data_4604 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES ; _BMRB_accession_number 4604 _BMRB_flat_file_name bmr4604.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Anders R. . . 2 Ohlenschlager O. . . 3 Soskic V. . . 4 Wenschuh H. . . 5 Heise B. . . 6 Brown L. R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 97 "13C chemical shifts" 75 "15N chemical shifts" 3 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20177705 _PubMed_ID 10712611 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Anders R. . . 2 Ohlenschlager O. . . 3 Soskic V. . . 4 Wenschuh H. . . 5 Heise B. . . 6 Brown L. R. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 267 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1784 _Page_last 1794 _Year 2000 _Details . loop_ _Keyword 'CHRYSOSPERMIN C' PEPTAIBOL 'PEPTIDE ANTIBIOTIC' 'ION CHANNEL' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'Guntert, P., Mumenthaler, C. and Wuthrich, K. (1997) J.Mol.Biol., 273: 283-298.' _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guentert P . . 2 Mumenthaler C . . 3 Wuethrich K . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ save_ref_2 _Saveframe_category citation _Citation_full 'Luginbuhl, P., Guntert, P., Billeter, M. and Wuthrich, K. (1996) J. Biomol. NMR 8: 136-146.' _Citation_title 'The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8914272 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Luginbuehl P . . 2 Guentert P . . 3 Billeter M . . 4 Wuethrich K . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 8 _Journal_issue 2 _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 136 _Page_last 146 _Year 1996 _Details ; A new program for molecular dynamics (MD) simulation and energy refinement of biological macromolecules, OPAL, is introduced. Combined with the supporting program TRAJEC for the analysis of MD trajectories, OPAL affords high efficiency and flexibility for work with different force fields, and offers a user-friendly interface and extensive trajectory analysis capabilities. Salient features are computational speeds of up to 1.5 GFlops on vector supercomputers such as the NEC SX-3, ellipsoidal boundaries to reduce the system size for studies in explicit solvents, and natural treatment of the hydrostatic pressure. Practical applications of OPAL are illustrated with MD simulations of pure water, energy minimization of the NMR structure of the mixed disulfide of a mutant E. coli glutaredoxin with glutathione in different solvent models, and MD simulations of a small protein, pheromone Er-2, using either instantaneous or time-averaged NMR restraints, or no restraints. ; save_ ################################## # Molecular system description # ################################## save_system_CSC _Saveframe_category molecular_system _Mol_system_name 'THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES' _Abbreviation_common CSC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CHRYSOSPERMIN $CSC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'PEPTIDE ANTIBIOTIC' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CSC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CHRYSOSPERMIN