.1 1 182 . 60 ARG CB C 32.081 0.1 1 183 . 61 TRP N N 121.128 0.1 1 184 . 61 TRP H H 8.262 0.01 1 185 . 61 TRP CA C 54.344 0.1 1 186 . 61 TRP CB C 29.600 0.1 1 187 . 62 ASP N N 123.596 0.1 1 188 . 62 ASP H H 9.282 0.01 1 189 . 62 ASP CA C 52.226 0.1 1 190 . 62 ASP CB C 41.358 0.1 1 191 . 63 GLU N N 118.808 0.1 1 192 . 63 GLU H H 8.999 0.01 1 193 . 63 GLU CA C 58.697 0.1 1 194 . 63 GLU CB C 28.134 0.1 1 195 . 64 LYS N N 119.607 0.1 1 196 . 64 LYS H H 8.016 0.01 1 197 . 64 LYS CA C 56.173 0.1 1 198 . 64 LYS CB C 32.126 0.1 1 199 . 65 GLY N N 108.529 0.1 1 200 . 65 GLY H H 8.261 0.01 1 201 . 65 GLY CA C 44.430 0.1 1 202 . 66 ASN N N 120.955 0.1 1 203 . 66 ASN H H 8.356 0.01 1 204 . 66 ASN CA C 52.210 0.1 1 205 . 66 ASN CB C 37.923 0.1 1 206 . 67 TRP N N 123.348 0.1 1 207 . 67 TRP H H 7.587 0.01 1 208 . 67 TRP CA C 58.472 0.1 1 209 . 67 TRP CB C 30.112 0.1 1 210 . 68 HIS N N 122.995 0.1 1 211 . 68 HIS H H 7.220 0.01 1 212 . 68 HIS CA C 53.631 0.1 1 213 . 68 HIS CB C 34.647 0.1 1 214 . 69 GLY N N 107.702 0.1 1 215 . 69 GLY H H 8.218 0.01 1 216 . 69 GLY CA C 43.757 0.1 1 217 . 70 LEU N N 122.607 0.1 1 218 . 70 LEU H H 8.825 0.01 1 219 . 70 LEU CA C 52.802 0.1 1 220 . 70 LEU CB C 44.989 0.1 1 221 . 71 TYR N N 119.734 0.1 1 222 . 71 TYR H H 8.534 0.01 1 223 . 71 TYR CA C 55.638 0.1 1 224 . 71 TYR CB C 41.209 0.1 1 225 . 72 ALA N N 120.417 0.1 1 226 . 72 ALA H H 8.620 0.01 1 227 . 72 ALA CA C 50.759 0.1 1 228 . 72 ALA CB C 20.615 0.1 1 229 . 73 MET N N 118.841 0.1 1 230 . 73 MET H H 9.109 0.01 1 231 . 73 MET CA C 53.499 0.1 1 232 . 73 MET CB C 37.930 0.1 1 233 . 74 ALA N N 120.157 0.1 1 234 . 74 ALA H H 8.406 0.01 1 235 . 74 ALA CA C 51.298 0.1 1 236 . 74 ALA CB C 22.167 0.1 1 237 . 75 PHE N N 116.566 0.1 1 238 . 75 PHE H H 7.838 0.01 1 239 . 75 PHE CA C 55.063 0.1 1 240 . 75 PHE CB C 42.151 0.1 1 241 . 78 SER N N 114.245 0.1 1 242 . 78 SER H H 8.441 0.01 1 243 . 78 SER CA C 60.513 0.1 1 244 . 78 SER CB C 62.103 0.1 1 245 . 79 TRP N N 123.827 0.1 1 246 . 79 TRP H H 8.379 0.01 1 247 . 79 TRP CA C 56.686 0.1 1 248 . 79 TRP CB C 27.664 0.1 1 249 . 80 ASN N N 116.235 0.1 1 250 . 80 ASN H H 8.340 0.01 1 251 . 80 ASN CA C 54.109 0.1 1 252 . 80 ASN CB C 37.157 0.1 1 253 . 81 LYS N N 120.192 0.1 1 254 . 