data_4637 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE MATA1 HOMEODOMAIN ; _BMRB_accession_number 4637 _BMRB_flat_file_name bmr4637.str _Entry_type original _Submission_date 2000-06-07 _Accession_date 2001-03-16 _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 Anderson J. S. . 2 Forman M. . . 3 Modleski S. . . 4 Dahlquist F. W. . 5 Baxter S. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 311 "13C chemical shifts" 119 "15N chemical shifts" 58 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-09 original author . stop_ _Original_release_date 2001-07-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10955992 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Anderson J. S. . 2 Forman M. . . 3 Modleski S. . . 4 Dahlquist F. W. . 5 Baxter S. M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10045 _Page_last 10054 _Year 2000 _Details . loop_ _Keyword Homeodomain helix-turn-helix stop_ save_ ################################## # Molecular system description # ################################## save_system_MATa1 _Saveframe_category molecular_system _Mol_system_name 'MATING-TYPE PROTEIN A-1' _Abbreviation_common MATa1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MATING-TYPE PROTEIN A-1' $MATa1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MATa1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MATING-TYPE PROTEIN A-1' _Abbreviation_common MATa1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; KKEKSPKGKSSISPQARAFL EQVFRRKQSLNSKEKEEVAK KCGITPLQVRVWFINKRMRS K ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 LYS 2 -2 LYS 3 -1 GLU 4 0 LYS 5 1 SER 6 2 PRO 7 3 LYS 8 4 GLY 9 5 LYS 10 6 SER 11 7 SER 12 8 ILE 13 9 SER 14 10 PRO 15 11 GLN 16 12 ALA 17 13 ARG 18 14 ALA 19 15 PHE 20 16 LEU 21 17 GLU 22 18 GLN 23 19 VAL 24 20 PHE 25 21 ARG 26 22 ARG 27 23 LYS 28 24 GLN 29 25 SER 30 26 LEU 31 27 ASN 32 28 SER 33 29 LYS 34 30 GLU 35 31 LYS 36 32 GLU 37 33 GLU 38 34 VAL 39 35 ALA 40 36 LYS 41 37 LYS 42 38 CYS 43 39 GLY 44 40 ILE 45 41 THR 46 42 PRO 47 43 LEU 48 44 GLN 49 45 VAL 50 46 ARG 51 47 VAL 52 48 TRP 53 49 PHE 54 50 ILE 55 51 ASN 56 52 LYS 57 53 ARG 58 54 MET 59 55 ARG 60 56 SER 61 57 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1AKH "Mat A1ALPHA2DNA TERNARY COMPLEX" 100.00 61 98.36 100.00 7.39e-33 PDB 1F43 "Solution Structure Of The Mata1 