data_4833 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N assignments for the Antifungal protein from Streptomyces tendae Tu901 ; _BMRB_accession_number 4833 _BMRB_flat_file_name bmr4833.str _Entry_type original _Submission_date 2000-09-18 _Accession_date 2000-09-18 _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 Campos-Olivas Ramon . . 2 Horr Ingmar . . 3 Bormann Christiane . . 4 Jung Guenther . . 5 Gronenborn Angela . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 495 "13C chemical shifts" 376 "15N chemical shifts" 97 "coupling constants" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-11 original author . stop_ _Original_release_date 2001-07-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure, Backbone Dynamics and Chitin Binding of the Anti-fungal Protein from Streptomyces tendae Tu901 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21248995 _PubMed_ID 11350173 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Campos-Olivas Ramon . . 2 Horr Ingmar . . 3 Bormann Christiane . . 4 Jung Guenther . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 308 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 765 _Page_last 782 _Year 2001 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; Bormann C, Baier D, Horr I, Raps C, Berger J, Jung G, Schwarz H. Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity. J Bacteriol. 1999 Dec; 181(24):7421-9. ; _Citation_title 'Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10601197 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bormann C . . 2 Baier D . . 3 Horr I . . 4 Raps C . . 5 Berger J . . 6 Jung G . . 7 Schwarz H . . stop_ _Journal_abbreviation 'J. Bacteriol.' _Journal_name_full 'Journal of bacteriology' _Journal_volume 181 _Journal_issue 24 _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 7421 _Page_last 7429 _Year 1999 _Details ; The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tu901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity against Paecilomyces variotii in agar diffusion assays. The 384-bp afp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes for Streptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to cellulose-binding domains of microbial plant cell wall hydrolases and bound to crab shell chitin, chitosan, and cell walls of P. variotii but showed no enzyme activity. The biological activity of AFP1, which represents the first chitin-binding protein from bacteria exhibiting antifungal activity, was directed against specific ascomycetes, and synergistic interaction with the chitin synthetase inhibitor nikkomycin inhibited growth of Aspergillus species. Microscopy studies revealed that fluorescein-labeled AFP1 strongly bound to the surface of germinated conidia and to tips of growing hyphae, causing severe alterations in cell morphogenesis that gave rise to large spherical conidia and/or swollen hyphae and to atypical branching. ; save_ ################################## # Molecular system description # ################################## save_system_AFP-1 _Saveframe_category molecular_system _Mol_system_name 'Antifungal protein from Streptomyces tendae Tu901' _Abbreviation_common AFP-1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'AFP-1 monomer' $AFP-1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Antifungal protein' 'Chitin-binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AFP-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Antifungal protein from Streptomyces tendae Tu901' _Abbreviation_common AFP-1 _Molecular_mass 9999.2 _Mol_thiol_state 'all disulfide bound' _Details ; The mature, wild-type protein contains only residues 2-87. The N-terminal methionine included in the system studied here is a cloning artifact. ; ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; MINRTDCNENSYLEIHNNEG RDTLCFANAGTMPVAIYGVN WVESGNNVVTLQFQRNLSDP RLETITLQKWGSWNPGHIHE ILSIRIY ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 ASN 4 ARG 5 THR 6 ASP 7 CYS 8 ASN 9 GLU 10 ASN 11 SER 12 TYR 13 LEU 14 GLU 15 ILE 16 HIS 17 ASN 18 ASN 19 GLU 20 GLY 21 ARG 22 ASP 23 THR 24 LEU 25 CYS 26 PHE 27 ALA 28 ASN 29 ALA 30 GLY 31 THR 32 MET 33 PRO 34 VAL 35 ALA 36 ILE 37 TYR 38 GLY 39 VAL 40 ASN 41 TRP 42 VAL 43 GLU 44 SER 45 GLY 46 ASN 47 ASN 48 VAL 49 VAL 50 THR 51 LEU 52 GLN 53 PHE 54 GLN 55 ARG 56 ASN 57 LEU 58 SER 59 ASP 60 PRO 61 ARG 62 LEU 63 GLU 64 THR 65 ILE 66 THR 67 LEU 68 GLN 69 LYS 70 TRP 71 GLY 72 SER 73 TRP 74 ASN 75 PRO 76 GLY 77 HIS 78 ILE 79 HIS 80 GLU 81 ILE 82 LEU 83 SER 84 ILE 85 ARG 86 ILE 87 TYR stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 EMBL CAB63113 'antifungal protein [Streptomyces tendae]' 98.85 128 100.00 100.00 8.04e-46 PDB 1GH5 'Antifungal Protein From Streptomyces Tendae Tu901, Nmr Average Structure' 97.70 87 100.00 100.00 3.08e-43 PDB 1G6E 'Antifungal Protein From Streptomyces Tendae Tu901, 30- Conformers Ensemble' 97.70 87 100.00 100.00 3.08e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $AFP-1 . 