data_5664 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Full 1H and 15N Chemical Shift Assignments for Oxytetracycline Acyl Carrier Protein ; _BMRB_accession_number 5664 _BMRB_flat_file_name bmr5664.str _Entry_type original _Submission_date 2003-01-20 _Accession_date 2003-01-21 _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 Findlow Stuart C . 2 Winsor Claire . . 3 Dempsey Christopher E . 4 Crosby John . . 5 Simpson Thomas J . 6 Crump Matthew P . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 457 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-08 original author . stop_ _Original_release_date 2003-08-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Dynamics of Oxytetracycline Polyketide Synthase Acyl Carrier Protein from Streptomyces rimosus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22744256 _PubMed_ID 12859187 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Findlow Stuart C. . 2 Winsor Claire . . 3 Simpson Thomas J. . 4 Crosby John . . 5 Crump Matthew P. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8423 _Page_last 8433 _Year 2003 _Details ; The paper reports a high resolution solution structure and dynamics of the oxytetracycline acyl carrier protein. Complete proton and nitrogen chemical shift assignments were achieved using 15N labelled ACP. ; loop_ _Keyword NMR 'solution structure' oxytetracycline 'polyketide synthase' dynamics ACP stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Kim ES, Bibb MJ, Butler MJ, Hopwood DA, Sherman DH. Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus. Gene. 1994 Apr 8;141(1):141-2. ; _Citation_title 'Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8163168 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'E S' S. . 2 Bibb 'M J' J. . 3 Butler 'M J' J. . 4 Hopwood 'D A' A. . 5 Sherman 'D H' H. . stop_ _Journal_abbreviation Gene _Journal_name_full Gene _Journal_volume 141 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 141 _Page_last 142 _Year 1994 _Details ; The complete nucleotide sequences of the Streptomyces rimosus oxytetracycline (oxyTc) polyketide synthase (PKS)-encoding genes (otcY) has been determined, revealing three open reading frames. The deduced amino-acid sequences correspond to the presumed heterodimeric beta-ketoacyl synthase and acyl carrier protein found in other type-II (multicomponent) PKS systems that specify construction of acetate-derived polyketide antibiotics. ; save_ ################################## # Molecular system description # ################################## save_system_otc_ACP _Saveframe_category molecular_system _Mol_system_name 'oxytetracycline acyl carrier protein' _Abbreviation_common 'otc ACP' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'otc ACP' $otc_ACP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'acyl carrier protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_otc_ACP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Acyl