data_4295 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Titin Module A71 from Human Cardiac Muscle ; _BMRB_accession_number 4295 _BMRB_flat_file_name bmr4295.str _Entry_type original _Submission_date 1999-01-18 _Accession_date 1999-01-19 _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 Muhle-Goll C. . . 2 Pastore A. . . 3 Nilges M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 615 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-12 original author . stop_ _Original_release_date 1999-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Muhle-Goll, C., Pastore, A., and Nilges, M., "The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains," Structure 6, 1291-1302 (1998). ; _Citation_title ; The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98455511 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Muhle-Goll C. . . 2 Pastore A. . . 3 Nilges M. . . stop_ _Journal_abbreviation Structure _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1291 _Page_last 1302 _Year 1998 _Details . loop_ _Keyword connectin 'fibronectin type III' titin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref2 _Saveframe_category citation _Citation_full ; Muhle-Goll C., Nilges M., Pastore A., "1H and 15N NMR Resonance Assignments and Secondary Structure of Titin Type I domains," J. Biomol. NMR 9, (1997) ; _Citation_title '1H and 15N NMR resonance assignments and secondary structure of titin type I domains.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9081541 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Muhle-Goll C . . 2 Nilges M . . 3 Pastore A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 9 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2 _Page_last 10 _Year 1997 _Details ; Titin/connectin is a giant muscle protein with a highly modular architecture consisting of multiple repeats of two sequence motifs, named type I and type II. Type I modules have been suggested to be intracellular members of the fibronectin type III (Fn3) domain family. Along the titin sequence they are exclusively present in the region of the molecule located in the sarcomere A-band. This region has been shown to interact with myosin and C-protein. One of the most noticeable features of type I modules is that they are particularly rich in semiconserved prolines, since these residues account for about 8% of their sequence. We have determined the secondary structure of a representative type I domain (A71) by 15N and 1H NMR. We show that the type I domains of titin have the Fn3 fold as proposed, consisting of a three- and a four-stranded beta-sheet. When the two sheets are placed on top of each other to form the beta-sandwich characteristic of the Fn3 fold, 8 out of 10 prolines are found on the same side of the molecule and form an exposed hydrophobic patch. This suggests that the semiconserved prolines might be relevant for the function of type I modules, providing a surface for binding to other A-band proteins. The secondary structure of A71 was structurally aligned to other extracellular Fn3 modules of known 3D structure. The alignment shows that titin type I modules have closest similarity to the first Fn3 domain of Drosophila neuroglian. ; save_ ################################## # Molecular system description # ################################## save_Titin _Saveframe_category molecular_system _Mol_system_name 'Titin type I domain' _Abbreviation_common