data_16196 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the acetyl Actinorhodin Acyl Carrier Protein from Streptomyces coelicolor ; _BMRB_accession_number 16196 _BMRB_flat_file_name bmr16196.str _Entry_type original _Submission_date 2009-03-06 _Accession_date 2009-03-06 _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 Crump Matthew P. . 2 Evans Simon E. . 3 Eliza Ploskon . . 4 Christopher Williams . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 479 "13C chemical shifts" 355 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-10-05 update BMRB 'update the assembly, add ligand, etc.' 2010-05-27 update BMRB 'edit entity/assembly name' 2009-05-27 update BMRB 'complete entry citation' 2009-04-17 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16197 'NMR Solution Structures of malonyl ACP from the actinorhodin polyketide synthase in Streptomyces coelicolor' 16199 'NMR Solution Structures of butyryl-ACP (a non-polar, non pathway intermediate) from Streptomyces coelicolor' 16200 'NMR Solution Structures of hexanoyl ACP (a non natural intermediate) from Streptomyces coelicolor' 16201 'NMR Solution Structures of octanoyl ACP (a non-natural intermediate) from Streptomyces coelicolor' 16202 'NMR Solution Structures of 3-oxo-butyl-ACP, an intermediate mimic from Streptomyces coelicolor' 16203 'NMR Solution Structures of 3,5-dioxohexyl ACP (a triketide mimic) from Streptomyces coelicolor' stop_ save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2)' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19361520 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evans Simon E. . 2 Williams Christopher . . 3 Arthur Christopher J. . 4 Ploskon Eliza . . 5 Wattana-Amorn Pakorn . . 6 Cox Russell J. . 7 Crosby John . . 8 Willis Christine L. . 9 Simpson Thomas J. . 10 Crump Matthew P. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 389 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 511 _Page_last 528 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'acetyl Actinorhodin Acyl Carrier' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'acetyl Actinorhodin Acyl Carrier' $Acyl_Carrier_Protein SXA $entity_SXA 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_Acyl_Carrier_Protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'acetyl Actinorhodin Acyl Carrier' _Molecular_mass 9133.160 _Mol_thiol_state 'not present' _Details 'The 42nd residue, SXA is Acetylated_4'-phosphopantetheine' ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; MATLLTTDDLRRALVESAGE TDGTDLSGDFLDLRFEDIGY DSLALMETAARLESRYGVSI PDDVAGRVDTPRELLDLING ALAEAA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 LEU 5 LEU 6 THR 7 THR 8 ASP 9 ASP 10 LEU 11 ARG 12 ARG 13 ALA 14 LEU 15 VAL 16 GLU 17 SER 18 ALA 19 GLY 20 GLU 21 THR 22 ASP 23 GLY 24 THR 25 ASP 26 LEU 27 SER 28 GLY 29 ASP 30 PHE 31 LEU 32 ASP 33 LEU 34 ARG 35 PHE 36 GLU 37 ASP 38 ILE 39 GLY 40 TYR 41 ASP 42 SER 43 LEU 44 ALA 45 LEU 46 MET 47 GLU 48 THR 49 ALA 50 ALA 51 ARG 52 LEU 53 GLU 54 SER 55 ARG 56 TYR 57 GLY 58 VAL 59 SER 60 ILE 61 PRO 62 ASP 63 ASP 64 VAL 65 ALA 66 GLY 67 ARG 68 VAL 69 ASP 70 THR 71 PRO 72 ARG 73 GLU 74 LEU 75 LEU 76 ASP 77 LEU 78 ILE 79 ASN 80 GLY 81 ALA 82 LEU 83 ALA 84 GLU 85 ALA 86 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 15658 act_holo-acp 100.00 86 100.00 100.00 1.16e-49 BMRB 15659 act_ACP 100.00 86 100.00 100.00 1.16e-49 BMRB 16197 "malonyl ACP" 100.00 86 100.00 100.00 1.16e-49 BMRB 16199 butyryl-ACP 100.00 86 100.00 100.00 1.16e-49 BMRB 16200 "hexanoyl ACP" 100.00 86 100.00 100.00 1.16e-49 BMRB 16201 "octanoyl ACP" 100.00 86 100.00 100.00 1.16e-49 BMRB 16202 3-oxo-butyl-ACP 100.00 86 100.00 100.00 1.16e-49 BMRB 16203 "3,5-dioxohexyl ACP" 100.00 86 100.00 100.00 1.16e-49 BMRB 25284 entity 100.00 86 100.00 100.00 1.16e-49 BMRB 25287 entity 100.00 86 100.00 100.00 1.16e-49 PDB 1AF8 "Actinorhodin Polyketide Synthase Acyl Carrier Protein From Streptomyces Coelicolor A3(2), Nmr, 24 Structures" 100.00 86 98.84 98.84 4.73e-49 PDB 2AF8 "Actinorhodin Polyketide Synthase Acyl Carrier Protein From Streptomyces Coelicolor A3(2), Nmr, Minimized Average Structure" 100.00 86 98.84 98.84 4.73e-49 PDB 2K0X "The Actinorhodin Holo Acyl Carrier Protein From S. Coelicolor" 100.00 86 100.00 100.00 1.16e-49 PDB 2K0Y "The Actinorhodin Apo Acyl Carrier Protein From S. Coelicolor" 100.00 86 100.00 100.00 1.16e-49 PDB 2KG6 "Solution Structure Of The Acetyl Actinorhodin Acyl Carrier Protein From Streptomyces Coelicolor" 100.00 86 100.00 100.00 1.16e-49 PDB 2KG8 "Nmr Solution Structures Of Malonyl Acp From The Actinorhodin Polyketide Synthase In Streptomyces Coelicolor" 100.00 86 100.00 100.00 1.16e-49 PDB 2KG9 "Nmr Solution Structures Of Butyryl-Acp (A Non-Polar, Non Pathway Intermediate) From The Actinorhodin Polyketide Synthase