C' _Abbreviation_common CSC _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence XFXSXXLQGXXAAXPXXXQX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ACE 2 3 PHE 3 4 AIB 4 5 SER 5 6 AIB 6 7 DIV 7 8 LEU 8 9 GLN 9 10 GLY 10 11 AIB 11 12 AIB 12 13 ALA 13 14 ALA 14 15 AIB 15 16 PRO 16 17 AIB 17 18 AIB 18 19 AIB 19 20 GLN 20 21 TPL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_AIB _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'ALPHA-AMINOISOBUTYRIC ACID' _BMRB_code AIB _PDB_code AIB _Standard_residue_derivative . _Molecular_mass 103.120 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB1 CB1 C . 0 . ? CB2 CB2 C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HB11 HB11 H . 0 . ? HB12 HB12 H . 0 . ? HB13 HB13 H . 0 . ? HB21 HB21 H . 0 . ? HB22 HB22 H . 0 . ? HB23 HB23 H . 0 . ? HO2 HO2 H . 0 . ? N N N . 0 . ? O O O . 0 . ? OXT OXT O . 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 N CA ? ? SING N H ? ? SING N H2 ? ? SING CA C ? ? SING CA CB1 ? ? SING CA CB2 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HO2 ? ? SING CB1 HB11 ? ? SING CB1 HB12 ? ? SING CB1 HB13 ? ? SING CB2 HB21 ? ? SING CB2 HB22 ? ? SING CB2 HB23 ? ? stop_ save_ save_chem_comp_DIV _Saveframe_category polymer_residue _Mol_type 'D-PEPTIDE LINKING' _Name_common D-ISOVALINE _BMRB_code DIV _PDB_code DIV _Standard_residue_derivative . _Molecular_mass 117.146 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB1 CB1 C . 0 . ? CB2 CB2 C . 0 . ? CG1 CG1 C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HB11 HB11 H . 0 . ? HB12 HB12 H . 0 . ? HB21 HB21 H . 0 . ? HB22 HB22 H . 0 . ? HB23 HB23 H . 0 . ? HG11 HG11 H . 0 . ? HG12 HG12 H . 0 . ? HG13 HG13 H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? O O O . 0 . ? OXT OXT O . 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 N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB1 ? ? SING CA CB2 ? ? SING CA C ? ? SING CB1 CG1 ? ? SING CB1 HB11 ? ? SING CB1 HB12 ? ? SING CG1 HG11 ? ? SING CG1 HG12 ? ? SING CG1 HG13 ? ? SING CB2 HB21 ? ? SING CB2 HB22 ? ? SING CB2 HB23 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? O O O . 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_TPL _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common TRYPTOPHANOL _BMRB_code TPL _PDB_code TPL _Standard_residue_derivative . _Molecular_mass 190.242 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB1 CB1 C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE2 CE2 C . 0 . ? CE3 CE3 C . 0 . ? CG CG C . 0 . ? CH2 CH2 C . 0 . ? CZ2 CZ2 C . 0 . ? CZ3 CZ3 C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HC1 HC1 H . 0 . ? HC2 HC2 H . 0 . ? HD1 HD1 H . 0 . ? HE1 HE1 H . 0 . ? HE3 HE3 H . 0 . ? HH2 HH2 H . 0 . ? HXT HXT H . 0 . ? HZ2 HZ2 H . 0 . ? HZ3 HZ3 H . 0 . ? N N N . 0 . ? NE1 NE1 N . 0 . ? OXT OXT O . 