Titin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Titin_type_I_domain-A71 $Titin_type_I_domain-A71 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'muscle protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Titin_type_I_domain-A71 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Titin type I domain' _Abbreviation_common Titin _Molecular_mass 12458 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; MHHHHHHSSPIDPPGKPVPL NITRHTVTLKWAKPEYTGGF KITSYIVEKRDLPNGRWLKA NFSNILENEFTVSGLTEDAA YEFRVIAKNAAGAISPPSEP SDAITCRDDVEA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 SER 9 SER 10 PRO 11 ILE 12 ASP 13 PRO 14 PRO 15 GLY 16 LYS 17 PRO 18 VAL 19 PRO 20 LEU 21 ASN 22 ILE 23 THR 24 ARG 25 HIS 26 THR 27 VAL 28 THR 29 LEU 30 LYS 31 TRP 32 ALA 33 LYS 34 PRO 35 GLU 36 TYR 37 THR 38 GLY 39 GLY 40 PHE 41 LYS 42 ILE 43 THR 44 SER 45 TYR 46 ILE 47 VAL 48 GLU 49 LYS 50 ARG 51 ASP 52 LEU 53 PRO 54 ASN 55 GLY 56 ARG 57 TRP 58 LEU 59 LYS 60 ALA 61 ASN 62 PHE 63 SER 64 ASN 65 ILE 66 LEU 67 GLU 68 ASN 69 GLU 70 PHE 71 THR 72 VAL 73 SER 74 GLY 75 LEU 76 THR 77 GLU 78 ASP 79 ALA 80 ALA 81 TYR 82 GLU 83 PHE 84 ARG 85 VAL 86 ILE 87 ALA 88 LYS 89 ASN 90 ALA 91 ALA 92 GLY 93 ALA 94 ILE 95 SER 96 PRO 97 PRO 98 SER 99 GLU 100 PRO 101 SER 102 ASP 103 ALA 104 ILE 105 THR 106 CYS 107 ARG 108 ASP 109 ASP 110 VAL 111 GLU 112 ALA stop_ _Sequence_homology_query_date . _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 PDB 1BPV 'Titin Module A71 From Human Cardiac Muscle, Nmr, 50 Structures' 100.00 112 100.00 100.00 4.22e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue _Organelle $Titin_type_I_domain-A71 Human 9606 . Eukaryota Homo sapiens heart muscle sarcomere stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Titin_type_I_domain-A71 'recombinant technology' 'E. coli' Escherichia coli Bl21 plasmid pLysS stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Titin_type_I_domain-A71 1.2 mM '[U-90% 15N]' NaCl 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_3D_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.2 na temperature 310 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; Some residues showed two sets of resonances indicative of a second minor conformational species ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Titin_type_I_domain-A71 _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 . 9 SER H H 8.11 0.02 1 2 . 9 SER HA H 4.81 0.02 1 3 . 9 SER HB2 H 3.87 0.02 1 4 . 9 SER HB3 H 3.87 0.02 1 5 . 10 PRO HA H 4.45 0.02 1 6 . 10 PRO HB2 H 2.22 0.02 1 7 . 10 PRO HB3 H 2.22 0.02 1 8 . 10 PRO HG2 H 2.58 0.02 1 9 . 10 PRO HG3 H 2.58 0.02 1 10 . 10 PRO HD2 H 3.79 0.02 1 11 . 10 PRO HD3 H 3.79 0.02 1 12 . 11 ILE H H 7.27 0.02 1 13 . 11 ILE HA H 3.98 0.02 1 14 . 11 ILE HB H 1.30 0.02 1 15 . 11 ILE HG12 H 0.65 0.02 1 16 . 11 ILE HG13 H 0.65 0.02 1 17 . 11 ILE HG2 H 0.84 0.02 1 18 . 11 ILE HD1 H 0.48 0.02 1 19 . 11 ILE N N 115.19 0.05 1 20 . 12 ASP H H 7.98 0.02 1 21 . 12 ASP HA H 4.80 0.02 1 22 . 12 ASP HB2 H 2.89 0.02 2 23 . 12 ASP HB3 H 2.60 0.02 2 24 . 12 ASP N N 126.78 0.05 1 25 . 13 PRO HA H 4.75 0.02 1 26 . 13 PRO HB2 H 2.02 0.02 1 27 . 13 PRO HB3 H 1.74 0.02 1 28 . 13 PRO HG2 H 1.85 0.02 1 29 . 13 PRO HG3 H 1.85 0.02 1 30 . 13 PRO HD2 H 3.90 0.02 1 31 . 13 PRO HD3 H 3.61 0.02 1 32 . 14 PRO HA H 4.33 0.02 1 33 . 14 PRO HB2 H 2.38 0.02 2 34 . 14 PRO HB3 H 2.25 0.02 2 35 . 14 PRO HG2 H 1.76 0.02 2 36 . 14 PRO HG3 H 1.62 0.02 2 37 . 14 PRO HD2 H 4.09 0.02 2 38 . 14 PRO HD3 H 3.36 0.02 2 39 . 