In Str" 100.00 86 100.00 100.00 1.16e-49 PDB 2KGA "Nmr Solution Structures Of Hexanoyl Acp (A Non Natural Intermediate) From The Actinorhodin Polyketide Synthase In Streptomyces " 100.00 86 100.00 100.00 1.16e-49 PDB 2KGC "Nmr Solution Structures Of Octanoyl Acp (A Non-Natural Intermediate) From The Actinorhodin Polyketide Synthase In Streptomyces " 100.00 86 100.00 100.00 1.16e-49 PDB 2KGD "Nmr Solution Structures Of 3-Oxo-Butyl-Acp, An Intermediate Mimic From The Actinorhodin Polyketide Synthase In Streptomyces Coe" 100.00 86 100.00 100.00 1.16e-49 PDB 2KGE "Nmr Solution Structures Of 3,5-Dioxohexyl Acp (A Triketide Mimic) From The Actinorhodin Polyketide Synthase In Streptomyces Coe" 100.00 86 100.00 100.00 1.16e-49 PDB 2MVU "Solution Structure Of The 3,7-dioxo-octyl Actinorhodin Acyl Carrier Protein From Streptomyces Coelicolor" 100.00 86 100.00 100.00 1.16e-49 PDB 2MVV "Solution Structure Of The 5-phenyl-3-oxo-pentyl Actinorhodin Acyl Carrier Protein From Streptomyces Coelicolor" 100.00 86 100.00 100.00 1.16e-49 EMBL CAA45045 "Acyl carrier protein [Streptomyces coelicolor A3(2)]" 100.00 86 98.84 98.84 4.73e-49 EMBL CAC44202 "actinorhodin polyketide synthase acyl carrier protein [Streptomyces coelicolor A3(2)]" 100.00 86 98.84 98.84 4.73e-49 GB AIJ13577 "actinorhodin polyketide synthase ACP [Streptomyces lividans TK24]" 100.00 86 98.84 98.84 4.73e-49 GB EFD66960 "acyl carrier protein [Streptomyces lividans TK24]" 100.00 86 98.84 98.84 4.73e-49 GB EOY50075 "Acyl carrier protein [Streptomyces lividans 1326]" 100.00 86 98.84 98.84 4.73e-49 GB KKD13304 "actinorhodin polyketide synthase acyl carrier protein [Streptomyces sp. WM6391]" 100.00 86 98.84 98.84 4.73e-49 REF NP_629239 "actinorhodin polyketide synthase ACP [Streptomyces coelicolor A3(2)]" 100.00 86 98.84 98.84 4.73e-49 REF WP_003973889 "MULTISPECIES: actinorhodin polyketide synthase [Streptomyces]" 100.00 86 98.84 98.84 4.73e-49 SP Q02054 "RecName: Full=Actinorhodin polyketide synthase acyl carrier protein; Short=ACP; AltName: Full=actI ORF3" 100.00 86 98.84 98.84 4.73e-49 stop_ save_ ############# # Ligands # ############# save_SXA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'THIOACETIC ACID S-{2-[3-(2-HYDROXY-3,3-DIMETHYL-4-PHOSPHONOOXY-BUTYRYLAMINO)-PROPIONYLAMINO]-ETHYL} ESTER' _BMRB_code SXA _PDB_code SXA _Molecular_mass 400.385 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons P24 P24 P . 0 . ? O26 O26 O . 0 . ? O23 O23 O . 0 . ? O27 O27 O . 0 . ? C28 C28 C . 0 . ? C29 C29 C . 0 . ? C30 C30 C . 0 . ? C31 C31 C . 0 . ? C32 C32 C . 0 . ? O33 O33 O . 0 . ? C34 C34 C . 0 . ? O35 O35 O . 0 . ? N36 N36 N . 0 . ? C37 C37 C . 0 . ? C38 C38 C . 0 . ? C39 C39 C . 0 . ? O40 O40 O . 0 . ? N41 N41 N . 0 . ? C42 C42 C . 0 . ? C43 C43 C . 0 . ? S1 S1 S . 0 . ? C1 C1 C . 0 . ? O1 O1 O . 0 . ? C2 C2 C . 0 . ? H28 H28 H . 0 . ? H28A H28A H . 0 . ? H30 H30 H . 0 . ? H30A H30A H . 0 . ? H30B H30B H . 0 . ? H31 H31 H . 0 . ? H31A H31A H . 0 . ? H31B H31B H . 0 . ? H32 H32 H . 0 . ? HO33 HO33 H . 0 . ? HN36 HN36 H . 0 . ? H37 H37 H . 0 . ? H37A H37A H . 0 . ? H38 H38 H . 0 . ? H38A H38A H . 0 . ? HN41 HN41 H . 0 . ? H42 H42 H . 0 . ? H42A H42A H . 0 . ? H43 H43 H . 0 . ? H43A H43A H . 0 . ? H2 H2 H . 0 . ? H2A H2A H . 0 . ? H2B H2B H . 0 . ? O8 O8 O . 0 . ? H24 H24 H . 0 . ? H25 H25 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING P24 O26 ? ? DOUB P24 O23 ? ? SING P24 O27 ? ? SING O27 C28 ? ? SING C28 C29 ? ? SING C28 H28 ? ? SING C28 H28A ? ? SING C29 C30 ? ? SING C29 C31 ? ? SING C29 C32 ? ? SING C30 H30 ? ? SING C30 H30A ? ? SING C30 H30B ? ? SING C31 H31 ? ? SING C31 H31A ? ? SING C31 H31B ? ? SING C32 O33 ? ? SING C32 C34 ? ? SING C32 H32 ? ? SING O33 HO33 ? ? DOUB C34 O35 ? ? SING C34 N36 ? ? SING N36 C37 ? ? SING N36 HN36 ? ? SING C37 C38 ? ? SING C37 H37 ? ? SING C37 H37A ? ? SING C38 C39 ? ? SING C38 H38 ? ? SING C38 H38A ? ? DOUB C39 O40 ? ? SING C39 N41 ? ? SING N41 C42 ? ? SING N41 HN41 ? ? SING C42 C43 ? ? SING C42 H42 ? ? SING C42 H42A ? ? SING C43 S1 ? ? SING C43 H43 ? ? SING C43 H43A ? ? SING S1 C1 ? ? DOUB C1 O1 ? ? SING C1 C2 ? ? SING C2 H2 ? ? SING C2 H2A ? ? SING C2 H2B ? ? SING P24 O8 ? ? SING O26 H24 ? ? SING O8 H25 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Acyl_Carrier_Protein 'high GC Gram+' 100226 Bacteria . Streptomyces coelicolor A3(2) stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name _Details $Acyl_Carrier_Protein 'recombinant technology' . Escherichia coli BL21 DE3 'pET 11c' 'Actinorhodin Acyl Carrier Protein (ACT ACP) from S. coelicolor was heterologously overexpressed in its apo form in E. coli BL21 (DE3) cells. These cells contained the plasmid PET11C bearing C17S ACT ACP. This IPTG inducible vector is both easier to use and more reliable than the heat inducible PT7-7 version originally constructed.' 