data_5493 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of the Staphylococcus aureus acyl carrier protein synthase (AcpS) ; _BMRB_accession_number 5493 _BMRB_flat_file_name bmr5493.str _Entry_type original _Submission_date 2002-08-07 _Accession_date 2002-08-07 _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 Liu Dingjiang . . 2 Black Todd . . 3 Macinga David R . 4 Palermo Robert . . 5 Wyss Daniel F . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 "13C chemical shifts" 312 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-23 original author . stop_ _Original_release_date 2002-12-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of the Staphylococcus aureus acyl carrier protein synthase (AcpS) ; _Citation_status published _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 Liu Dingjiang . . 2 Black Todd . . 3 Macinga David R . 4 Palermo Robert . . 5 Wyss Daniel F . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3 _Page_last 273 _Year 274 _Details . loop_ _Keyword 'acyl carrier protein synthase' 'antibiotics resistance' anti-microbial 'fatty acids biosynthesis' 'NMR assignments' stop_ save_ ################################## # Molecular system description # ################################## save_system_AcpS _Saveframe_category molecular_system _Mol_system_name 'Acyl carrier protein synthase' _Abbreviation_common AcpS _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'AcpS, unit I' $AcpS 'AcpS, unit II' $AcpS 'AcpS, unit III' $AcpS stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state trimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'AcpS, unit I' 1 'AcpS, unit II' 1 'AcpS, unit III' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AcpS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ACP synthase' _Abbreviation_common AcpS _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; MIHGIGVDLIEIDRIQALYS KQPKLVERILTKNEQHKFNN FTHEQRKIEFLAGRFATKEA FSKALGTGLGKHVAFNDIDC YNDELGKPKIDYEGFIVHVS ISHTEHYAMSQVVLEKSAF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 HIS 4 GLY 5 ILE 6 GLY 7 VAL 8 ASP 9 LEU 10 ILE 11 GLU 12 ILE 13 ASP 14 ARG 15 ILE 16 GLN 17 ALA 18 LEU 19 TYR 20 SER 21 LYS 22 GLN 23 PRO 24 LYS 25 LEU 26 VAL 27 GLU 28 ARG 29 ILE 30 LEU 31 THR 32 LYS 33 ASN 34 GLU 35 GLN 36 HIS 37 LYS 38 PHE 39 ASN 40 ASN 41 PHE 42 THR 43 HIS 44 GLU 45 GLN 46 ARG 47 LYS 48 ILE 49 GLU 50 PHE 51 LEU 52 ALA 53 GLY 54 ARG 55 PHE 56 ALA 57 THR 58 LYS 59 GLU 60 ALA 61 PHE 62 SER 63 LYS 64 ALA 65 LEU 66 GLY 67 THR 68 GLY 69 LEU 70 GLY 71 LYS 72 HIS 73 VAL 74 ALA 75 PHE 76 ASN 77 ASP 78 ILE 79 ASP 80 CYS 81 TYR 82 ASN 83 ASP 84 GLU 85 LEU 86 GLY 87 LYS 88 PRO 89 LYS 90 ILE 91 ASP 92 TYR 93 GLU 94 GLY 95 PHE 96 ILE 97 VAL 98 HIS 99 VAL 100 SER 101 ILE 102 SER 103 HIS 104 THR 105 GLU 106 HIS 107 TYR 108 ALA 109 MET 110 SER 111 GLN 112 VAL 113 VAL 114 LEU 115 GLU 116 LYS 117 SER 118 ALA 119 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 4DXE "2.52 Angstrom Resolution