data_6196 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Arath;CDC25; a dual-specificity tyrosine phosphatase from Arabidopsis thaliana ; _BMRB_accession_number 6196 _BMRB_flat_file_name bmr6196.str _Entry_type original _Submission_date 2004-04-26 _Accession_date 2004-04-28 _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 Landrieu Isabelle . . 2 Wieruszeski Jean-Michel . . 3 Hassan Sahar . . 4 Lippens Guy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 475 "13C chemical shifts" 388 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-09-07 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6195 'wild type protein' stop_ _Original_release_date 2004-09-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15329414 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Landrieu Isabelle . . 2 'Da Costa' M. . . 3 'De Veylder' L. . . 4 Dewitte F. . . 5 Vandepoele K. . . 6 Hassan Sahar . . 7 Wieruszeski Jean-Michel . . 8 Faure J. D. . 9 'Von Montagu' M. . . 10 Inze D. . . 11 Lippens Guy . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2004 _Details . loop_ _Keyword CDC25 'cell cycle' phosphorylation plant 'zinc binding loop' stop_ save_ ################################## # Molecular system description # ################################## save_system_CDC25 _Saveframe_category molecular_system _Mol_system_name 'Arath; CDC25; CYS131SER mutant' _Abbreviation_common CDC25 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Arath; CDC25 monomer; CYS131SER mutant' $CDC25 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' loop_ _Biological_function 'Dual-specificity tyrosine phosphatase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CDC25 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Dual-specificity tyrosine phosphatase; CYS131SER mutant' _Abbreviation_common CDC25 _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details 'Mutation C72S, Mutation C131S' ############################## # Polymer residue sequence # ############################## _Residue_count 146 _Mol_residue_sequence ; MGRSIFSFFTKKKKMAMARS ISYITSTQLLPLHRRPNIAI IDVRDEERNYDGHIAGSLHY ASGSFDDKISHLVQNVKDKD TLVFHSALSQVRGPTCARRL VNYLDEKKEDTGIKNIMILE RGFNGWEASGKPVCRCAEVP CKGDSA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -14 MET 2 -13 GLY 3 -12 ARG 4 -11 SER 5 -10 ILE 6 -9 PHE 7 -8 SER 8 -7 PHE 9 -6 PHE 10 -5 THR 11 -4 LYS 12 -3 LYS 13 -2 LYS 14 -1 LYS 15 1 MET 16 2 ALA 17 3 MET 18 4 ALA 19 5 ARG 20 6 SER 21 7 ILE 22 8 SER 23 9 TYR 24 10 ILE 25 11 THR 26 12 SER 27 13 THR 28 14 GLN 29 15 LEU 30 16 LEU 31 17 PRO 32 18 LEU 33 19 HIS 34 20 ARG 35 21 ARG 36 22 PRO 37 23 ASN 38 24 ILE 39 25 ALA 40 26 ILE 41 27 ILE 42 28 ASP 43 29 VAL 44 30 ARG 45 31 ASP 46 32 GLU 47 33 GLU 48 34 ARG 49 35 ASN 50 36 TYR 51 37 ASP 52 38 GLY 53 39 HIS 54 40 ILE 55 41 ALA 56 42 GLY 57 43 SER 58 44 LEU 59 45 HIS 60 46 TYR 61 47 ALA 62 48 SER 63 49 GLY 64 50 SER 65 51 PHE 66 52 ASP 67 53 ASP 68 54 LYS 69 55 ILE 70 56 SER 71 57 HIS 72 58 LEU 73 59 VAL 74 60 GLN 75 61 ASN 76 62 VAL 77 63 LYS 78 64 ASP 79 65 LYS 80 66 ASP 81 67 THR 82 68 LEU 83 69 VAL 84 70 PHE 85 71 HIS 86 72 SER 87 73 ALA 88 74 LEU 89 75 SER 90 76 GLN 91 77 VAL 92 78 ARG 93 79 GLY 94 80 PRO 95 81 THR 96 82 CYS 97 83 ALA 98 84 ARG 99 85 ARG 100 86 LEU 101 87 VAL 102 88 ASN 103 89 TYR 104 90 LEU 105 91 ASP 106 92 GLU 107 93 LYS 108 94 LYS 109 95 GLU 110 96 ASP 111 97 THR 112 98 GLY 113 99 ILE 114 100 LYS 115 101 ASN 116 102 ILE 117 103 MET 118 104 ILE 119 105 LEU 120 106 GLU 121 107 ARG 122 108 GLY 123 109 PHE 124 110 ASN 125 111 GLY 126 112 TRP 127 113 GLU 128 114 ALA 129 115 SER 130 116 GLY 131 117 LYS 132 118 PRO 133 119 VAL 134 120 CYS 135 121 ARG 136 122 CYS 137 123 ALA 138 124 GLU 139 125 VAL 140 126 PRO 141 127 CYS 142 128 LYS 143 129 GLY 144 130 ASP 145 131 SER 146 132 ALA 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 SWISS-PROT Q8GY31 'Dual specificity phosphatase Cdc25 (Arath;CDC25)' 100.00 146 98.63 98.63 9.56e-81 REF NP_568119 'CDC25 [Arabidopsis thaliana]' 100.00 146 98.63 98.63 9.56e-81 GenBank AAO39886 'At5g03455 [Arabidopsis thaliana]' 100.00 146 98.63 98.63 9.56e-81 GenBank AAM63780 'unknown [Arabidopsis thaliana]' 89.04 130 98.46 98.46 5.91e-71 EMBL CAB83305 'putative protein [Arabidopsis thaliana]' 90.41 132 98.48 98.48 3.03e-72 DBJ BAC42537 'unknown protein [Arabidopsis