15 GLY H H 8.42 0.02 1 40 . 15 GLY HA2 H 3.98 0.02 1 41 . 15 GLY HA3 H 3.72 0.02 1 42 . 15 GLY N N 106.02 0.05 1 43 . 16 LYS H H 7.45 0.02 1 44 . 16 LYS HA H 4.43 0.02 1 45 . 16 LYS HB2 H 1.74 0.02 2 46 . 16 LYS HB3 H 1.65 0.02 2 47 . 16 LYS HG2 H 1.35 0.02 2 48 . 16 LYS HG3 H 1.17 0.02 2 49 . 16 LYS HD2 H 1.58 0.02 1 50 . 16 LYS HD3 H 1.58 0.02 1 51 . 16 LYS HE2 H 3.04 0.02 1 52 . 16 LYS HE3 H 3.04 0.02 1 53 . 16 LYS N N 118.90 0.05 1 54 . 17 PRO HA H 5.16 0.02 1 55 . 17 PRO HB2 H 2.10 0.02 2 56 . 17 PRO HB3 H 1.86 0.02 2 57 . 17 PRO HG2 H 1.99 0.02 2 58 . 17 PRO HG3 H 1.64 0.02 2 59 . 17 PRO HD2 H 4.18 0.02 2 60 . 17 PRO HD3 H 3.92 0.02 2 61 . 18 VAL H H 9.00 0.02 1 62 . 18 VAL HA H 4.75 0.02 1 63 . 18 VAL HB H 2.08 0.02 1 64 . 18 VAL HG1 H 0.94 0.02 2 65 . 18 VAL HG2 H 0.90 0.02 2 66 . 18 VAL N N 118.09 0.05 1 67 . 19 PRO HA H 5.03 0.02 1 68 . 19 PRO HB2 H 1.76 0.02 2 69 . 19 PRO HB3 H 2.07 0.02 2 70 . 19 PRO HG2 H 1.86 0.02 2 71 . 19 PRO HG3 H 2.42 0.02 2 72 . 19 PRO HD2 H 3.93 0.02 2 73 . 19 PRO HD3 H 3.74 0.02 2 74 . 20 LEU H H 9.13 0.02 1 75 . 20 LEU HA H 4.35 0.02 1 76 . 20 LEU HB2 H 1.46 0.02 2 77 . 20 LEU HB3 H 1.27 0.02 2 78 . 20 LEU HG H 1.27 0.02 1 79 . 20 LEU HD1 H 0.90 0.02 2 80 . 20 LEU HD2 H 0.70 0.02 2 81 . 20 LEU N N 124.69 0.05 1 82 . 21 ASN H H 7.31 0.02 1 83 . 21 ASN HA H 4.76 0.02 1 84 . 21 ASN HB2 H 2.70 0.02 2 85 . 21 ASN HB3 H 2.31 0.02 2 86 . 21 ASN HD21 H 6.68 0.02 2 87 . 21 ASN HD22 H 7.54 0.02 2 88 . 21 ASN N N 114.71 0.05 1 89 . 21 ASN ND2 N 113.42 0.02 1 90 . 22 ILE H H 8.40 0.02 1 91 . 22 ILE HA H 4.56 0.02 1 92 . 22 ILE HB H 1.70 0.02 1 93 . 22 ILE HG12 H 1.56 0.02 1 94 . 22 ILE HG13 H 1.56 0.02 1 95 . 22 ILE HG2 H 1.26 0.02 1 96 . 22 ILE HD1 H 0.99 0.02 1 97 . 22 ILE N N 127.43 0.05 1 98 . 23 THR H H 8.90 0.02 1 99 . 23 THR HA H 4.86 0.02 1 100 . 23 THR HB H 4.57 0.02 1 101 . 23 THR HG2 H 1.09 0.02 1 102 . 23 THR N N 118.73 0.05 1 103 . 24 ARG H H 7.84 0.02 1 104 . 24 ARG HA H 3.47 0.02 1 105 . 24 ARG HB2 H 1.39 0.02 2 106 . 24 ARG HB3 H 1.35 0.02 2 107 . 24 ARG HG2 H 1.23 0.02 2 108 . 24 ARG HG3 H 1.05 0.02 2 109 . 24 ARG HD2 H 3.02 0.02 2 110 . 24 ARG HD3 H 2.99 0.02 2 111 . 24 ARG N N 113.75 0.05 1 112 . 25 HIS H H 7.10 0.02 1 113 . 25 HIS HA H 5.10 0.02 1 114 . 25 HIS HB2 H 3.62 0.02 2 115 . 25 HIS HB3 H 2.89 0.02 2 116 . 25 HIS HE1 H 7.32 0.02 2 117 . 25 HIS HD2 H 8.80 0.02 2 118 . 25 HIS N N 107.15 0.05 1 119 . 26 THR H H 7.37 0.02 1 120 . 26 THR HA H 5.51 0.02 1 121 . 26 THR HB H 3.86 0.02 1 122 . 26 THR HG2 H 0.94 0.02 1 123 . 26 THR N N 110.69 0.05 1 124 . 27 VAL H H 8.03 0.02 1 125 . 27 VAL HA H 4.56 0.02 1 126 . 27 VAL HB H 1.45 0.02 1 127 . 27 VAL HG1 H 0.86 0.02 2 128 . 27 VAL HG2 H 0.66 0.02 2 129 . 27 VAL N N 116.96 0.05 1 130 . 28 THR H H 8.91 0.02 1 131 . 28 THR HA H 4.89 0.02 1 132 . 28 THR HB H 3.74 0.02 1 133 . 28 THR HG2 H 1.03 0.02 1 134 . 28 THR N N 126.14 0.05 1 135 . 29 LEU H H 9.09 0.02 1 136 . 29 LEU HA H 5.17 0.02 1 137 . 29 LEU HB2 H 1.94 0.02 2 138 . 29 LEU HB3 H 1.44 0.02 2 139 . 29 LEU HG H 1.33 0.02 1 140 . 29 LEU HD1 H 0.39 0.02 2 141 . 29 LEU HD2 H 0.31 0.02 2 142 . 29 LEU N N 130.00 0.05 1 143 . 30 LYS H H 8.53 0.02 1 144 . 30 LYS HA H 4.66 0.02 1 145 . 30 LYS HB2 H 1.46 0.02 1 146 . 30 LYS HB3 H 1.46 0.02 1 147 . 30 LYS HG2 H 1.29 0.02 2 148 . 30 LYS HG3 H 1.20 0.02 2 149 . 30 LYS HD2 H 1.45 0.02 1 150 . 30 LYS HD3 H 1.45 0.02 1 151 . 30 LYS HE2 H 2.70 0.02 1 152 . 30 LYS HE3 H 2.70 0.02 1 153 . 30 LYS N N 118.73 0.05 1 154 . 