data_4779 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone sequential resonance assignments of the ligand binding domain of the human TGF-beta type II receptor ; _BMRB_accession_number 4779 _BMRB_flat_file_name bmr4779.str _Entry_type update _Submission_date 2000-07-07 _Accession_date 2000-07-08 _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 Hinck Andrew P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 585 "13C chemical shifts" 477 "15N chemical shifts" 105 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-01-09 update author 'chemical shift for PHE 97 CB revised' 2000-12-18 original author 'original release date for the entry' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequential resonance assignments of the extracellular ligand binding domain of the human TGF-b type II receptor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hinck Andrew P. . 2 Walker Kerfoot P. III 3 Martin Nathan R. . 4 Deep Shashank . . 5 Hinck Cynthia S. . 6 Freedberg Daron I. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 18 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 369 _Page_last 370 _Year 2000 _Details . loop_ _Keyword TGF ligand-receptor NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_TbR2 _Saveframe_category molecular_system _Mol_system_name 'Ligand Binding Domain of the Human TGF-beta type II receptor' _Abbreviation_common TbR2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TbR2 $TbR2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' loop_ _Biological_function 'eukaryotic signal transduction' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TbR2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TGF-bet type II receptor' _Name_variant N19A _Abbreviation_common TbR2 _Molecular_mass 13783.6 _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; VTDNAGAVKFPQLCKFCDVR FSTCDNQKSCMSNCSITSIC EKPQEVCVAVWRKNDENITL ETVCHDPKLPYHDFILEDAA SPKCIMKEKKKPGETFFMCS CSSDECNDNIIFSEEYNTSN PD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 15 VAL 2 16 THR 3 17 ASP 4 18 ASN 5 19 ALA 6 20 GLY 7 21 ALA 8 22 VAL 9 23 LYS 10 24 PHE 11 25 PRO 12 26 GLN 13 27 LEU 14 28 CYS 15 29 LYS 16 30 PHE 17 31 CYS 18 32 ASP 19 33 VAL 20 34 ARG 21 35 PHE 22 36 SER 23 37 THR 24 38 CYS 25 39 ASP 26 40 ASN 27 41 GLN 28 42 LYS 29 43 SER 30 44 CYS 31 45 MET 32 46 SER 33 47 ASN 34 48 CYS 35 49 SER 36 50 ILE 37 51 THR 38 52 SER 39 53 ILE 40 54 CYS 41 55 GLU 42 56 LYS 43 57 PRO 44 58 GLN 45 59 GLU 46 60 VAL 47 61 CYS 48 62 VAL 49 63 ALA 50 64 VAL 51 65 TRP 52 66 ARG 53 67 LYS 54 68 ASN 55 69 ASP 56 70 GLU 57 71 ASN 58 72 ILE 59 73 THR 60 74 LEU 61 75 GLU 62 76 THR 63 77 VAL 64 78 CYS 65 79 HIS 66 80 ASP 67 81 PRO 68 82 LYS 69 83 LEU 70 84 PRO 71 85 TYR 72 86 HIS 73 87 ASP 74 88 PHE 75 89 ILE 76 90 LEU 77 91 GLU 78 92 ASP 79 93 ALA 80 94 ALA 81 95 SER 82 96 PRO 83 97 LYS 84 98 CYS 85 99 ILE 86 100 MET 87 101 LYS 88 102 GLU 89 103 LYS 90 104 LYS 91 105 LYS 92 106 PRO 93 107 GLY 94 108 GLU 95 109 THR 96 110 PHE 97 111 PHE 98 112 MET 99 113 CYS 100 114 SER 101 115 CYS 102 116 SER 103 117 SER 104 118 ASP 105 119 GLU 106 120 CYS 107 121 ASN 108 122 ASP 109 123 ASN 110 124 ILE 111 125 ILE 112 126 PHE 113 127 SER 114 128 GLU 115 129 GLU 116 130 TYR 117 131 ASN 118 132 THR 119 133 SER 120 134 ASN 121 135 PRO 122 136 ASP 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 REF XP_001095987 'PREDICTED: similar to transforming growth factor, beta receptor II isoform B precursor isoform 3 [Macaca mulatta]' 100.00 567 98.36 99.18 2.20e-66 SWISS-PROT P37173 'TGF-beta receptor type-2 precursor (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TGF-beta type II receptor) (TbetaR-II) (TGFR-2)' 100.00 567 99.18 99.18 8.73e-67 REF XP_001095763 'PREDICTED: similar to transforming growth factor, beta receptor II isoform B precursor isoform 1 [Macaca mulatta]' 93.44 603 98.25 99.12 2.40e-61 REF XP_001095877 'PREDICTED: similar to transforming growth factor, beta receptor II isoform A precursor isoform 2 [Macaca mulatta]' 100.00 592 98.36 99.18 3.10e-66 REF NP_001020018 'transforming growth factor, beta receptor II isoform A precursor [Homo sapiens]' 100.00 592 99.18 99.18 1.14e-66 REF NP_003233 'transforming growth factor, beta receptor II isoform B precursor [Homo sapiens]' 100.00 567 99.18 99.18 8.73e-67 GenBank AAI52841 'Transforming growth factor, beta receptor II (70/80kDa) [synthetic construct]' 100.00 592 99.18 99.18 1.14e-66 GenBank AAQ02596 'transforming growth factor, beta receptor II [synthetic construct]' 100.00 568 99.18 99.18 7.51e-67 GenBank AAB17553 'transforming growth factor-beta type II receptor [Homo sapiens]' 100.00 567 99.18 99.18 9.03e-67 GenBank AAB40916 'transforming growth factor-beta type II receptor [Homo sapiens]' 100.00 567 99.18 99.18 9.03e-67 DBJ BAG62117 'unnamed protein product [Homo sapiens]' 100.00 592 99.18 99.18 1.14e-66 GenBank AAA61164 'TGF-beta type II receptor' 100.00 567 99.18 99.18 9.03e-67 DBJ BAG10803 'TGF-beta receptor type-2 precursor [synthetic construct]' 100.00 567 99.18 99.18 8.73e-67 DBJ BAG36796 'unnamed protein product [Homo sapiens]' 100.00 567 99.18 99.18 8.73e-67 DBJ BAA05673 'TGF-beta receptor type IIB [Homo sapiens]' 100.00 283 99.18 99.18 5.03e-66 DBJ BAA09332 'TGF-betaIIR alpha [Homo sapiens]' 100.00 567 99.18 99.18 9.73e-67 PDB 1PLO 'Transforming Growth Factor-Beta Type Ii Receptor Extracellular Domain' 100.00 122 100.00 