Crystal Structure Of The Acyl-Carrier-Protein Synthase (Acps)-Acyl Carrier Protein (Acp) Protein-Prote" 100.00 143 100.00 100.00 8.00e-81 PDB 4JM7 "1.82 Angstrom Resolution Crystal Structure Of Holo-(acyl-carrier- Protein) Synthase (acps) From Staphylococcus Aureus" 100.00 143 100.00 100.00 8.00e-81 DBJ BAB43158 "holo-ACP synthase [Staphylococcus aureus subsp. aureus N315]" 100.00 119 98.32 99.16 7.40e-80 DBJ BAB58233 "holo-ACP synthase [Staphylococcus aureus subsp. aureus Mu50]" 100.00 119 98.32 99.16 7.40e-80 DBJ BAB95860 "holo-ACP synthase [Staphylococcus aureus subsp. aureus MW2]" 100.00 119 98.32 99.16 7.40e-80 DBJ BAF68248 "holo-(acyl-carrier-protein) synthase [Staphylococcus aureus subsp. aureus str. Newman]" 100.00 119 100.00 100.00 3.22e-81 DBJ BAF78939 "holo-ACP synthase [Staphylococcus aureus subsp. aureus Mu3]" 100.00 119 98.32 99.16 7.40e-80 EMBL CAA76220 "dpj protein [Staphylococcus aureus]" 100.00 119 100.00 100.00 3.22e-81 EMBL CAG41140 "holo-[acyl-carrier protein] synthase [Staphylococcus aureus subsp. aureus MRSA252]" 100.00 119 98.32 99.16 7.40e-80 EMBL CAG43783 "holo-[acyl-carrier protein] synthase [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 119 98.32 99.16 7.40e-80 EMBL CAI81645 "holo-acyl-carrier protein synthase [Staphylococcus aureus RF122]" 100.00 119 98.32 99.16 7.40e-80 EMBL CAQ50498 "holo-(acyl-carrier-protein) synthase [Staphylococcus aureus subsp. aureus ST398]" 100.00 119 98.32 99.16 7.40e-80 GB AAW37023 "holo-(acyl-carrier-protein) synthase [Staphylococcus aureus subsp. aureus COL]" 100.00 119 100.00 100.00 3.22e-81 GB ABD20944 "holo-(acyl-carrier-protein) synthase [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 100.00 119 100.00 100.00 3.22e-81 GB ABD31340 "holo-(acyl-carrier-protein) synthase [Staphylococcus aureus subsp. aureus NCTC 8325]" 100.00 119 100.00 100.00 3.22e-81 GB ABQ49890 "holo-acyl-carrier-protein synthase [Staphylococcus aureus subsp. aureus JH9]" 100.00 119 98.32 99.16 7.40e-80 GB ABR52975 "holo-acyl-carrier-protein synthase [Staphylococcus aureus subsp. aureus JH1]" 100.00 119 98.32 99.16 7.40e-80 REF NP_372595 "4'-phosphopantetheinyl transferase [Staphylococcus aureus subsp. aureus Mu50]" 100.00 119 98.32 99.16 7.40e-80 REF NP_375179 "4'-phosphopantetheinyl transferase [Staphylococcus aureus subsp. aureus N315]" 100.00 119 98.32 99.16 7.40e-80 REF NP_646812 "4'-phosphopantetheinyl transferase [Staphylococcus aureus subsp. aureus MW2]" 100.00 119 98.32 99.16 7.40e-80 REF WP_000581193 "4'-phosphopantetheinyl transferase [Staphylococcus aureus]" 100.00 119 99.16 100.00 1.49e-80 REF WP_000581194 "4'-phosphopantetheinyl transferase [Staphylococcus aureus]" 100.00 119 97.48 98.32 3.84e-79 SP A5IUL7 "RecName: Full=Holo-[acyl-carrier-protein] synthase; Short=Holo-ACP synthase; AltName: Full=4'-phosphopantetheinyl transferase A" 100.00 119 98.32 99.16 7.40e-80 SP A6QIR6 "RecName: Full=Holo-[acyl-carrier-protein] synthase; Short=Holo-ACP