31 TRP H H 6.97 0.02 1 155 . 31 TRP HA H 4.91 0.02 1 156 . 31 TRP HB2 H 3.07 0.02 2 157 . 31 TRP HB3 H 2.85 0.02 2 158 . 31 TRP HD1 H 6.49 0.02 1 159 . 31 TRP HE1 H 5.81 0.02 1 160 . 31 TRP HZ2 H 6.60 0.02 1 161 . 31 TRP HH2 H 6.99 0.02 1 162 . 31 TRP HZ3 H 6.59 0.02 1 163 . 31 TRP HE3 H 6.73 0.02 1 164 . 31 TRP N N 120.51 0.05 1 165 . 31 TRP NE1 N 124.69 0.02 1 166 . 32 ALA H H 8.41 0.02 1 167 . 32 ALA HA H 4.33 0.02 1 168 . 32 ALA HB H 1.36 0.02 1 169 . 32 ALA N N 122.76 0.05 1 170 . 33 LYS H H 8.40 0.02 1 171 . 33 LYS HA H 4.36 0.02 1 172 . 33 LYS HB2 H 1.58 0.02 1 173 . 33 LYS HB3 H 1.58 0.02 1 174 . 33 LYS HG2 H 1.34 0.02 2 175 . 33 LYS HG3 H 1.18 0.02 2 176 . 33 LYS HD2 H 1.58 0.02 1 177 . 33 LYS HD3 H 1.58 0.02 1 178 . 33 LYS HE2 H 3.06 0.02 1 179 . 33 LYS HE3 H 3.06 0.02 1 180 . 33 LYS N N 122.92 0.05 1 181 . 34 PRO HA H 4.26 0.02 1 182 . 34 PRO HB2 H 2.38 0.02 1 183 . 34 PRO HB3 H 2.38 0.02 1 184 . 34 PRO HD2 H 4.11 0.02 2 185 . 34 PRO HD3 H 3.47 0.02 2 186 . 35 GLU H H 8.65 0.02 1 187 . 35 GLU HA H 4.05 0.02 1 188 . 35 GLU HB2 H 2.07 0.02 1 189 . 35 GLU HB3 H 2.07 0.02 1 190 . 35 GLU HG2 H 2.31 0.02 2 191 . 35 GLU HG3 H 2.19 0.02 2 192 . 35 GLU N N 124.85 0.05 1 193 . 36 TYR H H 8.19 0.02 1 194 . 36 TYR HA H 4.79 0.02 1 195 . 36 TYR HB2 H 2.95 0.02 2 196 . 36 TYR HB3 H 2.85 0.02 2 197 . 36 TYR HD1 H 7.10 0.02 1 198 . 36 TYR HD2 H 7.10 0.02 1 199 . 36 TYR HE1 H 6.75 0.02 1 200 . 36 TYR HE2 H 6.75 0.02 1 201 . 36 TYR N N 119.86 0.05 1 202 . 37 THR H H 8.29 0.02 1 203 . 37 THR HA H 4.37 0.02 1 204 . 37 THR HB H 4.66 0.02 1 205 . 37 THR HG2 H 0.96 0.02 1 206 . 37 THR N N 116.80 0.05 1 207 . 38 GLY H H 5.94 0.02 1 208 . 38 GLY HA2 H 3.85 0.02 1 209 . 38 GLY HA3 H 3.53 0.02 1 210 . 38 GLY N N 109.40 0.05 1 211 . 39 GLY H H 7.94 0.02 1 212 . 39 GLY HA2 H 3.87 0.02 1 213 . 39 GLY HA3 H 3.35 0.02 1 214 . 39 GLY N N 106.83 0.05 1 215 . 40 PHE H H 6.73 0.02 1 216 . 40 PHE HA H 4.70 0.02 1 217 . 40 PHE HB2 H 3.10 0.02 2 218 . 40 PHE HB3 H 2.52 0.02 2 219 . 40 PHE HD1 H 7.13 0.02 1 220 . 40 PHE HD2 H 7.13 0.02 1 221 . 40 PHE HE1 H 7.28 0.02 1 222 . 40 PHE HE2 H 7.28 0.02 1 223 . 40 PHE HZ H 7.35 0.02 1 224 . 40 PHE N N 116.32 0.05 1 225 . 41 LYS H H 8.74 0.02 1 226 . 41 LYS HA H 4.17 0.02 1 227 . 41 LYS HB2 H 1.73 0.02 1 228 . 41 LYS HB3 H 1.73 0.02 1 229 . 41 LYS HG2 H 1.46 0.02 1 230 . 41 LYS HG3 H 1.41 0.02 1 231 . 41 LYS HD2 H 1.71 0.02 1 232 . 41 LYS HD3 H 1.71 0.02 1 233 . 41 LYS HE2 H 2.94 0.02 1 234 . 41 LYS HE3 H 2.94 0.02 1 235 . 41 LYS N N 122.28 0.05 1 236 . 42 ILE H H 8.54 0.02 1 237 . 42 ILE HA H 4.13 0.02 1 238 . 42 ILE HB H 1.93 0.02 1 239 . 42 ILE HG12 H 1.28 0.02 1 240 . 42 ILE HG13 H 1.28 0.02 1 241 . 42 ILE HG2 H 0.39 0.02 1 242 . 42 ILE HD1 H 0.66 0.02 1 243 . 42 ILE N N 122.44 0.05 1 244 . 43 THR H H 8.55 0.02 1 245 . 43 THR HA H 4.30 0.02 1 246 . 43 THR HB H 4.03 0.02 1 247 . 43 THR HG2 H 1.00 0.02 1 248 . 43 THR N N 120.02 0.05 1 249 . 44 SER H H 7.25 0.02 1 250 . 44 SER HA H 4.79 0.02 1 251 . 44 SER HB2 H 3.75 0.02 2 252 . 44 SER HB3 H 3.57 0.02 2 253 . 44 SER N N 114.07 0.05 1 254 . 45 TYR H H 8.53 0.02 1 255 . 45 TYR HA H 5.40 0.02 1 256 . 45 TYR HB2 H 2.64 0.02 2 257 . 45 TYR HB3 H 2.53 0.02 2 258 . 45 TYR HD1 H 6.72 0.02 1 259 . 45 TYR HD2 H 6.72 0.02 1 260 . 45 TYR HE1 H 7.01 0.02 1 261 . 45 TYR HE2 H 7.01 0.02 1 262 . 45 TYR N N 118.73 0.05 1 263 . 46 ILE H H 9.13 0.02 1 264 . 46 ILE HA H 4.18 0.02 1 265 . 46 ILE HB H 1.47 0.02 1 266 . 46 ILE HG2 H 0.80 0.02 1 267 . 