data_4639 #Corrected using PDB structure: 1FEXA # #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 # 3 I HA 4.14 2.80 # 47 Q HA 3.24 2.52 # 56 H HA 3.24 4.66 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.16 N/A N/A N/A N/A -0.15 # #bmr4639.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4639.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 N/A N/A N/A N/A +/-0.09 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.704 N/A N/A N/A N/A 0.351 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.161 N/A N/A N/A N/A 0.340 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hanaoka S . . 2 Nagadoi A . . 3 Yoshimura S . . 4 Aimoto S . . 5 Li B . . 6 'de Lange' T . . 7 Nishimura Y . . stop_ _BMRB_accession_number 4639 _BMRB_flat_file_name bmr4639.str _Entry_type new _Submission_date 2000-07-24 _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' 325 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hanaoka S . . 2 Nagadoi A . . 3 Yoshimura S . . 4 Aimoto S . . 5 Li B . . 6 'de Lange' T . . 7 Nishimura Y . . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 312 _Journal_issue ? _Page_first 167 _Page_last 175 _Year 2001 loop_ _Keyword "NMR" "telomere" "Myb motif" stop_ save_ ################################## # Molecular system description # ################################## save_system_RAP1 _Saveframe_category molecular_system _Mol_system_name "human Rap1" _Abbreviation_common hRap1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "hRap1 Myb domain" $RAP1 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1FEX ? "SOLUTION STRUCTURE OF MYB-DOMAIN OF HUMAN RAP1" stop_ save_ ######################## # Monomeric polymers # ######################## save_RAP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "TRF2-INTERACTING TELOMERIC RAP1 PROTEIN" _Name_variant . _Abbreviation_common RAP1 _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; GRIAFTDADDVAILTYVKEN ARSPSSVTGNALWKAMEKSS LTQHSWQSLKDRYLKHLRG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ARG 3 ILE 4 ALA 5 PHE 6 THR 7 ASP 8 ALA 9 ASP 10 ASP 11 VAL 12 ALA 13 ILE 14 LEU 15 THR 16 TYR 17 VAL 18 LYS 19 GLU 20 ASN 21 ALA 22 ARG 23 SER 24 PRO 25 SER 26 SER 27 VAL 28 THR 29 GLY 30 ASN 31 ALA 32 LEU 33 TRP 34 LYS 35 ALA 36 MET 37 GLU 38 LYS 39 SER 40 SER 41 LEU 42 THR 43 GLN 44 HIS 45 SER 46 TRP 47 GLN 48 SER 49 LEU 50 LYS 51 ASP 52 ARG 53 TYR 54 LEU 55 LYS 56 HIS 57 LEU 58 ARG 59 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-04-29 