1932 Eubacteria . Streptomyces tendae Tu901 afp1 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_type _Vector_name $AFP-1 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pET-11a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AFP-1 . mM 0.5 0.8 '[U-99% 15N; U-10% 13C]' phosphate 20 mM . . . NaCl 0.1 M . . . EDTA 20 uM . . . NaN3 0.01 % . . . D2O 8.3 % . . . H2O 91.7 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AFP-1 . mM 0.5 0.8 '[U-99% 15N; U-13C]' phosphate 20 mM . . . NaCl 0.1 M . . . EDTA 20 uM . . . NaN3 0.01 % . . . D2O 8.3 % . . . H2O 91.7 % . . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AFP-1 . mM 0.5 0.8 '[U-99% 15N; U-10% 13C]' phosphate 20 mM . . . NaCl 0.1 M . . . EDTA 20 uM . . . NaN3 0.01 % . . . D2O 100 % . . . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AFP-1 . mM 0.5 0.8 '[U-99% 15N; U-13C]' phosphate 20 mM . . . NaCl 0.1 M . . . EDTA 20 uM . . . NaN3 0.01 % . . . D2O 100 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 4.1.1. _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_1H-13C_HSQC/HMQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC/HMQC' _Sample_label . save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_15N-edited_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _Sample_label . save_ save_4D_13C,13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,13C NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC/HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 8.0 0.1 n/a temperature 293 0.1 K 'ionic strength' 0.32 0.01 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 H2O H 1 proton ppm 4.821 internal direct . internal . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_CS_afp1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'AFP-1 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET CA C 54.99 0.05 1 2 . 1 MET HA H 3.86 0.02 1 3 . 1 MET CB C 34.58 0.05 1 4 . 1 MET HB2 H 2.01 0.02 2 5 . 1 MET CG C 31.71 0.05 1 6 . 1 MET HG3 H 2.70 0.02 2 7 . 1 MET HG2 H 2.77 0.02 2 8 . 1 MET CE C 16.65 0.05 1 9 . 1 MET HE H 2.18 0.02 1 10 . 1 MET C C 176.82 0.05 1 11 . 2 ILE N N 125.17 0.02 1 12 . 2 ILE H H 7.19 0.02 1 13 . 2 ILE CA C 60.40 0.05 1 14 . 2 ILE HA H 4.60 0.02 1 15 . 2 ILE CB C 37.88 0.05 1 16 . 2 ILE HB H 1.51 0.02 1 17 . 2 ILE CG1 C 28.22 0.05 1 18 . 2 ILE HG12 H 0.94 0.02 2 19 . 2 ILE HG13 H 1.65 0.02 2 20 . 2 ILE CD1 C 14.71 0.05 1 21 . 2 ILE HD1 H 0.58 0.02 1 22 . 2 ILE CG2 C 15.02 0.05 1 23 . 2 ILE HG2 H 0.75 0.02 1 24 . 2 ILE C C 173.40 0.05 1 25 . 3 ASN N N 120.34 0.02 1 26 . 3 ASN H H 8.75 0.02 1 27 . 3 ASN CA C 51.60 0.05 1 28 . 3 ASN HA H 4.87 0.02 1 29 . 3 ASN CB C 41.45 0.05 1 30 . 3 ASN HB3 H 2.70 0.02 2 31 . 3 ASN HB2 H 2.77 0.02 2 32 . 3 ASN CG C 177.02 0.05 1 33 . 3 ASN ND2 N 111.87 0.02 1 34 . 3 ASN HD21 H 7.31 0.02 1 35 . 3 ASN HD22 H 6.93 0.02 1 36 . 3 ASN C C 174.34 0.05 1 37 . 4 ARG N N 122.76 0.02 1 38 . 4 ARG H H 8.53 0.02 1 39 . 4 ARG CA C 55.32 0.05 1 40 . 4 ARG HA H 4.15 0.02 1 41 . 4 ARG CB C 29.84 0.05 1 42 . 4 ARG HB3 H 1.46 0.02 2 43 . 4 ARG HB2 H 1.55 0.02 2 44 . 4 ARG CG C 26.25 0.05 1 45 . 4 ARG HG2 H 1.31 0.02 2 46 . 4 ARG CD C 42.75 0.05 1 47 . 4 ARG HD3 H 2.82 0.02 2 48 . 4 ARG HD2 H 2.87 0.02 2 49 . 4 ARG C C 175.24 0.05 1 50 . 5 THR N N 120.83 0.02 1 51 . 5 THR H H 8.12 0.02 1 52 . 5 THR CA C 58.78 0.05 1 53 . 5 THR HA H 4.50 0.02 1 54 . 5 THR CB C 70.38 0.05 1 55 . 5 THR HB H 3.51 0.02 1 56 . 5 THR CG2 C 18.68 0.05 1 57 . 5 THR HG2 H 0.16 0.02 1 58 . 5 THR C C 181.43 0.05 1 59 . 6 ASP N N 124.31 0.02 1 60 . 6 ASP H H 8.13 0.02 1 61 . 6 ASP CA C 54.63 0.05 1 62 . 6 ASP HA H 4.49 0.02 1 63 . 6 ASP CB C 40.68 0.05 1 64 . 6 ASP HB3 H 2.55 0.02 2 65 . 6 ASP HB2 H 2.60 0.02 2 66 . 7 CYS CA C 53.49 0.05 1 67 . 7 CYS HA H 4.83 0.02 1 68 . 7 CYS CB C 39.77 0.05 1 69 . 7 CYS HB3 H 2.85 0.02 2 70 . 7 CYS HB2 H 3.32 0.02 2 71 . 7 CYS C C 175.23 0.05 1 72 . 8 ASN N N 120.14 0.02 1 73 . 8 ASN H H 8.48 0.02 1 74 . 8 ASN CA C 52.78 0.05 1 75 . 8 ASN HA H 4.73 0.02 1 76 . 8 ASN CB C 38.13 0.05 1 77 . 8 ASN HB3 H 2.83 0.02 2 78 . 8 ASN HB2 H 3.08 0.02 2 79 . 8 ASN CG C 176.52 0.05 1 80 . 8 ASN ND2 N 111.94 0.02 1 81 . 8 ASN HD21 H 7.65 0.02 1 82 . 8 ASN HD22 H 7.04 0.02 1 83 . 8 ASN C C 174.34 0.05 1 84 . 9 GLU N N 116.64 0.02 1 85 . 9 GLU H H 7.67 0.02 1 86 . 9 GLU CA C 55.24 0.05 1 87 . 9 GLU HA H 4.50 0.02 1 88 . 9 GLU CB C 31.63 0.05 1 89 . 9 GLU HB3 H 1.26 0.02 2 90 . 9 GLU HB2 H 1.91 0.02 2 91 . 9 GLU CG C 35.70 0.05 1 92 . 9 GLU HG3 H 2.13 0.02 2 93 . 9 GLU HG2 H 2.18 0.02 2 94 . 10 ASN CA C 53.47 0.05 1 95 . 10 ASN HA H 4.82 0.02 1 96 . 10 ASN CB C 38.53 0.05 1 97 . 10 ASN HB3 H 2.78 0.02 2 98 . 10 ASN HB2 H 2.91 0.02 2 99 . 10 ASN ND2 N 115.24 0.02 1 100 . 10 ASN HD21 H 8.09 0.02 1 101 . 10 ASN HD22 H 7.18 0.02 1 102 . 11 SER CA C 57.78 0.05 1 103 . 11 SER HA H 4.58 0.02 1 104 . 11 SER CB C 63.24 0.05 1 105 . 11 SER HB3 H 3.98 0.02 2 106 . 11 SER HB2 H 4.09 0.02 2 107 . 11 SER C C 175.23 0.05 1 108 . 12 TYR N N 123.64 0.02 1 109 . 