46 ILE HG12 H 1.31 0.02 1 268 . 46 ILE HG13 H 0.97 0.02 1 269 . 46 ILE HD1 H 0.65 0.02 1 270 . 46 ILE N N 123.08 0.05 1 271 . 47 VAL H H 8.03 0.02 1 272 . 47 VAL HA H 4.44 0.02 1 273 . 47 VAL HB H 1.47 0.02 1 274 . 47 VAL HG1 H 0.80 0.02 2 275 . 47 VAL HG2 H 0.37 0.02 2 276 . 47 VAL N N 126.62 0.05 1 277 . 48 GLU H H 9.07 0.02 1 278 . 48 GLU HA H 5.26 0.02 1 279 . 48 GLU HB2 H 1.72 0.02 2 280 . 48 GLU HB3 H 1.46 0.02 2 281 . 48 GLU HG2 H 1.93 0.02 2 282 . 48 GLU HG3 H 1.75 0.02 2 283 . 48 GLU N N 125.98 0.05 1 284 . 49 LYS H H 9.56 0.02 1 285 . 49 LYS HA H 5.56 0.02 1 286 . 49 LYS HB2 H 1.71 0.02 1 287 . 49 LYS HB3 H 1.56 0.02 1 288 . 49 LYS HG2 H 1.40 0.02 1 289 . 49 LYS HG3 H 1.38 0.02 1 290 . 49 LYS HD2 H 1.71 0.02 1 291 . 49 LYS HD3 H 1.71 0.02 1 292 . 49 LYS HE2 H 2.97 0.02 1 293 . 49 LYS HE3 H 2.97 0.02 1 294 . 49 LYS N N 120.18 0.05 1 295 . 50 ARG H H 8.43 0.02 1 296 . 50 ARG HA H 4.28 0.02 1 297 . 50 ARG HB2 H 0.43 0.02 2 298 . 50 ARG HB3 H -0.25 0.02 2 299 . 50 ARG HG2 H 0.14 0.02 2 300 . 50 ARG HG3 H 0.23 0.02 2 301 . 50 ARG HD2 H 2.14 0.02 2 302 . 50 ARG HD3 H 0.72 0.02 2 303 . 50 ARG HH11 H 6.30 0.02 1 304 . 50 ARG HH12 H 6.30 0.02 1 305 . 50 ARG HH21 H 6.11 0.02 1 306 . 50 ARG HH22 H 6.11 0.02 1 307 . 50 ARG HE H 6.93 0.02 1 308 . 50 ARG N N 122.76 0.05 1 309 . 50 ARG NE N 108.60 0.02 1 310 . 51 ASP H H 8.57 0.02 1 311 . 51 ASP HA H 4.35 0.02 1 312 . 51 ASP HB2 H 2.45 0.02 2 313 . 51 ASP HB3 H 2.29 0.02 2 314 . 51 ASP N N 125.33 0.05 1 315 . 52 LEU H H 7.71 0.02 1 316 . 52 LEU HA H 4.18 0.02 1 317 . 52 LEU HB2 H 1.24 0.02 2 318 . 52 LEU HB3 H 1.09 0.02 2 319 . 52 LEU HG H 1.24 0.02 1 320 . 52 LEU HD1 H 0.59 0.02 2 321 . 52 LEU HD2 H 0.46 0.02 2 322 . 52 LEU N N 122.60 0.05 1 323 . 53 PRO HA H 4.30 0.02 1 324 . 53 PRO HB2 H 2.24 0.02 1 325 . 53 PRO HB3 H 2.24 0.02 1 326 . 53 PRO HG2 H 1.87 0.02 2 327 . 53 PRO HG3 H 1.72 0.02 2 328 . 53 PRO HD2 H 3.49 0.02 2 329 . 53 PRO HD3 H 3.39 0.02 2 330 . 54 ASN H H 8.34 0.02 1 331 . 54 ASN HA H 4.95 0.02 1 332 . 54 ASN HB2 H 2.94 0.02 2 333 . 54 ASN HB3 H 2.58 0.02 2 334 . 54 ASN HD21 H 7.53 0.02 2 335 . 54 ASN HD22 H 6.91 0.02 2 336 . 54 ASN N N 119.38 0.05 1 337 . 54 ASN ND2 N 114.07 0.02 1 338 . 55 GLY H H 8.07 0.02 1 339 . 55 GLY HA2 H 4.01 0.02 1 340 . 55 GLY HA3 H 4.01 0.02 1 341 . 55 GLY N N 110.20 0.05 1 342 . 56 ARG H H 8.04 0.02 1 343 . 56 ARG HA H 4.44 0.02 1 344 . 56 ARG HB2 H 1.82 0.02 1 345 . 56 ARG HB3 H 1.82 0.02 1 346 . 56 ARG HG2 H 1.66 0.02 1 347 . 56 ARG HG3 H 1.66 0.02 1 348 . 56 ARG HD2 H 3.19 0.02 1 349 . 56 ARG HD3 H 3.19 0.02 1 350 . 56 ARG N N 120.02 0.05 1 351 . 57 TRP H H 7.89 0.02 1 352 . 57 TRP HA H 4.43 0.02 1 353 . 57 TRP HB2 H 2.95 0.02 2 354 . 57 TRP HB3 H 2.85 0.02 2 355 . 57 TRP HD1 H 7.25 0.02 1 356 . 57 TRP HE1 H 9.93 0.02 1 357 . 57 TRP HZ2 H 7.33 0.02 1 358 . 57 TRP HH2 H 6.71 0.02 1 359 . 57 TRP HZ3 H 6.78 0.02 1 360 . 57 TRP HE3 H 7.08 0.02 1 361 . 57 TRP N N 122.28 0.05 1 362 . 57 TRP NE1 N 130.00 0.02 1 363 . 58 LEU H H 9.20 0.02 1 364 . 58 LEU HA H 4.81 0.02 1 365 . 58 LEU HB2 H 1.74 0.02 2 366 . 58 LEU HB3 H 1.63 0.02 2 367 . 58 LEU HG H 1.74 0.02 1 368 . 58 LEU HD1 H 0.94 0.02 2 369 . 58 LEU HD2 H 0.88 0.02 2 370 . 58 LEU N N 126.14 0.05 1 371 . 59 LYS H H 8.54 0.02 1 372 . 59 LYS HA H 4.17 0.02 1 373 . 59 LYS HB2 H 1.73 0.02 2 374 . 59 LYS HB3 H 1.65 0.02 2 375 . 59 LYS HG2 H 1.46 0.02 2 376 . 59 LYS HG3 H 1.41 0.02 2 377 . 59 LYS HD2 H 1.71 0.02 1 378 . 59 LYS HD3 H 1.71 0.02 1 379 . 59 LYS HE2 H 2.94 0.02 1 380 . 