thaliana]' 100.00 146 98.63 98.63 9.56e-81 BMRB 6195 'Dual-specificity tyrosine phosphatase' 90.41 132 99.24 99.24 6.64e-73 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 15:29:31 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CDC25 'Thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana 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 $CDC25 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)star plasmid pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CDC25 400 uM '[U-90% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CDC25 400 uM '[U-95% 13C; U-90% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CDC25 400 uM '[U-95% 13C]' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CDC25 250 uM [15N]-Lys stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version . loop_ _Task 'data acquisition' stop_ _Details . save_ save_SNARF _Saveframe_category software _Name SNARF _Version . loop_ _Task 'data processing' 'peak picking (in-house development)' stop_ _Details 'Frank Van Hoesel, Groningen, the Netherlands' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _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_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.2 pH temperature 293 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation d4-TSPA H 1 'methyl protons' ppm 0.00 internal direct . internal . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_Arath;CDC25C72S_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 stop_ _Sample_conditions_label $cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Arath; CDC25 monomer; CYS131SER mutant' _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 15 MET CA C 55.41 . . 2 1 15 MET CB C 32.65 . . 3 2 16 ALA H H 8.30 . . 4 2 16 ALA HA H 4.28 . . 5 2 16 ALA HB H 1.39 . . 6 2 16 ALA C C 174.9 . . 7 2 16 ALA CA C 52.48 . . 8 2 16 ALA CB C 19.13 . . 9 2 16 ALA N N 125.0 . . 10 3 17 MET H H 8.35 . . 11 3 17 MET HA H 4.44 . . 12 3 17 MET C C 173.3 . . 13 3 17 MET CA C 55.58 . . 14 3 17 MET CB C 32.97 . . 15 3 17 MET N N 119.5 . . 16 4 18 ALA H H 8.35 . . 17 4 18 ALA HA H 4.31 . . 18 4 18 ALA C C 174.7 . . 19 4 18 ALA CA C 52.40 . . 20 4 18 ALA CB C 19.17 . . 21 4 18 ALA N N 125.4 . . 22 5 19 ARG H H 8.48 . . 23 5 19 ARG HA H 4.40 . . 24 5 19 ARG C C 173.3 . . 25 5 19 ARG CA C 56.44 . . 26 5 19 ARG CB C 31.08 . . 27 5 19 ARG N N 120.2 . . 28 6 20 SER H H 8.26 . . 29 6 20 SER HA H 4.59 . . 30 6 20 SER HB2 H 3.87 . . 31 6 20 SER C C 174.9 . . 32 6 20 SER CA C 58.10 . . 33 6 20 SER CB C 64.71 . . 34 6 20 SER N N 116.4 . . 35 7 21 ILE H H 8.31 . . 36 7 21 ILE HA H 4.58 . . 37 7 21 ILE HB H 1.56 . . 38 7 21 ILE HD1 H 0.62 . . 39 7 21 ILE C C 176.9 . . 40 7 21 ILE CA C 61.70 . . 41 7 21 ILE N N 123.2 . . 42 8 22 SER H H 8.19 . . 43 8 22 SER HA H 4.90 . . 44 8 22 SER HB2 H 3.97 . . 45 8 22 SER C C 174.9 . . 46 8 22 SER CA C 57.50 . . 47 8 22 SER CB C 65.65 . . 48 8 22 SER N N 121.6 . . 49 9 23 TYR H H 8.93 . . 50 9 23 TYR HA H 5.46 . . 51 9 23 TYR HB2 H 2.98 . . 52 9 23 TYR HD1 H 7.10 . . 53 9 23 TYR C C 177.8 . . 54 9 23 TYR CA C 58.03 . . 55 9 23 TYR CB C 41.16 . . 56 9 23 TYR N N 119.5 . . 57 10 24 ILE H H 9.07 . . 58 10 24 ILE HA H 4.92 . . 59 10 24 ILE HB H 1.88 . . 60 10 24 ILE HD1 H 0.82 . . 61 10 24 ILE C C 175.3 . . 62 10 24 ILE CA C 59.54 . . 63 10 24 ILE CB C 42.37 . . 64 10 24 ILE N N 120.8 . . 65 11 25 THR H H 8.56 . . 66 11 25 THR HA H 4.93 . . 67 11 25 THR HB H 4.89 . . 68 11 25 THR HG2 H 1.36 . . 69 11 25 THR C C 176.8 . . 70 11 25 THR CA C 61.28 . . 71 11 25 THR CB C 71.54 . . 72 11 25 THR CG2 C 21.57 . . 73 11 25 THR N N 116.4 . . 74 12 26 SER H H 9.56 . . 75 12 26 SER C C 174.2 . . 76 12 26 SER CA C 64.54 . . 77 12 26 SER CB C 61.84 . . 78 12 26 SER N N 117.9 . . 79 13 27 THR H H 7.98 . . 80 13 27 THR HA H 4.05 . . 81 13 27 THR HB H 3.70 . . 82 13 27 THR HG2 H 1.20 . . 83 13 27 THR C C 174.3 . . 84 13 27 THR CA C 68.32 . . 85 13 27 THR CB C 66.95 . . 86 13 27 THR CG2 C 21.78 . . 87 13 27 THR N N 119.1 . . 88 14 28 GLN H H 7.62 . . 89 14 28 GLN HA H 4.08 . . 90 14 28 GLN HB2 H 1.94 . . 91 14 28 GLN HG2 H 2.43 . . 92 14 28 GLN C C 174.7 . . 93 14 28 GLN CA C 58.34 . . 94 14 28 GLN CB C 29.18 . . 95 14 28 GLN N N 119.7 . . 96 15 29 LEU H H 8.57 . . 97 15 29 LEU HA H 4.12 . . 98 15 29 LEU HB2 H 1.52 . . 99 15 29 LEU HD1 H 0.84 . . 