Carrier Protein' _Abbreviation_common ACP _Molecular_mass 9916 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; MTLLTLSDLLTLLRECAGEE ESIDLGGDVEDVAFDALGYD SLALLNTVGRIERDYGVQLG DDAVEKATTPRALIEMTNAS LTGASPSAGGAARDK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 LEU 4 LEU 5 THR 6 LEU 7 SER 8 ASP 9 LEU 10 LEU 11 THR 12 LEU 13 LEU 14 ARG 15 GLU 16 CYS 17 ALA 18 GLY 19 GLU 20 GLU 21 GLU 22 SER 23 ILE 24 ASP 25 LEU 26 GLY 27 GLY 28 ASP 29 VAL 30 GLU 31 ASP 32 VAL 33 ALA 34 PHE 35 ASP 36 ALA 37 LEU 38 GLY 39 TYR 40 ASP 41 SER 42 LEU 43 ALA 44 LEU 45 LEU 46 ASN 47 THR 48 VAL 49 GLY 50 ARG 51 ILE 52 GLU 53 ARG 54 ASP 55 TYR 56 GLY 57 VAL 58 GLN 59 LEU 60 GLY 61 ASP 62 ASP 63 ALA 64 VAL 65 GLU 66 LYS 67 ALA 68 THR 69 THR 70 PRO 71 ARG 72 ALA 73 LEU 74 ILE 75 GLU 76 MET 77 THR 78 ASN 79 ALA 80 SER 81 LEU 82 THR 83 GLY 84 ALA 85 SER 86 PRO 87 SER 88 ALA 89 GLY 90 GLY 91 ALA 92 ALA 93 ARG 94 ASP 95 LYS 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 1NQ4 "Solution Structure Of Oxytetracycline Acyl Carrier Protein" 100.00 95 100.00 100.00 6.85e-58 EMBL CAA80986 "polyketide acyl carrier protein [Streptomyces rimosus]" 100.00 95 100.00 100.00 6.85e-58 GB AAA03334 "acyl-carrier protein [Streptomyces rimosus]" 100.00 95 100.00 100.00 6.85e-58 GB AAZ78327 "OxyC [Streptomyces rimosus]" 100.00 95 100.00 100.00 6.85e-58 GB ELQ83294 "phosphopantetheine-binding protein [Streptomyces rimosus subsp. rimosus ATCC 10970]" 100.00 95 100.00 100.00 6.85e-58 GB KEF12048 "actinorhodin polyketide synthase acyl carrier protein [Streptomyces rimosus R6-500]" 100.00 95 100.00 100.00 6.85e-58 REF WP_003981021 "MULTISPECIES: phosphopantetheine-binding protein [Streptomyces]" 100.00 95 100.00 100.00 6.85e-58 REF WP_030372734 "MULTISPECIES: actinorhodin polyketide synthase acyl carrier protein [Streptomyces]" 100.00 95 98.95 100.00 5.37e-57 SP P43677 "RecName: Full=Oxytetracycline polyketide synthase acyl carrier protein; Short=ACP [Streptomyces rimosus]" 100.00 95 100.00 100.00 6.85e-58 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $otc_ACP 'soil bacterium' 1927 Eubacteria . Streptomyces rimosus otcY1-3 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 $otc_ACP 'recombinant technology' 'E. coli' Escherichia coli . pT-7 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 $otc_ACP 1 mM '[U-97% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'NMR data processing' stop_ _Details . save_ save_Pipp _Saveframe_category software _Name Pipp _Version . loop_ _Task 'NMR data assignment' 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_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.3 0.2 na temperature 298 0.5 K 'ionic strength' 0.015 0.002 M 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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 '1H-1H NOESY' '1H-1H TOCSY' '1H-15N NOESY' '1H-15N TOCSY' '1H-15N HSQC' HNHA stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'otc ACP' _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 HA H 4.184 0.02 1 2 . 