59 LYS HE3 H 2.94 0.02 1 381 . 59 LYS N N 124.69 0.05 1 382 . 60 ALA H H 9.61 0.02 1 383 . 60 ALA HA H 4.61 0.02 1 384 . 60 ALA HB H 1.46 0.02 1 385 . 60 ALA N N 126.94 0.05 1 386 . 61 ASN H H 7.94 0.02 1 387 . 61 ASN HA H 4.91 0.02 1 388 . 61 ASN HB2 H 2.56 0.02 2 389 . 61 ASN HB3 H 1.89 0.02 2 390 . 61 ASN HD21 H 7.49 0.02 2 391 . 61 ASN HD22 H 6.17 0.02 2 392 . 61 ASN N N 114.39 0.05 1 393 . 61 ASN ND2 N 115.19 0.02 1 394 . 62 PHE HA H 4.66 0.02 1 395 . 62 PHE HB2 H 3.31 0.02 2 396 . 62 PHE HB3 H 2.98 0.02 2 397 . 62 PHE HD1 H 7.28 0.02 1 398 . 62 PHE HD2 H 7.28 0.02 1 399 . 62 PHE HE1 H 7.35 0.02 1 400 . 62 PHE HE2 H 7.35 0.02 1 401 . 63 SER H H 7.83 0.02 1 402 . 63 SER HA H 4.64 0.02 1 403 . 63 SER HB2 H 3.94 0.02 1 404 . 63 SER HB3 H 3.94 0.02 1 405 . 63 SER N N 115.52 0.05 1 406 . 64 ASN H H 8.59 0.02 1 407 . 64 ASN HA H 4.64 0.02 1 408 . 64 ASN HB2 H 2.74 0.02 2 409 . 64 ASN HB3 H 2.60 0.02 2 410 . 64 ASN HD21 H 7.48 0.02 2 411 . 64 ASN HD22 H 6.82 0.02 2 412 . 64 ASN ND2 N 113.58 0.02 1 413 . 65 ILE H H 8.00 0.02 1 414 . 65 ILE HA H 4.34 0.02 1 415 . 65 ILE HB H 2.05 0.02 1 416 . 65 ILE HG12 H 1.38 0.02 1 417 . 65 ILE HG13 H 0.68 0.02 1 418 . 65 ILE HG2 H 1.38 0.02 1 419 . 65 ILE HD1 H 0.10 0.02 1 420 . 65 ILE N N 124.53 0.05 1 421 . 66 LEU H H 8.74 0.02 1 422 . 66 LEU HA H 4.56 0.02 1 423 . 66 LEU HB2 H 1.75 0.02 2 424 . 66 LEU HB3 H 1.71 0.02 2 425 . 66 LEU HG H 1.71 0.02 1 426 . 66 LEU HD1 H 0.94 0.02 2 427 . 66 LEU HD2 H 1.09 0.02 2 428 . 66 LEU N N 126.94 0.05 1 429 . 67 GLU H H 7.64 0.02 1 430 . 67 GLU HA H 4.67 0.02 1 431 . 67 GLU HB2 H 1.98 0.02 1 432 . 67 GLU HB3 H 1.98 0.02 1 433 . 67 GLU HG2 H 2.32 0.02 2 434 . 67 GLU HG3 H 2.15 0.02 2 435 . 67 GLU N N 119.06 0.05 1 436 . 68 ASN H H 7.98 0.02 1 437 . 68 ASN HA H 3.64 0.02 1 438 . 68 ASN HB2 H 2.16 0.02 2 439 . 68 ASN HB3 H 1.82 0.02 2 440 . 68 ASN HD21 H 7.54 0.02 2 441 . 68 ASN HD22 H 6.45 0.02 2 442 . 68 ASN N N 116.48 0.05 1 443 . 68 ASN ND2 N 112.62 0.02 1 444 . 69 GLU H H 6.61 0.02 1 445 . 69 GLU HA H 4.53 0.02 1 446 . 69 GLU HB2 H 1.57 0.02 2 447 . 69 GLU HB3 H 1.51 0.02 2 448 . 69 GLU HG2 H 1.85 0.02 1 449 . 69 GLU HG3 H 1.85 0.02 1 450 . 69 GLU N N 115.36 0.05 1 451 . 70 PHE H H 8.53 0.02 1 452 . 70 PHE HA H 4.79 0.02 1 453 . 70 PHE HB2 H 2.71 0.02 2 454 . 70 PHE HB3 H 2.57 0.02 2 455 . 70 PHE HD1 H 7.15 0.02 1 456 . 70 PHE HD2 H 7.15 0.02 1 457 . 70 PHE HE1 H 7.26 0.02 1 458 . 70 PHE HE2 H 7.26 0.02 1 459 . 70 PHE HZ H 7.45 0.02 1 460 . 70 PHE N N 121.31 0.05 1 461 . 71 THR H H 7.53 0.02 1 462 . 71 THR HA H 4.74 0.02 1 463 . 71 THR HB H 3.61 0.02 1 464 . 71 THR HG2 H 0.77 0.02 1 465 . 71 THR N N 125.98 0.05 1 466 . 72 VAL H H 8.74 0.02 1 467 . 72 VAL HA H 3.78 0.02 1 468 . 72 VAL HB H 1.83 0.02 1 469 . 72 VAL HG1 H 1.08 0.02 2 470 . 72 VAL HG2 H 0.85 0.02 2 471 . 72 VAL N N 129.84 0.05 1 472 . 73 SER H H 8.21 0.02 1 473 . 73 SER HA H 5.15 0.02 1 474 . 73 SER HB2 H 3.89 0.02 2 475 . 73 SER HB3 H 3.62 0.02 2 476 . 73 SER N N 121.79 0.05 1 477 . 74 GLY H H 8.41 0.02 1 478 . 74 GLY HA2 H 3.92 0.02 1 479 . 74 GLY HA3 H 3.74 0.02 1 480 . 74 GLY N N 107.95 0.05 1 481 . 75 LEU H H 8.15 0.02 1 482 . 75 LEU HA H 4.34 0.02 1 483 . 75 LEU HB2 H 1.47 0.02 2 484 . 75 LEU HB3 H 1.39 0.02 2 485 . 75 LEU HG H 1.09 0.02 1 486 . 75 LEU HD1 H 0.39 0.02 2 487 . 75 LEU HD2 H 0.08 0.02 2 488 . 75 LEU N N 120.99 0.05 1 489 . 76 THR H H 8.59 0.02 1 490 . 76 THR HA H 4.35 0.02 1 491 . 76 THR HB H 4.13 0.02 1 492 . 76 THR HG2 H 1.34 0.02 1 493 . 