12 TYR H H 8.14 0.02 1 110 . 12 TYR CA C 55.10 0.05 1 111 . 12 TYR HA H 4.99 0.02 1 112 . 12 TYR CB C 37.08 0.05 1 113 . 12 TYR HB2 H 2.96 0.02 1 114 . 12 TYR HB3 H 3.38 0.02 1 115 . 12 TYR CD1 C 131.64 0.05 3 116 . 12 TYR HD1 H 7.22 0.02 3 117 . 12 TYR CE1 C 118.75 0.05 3 118 . 12 TYR HE1 H 6.99 0.02 3 119 . 12 TYR C C 175.32 0.05 1 120 . 13 LEU N N 119.81 0.02 1 121 . 13 LEU H H 7.39 0.02 1 122 . 13 LEU CA C 55.33 0.05 1 123 . 13 LEU HA H 4.67 0.02 1 124 . 13 LEU CB C 41.42 0.05 1 125 . 13 LEU HB3 H 1.28 0.02 2 126 . 13 LEU HB2 H 1.92 0.02 2 127 . 13 LEU CG C 28.08 0.05 1 128 . 13 LEU HG H 0.77 0.02 1 129 . 13 LEU CD1 C 25.28 0.05 1 130 . 13 LEU HD1 H 0.93 0.02 1 131 . 13 LEU CD2 C 28.00 0.05 1 132 . 13 LEU HD2 H 0.73 0.02 1 133 . 13 LEU C C 175.15 0.05 1 134 . 14 GLU N N 126.91 0.02 1 135 . 14 GLU H H 9.37 0.02 1 136 . 14 GLU CA C 54.11 0.05 1 137 . 14 GLU HA H 5.16 0.02 1 138 . 14 GLU CB C 33.39 0.05 1 139 . 14 GLU HB3 H 1.64 0.02 1 140 . 14 GLU HB2 H 2.08 0.02 1 141 . 14 GLU CG C 35.20 0.05 1 142 . 14 GLU HG3 H 2.30 0.02 2 143 . 14 GLU HG2 H 2.50 0.02 2 144 . 14 GLU C C 174.89 0.05 1 145 . 15 ILE N N 124.01 0.02 1 146 . 15 ILE H H 9.50 0.02 1 147 . 15 ILE CA C 60.48 0.05 1 148 . 15 ILE HA H 4.32 0.02 1 149 . 15 ILE CB C 39.20 0.05 1 150 . 15 ILE HB H 1.99 0.02 1 151 . 15 ILE CG1 C 27.98 0.05 1 152 . 15 ILE HG12 H 1.16 0.02 2 153 . 15 ILE HG13 H 1.61 0.02 2 154 . 15 ILE CD1 C 13.36 0.05 1 155 . 15 ILE HD1 H 0.69 0.02 1 156 . 15 ILE CG2 C 19.37 0.05 1 157 . 15 ILE HG2 H 0.81 0.02 1 158 . 15 ILE C C 173.70 0.05 1 159 . 16 HIS N N 127.19 0.02 1 160 . 16 HIS H H 8.68 0.02 1 161 . 16 HIS CA C 53.77 0.05 1 162 . 16 HIS HA H 5.36 0.02 1 163 . 16 HIS CB C 29.24 0.05 1 164 . 16 HIS HB3 H 2.29 0.02 2 165 . 16 HIS HB2 H 2.08 0.02 2 166 . 16 HIS HD2 H 6.18 0.02 1 167 . 16 HIS HE1 H 7.27 0.02 1 168 . 16 HIS C C 174.01 0.05 1 169 . 17 ASN N N 125.64 0.02 1 170 . 17 ASN H H 8.94 0.02 1 171 . 17 ASN CA C 51.30 0.05 1 172 . 17 ASN HA H 5.28 0.02 1 173 . 17 ASN CB C 40.52 0.05 1 174 . 17 ASN HB3 H 2.14 0.02 1 175 . 17 ASN HB2 H 3.16 0.02 1 176 . 17 ASN ND2 N 106.34 0.02 1 177 . 17 ASN HD21 H 7.15 0.02 1 178 . 17 ASN HD22 H 6.18 0.02 1 179 . 17 ASN C C 173.82 0.05 1 180 . 18 ASN N N 115.11 0.02 1 181 . 18 ASN H H 8.14 0.02 1 182 . 18 ASN CA C 52.95 0.05 1 183 . 18 ASN HA H 4.45 0.02 1 184 . 18 ASN CB C 35.86 0.05 1 185 . 18 ASN HB3 H 2.50 0.02 2 186 . 18 ASN HB2 H 3.31 0.02 2 187 . 18 ASN CG C 178.28 0.05 1 188 . 18 ASN ND2 N 112.02 0.02 1 189 . 18 ASN HD21 H 8.06 0.02 1 190 . 18 ASN HD22 H 6.85 0.02 1 191 . 18 ASN C C 175.54 0.05 1 192 . 19 GLU N N 119.71 0.02 1 193 . 19 GLU H H 9.84 0.02 1 194 . 19 GLU CA C 56.28 0.05 1 195 . 19 GLU HA H 3.93 0.02 1 196 . 19 GLU CB C 26.81 0.05 1 197 . 19 GLU HB2 H 2.15 0.02 2 198 . 19 GLU CG C 36.46 0.05 1 199 . 19 GLU HG3 H 2.23 0.02 2 200 . 19 GLU HG2 H 2.30 0.02 2 201 . 19 GLU C C 176.75 0.05 1 202 . 20 GLY N N 106.23 0.02 1 203 . 20 GLY H H 8.09 0.02 1 204 . 20 GLY CA C 45.77 0.05 1 205 . 20 GLY HA2 H 3.43 0.02 1 206 . 20 GLY HA3 H 4.28 0.02 1 207 . 20 GLY C C 175.17 0.05 1 208 . 21 ARG N N 120.29 0.02 1 209 . 21 ARG H H 8.02 0.02 1 210 . 21 ARG CA C 58.23 0.05 1 211 . 21 ARG HA H 4.28 0.02 1 212 . 21 ARG CB C 31.62 0.05 1 213 . 21 ARG HB3 H 1.90 0.02 2 214 . 21 ARG HB2 H 2.09 0.02 2 215 . 21 ARG CG C 27.72 0.05 1 216 . 21 ARG HG3 H 1.71 0.02 2 217 . 21 ARG HG2 H 1.88 0.02 2 218 . 21 ARG CD C 43.28 0.05 1 219 . 21 ARG HD3 H 3.26 0.02 2 220 . 21 ARG HD2 H 3.34 0.02 2 221 . 21 ARG C C 176.50 0.05 1 222 . 22 ASP N N 117.89 0.02 1 223 . 22 ASP H H 8.14 0.02 1 224 . 22 ASP CA C 53.33 0.05 1 225 . 22 ASP HA H 5.20 0.02 1 226 . 22 ASP CB C 43.47 0.05 1 227 . 22 ASP HB3 H 2.56 0.02 1 228 . 22 ASP HB2 H 2.79 0.02 1 229 . 22 ASP C C 175.20 0.05 1 230 . 23 THR N N 114.36 0.02 1 231 . 23 THR H H 8.34 0.02 1 232 . 23 THR CA C 61.52 0.05 1 233 . 23 THR HA H 4.58 0.02 1 234 . 23 THR CB C 70.45 0.05 1 235 . 23 THR HB H 3.75 0.02 1 236 . 23 THR CG2 C 22.17 0.05 1 237 . 23 THR HG2 H 0.53 0.02 1 238 . 23 THR C C 181.58 0.05 1 239 . 24 LEU N N 128.77 0.02 1 240 . 24 LEU H H 9.14 0.02 1 241 . 24 LEU CA C 54.34 0.05 1 242 . 24 LEU HA H 4.52 0.02 1 243 . 24 LEU CB C 44.98 0.05 1 244 . 24 LEU HB3 H 1.38 0.02 1 245 . 24 LEU HB2 H 1.61 0.02 1 246 . 24 LEU CG C 28.06 0.05 1 247 . 24 LEU HG H 1.56 0.02 1 248 . 24 LEU CD1 C 25.73 0.05 1 249 . 24 LEU HD1 H 0.81 0.02 1 250 . 24 LEU CD2 C 25.26 0.05 1 251 . 24 LEU HD2 H 0.86 0.02 1 252 . 24 LEU C C 174.76 0.05 1 253 . 25 CYS N N 118.95 0.02 1 254 . 25 CYS H H 8.49 0.02 1 255 . 25 CYS CA C 56.51 0.05 1 256 . 25 CYS HA H 5.91 0.02 1 257 . 25 CYS CB C 48.44 0.05 1 258 . 25 CYS HB2 H 2.76 0.02 1 259 . 25 CYS HB3 H 3.04 0.02 1 260 . 25 CYS C C 172.69 0.05 1 261 . 26 PHE N N 117.61 0.02 1 262 . 26 PHE H H 8.54 0.02 1 263 . 26 PHE CA C 56.19 0.05 1 264 . 26 PHE HA H 4.95 0.02 1 265 . 26 PHE CB C 44.33 0.05 1 266 . 26 PHE HB2 H 2.51 0.02 1 267 . 26 PHE HB3 H 2.68 0.02 1 268 . 26 PHE CD1 C 131.37 0.05 3 269 . 