1 MET HB2 H 2.173 0.02 2 3 . 1 MET HG2 H 2.545 0.02 2 4 . 2 THR N N 121.402 0.05 1 5 . 2 THR H H 8.590 0.02 1 6 . 2 THR HA H 4.400 0.02 1 7 . 2 THR HB H 4.099 0.02 1 8 . 2 THR HG2 H 1.304 0.02 1 9 . 3 LEU N N 123.119 0.05 1 10 . 3 LEU H H 7.990 0.02 1 11 . 3 LEU HA H 4.305 0.02 1 12 . 3 LEU HB3 H 1.552 0.02 2 13 . 3 LEU HB2 H 1.493 0.02 2 14 . 3 LEU HG H 1.369 0.02 1 15 . 3 LEU HD1 H 0.776 0.02 2 16 . 3 LEU HD2 H 0.767 0.02 2 17 . 4 LEU N N 125.172 0.05 1 18 . 4 LEU H H 9.403 0.02 1 19 . 4 LEU HA H 4.430 0.02 1 20 . 4 LEU HB2 H 1.643 0.02 2 21 . 4 LEU HG H 1.451 0.02 1 22 . 4 LEU HD1 H 0.680 0.02 2 23 . 4 LEU HD2 H 0.721 0.02 2 24 . 5 THR N N 115.421 0.05 1 25 . 5 THR H H 7.607 0.02 1 26 . 5 THR HA H 4.697 0.02 1 27 . 5 THR HB H 4.530 0.02 1 28 . 5 THR HG2 H 1.214 0.02 1 29 . 6 LEU N N 122.648 0.05 1 30 . 6 LEU H H 8.964 0.02 1 31 . 6 LEU HA H 4.017 0.02 1 32 . 6 LEU HB2 H 1.880 0.02 2 33 . 6 LEU HG H 1.389 0.02 1 34 . 6 LEU HD1 H 0.792 0.02 2 35 . 6 LEU HD2 H 0.924 0.02 2 36 . 7 SER N N 112.478 0.05 1 37 . 7 SER H H 8.582 0.02 1 38 . 7 SER HA H 4.053 0.02 1 39 . 7 SER HB3 H 3.870 0.02 2 40 . 7 SER HB2 H 3.860 0.02 2 41 . 8 ASP N N 120.568 0.05 1 42 . 8 ASP H H 7.511 0.02 1 43 . 8 ASP HA H 4.491 0.02 1 44 . 8 ASP HB3 H 2.667 0.02 1 45 . 8 ASP HB2 H 2.812 0.02 1 46 . 9 LEU N N 121.456 0.05 1 47 . 9 LEU H H 8.504 0.02 1 48 . 9 LEU HA H 4.035 0.02 1 49 . 9 LEU HB3 H 2.178 0.02 1 50 . 9 LEU HB2 H 1.347 0.02 1 51 . 9 LEU HG H 1.602 0.02 1 52 . 9 LEU HD1 H 0.794 0.02 2 53 . 9 LEU HD2 H 1.038 0.02 2 54 . 10 LEU N N 118.044 0.05 1 55 . 10 LEU H H 8.756 0.02 1 56 . 10 LEU HA H 4.042 0.02 1 57 . 10 LEU HB2 H 1.968 0.02 2 58 . 10 LEU HG H 1.507 0.02 1 59 . 10 LEU HD1 H 0.854 0.02 2 60 . 10 LEU HD2 H 0.862 0.02 2 61 . 11 THR N N 117.151 0.05 1 62 . 11 THR H H 7.714 0.02 1 63 . 11 THR HA H 3.930 0.02 1 64 . 11 THR HB H 4.389 0.02 1 65 . 11 THR HG2 H 1.224 0.02 1 66 . 12 LEU N N 122.565 0.05 1 67 . 12 LEU H H 7.894 0.02 1 68 . 12 LEU HA H 4.040 0.02 1 69 . 12 LEU HB3 H 2.062 0.02 2 70 . 12 LEU HB2 H 2.020 0.02 2 71 . 12 LEU HG H 1.388 0.02 1 72 . 12 LEU HD1 H 0.848 0.02 2 73 . 12 LEU HD2 H 0.930 0.02 2 74 . 13 LEU N N 120.535 0.05 1 75 . 13 LEU H H 8.697 0.02 1 76 . 13 LEU HA H 3.812 0.02 1 77 . 13 LEU HB2 H 1.564 0.02 2 78 . 13 LEU HG H 1.372 0.02 1 79 . 13 LEU HD1 H 0.412 0.02 2 80 . 13 LEU HD2 H 0.614 0.02 2 81 . 14 ARG N N 117.212 0.05 1 82 . 14 ARG H H 7.692 0.02 1 83 . 14 ARG HA H 4.166 0.02 1 84 . 14 ARG HB3 H 1.877 0.02 2 85 . 14 ARG HB2 H 1.711 0.02 2 86 . 14 ARG HG2 H 1.990 0.02 2 87 . 14 ARG HD2 H 3.221 0.02 2 88 . 14 ARG HE H 7.420 0.02 1 89 . 15 GLU N N 118.448 0.05 1 90 . 15 GLU H H 8.060 0.02 1 91 . 15 GLU HA H 4.115 0.02 1 92 . 15 GLU HB3 H 2.260 0.02 2 93 . 15 GLU HB2 H 2.170 0.02 2 94 . 