synthase; AltName: Full=4'-phosphopantetheinyl transferase A" 100.00 119 100.00 100.00 3.22e-81 SP A6U3F7 "RecName: Full=Holo-[acyl-carrier-protein] synthase; Short=Holo-ACP synthase; AltName: Full=4'-phosphopantetheinyl transferase A" 100.00 119 98.32 99.16 7.40e-80 SP A7X4P8 "RecName: Full=Holo-[acyl-carrier-protein] synthase; Short=Holo-ACP synthase; AltName: Full=4'-phosphopantetheinyl transferase A" 100.00 119 98.32 99.16 7.40e-80 SP A8Z4X4 "RecName: Full=Holo-[acyl-carrier-protein] synthase; Short=Holo-ACP synthase; AltName: Full=4'-phosphopantetheinyl transferase A" 100.00 119 100.00 100.00 3.22e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AcpS 'Staphylococcus aureus' 1280 Eubacteria . Staphylococcus aureus 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 $AcpS 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AcpS 1.0 mM '[U-13C; U-15N; U-2H]' KiPO4 0.075 M . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_1H-15N_NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.45 0.05 M pH 7.5 0.1 na temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCO CBCA(CO)NH HNCACB '1H-15N NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'AcpS, unit I' _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 MET CA C 53.890 0.05 1 2 . 1 MET CB C 32.050 0.05 1 3 . 1 MET C C 174.264 0.05 1 4 . 2 ILE N N 126.655 0.04 1 5 . 2 ILE H H 10.051 0.02 1 6 . 2 ILE CA C 62.106 0.05 1 7 . 2 ILE CB C 37.589 0.05 1 8 . 2 ILE C C 175.701 0.05 1 9 . 3 HIS N N 126.509 0.04 1 10 . 3 HIS H H 9.439 0.02 1 11 . 3 HIS CA C 57.706 0.05 1 12 . 3 HIS CB C 32.020 0.05 1 13 . 3 HIS C C 175.369 0.05 1 14 . 4 GLY N N 103.399 0.04 1 15 . 4 GLY H H 7.253 0.02 1 16 . 4 GLY CA C 44.322 0.05 1 17 . 4 GLY C C 170.636 0.05 1 18 . 5 ILE N N 111.709 0.04 1 19 . 5 ILE H H 8.475 0.02 1 20 . 5 ILE CA C 58.089 0.05 1 21 . 5 ILE CB C 39.737 0.05 1 22 . 5 ILE C C 173.224 0.05 1 23 . 6 GLY N N 106.580 0.04 1 24 . 6 GLY H H 8.747 0.02 1 25 . 6 GLY CA C 44.036 0.05 1 26 . 6 GLY C C 171.143 0.05 1 27 . 7 VAL N N 119.188 0.04 1 28 . 7 VAL H H 7.983 0.02 1 29 . 7 VAL CA C 57.566 0.05 1 30 . 7 VAL CB C 34.064 0.05 1 31 . 7 VAL C C 172.532 0.05 1 32 . 8 ASP N N 122.716 0.04 1 33 . 8 ASP H H 8.408 0.02 1 34 . 8 ASP CA C 54.165 0.05 1 35 . 8 ASP CB C 45.188 0.05 1 36 . 8 ASP C C 171.741 0.05 1 37 . 9 LEU N N 126.471 0.04 1 38 . 9 LEU H H 8.014 0.02 1 39 . 9 LEU CA C 52.547 0.05 1 40 . 9 LEU CB C 44.077 0.05 1 41 . 9 LEU C C 172.866 0.05 1 42 . 10 ILE N N 122.700 0.04 1 43 . 10 ILE H H 9.220 0.02 1 44 . 10 ILE CA C 60.338 0.05 1 45 . 10 ILE CB C 38.952 0.05 1 46 . 10 ILE C C 174.383 0.05 1 47 . 11 GLU N N 125.803 0.04 1 48 . 11 GLU H H 8.870 0.02 1 49 . 11 GLU CA C 54.515 0.05 1 50 . 11 GLU CB C 29.126 0.05 1 51 . 11 GLU C C 176.824 0.05 1 52 . 12 ILE N N 129.024 0.04 1 53 . 12 ILE H H 8.228 0.02 1 54 . 12 ILE CA C 64.297 0.05 1 55 . 12 ILE CB C 35.340 0.05 1 56 . 12 ILE C C 177.552 0.05 1 57 . 13 ASP N N 117.348 0.04 1 58 . 13 ASP H H 9.080 0.02 1 59 . 