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 1FEX "A Chain A, Solution Structure Of Myb-DomainOf Human Rap1" 100.00 59 100 100 2e-27 DBJ BAA91317.1 "unnamed protein product [Homo sapiens]" 19.80 298 100 100 2e-27 GenBank AAF72711.1 "TRF2-interacting telomeric RAP1 protein[Homo sapiens]" 14.79 399 100 100 2e-27 GenBank AAH04465.1 "TERF2IP protein [Homo sapiens]" 14.79 399 100 100 2e-27 GenBank AAH05841.1 "TERF2IP protein [Homo sapiens]" 14.79 399 100 100 2e-27 GenBank AAH22428.1 "TERF2IP protein [Homo sapiens]" 14.79 399 100 100 2e-27 REF NP_061848.1 "TRF2-interacting telomeric RAP1 protein[Homo sapiens]" 19.80 298 100 100 2e-27 SWISS-PROT Q9NYB0 "TE2I_HUMAN Telomeric repeat binding factor 2interacting protein 1 (TRF2-interacting telomericprotein Rap1) (hRap1)" 14.79 399 100 100 2e-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 $RAP1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $RAP1 'chemical synthesis' . . . . . 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 $RAP1 1.0 mM . "potassium phosphate" 100 mM . NaN3 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 4.2.5 loop_ _Task processing stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu,G., Pfeifer, J. and Bax,A. ; save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task "structure solution" stop_ _Details "Brunger,A.T." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D 1H-1H DQF-COSY 2D 1H-1H NOESY 2D 1H-1H TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . n/a temperature 300 . K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_reference _Mol_system_component_name "hRap1 Myb domain" 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 2 ARG H H 8.22 . 1 2 2 ARG HA H 4.19 . 1 3 2 ARG HB2 H 1.54 . 2 4 2 ARG HB3 H 1.69 . 2 5 2 ARG HG2 H 1.43 . 1 6 2 ARG HG3 H 1.43 . 1 7 2 ARG HD2 H 3.02 . 1 8 2 ARG HD3 H 3.02 . 1 9 3 ILE H H 8.10 . 1 10 3 ILE HA H 3.98 . 1 11 3 ILE HB H 1.57 . 1 12 3 ILE HG12 H 1.22 . 1 13 3 ILE HG13 H 1.22 . 1 14 3 ILE HG2 H 0.94 . 1 15 3 ILE HD1 H 0.57 . 1 16 4 ALA H H 8.27 . 1 17 4 ALA HA H 4.19 . 1 18 4 ALA HB H 1.20 . 1 19 5 PHE H H 8.52 . 1 20 5 PHE HB2 H 2.76 . 1 21 5 PHE HB3 H 2.59 . 1 22 5 PHE HD1 H 6.93 . 1 23 5 PHE HD2 H 6.93 . 1 24 5 PHE HE1 H 6.69 . 1 25 5 PHE HE2 H 6.69 . 1 26 5 PHE HZ H 6.47 . 1 27 6 THR H H 8.84 . 1 28 6 THR HA H 4.53 . 1 29 6 THR HG2 H 1.12 . 1 30 7 ASP H H 8.71 . 1 31 7 ASP HA H 4.28 . 1 32 7 ASP HB2 H 2.63 . 1 33 7 ASP HB3 H 2.54 . 