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 $Acyl_Carrier_Protein 1-2 mM '[U-98% 13C; U-98% 15N]' Phosphate 20 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'peak picking' refinement 'structure solution' stop_ _Details . save_ save_ANALYSIS _Saveframe_category software _Name ANALYSIS _Version 1.0 loop_ _Vendor _Address _Electronic_address 'Tim Stevens, Wayne Boucher (CCPN)' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details 'A peak picking and chemical shift assignment program' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details 'Data processing software' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _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 5.5 0.2 pH pressure 1 . atm temperature 298 0.5 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 water C 13 protons ppm 4.78 internal indirect . . . 0.251449530 water H 1 protons ppm 4.78 internal direct . . . 1 water N 15 protons ppm 4.78 internal 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D H(CCO)NH' '3D C(CO)NH' '3D HCCH-TOCSY' '3D HNCO' 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 'acetyl Actinorhodin Acyl Carrier' _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 2 ALA HA H 4.281 . 1 2 2 2 ALA HB H 1.647 . 1 3 2 2 ALA C C 173.684 . 1 4 2 2 ALA CA C 51.969 . 1 5 2 2 ALA CB C 19.952 . 1 6 3 3 THR H H 8.663 . 1 7 3 3 THR HA H 4.389 . 1 8 3 3 THR HB H 4.184 . 1 9 3 3 THR HG2 H 1.380 . 1 10 3 3 THR C C 172.902 . 1 11 3 3 THR CA C 62.655 . 1 12 3 3 THR CB C 69.887 . 1 13 3 3 THR CG2 C 22.036 . 1 14 3 3 THR N N 117.561 . 1 15 4 4 LEU H H 8.144 . 1 16 4 4 LEU HA H 4.359 . 1 17 4 4 LEU HB2 H 1.605 . 2 18 4 4 LEU HB3 H 1.481 . 2 19 4 4 LEU HD1 H 0.883 . 2 20 4 4 LEU HD2 H 0.956 . 2 21 4 4 LEU HG H 1.711 . 1 22 4 4 LEU C C 177.242 . 1 23 4 4 LEU CA C 54.715 . 1 24 4 4 LEU CB C 42.697 . 1 25 4 4 LEU CD1 C 23.587 . 2 26 4 4 LEU CD2 C 25.161 . 2 27 4 4 LEU CG C 27.372 . 1 28 4 4 LEU N N 124.427 . 1 29 5 5 LEU H H 9.425 . 1 30 5 5 LEU HA H 4.526 . 1 31 5 5 LEU HB2 H 1.585 . 2 32 5 5 LEU HB3 H 1.359 . 2 33 5 5 LEU HD1 H 0.603 . 2 34 5 5 LEU HD2 H 0.644 . 2 35 5 5 LEU HG H 1.560 . 1 36 5 5 LEU C C 177.916 . 1 37 5 5 LEU CA C 55.479 . 1 38 5 5 LEU CB C 42.745 . 1 39 5 5 LEU CD1 C 25.385 . 2 40 5 5 LEU CD2 C 25.385 . 2 41 5 5 LEU CG C 27.656 . 1 42 5 5 LEU N N 124.464 . 1 43 6 6 THR H H 9.024 . 1 44 6 6 THR HA H 4.771 . 1 45 6 6 THR HB H 4.849 . 1 46 6 6 THR HG2 H 1.415 . 1 47 6 6 THR C C 175.947 . 1 48 6 6 THR CA C 60.023 . 1 49 6 6 THR CB C 72.569 . 1 50 6 6 THR CG2 C 21.577 . 1 51 6 6 THR N N 114.658 . 1 52 7 7 THR H H 8.832 . 1 53 7 7 THR HA H 3.868 . 1 54 7 7 THR HB H 4.317 . 1 55 7 7 THR HG2 H 1.385 . 1 56 7 7 THR C C 176.547 . 1 57 7 7 THR CA C 67.267 . 1 58 7 7 THR CB C 68.695 . 1 59 7 7 THR CG2 C 23.464 . 1 60 7 7 THR N N 115.485 . 1 61 8 8 ASP H H 8.248 . 1 62 8 8 ASP HA H 4.622 . 1 63 8 8 ASP HB2 H 2.711 . 2 64 8 8 ASP HB3 H 2.711 . 2 65 8 8 ASP C C 178.529 . 1 66 8 8 ASP CA C 57.814 . 1 67 8 8 ASP CB C 41.253 . 1 68 8 8 ASP N N 119.940 . 1 69 9 9 ASP H H 7.883 . 1 70 9 9 ASP HA H 4.554 . 1 71 9 9 ASP HB2 H 3.035 . 2 72 9 9 ASP HB3 H 2.695 . 2 73 9 9 ASP C C 179.391 . 1 74 9 9 ASP CA C 57.767 . 1 75 9 9 ASP CB C 41.496 . 1 76 9 9 ASP N N 120.270 . 1 77 10 10 LEU H H 8.065 . 1 78 10 10 LEU HA H 4.212 . 1 79 10 10 LEU HB2 H 2.334 . 2 80 10 10 LEU HB3 H 1.571 . 2 81 10 10 LEU HD1 H 1.045 . 2 82 10 10 LEU HD2 H 1.127 . 2 83 10 10 LEU HG H 1.891 . 1 84 10 10 LEU C C 177.461 . 1 85 10 10 LEU CA C 57.987 . 1 86 10 10 LEU CB C 42.087 . 1 87 10 10 LEU CD1 C 23.609 . 2 88 10 10 LEU CD2 C 27.995 . 2 89 10 10 LEU CG C 27.500 . 1 90 10 10 LEU N N 121.287 . 1 91 11 11 ARG H H 8.830 . 1 92 11 11 ARG HA H 3.523 . 1 93 11 11 ARG HB2 H 2.051 . 2 94 11 11 ARG HB3 H 2.051 . 2 95 11 11 ARG HD2 H 3.216 . 2 96 11 11 ARG HD3 H 3.190 . 2 97 11 11 ARG HE H 7.317 . 1 98 11 11 ARG HG2 H 1.402 . 2 99 11 11 ARG HG3 H 1.167 . 2 100 11 11 ARG C C 177.719 . 1 101 11 11 ARG CA C 60.717 . 1 102 11 11 ARG CB C 30.610 . 1 103 11 11 ARG CD C 43.580 . 1 104 11 11 ARG CG C 27.478 . 1 105 11 11 ARG N N 119.777 . 1 106 11 11 ARG NE N 83.641 . 1 107 12 12 ARG H H 7.969 . 1 108 12 12 ARG HA H 4.031 . 1 109 12 12 ARG HB2 H 2.028 . 2 110 12 12 ARG HB3 H 2.028 . 2 111 12 12 ARG HD2 H 3.365 . 2 112 12 12 ARG HD3 H 3.308 . 2 113 12 12 ARG HE H 7.510 . 1 114 12 12 ARG HG2 H 1.926 . 2 115 12 12 ARG HG3 H 1.697 . 2 116 12 12 ARG C C 178.394 . 1 117 12 12 ARG CA C 59.779 . 1 118 12 12 ARG CB C 30.375 . 1 119 12 12 ARG CD C 43.616 . 1 120 12 12 ARG CG C 28.255 . 1 121 12 12 ARG N N 115.512 . 1 122 12 12 ARG NE N 85.010 . 1 123 13 13 ALA H H 7.701 . 1 124 13 13 ALA HA H 4.400 . 1 125 13 13 ALA HB H 1.670 . 1 126 13 13 ALA C C 180.036 . 1 127 13 13 ALA CA C 55.022 . 1 128 13 13 ALA CB C 18.617 . 1 129 13 13 ALA N N 119.876 . 