Homeodomain" 100.00 61 100.00 100.00 2.12e-33 PDB 1LE8 "Crystal Structure Of The Mata1MATALPHA2-3a Heterodimer Bound To Dna Complex" 86.89 53 100.00 100.00 4.68e-28 PDB 1YRN "Crystal Structure Of The Mata1MATALPHA2 HOMEODOMAIN Heterodimer Bound To Dna" 100.00 61 100.00 100.00 2.12e-33 DBJ GAA21999 "K7_Hmra1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 126 100.00 100.00 2.86e-34 EMBL CAA42252 "mating type regulatory protein, silenced copy at HMR locus [Saccharomyces cerevisiae]" 100.00 126 100.00 100.00 3.02e-34 EMBL CAY78246 "Hmra1p [Saccharomyces cerevisiae EC1118]" 100.00 126 100.00 100.00 3.15e-34 EMBL CAY78300 "Hmra1p [Saccharomyces cerevisiae EC1118]" 100.00 126 100.00 100.00 3.15e-34 GB AHY79765 "Hmra1p [Saccharomyces cerevisiae YJM993]" 100.00 126 100.00 100.00 3.05e-34 GB AJP37516 "Hmra1p [Saccharomyces cerevisiae YJM1078]" 100.00 126 100.00 100.00 3.15e-34 GB AJQ32001 "Hmra1p [Saccharomyces cerevisiae YJM1356]" 100.00 126 100.00 100.00 3.02e-34 GB AJQ32146 "Hmra1p [Saccharomyces cerevisiae YJM1381]" 100.00 126 100.00 100.00 3.15e-34 GB AJQ32291 "Hmra1p [Saccharomyces cerevisiae YJM1383]" 100.00 126 100.00 100.00 3.02e-34 REF NP_010021 "Hmra1p [Saccharomyces cerevisiae S288c]" 100.00 126 100.00 100.00 3.02e-34 SP P0CY10 "RecName: Full=Mating-type protein A1; Short=MATa1 protein" 100.00 126 100.00 100.00 3.02e-34 SP P0CY11 "RecName: Full=Silenced mating-type protein A1; Short=MATa1 protein" 100.00 126 100.00 100.00 3.02e-34 TPG DAA07567 "TPA: Hmra1p [Saccharomyces cerevisiae S288c]" 100.00 126 100.00 100.00 3.02e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MATa1 'baker's yeast' 4932 Eukaryota fungi Saccaromyces cerevisiae 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 $MATa1 'recombinant technology' 'E. coli' Escherichia coli . PCW/AL66-126 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 $MATa1 1.5 mM '[U-15N; U-13C]' acetate 25 mM [U-2H] KCl 100 mM . NaN3 0.01 % . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MATa1 1.5 mM [U-15N] acetate 25 mM [U-2H] KCl 100 mM . NaN3 0.01 % . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MATa1 1.5 mM . acetate 25 mM [U-2H] KCl 100 mM . NaN3 0.01 % . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.3 loop_ _Task collection stop_ _Details 'Bruker Instruments' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 970 loop_ _Task 'data analysis' processing stop_ _Details 'Molecular Simulations, Inc.