data_4637 #Corrected using PDB structure: 1AKHA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 28 Q HA 4.16 3.39 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.04 3.16 2.73 N/A -2.69 0.05 # #bmr4637.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4637.str file): #HA CA CB CO N HN #N/A +2.94 +2.94 N/A -2.69 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 +/-0.34 +/-0.28 N/A +/-0.52 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.708 0.949 0.994 N/A 0.740 0.577 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.169 1.141 0.922 N/A 1.778 0.220 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE MATA1 HOMEODOMAIN ; 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_ _BMRB_accession_number 4637 _BMRB_flat_file_name bmr4637.str _Entry_type new _Submission_date 2000-06-07 _Accession_date 2001-03-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR 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_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain ; _Citation_status published _Citation_type Journal _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_name_full . _Journal_volume 39 _Page_first 10045 _Page_last 10054 _Year 2000 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 loop_ _Mol_system_component_name _Mol_label "MATING-TYPE PROTEIN A-1" $MATa1 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1F43 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_MATa1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "MATING-TYPE PROTEIN A-1" _Name_variant . _Abbreviation_common MATa1 _Mol_thiol_state 'all free' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-28 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 1LE8 "A Chain A, Crystal Structure Of TheMata1MATALPHA2-3a Heterodimer Bound To Dna Complex" 115.09 53 100 100 8e-23 PDB 1F43 "A Chain A, Solution Structure Of The Mata1Homeodomain" 100.00 61 100 100 1e-27 PDB 1YRN "A Chain A, Mat A1ALPHA2DNA TERNARY COMPLEX(HOMEODOMAIN)" 100.00 61 100 100 1e-27 PDB 1AKH "A Chain A, Variant Mata1 Matalpha2 DnaTernary Complex" 100.00 61 98 100 2e-27 EMBL CAA42252.1 "mating type regulatory protein, silencedcopy at HMR locus [Saccharomyces cerevisiae]" 48.41 126 100 100 1e-27 PIR JEBY1 "mating-type regulatory protein a1 - yeast(Saccharomyces cerevisiae)" 48.41 126 100 100 1e-27 REF NP_010021.1 "Silenced copy of A1, encoding ahomeobox-domain containing corepressor that interactswith Alpha2p to repress haploid-specific genetranscription in diploid cells; Hmra1p [Saccharomycescerevisiae]" 48.41 126 100 100 1e-27 SWISS-PROT P01366 "MTA1_YEAST Mating-type protein A-1" 48.41 126 100 100 1e-27 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 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 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 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_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 3D 15N-separated NOESY HNHA HNCA-J 2D NOESY DQF-COSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . n/a 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 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 . H 1 . ppm . . . . . . . . . N 15 . ppm . . . . . . . . . C 13 . ppm . . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts 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" loop_ _Atom_shift_assign_ID _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 56.14 . 1 4 1 LYS CB C 32.64 . 1 5 1 LYS N N 124.61 . 1 6 2 LYS H H 8.50 . 1 7 2 LYS HA H 4.21 . 1 8 2 LYS CA C 56.24 . 1 9 2 LYS CB C 32.94 . 1 10 2 LYS N N 124.25 . 1 11 3 GLU H H 8.50 . 1 12 3 GLU HA H 4.26 . 1 13 3 GLU CA C 56.14 . 1 14 3 GLU CB C 30.44 . 1 15 3 GLU N N 122.91 . 1 16 4 LYS H H 8.50 . 1 17 4 LYS HA H 4.26 . 1 18 4 LYS CA C 56.14 . 1 19 4 LYS CB C 32.94 . 1 20 4 LYS N N 122.90 . 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 56.34 . 1 26 5 SER CB C 62.54 . 1 27 5 SER N N 117.13 . 1 28 6 PRO HA H 4.24 . 1 29 6 PRO CA C 62.54 . 1 30 7 LYS H H 8.37 . 1 31 7 LYS CA C 56.34 . 1 32 7 LYS CB C 32.34 . 1 33 7 LYS N N 121.54 . 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 44.94 . 1 38 8 GLY N N 110.01 . 1 39 9 LYS H H 8.19 . 1 40 9 LYS HA H 4.36 . 1 41 9 LYS CA C 56.34 . 1 42 9 LYS CB C 33.44 . 1 43 9 LYS N N 120.86 . 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 56.34 . 1 49 10 SER CB C 62.54 . 1 50 10 SER N N 118.15 . 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 56.34 . 1 56 11 SER CB C 62.54 . 1 57 11 SER N N 118.83 . 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 60.44 . 1 66 12 ILE CB C 38.74 . 1 67 12 ILE N N 120.86 . 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 56.74 . 1 73 13 SER CB C 62.44 . 1 74 13 SER N N 124.61 . 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 65.44 . 1 83 14 PRO CB C 30.64 . 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 59.44 . 1 93 15 GLN CB C 27.34 . 1 94 15 GLN N N 117.47 . 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 54.64 . 1 99 16 ALA CB C 18.94 . 1 100 16 ALA N N 124.59 . 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 59.44 . 1 110 17 ARG CB C 30.34 . 