26 PHE HD1 H 6.75 0.02 3 270 . 26 PHE CE1 C 131.02 0.05 3 271 . 26 PHE HE1 H 6.96 0.02 3 272 . 26 PHE CZ C 128.89 0.05 1 273 . 26 PHE HZ H 7.04 0.02 1 274 . 26 PHE C C 172.69 0.05 1 275 . 27 ALA N N 120.01 0.02 1 276 . 27 ALA H H 8.29 0.02 1 277 . 27 ALA CA C 51.31 0.05 1 278 . 27 ALA HA H 4.54 0.02 1 279 . 27 ALA CB C 24.02 0.05 1 280 . 27 ALA HB H 1.11 0.02 1 281 . 27 ALA C C 175.50 0.05 1 282 . 28 ASN N N 110.42 0.02 1 283 . 28 ASN H H 8.45 0.02 1 284 . 28 ASN CA C 54.97 0.05 1 285 . 28 ASN HA H 4.19 0.02 1 286 . 28 ASN CB C 37.50 0.05 1 287 . 28 ASN HB3 H 2.61 0.02 1 288 . 28 ASN HB2 H 3.55 0.02 1 289 . 28 ASN ND2 N 112.88 0.02 1 290 . 28 ASN HD21 H 7.16 0.02 1 291 . 28 ASN HD22 H 6.95 0.02 1 292 . 28 ASN C C 180.77 0.05 1 293 . 29 ALA N N 116.18 0.02 1 294 . 29 ALA H H 7.56 0.02 1 295 . 29 ALA CA C 52.07 0.05 1 296 . 29 ALA HA H 4.02 0.02 1 297 . 29 ALA CB C 19.52 0.05 1 298 . 29 ALA HB H 1.26 0.02 1 299 . 29 ALA C C 178.46 0.05 1 300 . 30 GLY N N 108.58 0.02 1 301 . 30 GLY H H 8.79 0.02 1 302 . 30 GLY CA C 44.11 0.05 1 303 . 30 GLY HA3 H 3.79 0.02 1 304 . 30 GLY HA2 H 4.50 0.02 1 305 . 30 GLY C C 173.21 0.05 1 306 . 31 THR N N 114.59 0.02 1 307 . 31 THR H H 8.52 0.02 1 308 . 31 THR CA C 60.84 0.05 1 309 . 31 THR HA H 5.38 0.02 1 310 . 31 THR CB C 70.47 0.05 1 311 . 31 THR HB H 3.75 0.02 1 312 . 31 THR CG2 C 20.34 0.05 1 313 . 31 THR HG2 H 0.95 0.02 1 314 . 31 THR C C 172.99 0.05 1 315 . 32 MET N N 126.09 0.02 1 316 . 32 MET H H 9.22 0.02 1 317 . 32 MET CA C 52.45 0.05 1 318 . 32 MET HA H 5.02 0.02 1 319 . 32 MET CB C 36.24 0.05 1 320 . 32 MET HB3 H 1.82 0.02 1 321 . 32 MET HB2 H 1.94 0.02 1 322 . 32 MET CG C 30.37 0.05 1 323 . 32 MET HG3 H 2.28 0.02 2 324 . 32 MET HG2 H 2.36 0.02 2 325 . 32 MET CE C 17.30 0.05 1 326 . 32 MET HE H 2.11 0.02 1 327 . 33 PRO CA C 61.85 0.05 1 328 . 33 PRO HA H 4.86 0.02 1 329 . 33 PRO CB C 31.62 0.05 1 330 . 33 PRO HB3 H 1.95 0.02 2 331 . 33 PRO HB2 H 2.31 0.02 2 332 . 33 PRO CG C 26.77 0.05 1 333 . 33 PRO HG3 H 1.99 0.02 2 334 . 33 PRO HG2 H 2.15 0.02 2 335 . 33 PRO CD C 51.03 0.05 1 336 . 33 PRO HD3 H 3.71 0.02 2 337 . 33 PRO HD2 H 3.79 0.02 2 338 . 33 PRO C C 176.23 0.05 1 339 . 34 VAL N N 115.35 0.02 1 340 . 34 VAL H H 7.88 0.02 1 341 . 34 VAL CA C 59.27 0.05 1 342 . 34 VAL HA H 4.49 0.02 1 343 . 34 VAL CB C 37.03 0.05 1 344 . 34 VAL HB H 2.02 0.02 1 345 . 34 VAL CG2 C 17.62 0.05 1 346 . 34 VAL HG2 H 0.35 0.02 1 347 . 34 VAL CG1 C 22.89 0.05 1 348 . 34 VAL HG1 H 0.68 0.02 1 349 . 34 VAL C C 172.95 0.05 1 350 . 35 ALA N N 122.84 0.02 1 351 . 35 ALA H H 8.08 0.02 1 352 . 35 ALA CA C 51.70 0.05 1 353 . 35 ALA HA H 4.67 0.02 1 354 . 35 ALA CB C 18.79 0.05 1 355 . 35 ALA HB H 1.17 0.02 1 356 . 35 ALA C C 175.11 0.05 1 357 . 36 ILE N N 121.46 0.02 1 358 . 36 ILE H H 7.51 0.02 1 359 . 36 ILE CA C 60.06 0.05 1 360 . 36 ILE HA H 4.13 0.02 1 361 . 36 ILE CB C 40.57 0.05 1 362 . 36 ILE HB H 1.31 0.02 1 363 . 36 ILE CG1 C 26.27 0.05 1 364 . 36 ILE HG12 H 0.94 0.02 2 365 . 36 ILE HG13 H 1.44 0.02 2 366 . 36 ILE CD1 C 15.32 0.05 1 367 . 36 ILE HD1 H 0.77 0.02 1 368 . 36 ILE CG2 C 18.42 0.05 1 369 . 36 ILE HG2 H 0.68 0.02 1 370 . 36 ILE C C 174.51 0.05 1 371 . 37 TYR N N 126.17 0.02 1 372 . 37 TYR H H 8.89 0.02 1 373 . 37 TYR CA C 57.04 0.05 1 374 . 37 TYR HA H 5.32 0.02 1 375 . 37 TYR CB C 40.12 0.05 1 376 . 37 TYR HB2 H 2.73 0.02 1 377 . 37 TYR HB3 H 3.15 0.02 1 378 . 37 TYR CD1 C 132.98 0.05 3 379 . 37 TYR HD1 H 6.93 0.02 3 380 . 37 TYR CE1 C 117.79 0.05 3 381 . 37 TYR HE1 H 6.60 0.02 3 382 . 37 TYR C C 178.50 0.05 1 383 . 38 GLY N N 113.83 0.02 1 384 . 38 GLY H H 8.46 0.02 1 385 . 38 GLY CA C 48.18 0.05 1 386 . 38 GLY HA2 H 3.58 0.02 1 387 . 38 GLY HA3 H 3.68 0.02 1 388 . 38 GLY C C 175.54 0.05 1 389 . 39 VAL N N 120.04 0.02 1 390 . 39 VAL H H 7.54 0.02 1 391 . 39 VAL CA C 63.25 0.05 1 392 . 39 VAL HA H 3.49 0.02 1 393 . 39 VAL CB C 32.86 0.05 1 394 . 39 VAL HB H 1.43 0.02 1 395 . 39 VAL CG2 C 20.58 0.05 1 396 . 39 VAL HG2 H 0.61 0.02 1 397 . 39 VAL CG1 C 23.45 0.05 1 398 . 39 VAL HG1 H 0.63 0.02 1 399 . 39 VAL C C 173.81 0.05 1 400 . 40 ASN N N 122.51 0.02 1 401 . 40 ASN H H 9.14 0.02 1 402 . 40 ASN CA C 54.70 0.05 1 403 . 40 ASN HA H 4.83 0.02 1 404 . 40 ASN CB C 43.31 0.05 1 405 . 40 ASN HB3 H 3.20 0.02 2 406 . 40 ASN HB2 H 3.25 0.02 2 407 . 40 ASN CG C 174.97 0.05 1 408 . 40 ASN ND2 N 105.18 0.02 1 409 . 40 ASN HD21 H 7.51 0.02 1 410 . 40 ASN HD22 H 6.87 0.02 1 411 . 40 ASN C C 173.99 0.05 1 412 . 41 TRP N N 113.70 0.02 1 413 . 41 TRP H H 7.43 0.02 1 414 . 41 TRP CA C 57.80 0.05 1 415 . 41 TRP HA H 5.08 0.02 1 416 . 41 TRP CB C 30.40 0.05 1 417 . 41 TRP HB3 H 3.36 0.02 2 418 . 41 TRP HB2 H 3.45 0.02 2 419 . 41 TRP CD1 C 126.84 0.05 1 420 . 41 TRP HD1 H 6.88 0.02 1 421 . 41 TRP NE1 N 131.01 0.02 1 422 . 41 TRP HE1 H 10.28 0.02 1 423 . 41 TRP CZ2 C 113.93 0.05 1 424 . 41 TRP HZ2 H 7.02 0.02 1 425 . 41 TRP CH2 C 124.23 0.05 1 426 . 41 TRP HH2 H 7.12 0.02 1 427 . 41 TRP CZ3 C 120.99 0.05 1 428 . 41 TRP HZ3 H 6.99 0.02 1 429 . 41 TRP C C 181.56 0.05 1 430 . 