1 34 8 ALA H H 8.03 . 1 35 8 ALA HA H 4.00 . 1 36 8 ALA HB H 1.29 . 1 37 9 ASP H H 7.96 . 1 38 9 ASP HA H 4.17 . 1 39 9 ASP HB2 H 2.50 . 1 40 9 ASP HB3 H 3.34 . 1 41 10 ASP H H 7.76 . 1 42 10 ASP HA H 4.39 . 1 43 10 ASP HB2 H 2.78 . 1 44 10 ASP HB3 H 2.44 . 1 45 11 VAL H H 8.15 . 1 46 11 VAL HA H 3.60 . 1 47 11 VAL HB H 1.99 . 1 48 11 VAL HG1 H 0.84 . 1 49 11 VAL HG2 H 0.98 . 1 50 12 ALA H H 8.15 . 1 51 12 ALA HA H 4.09 . 1 52 12 ALA HB H 1.48 . 1 53 13 ILE H H 8.52 . 1 54 13 ILE HA H 3.65 . 1 55 13 ILE HB H 2.10 . 1 56 13 ILE HG12 H 1.07 . 1 57 13 ILE HG13 H 1.07 . 1 58 13 ILE HG2 H 0.84 . 1 59 14 LEU H H 8.41 . 1 60 14 LEU HA H 3.89 . 1 61 14 LEU HB2 H 1.95 . 1 62 14 LEU HB3 H 1.95 . 1 63 14 LEU HG H 1.46 . 1 64 14 LEU HD1 H 0.88 . 1 65 14 LEU HD2 H 1.00 . 1 66 15 THR H H 8.75 . 1 67 15 THR HA H 3.75 . 1 68 15 THR HB H 4.19 . 1 69 15 THR HG2 H 1.09 . 1 70 16 TYR H H 8.34 . 1 71 16 TYR HA H 3.75 . 1 72 16 TYR HB2 H 3.05 . 1 73 16 TYR HB3 H 3.05 . 1 74 16 TYR HD1 H 6.58 . 1 75 16 TYR HD2 H 6.58 . 1 76 16 TYR HE1 H 6.48 . 1 77 16 TYR HE2 H 6.48 . 1 78 17 VAL H H 8.57 . 1 79 17 VAL HA H 3.02 . 1 80 17 VAL HB H 1.86 . 1 81 17 VAL HG1 H 0.56 . 1 82 17 VAL HG2 H 0.45 . 1 83 18 LYS H H 7.82 . 1 84 18 LYS HA H 3.81 . 1 85 18 LYS HB2 H 1.57 . 1 86 18 LYS HB3 H 1.86 . 1 87 18 LYS HG2 H 1.28 . 2 88 18 LYS HG3 H 1.39 . 2 89 19 GLU H H 7.82 . 1 90 19 GLU HA H 3.91 . 1 91 19 GLU HB2 H 1.63 . 1 92 19 GLU HB3 H 1.63 . 1 93 19 GLU HG2 H 2.23 . 2 94 19 GLU HG3 H 2.00 . 2 95 20 ASN H H 7.63 . 1 96 20 ASN HA H 4.52 . 1 97 20 ASN HB2 H 1.77 . 1 98 20 ASN HB3 H 2.91 . 1 99 20 ASN HD21 H 5.69 . 2 100 20 ASN HD22 H 6.68 . 2 101 21 ALA H H 8.26 . 1 102 21 ALA HA H 4.16 . 1 103 21 ALA HB H 1.17 . 1 104 22 ARG H H 8.14 . 1 105 22 ARG HA H 4.14 . 1 106 22 ARG HB2 H 1.79 . 1 107 22 ARG HB3 H 1.59 . 1 108 22 ARG HG2 H 1.40 . 1 109 22 ARG HG3 H 1.40 . 1 110 22 ARG HD2 H 3.00 . 2 111 22 ARG HD3 H 1.47 . 2 112 22 ARG HE H 7.10 . 1 113 23 SER H H 7.87 . 1 114 23 SER HA H 4.84 . 1 115 23 SER HB2 H 3.95 . 2 116 23 SER HB3 H 3.70 . 2 117 24 PRO HA H 4.33 . 1 118 24 PRO HB2 H 2.33 . 2 119 24 PRO HB3 H 2.04 . 2 120 24 PRO HG2 H 1.89 . 1 121 24 PRO HG3 H 1.89 . 1 122 24 PRO HD2 H 3.78 . 1 123 24 PRO HD3 H 3.78 . 1 124 25 SER H H 7.97 . 1 125 25 SER HA H 4.35 . 1 126 25 SER HB2 H 3.81 . 2 127 25 SER HB3 H 3.77 . 2 128 26 SER H H 8.08 . 1 129 26 SER HA H 4.14 . 1 130 26 SER HB2 H 3.84 . 1 131 26 SER HB3 H 3.84 . 1 132 27 VAL H H 7.59 . 1 133 27 VAL HA H 4.08 . 