76 THR N N 121.31 0.05 1 494 . 77 GLU H H 8.57 0.02 1 495 . 77 GLU HA H 4.34 0.02 1 496 . 77 GLU HB2 H 1.87 0.02 2 497 . 77 GLU HB3 H 1.75 0.02 2 498 . 77 GLU HG2 H 2.29 0.02 2 499 . 77 GLU HG3 H 2.13 0.02 2 500 . 77 GLU N N 129.03 0.05 1 501 . 78 ASP H H 9.25 0.02 1 502 . 78 ASP HA H 4.07 0.02 1 503 . 78 ASP HB2 H 2.96 0.02 2 504 . 78 ASP HB3 H 2.85 0.02 2 505 . 78 ASP N N 120.67 0.05 1 506 . 79 ALA H H 7.75 0.02 1 507 . 79 ALA HA H 4.35 0.02 1 508 . 79 ALA HB H 1.27 0.02 1 509 . 79 ALA N N 124.69 0.05 1 510 . 80 ALA H H 7.64 0.02 1 511 . 80 ALA HA H 5.48 0.02 1 512 . 80 ALA HB H 1.06 0.02 1 513 . 80 ALA N N 121.63 0.05 1 514 . 81 TYR H H 8.90 0.02 1 515 . 81 TYR HA H 5.12 0.02 1 516 . 81 TYR HB2 H 2.19 0.02 2 517 . 81 TYR HB3 H 2.12 0.02 2 518 . 81 TYR HD1 H 6.87 0.02 1 519 . 81 TYR HD2 H 6.87 0.02 1 520 . 81 TYR HE1 H 6.97 0.02 1 521 . 81 TYR HE2 H 6.97 0.02 1 522 . 81 TYR N N 119.54 0.05 1 523 . 82 GLU H H 7.92 0.02 1 524 . 82 GLU HA H 4.45 0.02 1 525 . 82 GLU HB2 H 2.27 0.02 1 526 . 82 GLU HB3 H 2.27 0.02 1 527 . 82 GLU N N 115.52 0.05 1 528 . 83 PHE H H 8.31 0.02 1 529 . 83 PHE HA H 6.09 0.02 1 530 . 83 PHE HB2 H 3.01 0.02 2 531 . 83 PHE HB3 H 2.43 0.02 2 532 . 83 PHE HD1 H 7.22 0.02 1 533 . 83 PHE HD2 H 7.22 0.02 1 534 . 83 PHE HE1 H 6.70 0.02 1 535 . 83 PHE HE2 H 6.70 0.02 1 536 . 83 PHE HZ H 6.97 0.02 1 537 . 83 PHE N N 115.52 0.05 1 538 . 84 ARG H H 9.13 0.02 1 539 . 84 ARG HA H 4.44 0.02 1 540 . 84 ARG HB2 H 1.71 0.02 1 541 . 84 ARG HB3 H 1.71 0.02 1 542 . 84 ARG HG2 H 1.64 0.02 1 543 . 84 ARG HG3 H 1.64 0.02 1 544 . 84 ARG HD2 H 2.95 0.02 1 545 . 84 ARG HD3 H 2.95 0.02 1 546 . 84 ARG HE H 6.64 0.02 1 547 . 84 ARG N N 118.25 0.05 1 548 . 85 VAL H H 8.22 0.02 1 549 . 85 VAL HA H 4.83 0.02 1 550 . 85 VAL HB H 0.88 0.02 1 551 . 85 VAL HG1 H -0.19 0.02 2 552 . 85 VAL HG2 H -0.42 0.02 2 553 . 85 VAL N N 119.70 0.05 1 554 . 86 ILE H H 8.91 0.02 1 555 . 86 ILE HA H 3.80 0.02 1 556 . 86 ILE HB H 1.32 0.02 1 557 . 86 ILE HG12 H 0.91 0.02 2 558 . 86 ILE HG13 H 0.63 0.02 2 559 . 86 ILE HG2 H 0.81 0.02 1 560 . 86 ILE HD1 H 0.52 0.02 1 561 . 86 ILE N N 128.71 0.05 1 562 . 87 ALA H H 8.71 0.02 1 563 . 87 ALA HA H 4.96 0.02 1 564 . 87 ALA HB H 1.28 0.02 1 565 . 87 ALA N N 129.03 0.05 1 566 . 88 LYS H H 8.24 0.02 1 567 . 88 LYS HA H 5.28 0.02 1 568 . 88 LYS HB2 H 1.63 0.02 2 569 . 88 LYS HB3 H 1.29 0.02 2 570 . 88 LYS HG2 H 1.39 0.02 2 571 . 88 LYS HG3 H 1.11 0.02 2 572 . 88 LYS HD2 H 1.39 0.02 1 573 . 88 LYS HD3 H 1.39 0.02 1 574 . 88 LYS HE2 H 2.72 0.02 2 575 . 88 LYS HE3 H 2.66 0.02 2 576 . 88 LYS N N 120.99 0.05 1 577 . 89 ASN H H 8.36 0.02 1 578 . 89 ASN HA H 5.52 0.02 1 579 . 89 ASN HB2 H 3.25 0.02 2 580 . 89 ASN HB3 H 2.39 0.02 2 581 . 89 ASN HD21 H 7.61 0.02 2 582 . 89 ASN HD22 H 7.75 0.02 2 583 . 89 ASN N N 121.47 0.05 1 584 . 89 ASN ND2 N 113.26 0.02 1 585 . 90 ALA H H 8.25 0.02 1 586 . 90 ALA HA H 4.01 0.02 1 587 . 90 ALA HB H 1.46 0.02 1 588 . 90 ALA N N 119.06 0.05 1 589 . 91 ALA H H 6.76 0.02 1 590 . 91 ALA HA H 3.98 0.02 1 591 . 91 ALA HB H 0.37 0.02 1 592 . 91 ALA N N 119.06 0.05 1 593 . 92 GLY H H 7.94 0.02 1 594 . 92 GLY HA2 H 4.14 0.02 1 595 . 92 GLY HA3 H 3.37 0.02 1 596 . 92 GLY N N 107.63 0.05 1 597 . 93 ALA H H 7.38 0.02 1 598 . 93 ALA HA H 4.22 0.02 1 599 . 93 ALA HB H 1.17 0.02 1 600 . 93 ALA N N 124.53 0.05 1 601 . 94 ILE H H 7.87 0.02 1 602 . 94 ILE HA H 4.85 0.02 1 603 . 94 ILE HB H 1.56 0.02 1 604 . 94 ILE HG12 H 1.43 0.02 2 605 . 94 ILE HG13 H 0.90 0.02 2 606 . 