81 LYS H H 8.123 0.01 1 255 . 81 LYS CA C 53.720 0.1 1 256 . 81 LYS CB C 32.635 0.1 1 257 . 82 TRP N N 122.994 0.1 1 258 . 82 TRP H H 8.689 0.01 1 259 . 82 TRP CA C 57.523 0.1 1 260 . 84 PRO CA C 60.281 0.1 1 261 . 84 PRO CB C 32.785 0.1 1 262 . 85 ILE N N 122.323 0.1 1 263 . 85 ILE H H 9.205 0.01 1 264 . 85 ILE CA C 60.134 0.1 1 265 . 85 ILE CB C 41.070 0.1 1 266 . 86 ALA N N 128.164 0.1 1 267 . 86 ALA H H 8.295 0.01 1 268 . 86 ALA CA C 49.859 0.1 1 269 . 86 ALA CB C 20.826 0.1 1 270 . 87 GLY N N 107.146 0.1 1 271 . 87 GLY H H 7.734 0.01 1 272 . 87 GLY CA C 46.164 0.1 1 273 . 88 TYR N N 118.163 0.1 1 274 . 88 TYR H H 8.737 0.01 1 275 . 88 TYR CA C 54.050 0.1 1 276 . 88 TYR CB C 42.029 0.1 1 277 . 89 GLY N N 120.566 0.1 1 278 . 89 GLY H H 9.453 0.01 1 279 . 89 GLY CA C 43.455 0.1 1 280 . 90 TRP N N 122.374 0.1 1 281 . 90 TRP H H 8.115 0.01 1 282 . 90 TRP CA C 54.655 0.1 1 283 . 90 TRP CB C 31.076 0.1 1 284 . 91 GLU N N 121.362 0.1 1 285 . 91 GLU H H 7.709 0.01 1 286 . 91 GLU CA C 54.854 0.1 1 287 . 91 GLU CB C 33.762 0.1 1 288 . 92 SER N N 122.231 0.1 1 289 . 92 SER H H 7.464 0.01 1 290 . 92 SER CA C 57.243 0.1 1 291 . 92 SER CB C 62.243 0.1 1 292 . 93 THR N N 123.757 0.1 1 293 . 93 THR H H 8.001 0.01 1 294 . 93 THR CA C 61.899 0.1 1 295 . 93 THR CB C 70.070 0.1 1 296 . 94 TRP N N 128.979 0.1 1 297 . 94 TRP H H 9.986 0.01 1 298 . 94 TRP CA C 57.697 0.1 1 299 . 94 TRP CB C 32.585 0.1 1 300 . 95 ARG N N 122.608 0.1 1 301 . 95 ARG H H 8.807 0.01 1 302 . 95 ARG CA C 53.039 0.1 1 303 . 95 ARG CB C 29.545 0.1 1 304 . 96 PRO CA C 63.441 0.1 1 305 . 96 PRO CB C 32.191 0.1 1 306 . 97 LEU N N 120.178 0.1 1 307 . 97 LEU H H 8.653 0.01 1 308 . 97 LEU CA C 52.760 0.1 1 309 . 97 LEU CB C 41.729 0.1 1 310 . 98 ALA N N 122.588 0.1 1 311 . 98 ALA H H 8.512 0.01 1 312 . 98 ALA CA C 54.107 0.1 1 313 . 98 ALA CB C 17.665 0.1 1 314 . 99 ASP N N 114.423 0.1 1 315 . 99 ASP H H 7.054 0.01 1 316 . 99 ASP CA C 52.766 0.1 1 317 . 99 ASP CB C 39.770 0.1 1 318 . 100 GLU N N 128.010 0.1 1 319 . 100 GLU H H 8.596 0.01 1 320 . 100 GLU CA C 57.198 0.1 1 321 . 100 GLU CB C 28.518 0.1 1 322 . 101 ASN N N 116.670 0.1 1 323 . 101 ASN H H 8.566 0.01 1 324 . 101 ASN CA C 54.250 0.1 1 325 . 101 ASN CB C 37.268 0.1 1 326 . 102 PHE N N 121.250 0.1 1 327 . 