data_5911 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of a Peptide from the mdm-2 Binding Domain of the p53 Protein that is Selectively Cytotoxic to Cancer Cells ; _BMRB_accession_number 5911 _BMRB_flat_file_name bmr5911.str _Entry_type original _Submission_date 2003-08-20 _Accession_date 2003-08-20 _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 Rosal R. . . 2 Pincus M. R. . 3 Brandt-Rauf P. W. . 4 Fine R. . . 5 Wang H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 202 "13C chemical shifts" 112 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-07 original author . stop_ _Original_release_date 2004-03-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Solution Structure of a Peptide from the mdm-2 Binding Domain of the p53 Protein that is Selectively Cytotoxic to Cancer Cells ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14967026 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rosal R. . . 2 Pincus M. R. . 3 Brandt-Rauf P. W. . 4 Fine R. L. . 5 Michl J. . . 6 Wang H. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1854 _Page_last 1861 _Year 2004 _Details . loop_ _Keyword Antitumor 'mdm-2 Binding Domain' NMR 'p53 Protein' Penetratin stop_ save_ ################################## # Molecular system description # ################################## save_system_PNC27 _Saveframe_category molecular_system _Mol_system_name PNC27 _Abbreviation_common PNC27 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PNC27 $PNC27 stop_ _System_molecular_weight . _System_physical_state 'not naturally occurring' _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PNC27 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PNC27 _Abbreviation_common PNC27 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; PPLSQETFSDLWKLLKKWKM RRNQFWVKVQRG ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 PRO 3 LEU 4 SER 5 GLN 6 GLU 7 THR 8 PHE 9 SER 10 ASP 11 LEU 12 TRP 13 LYS 14 LEU 15 LEU 16 LYS 17 LYS 18 TRP 19 LYS 20 MET 21 ARG 22 ARG 23 ASN 24 GLN 25 PHE 26 TRP 27 VAL 28 LYS 29 VAL 30 GLN 31 ARG 32 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1Q2F "Nmr Solution Structure Of A Peptide From The Mdm-2 Binding Domain Of The P53 Protein That Is Selectively Cytotoxic To Cancer Ce" 100.00 32 100.00 100.00 3.39e-13 PDB 1Q2I "Nmr Solution Structure Of A Peptide From The Mdm-2 Binding Domain Of The P53 Protein That Is Selectively Cytotoxic To Cancer Ce" 100.00 32 100.00 100.00 3.39e-13 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $PNC27 . . . . . . ; This is not a naturally occurring peptide. It is a chimeric peptide made of two segments from two proteins. The first segment (residues 1-15) is from residues 12-26 of P53_human (P04637). The second segment (residues 16-31) is from the sequence reversal of the residues 239-254 of Human Homeobox Proteien Hox-D8 (P13378) with the I243V substitution. ; 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 $PNC27 'chemical synthesis' . . . . . 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 $PNC27 4 mM . DMSO-d6 5 % . 