100.00 4.99e-65 PDB 2PJY 'Structural Basis For Cooperative Assembly Of The Tgf-Beta Signaling Complex' 88.52 108 100.00 100.00 8.83e-57 PDB 1KTZ 'Crystal Structure Of The Human Tgf-Beta Type Ii Receptor Extracellular Domain In Complex With Tgf-Beta3' 100.00 122 99.18 99.18 2.90e-64 PDB 1M9Z 'Crystal Structure Of Human Tgf-Beta Type Ii Receptor Ligand Binding Domain' 90.16 111 99.09 99.09 4.53e-57 BMRB 5953 'Transforming Growth Factor type II Receptor' 95.08 116 99.14 100.00 8.75e-61 BMRB 5954 'Transforming Growth Factor type II Receptor' 95.08 116 99.14 100.00 8.75e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TbR2 Human 9606 Eukaryota Metazoa Homo sapiens 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 $TbR2 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TbR2 . mM 0.5 2.0 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 'Feb, 2000' _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX2 _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_H(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CO)NH _Sample_label . save_ save_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.50 0.05 n/a temperature 300 0.5 K 'ionic strength' 0.05 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329112 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449519 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $condition1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TbR2 _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 VAL HA H 4.27 0.03 1 2 . 1 VAL HB H 2.08 0.03 1 3 . 1 VAL HG1 H 0.97 0.03 2 4 . 1 VAL C C 175.90 0.50 1 5 . 1 VAL CA C 62.50 0.50 1 6 . 1 VAL CB C 32.80 0.50 1 7 . 1 VAL CG1 C 21.40 0.50 2 8 . 2 THR H H 8.24 0.03 1 9 . 2 THR HA H 4.38 0.03 1 10 . 2 THR HB H 4.20 0.03 1 11 . 2 THR HG2 H 1.18 0.03 1 12 . 2 THR C C 174.10 0.50 1 13 . 2 THR CA C 61.50 0.50 1 14 . 2 THR CB C 69.90 0.50 1 15 . 2 THR CG2 C 21.60 0.50 1 16 . 2 THR N N 117.60 0.25 1 17 . 3 ASP H H 8.29 0.03 1 18 . 3 ASP HA H 4.59 0.03 1 19 . 3 ASP HB2 H 2.67 0.03 2 20 . 3 ASP C C 176.00 0.50 1 21 . 3 ASP CA C 54.20 0.50 1 22 . 3 ASP CB C 41.30 0.50 1 23 . 3 ASP N N 122.80 0.25 1 24 . 4 ASN H H 8.39 0.03 1 25 . 4 ASN HA H 4.66 0.03 1 26 . 4 ASN HB2 H 2.77 0.03 2 27 . 4 ASN HB3 H 2.83 0.03 2 28 . 4 ASN C C 175.20 0.50 1 29 . 4 ASN CA C 53.40 0.50 1 30 . 4 ASN CB C 38.80 0.50 1 31 . 4 ASN N N 119.40 0.25 1 32 . 5 ALA H H 8.31 0.03 1 33 . 5 ALA HA H 4.26 0.03 1 34 . 5 ALA HB H 1.39 0.03 1 35 . 5 ALA C C 178.20 0.50 1 36 . 5 ALA CA C 53.10 0.50 1 37 . 5 ALA CB C 19.00 0.50 1 38 . 5 ALA N N 124.50 0.25 1 39 . 6 GLY H H 8.29 0.03 1 40 . 6 GLY HA3 H 3.89 0.03 2 41 . 6 GLY C C 173.80 0.50 1 42 . 6 GLY CA C 45.20 0.50 1 43 . 6 GLY N N 107.70 0.25 1 44 . 7 ALA H H 7.96 0.03 1 45 . 7 ALA HA H 4.29 0.03 1 46 . 7 ALA HB H 1.33 0.03 1 47 . 7 ALA C C 177.50 0.50 1 48 . 7 ALA CA C 52.30 0.50 1 49 . 7 ALA CB C 19.40 0.50 1 50 . 7 ALA N N 123.70 0.25 1 51 . 8 VAL H H 8.01 0.03 1 52 . 8 VAL HA H 3.95 0.03 1 53 . 8 VAL HB H 1.91 0.03 1 54 . 8 VAL HG1 H 0.86 0.03 2 55 . 8 VAL HG2 H 0.71 0.03 2 56 . 8 VAL C C 175.10 0.50 1 57 . 8 VAL CA C 62.20 0.50 1 58 . 8 VAL CB C 32.90 0.50 1 59 . 8 VAL CG1 C 20.80 0.50 2 60 . 8 VAL CG2 C 21.20 0.50 2 61 . 8 VAL N N 120.10 0.25 1 62 . 9 LYS H H 8.31 0.03 1 63 . 9 LYS HA H 4.35 0.03 1 64 . 9 LYS HB2 H 1.68 0.03 2 65 . 9 LYS HG2 H 1.32 0.03 2 66 . 9 LYS HD2 H 1.73 0.03 2 67 . 9 LYS HD3 H 1.61 0.03 2 68 . 9 LYS HE2 H 3.07 0.03 2 69 . 9 LYS HE3 H 2.98 0.03 2 70 . 9 LYS C C 175.10 0.50 1 71 . 9 LYS CA C 55.30 0.50 1 72 . 9 LYS CB C 33.60 0.50 1 73 . 9 LYS CG C 24.40 0.50 1 74 . 9 LYS CD C 28.80 0.50 1 75 . 9 LYS CE C 42.50 0.50 1 76 . 9 LYS N N 126.10 0.25 1 77 . 10 PHE H H 8.49 0.03 1 78 . 10 PHE HA H 4.85 0.03 1 79 . 10 PHE HB2 H 3.27 0.03 2 80 . 10 PHE HB3 H 2.87 0.03 2 81 . 10 PHE HD2 H 7.34 0.03 3 82 . 10 PHE C C 173.70 0.50 1 83 . 10 PHE CA C 55.70 0.50 1 84 . 10 PHE CB C 39.00 0.50 1 85 . 10 PHE N N 124.90 0.25 1 86 . 11 PRO HA H 4.48 0.03 1 87 . 11 PRO HB2 H 1.92 0.03 2 88 . 11 PRO HB3 H 1.99 0.03 2 89 . 11 PRO HG2 H 1.72 0.03 2 90 . 11 PRO HG3 H 2.05 0.03 2 91 . 11 PRO HD2 H 3.83 0.03 2 92 . 11 PRO C C 175.30 0.50 1 93 . 11 PRO CA C 62.60 0.50 1 94 . 11 PRO CB C 32.50 0.50 1 95 . 11 PRO CG C 27.80 0.50 1 96 . 11 PRO CD C 50.20 0.50 1 97 . 12 GLN H H 8.95 0.03 1 98 . 12 GLN HA H 4.30 0.03 1 99 . 12 GLN HB2 H 2.01 0.03 2 100 . 12 GLN HB3 H 1.34 0.03 2 101 . 12 GLN HG2 H 2.27 0.03 2 102 . 12 GLN C C 173.70 0.50 1 103 . 12 GLN CA C 55.20 0.50 1 104 . 12 GLN CB C 32.00 0.50 1 105 . 12 GLN CG C 35.70 0.50 1 106 . 12 GLN N N 122.10 0.25 1 107 . 13 LEU H H 7.93 0.03 1 108 . 13 LEU HA H 5.04 0.03 1 109 . 13 LEU HB2 H 1.40 0.03 2 110 . 13 LEU HB3 H 1.17 0.03 2 111 . 13 LEU HG H 1.59 0.03 1 112 . 13 LEU HD1 H 0.82 0.03 2 113 . 13 LEU HD2 H 0.74 0.03 2 114 . 13 LEU C C 178.40 0.50 1 115 . 13 LEU CA C 54.00 0.50 1 116 . 13 LEU CB C 44.30 0.50 1 117 . 13 LEU CG C 27.60 0.50 1 118 . 13 LEU CD1 C 25.20 0.50 2 119 . 13 LEU CD2 C 24.80 0.50 2 120 . 13 LEU N N 120.00 0.25 1 121 . 14 CYS H H 9.02 0.03 1 122 . 14 CYS HA H 5.10 0.03 1 123 . 14 CYS HB2 H 2.94 0.03 2 124 . 14 CYS HB3 H 2.57 0.03 2 125 . 14 CYS C C 175.60 0.50 1 126 . 14 CYS CA C 52.50 0.50 1 127 . 14 CYS CB C 42.90 0.50 1 128 . 14 CYS N N 118.80 0.25 1 129 . 15 LYS H H 9.14 0.03 1 130 . 15 LYS HA H 5.02 0.03 1 131 . 15 LYS HB2 H 1.67 0.03 2 132 . 15 LYS HB3 H 1.53 0.03 2 133 . 15 LYS HG2 H 1.18 0.03 2 134 . 