102 PHE H H 7.298 0.01 1 328 . 102 PHE CA C 57.560 0.1 1 329 . 102 PHE CB C 38.524 0.1 1 330 . 103 HIS N N 122.643 0.1 1 331 . 103 HIS H H 7.778 0.01 1 332 . 103 HIS CA C 51.918 0.1 1 333 . 103 HIS CB C 29.907 0.1 1 334 . 104 LEU N N 122.410 0.1 1 335 . 104 LEU H H 8.688 0.01 1 336 . 104 LEU CA C 53.848 0.1 1 337 . 104 LEU CB C 45.266 0.1 1 338 . 105 GLY N N 111.469 0.1 1 339 . 105 GLY H H 8.881 0.01 1 340 . 105 GLY CA C 45.098 0.1 1 341 . 106 LEU N N 119.570 0.1 1 342 . 106 LEU H H 8.298 0.01 1 343 . 106 LEU CA C 53.721 0.1 1 344 . 106 LEU CB C 46.935 0.1 1 345 . 107 GLY N N 113.768 0.1 1 346 . 107 GLY H H 9.488 0.01 1 347 . 107 GLY CA C 46.669 0.1 1 348 . 108 PHE N N 121.805 0.1 1 349 . 108 PHE H H 9.174 0.01 1 350 . 108 PHE CA C 55.827 0.1 1 351 . 108 PHE CB C 41.909 0.1 1 352 . 109 THR N N 113.245 0.1 1 353 . 109 THR H H 9.539 0.01 1 354 . 109 THR CA C 57.471 0.1 1 355 . 109 THR CB C 70.734 0.1 1 356 . 110 ALA N N 131.341 0.1 1 357 . 110 ALA H H 8.602 0.01 1 358 . 110 ALA CA C 49.407 0.1 1 359 . 110 ALA CB C 21.447 0.1 1 360 . 111 GLY N N 109.014 0.1 1 361 . 111 GLY H H 8.974 0.01 1 362 . 111 GLY CA C 45.315 0.1 1 363 . 112 VAL N N 115.566 0.1 1 364 . 112 VAL H H 9.099 0.01 1 365 . 112 VAL CA C 58.985 0.1 1 366 . 112 VAL CB C 34.790 0.1 1 367 . 113 THR N N 117.187 0.1 1 368 . 113 THR H H 8.492 0.01 1 369 . 113 THR CA C 57.982 0.1 1 370 . 113 THR CB C 70.982 0.1 1 371 . 114 ALA N N 124.896 0.1 1 372 . 114 ALA H H 7.709 0.01 1 373 . 114 ALA CA C 51.257 0.1 1 374 . 114 ALA CB C 21.044 0.1 1 375 . 115 ARG N N 119.230 0.1 1 376 . 115 ARG H H 8.326 0.01 1 377 . 117 ASN N N 118.417 0.1 1 378 . 117 ASN H H 8.456 0.01 1 379 . 117 ASN CA C 53.158 0.1 1 380 . 117 ASN CB C 37.911 0.1 1 381 . 128 PRO CA C 61.943 0.1 1 382 . 128 PRO CB C 32.223 0.1 1 383 . 129 LEU N N 122.782 0.1 1 384 . 129 LEU H H 8.009 0.01 1 385 . 129 LEU CA C 53.563 0.1 1 386 . 129 LEU CB C 47.048 0.1 1 387 . 130 ALA N N 122.705 0.1 1 388 . 130 ALA H H 8.240 0.01 1 389 . 130 ALA CA C 51.056 0.1 1 390 . 130 ALA CB C 22.801 0.1 1 391 . 131 SER N N 113.014 0.1 1 392 . 131 SER H H 8.763 0.01 1 393 . 131 SER CA C 57.520 0.1 1 394 . 131 SER CB C 65.294 0.1 1 395 . 132 VAL N N 115.644 0.1 1 396 . 132 VAL H H 8.681 0.01 1 397 . 