42 VAL N N 120.78 0.02 1 431 . 42 VAL H H 9.10 0.02 1 432 . 42 VAL CA C 60.43 0.05 1 433 . 42 VAL HA H 5.15 0.02 1 434 . 42 VAL CB C 37.49 0.05 1 435 . 42 VAL HB H 2.21 0.02 1 436 . 42 VAL CG2 C 22.51 0.05 1 437 . 42 VAL HG2 H 1.02 0.02 1 438 . 42 VAL CG1 C 22.00 0.05 1 439 . 42 VAL HG1 H 0.94 0.02 1 440 . 42 VAL C C 174.07 0.05 1 441 . 43 GLU N N 125.40 0.02 1 442 . 43 GLU H H 9.09 0.02 1 443 . 43 GLU CA C 54.46 0.05 1 444 . 43 GLU HA H 5.43 0.02 1 445 . 43 GLU CB C 32.26 0.05 1 446 . 43 GLU HB2 H 2.10 0.02 1 447 . 43 GLU HB3 H 2.61 0.02 1 448 . 43 GLU CG C 36.23 0.05 1 449 . 43 GLU HG3 H 2.52 0.02 2 450 . 43 GLU HG2 H 2.61 0.02 2 451 . 43 GLU C C 175.53 0.05 1 452 . 44 SER N N 116.93 0.02 1 453 . 44 SER H H 8.66 0.02 1 454 . 44 SER CA C 59.80 0.05 1 455 . 44 SER HA H 4.14 0.02 1 456 . 44 SER CB C 63.78 0.05 1 457 . 44 SER HB2 H 3.67 0.02 1 458 . 44 SER HB3 H 4.22 0.02 1 459 . 44 SER C C 174.78 0.05 1 460 . 45 GLY N N 110.12 0.02 1 461 . 45 GLY H H 9.12 0.02 1 462 . 45 GLY CA C 45.11 0.05 1 463 . 45 GLY HA2 H 3.24 0.02 2 464 . 45 GLY HA3 H 3.29 0.02 2 465 . 45 GLY C C 174.71 0.05 1 466 . 46 ASN N N 124.51 0.02 1 467 . 46 ASN H H 8.16 0.02 1 468 . 46 ASN CA C 50.88 0.05 1 469 . 46 ASN HA H 3.94 0.02 1 470 . 46 ASN CB C 36.86 0.05 1 471 . 46 ASN HB3 H 2.45 0.02 2 472 . 46 ASN HB2 H 2.86 0.02 2 473 . 46 ASN ND2 N 109.93 0.02 1 474 . 46 ASN HD21 H 7.68 0.02 1 475 . 46 ASN HD22 H 6.93 0.02 1 476 . 46 ASN C C 174.90 0.05 1 477 . 47 ASN N N 115.55 0.02 1 478 . 47 ASN H H 7.50 0.02 1 479 . 47 ASN CA C 52.59 0.05 1 480 . 47 ASN HA H 4.82 0.02 1 481 . 47 ASN CB C 43.07 0.05 1 482 . 47 ASN HB2 H 2.24 0.02 1 483 . 47 ASN HB3 H 2.63 0.02 1 484 . 47 ASN CG C 175.95 0.05 1 485 . 47 ASN ND2 N 116.47 0.02 1 486 . 47 ASN HD21 H 7.91 0.02 1 487 . 47 ASN HD22 H 6.86 0.02 1 488 . 47 ASN C C 180.47 0.05 1 489 . 48 VAL N N 121.91 0.02 1 490 . 48 VAL H H 8.51 0.02 1 491 . 48 VAL CA C 61.62 0.05 1 492 . 48 VAL HA H 4.47 0.02 1 493 . 48 VAL CB C 31.73 0.05 1 494 . 48 VAL HB H 1.78 0.02 1 495 . 48 VAL CG2 C 22.52 0.05 1 496 . 48 VAL HG2 H 0.89 0.02 1 497 . 48 VAL CG1 C 20.50 0.05 1 498 . 48 VAL HG1 H 0.57 0.02 1 499 . 48 VAL C C 176.28 0.05 1 500 . 49 VAL N N 123.69 0.02 1 501 . 49 VAL H H 8.57 0.02 1 502 . 49 VAL CA C 58.79 0.05 1 503 . 49 VAL HA H 5.73 0.02 1 504 . 49 VAL CB C 37.09 0.05 1 505 . 49 VAL HB H 1.80 0.02 1 506 . 49 VAL CG2 C 22.02 0.05 1 507 . 49 VAL HG2 H 0.85 0.02 1 508 . 49 VAL CG1 C 21.59 0.05 1 509 . 49 VAL HG1 H 0.84 0.02 1 510 . 49 VAL C C 174.72 0.05 1 511 . 50 THR N N 122.29 0.02 1 512 . 50 THR H H 9.50 0.02 1 513 . 50 THR CA C 61.49 0.05 1 514 . 50 THR HA H 5.57 0.02 1 515 . 50 THR CB C 71.65 0.05 1 516 . 50 THR HB H 3.70 0.02 1 517 . 50 THR CG2 C 22.29 0.05 1 518 . 50 THR HG2 H 1.10 0.02 1 519 . 50 THR C C 173.75 0.05 1 520 . 51 LEU N N 127.36 0.02 1 521 . 51 LEU H H 9.19 0.02 1 522 . 51 LEU CA C 52.60 0.05 1 523 . 51 LEU HA H 5.22 0.02 1 524 . 51 LEU CB C 44.21 0.05 1 525 . 51 LEU HB3 H 1.35 0.02 1 526 . 51 LEU HB2 H 1.76 0.02 1 527 . 51 LEU CG C 27.05 0.05 1 528 . 51 LEU HG H 1.55 0.02 1 529 . 51 LEU CD1 C 26.66 0.05 1 530 . 51 LEU HD1 H 0.83 0.02 1 531 . 51 LEU CD2 C 25.73 0.05 1 532 . 51 LEU HD2 H 0.83 0.02 1 533 . 51 LEU C C 174.87 0.05 1 534 . 52 GLN N N 120.92 0.02 1 535 . 52 GLN H H 8.13 0.02 1 536 . 52 GLN CA C 53.99 0.05 1 537 . 52 GLN HA H 5.48 0.02 1 538 . 52 GLN CB C 31.25 0.05 1 539 . 52 GLN HB2 H 1.78 0.02 1 540 . 52 GLN HB3 H 2.11 0.02 1 541 . 52 GLN CG C 34.20 0.05 1 542 . 52 GLN HG3 H 2.01 0.02 2 543 . 52 GLN HG2 H 2.25 0.02 2 544 . 52 GLN CD C 178.78 0.05 1 545 . 52 GLN NE2 N 111.92 0.02 1 546 . 52 GLN HE21 H 7.20 0.02 1 547 . 52 GLN HE22 H 6.78 0.02 1 548 . 52 GLN C C 175.52 0.05 1 549 . 53 PHE N N 122.62 0.02 1 550 . 53 PHE H H 9.27 0.02 1 551 . 53 PHE CA C 55.41 0.05 1 552 . 53 PHE HA H 5.46 0.02 1 553 . 53 PHE CB C 43.53 0.05 1 554 . 53 PHE HB3 H 2.81 0.02 1 555 . 53 PHE HB2 H 3.13 0.02 1 556 . 53 PHE CD1 C 132.50 0.05 3 557 . 53 PHE HD1 H 6.74 0.02 3 558 . 53 PHE CE1 C 131.49 0.05 3 559 . 53 PHE HE1 H 6.95 0.02 3 560 . 53 PHE CZ C 130.79 0.05 1 561 . 53 PHE HZ H 7.26 0.02 1 562 . 53 PHE C C 179.06 0.05 1 563 . 54 GLN N N 121.16 0.02 1 564 . 54 GLN H H 9.45 0.02 1 565 . 54 GLN CA C 53.85 0.05 1 566 . 54 GLN HA H 4.82 0.02 1 567 . 54 GLN CB C 30.26 0.05 1 568 . 54 GLN HB3 H 1.97 0.02 2 569 . 54 GLN HB2 H 2.09 0.02 2 570 . 54 GLN CG C 33.39 0.05 1 571 . 54 GLN HG3 H 2.32 0.02 2 572 . 54 GLN HG2 H 2.62 0.02 2 573 . 54 GLN CD C 179.09 0.05 1 574 . 54 GLN NE2 N 112.65 0.02 1 575 . 54 GLN HE21 H 7.37 0.02 1 576 . 54 GLN HE22 H 6.72 0.02 1 577 . 54 GLN C C 174.90 0.05 1 578 . 55 ARG N N 129.96 0.02 1 579 . 55 ARG H H 10.21 0.02 1 580 . 55 ARG CA C 61.32 0.05 1 581 . 55 ARG HA H 4.26 0.02 1 582 . 55 ARG CB C 32.40 0.05 1 583 . 55 ARG HB3 H 2.06 0.02 2 584 . 55 ARG HB2 H 2.38 0.02 2 585 . 55 ARG CG C 27.95 0.05 1 586 . 55 ARG HG2 H 1.79 0.02 2 587 . 55 ARG CD C 43.26 0.05 1 588 . 55 ARG HD3 H 3.29 0.02 2 589 . 55 ARG HD2 H 3.79 0.02 2 590 . 