15 LYS HG3 H 1.43 0.03 2 135 . 15 LYS HD2 H 1.59 0.03 2 136 . 15 LYS HE2 H 2.92 0.03 2 137 . 15 LYS C C 177.70 0.50 1 138 . 15 LYS CA C 54.90 0.50 1 139 . 15 LYS CB C 29.60 0.50 1 140 . 15 LYS CG C 23.80 0.50 1 141 . 15 LYS CD C 27.50 0.50 1 142 . 15 LYS CE C 41.30 0.50 1 143 . 15 LYS N N 120.10 0.25 1 144 . 16 PHE H H 8.45 0.03 1 145 . 16 PHE HA H 5.28 0.03 1 146 . 16 PHE HB2 H 3.62 0.03 2 147 . 16 PHE HB3 H 2.41 0.03 2 148 . 16 PHE HD2 H 7.19 0.03 3 149 . 16 PHE C C 174.70 0.50 1 150 . 16 PHE CA C 54.30 0.50 1 151 . 16 PHE CB C 39.50 0.50 1 152 . 16 PHE N N 127.00 0.25 1 153 . 17 CYS H H 8.65 0.03 1 154 . 17 CYS HA H 4.89 0.03 1 155 . 17 CYS HB2 H 3.31 0.03 2 156 . 17 CYS C C 175.00 0.50 1 157 . 17 CYS CA C 61.10 0.50 1 158 . 17 CYS CB C 40.10 0.50 1 159 . 17 CYS N N 119.60 0.25 1 160 . 18 ASP H H 9.41 0.03 1 161 . 18 ASP HA H 4.10 0.03 1 162 . 18 ASP HB2 H 3.18 0.03 2 163 . 18 ASP HB3 H 3.01 0.03 2 164 . 18 ASP C C 174.90 0.50 1 165 . 18 ASP CA C 57.60 0.50 1 166 . 18 ASP CB C 40.10 0.50 1 167 . 18 ASP N N 118.10 0.25 1 168 . 19 VAL H H 8.19 0.03 1 169 . 19 VAL HA H 4.02 0.03 1 170 . 19 VAL HB H 2.02 0.03 1 171 . 19 VAL HG1 H 0.97 0.03 2 172 . 19 VAL HG2 H 0.77 0.03 2 173 . 19 VAL C C 176.00 0.50 1 174 . 19 VAL CA C 64.60 0.50 1 175 . 19 VAL CB C 31.90 0.50 1 176 . 19 VAL CG1 C 21.30 0.50 1 177 . 19 VAL CG2 C 21.30 0.50 1 178 . 19 VAL N N 121.90 0.25 1 179 . 20 ARG H H 8.65 0.03 1 180 . 20 ARG HA H 4.75 0.03 1 181 . 20 ARG HB2 H 2.03 0.03 2 182 . 20 ARG HB3 H 1.85 0.03 2 183 . 20 ARG HG2 H 1.58 0.03 2 184 . 20 ARG HG3 H 1.79 0.03 2 185 . 20 ARG HD2 H 3.35 0.03 2 186 . 20 ARG HD3 H 3.57 0.03 2 187 . 20 ARG C C 175.90 0.50 1 188 . 20 ARG CA C 52.40 0.50 1 189 . 20 ARG CB C 34.40 0.50 1 190 . 20 ARG CG C 26.50 0.50 1 191 . 20 ARG CD C 43.20 0.50 1 192 . 20 ARG N N 127.50 0.25 1 193 . 21 PHE H H 8.60 0.03 1 194 . 21 PHE HA H 4.91 0.03 1 195 . 21 PHE HB2 H 3.06 0.03 2 196 . 21 PHE HB3 H 3.22 0.03 2 197 . 21 PHE HD2 H 7.36 0.03 3 198 . 21 PHE C C 176.20 0.50 1 199 . 21 PHE CA C 59.20 0.50 1 200 . 21 PHE CB C 39.00 0.50 1 201 . 21 PHE N N 120.30 0.25 1 202 . 22 SER H H 8.14 0.03 1 203 . 22 SER HA H 4.83 0.03 1 204 . 22 SER HB2 H 3.88 0.03 2 205 . 22 SER HB3 H 3.19 0.03 2 206 . 22 SER C C 173.20 0.50 1 207 . 22 SER CA C 56.20 0.50 1 208 . 22 SER CB C 66.60 0.50 1 209 . 22 SER N N 117.30 0.25 1 210 . 23 THR H H 8.33 0.03 1 211 . 23 THR HA H 4.50 0.03 1 212 . 23 THR HB H 4.60 0.03 1 213 . 23 THR HG2 H 1.25 0.03 1 214 . 23 THR C C 175.10 0.50 1 215 . 23 THR CA C 60.80 0.50 1 216 . 23 THR CB C 68.90 0.50 1 217 . 23 THR CG2 C 21.60 0.50 1 218 . 23 THR N N 113.40 0.25 1 219 . 24 CYS H H 8.58 0.03 1 220 . 24 CYS HA H 4.45 0.03 1 221 . 24 CYS HB2 H 3.13 0.03 2 222 . 24 CYS HB3 H 3.35 0.03 2 223 . 24 CYS C C 173.40 0.50 1 224 . 24 CYS CA C 56.80 0.50 1 225 . 24 CYS CB C 40.60 0.50 1 226 . 24 CYS N N 123.30 0.25 1 227 . 25 ASP H H 8.14 0.03 1 228 . 25 ASP HA H 4.80 0.03 1 229 . 25 ASP HB2 H 2.74 0.03 2 230 . 25 ASP HB3 H 2.49 0.03 2 231 . 25 ASP C C 174.90 0.50 1 232 . 25 ASP CA C 53.40 0.50 1 233 . 25 ASP CB C 42.50 0.50 1 234 . 25 ASP N N 126.20 0.25 1 235 . 26 ASN H H 7.91 0.03 1 236 . 26 ASN HA H 2.92 0.03 1 237 . 26 ASN HB2 H 1.68 0.03 2 238 . 26 ASN HB3 H 1.39 0.03 2 239 . 26 ASN C C 173.70 0.50 1 240 . 26 ASN CA C 52.60 0.50 1 241 . 26 ASN CB C 36.60 0.50 1 242 . 26 ASN N N 118.60 0.25 1 243 . 27 GLN H H 7.39 0.03 1 244 . 27 GLN HA H 4.06 0.03 1 245 . 27 GLN HB2 H 2.00 0.03 2 246 . 27 GLN HB3 H 1.60 0.03 2 247 . 27 GLN HG2 H 2.10 0.03 2 248 . 27 GLN C C 175.20 0.50 1 249 . 27 GLN CA C 54.60 0.50 1 250 . 27 GLN CB C 31.80 0.50 1 251 . 27 GLN CG C 33.80 0.50 1 252 . 27 GLN N N 114.90 0.25 1 253 . 28 LYS H H 8.50 0.03 1 254 . 28 LYS HA H 4.13 0.03 1 255 . 28 LYS HB2 H 1.88 0.03 2 256 . 28 LYS HG2 H 1.46 0.03 2 257 . 28 LYS HG3 H 1.32 0.03 2 258 . 28 LYS HD2 H 1.63 0.03 2 259 . 28 LYS HE2 H 2.95 0.03 2 260 . 28 LYS C C 175.50 0.50 1 261 . 28 LYS CA C 58.00 0.50 1 262 . 28 LYS CB C 32.30 0.50 1 263 . 28 LYS CG C 25.20 0.50 1 264 . 28 LYS CD C 29.20 0.50 1 265 . 28 LYS CE C 42.40 0.50 1 266 . 28 LYS N N 118.80 0.25 1 267 . 29 SER H H 7.77 0.03 1 268 . 29 SER HA H 5.27 0.03 1 269 . 29 SER HB2 H 3.85 0.03 2 270 . 29 SER C C 172.70 0.50 1 271 . 29 SER CA C 57.50 0.50 1 272 . 29 SER CB C 65.20 0.50 1 273 . 29 SER N N 113.00 0.25 1 274 . 30 CYS H H 9.26 0.03 1 275 . 30 CYS HA H 4.85 0.03 1 276 . 30 CYS HB2 H 3.05 0.03 2 277 . 30 CYS HB3 H 3.33 0.03 2 278 . 30 CYS C C 172.60 0.50 1 279 . 30 CYS CA C 53.70 0.50 1 280 . 30 CYS CB C 46.70 0.50 1 281 . 30 CYS N N 119.30 0.25 1 282 . 31 MET H H 8.47 0.03 1 283 . 31 MET HA H 5.52 0.03 1 284 . 31 MET HB2 H 2.73 0.03 2 285 . 31 MET HB3 H 2.55 0.03 2 286 . 31 MET HG2 H 2.22 0.03 2 287 . 31 MET HG3 H 1.96 0.03 2 288 . 31 MET HE H 2.00 0.03 1 289 . 31 MET C C 178.90 0.50 1 290 . 31 MET CA C 53.10 0.50 1 291 . 31 MET CB C 31.70 0.50 1 292 . 31 MET CE C 16.10 0.50 1 293 . 31 MET N N 121.50 0.25 1 294 . 32 SER H H 9.28 0.03 1 295 . 32 SER HA H 3.78 0.03 1 296 . 32 SER HB2 H 3.70 0.03 2 297 . 32 SER HB3 H 4.57 0.03 2 298 . 32 SER C C 176.30 0.50 1 299 . 32 SER CA C 62.00 0.50 1 300 . 32 SER CB C 63.60 0.50 1 301 . 32 SER N N 116.90 0.25 1 302 . 33 ASN H H 9.03 0.03 1 303 . 33 ASN HA H 4.28 0.03 1 304 . 33 ASN HB2 H 3.26 0.03 2 305 . 33 ASN HB3 H 2.83 0.03 2 306 . 33 ASN C C 174.20 0.50 1 307 . 33 ASN CA C 54.50 0.50 1 308 . 33 ASN CB C 37.50 0.50 1 309 . 