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details 'A. Brunger' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNCA-J_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA-J _Sample_label . save_ save_2D_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_DQF-COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . pH temperature 298 . K 'ionic strength' 100 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $entry_citation $entry_citation . C 13 . ppm . . . . . . $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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'MATING-TYPE PROTEIN A-1' _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 LYS H H 8.67 . 1 2 . 1 LYS HA H 4.32 . 1 3 . 1 LYS CA C 53.2 . 1 4 . 1 LYS CB C 29.7 . 1 5 . 1 LYS N N 127.30 . 1 6 . 2 LYS H H 8.50 . 1 7 . 2 LYS HA H 4.21 . 1 8 . 2 LYS CA C 53.3 . 1 9 . 2 LYS CB C 30.0 . 1 10 . 2 LYS N N 126.94 . 1 11 . 3 GLU H H 8.50 . 1 12 . 3 GLU HA H 4.26 . 1 13 . 3 GLU CA C 53.2 . 1 14 . 3 GLU CB C 27.5 . 1 15 . 3 GLU N N 125.60 . 1 16 . 4 LYS H H 8.50 . 1 17 . 4 LYS HA H 4.26 . 1 18 . 4 LYS CA C 53.2 . 1 19 . 4 LYS CB C 30.0 . 1 20 . 4 LYS N N 125.59 . 1 21 . 5 SER H H 8.44 . 1 22 . 5 SER HA H 4.50 . 1 23 . 5 SER HB2 H 3.82 . 2 24 . 5 SER HB3 H 3.84 . 2 25 . 5 SER CA C 53.4 . 1 26 . 5 SER CB C 59.6 . 1 27 . 5 SER N N 119.82 . 1 28 . 6 PRO HA H 4.24 . 1 29 . 6 PRO CA C 59.6 . 1 30 . 7 LYS H H 8.37 . 1 31 . 7 LYS CA C 53.4 . 1 32 . 7 LYS CB C 29.4 . 1 33 . 7 LYS N N 124.23 . 1 34 . 8 GLY H H 8.39 . 1 35 . 8 GLY HA2 H 3.89 . 1 36 . 8 GLY HA3 H 3.89 . 1 37 . 8 GLY CA C 42.0 . 1 38 . 8 GLY N N 112.70 . 1 39 . 9 LYS H H 8.19 . 1 40 . 9 LYS HA H 4.36 . 1 41 . 9 LYS CA C 53.4 . 1 42 . 9 LYS CB C 30.5 . 1 43 . 9 LYS N N 123.55 . 1 44 . 10 SER H H 8.41 . 1 45 . 10 SER HA H 4.50 . 1 46 . 10 SER HB2 H 3.80 . 2 47 . 10 SER HB3 H 2.83 . 2 48 . 10 SER CA C 53.4 . 1 49 . 10 SER CB C 59.6 . 1 50 . 10 SER N N 120.84 . 1 51 . 11 SER H H 8.39 . 1 52 . 11 SER HA H 4.50 . 1 53 . 11 SER HB2 H 3.81 . 1 54 . 11 SER HB3 H 3.81 . 1 55 . 11 SER CA C 53.4 . 1 56 . 11 SER CB C 59.6 . 1 57 . 11 SER N N 121.52 . 1 58 . 12 ILE H H 8.10 . 1 59 . 12 ILE HA H 4.20 . 1 60 . 12 ILE HB H 1.77 . 1 61 . 12 ILE HG12 H 1.55 . 2 62 . 12 ILE HG13 H 1.02 . 2 63 . 