100 15 29 LEU HD2 H 0.79 . . 101 15 29 LEU C C 172.6 . . 102 15 29 LEU CA C 61.28 . . 103 15 29 LEU CB C 42.23 . . 104 15 29 LEU N N 117.0 . . 105 16 30 LEU H H 8.13 . . 106 16 30 LEU HA H 4.51 . . 107 16 30 LEU CA C 62.00 . . 108 16 30 LEU N N 120.5 . . 109 17 31 PRO C C 173.5 . . 110 17 31 PRO CA C 66.89 . . 111 17 31 PRO CB C 31.13 . . 112 18 32 LEU H H 7.44 . . 113 18 32 LEU HA H 4.44 . . 114 18 32 LEU HB2 H 1.85 . . 115 18 32 LEU HG H 1.66 . . 116 18 32 LEU HD1 H 0.85 . . 117 18 32 LEU C C 171.0 . . 118 18 32 LEU CA C 55.17 . . 119 18 32 LEU N N 116.3 . . 120 19 33 HIS H H 7.84 . . 121 19 33 HIS HA H 4.06 . . 122 19 33 HIS HB2 H 3.15 . . 123 19 33 HIS HB3 H 3.35 . . 124 19 33 HIS HD1 H 6.92 . . 125 19 33 HIS C C 176.7 . . 126 19 33 HIS CA C 61.77 . . 127 19 33 HIS CB C 28.44 . . 128 19 33 HIS N N 113.9 . . 129 20 34 ARG H H 8.25 . . 130 20 34 ARG HA H 4.51 . . 131 20 34 ARG C C 173.9 . . 132 20 34 ARG CA C 53.20 . . 133 20 34 ARG CB C 28.01 . . 134 20 34 ARG N N 117.2 . . 135 21 35 ARG H H 7.88 . . 136 21 35 ARG HA H 4.43 . . 137 21 35 ARG C C 174.0 . . 138 21 35 ARG CA C 55.13 . . 139 21 35 ARG N N 122.8 . . 140 22 36 PRO C C 174.2 . . 141 23 37 ASN H H 8.34 . . 142 23 37 ASN HA H 4.45 . . 143 23 37 ASN HB2 H 2.09 . . 144 23 37 ASN HB3 H 2.58 . . 145 23 37 ASN C C 177.4 . . 146 23 37 ASN CA C 54.29 . . 147 23 37 ASN CB C 37.43 . . 148 23 37 ASN ND2 N 111.4 . . 149 24 38 ILE H H 7.38 . . 150 24 38 ILE HA H 4.99 . . 151 24 38 ILE HB H 1.75 . . 152 24 38 ILE HG12 H 1.03 . . 153 24 38 ILE HG13 H 1.57 . . 154 24 38 ILE HG2 H 0.72 . . 155 24 38 ILE HD1 H 0.80 . . 156 24 38 ILE C C 175.5 . . 157 24 38 ILE CA C 59.71 . . 158 24 38 ILE CB C 40.19 . . 159 24 38 ILE CG1 C 27.94 . . 160 24 38 ILE CG2 C 16.86 . . 161 24 38 ILE CD1 C 13.60 . . 162 24 38 ILE N N 120.3 . . 163 25 39 ALA H H 8.57 . . 164 25 39 ALA HA H 4.92 . . 165 25 39 ALA HB H 1.18 . . 166 25 39 ALA C C 175.5 . . 167 25 39 ALA CA C 49.64 . . 168 25 39 ALA CB C 22.19 . . 169 25 39 ALA N N 127.2 . . 170 26 40 ILE H H 9.10 . . 171 26 40 ILE HA H 4.67 . . 172 26 40 ILE HB H 1.60 . . 173 26 40 ILE HG2 H 0.64 . . 174 26 40 ILE HD1 H 0.74 . . 175 26 40 ILE C C 176.8 . . 176 26 40 ILE CA C 60.04 . . 177 26 40 ILE CB C 38.14 . . 178 26 40 ILE N N 123.8 . . 179 27 41 ILE H H 9.3 . . 180 27 41 ILE HA H 4.26 . . 181 27 41 ILE C C 177.7 . . 182 27 41 ILE CA C 59.12 . . 183 27 41 ILE CB C 35.84 . . 184 27 41 ILE N N 128.9 . . 185 28 42 ASP H H 8.90 . . 186 28 42 ASP HB2 H 3.09 . . 187 28 42 ASP C C 174.2 . . 188 28 42 ASP CA C 51.23 . . 189 28 42 ASP CB C 42.27 . . 190 28 42 ASP N N 127.8 . . 191 29 43 VAL H H 8.04 . . 192 29 43 VAL HA H 5.42 . . 193 29 43 VAL HB H 2.64 . . 194 29 43 VAL HG1 H 1.09 . . 195 29 43 VAL HG2 H 0.69 . . 196 29 43 VAL C C 172.2 . . 197 29 43 VAL CA C 59.70 . . 198 29 43 VAL CB C 30.65 . . 199 29 43 VAL CG1 C 22.00 . . 200 29 43 VAL N N 116.7 . . 201 30 44 ARG H H 7.86 . . 202 30 44 ARG HA H 4.20 . . 203 30 44 ARG HB2 H 1.85 . . 204 30 44 ARG C C 176.5 . . 205 30 44 ARG CA C 57.59 . . 206 30 44 ARG CB C 33.32 . . 207 30 44 ARG N N 118.0 . . 208 31 45 ASP H H 7.65 . . 209 31 45 ASP HA H 5.20 . . 210 31 45 ASP HB2 H 2.67 . . 211 31 45 ASP HB3 H 2.87 . . 212 31 45 ASP C C 174.5 . . 213 31 45 ASP CA C 54.21 . . 214 31 45 ASP CB C 42.76 . . 215 31 45 ASP N N 121.9 . . 216 32 46 GLU H H 8.98 . . 217 32 46 GLU C C 173.8 . . 218 32 46 GLU CA C 59.62 . . 219 32 46 GLU CB C 28.79 . . 220 32 46 GLU N N 123.0 . . 221 33 47 GLU H H 9.87 . . 222 33 47 GLU HA H 4.05 . . 223 33 47 GLU C C 172.8 . . 224 33 47 GLU CA C 60.23 . . 225 33 47 GLU N N 117.9 . . 226 34 48 ARG H H 6.91 . . 227 34 48 ARG HA H 3.58 . . 228 34 48 ARG C C 172.8 . . 229 34 48 ARG CA C 56.94 . . 230 34 48 ARG CB C 29.54 . . 231 34 48 ARG N N 114.7 . . 232 35 49 ASN H H 7.80 . . 233 35 49 ASN HA H 4.42 . . 234 35 49 ASN HB2 H 2.67 . . 235 35 49 ASN C C 175.3 . . 236 35 49 ASN CA C 54.73 . . 237 35 49 ASN CB C 38.53 . . 238 35 49 ASN N N 113.9 . . 239 36 50 TYR H H 6.79 . . 240 36 50 TYR HA H 5.00 . . 241 36 50 TYR HB2 H 3.02 . . 242 36 50 TYR C C 174.5 . . 243 36 50 TYR CA C 58.41 . . 244 36 50 TYR N N 113.8 . . 245 37 51 ASP H H 8.40 . . 246 37 51 ASP HA H 3.99 . . 247 37 51 ASP HB2 H 2.67 . . 248 37 51 ASP C C 174.1 . . 249 37 51 ASP CA C 54.88 . . 250 37 51 ASP N N 121.9 . . 251 38 52 GLY H H 7.95 . . 