1 134 27 VAL HB H 2.48 . 1 135 27 VAL HG1 H 0.88 . 1 136 27 VAL HG2 H 1.11 . 1 137 28 THR H H 7.45 . 1 138 28 THR HA H 4.44 . 1 139 28 THR HG2 H 1.20 . 1 140 29 GLY H H 7.54 . 1 141 29 GLY HA2 H 3.81 . 1 142 29 GLY HA3 H 4.36 . 1 143 30 ASN H H 8.45 . 1 144 30 ASN HA H 4.99 . 1 145 30 ASN HB2 H 2.37 . 1 146 30 ASN HB3 H 1.89 . 1 147 30 ASN HD21 H 7.01 . 2 148 30 ASN HD22 H 7.38 . 2 149 31 ALA H H 8.18 . 1 150 31 ALA HA H 3.65 . 1 151 31 ALA HB H 1.26 . 1 152 32 LEU H H 8.82 . 1 153 32 LEU HA H 3.71 . 1 154 32 LEU HB2 H 1.17 . 1 155 32 LEU HB3 H 1.17 . 1 156 32 LEU HG H 0.65 . 1 157 32 LEU HD1 H 0.37 . 1 158 32 LEU HD2 H -0.26 . 1 159 33 TRP H H 6.13 . 1 160 33 TRP HA H 4.16 . 1 161 33 TRP HB2 H 4.03 . 1 162 33 TRP HB3 H 3.15 . 1 163 33 TRP HD1 H 7.93 . 1 164 33 TRP HE1 H 10.53 . 1 165 33 TRP HE3 H 7.06 . 1 166 33 TRP HZ2 H 7.34 . 1 167 33 TRP HZ3 H 6.31 . 1 168 33 TRP HH2 H 6.68 . 1 169 34 LYS H H 8.03 . 1 170 34 LYS HA H 3.72 . 1 171 34 LYS HB2 H 1.46 . 1 172 34 LYS HB3 H 1.30 . 1 173 34 LYS HG2 H 0.30 . 2 174 34 LYS HG3 H 0.04 . 2 175 34 LYS HD2 H 0.87 . 2 176 34 LYS HD3 H 1.00 . 2 177 34 LYS HE2 H 1.75 . 2 178 34 LYS HE3 H 1.98 . 2 179 35 ALA H H 7.81 . 1 180 35 ALA HA H 3.98 . 1 181 35 ALA HB H 1.35 . 1 182 36 MET H H 8.11 . 1 183 36 MET HA H 3.00 . 1 184 36 MET HB2 H 1.65 . 1 185 36 MET HB3 H 1.55 . 1 186 36 MET HG2 H 1.45 . 1 187 36 MET HG3 H 1.41 . 1 188 37 GLU H H 8.42 . 1 189 37 GLU HA H 3.94 . 1 190 37 GLU HB2 H 2.20 . 1 191 37 GLU HB3 H 2.10 . 1 192 37 GLU HG2 H 2.59 . 1 193 37 GLU HG3 H 2.59 . 1 194 38 LYS H H 7.59 . 1 195 38 LYS HA H 4.07 . 1 196 38 LYS HB2 H 1.80 . 1 197 38 LYS HB3 H 1.80 . 1 198 38 LYS HG2 H 1.55 . 2 199 38 LYS HG3 H 1.43 . 2 200 39 SER H H 7.77 . 1 201 39 SER HA H 4.29 . 1 202 39 SER HB2 H 3.88 . 1 203 39 SER HB3 H 3.88 . 1 204 40 SER H H 7.88 . 1 205 40 SER HA H 4.27 . 1 206 40 SER HB2 H 3.83 . 2 207 40 SER HB3 H 3.80 . 2 208 41 LEU H H 7.96 . 1 209 41 LEU HA H 4.17 . 1 210 41 LEU HB2 H 1.45 . 1 211 41 LEU HB3 H 1.45 . 1 212 41 LEU HD1 H 0.81 . 1 213 41 LEU HD2 H 0.90 . 1 214 42 THR H H 7.84 . 1 215 42 THR HA H 4.47 . 1 216 42 THR HG2 H 1.08 . 1 217 43 GLN H H 8.67 . 1 218 43 GLN HA H 4.25 . 1 219 43 GLN HB2 H 1.44 . 1 220 43 GLN HB3 H 1.44 . 1 221 43 GLN HG2 H 2.01 . 1 222 43 GLN HG3 H 1.91 . 1 223 43 GLN HE21 H 6.58 . 2 224 43 GLN HE22 H 7.30 . 2 225 44 HIS H H 7.67 . 1 226 44 HIS HA H 4.50 . 1 227 44 HIS HB2 H 2.99 . 1 228 44 HIS HB3 H 2.68 . 1 229 44 HIS HD1 H 7.12 . 