1 130 14 14 LEU H H 8.392 . 1 131 14 14 LEU HA H 4.398 . 1 132 14 14 LEU HB2 H 1.986 . 2 133 14 14 LEU HB3 H 1.444 . 2 134 14 14 LEU HD1 H 0.759 . 2 135 14 14 LEU HD2 H 0.895 . 2 136 14 14 LEU HG H 1.881 . 1 137 14 14 LEU C C 180.406 . 1 138 14 14 LEU CA C 57.533 . 1 139 14 14 LEU CB C 41.918 . 1 140 14 14 LEU CD1 C 23.304 . 2 141 14 14 LEU CD2 C 26.669 . 2 142 14 14 LEU CG C 27.122 . 1 143 14 14 LEU N N 119.070 . 1 144 15 15 VAL H H 8.451 . 1 145 15 15 VAL HA H 3.939 . 1 146 15 15 VAL HB H 2.273 . 1 147 15 15 VAL HG1 H 1.037 . 2 148 15 15 VAL HG2 H 1.115 . 2 149 15 15 VAL C C 178.877 . 1 150 15 15 VAL CA C 65.940 . 1 151 15 15 VAL CB C 32.077 . 1 152 15 15 VAL CG1 C 21.430 . 2 153 15 15 VAL CG2 C 22.657 . 2 154 15 15 VAL N N 120.240 . 1 155 16 16 GLU H H 8.212 . 1 156 16 16 GLU HA H 4.208 . 1 157 16 16 GLU HB2 H 2.262 . 2 158 16 16 GLU HB3 H 2.141 . 2 159 16 16 GLU HG2 H 2.623 . 2 160 16 16 GLU HG3 H 2.391 . 2 161 16 16 GLU C C 178.451 . 1 162 16 16 GLU CA C 59.089 . 1 163 16 16 GLU CB C 29.928 . 1 164 16 16 GLU CG C 36.776 . 1 165 16 16 GLU N N 119.815 . 1 166 17 17 SER H H 7.809 . 1 167 17 17 SER HA H 4.566 . 1 168 17 17 SER HB2 H 4.141 . 2 169 17 17 SER HB3 H 4.056 . 2 170 17 17 SER C C 174.235 . 1 171 17 17 SER CA C 59.795 . 1 172 17 17 SER CB C 64.140 . 1 173 17 17 SER N N 113.724 . 1 174 18 18 ALA H H 7.826 . 1 175 18 18 ALA HA H 4.370 . 1 176 18 18 ALA HB H 1.543 . 1 177 18 18 ALA C C 178.211 . 1 178 18 18 ALA CA C 52.952 . 1 179 18 18 ALA CB C 19.761 . 1 180 18 18 ALA N N 123.220 . 1 181 19 19 GLY H H 8.239 . 1 182 19 19 GLY HA2 H 4.057 . 2 183 19 19 GLY HA3 H 4.057 . 2 184 19 19 GLY C C 174.349 . 1 185 19 19 GLY CA C 45.363 . 1 186 19 19 GLY N N 107.444 . 1 187 20 20 GLU H H 8.474 . 1 188 20 20 GLU HA H 4.473 . 1 189 20 20 GLU HB2 H 2.235 . 2 190 20 20 GLU HB3 H 2.074 . 2 191 20 20 GLU HG2 H 2.408 . 2 192 20 20 GLU HG3 H 2.408 . 2 193 20 20 GLU C C 176.796 . 1 194 20 20 GLU CA C 56.757 . 1 195 20 20 GLU CB C 29.974 . 1 196 20 20 GLU CG C 35.764 . 1 197 20 20 GLU N N 120.373 . 1 198 21 21 THR H H 8.242 . 1 199 21 21 THR HA H 4.513 . 1 200 21 21 THR HB H 4.372 . 1 201 21 21 THR HG2 H 1.243 . 1 202 21 21 THR C C 174.495 . 1 203 21 21 THR CA C 61.845 . 1 204 21 21 THR CB C 70.210 . 1 205 21 21 THR CG2 C 21.579 . 1 206 21 21 THR N N 114.007 . 1 207 22 22 ASP H H 8.485 . 1 208 22 22 ASP HA H 4.722 . 1 209 22 22 ASP HB2 H 2.838 . 2 210 22 22 ASP HB3 H 2.838 . 2 211 22 22 ASP C C 176.815 . 1 212 22 22 ASP CA C 54.738 . 1 213 22 22 ASP CB C 40.927 . 1 214 22 22 ASP N N 122.133 . 1 215 23 23 GLY H H 8.487 . 1 216 23 23 GLY HA2 H 4.071 . 2 217 23 23 GLY HA3 H 4.071 . 2 218 23 23 GLY C C 174.753 . 1 219 23 23 GLY CA C 45.762 . 1 220 23 23 GLY N N 109.373 . 1 221 24 24 THR H H 8.130 . 1 222 24 24 THR HA H 4.330 . 1 223 24 24 THR HB H 4.225 . 1 224 24 24 THR HG2 H 1.279 . 1 225 24 24 THR C C 174.191 . 1 226 24 24 THR CA C 63.073 . 1 227 24 24 THR CB C 69.841 . 1 228 24 24 THR CG2 C 21.674 . 1 229 24 24 THR N N 115.860 . 1 230 25 25 ASP H H 8.602 . 1 231 25 25 ASP HA H 4.713 . 1 232 25 25 ASP HB2 H 2.871 . 2 233 25 25 ASP HB3 H 2.752 . 2 234 25 25 ASP C C 176.164 . 1 235 25 25 ASP CA C 54.488 . 1 236 25 25 ASP CB C 40.952 . 1 237 25 25 ASP N N 123.699 . 1 238 26 26 LEU H H 8.458 . 1 239 26 26 LEU HA H 4.364 . 1 240 26 26 LEU HB2 H 1.451 . 2 241 26 26 LEU HB3 H 1.235 . 2 242 26 26 LEU HD1 H 0.692 . 2 243 26 26 LEU HD2 H 0.802 . 2 244 26 26 LEU HG H 1.581 . 1 245 26 26 LEU C C 176.406 . 1 246 26 26 LEU CA C 54.171 . 1 247 26 26 LEU CB C 41.127 . 1 248 26 26 LEU CD1 C 23.328 . 2 249 26 26 LEU CD2 C 26.277 . 2 250 26 26 LEU CG C 26.739 . 1 251 26 26 LEU N N 123.646 . 1 252 27 27 SER H H 8.225 . 1 253 27 27 SER HA H 4.302 . 1 254 27 27 SER HB2 H 4.032 . 2 255 27 27 SER HB3 H 3.976 . 2 256 27 27 SER C C 175.066 . 1 257 27 27 SER CA C 59.905 . 1 258 27 27 SER CB C 64.219 . 1 259 27 27 SER N N 115.091 . 1 260 28 28 GLY H H 8.556 . 1 261 28 28 GLY HA2 H 4.257 . 2 262 28 28 GLY HA3 H 3.871 . 2 263 28 28 GLY C C 174.225 . 1 264 28 28 GLY CA C 45.371 . 1 265 28 28 GLY N N 111.409 . 1 266 29 29 ASP H H 8.663 . 1 267 29 29 ASP HA H 4.847 . 1 268 29 29 ASP HB2 H 2.888 . 2 269 29 29 ASP HB3 H 2.670 . 2 270 29 29 ASP C C 176.439 . 1 271 29 29 ASP CA C 54.318 . 1 272 29 29 ASP CB C 39.729 . 1 273 29 29 ASP N N 123.189 . 1 274 30 30 PHE H H 8.037 . 1 275 30 30 PHE HA H 4.739 . 1 276 30 30 PHE HB2 H 3.292 . 2 277 30 30 PHE HB3 H 3.015 . 2 278 30 30 PHE HD1 H 7.301 . 3 279 30 30 PHE HD2 H 7.301 . 3 280 30 30 PHE HE1 H 7.209 . 3 281 30 30 PHE HE2 H 7.209 . 3 282 30 30 PHE HZ H 7.339 . 1 283 30 30 PHE C C 175.435 . 1 284 30 30 PHE CA C 57.612 . 1 285 30 30 PHE CB C 40.471 . 1 286 30 30 PHE CD1 C 132.037 . 3 287 30 30 PHE CD2 C 132.037 . 3 288 30 30 PHE CE1 C 130.186 . 3 289 30 30 PHE CE2 C 130.186 . 3 290 30 30 PHE CZ C 128.519 . 