252 38 52 GLY HA2 H 3.89 . . 253 38 52 GLY CA C 42.59 . . 254 38 52 GLY N N 104.51 . . 255 39 53 HIS H H 8.59 . . 256 39 53 HIS HA H 4.29 . . 257 39 53 HIS HB2 H 2.92 . . 258 39 53 HIS C C 177.8 . . 259 39 53 HIS CA C 55.48 . . 260 39 53 HIS CB C 31.10 . . 261 39 53 HIS N N 112.3 . . 262 40 54 ILE H H 9.85 . . 263 40 54 ILE HA H 3.82 . . 264 40 54 ILE HB H 1.49 . . 265 40 54 ILE HG12 H 0.88 . . 266 40 54 ILE HG13 H 1.06 . . 267 40 54 ILE HG2 H 0.55 . . 268 40 54 ILE HD1 H -0.60 . . 269 40 54 ILE C C 173.9 . . 270 40 54 ILE CA C 63.39 . . 271 40 54 ILE CB C 37.99 . . 272 40 54 ILE CG2 C 16.65 . . 273 40 54 ILE CD1 C 11.99 . . 274 40 54 ILE N N 121.3 . . 275 41 55 ALA H H 9.85 . . 276 41 55 ALA HA H 4.62 . . 277 41 55 ALA HB H 1.49 . . 278 41 55 ALA C C 173.2 . . 279 41 55 ALA CA C 53.78 . . 280 41 55 ALA CB C 19.09 . . 281 41 55 ALA N N 135.4 . . 282 42 56 GLY H H 9.87 . . 283 42 56 GLY HA2 H 3.78 . . 284 42 56 GLY HA3 H 4.2 . . 285 42 56 GLY C C 175.6 . . 286 42 56 GLY CA C 43.87 . . 287 42 56 GLY N N 112.6 . . 288 43 57 SER H H 8.26 . . 289 43 57 SER HA H 4.58 . . 290 43 57 SER HB2 H 3.87 . . 291 43 57 SER C C 176.7 . . 292 43 57 SER CA C 58.90 . . 293 43 57 SER CB C 64.91 . . 294 43 57 SER N N 115.0 . . 295 44 58 LEU H H 9.15 . . 296 44 58 LEU HA H 4.56 . . 297 44 58 LEU HB2 H 1.62 . . 298 44 58 LEU HB3 H 1.87 . . 299 44 58 LEU HD1 H 0.90 . . 300 44 58 LEU HD2 H 0.38 . . 301 44 58 LEU C C 175.0 . . 302 44 58 LEU CA C 54.04 . . 303 44 58 LEU CB C 43.35 . . 304 44 58 LEU N N 122.8 . . 305 45 59 HIS H H 8.74 . . 306 45 59 HIS HA H 5.47 . . 307 45 59 HIS HB2 H 2.33 . . 308 45 59 HIS HB3 H 3.04 . . 309 45 59 HIS HD1 H 6.72 . . 310 45 59 HIS C C 176.5 . . 311 45 59 HIS CA C 54.00 . . 312 45 59 HIS CB C 32.62 . . 313 45 59 HIS N N 122.9 . . 314 46 60 TYR H H 8.37 . . 315 46 60 TYR HA H 4.05 . . 316 46 60 TYR HB2 H 2.45 . . 317 46 60 TYR HB3 H 2.82 . . 318 46 60 TYR HD1 H 6.73 . . 319 46 60 TYR C C 177.2 . . 320 46 60 TYR CA C 57.60 . . 321 46 60 TYR CB C 39.71 . . 322 46 60 TYR N N 132.3 . . 323 47 61 ALA H H 7.19 . . 324 47 61 ALA HA H 4.06 . . 325 47 61 ALA HB H 1.27 . . 326 47 61 ALA C C 170.5 . . 327 47 61 ALA CA C 52.25 . . 328 47 61 ALA CB C 19.22 . . 329 47 61 ALA N N 121.3 . . 330 48 62 SER H H 7.88 . . 331 48 62 SER HA H 4.09 . . 332 48 62 SER C C 170.6 . . 333 48 62 SER CA C 62.77 . . 334 48 62 SER N N 119.1 . . 335 49 63 GLY H H 9.92 . . 336 49 63 GLY HA2 H 3.85 . . 337 49 63 GLY HA3 H 3.97 . . 338 49 63 GLY C C 175.8 . . 339 49 63 GLY CA C 46.11 . . 340 49 63 GLY N N 110.8 . . 341 50 64 SER H H 7.44 . . 342 50 64 SER HA H 4.99 . . 343 50 64 SER HB2 H 4.05 . . 344 50 64 SER HB3 H 3.78 . . 345 50 64 SER C C 175.9 . . 346 50 64 SER CA C 56.96 . . 347 50 64 SER CB C 63.95 . . 348 50 64 SER N N 111.3 . . 349 51 65 PHE H H 7.65 . . 350 51 65 PHE HA H 3.87 . . 351 51 65 PHE HB2 H 3.01 . . 352 51 65 PHE HB3 H 3.44 . . 353 51 65 PHE HD1 H 7.43 . . 354 51 65 PHE HE1 H 7.57 . . 355 51 65 PHE C C 173.8 . . 356 51 65 PHE CA C 64.16 . . 357 51 65 PHE CB C 40.94 . . 358 51 65 PHE N N 124.8 . . 359 52 66 ASP H H 8.60 . . 360 52 66 ASP HA H 4.23 . . 361 52 66 ASP HB2 H 2.60 . . 362 52 66 ASP HB3 H 2.70 . . 363 52 66 ASP C C 172.6 . . 364 52 66 ASP CA C 57.92 . . 365 52 66 ASP CB C 40.28 . . 366 52 66 ASP N N 112.3 . . 367 53 67 ASP H H 7.74 . . 368 53 67 ASP HA H 4.52 . . 369 53 67 ASP HB2 H 2.70 . . 370 53 67 ASP C C 173.1 . . 371 53 67 ASP CA C 56.24 . . 372 53 67 ASP CB C 41.37 . . 373 53 67 ASP N N 116.9 . . 374 54 68 LYS H H 7.58 . . 375 54 68 LYS HA H 4.58 . . 376 54 68 LYS HB3 H 2.18 . . 377 54 68 LYS HG2 H 1.34 . . 378 54 68 LYS HG3 H 1.52 . . 379 54 68 LYS HD2 H 1.73 . . 380 54 68 LYS C C 174.1 . . 381 54 68 LYS CA C 55.10 . . 382 54 68 LYS CB C 33.50 . . 383 54 68 LYS N N 117.1 . . 384 55 69 ILE H H 7.05 . . 385 55 69 ILE HA H 3.07 . . 386 55 69 ILE HB H 1.26 . . 387 55 69 ILE HG12 H 1.11 . . 388 55 69 ILE HG13 H 0.95 . . 389 55 69 ILE HG2 H 0.15 . . 390 55 69 ILE HD1 H 0.65 . . 391 55 69 ILE C C 174.8 . . 392 55 69 ILE CA C 67.16 . . 393 55 69 ILE CB C 37.58 . . 394 55 69 ILE CG1 C 28.11 . . 395 55 69 ILE CG2 C 16.45 . . 396 55 69 ILE CD1 C 15.00 . . 397 55 69 ILE N N 122.5 . . 398 56 70 SER H H 8.23 . . 399 56 70 SER HA H 3.90 . . 400 56 70 SER C C 174.8 . . 401 56 70 SER CA C 62.16 . . 402 56 70 SER N N 114.4 . . 