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 N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB1 ? ? SING CA C ? ? SING CA HA ? ? SING CB1 CG ? ? SING CB1 HB1 ? ? SING CB1 HB2 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 NE1 ? ? SING CD1 HD1 ? ? SING CD2 CE3 ? ? DOUB CD2 CE2 ? ? DOUB CE3 CZ3 ? ? SING CE3 HE3 ? ? SING CE2 NE1 ? ? SING CE2 CZ2 ? ? SING NE1 HE1 ? ? SING CZ3 CH2 ? ? SING CZ3 HZ3 ? ? DOUB CZ2 CH2 ? ? SING CZ2 HZ2 ? ? SING CH2 HH2 ? ? SING C OXT ? ? SING C HC1 ? ? SING C HC2 ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CSC 'Apiocrea chrysospermum' 5131 Eukaryota Fungi Hypomyces chrysospermus 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 $CSC 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelles _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CSC 6.0 mM . 'DPC micelles' 0.02 v/v . H2O 94 % . D2O 6 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type micelles _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CSC 4.3 mM '[U-15N; U-13C]-AIB8, [U-15N; U-13C]-AIB9, [U-15N; U-13C]-AIB12, [U-13C]-AIB14(CB), [U-13C]-AIB15(CB), [U-13C]-AIB16(CB)' 'DPC micelles' 0.02 v/v . H2O 94 % . D2O 6 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'STRUCTURE SOLUTION' stop_ _Details . _Citation_label $ref_1 save_ save_OPAL _Saveframe_category software _Name OPAL _Version 2.6 loop_ _Task REFINEMENT stop_ _Details . _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.2 pH temperature 318 0.2 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name CHRYSOSPERMIN _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 ACE H1 H 2.14 0.01 1 2 . 1 ACE H2 H 2.14 0.01 1 3 . 1 ACE H3 H 2.14 0.01 1 4 . 2 PHE H H 8.86 0.01 1 5 . 2 PHE HA H 4.20 0.01 1 6 . 2 PHE CB C 39.9 0.2 1 7 . 2 PHE HB2 H 3.20 0.01 2 8 . 2 PHE HB3 H 3.01 0.01 2 9 . 2 PHE CG C 139.4 0.2 1 10 . 2 PHE CD1 C 132.1 0.2 1 11 . 2 PHE HD1 H 7.23 0.01 1 12 . 2 PHE CE1 C 130.8 0.2 1 13 . 2 PHE HE1 H 7.20 0.01 1 14 . 2 PHE CZ C 129.1 0.2 1 15 . 2 PHE HZ H 7.12 0.01 1 16 . 2 PHE CE2 C 130.8 0.2 1 17 . 2 PHE HE2 H 7.20 0.01 1 18 . 2 PHE CD2 C 132.1 0.2 1 19 . 2 PHE HD2 H 7.23 0.01 1 20 . 3 AIB H H 8.72 0.01 1 21 . 3 AIB CA C 58.5 0.2 1 22 . 3 AIB HB11 H 1.45 0.01 2 23 . 3 AIB CB1 C 28.7 0.2 1 24 . 3 AIB HB21 H 1.31 0.01 2 25 . 3 AIB CB2 C 25.7 0.2 1 26 . 3 AIB C C 179.2 0.2 1 27 . 4 SER H H 7.51 0.01 1 28 . 4 SER HA H 4.04 0.01 1 29 . 4 SER CB C 63.1 0.2 1 30 . 4 SER HB2 H 3.84 0.01 1 31 . 4 SER HB3 H 3.84 0.01 1 32 . 5 AIB H H 7.93 0.01 1 33 . 5 AIB CA C 58.9 0.2 1 34 . 5 AIB HB11 H 1.48 0.01 2 35 . 5 AIB CB1 C 29.1 0.2 1 36 . 5 AIB HB21 H 1.40 0.01 2 37 . 5 AIB CB2 C 24.8 0.2 1 38 . 5 AIB C C 179.8 0.2 1 39 . 6 DIV H H 8.06 0.01 1 40 . 6 DIV CA C 61.3 0.2 1 41 . 6 DIV HB11 H 1.19 0.01 1 42 . 6 DIV CB1 C 25.2 0.2 1 43 . 6 DIV CB2 C 27.9 0.2 1 44 . 6 DIV HB22 H 2.23 0.01 2 45 . 6 DIV HB23 H 1.59 0.01 2 46 . 6 DIV HG11 H 0.63 0.01 1 47 . 6 DIV HG12 H 0.63 0.01 1 48 . 6 DIV HG13 H 0.63 0.01 1 49 . 6 DIV CG1 C 9.7 0.2 1 50 . 6 DIV C C 180.5 0.2 1 51 . 7 LEU H H 7.61 0.01 1 52 . 7 LEU CA C 58.1 0.2 1 53 . 7 LEU HA H 4.00 0.01 1 54 . 7 LEU CB C 41.8 0.2 1 55 . 7 LEU HB2 H 1.89 0.01 2 56 . 7 LEU HB3 H 1.67 0.01 2 57 . 7 LEU CG C 27.4 0.2 1 58 . 7 LEU HG H 1.90 0.01 1 59 . 7 LEU HD1 H 0.89 0.01 2 60 . 7 LEU HD2 H 0.95 0.01 2 61 . 7 LEU CD1 C 23.9 0.2 1 62 . 7 LEU CD2 C 25.2 0.2 1 63 . 8 GLN H H 7.93 0.01 1 64 . 8 GLN HA H 4.11 0.01 1 65 . 8 GLN CB C 28.7 0.2 1 66 . 8 GLN HB2 H 2.12 0.01 2 67 . 8 GLN HB3 H 2.17 0.01 2 68 . 8 GLN CG C 34.4 0.2 1 69 . 8 GLN HG2 H 2.36 0.01 2 70 . 