1 291 30 30 PHE N N 122.086 . 1 292 31 31 LEU H H 7.503 . 1 293 31 31 LEU HA H 3.307 . 1 294 31 31 LEU HB2 H 1.631 . 2 295 31 31 LEU HB3 H 1.029 . 2 296 31 31 LEU HD1 H 0.459 . 2 297 31 31 LEU HD2 H 0.780 . 2 298 31 31 LEU HG H 1.199 . 1 299 31 31 LEU C C 176.418 . 1 300 31 31 LEU CA C 57.879 . 1 301 31 31 LEU CB C 42.118 . 1 302 31 31 LEU CD1 C 23.772 . 2 303 31 31 LEU CD2 C 25.317 . 2 304 31 31 LEU CG C 26.964 . 1 305 31 31 LEU N N 118.850 . 1 306 32 32 ASP H H 8.046 . 1 307 32 32 ASP HA H 5.047 . 1 308 32 32 ASP HB2 H 3.033 . 2 309 32 32 ASP HB3 H 2.359 . 2 310 32 32 ASP C C 175.984 . 1 311 32 32 ASP CA C 53.779 . 1 312 32 32 ASP CB C 41.775 . 1 313 32 32 ASP N N 111.799 . 1 314 33 33 LEU H H 7.203 . 1 315 33 33 LEU HA H 4.317 . 1 316 33 33 LEU HB2 H 1.775 . 2 317 33 33 LEU HB3 H 1.411 . 2 318 33 33 LEU HD1 H 0.955 . 2 319 33 33 LEU HD2 H 1.062 . 2 320 33 33 LEU HG H 1.782 . 1 321 33 33 LEU C C 174.826 . 1 322 33 33 LEU CA C 54.442 . 1 323 33 33 LEU CB C 42.446 . 1 324 33 33 LEU CD1 C 22.391 . 2 325 33 33 LEU CD2 C 26.159 . 2 326 33 33 LEU CG C 26.958 . 1 327 33 33 LEU N N 122.082 . 1 328 34 34 ARG H H 8.452 . 1 329 34 34 ARG HA H 4.734 . 1 330 34 34 ARG HB2 H 2.179 . 2 331 34 34 ARG HB3 H 1.857 . 2 332 34 34 ARG HD2 H 3.445 . 2 333 34 34 ARG HD3 H 3.349 . 2 334 34 34 ARG HE H 7.983 . 1 335 34 34 ARG HG2 H 1.940 . 2 336 34 34 ARG HG3 H 1.625 . 2 337 34 34 ARG C C 179.799 . 1 338 34 34 ARG CA C 55.436 . 1 339 34 34 ARG CB C 30.117 . 1 340 34 34 ARG CD C 43.563 . 1 341 34 34 ARG CG C 28.310 . 1 342 34 34 ARG N N 116.149 . 1 343 34 34 ARG NE N 85.138 . 1 344 35 35 PHE H H 8.452 . 1 345 35 35 PHE HA H 4.373 . 1 346 35 35 PHE HB2 H 3.586 . 2 347 35 35 PHE HB3 H 3.091 . 2 348 35 35 PHE HD1 H 7.113 . 3 349 35 35 PHE HD2 H 7.113 . 3 350 35 35 PHE HE1 H 6.921 . 3 351 35 35 PHE HE2 H 6.921 . 3 352 35 35 PHE HZ H 6.883 . 1 353 35 35 PHE C C 178.738 . 1 354 35 35 PHE CA C 63.140 . 1 355 35 35 PHE CB C 37.924 . 1 356 35 35 PHE CD1 C 130.893 . 3 357 35 35 PHE CD2 C 130.893 . 3 358 35 35 PHE CE1 C 130.766 . 3 359 35 35 PHE CE2 C 130.766 . 3 360 35 35 PHE CZ C 127.444 . 1 361 35 35 PHE N N 123.134 . 1 362 36 36 GLU H H 9.554 . 1 363 36 36 GLU HA H 4.362 . 1 364 36 36 GLU HB2 H 2.259 . 2 365 36 36 GLU HB3 H 2.135 . 2 366 36 36 GLU HG2 H 2.500 . 2 367 36 36 GLU HG3 H 2.500 . 2 368 36 36 GLU C C 178.578 . 1 369 36 36 GLU CA C 59.146 . 1 370 36 36 GLU CB C 29.368 . 1 371 36 36 GLU CG C 35.657 . 1 372 36 36 GLU N N 117.069 . 1 373 37 37 ASP H H 7.551 . 1 374 37 37 ASP HA H 4.808 . 1 375 37 37 ASP HB2 H 3.088 . 2 376 37 37 ASP HB3 H 2.994 . 2 377 37 37 ASP C C 177.910 . 1 378 37 37 ASP CA C 56.484 . 1 379 37 37 ASP CB C 41.361 . 1 380 37 37 ASP N N 118.294 . 1 381 38 38 ILE H H 7.708 . 1 382 38 38 ILE HA H 4.663 . 1 383 38 38 ILE HB H 2.456 . 1 384 38 38 ILE HD1 H 0.871 . 1 385 38 38 ILE HG12 H 1.826 . 2 386 38 38 ILE HG13 H 1.541 . 2 387 38 38 ILE HG2 H 1.059 . 1 388 38 38 ILE C C 176.044 . 1 389 38 38 ILE CA C 61.997 . 1 390 38 38 ILE CB C 38.669 . 1 391 38 38 ILE CD1 C 13.858 . 1 392 38 38 ILE CG1 C 27.349 . 1 393 38 38 ILE CG2 C 18.762 . 1 394 38 38 ILE N N 112.894 . 1 395 39 39 GLY H H 7.710 . 1 396 39 39 GLY HA2 H 4.260 . 2 397 39 39 GLY HA3 H 3.879 . 2 398 39 39 GLY C C 174.469 . 1 399 39 39 GLY CA C 46.399 . 1 400 39 39 GLY N N 106.989 . 1 401 40 40 TYR H H 8.054 . 1 402 40 40 TYR HA H 4.585 . 1 403 40 40 TYR HB2 H 3.009 . 2 404 40 40 TYR HB3 H 2.786 . 2 405 40 40 TYR HD1 H 6.966 . 3 406 40 40 TYR HD2 H 6.966 . 3 407 40 40 TYR HE1 H 6.750 . 3 408 40 40 TYR HE2 H 6.750 . 3 409 40 40 TYR C C 174.436 . 1 410 40 40 TYR CA C 58.203 . 1 411 40 40 TYR CB C 40.366 . 1 412 40 40 TYR CD1 C 131.768 . 3 413 40 40 TYR CD2 C 131.768 . 3 414 40 40 TYR CE1 C 117.848 . 3 415 40 40 TYR CE2 C 117.848 . 3 416 40 40 TYR N N 121.559 . 1 417 41 41 ASP H H 7.973 . 1 418 41 41 ASP HA H 4.746 . 1 419 41 41 ASP HB2 H 3.296 . 2 420 41 41 ASP HB3 H 2.856 . 2 421 41 41 ASP C C 175.772 . 1 422 41 41 ASP CA C 52.600 . 1 423 41 41 ASP CB C 41.726 . 1 424 41 41 ASP N N 123.474 . 1 425 42 42 SER H H 8.920 . 1 426 42 42 SER HA H 4.262 . 1 427 42 42 SER HB2 H 4.186 . 2 428 42 42 SER HB3 H 4.346 . 2 429 42 42 SER C C 176.039 . 1 430 42 42 SER CA C 60.564 . 1 431 42 42 SER CB C 65.887 . 1 432 42 42 SER N N 113.917 . 1 433 43 43 LEU H H 7.783 . 1 434 43 43 LEU HA H 4.271 . 1 435 43 43 LEU HB2 H 1.886 . 2 436 43 43 LEU HB3 H 1.832 . 2 437 43 43 LEU HD1 H 1.007 . 2 438 43 43 LEU HD2 H 1.053 . 2 439 43 43 LEU HG H 1.736 . 1 440 43 43 LEU C C 179.069 . 1 441 43 43 LEU CA C 58.475 . 1 442 43 43 LEU CB C 41.117 . 1 443 43 43 LEU CD1 C 24.510 . 2 444 43 43 LEU CD2 C 24.575 . 2 445 43 43 LEU CG C 27.398 . 1 446 43 43 LEU N N 124.046 . 1 447 44 44 ALA H H 8.152 . 1 448 44 44 ALA HA H 4.311 . 1 449 44 44 ALA HB H 1.521 . 1 450 44 44 ALA C C 181.873 . 