12 ILE HG2 H 0.83 . 1 64 . 12 ILE HD1 H 0.72 . 1 65 . 12 ILE CA C 57.5 . 1 66 . 12 ILE CB C 35.8 . 1 67 . 12 ILE N N 123.55 . 1 68 . 13 SER H H 8.73 . 1 69 . 13 SER HA H 4.64 . 1 70 . 13 SER HB2 H 4.06 . 1 71 . 13 SER HB3 H 4.06 . 1 72 . 13 SER CA C 53.8 . 1 73 . 13 SER CB C 59.5 . 1 74 . 13 SER N N 127.30 . 1 75 . 14 PRO HA H 4.19 . 1 76 . 14 PRO HB2 H 2.19 . 2 77 . 14 PRO HB3 H 2.38 . 2 78 . 14 PRO HG2 H 3.65 . 2 79 . 14 PRO HG3 H 3.90 . 2 80 . 14 PRO HD2 H 1.94 . 2 81 . 14 PRO HD3 H 2.04 . 2 82 . 14 PRO CA C 62.5 . 1 83 . 14 PRO CB C 27.7 . 1 84 . 15 GLN H H 8.45 . 1 85 . 15 GLN HA H 4.08 . 1 86 . 15 GLN HB2 H 1.93 . 2 87 . 15 GLN HB3 H 2.07 . 2 88 . 15 GLN HG2 H 2.40 . 1 89 . 15 GLN HG3 H 2.40 . 1 90 . 15 GLN HE21 H 6.85 . 2 91 . 15 GLN HE22 H 7.62 . 2 92 . 15 GLN CA C 56.5 . 1 93 . 15 GLN CB C 24.4 . 1 94 . 15 GLN N N 120.16 . 1 95 . 16 ALA H H 7.98 . 1 96 . 16 ALA HA H 4.12 . 1 97 . 16 ALA HB H 1.42 . 1 98 . 16 ALA CA C 51.7 . 1 99 . 16 ALA CB C 16.0 . 1 100 . 16 ALA N N 127.28 . 1 101 . 17 ARG H H 8.46 . 1 102 . 17 ARG HA H 3.45 . 1 103 . 17 ARG HB2 H 1.79 . 2 104 . 17 ARG HB3 H 1.88 . 2 105 . 17 ARG HG2 H 1.59 . 2 106 . 17 ARG HG3 H 1.70 . 2 107 . 17 ARG HD2 H 3.23 . 2 108 . 17 ARG HD3 H 3.33 . 2 109 . 17 ARG CA C 56.5 . 1 110 . 17 ARG CB C 27.4 . 1 111 . 17 ARG N N 120.16 . 1 112 . 18 ALA H H 7.77 . 1 113 . 18 ALA HA H 3.90 . 1 114 . 18 ALA HB H 1.43 . 1 115 . 18 ALA CA C 51.2 . 1 116 . 18 ALA CB C 15.0 . 1 117 . 18 ALA N N 122.87 . 1 118 . 19 PHE H H 7.62 . 1 119 . 19 PHE HA H 4.21 . 1 120 . 19 PHE HB2 H 3.15 . 2 121 . 19 PHE HB3 H 3.21 . 2 122 . 19 PHE HD1 H 7.11 . 3 123 . 19 PHE HD2 H 7.12 . 3 124 . 19 PHE HE1 H 7.26 . 1 125 . 19 PHE HE2 H 7.26 . 1 126 . 19 PHE CA C 57.5 . 1 127 . 19 PHE CB C 35.8 . 1 128 . 19 PHE N N 122.87 . 1 129 . 20 LEU H H 8.36 . 1 130 . 20 LEU HA H 3.41 . 1 131 . 20 LEU HB2 H 1.53 . 2 132 . 20 LEU HB3 H -0.21 . 4 133 . 20 LEU HG H 0.548 . 4 134 . 20 LEU HD1 H -0.65 . 4 135 . 20 LEU CA C 55.4 . 1 136 . 20 LEU CB C 35.0 . 1 137 . 20 LEU N N 123.55 . 1 138 . 21 GLU H H 8.09 . 1 139 . 21 GLU HA H 4.09 . 1 140 . 21 GLU HB2 H 2.09 . 2 141 . 21 GLU HG2 H 2.54 . 2 142 . 21 GLU CA C 55.3 . 1 143 . 21 GLU CB C 26.0 . 1 144 . 21 GLU N N 118.80 . 1 145 . 22 GLN H H 7.46 . 1 146 . 22 GLN HA H 3.97 . 1 147 . 22 GLN HB2 H 2.03 . 2 148 . 22 GLN HB3 H 2.12 . 2 149 . 