15 GLU HG3 H 2.670 0.02 2 95 . 15 GLU HG2 H 2.360 0.02 2 96 . 16 CYS N N 116.758 0.05 1 97 . 16 CYS H H 8.490 0.02 1 98 . 16 CYS HA H 4.299 0.02 1 99 . 16 CYS HB3 H 3.032 0.02 1 100 . 16 CYS HB2 H 2.760 0.02 1 101 . 17 ALA N N 121.861 0.05 1 102 . 17 ALA H H 8.202 0.02 1 103 . 17 ALA HA H 4.451 0.02 1 104 . 17 ALA HB H 1.627 0.02 1 105 . 18 GLY N N 107.512 0.05 1 106 . 18 GLY H H 7.977 0.02 1 107 . 18 GLY HA3 H 4.097 0.02 2 108 . 18 GLY HA2 H 3.930 0.02 2 109 . 19 GLU N N 119.332 0.05 1 110 . 19 GLU H H 8.260 0.02 1 111 . 19 GLU HA H 4.356 0.02 1 112 . 19 GLU HB3 H 2.123 0.02 1 113 . 19 GLU HB2 H 1.974 0.02 1 114 . 19 GLU HG2 H 2.306 0.02 2 115 . 20 GLU N N 121.441 0.05 1 116 . 20 GLU H H 8.526 0.02 1 117 . 20 GLU HA H 4.302 0.02 1 118 . 20 GLU HB3 H 2.120 0.02 2 119 . 20 GLU HB2 H 1.942 0.02 2 120 . 20 GLU HG2 H 2.299 0.02 2 121 . 21 GLU N N 120.986 0.05 1 122 . 21 GLU H H 8.308 0.02 1 123 . 21 GLU HA H 4.322 0.02 1 124 . 21 GLU HB3 H 2.073 0.02 2 125 . 21 GLU HB2 H 1.935 0.02 2 126 . 21 GLU HG2 H 2.299 0.02 2 127 . 22 SER N N 116.748 0.05 1 128 . 22 SER H H 8.347 0.02 1 129 . 22 SER HA H 4.439 0.02 1 130 . 22 SER HB2 H 3.838 0.02 2 131 . 23 ILE N N 122.237 0.05 1 132 . 23 ILE H H 7.958 0.02 1 133 . 23 ILE HA H 4.194 0.02 1 134 . 23 ILE HB H 1.840 0.02 1 135 . 23 ILE HG13 H 1.401 0.02 2 136 . 23 ILE HG12 H 1.154 0.02 2 137 . 23 ILE HD1 H 0.829 0.02 1 138 . 23 ILE HG2 H 0.877 0.02 1 139 . 24 ASP N N 124.778 0.05 1 140 . 24 ASP H H 8.410 0.02 1 141 . 24 ASP HA H 4.639 0.02 1 142 . 24 ASP HB3 H 2.756 0.02 1 143 . 24 ASP HB2 H 2.565 0.02 1 144 . 25 LEU N N 124.815 0.05 1 145 . 25 LEU H H 8.297 0.02 1 146 . 25 LEU HA H 4.352 0.02 1 147 . 25 LEU HB2 H 1.664 0.02 2 148 . 25 LEU HG H 1.720 0.02 1 149 . 25 LEU HD1 H 0.890 0.02 2 150 . 25 LEU HD2 H 0.959 0.02 2 151 . 26 GLY N N 108.268 0.05 1 152 . 26 GLY H H 8.297 0.02 1 153 . 26 GLY HA3 H 3.989 0.02 2 154 . 26 GLY HA2 H 3.897 0.02 2 155 . 27 GLY N N 107.010 0.05 1 156 . 27 GLY H H 8.041 0.02 1 157 . 27 GLY HA3 H 3.987 0.02 2 158 . 27 GLY HA2 H 3.820 0.02 2 159 . 28 ASP N N 121.033 0.05 1 160 . 28 ASP H H 8.477 0.02 1 161 . 28 ASP HA H 4.800 0.02 1 162 . 28 ASP HB3 H 2.814 0.02 2 163 . 28 ASP HB2 H 2.605 0.02 2 164 . 29 VAL N N 116.745 0.05 1 165 . 29 VAL H H 7.782 0.02 1 166 . 29 VAL HA H 4.331 0.02 1 167 . 29 VAL HB H 2.457 0.02 1 168 . 29 VAL HG1 H 0.864 0.02 2 169 . 30 GLU N N 119.221 0.05 1 170 . 30 GLU H H 8.358 0.02 1 171 . 30 GLU HA H 3.677 0.02 1 172 . 30 GLU HB3 H 2.040 0.02 1 173 . 30 GLU HB2 H 1.941 0.02 1 174 . 30 GLU HG3 H 2.370 0.02 2 175 . 30 GLU HG2 H 2.208 0.02 2 176 . 31 ASP N N 113.369 0.05 1 177 . 31 ASP H H 8.219 0.02 1 178 . 31 ASP HA H 5.030 0.02 1 179 . 31 ASP HB3 H 2.983 0.02 1 180 . 31 ASP HB2 H 2.303 0.02 1 181 . 32 VAL N N 124.370 0.05 1 182 . 32 VAL H H 7.323 0.02 1 183 . 32 VAL HA H 3.800 0.02 1 184 . 32 VAL HB H 1.899 0.02 1 185 . 32 VAL HG2 H 1.024 0.02 2 186 . 32 VAL HG1 H 0.874 0.02 2 187 . 