13 ASP CA C 56.465 0.05 1 60 . 13 ASP CB C 39.508 0.05 1 61 . 13 ASP C C 178.765 0.05 1 62 . 14 ARG N N 117.847 0.04 1 63 . 14 ARG H H 7.109 0.02 1 64 . 14 ARG CA C 57.673 0.05 1 65 . 14 ARG CB C 28.667 0.05 1 66 . 14 ARG C C 178.759 0.05 1 67 . 15 ILE N N 119.337 0.04 1 68 . 15 ILE H H 7.255 0.02 1 69 . 15 ILE CA C 60.650 0.05 1 70 . 15 ILE CB C 33.819 0.05 1 71 . 15 ILE C C 177.259 0.05 1 72 . 16 GLN N N 120.847 0.04 1 73 . 16 GLN H H 8.651 0.02 1 74 . 16 GLN CA C 59.184 0.05 1 75 . 16 GLN CB C 27.053 0.05 1 76 . 16 GLN C C 178.166 0.05 1 77 . 17 ALA N N 120.578 0.04 1 78 . 17 ALA H H 7.684 0.02 1 79 . 17 ALA CA C 54.322 0.05 1 80 . 17 ALA CB C 17.028 0.05 1 81 . 17 ALA C C 180.311 0.05 1 82 . 18 LEU N N 119.355 0.04 1 83 . 18 LEU H H 7.800 0.02 1 84 . 18 LEU CA C 57.228 0.05 1 85 . 18 LEU CB C 40.850 0.05 1 86 . 18 LEU C C 178.471 0.05 1 87 . 19 TYR N N 118.239 0.04 1 88 . 19 TYR H H 8.602 0.02 1 89 . 19 TYR CA C 59.327 0.05 1 90 . 19 TYR CB C 38.090 0.05 1 91 . 19 TYR C C 176.562 0.05 1 92 . 20 SER N N 110.966 0.04 1 93 . 20 SER H H 8.025 0.02 1 94 . 20 SER CA C 60.368 0.05 1 95 . 20 SER CB C 62.604 0.05 1 96 . 20 SER C C 175.853 0.05 1 97 . 21 LYS N N 117.554 0.04 1 98 . 21 LYS H H 7.345 0.02 1 99 . 21 LYS CA C 56.459 0.05 1 100 . 21 LYS CB C 32.694 0.05 1 101 . 21 LYS C C 176.754 0.05 1 102 . 22 GLN N N 118.031 0.04 1 103 . 22 GLN H H 8.052 0.02 1 104 . 22 GLN CA C 52.257 0.05 1 105 . 22 GLN CB C 28.675 0.05 1 106 . 23 PRO CA C 64.135 0.05 1 107 . 23 PRO CB C 30.209 0.05 1 108 . 23 PRO C C 179.291 0.05 1 109 . 24 LYS N N 115.536 0.04 1 110 . 24 LYS H H 8.384 0.02 1 111 . 24 LYS CA C 56.866 0.05 1 112 . 24 LYS CB C 30.209 0.05 1 113 . 24 LYS C C 177.847 0.05 1 114 . 25 LEU N N 121.446 0.04 1 115 . 25 LEU H H 8.297 0.02 1 116 . 25 LEU CA C 57.372 0.05 1 117 . 25 LEU CB C 40.990 0.05 1 118 . 25 LEU C C 178.812 0.05 1 119 . 26 VAL N N 112.873 0.04 1 120 . 26 VAL H H 7.475 0.02 1 121 . 26 VAL CA C 65.755 0.05 1 122 . 26 VAL CB C 30.060 0.05 1 123 . 26 VAL C C 176.782 0.05 1 124 . 27 GLU N N 116.340 0.04 1 125 . 27 GLU H H 7.605 0.02 1 126 . 27 GLU CA C 57.368 0.05 1 127 . 27 GLU CB C 28.369 0.05 1 128 . 27 GLU C C 175.466 0.05 1 129 . 28 ARG N N 115.146 0.04 1 130 . 28 ARG H H 7.459 0.02 1 131 . 28 ARG CA C 56.124 0.05 1 132 . 28 ARG CB C 29.544 0.05 1 133 . 28 ARG C C 176.672 0.05 1 134 . 29 ILE N N 113.734 0.04 1 135 . 29 ILE H H 7.290 0.02 1 136 . 29 ILE CA C 60.338 0.05 1 137 . 29 ILE CB C 38.952 0.05 1 138 . 29 ILE C C 174.179 0.05 1 139 . 30 LEU N N 116.286 0.04 1 140 . 30 LEU H H 7.801 0.02 1 141 . 30 LEU CA C 52.255 0.05 1 142 . 30 LEU CB C 41.012 0.05 1 143 . 30 LEU C C 177.940 0.05 1 144 . 31 THR N N 112.512 0.04 1 145 . 31 THR H H 9.539 0.02 1 146 . 31 THR CA C 60.219 0.05 1 147 . 31 THR CB C 69.959 0.05 1 148 . 31 THR C C 175.831 0.05 1 149 . 32 LYS N N 120.301 0.04 1 150 . 32 LYS H H 8.926 0.02 1 151 . 32 LYS CA C 59.367 0.05 1 152 . 32 LYS CB C 30.281 0.05 1 153 . 32 LYS C C 179.356 0.05 1 154 . 