33 ASN N N 118.70 0.25 1 310 . 34 CYS H H 8.12 0.03 1 311 . 34 CYS HA H 5.02 0.03 1 312 . 34 CYS HB2 H 2.88 0.03 2 313 . 34 CYS HB3 H 3.12 0.03 2 314 . 34 CYS C C 174.80 0.50 1 315 . 34 CYS CA C 53.90 0.50 1 316 . 34 CYS CB C 37.50 0.50 1 317 . 34 CYS N N 116.50 0.25 1 318 . 35 SER H H 9.00 0.03 1 319 . 35 SER HA H 4.52 0.03 1 320 . 35 SER HB2 H 4.13 0.03 2 321 . 35 SER HB3 H 3.91 0.03 2 322 . 35 SER C C 173.00 0.50 1 323 . 35 SER CA C 58.90 0.50 1 324 . 35 SER CB C 63.40 0.50 1 325 . 35 SER N N 125.50 0.25 1 326 . 36 ILE H H 7.50 0.03 1 327 . 36 ILE HA H 4.18 0.03 1 328 . 36 ILE HB H 1.77 0.03 1 329 . 36 ILE HG12 H 0.95 0.03 2 330 . 36 ILE HG13 H 1.52 0.03 2 331 . 36 ILE HG2 H 0.77 0.03 1 332 . 36 ILE HD1 H 0.90 0.03 1 333 . 36 ILE C C 174.50 0.50 1 334 . 36 ILE CA C 61.60 0.50 1 335 . 36 ILE CB C 38.70 0.50 1 336 . 36 ILE CG1 C 26.80 0.50 1 337 . 36 ILE CG2 C 17.40 0.50 1 338 . 36 ILE CD1 C 13.10 0.50 1 339 . 36 ILE N N 123.50 0.25 1 340 . 37 THR H H 8.54 0.03 1 341 . 37 THR HA H 4.76 0.03 1 342 . 37 THR HB H 3.93 0.03 1 343 . 37 THR HG2 H 1.06 0.03 1 344 . 37 THR C C 174.10 0.50 1 345 . 37 THR CA C 62.00 0.50 1 346 . 37 THR CB C 69.50 0.50 1 347 . 37 THR CG2 C 23.60 0.50 1 348 . 37 THR N N 126.10 0.25 1 349 . 38 SER H H 9.06 0.03 1 350 . 38 SER HA H 4.88 0.03 1 351 . 38 SER HB2 H 3.57 0.03 2 352 . 38 SER HB3 H 3.80 0.03 2 353 . 38 SER C C 172.50 0.50 1 354 . 38 SER CA C 56.60 0.50 1 355 . 38 SER CB C 66.60 0.50 1 356 . 38 SER N N 122.60 0.25 1 357 . 39 ILE H H 8.29 0.03 1 358 . 39 ILE HA H 4.51 0.03 1 359 . 39 ILE HB H 1.66 0.03 1 360 . 39 ILE HG12 H 1.56 0.03 2 361 . 39 ILE HG13 H 1.04 0.03 2 362 . 39 ILE HG2 H 0.92 0.03 1 363 . 39 ILE HD1 H 0.86 0.03 1 364 . 39 ILE C C 177.20 0.50 1 365 . 39 ILE CA C 61.00 0.50 1 366 . 39 ILE CB C 38.90 0.50 1 367 . 39 ILE CG1 C 28.00 0.50 1 368 . 39 ILE CG2 C 17.60 0.50 1 369 . 39 ILE CD1 C 14.00 0.50 1 370 . 39 ILE N N 124.30 0.25 1 371 . 40 CYS H H 8.86 0.03 1 372 . 40 CYS HA H 4.82 0.03 1 373 . 40 CYS HB2 H 3.87 0.03 2 374 . 40 CYS HB3 H 3.00 0.03 2 375 . 40 CYS C C 175.10 0.50 1 376 . 40 CYS CA C 53.50 0.50 1 377 . 40 CYS CB C 37.10 0.50 1 378 . 40 CYS N N 127.40 0.25 1 379 . 41 GLU H H 8.95 0.03 1 380 . 41 GLU HA H 3.97 0.03 1 381 . 41 GLU HB2 H 2.12 0.03 2 382 . 41 GLU HB3 H 2.21 0.03 2 383 . 41 GLU HG2 H 2.46 0.03 2 384 . 41 GLU HG3 H 2.31 0.03 2 385 . 41 GLU C C 176.90 0.50 1 386 . 41 GLU CA C 59.30 0.50 1 387 . 41 GLU CB C 30.60 0.50 1 388 . 41 GLU CG C 36.60 0.50 1 389 . 41 GLU N N 120.50 0.25 1 390 . 42 LYS H H 7.72 0.03 1 391 . 42 LYS HA H 4.98 0.03 1 392 . 42 LYS HB2 H 2.02 0.03 2 393 . 42 LYS HB3 H 1.48 0.03 2 394 . 42 LYS HG2 H 1.39 0.03 2 395 . 42 LYS HD2 H 1.72 0.03 2 396 . 42 LYS HD3 H 1.61 0.03 2 397 . 42 LYS HE2 H 2.95 0.03 2 398 . 42 LYS C C 176.00 0.50 1 399 . 42 LYS CA C 52.50 0.50 1 400 . 42 LYS CB C 33.60 0.50 1 401 . 42 LYS CG C 25.00 0.50 1 402 . 42 LYS CD C 29.30 0.50 1 403 . 42 LYS CE C 41.80 0.50 1 404 . 42 LYS N N 114.70 0.25 1 405 . 43 PRO HA H 4.01 0.03 1 406 . 43 PRO HB2 H 2.18 0.03 2 407 . 43 PRO HB3 H 1.91 0.03 2 408 . 43 PRO HG2 H 2.15 0.03 2 409 . 43 PRO HG3 H 2.01 0.03 2 410 . 43 PRO HD2 H 3.91 0.03 2 411 . 43 PRO C C 175.70 0.50 1 412 . 43 PRO CA C 65.00 0.50 1 413 . 43 PRO CB C 32.00 0.50 1 414 . 43 PRO CG C 27.40 0.50 1 415 . 43 PRO CD C 50.90 0.50 1 416 . 44 GLN H H 8.54 0.03 1 417 . 44 GLN HA H 4.05 0.03 1 418 . 44 GLN HB2 H 2.01 0.03 2 419 . 44 GLN HG2 H 2.05 0.03 2 420 . 44 GLN HG3 H 2.45 0.03 2 421 . 44 GLN C C 176.30 0.50 1 422 . 44 GLN CA C 56.50 0.50 1 423 . 44 GLN CB C 27.40 0.50 1 424 . 44 GLN CG C 33.40 0.50 1 425 . 44 GLN N N 113.40 0.25 1 426 . 45 GLU H H 7.13 0.03 1 427 . 45 GLU HA H 4.07 0.03 1 428 . 45 GLU HB2 H 2.22 0.03 2 429 . 45 GLU HB3 H 1.86 0.03 2 430 . 45 GLU HG2 H 1.75 0.03 2 431 . 45 GLU HG3 H 2.24 0.03 2 432 . 45 GLU C C 175.70 0.50 1 433 . 45 GLU CA C 57.80 0.50 1 434 . 45 GLU CB C 30.70 0.50 1 435 . 45 GLU CG C 38.30 0.50 1 436 . 45 GLU N N 116.50 0.25 1 437 . 46 VAL H H 8.48 0.03 1 438 . 46 VAL HA H 4.83 0.03 1 439 . 46 VAL HB H 2.75 0.03 1 440 . 46 VAL HG1 H 1.02 0.03 2 441 . 46 VAL HG2 H 0.91 0.03 2 442 . 46 VAL C C 174.60 0.50 1 443 . 46 VAL CA C 58.70 0.50 1 444 . 46 VAL CB C 33.00 0.50 1 445 . 46 VAL CG1 C 21.80 0.50 2 446 . 46 VAL CG2 C 18.10 0.50 2 447 . 46 VAL N N 112.80 0.25 1 448 . 47 CYS H H 8.14 0.03 1 449 . 47 CYS HA H 5.28 0.03 1 450 . 47 CYS HB2 H 3.13 0.03 2 451 . 47 CYS HB3 H 3.01 0.03 2 452 . 47 CYS C C 174.90 0.50 1 453 . 47 CYS CA C 52.90 0.50 1 454 . 47 CYS CB C 35.50 0.50 1 455 . 47 CYS N N 115.20 0.25 1 456 . 48 VAL H H 8.58 0.03 1 457 . 48 VAL HA H 5.02 0.03 1 458 . 48 VAL HB H 1.54 0.03 1 459 . 48 VAL HG1 H 0.71 0.03 2 460 . 48 VAL HG2 H 0.67 0.03 2 461 . 48 VAL C C 176.20 0.50 1 462 . 48 VAL CA C 60.60 0.50 1 463 . 48 VAL CB C 36.40 0.50 1 464 . 48 VAL CG1 C 22.10 0.50 2 465 . 48 VAL CG2 C 24.40 0.50 2 466 . 48 VAL N N 118.60 0.25 1 467 . 49 ALA H H 9.02 0.03 1 468 . 49 ALA HA H 5.97 0.03 1 469 . 49 ALA HB H 1.43 0.03 1 470 . 49 ALA C C 175.80 0.50 1 471 . 49 ALA CA C 51.00 0.50 1 472 . 49 ALA CB C 23.00 0.50 1 473 . 49 ALA N N 129.20 0.25 1 474 . 50 VAL H H 8.98 0.03 1 475 . 50 VAL HA H 4.95 0.03 1 476 . 50 VAL HB H 2.24 0.03 1 477 . 50 VAL HG1 H 0.89 0.03 2 478 . 50 VAL HG2 H 0.63 0.03 2 479 . 50 VAL C C 174.80 0.50 1 480 . 50 VAL CA C 60.90 0.50 1 481 . 50 VAL CB C 35.20 0.50 1 482 . 50 VAL CG1 C 21.40 0.50 2 483 . 