55 ARG NE N 82.88 0.02 1 591 . 55 ARG HE H 8.87 0.02 1 592 . 55 ARG C C 176.83 0.05 1 593 . 56 ASN N N 117.56 0.02 1 594 . 56 ASN H H 9.94 0.02 1 595 . 56 ASN CA C 51.83 0.05 1 596 . 56 ASN HA H 5.32 0.02 1 597 . 56 ASN CB C 42.49 0.05 1 598 . 56 ASN HB2 H 2.76 0.02 1 599 . 56 ASN HB3 H 2.87 0.02 1 600 . 56 ASN ND2 N 111.86 0.02 1 601 . 56 ASN HD21 H 7.64 0.02 1 602 . 56 ASN HD22 H 6.89 0.02 1 603 . 56 ASN C C 174.75 0.05 1 604 . 57 LEU N N 126.20 0.02 1 605 . 57 LEU H H 9.00 0.02 1 606 . 57 LEU CA C 57.92 0.05 1 607 . 57 LEU HA H 3.22 0.02 1 608 . 57 LEU CB C 41.67 0.05 1 609 . 57 LEU HB3 H 1.16 0.02 2 610 . 57 LEU HB2 H 1.38 0.02 2 611 . 57 LEU CG C 26.53 0.05 1 612 . 57 LEU HG H 1.24 0.02 1 613 . 57 LEU CD1 C 23.76 0.05 1 614 . 57 LEU HD1 H 0.72 0.02 1 615 . 57 LEU CD2 C 25.00 0.05 1 616 . 57 LEU HD2 H 0.76 0.02 1 617 . 57 LEU C C 176.83 0.05 1 618 . 58 SER N N 110.06 0.02 1 619 . 58 SER H H 8.23 0.02 1 620 . 58 SER CA C 59.13 0.05 1 621 . 58 SER HA H 4.16 0.02 1 622 . 58 SER CB C 63.23 0.05 1 623 . 58 SER HB3 H 3.85 0.02 2 624 . 58 SER HB2 H 3.97 0.02 2 625 . 58 SER C C 173.01 0.05 1 626 . 59 ASP N N 121.09 0.02 1 627 . 59 ASP H H 7.32 0.02 1 628 . 59 ASP CA C 49.97 0.05 1 629 . 59 ASP HA H 5.25 0.02 1 630 . 59 ASP CB C 42.86 0.05 1 631 . 59 ASP HB3 H 2.56 0.02 2 632 . 59 ASP HB2 H 3.15 0.02 2 633 . 60 PRO CA C 62.74 0.05 1 634 . 60 PRO HA H 4.40 0.02 1 635 . 60 PRO CB C 31.64 0.05 1 636 . 60 PRO HB3 H 2.11 0.02 2 637 . 60 PRO HB2 H 2.17 0.02 2 638 . 60 PRO CG C 26.30 0.05 1 639 . 60 PRO HG3 H 1.90 0.02 2 640 . 60 PRO HG2 H 2.02 0.02 2 641 . 60 PRO CD C 50.66 0.05 1 642 . 60 PRO HD3 H 3.71 0.02 2 643 . 60 PRO HD2 H 3.97 0.02 2 644 . 60 PRO C C 175.98 0.05 1 645 . 61 ARG N N 122.39 0.02 1 646 . 61 ARG H H 7.92 0.02 1 647 . 61 ARG CA C 56.92 0.05 1 648 . 61 ARG HA H 4.10 0.02 1 649 . 61 ARG CB C 30.59 0.05 1 650 . 61 ARG HB3 H 1.72 0.02 2 651 . 61 ARG HB2 H 1.89 0.02 2 652 . 61 ARG CG C 26.81 0.05 1 653 . 61 ARG HG3 H 1.57 0.02 2 654 . 61 ARG HG2 H 1.63 0.02 2 655 . 61 ARG CD C 43.30 0.05 1 656 . 61 ARG HD3 H 3.23 0.02 2 657 . 61 ARG C C 175.06 0.05 1 658 . 62 LEU N N 124.38 0.02 1 659 . 62 LEU H H 8.38 0.02 1 660 . 62 LEU CA C 53.44 0.05 1 661 . 62 LEU HA H 4.77 0.02 1 662 . 62 LEU CB C 43.04 0.05 1 663 . 62 LEU HB3 H 1.15 0.02 2 664 . 62 LEU HB2 H 1.67 0.02 2 665 . 62 LEU CG C 26.65 0.05 1 666 . 62 LEU HG H 1.71 0.02 1 667 . 62 LEU CD1 C 25.25 0.05 1 668 . 62 LEU HD1 H 0.78 0.02 1 669 . 62 LEU CD2 C 23.53 0.05 1 670 . 62 LEU HD2 H 0.72 0.02 1 671 . 62 LEU C C 176.96 0.05 1 672 . 63 GLU N N 123.20 0.02 1 673 . 63 GLU H H 8.76 0.02 1 674 . 63 GLU CA C 54.28 0.05 1 675 . 63 GLU HA H 4.42 0.02 1 676 . 63 GLU CB C 36.45 0.05 1 677 . 63 GLU HB2 H 0.64 0.02 1 678 . 63 GLU HB3 H 1.68 0.02 1 679 . 63 GLU CG C 38.11 0.05 1 680 . 63 GLU HG3 H 1.78 0.02 2 681 . 63 GLU HG2 H 2.15 0.02 2 682 . 63 GLU C C 173.61 0.05 1 683 . 64 THR N N 109.89 0.02 1 684 . 64 THR H H 8.17 0.02 1 685 . 64 THR CA C 59.28 0.05 1 686 . 64 THR HA H 5.60 0.02 1 687 . 64 THR CB C 71.89 0.05 1 688 . 64 THR HB H 3.85 0.02 1 689 . 64 THR CG2 C 20.79 0.05 1 690 . 64 THR HG2 H 1.03 0.02 1 691 . 64 THR C C 173.70 0.05 1 692 . 65 ILE N N 121.86 0.02 1 693 . 65 ILE H H 8.65 0.02 1 694 . 65 ILE CA C 59.82 0.05 1 695 . 65 ILE HA H 4.50 0.02 1 696 . 65 ILE CB C 41.69 0.05 1 697 . 65 ILE HB H 1.34 0.02 1 698 . 65 ILE CG1 C 28.72 0.05 1 699 . 65 ILE HG12 H 0.32 0.02 2 700 . 65 ILE HG13 H 1.21 0.02 2 701 . 65 ILE CD1 C 12.73 0.05 1 702 . 65 ILE HD1 H -0.04 0.02 1 703 . 65 ILE CG2 C 15.36 0.05 1 704 . 65 ILE HG2 H -0.18 0.02 1 705 . 65 ILE C C 180.82 0.05 1 706 . 66 THR N N 123.54 0.02 1 707 . 66 THR H H 8.36 0.02 1 708 . 66 THR CA C 60.68 0.05 1 709 . 66 THR HA H 5.62 0.02 1 710 . 66 THR CB C 70.73 0.05 1 711 . 66 THR HB H 3.77 0.02 1 712 . 66 THR CG2 C 20.04 0.05 1 713 . 66 THR HG2 H 0.89 0.02 1 714 . 66 THR C C 173.37 0.05 1 715 . 67 LEU N N 129.84 0.02 1 716 . 67 LEU H H 9.66 0.02 1 717 . 67 LEU CA C 53.47 0.05 1 718 . 67 LEU HA H 4.60 0.02 1 719 . 67 LEU CB C 44.06 0.05 1 720 . 67 LEU HB3 H 1.59 0.02 2 721 . 67 LEU HB2 H 1.65 0.02 2 722 . 67 LEU CG C 27.81 0.05 1 723 . 67 LEU HG H 1.44 0.02 1 724 . 67 LEU CD1 C 25.32 0.05 1 725 . 67 LEU HD1 H 0.66 0.02 1 726 . 67 LEU CD2 C 24.41 0.05 1 727 . 67 LEU HD2 H 0.72 0.02 1 728 . 67 LEU C C 175.29 0.05 1 729 . 68 GLN N N 117.63 0.02 1 730 . 68 GLN H H 8.22 0.02 1 731 . 68 GLN CA C 53.29 0.05 1 732 . 68 GLN HA H 4.25 0.02 1 733 . 68 GLN CB C 28.20 0.05 1 734 . 68 GLN HB2 H 1.86 0.02 1 735 . 68 GLN HB3 H 2.38 0.02 1 736 . 68 GLN CG C 33.20 0.05 1 737 . 68 GLN HG2 H 2.47 0.02 2 738 . 68 GLN CD C 179.69 0.05 1 739 . 68 GLN NE2 N 113.83 0.02 1 740 . 68 GLN HE21 H 7.62 0.02 1 741 . 68 GLN HE22 H 6.83 0.02 1 742 . 68 GLN C C 174.42 0.05 1 743 . 69 LYS N N 118.42 0.02 1 744 . 69 LYS H H 7.89 0.02 1 745 . 69 LYS CA C 58.11 0.05 1 746 . 69 LYS HA H 4.15 0.02 1 747 . 69 LYS CB C 33.38 0.05 1 748 . 69 LYS HB3 H 1.20 0.02 1 749 . 69 LYS HB2 H 1.56 0.02 1 750 . 69 LYS CG C 26.05 0.05 1 751 . 