'sodium phosphate' 10 mM . H2O 95 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2001 loop_ _Task processing stop_ _Details Delaglio save_ save_NMRVIEW _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'data analysis' stop_ _Details Johnson save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure refinement' 'structure solution' stop_ _Details Guentert save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_13C-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _Sample_label . save_ save_13C-HSQCTOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQCTOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQCTOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 10 . mM pH 5.7 . n/a pressure 1 . atm temperature 310 . 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 DSS C 13 'methyl carbons' ppm 0.0 . . . . . DSS H 1 'methyl protons' ppm 0.0 . . . . . 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_reference _Mol_system_component_name PNC27 _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 PRO CB C 31.971 0.2 1 2 . 1 PRO HB3 H 2.535 0.02 2 3 . 1 PRO HB2 H 2.009 0.02 2 4 . 1 PRO CG C 27.475 0.2 1 5 . 1 PRO HG3 H 2.063 0.02 2 6 . 1 PRO HG2 H 2.018 0.02 2 7 . 1 PRO CD C 50.444 0.2 1 8 . 1 PRO HD3 H 3.397 0.02 2 9 . 1 PRO HD2 H 3.399 0.02 2 10 . 2 PRO CA C 63.950 0.2 1 11 . 2 PRO HA H 4.490 0.02 1 12 . 2 PRO CB C 32.968 0.2 1 13 . 2 PRO HB3 H 2.321 0.02 2 14 . 2 PRO HB2 H 1.913 0.02 2 15 . 2 PRO CG C 28.252 0.2 1 16 . 2 PRO HG2 H 2.009 0.02 2 17 . 2 PRO CD C 51.256 0.2 1 18 . 2 PRO HD3 H 3.678 0.02 2 19 . 2 PRO HD2 H 3.539 0.02 2 20 . 3 LEU H H 8.364 0.02 1 21 . 3 LEU CA C 56.539 0.2 1 22 . 3 LEU HA H 4.296 0.02 1 23 . 3 LEU CB C 43.303 0.2 1 24 . 3 LEU HB3 H 1.627 0.02 2 25 . 3 LEU HB2 H 1.577 0.02 2 26 . 3 LEU CG C 27.912 0.2 1 27 . 3 LEU HG H 1.662 0.02 1 28 . 3 LEU CD1 C 24.688 0.2 2 29 . 3 LEU HD1 H 0.865 0.02 4 30 . 3 LEU CD2 C 25.800 0.2 2 31 . 3 LEU HD2 H 0.904 0.02 4 32 . 4 SER H H 8.238 0.02 1 33 . 4 SER CA C 59.355 0.2 1 34 . 4 SER HA H 4.394 0.02 1 35 . 4 SER CB C 64.729 0.2 1 36 . 4 SER HB3 H 3.933 0.02 2 37 . 4 SER HB2 H 3.855 0.02 2 38 . 5 GLN H H 8.342 0.02 1 39 . 5 GLN CA C 57.414 0.2 1 40 . 5 GLN HA H 4.298 0.02 1 41 . 5 GLN CB C 30.174 0.2 1 42 . 5 GLN HB3 H 2.133 0.02 2 43 . 5 GLN HB2 H 1.965 0.02 2 44 . 5 GLN CG C 34.764 0.2 1 45 . 5 GLN HG3 H 2.341 0.02 2 46 . 5 GLN HG2 H 2.343 0.02 2 47 . 6 GLU H H 8.213 0.02 1 48 . 6 GLU CA C 57.414 0.2 1 49 . 6 GLU HA H 4.330 0.02 1 50 . 6 GLU CB C 29.630 0.2 1 51 . 6 GLU HB3 H 2.009 0.02 2 52 . 6 GLU HB2 H 1.995 0.02 2 53 . 6 GLU CG C 33.849 0.2 1 54 . 6 GLU HG3 H 2.390 0.02 2 55 . 6 GLU HG2 H 2.395 0.02 2 56 . 7 THR H H 7.911 0.02 1 57 . 7 THR CA C 63.509 0.2 1 58 . 7 THR HA H 4.208 0.02 1 59 . 7 THR CB C 70.661 0.2 1 60 . 7 THR HB H 4.183 0.02 1 61 . 7 THR CG2 C 22.657 0.2 1 62 . 7 THR HG2 H 1.113 0.02 1 63 . 8 PHE H H 8.224 0.02 1 64 . 8 PHE CA C 60.297 0.2 1 65 . 8 PHE CB C 39.936 0.2 1 66 . 8 PHE HB3 H 3.056 0.02 2 67 . 8 PHE HB2 H 2.981 0.02 2 68 . 8 PHE CD1 C 132.611 0.2 2 69 . 