22 GLN HG2 H 2.26 . 2 150 . 22 GLN HG3 H 2.43 . 2 151 . 22 GLN HE21 H 7.08 . 2 152 . 22 GLN HE22 H 7.15 . 2 153 . 22 GLN CA C 55.4 . 1 154 . 22 GLN CB C 25.5 . 1 155 . 22 GLN N N 121.52 . 1 156 . 23 VAL H H 8.04 . 1 157 . 23 VAL HA H 3.49 . 1 158 . 23 VAL HB H 2.15 . 1 159 . 23 VAL HG1 H 0.64 . 2 160 . 23 VAL HG2 H 1.03 . 2 161 . 23 VAL CA C 62.6 . 1 162 . 23 VAL CB C 28.6 . 1 163 . 23 VAL N N 123.55 . 1 164 . 24 PHE H H 8.75 . 1 165 . 24 PHE HA H 4.65 . 1 166 . 24 PHE HB2 H 3.13 . 1 167 . 24 PHE HB3 H 3.16 . 1 168 . 24 PHE HD1 H 7.14 . 3 169 . 24 PHE HD2 H 7.15 . 3 170 . 24 PHE HE1 H 7.53 . 3 171 . 24 PHE HZ H 7.30 . 1 172 . 24 PHE CA C 56.2 . 1 173 . 24 PHE CB C 36.0 . 1 174 . 24 PHE N N 122.87 . 1 175 . 25 ARG H H 7.44 . 1 176 . 25 ARG HA H 3.96 . 1 177 . 25 ARG HB2 H 1.71 . 4 178 . 25 ARG HB3 H 1.90 . 4 179 . 25 ARG HG2 H 1.71 . 4 180 . 25 ARG HD2 H 3.16 . 2 181 . 25 ARG CA C 55.4 . 1 182 . 25 ARG CB C 27.6 . 1 183 . 25 ARG N N 116.77 . 1 184 . 26 ARG H H 7.59 . 1 185 . 26 ARG HA H 4.28 . 1 186 . 26 ARG HB2 H 1.86 . 1 187 . 26 ARG HB3 H 1.86 . 1 188 . 26 ARG HG2 H 1.62 . 2 189 . 26 ARG HD2 H 3.16 . 2 190 . 26 ARG CA C 54.2 . 1 191 . 26 ARG CB C 28.2 . 1 192 . 26 ARG N N 119.48 . 1 193 . 27 LYS H H 8.55 . 1 194 . 27 LYS HA H 4.26 . 1 195 . 27 LYS HB2 H 1.75 . 1 196 . 27 LYS HB3 H 1.75 . 1 197 . 27 LYS HG2 H 1.29 . 2 198 . 27 LYS HG3 H 1.32 . 2 199 . 27 LYS HD2 H 1.56 . 2 200 . 27 LYS CA C 53.4 . 1 201 . 27 LYS CB C 31.6 . 1 202 . 27 LYS N N 124.23 . 1 203 . 28 GLN H H 7.91 . 1 204 . 28 GLN HA H 4.12 . 1 205 . 28 GLN HB2 H 2.00 . 2 206 . 28 GLN HG2 H 1.62 . 2 207 . 28 GLN HG3 H 1.75 . 2 208 . 28 GLN HE21 H 6.51 . 2 209 . 28 GLN HE22 H 7.32 . 2 210 . 28 GLN CA C 53.3 . 1 211 . 28 GLN CB C 31.5 . 1 212 . 28 GLN N N 120.16 . 1 213 . 29 SER H H 7.42 . 1 214 . 29 SER HA H 4.52 . 1 215 . 29 SER HB2 H 3.68 . 2 216 . 29 SER HB3 H 2.69 . 2 217 . 29 SER CA C 53.4 . 1 218 . 29 SER CB C 61.6 . 1 219 . 29 SER N N 113.76 . 1 220 . 30 LEU H H 8.19 . 1 221 . 30 LEU HA H 4.52 . 1 222 . 30 LEU HB2 H 1.21 . 2 223 . 30 LEU HB3 H 1.30 . 2 224 . 30 LEU HG H 0.77 . 1 225 . 30 LEU HD1 H 0.26 . 2 226 . 30 LEU HD2 H 0.47 . 2 227 . 30 LEU CA C 50.1 . 1 228 . 30 LEU CB C 41.9 . 1 229 . 30 LEU N N 125.93 . 1 230 . 31 ASN H H 9.24 . 1 231 . 31 ASN HA H 4.71 . 1 232 . 31 ASN HB2 H 2.80 . 2 233 . 31 ASN HB3 H 3.31 . 2 234 . 