50 VAL CG2 C 22.30 0.50 2 484 . 50 VAL N N 120.10 0.25 1 485 . 51 TRP H H 9.91 0.03 1 486 . 51 TRP HA H 5.59 0.03 1 487 . 51 TRP HB2 H 3.50 0.03 2 488 . 51 TRP HB3 H 2.89 0.03 2 489 . 51 TRP HZ2 H 7.48 0.03 1 490 . 51 TRP HZ3 H 7.75 0.03 1 491 . 51 TRP HE3 H 6.96 0.03 1 492 . 51 TRP HH2 H 6.98 0.03 1 493 . 51 TRP HD1 H 6.83 0.03 1 494 . 51 TRP HE1 H 9.92 0.03 1 495 . 51 TRP C C 174.10 0.50 1 496 . 51 TRP CA C 56.90 0.50 1 497 . 51 TRP CB C 34.10 0.50 1 498 . 51 TRP CZ2 C 114.60 0.50 1 499 . 51 TRP CZ3 C 121.30 0.50 1 500 . 51 TRP CE3 C 121.20 0.50 1 501 . 51 TRP CH2 C 124.90 0.50 1 502 . 51 TRP CD1 C 125.00 0.50 1 503 . 51 TRP N N 134.50 0.25 1 504 . 51 TRP NE1 N 131.10 0.25 1 505 . 52 ARG H H 8.31 0.03 1 506 . 52 ARG HA H 5.03 0.03 1 507 . 52 ARG HB2 H 1.42 0.03 2 508 . 52 ARG HB3 H 1.72 0.03 2 509 . 52 ARG HG2 H 1.35 0.03 2 510 . 52 ARG HG3 H 1.39 0.03 2 511 . 52 ARG HD2 H 2.67 0.03 2 512 . 52 ARG HD3 H 2.84 0.03 2 513 . 52 ARG C C 173.00 0.50 1 514 . 52 ARG CA C 54.70 0.50 1 515 . 52 ARG CB C 35.10 0.50 1 516 . 52 ARG CG C 27.10 0.50 1 517 . 52 ARG CD C 44.30 0.50 1 518 . 52 ARG N N 125.70 0.25 1 519 . 53 LYS H H 8.49 0.03 1 520 . 53 LYS HA H 4.65 0.03 1 521 . 53 LYS HB2 H 1.49 0.03 2 522 . 53 LYS HB3 H 1.02 0.03 2 523 . 53 LYS HG2 H 1.36 0.03 2 524 . 53 LYS HD2 H 1.73 0.03 2 525 . 53 LYS HE2 H 2.96 0.03 2 526 . 53 LYS C C 175.10 0.50 1 527 . 53 LYS CA C 55.00 0.50 1 528 . 53 LYS CB C 35.90 0.50 1 529 . 53 LYS CG C 25.50 0.50 1 530 . 53 LYS CD C 30.20 0.50 1 531 . 53 LYS CE C 42.40 0.50 1 532 . 53 LYS N N 122.70 0.25 1 533 . 54 ASN H H 8.40 0.03 1 534 . 54 ASN HA H 4.98 0.03 1 535 . 54 ASN HB2 H 2.95 0.03 2 536 . 54 ASN HB3 H 2.79 0.03 2 537 . 54 ASN C C 174.30 0.50 1 538 . 54 ASN CA C 52.00 0.50 1 539 . 54 ASN CB C 41.00 0.50 1 540 . 54 ASN N N 126.00 0.25 1 541 . 55 ASP H H 8.83 0.03 1 542 . 55 ASP HA H 4.27 0.03 1 543 . 55 ASP HB2 H 2.86 0.03 2 544 . 55 ASP HB3 H 2.75 0.03 2 545 . 55 ASP C C 175.70 0.50 1 546 . 55 ASP CA C 56.70 0.50 1 547 . 55 ASP CB C 39.70 0.50 1 548 . 55 ASP N N 121.20 0.25 1 549 . 56 GLU H H 8.49 0.03 1 550 . 56 GLU HA H 4.29 0.03 1 551 . 56 GLU HB2 H 2.16 0.03 2 552 . 56 GLU HB3 H 1.99 0.03 2 553 . 56 GLU HG2 H 2.00 0.03 2 554 . 56 GLU C C 175.80 0.50 1 555 . 56 GLU CA C 57.20 0.50 1 556 . 56 GLU CB C 30.40 0.50 1 557 . 56 GLU CG C 36.10 0.50 1 558 . 56 GLU N N 117.20 0.25 1 559 . 57 ASN H H 8.22 0.03 1 560 . 57 ASN HA H 4.83 0.03 1 561 . 57 ASN HB2 H 2.79 0.03 2 562 . 57 ASN C C 173.10 0.50 1 563 . 57 ASN CA C 53.40 0.50 1 564 . 57 ASN CB C 40.90 0.50 1 565 . 57 ASN N N 117.60 0.25 1 566 . 58 ILE H H 8.31 0.03 1 567 . 58 ILE HA H 4.68 0.03 1 568 . 58 ILE HB H 1.86 0.03 1 569 . 58 ILE HG12 H 0.56 0.03 2 570 . 58 ILE HG13 H 1.53 0.03 2 571 . 58 ILE HG2 H 0.46 0.03 1 572 . 58 ILE HD1 H 0.90 0.03 1 573 . 58 ILE C C 176.50 0.50 1 574 . 58 ILE CA C 60.70 0.50 1 575 . 58 ILE CB C 39.50 0.50 1 576 . 58 ILE CG1 C 28.30 0.50 1 577 . 58 ILE CG2 C 17.90 0.50 1 578 . 58 ILE CD1 C 14.20 0.50 1 579 . 58 ILE N N 124.30 0.25 1 580 . 59 THR H H 8.70 0.03 1 581 . 59 THR HA H 5.07 0.03 1 582 . 59 THR HB H 3.88 0.03 1 583 . 59 THR HG2 H 0.79 0.03 1 584 . 59 THR C C 172.10 0.50 1 585 . 59 THR CA C 58.50 0.50 1 586 . 59 THR CB C 73.00 0.50 1 587 . 59 THR CG2 C 21.40 0.50 1 588 . 59 THR N N 115.90 0.25 1 589 . 60 LEU H H 9.15 0.03 1 590 . 60 LEU HA H 5.49 0.03 1 591 . 60 LEU HB2 H 1.35 0.03 2 592 . 60 LEU HB3 H 1.99 0.03 2 593 . 60 LEU HG H 1.62 0.03 1 594 . 60 LEU HD1 H 1.07 0.03 2 595 . 60 LEU HD2 H 1.00 0.03 2 596 . 60 LEU C C 174.70 0.50 1 597 . 60 LEU CA C 53.20 0.50 1 598 . 60 LEU CB C 46.90 0.50 1 599 . 60 LEU CG C 28.00 0.50 1 600 . 60 LEU CD1 C 24.40 0.50 2 601 . 60 LEU CD2 C 27.30 0.50 2 602 . 60 LEU N N 120.60 0.25 1 603 . 61 GLU H H 9.68 0.03 1 604 . 61 GLU HA H 5.71 0.03 1 605 . 61 GLU HB2 H 2.25 0.03 2 606 . 61 GLU HB3 H 1.86 0.03 2 607 . 61 GLU HG2 H 2.01 0.03 2 608 . 61 GLU C C 176.00 0.50 1 609 . 61 GLU CA C 52.80 0.50 1 610 . 61 GLU CB C 32.90 0.50 1 611 . 61 GLU CG C 36.30 0.50 1 612 . 61 GLU N N 131.30 0.25 1 613 . 62 THR H H 8.05 0.03 1 614 . 62 THR HA H 5.23 0.03 1 615 . 62 THR HB H 3.98 0.03 1 616 . 62 THR HG2 H 1.21 0.03 1 617 . 62 THR C C 174.10 0.50 1 618 . 62 THR CA C 58.10 0.50 1 619 . 62 THR CB C 70.80 0.50 1 620 . 62 THR CG2 C 22.70 0.50 1 621 . 62 THR N N 116.20 0.25 1 622 . 63 VAL H H 7.49 0.03 1 623 . 63 VAL HA H 3.97 0.03 1 624 . 63 VAL HB H 1.85 0.03 1 625 . 63 VAL HG1 H 1.02 0.03 2 626 . 63 VAL HG2 H 0.22 0.03 2 627 . 63 VAL C C 175.70 0.50 1 628 . 63 VAL CA C 59.20 0.50 1 629 . 63 VAL CB C 38.00 0.50 1 630 . 63 VAL CG1 C 23.30 0.50 2 631 . 63 VAL CG2 C 18.30 0.50 2 632 . 63 VAL N N 112.70 0.25 1 633 . 64 CYS HA H 5.37 0.03 1 634 . 64 CYS HB2 H 3.42 0.03 2 635 . 64 CYS HB3 H 2.78 0.03 2 636 . 64 CYS C C 175.40 0.50 1 637 . 64 CYS CA C 57.50 0.50 1 638 . 64 CYS CB C 48.00 0.50 1 639 . 65 HIS H H 9.40 0.03 1 640 . 65 HIS HA H 4.61 0.03 1 641 . 65 HIS HB2 H 2.51 0.03 2 642 . 65 HIS HB3 H 2.34 0.03 2 643 . 65 HIS HD2 H 6.70 0.03 1 644 . 65 HIS HE1 H 8.68 0.03 1 645 . 65 HIS C C 172.60 0.50 1 646 . 65 HIS CA C 56.10 0.50 1 647 . 65 HIS CB C 33.10 0.50 1 648 . 65 HIS CD2 C 120.60 0.50 1 649 . 65 HIS CE1 C 137.10 0.50 1 650 . 65 HIS N N 117.90 0.25 1 651 . 66 ASP H H 8.32 0.03 1 652 . 66 ASP HA H 4.47 0.03 1 653 . 66 ASP HB2 H 2.36 0.03 2 654 . 66 ASP HB3 H 2.69 0.03 2 655 . 66 ASP C C 174.30 0.50 1 656 . 66 ASP CA C 51.60 0.50 1 657 . 