69 LYS HG3 H 0.81 0.02 2 752 . 69 LYS HG2 H 1.39 0.02 2 753 . 69 LYS CD C 29.63 0.05 1 754 . 69 LYS HD3 H 1.59 0.02 2 755 . 69 LYS CE C 41.97 0.05 1 756 . 69 LYS HE3 H 2.60 0.02 2 757 . 69 LYS HE2 H 2.89 0.02 2 758 . 69 LYS C C 177.68 0.05 1 759 . 70 TRP N N 119.59 0.02 1 760 . 70 TRP H H 9.43 0.02 1 761 . 70 TRP CA C 56.29 0.05 1 762 . 70 TRP HA H 4.89 0.02 1 763 . 70 TRP CB C 25.75 0.05 1 764 . 70 TRP HB3 H 3.39 0.02 2 765 . 70 TRP HB2 H 3.44 0.02 2 766 . 70 TRP CD1 C 127.16 0.05 1 767 . 70 TRP HD1 H 7.04 0.02 1 768 . 70 TRP NE1 N 126.86 0.02 1 769 . 70 TRP HE1 H 9.97 0.02 1 770 . 70 TRP CZ2 C 113.89 0.05 1 771 . 70 TRP HZ2 H 7.40 0.02 1 772 . 70 TRP CH2 C 124.18 0.05 1 773 . 70 TRP HH2 H 7.10 0.02 1 774 . 70 TRP CZ3 C 121.64 0.05 1 775 . 70 TRP HZ3 H 7.17 0.02 1 776 . 70 TRP CE3 C 121.30 0.05 1 777 . 70 TRP HE3 H 7.70 0.02 1 778 . 70 TRP C C 176.35 0.05 1 779 . 71 GLY N N 108.20 0.02 1 780 . 71 GLY H H 8.31 0.02 1 781 . 71 GLY CA C 44.06 0.05 1 782 . 71 GLY HA2 H 3.69 0.02 1 783 . 71 GLY HA3 H 4.64 0.02 1 784 . 71 GLY C C 179.77 0.05 1 785 . 72 SER N N 113.79 0.02 1 786 . 72 SER H H 8.24 0.02 1 787 . 72 SER CA C 56.89 0.05 1 788 . 72 SER HA H 5.60 0.02 1 789 . 72 SER CB C 65.51 0.05 1 790 . 72 SER HB3 H 3.88 0.02 2 791 . 72 SER HB2 H 4.01 0.02 2 792 . 72 SER C C 173.22 0.05 1 793 . 73 TRP N N 125.90 0.02 1 794 . 73 TRP H H 9.26 0.02 1 795 . 73 TRP CA C 55.50 0.05 1 796 . 73 TRP HA H 5.09 0.02 1 797 . 73 TRP CB C 31.70 0.05 1 798 . 73 TRP HB3 H 3.00 0.02 2 799 . 73 TRP HB2 H 3.16 0.02 2 800 . 73 TRP CD1 C 125.56 0.05 1 801 . 73 TRP HD1 H 7.32 0.02 1 802 . 73 TRP NE1 N 130.92 0.02 1 803 . 73 TRP HE1 H 10.33 0.02 1 804 . 73 TRP CZ2 C 113.64 0.05 1 805 . 73 TRP HZ2 H 6.78 0.02 1 806 . 73 TRP CH2 C 124.61 0.05 1 807 . 73 TRP HH2 H 4.96 0.02 1 808 . 73 TRP CZ3 C 119.71 0.05 1 809 . 73 TRP HZ3 H 6.13 0.02 1 810 . 73 TRP CE3 C 118.63 0.05 1 811 . 73 TRP HE3 H 6.94 0.02 1 812 . 74 ASN CA C 50.27 0.05 1 813 . 74 ASN HA H 5.26 0.02 1 814 . 74 ASN CB C 38.52 0.05 1 815 . 74 ASN HB3 H 2.45 0.02 2 816 . 74 ASN HB2 H 2.85 0.02 2 817 . 74 ASN CG C 176.90 0.05 1 818 . 74 ASN ND2 N 109.54 0.02 1 819 . 74 ASN HD21 H 7.22 0.02 1 820 . 74 ASN HD22 H 6.41 0.02 1 821 . 75 PRO CA C 62.48 0.05 1 822 . 75 PRO HA H 4.34 0.02 1 823 . 75 PRO CB C 32.17 0.05 1 824 . 75 PRO HB3 H 1.33 0.02 2 825 . 75 PRO HB2 H 1.55 0.02 2 826 . 75 PRO CG C 24.92 0.05 1 827 . 75 PRO HG3 H -0.53 0.02 2 828 . 75 PRO HG2 H 0.72 0.02 2 829 . 75 PRO CD C 48.90 0.05 1 830 . 75 PRO HD3 H 1.14 0.02 2 831 . 75 PRO HD2 H 3.31 0.02 2 832 . 75 PRO C C 176.80 0.05 1 833 . 76 GLY N N 113.44 0.02 1 834 . 76 GLY H H 7.91 0.02 1 835 . 76 GLY CA C 46.86 0.05 1 836 . 76 GLY HA3 H 3.49 0.02 1 837 . 76 GLY HA2 H 4.52 0.02 1 838 . 76 GLY C C 174.39 0.05 1 839 . 77 HIS N N 120.22 0.02 1 840 . 77 HIS H H 7.43 0.02 1 841 . 77 HIS CA C 59.06 0.05 1 842 . 77 HIS HA H 4.49 0.02 1 843 . 77 HIS CB C 32.39 0.05 1 844 . 77 HIS HB3 H 2.86 0.02 2 845 . 77 HIS HB2 H 3.11 0.02 2 846 . 77 HIS HD2 H 6.99 0.02 1 847 . 77 HIS CE1 C 137.92 0.05 1 848 . 77 HIS HE1 H 7.89 0.02 1 849 . 77 HIS C C 173.26 0.05 1 850 . 78 ILE N N 127.36 0.02 1 851 . 78 ILE H H 8.10 0.02 1 852 . 78 ILE CA C 56.49 0.05 1 853 . 78 ILE HA H 4.63 0.02 1 854 . 78 ILE CB C 39.38 0.05 1 855 . 78 ILE HB H 1.69 0.02 1 856 . 78 ILE CG1 C 25.94 0.05 1 857 . 78 ILE HG12 H 0.61 0.02 2 858 . 78 ILE HG13 H 0.79 0.02 2 859 . 78 ILE CD1 C 11.08 0.05 1 860 . 78 ILE HD1 H 0.64 0.02 1 861 . 78 ILE CG2 C 18.70 0.05 1 862 . 78 ILE HG2 H 0.74 0.02 1 863 . 78 ILE C C 174.84 0.05 1 864 . 79 HIS N N 126.30 0.02 1 865 . 79 HIS H H 8.32 0.02 1 866 . 79 HIS CA C 60.73 0.05 1 867 . 79 HIS HA H 4.42 0.02 1 868 . 79 HIS CB C 30.48 0.05 1 869 . 79 HIS HB3 H 3.07 0.02 2 870 . 79 HIS HB2 H 3.14 0.02 2 871 . 79 HIS HD2 H 6.83 0.02 1 872 . 79 HIS CE1 C 139.32 0.05 1 873 . 79 HIS HE1 H 7.88 0.02 1 874 . 79 HIS C C 175.43 0.05 1 875 . 80 GLU N N 116.12 0.02 1 876 . 80 GLU H H 8.27 0.02 1 877 . 80 GLU CA C 55.11 0.05 1 878 . 80 GLU HA H 4.91 0.02 1 879 . 80 GLU CB C 34.49 0.05 1 880 . 80 GLU HB2 H 1.47 0.02 2 881 . 80 GLU C C 175.65 0.05 1 882 . 81 ILE N N 125.48 0.02 1 883 . 81 ILE H H 9.11 0.02 1 884 . 81 ILE CA C 61.31 0.05 1 885 . 81 ILE HA H 4.32 0.02 1 886 . 81 ILE CB C 38.38 0.05 1 887 . 81 ILE HB H 1.58 0.02 1 888 . 81 ILE CG1 C 28.46 0.05 1 889 . 81 ILE HG12 H 1.10 0.02 2 890 . 81 ILE HG13 H 1.55 0.02 2 891 . 81 ILE CD1 C 14.18 0.05 1 892 . 81 ILE HD1 H 0.84 0.02 1 893 . 81 ILE CG2 C 17.62 0.05 1 894 . 81 ILE HG2 H 0.82 0.02 1 895 . 81 ILE C C 174.10 0.05 1 896 . 82 LEU N N 125.61 0.02 1 897 . 82 LEU H H 8.60 0.02 1 898 . 82 LEU CA C 55.47 0.05 1 899 . 82 LEU HA H 5.11 0.02 1 900 . 82 LEU CB C 45.06 0.05 1 901 . 82 LEU HB2 H 1.21 0.02 1 902 . 82 LEU HB3 H 1.75 0.02 1 903 . 82 LEU CG C 29.08 0.05 1 904 . 82 LEU HG H 1.53 0.02 1 905 . 82 LEU CD1 C 26.18 0.05 1 906 . 82 LEU HD1 H 0.86 0.02 1 907 . 82 LEU CD2 C 25.18 0.05 1 908 . 82 LEU HD2 H 0.85 0.02 1 909 . 82 LEU C C 178.54 0.05 1 910 . 