8 PHE HD1 H 7.135 0.02 2 70 . 8 PHE CE1 C 132.283 0.2 2 71 . 8 PHE HE1 H 7.216 0.02 2 72 . 8 PHE CZ C 130.683 0.2 1 73 . 8 PHE HZ H 7.150 0.02 1 74 . 9 SER H H 8.146 0.02 1 75 . 9 SER CA C 60.952 0.2 1 76 . 9 SER HA H 4.260 0.02 1 77 . 9 SER CB C 64.275 0.2 1 78 . 9 SER HB3 H 3.929 0.02 2 79 . 9 SER HB2 H 3.851 0.02 2 80 . 10 ASP H H 8.188 0.02 1 81 . 10 ASP HA H 4.545 0.02 1 82 . 10 ASP CB C 38.950 0.2 1 83 . 10 ASP HB3 H 2.900 0.02 2 84 . 10 ASP HB2 H 2.828 0.02 2 85 . 11 LEU H H 7.957 0.02 1 86 . 11 LEU CA C 58.289 0.2 1 87 . 11 LEU HA H 4.016 0.02 1 88 . 11 LEU CB C 42.624 0.2 1 89 . 11 LEU HB3 H 1.577 0.02 2 90 . 11 LEU HB2 H 1.486 0.02 2 91 . 11 LEU CG C 27.795 0.2 1 92 . 11 LEU HG H 1.526 0.02 1 93 . 11 LEU CD1 C 24.935 0.2 2 94 . 11 LEU HD1 H 0.734 0.02 4 95 . 11 LEU CD2 C 25.438 0.2 2 96 . 11 LEU HD2 H 0.786 0.02 4 97 . 12 TRP H H 7.987 0.02 1 98 . 12 TRP CA C 60.228 0.2 1 99 . 12 TRP HA H 4.337 0.02 1 100 . 12 TRP CB C 29.799 0.2 1 101 . 12 TRP HB3 H 3.283 0.02 2 102 . 12 TRP HB2 H 3.188 0.02 2 103 . 12 TRP CD1 C 128.011 0.2 2 104 . 12 TRP HD1 H 7.199 0.02 1 105 . 12 TRP HE1 H 10.069 0.02 2 106 . 12 TRP CZ2 C 115.554 0.2 2 107 . 12 TRP HZ2 H 7.440 0.02 2 108 . 12 TRP CH2 C 125.442 0.2 1 109 . 12 TRP HH2 H 7.137 0.02 1 110 . 12 TRP CZ3 C 122.725 0.2 2 111 . 12 TRP HZ3 H 7.003 0.02 2 112 . 12 TRP CE3 C 121.701 0.2 2 113 . 12 TRP HE3 H 7.446 0.02 2 114 . 13 LYS H H 7.581 0.02 1 115 . 13 LYS CA C 59.764 0.2 1 116 . 13 LYS HA H 3.877 0.02 1 117 . 13 LYS CB C 33.411 0.2 1 118 . 13 LYS HB3 H 1.745 0.02 2 119 . 13 LYS HB2 H 1.630 0.02 2 120 . 13 LYS CG C 26.128 0.2 1 121 . 13 LYS HG3 H 1.326 0.02 2 122 . 13 LYS HG2 H 1.211 0.02 2 123 . 13 LYS CE C 43.057 0.2 1 124 . 13 LYS HE2 H 2.927 0.02 2 125 . 14 LEU H H 7.613 0.02 1 126 . 14 LEU CA C 57.681 0.2 1 127 . 14 LEU HA H 4.078 0.02 1 128 . 14 LEU CB C 42.812 0.2 1 129 . 14 LEU HB3 H 1.681 0.02 2 130 . 14 LEU HB2 H 1.483 0.02 2 131 . 14 LEU CG C 27.792 0.2 1 132 . 14 LEU HG H 1.548 0.02 1 133 . 14 LEU CD1 C 24.522 0.2 2 134 . 14 LEU HD1 H 0.769 0.02 4 135 . 14 LEU CD2 C 25.794 0.2 2 136 . 14 LEU HD2 H 0.834 0.02 4 137 . 15 LEU H H 7.923 0.02 1 138 . 15 LEU CA C 57.678 0.2 1 139 . 15 LEU HA H 4.101 0.02 1 140 . 15 LEU CB C 42.803 0.2 1 141 . 15 LEU HB3 H 1.665 0.02 2 142 . 15 LEU HB2 H 1.523 0.02 2 143 . 15 LEU CG C 27.826 0.2 1 144 . 15 LEU HG H 1.653 0.02 1 145 . 15 LEU CD1 C 24.312 0.2 2 146 . 15 LEU HD1 H 0.752 0.02 4 147 . 15 LEU CD2 C 26.087 0.2 2 148 . 15 LEU HD2 H 0.768 0.02 4 149 . 16 LYS H H 7.839 0.02 1 150 . 16 LYS CA C 58.942 0.2 1 151 . 16 LYS HA H 3.970 0.02 1 152 . 16 LYS CB C 33.112 0.2 1 153 . 16 LYS HB3 H 1.658 0.02 2 154 . 16 LYS HG3 H 1.320 0.02 2 155 . 16 LYS HG2 H 1.271 0.02 2 156 . 16 LYS HD2 H 1.575 0.02 2 157 . 16 LYS HE2 H 2.880 0.02 2 158 . 17 LYS H H 7.734 0.02 1 159 . 17 LYS CA C 58.637 0.2 1 160 . 17 LYS HA H 4.114 0.02 1 161 . 17 LYS HB3 H 1.754 0.02 2 162 . 17 LYS HB2 H 1.586 0.02 2 163 . 17 LYS HG3 H 1.359 0.02 2 164 . 17 LYS HG2 H 1.250 0.02 2 165 . 17 LYS HE2 H 2.878 0.02 2 166 . 18 TRP H H 7.985 0.02 1 167 . 