403 57 71 HIS H H 7.44 . . 404 57 71 HIS HA H 4.10 . . 405 57 71 HIS HB2 H 3.24 . . 406 57 71 HIS HB3 H 3.39 . . 407 57 71 HIS HD1 H 7.11 . . 408 57 71 HIS HD2 H 6.73 . . 409 57 71 HIS C C 173.0 . . 410 57 71 HIS CA C 61.01 . . 411 57 71 HIS CB C 30.67 . . 412 57 71 HIS N N 124.3 . . 413 58 72 LEU H H 8.05 . . 414 58 72 LEU HA H 3.90 . . 415 58 72 LEU HB2 H 1.61 . . 416 58 72 LEU HB3 H 0.41 . . 417 58 72 LEU HD1 H 0.91 . . 418 58 72 LEU HD2 H 0.57 . . 419 58 72 LEU C C 172.6 . . 420 58 72 LEU CA C 59.36 . . 421 58 72 LEU CB C 40.49 . . 422 58 72 LEU N N 122.3 . . 423 59 73 VAL H H 7.99 . . 424 59 73 VAL HA H 3.25 . . 425 59 73 VAL HB H 2.05 . . 426 59 73 VAL HG1 H 0.90 . . 427 59 73 VAL HG2 H 0.62 . . 428 59 73 VAL C C 173.0 . . 429 59 73 VAL CA C 68.69 . . 430 59 73 VAL CB C 31.40 . . 431 59 73 VAL CG1 C 24.29 . . 432 59 73 VAL N N 116.1 . . 433 60 74 GLN H H 7.52 . . 434 60 74 GLN HA H 4.01 . . 435 60 74 GLN HB2 H 2.05 . . 436 60 74 GLN HG2 H 2.41 . . 437 60 74 GLN C C 173.5 . . 438 60 74 GLN CA C 58.60 . . 439 60 74 GLN CB C 28.37 . . 440 60 74 GLN CG C 33.64 . . 441 60 74 GLN N N 116.1 . . 442 61 75 ASN H H 7.88 . . 443 61 75 ASN HA H 4.61 . . 444 61 75 ASN HB2 H 2.79 . . 445 61 75 ASN C C 174.3 . . 446 61 75 ASN CA C 55.18 . . 447 61 75 ASN CB C 39.90 . . 448 61 75 ASN N N 116.5 . . 449 62 76 VAL H H 7.58 . . 450 62 76 VAL HA H 4.59 . . 451 62 76 VAL HB H 2.35 . . 452 62 76 VAL HG1 H 0.88 . . 453 62 76 VAL HG2 H 0.64 . . 454 62 76 VAL C C 175.3 . . 455 62 76 VAL CA C 60.75 . . 456 62 76 VAL CB C 31.11 . . 457 62 76 VAL CG1 C 18.28 . . 458 62 76 VAL CG2 C 21.08 . . 459 62 76 VAL N N 110.35 . . 460 63 77 LYS H H 7.26 . . 461 63 77 LYS HA H 4.12 . . 462 63 77 LYS HB2 H 1.89 . . 463 63 77 LYS C C 174.6 . . 464 63 77 LYS CA C 59.47 . . 465 63 77 LYS CB C 32.16 . . 466 63 77 LYS N N 120.1 . . 467 64 78 ASP H H 8.61 . . 468 64 78 ASP HA H 4.63 . . 469 64 78 ASP HB2 H 2.76 . . 470 64 78 ASP C C 175.1 . . 471 64 78 ASP CA C 54.37 . . 472 64 78 ASP CB C 40.07 . . 473 64 78 ASP N N 116.8 . . 474 65 79 LYS H H 7.87 . . 475 65 79 LYS HA H 4.36 . . 476 65 79 LYS HB2 H 1.61 . . 477 65 79 LYS HB3 H 1.15 . . 478 65 79 LYS HG2 H 1.35 . . 479 65 79 LYS C C 175.6 . . 480 65 79 LYS CA C 54.26 . . 481 65 79 LYS CB C 32.53 . . 482 65 79 LYS N N 120.2 . . 483 66 80 ASP H H 8.23 . . 484 66 80 ASP HA H 4.36 . . 485 66 80 ASP HB2 H 2.58 . . 486 66 80 ASP HB3 H 3.02 . . 487 66 80 ASP C C 170.5 . . 488 66 80 ASP CA C 53.70 . . 489 66 80 ASP CB C 42.86 . . 490 66 80 ASP N N 115.7 . . 491 67 81 THR H H 7.88 . . 492 67 81 THR HA H 5.49 . . 493 67 81 THR HB H 4.03 . . 494 67 81 THR HG2 H 1.03 . . 495 67 81 THR C C 178.5 . . 496 67 81 THR CA C 62.77 . . 497 67 81 THR CB C 73.25 . . 498 67 81 THR CG2 C 20.36 . . 499 67 81 THR N N 119.1 . . 500 68 82 LEU H H 8.81 . . 501 68 82 LEU HA H 5.35 . . 502 68 82 LEU HB2 H 1.84 . . 503 68 82 LEU HB3 H 1.65 . . 504 68 82 LEU HG H 1.29 . . 505 68 82 LEU HD1 H 0.83 . . 506 68 82 LEU HD2 H 0.68 . . 507 68 82 LEU C C 175.4 . . 508 68 82 LEU CA C 52.42 . . 509 68 82 LEU CB C 44.94 . . 510 68 82 LEU CD1 C 24.60 . . 511 68 82 LEU N N 125.9 . . 512 69 83 VAL H H 8.95 . . 513 69 83 VAL HA H 4.74 . . 514 69 83 VAL HB H 2.0 . . 515 69 83 VAL HG1 H 0.79 . . 516 69 83 VAL C C 175.5 . . 517 69 83 VAL CA C 60.94 . . 518 69 83 VAL CB C 33.15 . . 519 69 83 VAL N N 121.8 . . 520 70 84 PHE H H 9.79 . . 521 70 84 PHE HA H 5.24 . . 522 70 84 PHE HB2 H 2.52 . . 523 70 84 PHE HB3 H 3.03 . . 524 70 84 PHE HD1 H 7.12 . . 525 70 84 PHE C C 173.6 . . 526 70 84 PHE CA C 57.68 . . 527 70 84 PHE CB C 43.23 . . 528 70 84 PHE N N 126.4 . . 529 71 85 HIS H H 9.10 . . 530 71 85 HIS HA H 4.98 . . 531 71 85 HIS HB2 H 3.08 . . 532 71 85 HIS HB3 H 3.20 . . 533 71 85 HIS C C 178.9 . . 534 71 85 HIS CA C 55.67 . . 535 71 85 HIS N N 112.7 . . 536 72 86 SER H H 8.59 . . 537 72 86 SER HA H 4.30 . . 538 72 86 SER C C 177.8 . . 539 72 86 SER CA C 55.5 . . 540 72 86 SER N N 112.3 . . 541 73 87 ALA CA C 57.89 . . 542 73 87 ALA CB C 17.93 . . 543 74 88 LEU H H 8.98 . . 544 74 88 LEU C C 173.2 . . 545 74 88 LEU CA C 54.09 . . 546 74 88 LEU N N 114.7 . . 547 75 89 SER H H 7.68 . . 548 75 89 SER HA H 4.27 . . 549 75 89 SER C C 177.9 . . 550 75 89 SER CA C 59.62 . . 551 75 89 SER CB C 64.47 . . 552 75 89 SER N N 111.3 . . 553 76 90 GLN H H 9.81 . . 554 76 90 GLN HA H 4.53 . . 