8 GLN HG3 H 2.51 0.01 2 71 . 8 GLN CD C 179.7 0.2 1 72 . 8 GLN HE21 H 6.70 0.01 2 73 . 8 GLN HE22 H 7.35 0.01 2 74 . 9 GLY H H 8.17 0.01 1 75 . 9 GLY HA2 H 3.83 0.01 2 76 . 9 GLY HA3 H 3.58 0.01 2 77 . 10 AIB H H 8.45 0.01 1 78 . 10 AIB CA C 58.7 0.2 1 79 . 10 AIB HB11 H 1.49 0.01 2 80 . 10 AIB CB1 C 28.8 0.2 1 81 . 10 AIB HB21 H 1.41 0.01 2 82 . 10 AIB CB2 C 25.3 0.2 1 83 . 10 AIB C C 178.3 0.2 1 84 . 10 AIB N N 132.0 0.2 1 85 . 11 AIB H H 7.91 0.01 1 86 . 11 AIB CA C 59.6 0.2 1 87 . 11 AIB HB11 H 1.53 0.01 2 88 . 11 AIB CB1 C 29.1 0.2 1 89 . 11 AIB HB21 H 1.50 0.01 2 90 . 11 AIB CB2 C 25.2 0.2 1 91 . 11 AIB C C 180.6 0.2 1 92 . 11 AIB N N 125.5 0.2 1 93 . 12 ALA H H 7.64 0.01 1 94 . 12 ALA CA C 54.1 0.2 1 95 . 12 ALA HA H 4.14 0.01 1 96 . 12 ALA HB H 1.53 0.01 1 97 . 12 ALA CB C 19.1 0.2 1 98 . 12 ALA C C 178.7 0.2 1 99 . 13 ALA H H 7.94 0.01 1 100 . 13 ALA CA C 52.3 0.2 1 101 . 13 ALA HA H 4.34 0.01 1 102 . 13 ALA HB H 1.43 0.01 1 103 . 13 ALA CB C 19.7 0.2 1 104 . 13 ALA C C 176.3 0.2 1 105 . 14 AIB H H 7.71 0.01 1 106 . 14 AIB CA C 59.0 0.2 1 107 . 14 AIB HB11 H 1.54 0.01 2 108 . 14 AIB CB1 C 28.1 0.2 1 109 . 14 AIB HB21 H 1.47 0.01 2 110 . 14 AIB CB2 C 26.1 0.2 1 111 . 14 AIB C C 176.5 0.2 1 112 . 14 AIB N N 128.7 0.2 1 113 . 15 PRO CD C 52.1 0.2 1 114 . 15 PRO HA H 4.25 0.01 1 115 . 15 PRO CB C 31.2 0.2 1 116 . 15 PRO HB2 H 2.39 0.01 2 117 . 15 PRO HB3 H 1.73 0.01 2 118 . 15 PRO CG C 28.7 0.2 1 119 . 15 PRO HG2 H 2.10 0.01 2 120 . 15 PRO HG3 H 1.95 0.01 2 121 . 15 PRO HD2 H 3.82 0.01 2 122 . 15 PRO HD3 H 3.47 0.01 2 123 . 16 AIB H H 7.90 0.01 1 124 . 16 AIB CA C 59.3 0.2 1 125 . 16 AIB HB11 H 1.45 0.01 2 126 . 16 AIB CB1 C 29.4 0.2 1 127 . 16 AIB HB21 H 1.46 0.01 2 128 . 16 AIB CB2 C 25.1 0.2 1 129 . 16 AIB C C 179.5 0.2 1 130 . 17 AIB H H 7.87 0.01 1 131 . 17 AIB CA C 59.1 0.2 1 132 . 17 AIB HB11 H 1.49 0.01 2 133 . 17 AIB CB1 C 29.4 0.2 1 134 . 17 AIB HB21 H 1.40 0.01 2 135 . 17 AIB CB2 C 25.4 0.2 1 136 . 17 AIB C C 178.9 0.2 1 137 . 18 AIB H H 7.45 0.01 1 138 . 18 AIB CA C 58.9 0.2 1 139 . 18 AIB HB11 H 1.54 0.01 2 140 . 18 AIB CB1 C 29.9 0.2 1 141 . 18 AIB HB21 H 1.52 0.01 2 142 . 18 AIB CB2 C 25.2 0.2 1 143 . 18 AIB C C 180.8 0.2 1 144 . 19 GLN H H 7.89 0.01 1 145 . 19 GLN HA H 4.18 0.01 1 146 . 19 GLN CB C 29.2 0.2 1 147 . 19 GLN HB2 H 2.23 0.01 2 148 . 19 GLN HB3 H 2.01 0.01 2 149 . 19 GLN CG C 34.3 0.2 1 150 . 19 GLN HG2 H 2.33 0.01 1 151 . 19 GLN HG3 H 2.33 0.01 1 152 . 19 GLN CD C 179.7 0.2 1 153 . 19 GLN HE21 H 6.71 0.01 2 154 . 19 GLN HE22 H 7.30 0.01 2 155 . 20 TPL H H 7.57 0.01 1 156 . 20 TPL CA C 56.2 0.2 1 157 . 20 TPL HA H 4.24 0.01 1 158 . 20 TPL CB1 C 29.5 0.2 1 159 . 20 TPL HB1 H 2.94 0.01 2 160 . 20 TPL HB2 H 2.83 0.01 2 161 . 20 TPL CG C 113.7 0.2 1 162 . 20 TPL CD1 C 126.0 0.2 1 163 . 20 TPL CD2 C 130.5 0.2 1 164 . 20 TPL CE3 C 120.5 0.2 1 165 . 20 TPL CE2 C 139.1 0.2 1 166 . 20 TPL HD1 H 7.26 0.01 1 167 . 20 TPL HE3 H 7.44 0.01 1 168 . 20 TPL CZ3 C 121.1 0.2 1 169 . 20 TPL CZ2 C 114.4 0.2 1 170 . 20 TPL HE1 H 10.47 0.01 1 171 . 20 TPL HZ3 H 6.93 0.01 1 172 . 20 TPL CH2 C 123.7 0.2 1 173 . 20 TPL HZ2 H 7.43 0.01 1 174 . 20 TPL HH2 H 7.04 0.01 1 175 . 20 TPL H2 H 3.69 0.01 2 stop_ save_