33 ASN N N 117.084 0.04 1 155 . 33 ASN H H 8.359 0.02 1 156 . 33 ASN CA C 55.045 0.05 1 157 . 33 ASN CB C 36.911 0.05 1 158 . 33 ASN C C 176.866 0.05 1 159 . 34 GLU N N 121.262 0.04 1 160 . 34 GLU H H 8.066 0.02 1 161 . 34 GLU CA C 58.647 0.05 1 162 . 34 GLU CB C 31.332 0.05 1 163 . 34 GLU C C 179.300 0.05 1 164 . 35 GLN N N 120.144 0.04 1 165 . 35 GLN H H 9.177 0.02 1 166 . 35 GLN CA C 58.751 0.05 1 167 . 35 GLN CB C 27.493 0.05 1 168 . 35 GLN C C 177.461 0.05 1 169 . 36 HIS N N 118.050 0.04 1 170 . 36 HIS H H 7.737 0.02 1 171 . 36 HIS CA C 58.910 0.05 1 172 . 36 HIS CB C 28.575 0.05 1 173 . 36 HIS C C 177.678 0.05 1 174 . 37 LYS N N 117.169 0.04 1 175 . 37 LYS H H 7.028 0.02 1 176 . 37 LYS CA C 58.303 0.05 1 177 . 37 LYS CB C 30.793 0.05 1 178 . 37 LYS C C 178.309 0.05 1 179 . 38 PHE N N 119.392 0.04 1 180 . 38 PHE H H 8.411 0.02 1 181 . 38 PHE CA C 60.624 0.05 1 182 . 38 PHE CB C 39.660 0.05 1 183 . 38 PHE C C 176.287 0.05 1 184 . 39 ASN N N 112.697 0.04 1 185 . 39 ASN H H 8.360 0.02 1 186 . 39 ASN CA C 53.887 0.05 1 187 . 39 ASN CB C 37.870 0.05 1 188 . 39 ASN C C 175.700 0.05 1 189 . 40 ASN N N 115.978 0.04 1 190 . 40 ASN H H 7.272 0.02 1 191 . 40 ASN CA C 52.796 0.05 1 192 . 40 ASN CB C 38.669 0.05 1 193 . 40 ASN C C 176.150 0.05 1 194 . 41 PHE N N 117.602 0.04 1 195 . 41 PHE H H 6.820 0.02 1 196 . 41 PHE CA C 58.359 0.05 1 197 . 41 PHE CB C 38.921 0.05 1 198 . 43 HIS H H 8.654 0.02 1 199 . 43 HIS N N 120.928 0.04 1 200 . 43 HIS CA C 61.400 0.05 1 201 . 43 HIS CB C 34.400 0.05 1 202 . 43 HIS C C 178.008 0.05 1 203 . 44 GLU N N 120.639 0.04 1 204 . 44 GLU H H 7.853 0.02 1 205 . 44 GLU CA C 59.178 0.05 1 206 . 44 GLU CB C 28.703 0.05 1 207 . 44 GLU C C 178.000 0.05 1 208 . 45 GLN N N 118.807 0.04 1 209 . 45 GLN H H 9.168 0.02 1 210 . 45 GLN CA C 58.053 0.05 1 211 . 45 GLN CB C 26.929 0.05 1 212 . 45 GLN C C 178.715 0.05 1 213 . 46 ARG N N 115.958 0.04 1 214 . 46 ARG H H 7.133 0.02 1 215 . 46 ARG CA C 56.757 0.05 1 216 . 46 ARG CB C 29.286 0.05 1 217 . 46 ARG C C 178.981 0.05 1 218 . 47 LYS N N 118.922 0.04 1 219 . 47 LYS H H 7.333 0.02 1 220 . 47 LYS CA C 59.249 0.05 1 221 . 47 LYS CB C 31.075 0.05 1 222 . 47 LYS C C 177.954 0.05 1 223 . 48 ILE N N 118.333 0.04 1 224 . 48 ILE H H 7.693 0.02 1 225 . 48 ILE CA C 61.449 0.05 1 226 . 48 ILE CB C 34.608 0.05 1 227 . 49 GLU C C 175.770 0.05 1 228 . 50 PHE N N 119.188 0.04 1 229 . 50 PHE H H 7.983 0.02 1 230 . 50 PHE CA C 60.455 0.05 1 231 . 50 PHE CB C 38.550 0.05 1 232 . 50 PHE C C 178.545 0.05 1 233 . 51 LEU N N 121.020 0.04 1 234 . 51 LEU H H 8.535 0.02 1 235 . 51 LEU CA C 57.546 0.05 1 236 . 51 LEU CB C 41.193 0.05 1 237 . 51 LEU C C 177.621 0.05 1 238 . 52 ALA N N 119.867 0.04 1 239 . 52 ALA H H 9.076 0.02 1 240 . 52 ALA CA C 54.669 0.05 1 241 . 52 ALA CB C 18.287 0.05 1 242 . 52 ALA C C 178.863 0.05 1 243 . 53 GLY N N 102.430 0.04 1 244 . 53 GLY H H 8.384 0.02 1 245 . 53 GLY CA C 46.278 0.05 1 246 . 53 GLY C C 177.204 0.05 1 247 . 