555 76 90 GLN C C 174.5 . . 556 76 90 GLN CA C 57.33 . . 557 76 90 GLN N N 119.0 . . 558 77 91 VAL H H 10.23 . . 559 77 91 VAL HA H 4.27 . . 560 77 91 VAL HB H 1.99 . . 561 77 91 VAL HG1 H 0.98 . . 562 77 91 VAL C C 173.1 . . 563 77 91 VAL CA C 65.9 . . 564 77 91 VAL CB C 33.93 . . 565 77 91 VAL N N 122.3 . . 566 78 92 ARG H H 10.21 . . 567 78 92 ARG C C 172.6 . . 568 78 92 ARG CA C 61.44 . . 569 78 92 ARG N N 124.8 . . 570 79 93 GLY H H 9.86 . . 571 79 93 GLY HA2 H 3.85 . . 572 79 93 GLY HA3 H 3.98 . . 573 79 93 GLY C C 175.9 . . 574 79 93 GLY CA C 46.25 . . 575 79 93 GLY N N 110.8 . . 576 80 94 PRO CA C 65.15 . . 577 80 94 PRO CB C 31.55 . . 578 81 95 THR H H 7.66 . . 579 81 95 THR HA H 3.80 . . 580 81 95 THR HB H 4.24 . . 581 81 95 THR HG2 H 1.20 . . 582 81 95 THR C C 174.0 . . 583 81 95 THR CA C 67.23 . . 584 81 95 THR CB C 68.49 . . 585 81 95 THR N N 112.8 . . 586 82 96 CYS H H 8.19 . . 587 82 96 CYS HA H 3.50 . . 588 82 96 CYS HB2 H 2.30 . . 589 82 96 CYS HB3 H 2.50 . . 590 82 96 CYS C C 175.9 . . 591 82 96 CYS CA C 65.32 . . 592 82 96 CYS CB C 26.93 . . 593 82 96 CYS N N 119.8 . . 594 83 97 ALA H H 7.27 . . 595 83 97 ALA HA H 2.38 . . 596 83 97 ALA HB H 0.64 . . 597 83 97 ALA C C 172.6 . . 598 83 97 ALA CA C 54.86 . . 599 83 97 ALA CB C 17.96 . . 600 83 97 ALA N N 121.3 . . 601 84 98 ARG H H 7.5 . . 602 84 98 ARG HA H 3.72 . . 603 84 98 ARG HB2 H 1.84 . . 604 84 98 ARG HG2 H 1.70 . . 605 84 98 ARG HG3 H 1.60 . . 606 84 98 ARG C C 172.5 . . 607 84 98 ARG CA C 59.48 . . 608 84 98 ARG CB C 29.37 . . 609 84 98 ARG CG C 27.33 . . 610 84 98 ARG N N 115.4 . . 611 85 99 ARG H H 7.93 . . 612 85 99 ARG HA H 4.20 . . 613 85 99 ARG HB2 H 2.07 . . 614 85 99 ARG HG2 H 1.79 . . 615 85 99 ARG HD2 H 3.39 . . 616 85 99 ARG C C 171.8 . . 617 85 99 ARG CA C 58.99 . . 618 85 99 ARG CB C 29.19 . . 619 85 99 ARG CD C 42.49 . . 620 85 99 ARG N N 119.5 . . 621 86 100 LEU H H 8.07 . . 622 86 100 LEU HA H 4.33 . . 623 86 100 LEU HD1 H 0.95 . . 624 86 100 LEU HD2 H 0.65 . . 625 86 100 LEU C C 173.1 . . 626 86 100 LEU CA C 58.54 . . 627 86 100 LEU CB C 40.83 . . 628 86 100 LEU N N 120.1 . . 629 87 101 VAL H H 8.00 . . 630 87 101 VAL HA H 4.32 . . 631 87 101 VAL HB H 2.16 . . 632 87 101 VAL HG1 H 0.96 . . 633 87 101 VAL C C 173.3 . . 634 87 101 VAL CA C 69.43 . . 635 87 101 VAL CB C 31.5 . . 636 87 101 VAL N N 119.7 . . 637 88 102 ASN H H 8.19 . . 638 88 102 ASN HA H 4.48 . . 639 88 102 ASN HB2 H 2.91 . . 640 88 102 ASN HB3 H 3.36 . . 641 88 102 ASN C C 173.8 . . 642 88 102 ASN CA C 56.56 . . 643 88 102 ASN CB C 38.29 . . 644 88 102 ASN N N 117.0 . . 645 89 103 TYR H H 8.30 . . 646 89 103 TYR HA H 4.25 . . 647 89 103 TYR HB2 H 3.15 . . 648 89 103 TYR HB3 H 3.32 . . 649 89 103 TYR HD1 H 6.96 . . 650 89 103 TYR C C 173.2 . . 651 89 103 TYR CA C 62.38 . . 652 89 103 TYR CB C 39.28 . . 653 89 103 TYR N N 122.01 . . 654 90 104 LEU H H 8.73 . . 655 90 104 LEU HA H 3.97 . . 656 90 104 LEU HB2 H 2.04 . . 657 90 104 LEU HB3 H 1.99 . . 658 90 104 LEU C C 171.2 . . 659 90 104 LEU CA C 57.93 . . 660 90 104 LEU CB C 41.06 . . 661 90 104 LEU N N 118.3 . . 662 91 105 ASP H H 8.19 . . 663 91 105 ASP HA H 4.48 . . 664 91 105 ASP HB2 H 2.72 . . 665 91 105 ASP HB3 H 2.86 . . 666 91 105 ASP C C 173.0 . . 667 91 105 ASP CA C 57.11 . . 668 91 105 ASP CB C 41.02 . . 669 91 105 ASP N N 118.8 . . 670 92 106 GLU H H 7.93 . . 671 92 106 GLU HA H 4.06 . . 672 92 106 GLU HB2 H 2.02 . . 673 92 106 GLU HG2 H 2.38 . . 674 92 106 GLU C C 173.1 . . 675 92 106 GLU CA C 58.68 . . 676 92 106 GLU CB C 30.00 . . 677 92 106 GLU CG C 36.42 . . 678 92 106 GLU N N 119.1 . . 679 93 107 LYS H H 7.83 . . 680 93 107 LYS HA H 4.05 . . 681 93 107 LYS HB2 H 1.53 . . 682 93 107 LYS HB3 H 1.73 . . 683 93 107 LYS HG2 H 1.09 . . 684 93 107 LYS HG3 H 1.16 . . 685 93 107 LYS HD2 H 1.41 . . 686 93 107 LYS C C 174.2 . . 687 93 107 LYS CA C 56.13 . . 688 93 107 LYS CB C 31.90 . . 689 93 107 LYS CG C 24.33 . . 690 93 107 LYS CD C 28.13 . . 691 93 107 LYS N N 117.6 . . 692 94 108 LYS H H 7.98 . . 693 94 108 LYS HA H 4.00 . . 694 94 108 LYS HB2 H 1.86 . . 695 94 108 LYS HG2 H 1.37 . . 696 94 108 LYS C C 174.4 . . 697 94 108 LYS CA C 57.52 . . 698 94 108 LYS CB C 30.55 . . 699 94 108 LYS CG C 24.84 . . 700 94 108 LYS N N 117.3 . . 701 95 109 GLU H H 7.81 . . 702 95 109 GLU HA H 4.31 . . 703 95 109 GLU HB2 H 1.92 . . 