33 ALA N N 125.327 0.05 1 188 . 33 ALA H H 8.070 0.02 1 189 . 33 ALA HA H 4.456 0.02 1 190 . 33 ALA HB H 1.525 0.02 1 191 . 34 PHE N N 118.816 0.05 1 192 . 34 PHE H H 8.008 0.02 1 193 . 34 PHE HA H 4.269 0.02 1 194 . 34 PHE HB3 H 3.394 0.02 1 195 . 34 PHE HB2 H 2.983 0.02 1 196 . 34 PHE HD1 H 7.240 0.02 1 197 . 34 PHE HE1 H 6.952 0.02 1 198 . 34 PHE HZ H 6.805 0.02 1 199 . 34 PHE HE2 H 6.952 0.02 1 200 . 34 PHE HD2 H 7.240 0.02 1 201 . 35 ASP N N 116.044 0.05 1 202 . 35 ASP H H 8.773 0.02 1 203 . 35 ASP HA H 4.430 0.02 1 204 . 35 ASP HB3 H 2.757 0.02 2 205 . 35 ASP HB2 H 2.712 0.02 2 206 . 36 ALA N N 124.800 0.05 1 207 . 36 ALA H H 7.384 0.02 1 208 . 36 ALA HA H 4.245 0.02 1 209 . 36 ALA HB H 1.526 0.02 1 210 . 37 LEU N N 117.941 0.05 1 211 . 37 LEU H H 7.734 0.02 1 212 . 37 LEU HA H 4.259 0.02 1 213 . 37 LEU HB2 H 2.239 0.02 2 214 . 37 LEU HG H 1.784 0.02 1 215 . 37 LEU HD1 H 0.890 0.02 2 216 . 37 LEU HD2 H 0.848 0.02 2 217 . 38 GLY N N 103.580 0.05 1 218 . 38 GLY H H 7.473 0.02 1 219 . 38 GLY HA3 H 4.042 0.02 2 220 . 38 GLY HA2 H 3.523 0.02 2 221 . 39 TYR N N 120.533 0.05 1 222 . 39 TYR H H 7.724 0.02 1 223 . 39 TYR HA H 4.685 0.02 1 224 . 39 TYR HB3 H 2.730 0.02 2 225 . 39 TYR HB2 H 2.640 0.02 2 226 . 39 TYR HD1 H 6.920 0.02 3 227 . 39 TYR HE1 H 6.600 0.02 3 228 . 39 TYR HE2 H 6.602 0.02 3 229 . 39 TYR HD2 H 6.918 0.02 3 230 . 40 ASP N N 123.133 0.05 1 231 . 40 ASP H H 8.228 0.02 1 232 . 40 ASP HA H 4.620 0.02 1 233 . 40 ASP HB3 H 3.212 0.02 2 234 . 40 ASP HB2 H 2.768 0.02 2 235 . 41 SER N N 112.625 0.05 1 236 . 41 SER H H 8.280 0.02 1 237 . 41 SER HA H 4.027 0.02 1 238 . 41 SER HB3 H 3.920 0.02 2 239 . 41 SER HB2 H 3.870 0.02 2 240 . 42 LEU N N 123.631 0.05 1 241 . 42 LEU H H 7.644 0.02 1 242 . 42 LEU HA H 4.163 0.02 1 243 . 42 LEU HB2 H 1.719 0.02 2 244 . 42 LEU HG H 1.571 0.02 1 245 . 42 LEU HD1 H 0.893 0.02 2 246 . 42 LEU HD2 H 0.926 0.02 2 247 . 43 ALA N N 122.978 0.05 1 248 . 43 ALA H H 8.025 0.02 1 249 . 43 ALA HA H 4.155 0.02 1 250 . 43 ALA HB H 1.573 0.02 1 251 . 44 LEU N N 121.403 0.05 1 252 . 44 LEU H H 8.193 0.02 1 253 . 44 LEU HA H 3.666 0.02 1 254 . 44 LEU HB2 H 1.543 0.02 2 255 . 44 LEU HG H 1.361 0.02 1 256 . 44 LEU HD1 H 0.108 0.02 2 257 . 44 LEU HD2 H 0.187 0.02 2 258 . 45 LEU N N 122.278 0.05 1 259 . 45 LEU H H 8.495 0.02 1 260 . 45 LEU HA H 3.845 0.02 1 261 . 45 LEU HB2 H 1.791 0.02 2 262 . 45 LEU HG H 1.613 0.02 1 263 . 45 LEU HD1 H 0.810 0.02 2 264 . 45 LEU HD2 H 0.885 0.02 2 265 . 46 ASN N N 118.473 0.05 1 266 . 46 ASN H H 8.272 0.02 1 267 . 46 ASN HA H 4.472 0.02 1 268 . 46 ASN HB3 H 2.894 0.02 2 269 . 46 ASN HB2 H 2.814 0.02 2 270 . 46 ASN ND2 N 111.994 0.05 1 271 . 46 ASN HD21 H 6.835 0.02 2 272 . 46 ASN HD22 H 7.469 0.02 2 273 . 47 THR N N 120.904 0.05 1 274 . 47 THR H H 8.102 0.02 1 275 . 47 THR HA H 4.079 0.02 1 276 . 47 THR HB H 4.107 0.02 1 277 . 47 THR HG2 H 0.858 0.02 1 278 . 48 VAL N N 122.695 0.05 1 279 . 