94 ILE HG2 H 0.80 0.02 1 607 . 94 ILE HD1 H 0.72 0.02 1 608 . 94 ILE N N 118.41 0.05 1 609 . 95 SER H H 9.13 0.02 1 610 . 95 SER HA H 4.50 0.02 1 611 . 95 SER HB2 H 4.20 0.02 2 612 . 95 SER HB3 H 3.47 0.02 2 613 . 95 SER HG H 5.21 0.02 1 614 . 95 SER N N 126.14 0.05 1 615 . 96 PRO HA H 4.79 0.02 1 616 . 96 PRO HB2 H 2.01 0.02 1 617 . 96 PRO HB3 H 2.01 0.02 1 618 . 96 PRO HG2 H 1.73 0.02 1 619 . 96 PRO HG3 H 1.73 0.02 1 620 . 96 PRO HD2 H 3.94 0.02 2 621 . 96 PRO HD3 H 3.41 0.02 2 622 . 97 PRO HA H 4.37 0.02 1 623 . 97 PRO HB2 H 2.45 0.02 2 624 . 97 PRO HB3 H 1.52 0.02 2 625 . 97 PRO HG2 H 1.76 0.02 2 626 . 97 PRO HG3 H 1.58 0.02 2 627 . 97 PRO HD2 H 3.67 0.02 2 628 . 97 PRO HD3 H 3.43 0.02 2 629 . 98 SER H H 8.70 0.02 1 630 . 98 SER HA H 4.13 0.02 1 631 . 98 SER HB2 H 4.00 0.02 2 632 . 98 SER HB3 H 3.47 0.02 2 633 . 98 SER N N 116.00 0.05 1 634 . 99 GLU H H 8.49 0.02 1 635 . 99 GLU HA H 4.41 0.02 1 636 . 99 GLU HB2 H 2.02 0.02 2 637 . 99 GLU HB3 H 1.88 0.02 2 638 . 99 GLU HG2 H 2.43 0.02 1 639 . 99 GLU HG3 H 2.43 0.02 1 640 . 99 GLU N N 121.79 0.05 1 641 . 100 PRO HA H 4.93 0.02 1 642 . 100 PRO HB2 H 2.27 0.02 1 643 . 100 PRO HB3 H 2.27 0.02 1 644 . 100 PRO HG2 H 2.01 0.02 1 645 . 100 PRO HG3 H 2.01 0.02 1 646 . 100 PRO HD2 H 3.86 0.02 2 647 . 100 PRO HD3 H 3.71 0.02 2 648 . 101 SER H H 9.50 0.02 1 649 . 101 SER HA H 4.32 0.02 1 650 . 101 SER HB2 H 4.60 0.02 2 651 . 101 SER HB3 H 3.99 0.02 2 652 . 101 SER HG H 5.26 0.02 1 653 . 101 SER N N 115.19 0.05 1 654 . 102 ASP H H 8.65 0.02 1 655 . 102 ASP HA H 4.64 0.02 1 656 . 102 ASP HB2 H 2.88 0.02 2 657 . 102 ASP HB3 H 2.46 0.02 2 658 . 102 ASP N N 119.70 0.05 1 659 . 103 ALA H H 8.37 0.02 1 660 . 103 ALA HA H 4.35 0.02 1 661 . 103 ALA HB H 1.17 0.02 1 662 . 103 ALA N N 125.01 0.05 1 663 . 104 ILE H H 9.31 0.02 1 664 . 104 ILE HA H 4.35 0.02 1 665 . 104 ILE HB H 1.93 0.02 1 666 . 104 ILE HG2 H 1.24 0.02 1 667 . 104 ILE HD1 H 1.04 0.02 1 668 . 104 ILE N N 127.75 0.05 1 669 . 105 THR H H 8.29 0.02 1 670 . 105 THR HA H 5.11 0.02 1 671 . 105 THR HB H 3.79 0.02 1 672 . 105 THR HG2 H 0.91 0.02 1 673 . 105 THR N N 123.40 0.05 1 674 . 106 CYS H H 8.30 0.02 1 675 . 106 CYS HA H 4.00 0.02 1 676 . 106 CYS HB2 H 3.26 0.02 2 677 . 106 CYS HB3 H 2.77 0.02 2 678 . 106 CYS N N 127.43 0.05 1 679 . 107 ARG H H 6.93 0.02 1 680 . 107 ARG HA H 4.36 0.02 1 681 . 107 ARG HB2 H 1.96 0.02 2 682 . 107 ARG HB3 H 1.62 0.02 2 683 . 107 ARG HG2 H 1.54 0.02 2 684 . 107 ARG HG3 H 1.34 0.02 2 685 . 107 ARG HD2 H 3.08 0.02 1 686 . 107 ARG HD3 H 3.08 0.02 1 687 . 107 ARG HE H 7.36 0.02 1 688 . 107 ARG N N 123.88 0.05 1 689 . 107 ARG NE N 108.11 0.02 1 690 . 108 ASP H H 8.55 0.02 1 691 . 108 ASP HA H 4.77 0.02 1 692 . 108 ASP HB2 H 2.72 0.02 2 693 . 108 ASP HB3 H 2.63 0.02 2 694 . 108 ASP N N 120.83 0.05 1 695 . 109 ASP H H 8.41 0.02 1 696 . 109 ASP HA H 4.60 0.02 1 697 . 109 ASP HB2 H 2.69 0.02 2 698 . 109 ASP HB3 H 2.51 0.02 2 699 . 109 ASP N N 122.28 0.05 1 700 . 110 VAL H H 7.92 0.02 1 701 . 110 VAL HA H 4.10 0.02 1 702 . 110 VAL HB H 2.07 0.02 1 703 . 110 VAL HG1 H 0.88 0.02 1 704 . 110 VAL HG2 H 0.88 0.02 1 705 . 110 VAL N N 120.51 0.05 1 706 . 111 GLU H H 8.28 0.02 1 707 . 111 GLU HA H 4.28 0.02 1 708 . 111 GLU HB2 H 2.06 0.02 2 709 . 111 GLU HB3 H 1.89 0.02 2 710 . 111 GLU HG2 H 2.26 0.02 1 711 . 111 GLU HG3 H 2.26 0.02 1 712 . 111 GLU N N 125.66 0.05 1 713 . 112 ALA H H 7.80 0.02 1 714 . 112 ALA HA H 4.09 0.02 1 715 . 112 ALA HB H 1.28 0.02 1 716 . 112 ALA N N 131.93 0.05 1 stop_ save_