66 ASP CB C 41.40 0.50 1 658 . 66 ASP N N 129.20 0.25 1 659 . 67 PRO HA H 4.54 0.03 1 660 . 67 PRO HB2 H 2.22 0.03 2 661 . 67 PRO HB3 H 2.04 0.03 2 662 . 67 PRO HG2 H 2.08 0.03 2 663 . 67 PRO HD2 H 3.79 0.03 2 664 . 67 PRO C C 177.40 0.50 1 665 . 67 PRO CA C 64.40 0.50 1 666 . 67 PRO CB C 31.90 0.50 1 667 . 67 PRO CG C 26.80 0.50 1 668 . 67 PRO CD C 51.50 0.50 1 669 . 68 LYS H H 8.58 0.03 1 670 . 68 LYS HA H 4.23 0.03 1 671 . 68 LYS HB2 H 1.78 0.03 2 672 . 68 LYS HG2 H 1.44 0.03 2 673 . 68 LYS HD2 H 1.69 0.03 2 674 . 68 LYS HE2 H 2.98 0.03 2 675 . 68 LYS C C 176.50 0.50 1 676 . 68 LYS CA C 57.60 0.50 1 677 . 68 LYS CB C 32.10 0.50 1 678 . 68 LYS CG C 25.20 0.50 1 679 . 68 LYS CD C 28.80 0.50 1 680 . 68 LYS CE C 42.00 0.50 1 681 . 68 LYS N N 122.00 0.25 1 682 . 69 LEU H H 8.02 0.03 1 683 . 69 LEU HA H 4.98 0.03 1 684 . 69 LEU HB2 H 1.75 0.03 2 685 . 69 LEU HG H 1.53 0.03 1 686 . 69 LEU HD1 H 0.94 0.03 2 687 . 69 LEU HD2 H 0.89 0.03 2 688 . 69 LEU C C 176.30 0.50 1 689 . 69 LEU CA C 51.50 0.50 1 690 . 69 LEU CB C 42.60 0.50 1 691 . 69 LEU CG C 26.80 0.50 1 692 . 69 LEU CD1 C 22.90 0.50 2 693 . 69 LEU CD2 C 25.40 0.50 2 694 . 69 LEU N N 120.10 0.25 1 695 . 70 PRO HA H 4.61 0.03 1 696 . 70 PRO HB2 H 1.88 0.03 2 697 . 70 PRO HB3 H 1.73 0.03 2 698 . 70 PRO HG2 H 2.06 0.03 2 699 . 70 PRO HG3 H 1.93 0.03 2 700 . 70 PRO HD2 H 3.91 0.03 2 701 . 70 PRO HD3 H 3.73 0.03 2 702 . 70 PRO C C 175.40 0.50 1 703 . 70 PRO CA C 63.10 0.50 1 704 . 70 PRO CB C 32.30 0.50 1 705 . 70 PRO CG C 27.40 0.50 1 706 . 70 PRO CD C 50.70 0.50 1 707 . 71 TYR H H 9.42 0.03 1 708 . 71 TYR HA H 4.58 0.03 1 709 . 71 TYR HB2 H 2.71 0.03 2 710 . 71 TYR HB3 H 1.83 0.03 2 711 . 71 TYR HD2 H 6.61 0.03 3 712 . 71 TYR HE2 H 6.38 0.03 3 713 . 71 TYR C C 175.20 0.50 1 714 . 71 TYR CA C 58.10 0.50 1 715 . 71 TYR CB C 41.10 0.50 1 716 . 71 TYR CD1 C 132.00 0.50 3 717 . 71 TYR CE1 C 118.30 0.50 3 718 . 71 TYR N N 122.80 0.25 1 719 . 72 HIS H H 8.68 0.03 1 720 . 72 HIS HA H 3.83 0.03 1 721 . 72 HIS HB2 H 3.19 0.03 2 722 . 72 HIS HB3 H 3.27 0.03 2 723 . 72 HIS HD2 H 6.33 0.03 1 724 . 72 HIS HE1 H 8.34 0.03 1 725 . 72 HIS C C 173.20 0.50 1 726 . 72 HIS CA C 57.00 0.50 1 727 . 72 HIS CB C 26.60 0.50 1 728 . 72 HIS CD2 C 119.00 0.50 1 729 . 72 HIS CE1 C 136.40 0.50 1 730 . 72 HIS N N 123.20 0.25 1 731 . 73 ASP H H 8.29 0.03 1 732 . 73 ASP HA H 3.91 0.03 1 733 . 73 ASP HB2 H 2.61 0.03 2 734 . 73 ASP C C 174.60 0.50 1 735 . 73 ASP CA C 56.50 0.50 1 736 . 73 ASP CB C 39.70 0.50 1 737 . 73 ASP N N 105.50 0.25 1 738 . 74 PHE H H 7.85 0.03 1 739 . 74 PHE HA H 4.92 0.03 1 740 . 74 PHE HB2 H 3.14 0.03 2 741 . 74 PHE HB3 H 2.91 0.03 2 742 . 74 PHE HD2 H 7.38 0.03 3 743 . 74 PHE C C 174.80 0.50 1 744 . 74 PHE CA C 57.40 0.50 1 745 . 74 PHE CB C 41.90 0.50 1 746 . 74 PHE N N 118.60 0.25 1 747 . 75 ILE H H 8.59 0.03 1 748 . 75 ILE HA H 4.35 0.03 1 749 . 75 ILE HB H 1.93 0.03 1 750 . 75 ILE HG12 H 1.55 0.03 2 751 . 75 ILE HG13 H 1.35 0.03 2 752 . 75 ILE HG2 H 0.87 0.03 1 753 . 75 ILE HD1 H 0.79 0.03 1 754 . 75 ILE C C 177.40 0.50 1 755 . 75 ILE CA C 59.40 0.50 1 756 . 75 ILE CB C 37.80 0.50 1 757 . 75 ILE CG1 C 27.60 0.50 1 758 . 75 ILE CG2 C 17.60 0.50 1 759 . 75 ILE CD1 C 11.30 0.50 1 760 . 75 ILE N N 121.50 0.25 1 761 . 76 LEU H H 9.47 0.03 1 762 . 76 LEU HA H 4.45 0.03 1 763 . 76 LEU HB2 H 1.85 0.03 2 764 . 76 LEU HB3 H 1.91 0.03 2 765 . 76 LEU HG H 1.92 0.03 1 766 . 76 LEU HD1 H 0.97 0.03 2 767 . 76 LEU HD2 H 0.94 0.03 2 768 . 76 LEU C C 176.80 0.50 1 769 . 76 LEU CA C 54.30 0.50 1 770 . 76 LEU CB C 39.30 0.50 1 771 . 76 LEU CG C 27.60 0.50 1 772 . 76 LEU CD1 C 23.60 0.50 2 773 . 76 LEU CD2 C 26.30 0.50 2 774 . 76 LEU N N 129.50 0.25 1 775 . 77 GLU H H 8.52 0.03 1 776 . 77 GLU HA H 4.31 0.03 1 777 . 77 GLU HB2 H 2.20 0.03 2 778 . 77 GLU HB3 H 1.99 0.03 2 779 . 77 GLU HG2 H 2.26 0.03 2 780 . 77 GLU C C 176.40 0.50 1 781 . 77 GLU CA C 57.20 0.50 1 782 . 77 GLU CB C 30.40 0.50 1 783 . 77 GLU CG C 36.60 0.50 1 784 . 77 GLU N N 124.10 0.25 1 785 . 78 ASP H H 9.31 0.03 1 786 . 78 ASP HA H 4.66 0.03 1 787 . 78 ASP HB2 H 3.30 0.03 2 788 . 78 ASP HB3 H 2.62 0.03 2 789 . 78 ASP C C 175.10 0.50 1 790 . 78 ASP CA C 53.00 0.50 1 791 . 78 ASP CB C 39.90 0.50 1 792 . 78 ASP N N 118.30 0.25 1 793 . 79 ALA H H 7.06 0.03 1 794 . 79 ALA HA H 4.11 0.03 1 795 . 79 ALA HB H 1.42 0.03 1 796 . 79 ALA C C 177.50 0.50 1 797 . 79 ALA CA C 55.10 0.50 1 798 . 79 ALA CB C 19.70 0.50 1 799 . 79 ALA N N 120.00 0.25 1 800 . 80 ALA H H 8.16 0.03 1 801 . 80 ALA HA H 4.21 0.03 1 802 . 80 ALA HB H 1.38 0.03 1 803 . 80 ALA C C 178.30 0.50 1 804 . 80 ALA CA C 52.60 0.50 1 805 . 80 ALA CB C 18.70 0.50 1 806 . 80 ALA N N 116.70 0.25 1 807 . 81 SER H H 8.42 0.03 1 808 . 81 SER HA H 4.65 0.03 1 809 . 81 SER HB2 H 4.51 0.03 2 810 . 81 SER HB3 H 4.26 0.03 2 811 . 81 SER C C 174.60 0.50 1 812 . 81 SER CA C 56.60 0.50 1 813 . 81 SER CB C 65.10 0.50 1 814 . 81 SER N N 117.00 0.25 1 815 . 82 PRO HA H 4.53 0.03 1 816 . 82 PRO HB2 H 2.37 0.03 2 817 . 82 PRO HB3 H 2.02 0.03 2 818 . 82 PRO HG2 H 2.06 0.03 2 819 . 82 PRO HG3 H 2.16 0.03 2 820 . 82 PRO C C 176.80 0.50 1 821 . 82 PRO CA C 64.60 0.50 1 822 . 82 PRO CB C 32.10 0.50 1 823 . 82 PRO CG C 27.40 0.50 1 824 . 82 PRO CD C 50.80 0.50 1 825 . 83 LYS H H 7.47 0.03 1 826 . 83 LYS HA H 4.68 0.03 1 827 . 83 LYS HB2 H 1.63 0.03 2 828 . 83 LYS HG2 H 1.36 0.03 2 829 . 83 LYS HD2 H 1.64 0.03 2 830 . 83 LYS HE2 H 2.92 0.03 2 831 . 