54 ARG N N 121.072 0.04 1 248 . 54 ARG H H 7.900 0.02 1 249 . 54 ARG CA C 56.099 0.05 1 250 . 54 ARG CB C 29.334 0.05 1 251 . 54 ARG C C 179.288 0.05 1 252 . 55 PHE N N 121.684 0.04 1 253 . 55 PHE H H 8.701 0.02 1 254 . 55 PHE CA C 60.958 0.05 1 255 . 55 PHE C C 177.205 0.05 1 256 . 56 ALA N N 117.801 0.04 1 257 . 56 ALA H H 8.131 0.02 1 258 . 56 ALA CA C 53.481 0.05 1 259 . 56 ALA CB C 15.700 0.05 1 260 . 56 ALA C C 179.288 0.05 1 261 . 57 THR N N 114.158 0.04 1 262 . 57 THR H H 7.623 0.02 1 263 . 57 THR CA C 65.381 0.05 1 264 . 57 THR CB C 68.200 0.05 1 265 . 57 THR C C 175.456 0.05 1 266 . 58 LYS N N 120.906 0.04 1 267 . 58 LYS H H 7.952 0.02 1 268 . 58 LYS CA C 59.075 0.05 1 269 . 58 LYS CB C 28.200 0.05 1 270 . 58 LYS C C 178.572 0.05 1 271 . 59 GLU N N 120.380 0.04 1 272 . 59 GLU H H 7.817 0.02 1 273 . 59 GLU CA C 58.790 0.05 1 274 . 59 GLU CB C 28.200 0.05 1 275 . 59 GLU C C 179.080 0.05 1 276 . 60 ALA N N 121.627 0.04 1 277 . 60 ALA H H 8.509 0.02 1 278 . 60 ALA CA C 55.437 0.05 1 279 . 60 ALA CB C 15.700 0.05 1 280 . 60 ALA C C 179.002 0.05 1 281 . 61 PHE N N 118.040 0.04 1 282 . 61 PHE H H 8.780 0.02 1 283 . 61 PHE CA C 60.973 0.05 1 284 . 61 PHE CB C 37.625 0.05 1 285 . 61 PHE C C 175.604 0.05 1 286 . 62 SER N N 113.730 0.04 1 287 . 62 SER H H 8.006 0.02 1 288 . 62 SER CA C 61.260 0.05 1 289 . 62 SER CB C 62.870 0.05 1 290 . 62 SER C C 179.100 0.05 1 291 . 63 LYS N N 121.037 0.04 1 292 . 63 LYS H H 8.053 0.02 1 293 . 63 LYS CA C 58.760 0.05 1 294 . 63 LYS CB C 32.170 0.05 1 295 . 63 LYS C C 178.266 0.05 1 296 . 64 ALA N N 121.047 0.04 1 297 . 64 ALA H H 7.606 0.02 1 298 . 64 ALA CA C 53.936 0.05 1 299 . 64 ALA CB C 17.325 0.05 1 300 . 64 ALA C C 178.432 0.05 1 301 . 65 LEU N N 116.806 0.04 1 302 . 65 LEU H H 7.752 0.02 1 303 . 65 LEU CA C 56.192 0.05 1 304 . 65 LEU CB C 41.228 0.05 1 305 . 65 LEU C C 179.539 0.05 1 306 . 66 GLY N N 105.042 0.04 1 307 . 66 GLY H H 7.509 0.02 1 308 . 66 GLY CA C 44.381 0.05 1 309 . 66 GLY C C 174.426 0.05 1 310 . 67 THR N N 112.524 0.04 1 311 . 67 THR H H 8.284 0.02 1 312 . 67 THR CA C 61.898 0.05 1 313 . 67 THR CB C 68.820 0.05 1 314 . 67 THR C C 175.721 0.05 1 315 . 68 GLY N N 109.544 0.04 1 316 . 68 GLY H H 8.432 0.02 1 317 . 68 GLY CA C 45.226 0.05 1 318 . 68 GLY C C 174.515 0.05 1 319 . 69 LEU N N 120.430 0.04 1 320 . 69 LEU H H 8.327 0.02 1 321 . 69 LEU CA C 54.895 0.05 1 322 . 69 LEU CB C 40.802 0.05 1 323 . 69 LEU C C 178.323 0.05 1 324 . 70 GLY N N 107.956 0.04 1 325 . 70 GLY H H 8.350 0.02 1 326 . 70 GLY CA C 44.990 0.05 1 327 . 70 GLY C C 174.195 0.05 1 328 . 71 LYS N N 119.219 0.04 1 329 . 71 LYS H H 7.635 0.02 1 330 . 71 LYS CA C 55.515 0.05 1 331 . 71 LYS CB C 31.890 0.05 1 332 . 71 LYS C C 175.854 0.05 1 333 . 72 HIS N N 119.418 0.04 1 334 . 72 HIS H H 8.229 0.02 1 335 . 72 HIS CA C 55.336 0.05 1 336 . 72 HIS CB C 29.897 0.05 1 337 . 72 HIS C C 174.857 0.05 1 338 . 73 VAL N N 122.993 0.04 1 339 . 73 VAL H H 7.919 0.02 1 340 . 73 VAL CA C 61.070 0.05 1 341 . 