704 95 109 GLU HB3 H 1.79 . . 705 95 109 GLU HG2 H 2.15 . . 706 95 109 GLU C C 174.8 . . 707 95 109 GLU CA C 56.05 . . 708 95 109 GLU CB C 31.14 . . 709 95 109 GLU CG C 35.98 . . 710 95 109 GLU N N 118.3 . . 711 96 110 ASP H H 8.71 . . 712 96 110 ASP HA H 4.68 . . 713 96 110 ASP HB2 H 2.72 . . 714 96 110 ASP HB3 H 2.61 . . 715 96 110 ASP C C 174.7 . . 716 96 110 ASP CA C 54.45 . . 717 96 110 ASP CB C 40.67 . . 718 96 110 ASP N N 123.6 . . 719 97 111 THR H H 8.30 . . 720 97 111 THR HA H 4.64 . . 721 97 111 THR HB H 4.33 . . 722 97 111 THR HG2 H 1.18 . . 723 97 111 THR C C 176.1 . . 724 97 111 THR CA C 62.02 . . 725 97 111 THR CB C 71.25 . . 726 97 111 THR N N 115.5 . . 727 98 112 GLY H H 8.66 . . 728 98 112 GLY HA2 H 4.11 . . 729 98 112 GLY HA3 H 3.89 . . 730 98 112 GLY C C 176.1 . . 731 98 112 GLY CA C 44.14 . . 732 98 112 GLY N N 111.1 . . 733 99 113 ILE H H 7.91 . . 734 99 113 ILE HA H 3.72 . . 735 99 113 ILE HB H 1.72 . . 736 99 113 ILE HG2 H 0.85 . . 737 99 113 ILE HD1 H 0.67 . . 738 99 113 ILE C C 174.8 . . 739 99 113 ILE CA C 64.09 . . 740 99 113 ILE CB C 37.7 . . 741 99 113 ILE N N 120.2 . . 742 100 114 LYS H H 8.84 . . 743 100 114 LYS HA H 4.53 . . 744 100 114 LYS HB2 H 1.83 . . 745 100 114 LYS HB3 H 1.67 . . 746 100 114 LYS HG2 H 1.43 . . 747 100 114 LYS HG3 H 1.58 . . 748 100 114 LYS C C 174.8 . . 749 100 114 LYS CA C 56.81 . . 750 100 114 LYS CB C 35.11 . . 751 100 114 LYS CG C 24.70 . . 752 100 114 LYS N N 128.8 . . 753 101 115 ASN H H 8.19 . . 754 101 115 ASN HA H 5.16 . . 755 101 115 ASN HB2 H 2.62 . . 756 101 115 ASN HB3 H 2.87 . . 757 101 115 ASN C C 177.5 . . 758 101 115 ASN CA C 52.13 . . 759 101 115 ASN CB C 42.08 . . 760 101 115 ASN N N 116.5 . . 761 102 116 ILE H H 9.01 . . 762 102 116 ILE HA H 4.83 . . 763 102 116 ILE HB H 1.79 . . 764 102 116 ILE HG12 H 1.05 . . 765 102 116 ILE HG13 H 1.46 . . 766 102 116 ILE HG2 H 0.83 . . 767 102 116 ILE HD1 H 0.68 . . 768 102 116 ILE C C 177.4 . . 769 102 116 ILE CA C 61.85 . . 770 102 116 ILE CB C 38.80 . . 771 102 116 ILE N N 125.4 . . 772 103 117 MET H H 9.20 . . 773 103 117 MET HA H 5.67 . . 774 103 117 MET HB2 H 1.87 . . 775 103 117 MET HB3 H 1.77 . . 776 103 117 MET HE H 2.23 . . 777 103 117 MET C C 175.4 . . 778 103 117 MET CA C 52.9 . . 779 103 117 MET CB C 38.36 . . 780 103 117 MET N N 123.7 . . 781 104 118 ILE H H 8.63 . . 782 104 118 ILE HA H 4.77 . . 783 104 118 ILE HG12 H 1.08 . . 784 104 118 ILE HG2 H 0.73 . . 785 104 118 ILE HD1 H 0.44 . . 786 104 118 ILE C C 175.3 . . 787 104 118 ILE CA C 59.4 . . 788 104 118 ILE CB C 40.24 . . 789 104 118 ILE CG2 C 18.47 . . 790 104 118 ILE CD1 C 14.62 . . 791 104 118 ILE N N 120.2 . . 792 105 119 LEU H H 8.46 . . 793 105 119 LEU HA H 4.90 . . 794 105 119 LEU HB2 H 1.92 . . 795 105 119 LEU HG H 0.80 . . 796 105 119 LEU HD1 H 0.34 . . 797 105 119 LEU HD2 H 0.94 . . 798 105 119 LEU C C 175.3 . . 799 105 119 LEU CA C 53.50 . . 800 105 119 LEU CB C 42.61 . . 801 105 119 LEU CD1 C 25.49 . . 802 105 119 LEU N N 125.6 . . 803 106 120 GLU H H 9.73 . . 804 106 120 GLU HA H 4.51 . . 805 106 120 GLU HB2 H 2.08 . . 806 106 120 GLU HB3 H 2.14 . . 807 106 120 GLU HG2 H 2.32 . . 808 106 120 GLU CA C 58.4 . . 809 106 120 GLU CB C 30.82 . . 810 106 120 GLU N N 138.6 . . 811 107 121 ARG H H 10.02 . . 812 107 121 ARG HA H 4.05 . . 813 107 121 ARG HB2 H 1.73 . . 814 107 121 ARG HB3 H 1.84 . . 815 107 121 ARG C C 173.1 . . 816 107 121 ARG CA C 59.83 . . 817 107 121 ARG N N 121.4 . . 818 108 122 GLY H H 7.77 . . 819 108 122 GLY HA2 H 3.77 . . 820 108 122 GLY C C 177.3 . . 821 108 122 GLY CA C 46.3 . . 822 108 122 GLY N N 101.6 . . 823 109 123 PHE H H 8.28 . . 824 109 123 PHE HA H 3.66 . . 825 109 123 PHE HB2 H 2.96 . . 826 109 123 PHE C C 173.3 . . 827 109 123 PHE CA C 62.82 . . 828 109 123 PHE CB C 39.84 . . 829 109 123 PHE N N 119.6 . . 830 110 124 ASN H H 9.60 . . 831 110 124 ASN HA H 3.66 . . 832 110 124 ASN HB2 H 2.90 . . 833 110 124 ASN C C 172.5 . . 834 110 124 ASN CA C 57.06 . . 835 110 124 ASN CB C 36.93 . . 836 110 124 ASN N N 119.3 . . 837 111 125 GLY H H 7.77 . . 838 111 125 GLY HA2 H 3.97 . . 839 111 125 GLY HA3 H 3.70 . . 840 111 125 GLY CA C 46.08 . . 841 111 125 GLY N N 105.3 . . 842 112 126 TRP H H 7.27 . . 843 112 126 TRP HA H 3.80 . . 844 112 126 TRP HB3 H 3.21 . . 845 112 126 TRP HD1 H 6.09 . . 846 112 126 TRP HE1 H 10.39 . . 