1 451 44 44 ALA CA C 55.105 . 1 452 44 44 ALA CB C 18.487 . 1 453 44 44 ALA N N 123.174 . 1 454 45 45 LEU H H 8.456 . 1 455 45 45 LEU HA H 3.893 . 1 456 45 45 LEU HB2 H 1.629 . 2 457 45 45 LEU HB3 H 1.511 . 2 458 45 45 LEU HD1 H 0.234 . 2 459 45 45 LEU HD2 H 0.354 . 2 460 45 45 LEU HG H 1.352 . 1 461 45 45 LEU C C 178.390 . 1 462 45 45 LEU CA C 58.462 . 1 463 45 45 LEU CB C 41.633 . 1 464 45 45 LEU CD1 C 23.382 . 2 465 45 45 LEU CD2 C 23.704 . 2 466 45 45 LEU CG C 27.053 . 1 467 45 45 LEU N N 121.281 . 1 468 46 46 MET H H 8.222 . 1 469 46 46 MET HA H 4.258 . 1 470 46 46 MET HB2 H 2.321 . 2 471 46 46 MET HB3 H 2.321 . 2 472 46 46 MET HG2 H 2.840 . 2 473 46 46 MET HG3 H 2.753 . 2 474 46 46 MET C C 179.704 . 1 475 46 46 MET CA C 58.810 . 1 476 46 46 MET CB C 32.040 . 1 477 46 46 MET CG C 32.321 . 1 478 46 46 MET N N 119.424 . 1 479 47 47 GLU H H 8.500 . 1 480 47 47 GLU HA H 4.229 . 1 481 47 47 GLU HB2 H 2.345 . 2 482 47 47 GLU HB3 H 2.204 . 2 483 47 47 GLU HG2 H 2.609 . 2 484 47 47 GLU HG3 H 2.464 . 2 485 47 47 GLU C C 179.293 . 1 486 47 47 GLU CA C 59.335 . 1 487 47 47 GLU CB C 29.144 . 1 488 47 47 GLU CG C 35.587 . 1 489 47 47 GLU N N 120.629 . 1 490 48 48 THR H H 8.317 . 1 491 48 48 THR HA H 3.959 . 1 492 48 48 THR HB H 4.414 . 1 493 48 48 THR HG2 H 1.126 . 1 494 48 48 THR C C 176.278 . 1 495 48 48 THR CA C 67.932 . 1 496 48 48 THR CB C 68.528 . 1 497 48 48 THR CG2 C 20.696 . 1 498 48 48 THR N N 118.596 . 1 499 49 49 ALA H H 8.753 . 1 500 49 49 ALA HA H 3.952 . 1 501 49 49 ALA HB H 1.527 . 1 502 49 49 ALA C C 178.630 . 1 503 49 49 ALA CA C 56.319 . 1 504 49 49 ALA CB C 17.459 . 1 505 49 49 ALA N N 123.688 . 1 506 50 50 ALA H H 8.222 . 1 507 50 50 ALA HA H 4.263 . 1 508 50 50 ALA HB H 1.648 . 1 509 50 50 ALA C C 181.263 . 1 510 50 50 ALA CA C 55.546 . 1 511 50 50 ALA CB C 18.039 . 1 512 50 50 ALA N N 119.424 . 1 513 51 51 ARG H H 8.110 . 1 514 51 51 ARG HA H 4.238 . 1 515 51 51 ARG HB2 H 2.195 . 2 516 51 51 ARG HB3 H 2.030 . 2 517 51 51 ARG HD2 H 3.442 . 2 518 51 51 ARG HD3 H 3.309 . 2 519 51 51 ARG HE H 7.548 . 1 520 51 51 ARG HG2 H 1.973 . 2 521 51 51 ARG HG3 H 1.733 . 2 522 51 51 ARG C C 179.747 . 1 523 51 51 ARG CA C 59.590 . 1 524 51 51 ARG CB C 30.381 . 1 525 51 51 ARG CD C 43.639 . 1 526 51 51 ARG CG C 28.302 . 1 527 51 51 ARG N N 119.589 . 1 528 51 51 ARG NE N 84.807 . 1 529 52 52 LEU H H 8.408 . 1 530 52 52 LEU HA H 4.310 . 1 531 52 52 LEU HB2 H 2.213 . 2 532 52 52 LEU HB3 H 1.446 . 2 533 52 52 LEU HD1 H 0.866 . 2 534 52 52 LEU HD2 H 1.034 . 2 535 52 52 LEU HG H 2.041 . 1 536 52 52 LEU C C 179.131 . 1 537 52 52 LEU CA C 58.056 . 1 538 52 52 LEU CB C 42.626 . 1 539 52 52 LEU CD1 C 26.413 . 2 540 52 52 LEU CD2 C 23.615 . 2 541 52 52 LEU CG C 26.719 . 1 542 52 52 LEU N N 120.390 . 1 543 53 53 GLU H H 8.959 . 1 544 53 53 GLU HA H 4.093 . 1 545 53 53 GLU HB2 H 2.503 . 2 546 53 53 GLU HB3 H 2.357 . 2 547 53 53 GLU HG2 H 2.763 . 2 548 53 53 GLU HG3 H 2.318 . 2 549 53 53 GLU C C 179.299 . 1 550 53 53 GLU CA C 60.221 . 1 551 53 53 GLU CB C 29.050 . 1 552 53 53 GLU CG C 34.795 . 1 553 53 53 GLU N N 119.322 . 1 554 54 54 SER H H 8.032 . 1 555 54 54 SER HA H 4.384 . 1 556 54 54 SER HB2 H 4.107 . 2 557 54 54 SER HB3 H 4.107 . 2 558 54 54 SER C C 176.960 . 1 559 54 54 SER CA C 61.157 . 1 560 54 54 SER CB C 63.271 . 1 561 54 54 SER N N 112.831 . 1 562 55 55 ARG H H 8.086 . 1 563 55 55 ARG HA H 4.092 . 1 564 55 55 ARG HB2 H 1.897 . 2 565 55 55 ARG HB3 H 1.613 . 2 566 55 55 ARG HD2 H 3.094 . 2 567 55 55 ARG HD3 H 3.015 . 2 568 55 55 ARG HE H 7.178 . 1 569 55 55 ARG HG2 H 1.364 . 2 570 55 55 ARG HG3 H 0.983 . 2 571 55 55 ARG C C 177.832 . 1 572 55 55 ARG CA C 58.864 . 1 573 55 55 ARG CB C 30.806 . 1 574 55 55 ARG CD C 43.531 . 1 575 55 55 ARG CG C 26.965 . 1 576 55 55 ARG N N 120.687 . 1 577 55 55 ARG NE N 84.831 . 1 578 56 56 TYR H H 8.117 . 1 579 56 56 TYR HA H 4.681 . 1 580 56 56 TYR HB2 H 3.456 . 2 581 56 56 TYR HB3 H 2.789 . 2 582 56 56 TYR HD1 H 7.439 . 3 583 56 56 TYR HD2 H 7.439 . 3 584 56 56 TYR HE1 H 6.807 . 3 585 56 56 TYR HE2 H 6.807 . 3 586 56 56 TYR C C 175.961 . 1 587 56 56 TYR CA C 59.144 . 1 588 56 56 TYR CB C 39.302 . 1 589 56 56 TYR CD1 C 132.652 . 3 590 56 56 TYR CD2 C 132.652 . 3 591 56 56 TYR CE1 C 117.788 . 3 592 56 56 TYR CE2 C 117.788 . 3 593 56 56 TYR N N 113.447 . 1 594 57 57 GLY H H 7.955 . 1 595 57 57 GLY HA2 H 4.090 . 2 596 57 57 GLY HA3 H 4.090 . 2 597 57 57 GLY C C 174.609 . 1 598 57 57 GLY CA C 47.363 . 1 599 57 57 GLY N N 109.538 . 1 600 58 58 VAL H H 7.529 . 1 601 58 58 VAL HA H 4.683 . 1 602 58 58 VAL HB H 2.135 . 1 603 58 58 VAL HG1 H 0.921 . 2 604 58 58 VAL HG2 H 0.971 . 2 605 58 58 VAL C C 174.043 . 1 606 58 58 VAL CA C 59.391 . 1 607 58 58 VAL CB C 34.772 . 1 608 58 58 VAL CG1 C 19.527 . 2 609 58 58 VAL CG2 C 21.589 . 2 610 58 58 VAL N N 112.302 . 1 611 59 59 SER H H 8.481 . 