83 LYS C C 174.10 0.50 1 832 . 83 LYS CA C 54.20 0.50 1 833 . 83 LYS CB C 36.00 0.50 1 834 . 83 LYS CG C 25.40 0.50 1 835 . 83 LYS CD C 29.00 0.50 1 836 . 83 LYS N N 115.00 0.25 1 837 . 87 LYS HA H 4.75 0.03 1 838 . 87 LYS HB2 H 1.78 0.03 2 839 . 87 LYS HB3 H 1.89 0.03 2 840 . 87 LYS HG2 H 1.62 0.03 2 841 . 87 LYS HD2 H 1.77 0.03 2 842 . 87 LYS HE2 H 2.97 0.03 2 843 . 87 LYS HE3 H 3.07 0.03 2 844 . 87 LYS C C 175.30 0.50 1 845 . 87 LYS CA C 54.30 0.50 1 846 . 87 LYS CB C 35.20 0.50 1 847 . 87 LYS CG C 24.80 0.50 1 848 . 87 LYS CD C 28.50 0.50 1 849 . 88 GLU H H 8.66 0.03 1 850 . 88 GLU HA H 3.37 0.03 1 851 . 88 GLU HB2 H 1.37 0.03 2 852 . 88 GLU HB3 H 1.61 0.03 2 853 . 88 GLU HG2 H 1.70 0.03 2 854 . 88 GLU HG3 H 1.52 0.03 2 855 . 88 GLU C C 175.70 0.50 1 856 . 88 GLU CA C 56.90 0.50 1 857 . 88 GLU CB C 30.10 0.50 1 858 . 88 GLU CG C 36.30 0.50 1 859 . 88 GLU N N 125.20 0.25 1 860 . 89 LYS H H 8.68 0.03 1 861 . 89 LYS HA H 4.27 0.03 1 862 . 89 LYS HB2 H 0.41 0.03 2 863 . 89 LYS HB3 H 0.13 0.03 2 864 . 89 LYS HG2 H 0.50 0.03 2 865 . 89 LYS HG3 H 0.98 0.03 2 866 . 89 LYS HD2 H 0.89 0.03 2 867 . 89 LYS HD3 H 1.26 0.03 2 868 . 89 LYS HE2 H 2.40 0.03 2 869 . 89 LYS HE3 H 2.48 0.03 2 870 . 89 LYS C C 174.60 0.50 1 871 . 89 LYS CA C 52.20 0.50 1 872 . 89 LYS CB C 31.90 0.50 1 873 . 89 LYS CG C 23.40 0.50 1 874 . 89 LYS CD C 27.40 0.50 1 875 . 89 LYS CE C 40.10 0.50 1 876 . 89 LYS N N 126.70 0.25 1 877 . 90 LYS H H 8.21 0.03 1 878 . 90 LYS HA H 4.69 0.03 1 879 . 90 LYS HB2 H 1.73 0.03 2 880 . 90 LYS HG2 H 1.36 0.03 2 881 . 90 LYS HD2 H 1.64 0.03 2 882 . 90 LYS HE2 H 2.92 0.03 2 883 . 90 LYS C C 175.20 0.50 1 884 . 90 LYS CA C 55.90 0.50 1 885 . 90 LYS CB C 33.70 0.50 1 886 . 90 LYS CG C 24.70 0.50 1 887 . 90 LYS CD C 29.20 0.50 1 888 . 90 LYS CE C 42.00 0.50 1 889 . 90 LYS N N 121.40 0.25 1 890 . 91 LYS H H 8.94 0.03 1 891 . 91 LYS HA H 4.83 0.03 1 892 . 91 LYS HB2 H 2.00 0.03 2 893 . 91 LYS HB3 H 1.67 0.03 2 894 . 91 LYS HG2 H 1.52 0.03 2 895 . 91 LYS HG3 H 1.40 0.03 2 896 . 91 LYS HD2 H 1.68 0.03 2 897 . 91 LYS HE2 H 2.87 0.03 2 898 . 91 LYS C C 173.30 0.50 1 899 . 91 LYS CA C 53.50 0.50 1 900 . 91 LYS CB C 34.30 0.50 1 901 . 91 LYS CG C 24.70 0.50 1 902 . 91 LYS CD C 29.30 0.50 1 903 . 91 LYS CE C 41.80 0.50 1 904 . 91 LYS N N 126.00 0.25 1 905 . 92 PRO HA H 4.34 0.03 1 906 . 92 PRO HB2 H 2.31 0.03 2 907 . 92 PRO HB3 H 1.93 0.03 2 908 . 92 PRO HG2 H 2.18 0.03 2 909 . 92 PRO HG3 H 2.00 0.03 2 910 . 92 PRO HD2 H 3.80 0.03 2 911 . 92 PRO HD3 H 3.66 0.03 2 912 . 92 PRO C C 178.10 0.50 1 913 . 92 PRO CA C 64.80 0.50 1 914 . 92 PRO CB C 31.30 0.50 1 915 . 92 PRO CG C 28.00 0.50 1 916 . 92 PRO CD C 50.30 0.50 1 917 . 93 GLY H H 8.78 0.03 1 918 . 93 GLY HA2 H 4.18 0.03 2 919 . 93 GLY HA3 H 3.85 0.03 2 920 . 93 GLY C C 173.80 0.50 1 921 . 93 GLY CA C 45.80 0.50 1 922 . 93 GLY N N 111.90 0.25 1 923 . 94 GLU H H 8.03 0.03 1 924 . 94 GLU HA H 4.92 0.03 1 925 . 94 GLU HB2 H 2.14 0.03 2 926 . 94 GLU HB3 H 2.02 0.03 2 927 . 94 GLU HG2 H 2.16 0.03 2 928 . 94 GLU C C 173.90 0.50 1 929 . 94 GLU CA C 56.00 0.50 1 930 . 94 GLU CB C 33.20 0.50 1 931 . 94 GLU CG C 36.00 0.50 1 932 . 94 GLU N N 118.50 0.25 1 933 . 95 THR H H 8.65 0.03 1 934 . 95 THR HA H 5.07 0.03 1 935 . 95 THR HB H 4.21 0.03 1 936 . 95 THR HG2 H 1.47 0.03 1 937 . 95 THR C C 173.20 0.50 1 938 . 95 THR CA C 62.20 0.50 1 939 . 95 THR CB C 70.50 0.50 1 940 . 95 THR CG2 C 22.60 0.50 1 941 . 95 THR N N 118.90 0.25 1 942 . 96 PHE H H 9.16 0.03 1 943 . 96 PHE HA H 5.41 0.03 1 944 . 96 PHE HB2 H 3.41 0.03 2 945 . 96 PHE HB3 H 3.06 0.03 2 946 . 96 PHE HD2 H 6.98 0.03 3 947 . 96 PHE C C 172.20 0.50 1 948 . 96 PHE CA C 56.70 0.50 1 949 . 96 PHE CB C 41.70 0.50 1 950 . 96 PHE N N 127.10 0.25 1 951 . 97 PHE H H 9.69 0.03 1 952 . 97 PHE HA H 5.53 0.03 1 953 . 97 PHE HB2 H 3.41 0.03 2 954 . 97 PHE HB3 H 3.14 0.03 2 955 . 97 PHE HD2 H 7.21 0.03 3 956 . 97 PHE C C 173.90 0.50 1 957 . 97 PHE CA C 56.60 0.50 1 958 . 97 PHE CB C 41.75 0.50 1 959 . 97 PHE N N 123.50 0.25 1 960 . 100 SER HA H 5.57 0.03 1 961 . 100 SER HB2 H 3.84 0.03 2 962 . 100 SER HB3 H 3.95 0.03 2 963 . 100 SER C C 171.30 0.50 1 964 . 100 SER CA C 57.40 0.50 1 965 . 100 SER CB C 68.50 0.50 1 966 . 101 CYS H H 8.72 0.03 1 967 . 101 CYS HA H 5.38 0.03 1 968 . 101 CYS HB2 H 3.28 0.03 2 969 . 101 CYS HB3 H 2.86 0.03 2 970 . 101 CYS C C 174.80 0.50 1 971 . 101 CYS CA C 54.70 0.50 1 972 . 101 CYS CB C 46.30 0.50 1 973 . 101 CYS N N 110.30 0.25 1 974 . 102 SER H H 8.73 0.03 1 975 . 102 SER HA H 5.01 0.03 1 976 . 102 SER HB2 H 4.08 0.03 2 977 . 102 SER HB3 H 3.87 0.03 2 978 . 102 SER C C 174.20 0.50 1 979 . 102 SER CA C 57.00 0.50 1 980 . 102 SER CB C 63.70 0.50 1 981 . 102 SER N N 113.20 0.25 1 982 . 103 SER H H 7.47 0.03 1 983 . 103 SER HA H 4.89 0.03 1 984 . 103 SER HB2 H 3.95 0.03 2 985 . 103 SER HB3 H 3.99 0.03 2 986 . 103 SER C C 174.30 0.50 1 987 . 103 SER CA C 57.90 0.50 1 988 . 103 SER CB C 66.40 0.50 1 989 . 103 SER N N 115.00 0.25 1 990 . 104 ASP H H 8.88 0.03 1 991 . 104 ASP HA H 5.01 0.03 1 992 . 104 ASP HB2 H 2.65 0.03 2 993 . 104 ASP HB3 H 2.57 0.03 2 994 . 104 ASP C C 177.70 0.50 1 995 . 104 ASP CA C 56.60 0.50 1 996 . 104 ASP CB C 40.70 0.50 1 997 . 104 ASP N N 123.90 0.25 1 998 . 105 GLU H H 9.66 0.03 1 999 . 105 GLU HA H 3.41 0.03 1 1000 . 105 GLU HB2 H 2.35 0.03 2 1001 . 105 GLU HB3 H 2.24 0.03 2 1002 . 105 GLU HG2 H 1.78 0.03 2 1003 . 105 GLU HG3 H 2.08 0.03 2 1004 . 105 GLU C C 177.10 0.50 1 1005 . 