73 VAL CB C 31.828 0.05 1 342 . 73 VAL C C 174.434 0.05 1 343 . 74 ALA N N 129.774 0.04 1 344 . 74 ALA H H 8.865 0.02 1 345 . 74 ALA CA C 50.333 0.05 1 346 . 74 ALA CB C 18.796 0.05 1 347 . 74 ALA C C 179.087 0.05 1 348 . 75 PHE N N 122.170 0.04 1 349 . 75 PHE H H 9.037 0.02 1 350 . 75 PHE CA C 58.509 0.05 1 351 . 75 PHE CB C 35.100 0.05 1 352 . 75 PHE C C 177.254 0.05 1 353 . 76 ASN N N 111.200 0.04 1 354 . 76 ASN H H 7.877 0.02 1 355 . 76 ASN CA C 53.121 0.05 1 356 . 76 ASN CB C 35.393 0.05 1 357 . 76 ASN C C 173.624 0.05 1 358 . 77 ASP N N 116.098 0.04 1 359 . 77 ASP H H 7.685 0.02 1 360 . 77 ASP CA C 53.696 0.05 1 361 . 77 ASP CB C 41.722 0.05 1 362 . 77 ASP C C 176.003 0.05 1 363 . 78 ILE N N 121.728 0.04 1 364 . 78 ILE H H 7.136 0.02 1 365 . 78 ILE CA C 59.185 0.05 1 366 . 78 ILE CB C 37.347 0.05 1 367 . 78 ILE C C 172.983 0.05 1 368 . 79 ASP N N 126.458 0.04 1 369 . 79 ASP H H 8.709 0.02 1 370 . 79 ASP CA C 53.042 0.05 1 371 . 79 ASP CB C 41.584 0.05 1 372 . 79 ASP C C 174.539 0.05 1 373 . 80 CYS N N 126.785 0.04 1 374 . 80 CYS H H 7.959 0.02 1 375 . 80 CYS CA C 56.170 0.05 1 376 . 80 CYS CB C 25.600 0.05 1 377 . 90 ILE H H 7.500 0.04 1 378 . 90 ILE N N 118.060 0.02 1 379 . 90 ILE CA C 59.450 0.05 1 380 . 90 ILE CB C 43.200 0.05 1 381 . 90 ILE C C 173.903 0.05 1 382 . 91 ASP N N 126.213 0.04 1 383 . 91 ASP H H 9.465 0.02 1 384 . 91 ASP CA C 52.640 0.05 1 385 . 91 ASP CB C 40.792 0.05 1 386 . 91 ASP C C 174.720 0.05 1 387 . 92 TYR N N 126.071 0.04 1 388 . 92 TYR H H 9.369 0.02 1 389 . 92 TYR CA C 58.422 0.05 1 390 . 92 TYR CB C 40.974 0.05 1 391 . 92 TYR C C 173.415 0.05 1 392 . 93 GLU N N 127.302 0.04 1 393 . 93 GLU H H 8.033 0.02 1 394 . 93 GLU CA C 57.879 0.05 1 395 . 93 GLU CB C 28.329 0.05 1 396 . 93 GLU C C 176.199 0.05 1 397 . 94 GLY N N 111.484 0.04 1 398 . 94 GLY H H 8.578 0.02 1 399 . 94 GLY CA C 43.855 0.05 1 400 . 94 GLY C C 173.996 0.05 1 401 . 95 PHE N N 116.871 0.04 1 402 . 95 PHE H H 8.164 0.02 1 403 . 95 PHE CA C 56.063 0.05 1 404 . 95 PHE CB C 42.613 0.05 1 405 . 95 PHE C C 175.048 0.05 1 406 . 96 ILE N N 122.748 0.04 1 407 . 96 ILE H H 9.156 0.02 1 408 . 96 ILE CA C 61.045 0.05 1 409 . 96 ILE CB C 37.454 0.05 1 410 . 96 ILE C C 174.887 0.05 1 411 . 97 VAL N N 126.945 0.04 1 412 . 97 VAL H H 8.807 0.02 1 413 . 97 VAL CA C 60.795 0.05 1 414 . 97 VAL CB C 30.760 0.05 1 415 . 97 VAL C C 175.013 0.05 1 416 . 98 HIS N N 127.609 0.04 1 417 . 98 HIS H H 8.837 0.02 1 418 . 98 HIS CA C 54.196 0.05 1 419 . 98 HIS CB C 31.887 0.05 1 420 . 98 HIS C C 174.208 0.05 1 421 . 99 VAL N N 121.684 0.04 1 422 . 99 VAL H H 8.701 0.02 1 423 . 99 VAL CA C 59.379 0.05 1 424 . 99 VAL CB C 34.156 0.05 1 425 . 99 VAL C C 175.046 0.05 1 426 . 100 SER N N 118.020 0.04 1 427 . 100 SER H H 8.590 0.02 1 428 . 100 SER CA C 57.115 0.05 1 429 . 100 SER CB C 63.580 0.05 1 430 . 100 SER C C 171.530 0.05 1 431 . 101 ILE N N 124.154 0.04 1 432 . 101 ILE H H 7.839 0.02 1 433 . 101 ILE CA C 59.214 0.05 1 434 . 