132 VAL CA C 59.403 0.1 1 398 . 132 VAL CB C 33.920 0.1 1 399 . 133 GLY N N 111.469 0.1 1 400 . 133 GLY H H 8.881 0.01 1 401 . 133 GLY CA C 45.501 0.1 1 402 . 134 TYR N N 119.599 0.1 1 403 . 134 TYR H H 8.388 0.01 1 404 . 134 TYR CA C 56.557 0.1 1 405 . 134 TYR CB C 41.083 0.1 1 406 . 135 GLY N N 116.038 0.1 1 407 . 135 GLY H H 8.770 0.01 1 408 . 135 GLY CA C 44.149 0.1 1 409 . 136 PRO CA C 63.645 0.1 1 410 . 136 PRO CB C 32.578 0.1 1 411 . 137 VAL N N 123.867 0.1 1 412 . 137 VAL H H 7.649 0.01 1 413 . 137 VAL CA C 61.730 0.1 1 414 . 137 VAL CB C 32.587 0.1 1 415 . 138 THR N N 122.969 0.1 1 416 . 138 THR H H 8.084 0.01 1 417 . 138 THR CA C 61.776 0.1 1 418 . 138 THR CB C 70.825 0.1 1 419 . 139 PHE N N 130.350 0.1 1 420 . 139 PHE H H 9.155 0.01 1 421 . 139 PHE CA C 56.619 0.1 1 422 . 139 PHE CB C 39.321 0.1 1 423 . 140 GLN N N 130.509 0.1 1 424 . 140 GLN H H 8.278 0.01 1 425 . 140 GLN CA C 53.084 0.1 1 426 . 140 GLN CB C 32.860 0.1 1 427 . 141 MET N N 119.971 0.1 1 428 . 141 MET H H 8.603 0.01 1 429 . 141 MET CA C 53.532 0.1 1 430 . 141 MET CB C 37.053 0.1 1 431 . 142 THR N N 112.844 0.1 1 432 . 142 THR H H 8.421 0.01 1 433 . 142 THR CA C 59.356 0.1 1 434 . 142 THR CB C 70.295 0.1 1 435 . 143 TYR N N 124.320 0.1 1 436 . 143 TYR H H 7.742 0.01 1 437 . 143 TYR CA C 55.441 0.1 1 438 . 143 TYR CB C 42.535 0.1 1 439 . 144 ILE N N 125.719 0.1 1 440 . 144 ILE H H 8.142 0.01 1 441 . 144 ILE CA C 56.992 0.1 1 442 . 144 ILE CB C 37.098 0.1 1 443 . 157 TRP N N 120.793 0.1 1 444 . 157 TRP H H 8.769 0.01 1 445 . 157 TRP CA C 55.386 0.1 1 446 . 157 TRP CB C 31.260 0.1 1 447 . 158 MET N N 116.988 0.1 1 448 . 158 MET H H 8.822 0.01 1 449 . 158 MET CA C 55.431 0.1 1 450 . 158 MET CB C 31.385 0.1 1 451 . 159 ARG N N 126.571 0.1 1 452 . 159 ARG H H 9.322 0.01 1 453 . 159 ARG CA C 53.417 0.1 1 454 . 159 ARG CB C 32.760 0.1 1 455 . 160 PHE N N 128.341 0.1 1 456 . 160 PHE H H 9.336 0.01 1 457 . 160 PHE CA C 55.582 0.1 1 458 . 160 PHE CB C 40.899 0.1 1 459 . 161 GLN N N 126.819 0.1 1 460 . 161 GLN H H 8.516 0.01 1 461 . 161 GLN CA C 55.257 0.1 1 462 . 161 GLN CB C 31.461 0.1 1 463 . 162 PHE N N 124.822 0.1 1 464 . 162 PHE H H 9.060 0.01 1 465 . 162 PHE CA C 56.805 0.1 1 466 . 162 PHE CB C 41.081 0.1 1 stop_ save_