847 112 126 TRP HZ2 H 6.87 . . 848 112 126 TRP C C 174.2 . . 849 112 126 TRP CA C 61.53 . . 850 112 126 TRP CB C 27.64 . . 851 112 126 TRP N N 126.7 . . 852 113 127 GLU H H 8.27 . . 853 113 127 GLU HA H 3.55 . . 854 113 127 GLU HB2 H 1.38 . . 855 113 127 GLU HB3 H 1.79 . . 856 113 127 GLU HG2 H 2.16 . . 857 113 127 GLU HG3 H 2.28 . . 858 113 127 GLU C C 170.6 . . 859 113 127 GLU CA C 60.01 . . 860 113 127 GLU CB C 29.12 . . 861 113 127 GLU CG C 35.98 . . 862 113 127 GLU N N 118.7 . . 863 114 128 ALA H H 8.35 . . 864 114 128 ALA HA H 4.11 . . 865 114 128 ALA HB H 1.49 . . 866 114 128 ALA C C 172.4 . . 867 114 128 ALA CA C 54.8 . . 868 114 128 ALA CB C 18.41 . . 869 114 128 ALA N N 121.2 . . 870 115 129 SER H H 7.41 . . 871 115 129 SER HA H 3.85 . . 872 115 129 SER HB2 H 4.46 . . 873 115 129 SER C C 175.5 . . 874 115 129 SER CA C 58.57 . . 875 115 129 SER CB C 63.45 . . 876 115 129 SER N N 109.5 . . 877 116 130 GLY H H 7.73 . . 878 116 130 GLY HA2 H 3.74 . . 879 116 130 GLY HA3 H 4.01 . . 880 116 130 GLY C C 175.9 . . 881 116 130 GLY CA C 44.81 . . 882 116 130 GLY N N 109.0 . . 883 117 131 LYS H H 6.85 . . 884 117 131 LYS HA H 3.96 . . 885 117 131 LYS HB2 H 0.69 . . 886 117 131 LYS HB3 H 0.89 . . 887 117 131 LYS HG2 H -0.08 . . 888 117 131 LYS HG3 H -0.60 . . 889 117 131 LYS C C 177.1 . . 890 117 131 LYS CA C 54.22 . . 891 117 131 LYS CB C 27.90 . . 892 117 131 LYS CG C 26.83 . . 893 117 131 LYS N N 119.5 . . 894 118 132 PRO HD3 H 3.60 . . 895 118 132 PRO C C 172.7 . . 896 118 132 PRO CA C 63.85 . . 897 118 132 PRO CB C 32.01 . . 898 118 132 PRO CD C 50.24 . . 899 119 133 VAL H H 9.02 . . 900 119 133 VAL HA H 4.39 . . 901 119 133 VAL HB H 2.10 . . 902 119 133 VAL HG1 H 1.13 . . 903 119 133 VAL HG2 H 1.09 . . 904 119 133 VAL C C 176.9 . . 905 119 133 VAL CA C 62.55 . . 906 119 133 VAL CB C 35.92 . . 907 119 133 VAL CG1 C 22.65 . . 908 119 133 VAL CG2 C 21.30 . . 909 119 133 VAL N N 126.8 . . 910 120 134 CYS H H 9.23 . . 911 120 134 CYS HA H 4.31 . . 912 120 134 CYS HB2 H 2.25 . . 913 120 134 CYS HB3 H 2.56 . . 914 120 134 CYS C C 172.14 . . 915 120 134 CYS CA C 59.68 . . 916 120 134 CYS CB C 30.50 . . 917 120 134 CYS N N 130.6 . . 918 121 135 ARG H H 8.51 . . 919 121 135 ARG HA H 4.43 . . 920 121 135 ARG C C 174.4 . . 921 121 135 ARG CA C 54.42 . . 922 121 135 ARG N N 126.7 . . 923 122 136 CYS H H 9.01 . . 924 122 136 CYS HA H 4.66 . . 925 122 136 CYS HB2 H 3.10 . . 926 122 136 CYS HB3 H 3.36 . . 927 122 136 CYS C C 175.52 . . 928 122 136 CYS CA C 61.04 . . 929 122 136 CYS CB C 28.77 . . 930 122 136 CYS N N 123.5 . . 931 123 137 ALA H H 8.8 . . 932 123 137 ALA HA H 4.73 . . 933 123 137 ALA HB H 1.39 . . 934 123 137 ALA C C 173.2 . . 935 123 137 ALA CA C 49.98 . . 936 123 137 ALA CB C 19.56 . . 937 123 137 ALA N N 122.1 . . 938 124 138 GLU H H 8.04 . . 939 124 138 GLU HA H 4.32 . . 940 124 138 GLU HB2 H 2.08 . . 941 124 138 GLU HB3 H 2.14 . . 942 124 138 GLU HG2 H 2.27 . . 943 124 138 GLU HG3 H 2.40 . . 944 124 138 GLU C C 175.3 . . 945 124 138 GLU CA C 56.46 . . 946 124 138 GLU N N 121.3 . . 947 125 139 VAL H H 8.35 . . 948 125 139 VAL HA H 4.11 . . 949 125 139 VAL C C 176.1 . . 950 125 139 VAL CA C 59.70 . . 951 125 139 VAL N N 121.2 . . 952 127 141 CYS CA C 60.84 . . 953 127 141 CYS CB C 28.86 . . 954 128 142 LYS H H 9.02 . . 955 128 142 LYS HA H 4.38 . . 956 128 142 LYS HB2 H 1.81 . . 957 128 142 LYS HB3 H 1.93 . . 958 128 142 LYS HG2 H 1.79 . . 959 128 142 LYS HD2 H 1.47 . . 960 128 142 LYS C C 173.1 . . 961 128 142 LYS CA C 56.46 . . 962 128 142 LYS CB C 32.98 . . 963 128 142 LYS N N 130.5 . . 964 129 143 GLY H H 9.51 . . 965 129 143 GLY HA2 H 3.93 . . 966 129 143 GLY C C 176.5 . . 967 129 143 GLY CA C 44.86 . . 968 129 143 GLY N N 113.5 . . 969 130 144 ASP H H 8.41 . . 970 130 144 ASP HA H 4.72 . . 971 130 144 ASP HB2 H 2.71 . . 972 130 144 ASP C C 174.8 . . 973 130 144 ASP CA C 54.01 . . 974 130 144 ASP CB C 41.32 . . 975 130 144 ASP N N 120.6 . . 976 131 145 SER H H 8.3 . . 977 131 145 SER HA H 3.93 . . 978 131 145 SER C C 176.2 . . 979 131 145 SER CA C 58.78 . . 980 131 145 SER CB C 64.18 . . 981 131 145 SER N N 115.9 . . 982 132 146 ALA H H 7.77 . . 983 132 146 ALA HA H 4.51 . . 984 132 146 ALA HB H 1.36 . . 985 132 146 ALA C C 169.2 . . 986 132 146 ALA CA C 53.9 . . 987 132 146 ALA N N 131.4 . . stop_ save_