101 ILE CB C 40.700 0.05 1 435 . 101 ILE C C 175.384 0.05 1 436 . 102 SER N N 118.629 0.04 1 437 . 102 SER H H 8.697 0.02 1 438 . 102 SER CA C 56.448 0.05 1 439 . 102 SER CB C 64.450 0.05 1 440 . 102 SER C C 174.193 0.05 1 441 . 103 HIS N N 121.006 0.04 1 442 . 103 HIS H H 7.493 0.02 1 443 . 103 HIS CA C 55.423 0.05 1 444 . 103 HIS CB C 31.826 0.05 1 445 . 103 HIS C C 174.771 0.05 1 446 . 104 THR N N 113.506 0.04 1 447 . 104 THR H H 9.086 0.02 1 448 . 104 THR CA C 59.606 0.05 1 449 . 104 THR CB C 69.110 0.05 1 450 . 104 THR C C 173.877 0.05 1 451 . 105 GLU N N 116.733 0.04 1 452 . 105 GLU H H 8.280 0.02 1 453 . 105 GLU CA C 59.250 0.05 1 454 . 105 GLU CB C 29.080 0.05 1 455 . 105 GLU C C 175.930 0.05 1 456 . 106 HIS N N 121.595 0.04 1 457 . 106 HIS H H 8.326 0.02 1 458 . 106 HIS CA C 55.670 0.05 1 459 . 106 HIS CB C 30.550 0.05 1 460 . 106 HIS C C 175.355 0.05 1 461 . 107 TYR N N 118.333 0.04 1 462 . 107 TYR H H 7.663 0.02 1 463 . 107 TYR CA C 57.170 0.05 1 464 . 107 TYR CB C 42.200 0.05 1 465 . 107 TYR C C 173.527 0.05 1 466 . 108 ALA N N 121.120 0.04 1 467 . 108 ALA H H 9.117 0.02 1 468 . 108 ALA CA C 49.511 0.05 1 469 . 108 ALA CB C 21.284 0.05 1 470 . 108 ALA C C 174.239 0.05 1 471 . 109 MET N N 118.229 0.04 1 472 . 109 MET H H 9.068 0.02 1 473 . 109 MET CA C 53.017 0.05 1 474 . 109 MET CB C 35.961 0.05 1 475 . 109 MET C C 173.108 0.05 1 476 . 110 SER N N 114.419 0.04 1 477 . 110 SER H H 8.248 0.02 1 478 . 110 SER CA C 55.013 0.05 1 479 . 110 SER CB C 63.914 0.05 1 480 . 110 SER C C 172.305 0.05 1 481 . 111 GLN N N 123.910 0.04 1 482 . 111 GLN H H 8.623 0.02 1 483 . 111 GLN CA C 53.039 0.05 1 484 . 111 GLN CB C 31.581 0.05 1 485 . 111 GLN C C 173.081 0.05 1 486 . 112 VAL N N 121.444 0.04 1 487 . 112 VAL H H 8.854 0.02 1 488 . 112 VAL CA C 59.157 0.05 1 489 . 112 VAL CB C 34.950 0.05 1 490 . 112 VAL C C 175.505 0.05 1 491 . 113 VAL N N 125.012 0.04 1 492 . 113 VAL H H 8.953 0.02 1 493 . 113 VAL CA C 61.017 0.05 1 494 . 113 VAL CB C 34.670 0.05 1 495 . 113 VAL C C 173.906 0.05 1 496 . 114 LEU N N 124.884 0.04 1 497 . 114 LEU H H 8.463 0.02 1 498 . 114 LEU CA C 52.411 0.05 1 499 . 114 LEU CB C 43.032 0.05 1 500 . 114 LEU C C 176.160 0.05 1 501 . 115 GLU N N 124.499 0.04 1 502 . 115 GLU H H 9.702 0.02 1 503 . 115 GLU CA C 54.341 0.05 1 504 . 115 GLU CB C 33.277 0.05 1 505 . 115 GLU C C 175.592 0.05 1 506 . 116 LYS N N 121.781 0.04 1 507 . 116 LYS H H 8.760 0.02 1 508 . 116 LYS CA C 55.956 0.05 1 509 . 116 LYS CB C 32.914 0.05 1 510 . 116 LYS C C 176.202 0.05 1 511 . 117 SER N N 117.443 0.04 1 512 . 117 SER H H 8.141 0.02 1 513 . 117 SER CA C 57.554 0.05 1 514 . 117 SER CB C 63.089 0.05 1 515 . 117 SER C C 173.860 0.05 1 516 . 118 ALA N N 125.797 0.04 1 517 . 118 ALA H H 8.137 0.02 1 518 . 118 ALA CA C 51.725 0.05 1 519 . 118 ALA CB C 18.655 0.05 1 520 . 118 ALA C C 176.011 0.05 1 521 . 119 PHE N N 122.921 0.04 1 522 . 119 PHE H H 7.573 0.02 1 523 . 119 PHE CA C 58.246 0.05 1 524 . 119 PHE CB C 39.422 0.05 1 stop_ save_