31 ASN HD21 H 6.81 . 2 235 . 31 ASN HD22 H 7.37 . 2 236 . 31 ASN CA C 48.2 . 1 237 . 31 ASN CB C 34.7 . 1 238 . 31 ASN N N 124.57 . 1 239 . 32 SER H H 8.46 . 1 240 . 32 SER HA H 3.93 . 1 241 . 32 SER HB2 H 3.22 . 2 242 . 32 SER HB3 H 3.48 . 2 243 . 32 SER CA C 59.6 . 1 244 . 32 SER CB C 61.8 . 1 245 . 32 SER N N 115.76 . 1 246 . 33 LYS H H 7.90 . 1 247 . 33 LYS HB2 H 1.82 . 2 248 . 33 LYS HB3 H 1.83 . 2 249 . 33 LYS HG2 H 1.38 . 2 250 . 33 LYS HG3 H 1.44 . 2 251 . 33 LYS HD2 H 1.62 . 2 252 . 33 LYS HE2 H 3.26 . 2 253 . 33 LYS HE3 H 3.49 . 2 254 . 33 LYS CA C 55.4 . 1 255 . 33 LYS CB C 29.0 . 1 256 . 33 LYS N N 125.93 . 1 257 . 34 GLU H H 8.60 . 1 258 . 34 GLU HA H 4.01 . 1 259 . 34 GLU HB2 H 2.14 . 2 260 . 34 GLU HB3 H 2.17 . 2 261 . 34 GLU HG2 H 2.47 . 2 262 . 34 GLU HG3 H 2.51 . 2 263 . 34 GLU CA C 55.4 . 1 264 . 34 GLU CB C 27.6 . 1 265 . 34 GLU N N 122.87 . 1 266 . 35 LYS H H 8.55 . 1 267 . 35 LYS HA H 3.72 . 1 268 . 35 LYS HB2 H 1.90 . 2 269 . 35 LYS HG2 H 1.02 . 2 270 . 35 LYS HG3 H 1.38 . 2 271 . 35 LYS HD2 H 1.62 . 2 272 . 35 LYS HD3 H 1.65 . 2 273 . 35 LYS HE2 H 2.89 . 2 274 . 35 LYS CA C 57.5 . 1 275 . 35 LYS CB C 29.6 . 1 276 . 35 LYS N N 120.84 . 1 277 . 36 GLU H H 7.55 . 1 278 . 36 GLU HA H 3.89 . 1 279 . 36 GLU HB2 H 2.14 . 2 280 . 36 GLU HB3 H 2.22 . 2 281 . 36 GLU HG2 H 2.46 . 2 282 . 36 GLU CA C 56.5 . 1 283 . 36 GLU CB C 25.7 . 1 284 . 36 GLU N N 119.82 . 1 285 . 37 GLU H H 8.05 . 1 286 . 37 GLU HA H 4.03 . 1 287 . 37 GLU HB2 H 2.09 . 2 288 . 37 GLU HB3 H 2.18 . 2 289 . 37 GLU HG2 H 2.28 . 2 290 . 37 GLU HG3 H 2.44 . 2 291 . 37 GLU CA C 55.8 . 1 292 . 37 GLU CB C 26.5 . 1 293 . 37 GLU N N 122.81 . 1 294 . 38 VAL H H 8.59 . 1 295 . 38 VAL HA H 3.62 . 1 296 . 38 VAL HB H 2.11 . 1 297 . 38 VAL HG1 H 0.99 . 2 298 . 38 VAL HG2 H 1.15 . 2 299 . 38 VAL CA C 63.7 . 1 300 . 38 VAL CB C 28.5 . 1 301 . 38 VAL N N 123.55 . 1 302 . 39 ALA H H 8.16 . 1 303 . 39 ALA HA H 3.51 . 1 304 . 39 ALA HB H 1.39 . 1 305 . 39 ALA CA C 52.4 . 1 306 . 39 ALA CB C 14.5 . 1 307 . 39 ALA N N 124.57 . 1 308 . 40 LYS H H 7.70 . 1 309 . 40 LYS HA H 4.03 . 1 310 . 40 LYS HB2 H 1.87 . 2 311 . 40 LYS HB3 H 1.90 . 2 312 . 40 LYS HG2 H 1.37 . 4 313 . 40 LYS HG3 H 1.53 . 4 314 . 40 LYS CA C 55.4 . 1 315 . 40 LYS CB C 29.6 . 1 316 . 40 LYS N N 118.8 . 1 317 . 41 LYS H H 7.77 . 1 318 . 41 LYS HA H 3.92 . 1 319 . 