48 VAL H H 8.869 0.02 1 280 . 48 VAL HA H 3.349 0.02 1 281 . 48 VAL HB H 2.099 0.02 1 282 . 48 VAL HG1 H 0.804 0.02 2 283 . 49 GLY N N 105.656 0.05 1 284 . 49 GLY H H 7.915 0.02 1 285 . 49 GLY HA2 H 3.940 0.02 2 286 . 50 ARG N N 122.711 0.05 1 287 . 50 ARG H H 7.759 0.02 1 288 . 50 ARG HA H 4.077 0.02 1 289 . 50 ARG HB3 H 2.080 0.02 1 290 . 50 ARG HB2 H 1.922 0.02 1 291 . 50 ARG HG2 H 1.606 0.02 2 292 . 50 ARG HD3 H 3.165 0.02 2 293 . 50 ARG HD2 H 3.089 0.02 2 294 . 50 ARG HE H 8.030 0.02 1 295 . 51 ILE N N 121.333 0.05 1 296 . 51 ILE H H 8.609 0.02 1 297 . 51 ILE HA H 3.710 0.02 1 298 . 51 ILE HB H 2.080 0.02 1 299 . 51 ILE HG12 H 1.875 0.02 2 300 . 51 ILE HD1 H 0.621 0.02 1 301 . 51 ILE HG2 H 0.771 0.02 1 302 . 52 GLU N N 118.132 0.05 1 303 . 52 GLU H H 8.542 0.02 1 304 . 52 GLU HA H 4.111 0.02 1 305 . 52 GLU HB3 H 2.152 0.02 1 306 . 52 GLU HB2 H 1.897 0.02 1 307 . 52 GLU HG2 H 2.320 0.02 2 308 . 53 ARG N N 117.640 0.05 1 309 . 53 ARG H H 7.826 0.02 1 310 . 53 ARG HA H 4.115 0.02 1 311 . 53 ARG HB3 H 1.994 0.02 2 312 . 53 ARG HB2 H 1.956 0.02 2 313 . 53 ARG HG2 H 1.594 0.02 2 314 . 53 ARG HD2 H 3.209 0.02 2 315 . 53 ARG HE H 7.326 0.02 1 316 . 54 ASP N N 119.589 0.05 1 317 . 54 ASP H H 9.102 0.02 1 318 . 54 ASP HA H 4.377 0.02 1 319 . 54 ASP HB3 H 2.763 0.02 1 320 . 54 ASP HB2 H 2.329 0.02 1 321 . 55 TYR N N 115.770 0.05 1 322 . 55 TYR H H 8.938 0.02 1 323 . 55 TYR HA H 4.396 0.02 1 324 . 55 TYR HB3 H 3.157 0.02 2 325 . 55 TYR HB2 H 3.015 0.02 2 326 . 55 TYR HD1 H 7.400 0.02 1 327 . 55 TYR HE1 H 6.593 0.02 1 328 . 55 TYR HE2 H 6.588 0.02 1 329 . 55 TYR HD2 H 7.400 0.02 1 330 . 56 GLY N N 109.534 0.05 1 331 . 56 GLY H H 7.484 0.02 1 332 . 56 GLY HA3 H 3.983 0.02 2 333 . 56 GLY HA2 H 3.910 0.02 2 334 . 57 VAL N N 111.207 0.05 1 335 . 57 VAL H H 7.411 0.02 1 336 . 57 VAL HA H 4.636 0.02 1 337 . 57 VAL HB H 2.030 0.02 1 338 . 57 VAL HG2 H 0.890 0.02 2 339 . 57 VAL HG1 H 0.818 0.02 2 340 . 58 GLN N N 120.647 0.05 1 341 . 58 GLN H H 8.250 0.02 1 342 . 58 GLN HA H 4.522 0.02 1 343 . 58 GLN HB3 H 1.907 0.02 2 344 . 58 GLN HB2 H 2.020 0.02 2 345 . 58 GLN HG2 H 2.261 0.02 2 346 . 58 GLN NE2 N 115.600 0.05 1 347 . 58 GLN HE21 H 6.770 0.02 2 348 . 58 GLN HE22 H 7.540 0.02 2 349 . 59 LEU N N 124.345 0.05 1 350 . 59 LEU H H 9.115 0.02 1 351 . 59 LEU HA H 4.390 0.02 1 352 . 59 LEU HB2 H 1.672 0.02 2 353 . 59 LEU HG H 1.504 0.02 1 354 . 59 LEU HD1 H 0.789 0.02 2 355 . 59 LEU HD2 H 0.862 0.02 2 356 . 60 GLY N N 107.407 0.05 1 357 . 60 GLY H H 8.312 0.02 1 358 . 60 GLY HA3 H 4.293 0.02 2 359 . 60 GLY HA2 H 3.849 0.02 2 360 . 61 ASP N N 120.906 0.05 1 361 . 61 ASP H H 8.685 0.02 1 362 . 61 ASP HA H 4.352 0.02 1 363 . 61 ASP HB3 H 2.694 0.02 1 364 . 61 ASP HB2 H 2.588 0.02 1 365 . 62 ASP N N 117.595 0.05 1 366 . 62 ASP H H 8.582 0.02 1 367 . 62 ASP HA H 4.695 0.02 1 368 . 62 ASP HB3 H 2.871 0.02 1 369 . 62 ASP HB2 H 2.591 0.02 1 370 . 63 ALA N N 122.240 0.05 1 371 . 