1 612 59 59 SER HA H 4.833 . 1 613 59 59 SER HB2 H 3.798 . 2 614 59 59 SER HB3 H 3.752 . 2 615 59 59 SER C C 173.599 . 1 616 59 59 SER CA C 57.235 . 1 617 59 59 SER CB C 64.342 . 1 618 59 59 SER N N 116.827 . 1 619 60 60 ILE H H 8.168 . 1 620 60 60 ILE HA H 4.655 . 1 621 60 60 ILE HB H 1.790 . 1 622 60 60 ILE HD1 H 0.846 . 1 623 60 60 ILE HG12 H 1.485 . 2 624 60 60 ILE HG13 H 1.112 . 2 625 60 60 ILE HG2 H 1.025 . 1 626 60 60 ILE CA C 57.804 . 1 627 60 60 ILE CB C 40.438 . 1 628 60 60 ILE CD1 C 13.683 . 1 629 60 60 ILE CG1 C 27.102 . 1 630 60 60 ILE CG2 C 17.289 . 1 631 60 60 ILE N N 125.502 . 1 632 61 61 PRO HA H 4.528 . 1 633 61 61 PRO HB2 H 2.542 . 2 634 61 61 PRO HB3 H 2.061 . 2 635 61 61 PRO HD2 H 4.012 . 2 636 61 61 PRO HD3 H 3.574 . 2 637 61 61 PRO HG2 H 2.138 . 2 638 61 61 PRO HG3 H 2.138 . 2 639 61 61 PRO C C 177.478 . 1 640 61 61 PRO CA C 63.589 . 1 641 61 61 PRO CB C 32.701 . 1 642 61 61 PRO CD C 51.429 . 1 643 61 61 PRO CG C 27.935 . 1 644 62 62 ASP H H 8.821 . 1 645 62 62 ASP HA H 4.458 . 1 646 62 62 ASP HB2 H 2.822 . 2 647 62 62 ASP HB3 H 2.748 . 2 648 62 62 ASP C C 177.237 . 1 649 62 62 ASP CA C 57.099 . 1 650 62 62 ASP CB C 40.602 . 1 651 62 62 ASP N N 123.215 . 1 652 63 63 ASP H H 8.614 . 1 653 63 63 ASP HA H 4.521 . 1 654 63 63 ASP HB2 H 2.827 . 2 655 63 63 ASP HB3 H 2.741 . 2 656 63 63 ASP C C 177.196 . 1 657 63 63 ASP CA C 55.003 . 1 658 63 63 ASP CB C 39.619 . 1 659 63 63 ASP N N 116.530 . 1 660 64 64 VAL H H 7.396 . 1 661 64 64 VAL HA H 3.827 . 1 662 64 64 VAL HB H 2.213 . 1 663 64 64 VAL HG1 H 0.976 . 2 664 64 64 VAL HG2 H 1.031 . 2 665 64 64 VAL C C 177.517 . 1 666 64 64 VAL CA C 65.003 . 1 667 64 64 VAL CB C 32.363 . 1 668 64 64 VAL CG1 C 21.223 . 2 669 64 64 VAL CG2 C 21.898 . 2 670 64 64 VAL N N 118.858 . 1 671 65 65 ALA H H 8.214 . 1 672 65 65 ALA HA H 3.989 . 1 673 65 65 ALA HB H 1.393 . 1 674 65 65 ALA C C 177.967 . 1 675 65 65 ALA CA C 55.076 . 1 676 65 65 ALA CB C 18.408 . 1 677 65 65 ALA N N 122.297 . 1 678 66 66 GLY H H 8.031 . 1 679 66 66 GLY HA2 H 4.115 . 2 680 66 66 GLY HA3 H 3.888 . 2 681 66 66 GLY C C 174.306 . 1 682 66 66 GLY CA C 45.873 . 1 683 66 66 GLY N N 100.410 . 1 684 67 67 ARG H H 7.485 . 1 685 67 67 ARG HA H 4.624 . 1 686 67 67 ARG HB2 H 2.078 . 2 687 67 67 ARG HB3 H 1.860 . 2 688 67 67 ARG HD2 H 3.271 . 2 689 67 67 ARG HD3 H 3.271 . 2 690 67 67 ARG HE H 7.391 . 1 691 67 67 ARG HG2 H 1.751 . 2 692 67 67 ARG HG3 H 1.751 . 2 693 67 67 ARG C C 176.427 . 1 694 67 67 ARG CA C 55.665 . 1 695 67 67 ARG CB C 31.863 . 1 696 67 67 ARG CD C 43.792 . 1 697 67 67 ARG CG C 27.437 . 1 698 67 67 ARG N N 116.687 . 1 699 67 67 ARG NE N 85.086 . 1 700 68 68 VAL H H 7.320 . 1 701 68 68 VAL HA H 4.444 . 1 702 68 68 VAL HB H 2.403 . 1 703 68 68 VAL HG1 H 1.131 . 2 704 68 68 VAL HG2 H 1.207 . 2 705 68 68 VAL C C 175.122 . 1 706 68 68 VAL CA C 61.805 . 1 707 68 68 VAL CB C 33.395 . 1 708 68 68 VAL CG1 C 23.229 . 2 709 68 68 VAL CG2 C 20.169 . 2 710 68 68 VAL N N 114.967 . 1 711 69 69 ASP H H 9.091 . 1 712 69 69 ASP HA H 5.269 . 1 713 69 69 ASP HB2 H 3.009 . 2 714 69 69 ASP HB3 H 2.880 . 2 715 69 69 ASP C C 176.735 . 1 716 69 69 ASP CA C 55.684 . 1 717 69 69 ASP CB C 44.187 . 1 718 69 69 ASP N N 120.632 . 1 719 70 70 THR H H 7.469 . 1 720 70 70 THR HA H 4.953 . 1 721 70 70 THR HB H 4.623 . 1 722 70 70 THR HG2 H 1.074 . 1 723 70 70 THR CA C 57.767 . 1 724 70 70 THR CB C 71.449 . 1 725 70 70 THR CG2 C 21.615 . 1 726 70 70 THR N N 108.006 . 1 727 71 71 PRO HA H 4.229 . 1 728 71 71 PRO HB2 H 2.250 . 2 729 71 71 PRO HB3 H 2.016 . 2 730 71 71 PRO HD2 H 4.030 . 2 731 71 71 PRO HD3 H 2.812 . 2 732 71 71 PRO HG2 H 2.182 . 2 733 71 71 PRO HG3 H 1.316 . 2 734 71 71 PRO C C 177.363 . 1 735 71 71 PRO CA C 65.826 . 1 736 71 71 PRO CB C 32.653 . 1 737 71 71 PRO CD C 51.892 . 1 738 71 71 PRO CG C 26.760 . 1 739 72 72 ARG H H 8.996 . 1 740 72 72 ARG HA H 3.609 . 1 741 72 72 ARG HB2 H 1.871 . 2 742 72 72 ARG HB3 H 1.607 . 2 743 72 72 ARG HD2 H 3.494 . 2 744 72 72 ARG HD3 H 3.019 . 2 745 72 72 ARG HE H 9.066 . 1 746 72 72 ARG HG2 H 1.661 . 2 747 72 72 ARG HG3 H 1.512 . 2 748 72 72 ARG HH11 H 6.886 . 2 749 72 72 ARG HH12 H 6.886 . 2 750 72 72 ARG HH21 H 6.886 . 2 751 72 72 ARG HH22 H 6.886 . 2 752 72 72 ARG C C 177.582 . 1 753 72 72 ARG CA C 60.292 . 1 754 72 72 ARG CB C 30.517 . 1 755 72 72 ARG CD C 42.908 . 1 756 72 72 ARG CG C 27.554 . 1 757 72 72 ARG N N 117.649 . 1 758 72 72 ARG NE N 83.499 . 1 759 72 72 ARG NH1 N 71.210 . 2 760 72 72 ARG NH2 N 71.210 . 2 761 73 73 GLU H H 7.832 . 1 762 73 73 GLU HA H 4.238 . 1 763 73 73 GLU HB2 H 2.467 . 2 764 73 73 GLU HB3 H 2.267 . 2 765 73 73 GLU HG2 H 2.639 . 2 766 73 73 GLU HG3 H 2.509 . 2 767 73 73 GLU C C 180.096 . 1 768 73 73 GLU CA C 58.902 . 1 769 73 73 GLU CB C 29.958 . 1 770 73 73 GLU CG C 36.283 . 1 771 73 73 GLU N N 116.481 . 1 772 74 74 LEU H H 7.708 . 