1 230 44 HIS HD2 H 6.43 . 1 231 45 SER H H 8.49 . 1 232 45 SER HA H 4.50 . 1 233 45 SER HB2 H 4.12 . 2 234 45 SER HB3 H 3.89 . 2 235 46 TRP H H 9.26 . 1 236 46 TRP HA H 4.26 . 1 237 46 TRP HB2 H 3.17 . 1 238 46 TRP HB3 H 3.11 . 1 239 46 TRP HD1 H 7.65 . 1 240 46 TRP HE1 H 10.09 . 1 241 46 TRP HE3 H 7.35 . 1 242 46 TRP HZ2 H 7.16 . 1 243 46 TRP HZ3 H 7.03 . 1 244 46 TRP HH2 H 6.90 . 1 245 47 GLN H H 7.72 . 1 246 47 GLN HA H 3.08 . 1 247 47 GLN HB2 H 1.21 . 1 248 47 GLN HB3 H 0.99 . 1 249 47 GLN HG2 H 0.25 . 1 250 47 GLN HG3 H 1.50 . 1 251 47 GLN HE21 H 6.24 . 2 252 47 GLN HE22 H 6.95 . 2 253 48 SER H H 7.61 . 1 254 48 SER HA H 3.97 . 1 255 48 SER HB2 H 3.87 . 2 256 48 SER HB3 H 3.97 . 2 257 49 LEU H H 8.12 . 1 258 49 LEU HA H 3.75 . 1 259 49 LEU HB2 H 2.24 . 1 260 49 LEU HB3 H 1.79 . 1 261 49 LEU HG H 1.62 . 1 262 50 LYS H H 7.64 . 1 263 50 LYS HB2 H 1.55 . 1 264 50 LYS HB3 H 1.55 . 1 265 50 LYS HG2 H 1.36 . 1 266 50 LYS HG3 H 0.93 . 1 267 50 LYS HD2 H 0.39 . 1 268 50 LYS HD3 H 0.39 . 1 269 51 ASP H H 7.49 . 1 270 51 ASP HA H 4.01 . 1 271 51 ASP HB2 H 2.40 . 1 272 51 ASP HB3 H 2.27 . 1 273 52 ARG H H 7.82 . 1 274 52 ARG HA H 3.51 . 1 275 52 ARG HB2 H 0.88 . 1 276 52 ARG HB3 H 0.88 . 1 277 52 ARG HG2 H 0.78 . 1 278 52 ARG HG3 H 0.78 . 1 279 52 ARG HD2 H 2.24 . 1 280 52 ARG HD3 H 2.24 . 1 281 52 ARG HE H 9.45 . 1 282 53 TYR H H 8.01 . 1 283 53 TYR HA H 3.94 . 1 284 53 TYR HB2 H 2.73 . 1 285 53 TYR HB3 H 2.91 . 1 286 53 TYR HD1 H 6.95 . 1 287 53 TYR HD2 H 6.95 . 1 288 53 TYR HE1 H 6.72 . 1 289 53 TYR HE2 H 6.72 . 1 290 54 LEU H H 8.66 . 1 291 54 LEU HA H 3.54 . 1 292 54 LEU HB2 H 1.66 . 1 293 54 LEU HB3 H 1.66 . 1 294 54 LEU HG H 1.91 . 1 295 55 LYS H H 8.38 . 1 296 55 LYS HA H 4.09 . 1 297 55 LYS HB2 H 1.62 . 1 298 55 LYS HB3 H 1.38 . 1 299 55 LYS HG2 H 1.24 . 1 300 55 LYS HG3 H 1.24 . 1 301 55 LYS HD2 H 1.06 . 1 302 55 LYS HD3 H 1.06 . 1 303 56 HIS H H 7.30 . 1 304 56 HIS HA H 3.08 . 1 305 56 HIS HB2 H 2.97 . 1 306 56 HIS HB3 H 2.97 . 1 307 57 LEU H H 7.82 . 1 308 57 LEU HA H 4.21 . 1 309 57 LEU HB2 H 1.79 . 1 310 57 LEU HB3 H 1.79 . 1 311 57 LEU HG H 1.46 . 1 312 57 LEU HD1 H 0.69 . 1 313 57 LEU HD2 H 0.94 . 1 314 58 ARG H H 7.87 . 1 315 58 ARG HA H 3.66 . 1 316 58 ARG HB2 H 1.34 . 1 317 58 ARG HB3 H 1.28 . 1 318 58 ARG HG2 H 1.09 . 1 319 58 ARG HG3 H 1.09 . 1 320 58 ARG HD2 H 2.94 . 1 321 58 ARG HD3 H 2.94 . 1 322 58 ARG HE H 7.19 . 1 323 59 GLY H H 7.95 . 1 324 59 GLY HA2 H 3.59 . 1 325 59 GLY HA3 H 3.59 . 1 stop_ save_