41 LYS HB2 H 1.66 . 4 320 . 41 LYS HB3 H 1.70 . 4 321 . 41 LYS HG2 H 1.27 . 4 322 . 41 LYS CA C 55.3 . 1 323 . 41 LYS CB C 29.5 . 1 324 . 41 LYS N N 121.5 . 1 325 . 42 CYS H H 7.69 . 1 326 . 42 CYS HA H 4.26 . 1 327 . 42 CYS HB2 H 2.56 . 2 328 . 42 CYS HB3 H 2.75 . 2 329 . 42 CYS CA C 56.5 . 1 330 . 42 CYS CB C 26.5 . 1 331 . 42 CYS N N 114.4 . 1 332 . 43 GLY H H 7.85 . 1 333 . 43 GLY HA2 H 3.92 . 2 334 . 43 GLY CA C 44.1 . 1 335 . 43 GLY N N 112.7 . 1 336 . 44 ILE H H 7.74 . 1 337 . 44 ILE HA H 4.92 . 1 338 . 44 ILE HB H 2.21 . 1 339 . 44 ILE HG12 H 0.75 . 2 340 . 44 ILE HG13 H 0.89 . 2 341 . 44 ILE HG2 H 1.31 . 1 342 . 44 ILE HD1 H 0.59 . 1 343 . 44 ILE CA C 55.4 . 1 344 . 44 ILE CB C 36.7 . 1 345 . 44 ILE N N 115.41 . 1 346 . 45 THR H H 8.43 . 1 347 . 45 THR HA H 4.84 . 1 348 . 45 THR HB H 2.47 . 1 349 . 45 THR HG2 H 1.28 . 1 350 . 45 THR CA C 56.5 . 1 351 . 45 THR CB C 65.6 . 1 352 . 45 THR N N 112.02 . 1 353 . 46 PRO HB2 H 2.18 . 2 354 . 46 PRO HB3 H 2.28 . 2 355 . 46 PRO HG2 H 1.83 . 2 356 . 46 PRO HG3 H 1.98 . 2 357 . 46 PRO HD2 H 3.82 . 2 358 . 46 PRO CA C 62.6 . 1 359 . 46 PRO CB C 29.4 . 1 360 . 47 LEU H H 7.75 . 1 361 . 47 LEU HA H 4.18 . 1 362 . 47 LEU HB2 H 1.61 . 2 363 . 47 LEU HB3 H 1.64 . 2 364 . 47 LEU HG H 1.31 . 1 365 . 47 LEU HD1 H 0.86 . 2 366 . 47 LEU HD2 H 0.91 . 2 367 . 47 LEU CA C 55.3 . 1 368 . 47 LEU CB C 38.9 . 1 369 . 47 LEU N N 120.84 . 1 370 . 48 GLN H H 7.83 . 1 371 . 48 GLN HA H 3.99 . 1 372 . 48 GLN HB2 H 1.86 . 2 373 . 48 GLN HG2 H 2.39 . 2 374 . 48 GLN HG3 H 2.45 . 2 375 . 48 GLN HE21 H 6.80 . 2 376 . 48 GLN HE22 H 7.39 . 2 377 . 48 GLN CA C 55.4 . 1 378 . 48 GLN CB C 26.5 . 1 379 . 48 GLN N N 120.16 . 1 380 . 49 VAL H H 7.84 . 1 381 . 49 VAL HA H 3.59 . 1 382 . 49 VAL HB H 2.37 . 1 383 . 49 VAL HG1 H 0.94 . 2 384 . 49 VAL HG2 H 0.99 . 2 385 . 49 VAL CA C 63.7 . 1 386 . 49 VAL CB C 28.5 . 1 387 . 49 VAL N N 122.20 . 1 388 . 50 ARG H H 8.26 . 1 389 . 50 ARG HA H 4.07 . 1 390 . 50 ARG HB2 H 2.20 . 2 391 . 50 ARG HB3 H 2.39 . 2 392 . 50 ARG HG2 H 1.54 . 4 393 . 50 ARG HG3 H 1.88 . 4 394 . 50 ARG HD2 H 3.23 . 2 395 . 50 ARG CA C 56.8 . 1 396 . 50 ARG CB C 27.6 . 1 397 . 50 ARG N N 122.53 . 1 398 . 51 VAL H H 8.57 . 1 399 . 51 VAL HA H 3.59 . 1 400 . 51 VAL HB H 2.07 . 1 401 . 51 VAL HG1 H 0.92 . 2 402 . 51 VAL HG2 H 1.12 . 2 403 . 51 VAL CA C 62.6 . 1 404 . 