83 SER N N 112.83 0.02 1 911 . 83 SER H H 7.55 0.02 1 912 . 83 SER CA C 57.93 0.05 1 913 . 83 SER HA H 4.91 0.02 1 914 . 83 SER CB C 64.01 0.05 1 915 . 83 SER HB2 H 3.61 0.02 2 916 . 83 SER C C 181.06 0.05 1 917 . 84 ILE N N 122.25 0.02 1 918 . 84 ILE H H 8.16 0.02 1 919 . 84 ILE CA C 60.18 0.05 1 920 . 84 ILE HA H 4.25 0.02 1 921 . 84 ILE CB C 42.18 0.05 1 922 . 84 ILE HB H 1.12 0.02 1 923 . 84 ILE CG1 C 25.96 0.05 1 924 . 84 ILE HG12 H 0.41 0.02 2 925 . 84 ILE HG13 H 1.14 0.02 2 926 . 84 ILE CD1 C 13.38 0.05 1 927 . 84 ILE HD1 H -0.36 0.02 1 928 . 84 ILE CG2 C 18.00 0.05 1 929 . 84 ILE HG2 H 0.31 0.02 1 930 . 84 ILE C C 172.72 0.05 1 931 . 85 ARG N N 126.25 0.02 1 932 . 85 ARG H H 8.48 0.02 1 933 . 85 ARG CA C 53.84 0.05 1 934 . 85 ARG HA H 5.36 0.02 1 935 . 85 ARG CB C 33.01 0.05 1 936 . 85 ARG HB2 H 1.55 0.02 2 937 . 85 ARG CG C 26.33 0.05 1 938 . 85 ARG HG3 H 0.40 0.02 2 939 . 85 ARG HG2 H 1.13 0.02 2 940 . 85 ARG CD C 43.43 0.05 1 941 . 85 ARG HD3 H 2.47 0.02 2 942 . 85 ARG HD2 H 2.64 0.02 2 943 . 85 ARG C C 174.76 0.05 1 944 . 86 ILE N N 126.80 0.02 1 945 . 86 ILE H H 8.67 0.02 1 946 . 86 ILE CA C 60.84 0.05 1 947 . 86 ILE HA H 4.72 0.02 1 948 . 86 ILE CB C 38.96 0.05 1 949 . 86 ILE HB H 2.04 0.02 1 950 . 86 ILE CG1 C 29.10 0.05 1 951 . 86 ILE HG12 H 0.73 0.02 2 952 . 86 ILE HG13 H 1.48 0.02 2 953 . 86 ILE CD1 C 11.91 0.05 1 954 . 86 ILE HD1 H 0.69 0.02 1 955 . 86 ILE CG2 C 17.36 0.05 1 956 . 86 ILE HG2 H 0.93 0.02 1 957 . 86 ILE C C 176.55 0.05 1 958 . 87 TYR N N 133.93 0.02 1 959 . 87 TYR H H 8.37 0.02 1 960 . 87 TYR CA C 61.50 0.05 1 961 . 87 TYR HA H 4.02 0.02 1 962 . 87 TYR CB C 38.71 0.05 1 963 . 87 TYR HB2 H 2.70 0.02 1 964 . 87 TYR HB3 H 3.01 0.02 1 965 . 87 TYR CD1 C 132.99 0.05 3 966 . 87 TYR HD1 H 7.11 0.02 3 967 . 87 TYR CE1 C 116.86 0.05 3 968 . 87 TYR HE1 H 6.78 0.02 3 stop_ save_ ######################## # Coupling constants # ######################## save_afp_JHNHa _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'AFP-1 monomer' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 ASN H 3 ASN HA 8.16 . . 1.00 2 3JHNHA 4 ARG H 4 ARG HA 7.24 . . 1.00 3 3JHNHA 5 THR H 5 THR HA 7.97 . . 1.00 4 3JHNHA 8 ASN H 8 ASN HA 7.78 . . 1.00 5 3JHNHA 12 TYR H 12 TYR HA 7.33 . . 1.00 6 3JHNHA 13 LEU H 13 LEU HA 7.64 . . 1.00 7 3JHNHA 14 GLU H 14 GLU HA 9.48 . . 1.00 8 3JHNHA 15 ILE H 15 ILE HA 8.99 . . 1.00 9 3JHNHA 16 HIS H 16 HIS HA 8.63 . . 1.00 10 3JHNHA 17 ASN H 17 ASN HA 7.98 . . 1.00 11 3JHNHA 18 ASN H 18 ASN HA 8.10 . . 1.00 12 3JHNHA 19 GLU H 19 GLU HA 6.61 . . 1.00 13 3JHNHA 21 ARG H 21 ARG HA 7.95 . . 1.00 14 3JHNHA 22 ASP H 22 ASP HA 10.19 . . 1.00 15 3JHNHA 23 THR H 23 THR HA 8.49 . . 1.00 16 3JHNHA 24 LEU H 24 LEU HA 9.43 . . 1.00 17 3JHNHA 25 CYS H 25 CYS HA 9.90 . . 1.00 18 3JHNHA 26 PHE H 26 PHE HA 9.49 . . 1.00 19 3JHNHA 27 ALA H 27 ALA HA 8.81 . . 1.00 20 3JHNHA 28 ASN H 28 ASN HA 6.37 . . 1.00 21 3JHNHA 29 ALA H 29 ALA HA 3.76 . . 1.00 22 3JHNHA 31 THR H 31 THR HA 8.34 . . 1.00 23 3JHNHA 32 MET H 32 MET HA 8.92 . . 1.00 24 3JHNHA 34 VAL H 34 VAL HA 8.79 . . 1.00 25 3JHNHA 35 ALA H 35 ALA HA 8.79 . . 1.00 26 3JHNHA 36 ILE H 36 ILE HA 10.65 . . 1.00 27 3JHNHA 37 TYR H 37 TYR HA 8.30 . . 1.00 28 3JHNHA 39 VAL H 39 VAL HA 6.28 . . 1.00 29 3JHNHA 40 ASN H 40 ASN HA 10.40 . . 1.00 30 3JHNHA 41 TRP H 41 TRP HA 5.34 . . 1.00 31 3JHNHA 42 VAL H 42 VAL HA 9.78 . . 1.00 32 3JHNHA 43 GLU H 43 GLU HA 8.58 . . 1.00 33 3JHNHA 44 SER H 44 SER HA 6.64 . . 1.00 34 3JHNHA 46 ASN H 46 ASN HA 3.00 . . 2.00 35 3JHNHA 47 ASN H 47 ASN HA 9.16 . . 1.00 36 3JHNHA 48 VAL H 48 VAL HA 9.54 . . 1.00 37 3JHNHA 49 VAL H 49 VAL HA 10.41 . . 1.00 38 3JHNHA 50 THR H 50 THR HA 9.45 . . 1.00 39 3JHNHA 51 LEU H 51 LEU HA 10.21 . . 1.00 40 3JHNHA 52 GLN H 52 GLN HA 8.09 . . 1.00 41 3JHNHA 53 PHE H 53 PHE HA 9.00 . . 1.00 42 3JHNHA 54 GLN H 54 GLN HA 10.04 . . 1.00 43 3JHNHA 55 ARG H 55 ARG HA 3.64 . . 1.00 44 3JHNHA 56 ASN H 56 ASN HA 9.80 . . 1.00 45 3JHNHA 59 ASP H 59 ASP HA 9.82 . . 1.00 46 3JHNHA 61 ARG H 61 ARG HA 5.15 . . 1.00 47 3JHNHA 62 LEU H 62 LEU HA 7.81 . . 1.00 48 3JHNHA 63 GLU H 63 GLU HA 10.11 . . 1.00 49 3JHNHA 64 THR H 64 THR HA 9.11 . . 1.00 50 3JHNHA 65 ILE H 65 ILE HA 8.12 . . 1.00 51 3JHNHA 66 THR H 66 THR HA 9.51 . . 1.00 52 3JHNHA 67 LEU H 67 LEU HA 10.07 . . 1.00 53 3JHNHA 68 GLN H 68 GLN HA 8.45 . . 1.00 54 3JHNHA 69 LYS H 69 LYS HA 3.04 . . 1.00 55 3JHNHA 70 TRP H 70 TRP HA 7.63 . . 1.00 56 3JHNHA 72 SER H 72 SER HA 10.35 . . 1.00 57 3JHNHA 73 TRP H 73 TRP HA 10.00 . . 1.00 58 3JHNHA 77 HIS H 77 HIS HA 7.27 . . 1.00 59 3JHNHA 78 ILE H 78 ILE HA 9.17 . . 1.00 60 3JHNHA 79 HIS H 79 HIS HA 3.18 . . 1.00 61 3JHNHA 80 GLU H 80 GLU HA 7.69 . . 1.00 62 3JHNHA 81 ILE H 81 ILE HA 8.46 . . 1.00 63 3JHNHA 82 LEU H 82 LEU HA 10.28 . . 1.00 64 3JHNHA 83 SER H 83 SER HA 6.50 . . 1.00 65 3JHNHA 84 ILE H 84 ILE HA 10.04 . . 1.00 66 3JHNHA 85 ARG H 85 ARG HA 9.25 . . 1.00 67 3JHNHA 86 ILE H 86 ILE HA 9.36 . . 1.00 68 3JHNHA 87 TYR H 87 TYR HA 8.58 . . 1.00 stop_ save_