63 ALA H H 7.271 0.02 1 372 . 63 ALA HA H 3.801 0.02 1 373 . 63 ALA HB H 1.333 0.02 1 374 . 64 VAL N N 112.920 0.05 1 375 . 64 VAL H H 8.087 0.02 1 376 . 64 VAL HA H 3.487 0.02 1 377 . 64 VAL HB H 2.032 0.02 1 378 . 64 VAL HG2 H 0.891 0.02 2 379 . 64 VAL HG1 H 0.876 0.02 2 380 . 65 GLU N N 118.022 0.05 1 381 . 65 GLU H H 7.544 0.02 1 382 . 65 GLU HA H 4.028 0.02 1 383 . 65 GLU HB3 H 2.100 0.02 2 384 . 65 GLU HB2 H 2.062 0.02 2 385 . 65 GLU HG2 H 2.290 0.02 2 386 . 66 LYS N N 116.217 0.05 1 387 . 66 LYS H H 7.531 0.02 1 388 . 66 LYS HA H 4.224 0.02 1 389 . 66 LYS HB3 H 1.684 0.02 2 390 . 66 LYS HB2 H 1.900 0.02 2 391 . 66 LYS HG3 H 1.514 0.02 4 392 . 66 LYS HG2 H 1.386 0.02 4 393 . 66 LYS HD2 H 1.610 0.02 4 394 . 66 LYS HE2 H 2.898 0.02 2 395 . 67 ALA N N 124.801 0.05 1 396 . 67 ALA H H 7.929 0.02 1 397 . 67 ALA HA H 4.479 0.02 1 398 . 67 ALA HB H 1.321 0.02 1 399 . 68 THR N N 111.567 0.05 1 400 . 68 THR H H 7.944 0.02 1 401 . 68 THR HA H 4.360 0.02 1 402 . 68 THR HB H 4.370 0.02 1 403 . 68 THR HG2 H 1.301 0.02 1 404 . 69 THR N N 109.843 0.05 1 405 . 69 THR H H 7.233 0.02 1 406 . 69 THR HA H 4.297 0.02 1 407 . 69 THR HB H 4.298 0.02 1 408 . 69 THR HG2 H 0.874 0.02 1 409 . 70 PRO HA H 3.968 0.02 1 410 . 70 PRO HB3 H 2.380 0.02 2 411 . 70 PRO HB2 H 2.160 0.02 2 412 . 70 PRO HG2 H 1.850 0.02 2 413 . 70 PRO HD3 H 3.610 0.02 2 414 . 70 PRO HD2 H 3.550 0.02 2 415 . 71 ARG N N 116.203 0.05 1 416 . 71 ARG H H 8.704 0.02 1 417 . 71 ARG HA H 3.752 0.02 1 418 . 71 ARG HB3 H 1.356 0.02 1 419 . 71 ARG HB2 H 1.522 0.02 1 420 . 71 ARG HG2 H 1.797 0.02 2 421 . 71 ARG HD3 H 3.275 0.02 2 422 . 71 ARG HD2 H 2.953 0.02 2 423 . 71 ARG HE H 9.150 0.02 1 424 . 72 ALA N N 119.711 0.05 1 425 . 72 ALA H H 7.829 0.02 1 426 . 72 ALA HA H 4.173 0.02 1 427 . 72 ALA HB H 1.656 0.02 1 428 . 73 LEU N N 118.868 0.05 1 429 . 73 LEU H H 7.934 0.02 1 430 . 73 LEU HA H 4.302 0.02 1 431 . 73 LEU HB2 H 2.077 0.02 2 432 . 73 LEU HG H 1.507 0.02 1 433 . 73 LEU HD1 H 0.787 0.02 2 434 . 73 LEU HD2 H 0.852 0.02 2 435 . 74 ILE N N 123.998 0.05 1 436 . 74 ILE H H 8.817 0.02 1 437 . 74 ILE HA H 3.440 0.02 1 438 . 74 ILE HB H 1.888 0.02 1 439 . 74 ILE HG13 H 0.519 0.02 2 440 . 74 ILE HG12 H 1.754 0.02 2 441 . 74 ILE HD1 H 0.685 0.02 1 442 . 74 ILE HG2 H 0.790 0.02 1 443 . 75 GLU N N 118.422 0.05 1 444 . 75 GLU H H 8.638 0.02 1 445 . 75 GLU HA H 4.005 0.02 1 446 . 75 GLU HB3 H 2.061 0.02 2 447 . 75 GLU HB2 H 2.099 0.02 2 448 . 75 GLU HG3 H 2.500 0.02 2 449 . 75 GLU HG2 H 2.267 0.02 2 450 . 76 MET N N 118.033 0.05 1 451 . 76 MET H H 8.215 0.02 1 452 . 76 MET HA H 4.151 0.02 1 453 . 76 MET HB3 H 2.290 0.02 2 454 . 76 MET HB2 H 2.200 0.02 2 455 . 76 MET HG3 H 2.666 0.02 2 456 . 76 MET HG2 H 2.638 0.02 2 457 . 77 THR N N 118.804 0.05 1 458 . 77 THR H H 7.997 0.02 1 459 . 77 THR HA H 3.641 0.02 1 460 . 77 THR HB H 3.998 0.02 1 461 . 77 THR HG2 H 0.803 0.02 1 462 . 77 THR HG1 H 3.776 0.02 1 463 . 