1 773 74 74 LEU HA H 4.308 . 1 774 74 74 LEU HB2 H 2.424 . 2 775 74 74 LEU HB3 H 1.699 . 2 776 74 74 LEU HD1 H 1.066 . 2 777 74 74 LEU HD2 H 1.066 . 2 778 74 74 LEU HG H 0.978 . 1 779 74 74 LEU C C 176.980 . 1 780 74 74 LEU CA C 58.215 . 1 781 74 74 LEU CB C 42.245 . 1 782 74 74 LEU CD1 C 22.475 . 2 783 74 74 LEU CD2 C 22.475 . 2 784 74 74 LEU CG C 26.335 . 1 785 74 74 LEU N N 120.457 . 1 786 75 75 LEU H H 8.724 . 1 787 75 75 LEU HA H 3.890 . 1 788 75 75 LEU HB2 H 2.194 . 2 789 75 75 LEU HB3 H 1.549 . 2 790 75 75 LEU HD1 H 0.794 . 2 791 75 75 LEU HD2 H 0.874 . 2 792 75 75 LEU HG H 1.691 . 1 793 75 75 LEU C C 178.086 . 1 794 75 75 LEU CA C 58.425 . 1 795 75 75 LEU CB C 42.379 . 1 796 75 75 LEU CD1 C 24.801 . 2 797 75 75 LEU CD2 C 26.460 . 2 798 75 75 LEU CG C 26.484 . 1 799 75 75 LEU N N 121.083 . 1 800 76 76 ASP H H 8.689 . 1 801 76 76 ASP HA H 4.484 . 1 802 76 76 ASP HB2 H 2.770 . 2 803 76 76 ASP HB3 H 2.715 . 2 804 76 76 ASP C C 180.043 . 1 805 76 76 ASP CA C 56.826 . 1 806 76 76 ASP CB C 39.739 . 1 807 76 76 ASP N N 117.520 . 1 808 77 77 LEU H H 7.998 . 1 809 77 77 LEU HA H 4.276 . 1 810 77 77 LEU HB2 H 2.029 . 2 811 77 77 LEU HB3 H 1.913 . 2 812 77 77 LEU HD1 H 0.966 . 2 813 77 77 LEU HD2 H 0.966 . 2 814 77 77 LEU HG H 1.826 . 1 815 77 77 LEU C C 179.828 . 1 816 77 77 LEU CA C 58.332 . 1 817 77 77 LEU CB C 42.875 . 1 818 77 77 LEU CD1 C 25.268 . 2 819 77 77 LEU CD2 C 25.268 . 2 820 77 77 LEU CG C 27.058 . 1 821 77 77 LEU N N 122.934 . 1 822 78 78 ILE H H 8.270 . 1 823 78 78 ILE HA H 3.741 . 1 824 78 78 ILE HB H 1.939 . 1 825 78 78 ILE HD1 H 0.797 . 1 826 78 78 ILE HG12 H 1.731 . 2 827 78 78 ILE HG13 H 1.283 . 2 828 78 78 ILE HG2 H 0.871 . 1 829 78 78 ILE C C 177.669 . 1 830 78 78 ILE CA C 64.712 . 1 831 78 78 ILE CB C 37.386 . 1 832 78 78 ILE CD1 C 13.142 . 1 833 78 78 ILE CG1 C 28.910 . 1 834 78 78 ILE CG2 C 17.403 . 1 835 78 78 ILE N N 119.758 . 1 836 79 79 ASN H H 8.871 . 1 837 79 79 ASN HA H 4.906 . 1 838 79 79 ASN HB2 H 3.092 . 2 839 79 79 ASN HB3 H 2.769 . 2 840 79 79 ASN HD21 H 7.325 . 2 841 79 79 ASN HD22 H 7.666 . 2 842 79 79 ASN C C 179.440 . 1 843 79 79 ASN CA C 55.412 . 1 844 79 79 ASN CB C 37.266 . 1 845 79 79 ASN N N 117.866 . 1 846 79 79 ASN ND2 N 107.702 . 1 847 80 80 GLY H H 8.414 . 1 848 80 80 GLY HA2 H 4.023 . 2 849 80 80 GLY HA3 H 4.023 . 2 850 80 80 GLY C C 175.715 . 1 851 80 80 GLY CA C 47.068 . 1 852 80 80 GLY N N 110.064 . 1 853 81 81 ALA H H 7.580 . 1 854 81 81 ALA HA H 4.460 . 1 855 81 81 ALA HB H 1.629 . 1 856 81 81 ALA C C 180.487 . 1 857 81 81 ALA CA C 54.248 . 1 858 81 81 ALA CB C 18.492 . 1 859 81 81 ALA N N 124.034 . 1 860 82 82 LEU H H 8.270 . 1 861 82 82 LEU HA H 4.215 . 1 862 82 82 LEU HB2 H 2.010 . 2 863 82 82 LEU HB3 H 1.558 . 2 864 82 82 LEU HD1 H 0.985 . 2 865 82 82 LEU HD2 H 0.989 . 2 866 82 82 LEU HG H 1.844 . 1 867 82 82 LEU C C 178.766 . 1 868 82 82 LEU CA C 56.924 . 1 869 82 82 LEU CB C 42.621 . 1 870 82 82 LEU CD1 C 26.051 . 2 871 82 82 LEU CD2 C 23.849 . 2 872 82 82 LEU CG C 27.150 . 1 873 82 82 LEU N N 119.924 . 1 874 83 83 ALA H H 7.951 . 1 875 83 83 ALA HA H 4.282 . 1 876 83 83 ALA HB H 1.604 . 1 877 83 83 ALA C C 178.659 . 1 878 83 83 ALA CA C 53.966 . 1 879 83 83 ALA CB C 18.890 . 1 880 83 83 ALA N N 121.324 . 1 881 84 84 GLU H H 7.742 . 1 882 84 84 GLU HA H 4.391 . 1 883 84 84 GLU HB2 H 2.277 . 2 884 84 84 GLU HB3 H 2.125 . 2 885 84 84 GLU HG2 H 2.535 . 2 886 84 84 GLU HG3 H 2.464 . 2 887 84 84 GLU C C 176.280 . 1 888 84 84 GLU CA C 56.608 . 1 889 84 84 GLU CB C 30.109 . 1 890 84 84 GLU CG C 35.700 . 1 891 84 84 GLU N N 117.064 . 1 892 85 85 ALA H H 7.822 . 1 893 85 85 ALA HA H 4.474 . 1 894 85 85 ALA HB H 1.570 . 1 895 85 85 ALA C C 176.520 . 1 896 85 85 ALA CA C 52.470 . 1 897 85 85 ALA CB C 19.493 . 1 898 85 85 ALA N N 124.162 . 1 899 86 86 ALA H H 7.968 . 1 900 86 86 ALA HA H 4.224 . 1 901 86 86 ALA HB H 1.481 . 1 902 86 86 ALA CA C 54.245 . 1 903 86 86 ALA CB C 20.065 . 1 904 86 86 ALA N N 129.204 . 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D H(CCO)NH' '3D C(CO)NH' '3D HCCH-TOCSY' '3D HNCO' 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 SXA _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 42 1 SXA H2A H 2.439 . 1 2 42 1 SXA H2B H 2.439 . 1 3 42 1 SXA H2C H 2.439 . 1 4 42 1 SXA H28A H 3.453 . 2 5 42 1 SXA H28B H 3.899 . 2 6 42 1 SXA H30A H 0.942 . 2 7 42 1 SXA H30B H 0.942 . 2 8 42 1 SXA H30C H 0.942 . 2 9 42 1 SXA H31A H 1.068 . 2 10 42 1 SXA H31B H 1.068 . 2 11 42 1 SXA H31C H 1.068 . 2 12 42 1 SXA H32A H 4.119 . 1 13 42 1 SXA H36A H 8.112 . 1 14 42 1 SXA H37A H 3.583 . 2 15 42 1 SXA H37B H 3.583 . 2 16 42 1 SXA H38A H 2.564 . 2 17 42 1 SXA H38B H 2.564 . 2 18 42 1 SXA H41A H 8.294 . 1 19 42 1 SXA H42A H 3.448 . 2 20 42 1 SXA H42B H 3.448 . 2 21 42 1 SXA H43A H 3.085 . 2 22 42 1 SXA H43B H 3.085 . 2 stop_ save_