51 VAL CB C 29.6 . 1 405 . 51 VAL N N 121.18 . 1 406 . 52 TRP H H 8.24 . 1 407 . 52 TRP HA H 4.03 . 1 408 . 52 TRP HB2 H 3.22 . 2 409 . 52 TRP HB3 H 3.50 . 2 410 . 52 TRP HD1 H 7.17 . 1 411 . 52 TRP HE1 H 9.81 . 1 412 . 52 TRP HE3 H 6.94 . 1 413 . 52 TRP HZ2 H 7.22 . 1 414 . 52 TRP HZ3 H 5.87 . 1 415 . 52 TRP HH2 H 6.39 . 1 416 . 52 TRP CA C 59.6 . 1 417 . 52 TRP CB C 29.4 . 1 418 . 52 TRP N N 124.23 . 1 419 . 53 PHE H H 8.76 . 1 420 . 53 PHE HA H 3.60 . 1 421 . 53 PHE HB2 H 3.24 . 2 422 . 53 PHE HD1 H 7.30 . 3 423 . 53 PHE HE1 H 7.86 . 3 424 . 53 PHE HZ H 6.83 . 1 425 . 53 PHE CA C 59.6 . 1 426 . 53 PHE CB C 36.8 . 1 427 . 53 PHE N N 121.18 . 1 428 . 54 ILE H H 8.22 . 1 429 . 54 ILE HA H 3.64 . 1 430 . 54 ILE HB H 1.88 . 1 431 . 54 ILE HG12 H 0.88 . 2 432 . 54 ILE HG13 H 1.10 . 2 433 . 54 ILE CA C 62.4 . 1 434 . 54 ILE CB C 35.8 . 1 435 . 54 ILE N N 122.53 . 1 436 . 55 ASN H H 7.98 . 1 437 . 55 ASN HA H 4.27 . 1 438 . 55 ASN HB2 H 2.42 . 2 439 . 55 ASN HB3 H 2.60 . 2 440 . 55 ASN HD21 H 6.85 . 2 441 . 55 ASN HD22 H 7.49 . 2 442 . 55 ASN CA C 52.3 . 1 443 . 55 ASN CB C 34.7 . 1 444 . 55 ASN N N 120.50 . 1 445 . 56 LYS H H 7.87 . 1 446 . 56 LYS HA H 3.38 . 1 447 . 56 LYS HB2 H 0.71 . 4 448 . 56 LYS HG2 H -0.06 . 4 449 . 56 LYS HE2 H 2.20 . 4 450 . 56 LYS CA C 53.4 . 1 451 . 56 LYS CB C 28.1 . 1 452 . 56 LYS N N 124.22 . 1 453 . 57 ARG H H 7.94 . 1 454 . 57 ARG HA H 4.12 . 1 455 . 57 ARG HB2 H 1.99 . 2 456 . 57 ARG HG2 H 1.61 . 4 457 . 57 ARG HG3 H 1.74 . 4 458 . 57 ARG CA C 55.3 . 1 459 . 57 ARG CB C 28.4 . 1 460 . 57 ARG N N 120.50 . 1 461 . 58 MET H H 7.65 . 1 462 . 58 MET HA H 4.27 . 1 463 . 58 MET HB2 H 2.07 . 2 464 . 58 MET HG2 H 2.56 . 1 465 . 58 MET HG3 H 2.65 . 1 466 . 58 MET CA C 53.4 . 1 467 . 58 MET CB C 29.6 . 1 468 . 58 MET N N 120.16 . 1 469 . 59 ARG H H 7.67 . 1 470 . 59 ARG HA H 4.28 . 1 471 . 59 ARG HB2 H 1.70 . 1 472 . 59 ARG HB3 H 1.84 . 1 473 . 59 ARG HG2 H 1.59 . 4 474 . 59 ARG HD2 H 3.06 . 2 475 . 59 ARG CA C 53.4 . 1 476 . 59 ARG CB C 27.6 . 1 477 . 59 ARG N N 121.18 . 1 478 . 60 SER H H 7.86 . 1 479 . 60 SER HA H 4.40 . 1 480 . 60 SER HB2 H 3.87 . 2 481 . 60 SER CA C 55.4 . 1 482 . 60 SER CB C 60.6 . 1 483 . 60 SER N N 119.14 . 1 484 . 61 LYS H H 7.78 . 1 485 . 61 LYS HA H 4.11 . 1 486 . 61 LYS CA C 54.3 . 1 487 . 61 LYS CB C 30.5 . 1 488 . 61 LYS N N 130.00 . 1 stop_ save_