78 ASN N N 120.076 0.05 1 464 . 78 ASN H H 8.536 0.02 1 465 . 78 ASN HA H 4.639 0.02 1 466 . 78 ASN HB2 H 2.777 0.02 2 467 . 78 ASN ND2 N 109.586 0.05 1 468 . 78 ASN HD21 H 7.321 0.02 2 469 . 78 ASN HD22 H 7.392 0.02 2 470 . 79 ALA N N 124.386 0.05 1 471 . 79 ALA H H 8.289 0.02 1 472 . 79 ALA HA H 4.171 0.02 1 473 . 79 ALA HB H 1.483 0.02 1 474 . 80 SER N N 113.733 0.05 1 475 . 80 SER H H 7.448 0.02 1 476 . 80 SER HA H 4.348 0.02 1 477 . 80 SER HB3 H 3.994 0.02 2 478 . 80 SER HB2 H 3.990 0.02 2 479 . 81 LEU N N 121.405 0.05 1 480 . 81 LEU H H 7.968 0.02 1 481 . 81 LEU HA H 4.206 0.02 1 482 . 81 LEU HB3 H 1.609 0.02 1 483 . 81 LEU HB2 H 1.945 0.02 1 484 . 81 LEU HG H 1.767 0.02 1 485 . 81 LEU HD1 H 1.028 0.02 2 486 . 81 LEU HD2 H 1.099 0.02 2 487 . 82 THR N N 108.991 0.05 1 488 . 82 THR H H 7.953 0.02 1 489 . 82 THR HA H 4.251 0.02 1 490 . 82 THR HB H 4.312 0.02 1 491 . 82 THR HG2 H 1.282 0.02 1 492 . 83 GLY N N 110.379 0.05 1 493 . 83 GLY H H 7.851 0.02 1 494 . 83 GLY HA2 H 3.999 0.02 2 495 . 84 ALA N N 123.117 0.05 1 496 . 84 ALA H H 7.951 0.02 1 497 . 84 ALA HA H 4.384 0.02 1 498 . 84 ALA HB H 1.385 0.02 1 499 . 85 SER N N 116.297 0.05 1 500 . 85 SER H H 8.215 0.02 1 501 . 85 SER HA H 4.550 0.02 1 502 . 85 SER HB2 H 3.854 0.02 2 503 . 86 PRO HA H 4.490 0.02 1 504 . 86 PRO HB3 H 2.320 0.02 2 505 . 86 PRO HB2 H 1.961 0.02 2 506 . 86 PRO HG2 H 2.050 0.02 2 507 . 86 PRO HD3 H 3.850 0.02 2 508 . 86 PRO HD2 H 3.760 0.02 2 509 . 87 SER N N 115.537 0.05 1 510 . 87 SER H H 8.325 0.02 1 511 . 87 SER HA H 4.430 0.02 1 512 . 87 SER HB3 H 3.900 0.02 2 513 . 87 SER HB2 H 3.860 0.02 2 514 . 88 ALA N N 126.126 0.05 1 515 . 88 ALA H H 8.296 0.02 1 516 . 88 ALA HA H 4.369 0.02 1 517 . 88 ALA HB H 1.405 0.02 1 518 . 89 GLY N N 107.937 0.05 1 519 . 89 GLY H H 8.340 0.02 1 520 . 89 GLY HA2 H 3.949 0.02 2 521 . 90 GLY N N 108.710 0.05 1 522 . 90 GLY H H 8.212 0.02 1 523 . 90 GLY HA2 H 3.947 0.02 2 524 . 91 ALA N N 123.894 0.05 1 525 . 91 ALA H H 8.161 0.02 1 526 . 91 ALA HA H 4.315 0.02 1 527 . 91 ALA HB H 1.365 0.02 1 528 . 92 ALA N N 123.520 0.05 1 529 . 92 ALA H H 8.262 0.02 1 530 . 92 ALA HA H 4.281 0.02 1 531 . 92 ALA HB H 1.388 0.02 1 532 . 93 ARG N N 120.136 0.05 1 533 . 93 ARG H H 8.251 0.02 1 534 . 93 ARG HA H 4.344 0.02 1 535 . 93 ARG HB3 H 1.873 0.02 2 536 . 93 ARG HB2 H 1.754 0.02 2 537 . 93 ARG HG2 H 1.626 0.02 2 538 . 93 ARG HD2 H 3.199 0.02 2 539 . 93 ARG HE H 7.230 0.02 1 540 . 94 ASP N N 121.407 0.05 1 541 . 94 ASP H H 8.357 0.02 1 542 . 94 ASP HA H 4.571 0.02 1 543 . 94 ASP HB3 H 2.706 0.02 2 544 . 94 ASP HB2 H 2.614 0.02 2 545 . 95 LYS N N 125.439 0.05 1 546 . 95 LYS H H 7.764 0.02 1 547 . 95 LYS HA H 4.133 0.02 1 548 . 95 LYS HB3 H 1.801 0.02 2 549 . 95 LYS HB2 H 1.722 0.02 2 550 . 95 LYS HG2 H 1.377 0.02 4 551 . 95 LYS HD2 H 1.682 0.02 4 552 . 95 LYS HE2 H 3.000 0.02 2 stop_ loop_ _Atom_shift_assign_ID_ambiguity 393 '392,391' '551,550' stop_ save_