105 GLU CA C 58.50 0.50 1 1006 . 105 GLU CB C 28.20 0.50 1 1007 . 105 GLU CG C 39.10 0.50 1 1008 . 105 GLU N N 114.10 0.25 1 1009 . 106 CYS H H 8.16 0.03 1 1010 . 106 CYS HA H 4.52 0.03 1 1011 . 106 CYS HB2 H 3.88 0.03 2 1012 . 106 CYS HB3 H 3.22 0.03 2 1013 . 106 CYS C C 174.00 0.50 1 1014 . 106 CYS CA C 59.00 0.50 1 1015 . 106 CYS CB C 46.90 0.50 1 1016 . 106 CYS N N 116.60 0.25 1 1017 . 107 ASN H H 8.07 0.03 1 1018 . 107 ASN HA H 4.30 0.03 1 1019 . 107 ASN HB2 H 3.13 0.03 2 1020 . 107 ASN HB3 H 2.14 0.03 2 1021 . 107 ASN C C 170.70 0.50 1 1022 . 107 ASN CA C 52.50 0.50 1 1023 . 107 ASN CB C 36.20 0.50 1 1024 . 107 ASN N N 116.70 0.25 1 1025 . 108 ASP H H 7.43 0.03 1 1026 . 108 ASP HA H 4.66 0.03 1 1027 . 108 ASP HB2 H 2.85 0.03 2 1028 . 108 ASP HB3 H 2.45 0.03 2 1029 . 108 ASP C C 174.90 0.50 1 1030 . 108 ASP CA C 55.00 0.50 1 1031 . 108 ASP CB C 43.70 0.50 1 1032 . 108 ASP N N 111.50 0.25 1 1033 . 109 ASN H H 7.25 0.03 1 1034 . 109 ASN HA H 5.15 0.03 1 1035 . 109 ASN HB2 H 2.79 0.03 2 1036 . 109 ASN HB3 H 2.55 0.03 2 1037 . 109 ASN C C 173.00 0.50 1 1038 . 109 ASN CA C 52.00 0.50 1 1039 . 109 ASN CB C 39.40 0.50 1 1040 . 109 ASN N N 115.10 0.25 1 1041 . 110 ILE HA H 4.09 0.03 1 1042 . 110 ILE HB H 1.74 0.03 1 1043 . 110 ILE HG12 H 1.25 0.03 2 1044 . 110 ILE HG13 H 0.92 0.03 2 1045 . 110 ILE HG2 H 0.40 0.03 1 1046 . 110 ILE HD1 H 0.62 0.03 1 1047 . 110 ILE CA C 60.50 0.50 1 1048 . 110 ILE CB C 38.20 0.50 1 1049 . 110 ILE CG1 C 27.20 0.50 1 1050 . 110 ILE CG2 C 20.20 0.50 1 1051 . 110 ILE CD1 C 14.30 0.50 1 1052 . 111 ILE HA H 4.12 0.03 1 1053 . 111 ILE HB H 1.81 0.03 1 1054 . 111 ILE HG12 H 0.92 0.03 2 1055 . 111 ILE HG13 H 1.39 0.03 2 1056 . 111 ILE HG2 H 0.76 0.03 1 1057 . 111 ILE HD1 H 0.72 0.03 1 1058 . 111 ILE C C 174.90 0.50 1 1059 . 111 ILE CA C 61.10 0.50 1 1060 . 111 ILE CB C 39.80 0.50 1 1061 . 111 ILE CG1 C 27.60 0.50 1 1062 . 111 ILE CG2 C 18.00 0.50 1 1063 . 111 ILE CD1 C 13.80 0.50 1 1064 . 112 PHE H H 8.66 0.03 1 1065 . 112 PHE HA H 4.38 0.03 1 1066 . 112 PHE HB2 H 2.62 0.03 2 1067 . 112 PHE HB3 H 2.51 0.03 2 1068 . 112 PHE HZ H 5.72 0.03 1 1069 . 112 PHE HD2 H 6.44 0.03 3 1070 . 112 PHE HE2 H 6.03 0.03 3 1071 . 112 PHE C C 176.10 0.50 1 1072 . 112 PHE CA C 58.80 0.50 1 1073 . 112 PHE CB C 39.80 0.50 1 1074 . 112 PHE CZ C 128.00 0.50 1 1075 . 112 PHE CD1 C 131.80 0.50 3 1076 . 112 PHE CE1 C 130.60 0.50 3 1077 . 112 PHE N N 124.70 0.25 1 1078 . 113 SER H H 8.21 0.03 1 1079 . 113 SER HA H 4.54 0.03 1 1080 . 113 SER HB2 H 3.78 0.03 2 1081 . 113 SER HB3 H 3.88 0.03 2 1082 . 113 SER C C 173.60 0.50 1 1083 . 113 SER CA C 57.70 0.50 1 1084 . 113 SER CB C 64.50 0.50 1 1085 . 113 SER N N 114.70 0.25 1 1086 . 114 GLU H H 8.71 0.03 1 1087 . 114 GLU HA H 4.27 0.03 1 1088 . 114 GLU HB2 H 2.04 0.03 2 1089 . 114 GLU HB3 H 1.87 0.03 2 1090 . 114 GLU HG2 H 2.19 0.03 2 1091 . 114 GLU C C 176.10 0.50 1 1092 . 114 GLU CA C 56.80 0.50 1 1093 . 114 GLU CB C 30.50 0.50 1 1094 . 114 GLU CG C 36.60 0.50 1 1095 . 114 GLU N N 123.90 0.25 1 1096 . 115 GLU H H 8.38 0.03 1 1097 . 115 GLU HA H 4.20 0.03 1 1098 . 115 GLU HB2 H 1.83 0.03 2 1099 . 115 GLU HB3 H 1.91 0.03 2 1100 . 115 GLU HG2 H 2.11 0.03 2 1101 . 115 GLU C C 175.90 0.50 1 1102 . 115 GLU CA C 56.60 0.50 1 1103 . 115 GLU CB C 30.20 0.50 1 1104 . 115 GLU CG C 36.00 0.50 1 1105 . 115 GLU N N 121.30 0.25 1 1106 . 116 TYR H H 8.13 0.03 1 1107 . 116 TYR HA H 4.57 0.03 1 1108 . 116 TYR HB2 H 3.10 0.03 2 1109 . 116 TYR HB3 H 2.92 0.03 2 1110 . 116 TYR HD2 H 7.09 0.03 3 1111 . 116 TYR HE2 H 6.81 0.03 3 1112 . 116 TYR C C 175.30 0.50 1 1113 . 116 TYR CA C 57.80 0.50 1 1114 . 116 TYR CB C 38.70 0.50 1 1115 . 116 TYR CD1 C 133.30 0.50 3 1116 . 116 TYR CE1 C 118.40 0.50 3 1117 . 116 TYR N N 120.90 0.25 1 1118 . 117 ASN H H 8.30 0.03 1 1119 . 117 ASN HA H 4.72 0.03 1 1120 . 117 ASN HB2 H 2.83 0.03 2 1121 . 117 ASN HB3 H 2.68 0.03 2 1122 . 117 ASN C C 175.20 0.50 1 1123 . 117 ASN CA C 53.20 0.50 1 1124 . 117 ASN CB C 39.10 0.50 1 1125 . 117 ASN N N 120.90 0.25 1 1126 . 118 THR H H 8.13 0.03 1 1127 . 118 THR HA H 4.32 0.03 1 1128 . 118 THR HB H 4.28 0.03 1 1129 . 118 THR HG2 H 1.18 0.03 1 1130 . 118 THR C C 174.60 0.50 1 1131 . 118 THR CA C 62.10 0.50 1 1132 . 118 THR CB C 69.60 0.50 1 1133 . 118 THR CG2 C 21.40 0.50 1 1134 . 118 THR N N 114.40 0.25 1 1135 . 119 SER H H 8.26 0.03 1 1136 . 119 SER HA H 4.46 0.03 1 1137 . 119 SER HB2 H 3.84 0.03 2 1138 . 119 SER C C 173.70 0.50 1 1139 . 119 SER CA C 58.50 0.50 1 1140 . 119 SER CB C 63.90 0.50 1 1141 . 119 SER N N 117.80 0.25 1 1142 . 120 ASN H H 8.38 0.03 1 1143 . 120 ASN HA H 5.00 0.03 1 1144 . 120 ASN HB2 H 2.81 0.03 2 1145 . 120 ASN HB3 H 2.65 0.03 2 1146 . 120 ASN C C 173.10 0.50 1 1147 . 120 ASN CA C 51.60 0.50 1 1148 . 120 ASN CB C 39.00 0.50 1 1149 . 120 ASN N N 121.60 0.25 1 1150 . 121 PRO HA H 4.44 0.03 1 1151 . 121 PRO HB2 H 2.01 0.03 2 1152 . 121 PRO HB3 H 2.22 0.03 2 1153 . 121 PRO HG2 H 2.00 0.03 2 1154 . 121 PRO HD2 H 3.72 0.03 2 1155 . 121 PRO C C 175.80 0.50 1 1156 . 121 PRO CA C 63.50 0.50 1 1157 . 121 PRO CB C 32.00 0.50 1 1158 . 121 PRO CG C 27.00 0.50 1 1159 . 121 PRO CD C 50.50 0.50 1 1160 . 122 ASP H H 7.93 0.03 1 1161 . 122 ASP HA H 4.36 0.03 1 1162 . 122 ASP HB2 H 2.57 0.03 2 1163 . 122 ASP HB3 H 2.67 0.03 2 1164 . 122 ASP C C 180.60 0.50 1 1165 . 122 ASP CA C 55.70 0.50 1 1166 . 122 ASP CB C 41.80 0.50 1 1167 . 122 ASP N N 125.60 0.25 1 stop_ save_