1 111 17 ARG N N 117.47 . 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 54.14 . 1 116 18 ALA CB C 17.94 . 1 117 18 ALA N N 120.18 . 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 60.44 . 1 127 19 PHE CB C 38.74 . 1 128 19 PHE N N 120.18 . 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 0.55 . 4 134 20 LEU HD1 H -0.65 . 4 135 20 LEU CA C 58.34 . 1 136 20 LEU CB C 37.94 . 1 137 20 LEU N N 120.86 . 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 58.24 . 1 143 21 GLU CB C 28.94 . 1 144 21 GLU N N 116.11 . 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 58.34 . 1 154 22 GLN CB C 28.44 . 1 155 22 GLN N N 118.83 . 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 65.54 . 1 162 23 VAL CB C 31.54 . 1 163 23 VAL N N 120.86 . 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 59.14 . 1 173 24 PHE CB C 38.94 . 1 174 24 PHE N N 120.18 . 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 58.34 . 1 182 25 ARG CB C 30.54 . 1 183 25 ARG N N 114.08 . 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 57.14 . 1 191 26 ARG CB C 31.14 . 1 192 26 ARG N N 116.79 . 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 56.34 . 1 201 27 LYS CB C 34.54 . 1 202 27 LYS N N 121.54 . 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 56.24 . 1 211 28 GLN CB C 34.44 . 1 212 28 GLN N N 117.47 . 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 56.34 . 1 218 29 SER CB C 64.54 . 1 219 29 SER N N 111.07 . 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 53.04 . 1 228 30 LEU CB C 44.84 . 1 229 30 LEU N N 123.24 . 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 51.14 . 1 237 31 ASN CB C 37.64 . 1 238 31 ASN N N 121.88 . 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 62.54 . 1 244 32 SER CB C 64.74 . 1 245 32 SER N N 113.07 . 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 58.34 . 1 255 33 LYS CB C 31.94 . 1 256 33 LYS N N 123.24 . 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 58.34 . 1 264 34 GLU CB C 30.54 . 1 265 34 GLU N N 120.18 . 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 60.44 . 1 275 35 LYS CB C 32.54 . 1 276 35 LYS N N 118.15 . 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 59.44 . 1 283 36 GLU CB C 28.64 . 1 284 36 GLU N N 117.13 . 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 58.74 . 1 292 37 GLU CB C 29.44 . 1 293 37 GLU N N 120.12 . 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 66.64 . 1 300 38 VAL CB C 31.44 . 1 301 38 VAL N N 120.86 . 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 55.34 . 1 306 39 ALA CB C 17.44 . 1 307 39 ALA N N 121.88 . 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 58.34 . 1 315 40 LYS CB C 32.54 . 1 316 40 LYS N N 116.11 . 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 58.24 . 1 323 41 LYS CB C 32.44 . 1 324 41 LYS N N 118.81 . 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 59.44 . 1 330 42 CYS CB C 29.44 . 1 331 42 CYS N N 111.71 . 1 332 43 GLY H H 7.85 . 1 333 43 GLY HA2 H 3.92 . 2 334 43 GLY CA C 47.04 . 1 335 43 GLY N N 110.01 . 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 58.34 . 1 344 44 ILE CB C 39.64 . 1 345 44 ILE N N 112.72 . 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 59.44 . 1 351 45 THR CB C 68.54 . 1 352 45 THR N N 109.33 . 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 65.54 . 1 359 46 PRO CB C 32.34 . 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 58.24 . 1 368 47 LEU CB C 41.84 . 1 369 47 LEU N N 118.15 . 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 58.34 . 1 378 48 GLN CB C 29.44 . 1 379 48 GLN N N 117.47 . 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 66.64 . 1 386 49 VAL CB C 31.44 . 1 387 49 VAL N N 119.51 . 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 59.74 . 1 396 50 ARG CB C 30.54 . 1 397 50 ARG N N 119.84 . 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 65.54 . 1 404 51 VAL CB C 32.54 . 1 405 51 VAL N N 118.49 . 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 62.54 . 1 417 52 TRP CB C 32.34 . 1 418 52 TRP N N 121.54 . 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 62.54 . 1 426 53 PHE CB C 39.74 . 1 427 53 PHE N N 118.49 . 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 65.34 . 1 434 54 ILE CB C 38.74 . 1 435 54 ILE N N 119.84 . 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 55.24 . 1 443 55 ASN CB C 37.64 . 1 444 55 ASN N N 117.81 . 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 56.34 . 1 451 56 LYS CB C 31.04 . 1 452 56 LYS N N 121.53 . 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 58.24 . 1 459 57 ARG CB C 31.34 . 1 460 57 ARG N N 117.81 . 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 56.34 . 1 467 58 MET CB C 32.54 . 1 468 58 MET N N 117.47 . 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 56.34 . 1 476 59 ARG CB C 30.54 . 1 477 59 ARG N N 118.49 . 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 58.34 . 1 482 60 SER CB C 63.54 . 1 483 60 SER N N 116.45 . 1 484 61 LYS H H 7.78 . 1 485 61 LYS HA H 4.11 . 1 486 61 LYS CA C 57.24 . 1 487 61 LYS CB C 33.44 . 1 488 61 LYS N N 127.31 . 1 stop_ save_