18 TRP CA C 59.005 0.2 1 168 . 18 TRP HA H 4.533 0.02 1 169 . 18 TRP CB C 30.390 0.2 1 170 . 18 TRP HB3 H 3.336 0.02 2 171 . 18 TRP HB2 H 3.229 0.02 2 172 . 18 TRP CD1 C 127.351 0.2 2 173 . 18 TRP HD1 H 7.145 0.02 1 174 . 18 TRP HE1 H 10.062 0.02 2 175 . 18 TRP CZ2 C 115.471 0.2 2 176 . 18 TRP HZ2 H 7.410 0.02 2 177 . 18 TRP CH2 C 125.386 0.2 1 178 . 18 TRP HH2 H 7.124 0.02 1 179 . 18 TRP CZ3 C 122.706 0.2 2 180 . 18 TRP HZ3 H 7.003 0.02 2 181 . 18 TRP CE3 C 121.651 0.2 2 182 . 18 TRP HE3 H 7.505 0.02 2 183 . 19 LYS H H 8.027 0.02 1 184 . 19 LYS CA C 58.224 0.2 1 185 . 19 LYS HA H 4.039 0.02 1 186 . 19 LYS CB C 33.482 0.2 1 187 . 19 LYS HB2 H 1.743 0.02 2 188 . 19 LYS HG2 H 1.317 0.02 2 189 . 20 MET H H 7.914 0.02 1 190 . 20 MET CA C 56.968 0.2 1 191 . 20 MET HA H 4.346 0.02 1 192 . 20 MET CB C 33.871 0.2 1 193 . 20 MET HB3 H 2.077 0.02 2 194 . 20 MET HB2 H 1.986 0.02 2 195 . 20 MET CG C 33.024 0.2 1 196 . 20 MET HG3 H 2.584 0.02 2 197 . 20 MET HG2 H 2.502 0.02 2 198 . 20 MET CE C 17.896 0.2 1 199 . 20 MET HE H 2.037 0.02 1 200 . 21 ARG H H 8.032 0.02 1 201 . 21 ARG CA C 57.335 0.2 1 202 . 21 ARG HA H 4.275 0.02 1 203 . 21 ARG CB C 31.593 0.2 1 204 . 21 ARG HB3 H 1.840 0.02 2 205 . 21 ARG HB2 H 1.755 0.02 2 206 . 21 ARG CG C 28.044 0.2 1 207 . 21 ARG HG3 H 1.618 0.02 2 208 . 21 ARG HG2 H 1.566 0.02 2 209 . 21 ARG CD C 44.236 0.2 1 210 . 21 ARG HD3 H 3.068 0.02 2 211 . 21 ARG HD2 H 3.067 0.02 2 212 . 21 ARG HE H 7.160 0.02 1 213 . 22 ARG H H 8.207 0.02 1 214 . 22 ARG CA C 57.618 0.2 1 215 . 22 ARG HA H 4.172 0.02 1 216 . 22 ARG CB C 31.399 0.2 1 217 . 22 ARG HB3 H 1.775 0.02 2 218 . 22 ARG HB2 H 1.696 0.02 2 219 . 22 ARG CG C 27.912 0.2 1 220 . 22 ARG HG2 H 1.524 0.02 2 221 . 22 ARG CD C 44.209 0.2 1 222 . 22 ARG HD2 H 3.026 0.02 2 223 . 22 ARG HE H 7.127 0.02 1 224 . 23 ASN H H 8.238 0.02 1 225 . 23 ASN HA H 4.573 0.02 1 226 . 23 ASN CB C 39.578 0.2 1 227 . 23 ASN HB3 H 2.742 0.02 2 228 . 23 ASN HB2 H 2.745 0.02 2 229 . 23 ASN HD21 H 6.818 0.02 2 230 . 23 ASN HD22 H 7.477 0.02 2 231 . 24 GLN H H 8.106 0.02 1 232 . 24 GLN CA C 57.204 0.2 1 233 . 24 GLN HA H 4.105 0.02 1 234 . 24 GLN CB C 30.016 0.2 1 235 . 24 GLN HB3 H 1.818 0.02 2 236 . 24 GLN HB2 H 1.814 0.02 2 237 . 24 GLN CG C 34.621 0.2 1 238 . 24 GLN HG3 H 2.119 0.02 2 239 . 24 GLN HG2 H 2.117 0.02 2 240 . 24 GLN HE21 H 6.749 0.02 2 241 . 24 GLN HE22 H 7.313 0.02 2 242 . 25 PHE H H 7.934 0.02 1 243 . 25 PHE CA C 59.105 0.2 1 244 . 25 PHE HA H 4.477 0.02 1 245 . 25 PHE CB C 40.286 0.2 1 246 . 25 PHE HB3 H 2.922 0.02 2 247 . 25 PHE HB2 H 2.996 0.02 2 248 . 25 PHE CD1 C 132.672 0.2 2 249 . 25 PHE HD1 H 7.062 0.02 2 250 . 25 PHE CE1 C 132.255 0.2 2 251 . 25 PHE HE1 H 7.212 0.02 2 252 . 25 PHE CZ C 130.739 0.2 1 253 . 25 PHE HZ H 7.203 0.02 1 254 . 26 TRP H H 7.773 0.02 1 255 . 26 TRP CB C 30.546 0.2 1 256 . 26 TRP HB3 H 3.168 0.02 2 257 . 26 TRP HB2 H 3.235 0.02 2 258 . 26 TRP CD1 C 128.002 0.2 2 259 . 26 TRP HD1 H 7.172 0.02 1 260 . 26 TRP HE1 H 10.055 0.02 2 261 . 26 TRP CZ2 C 115.495 0.2 2 262 . 26 TRP HZ2 H 7.428 0.02 2 263 . 26 TRP CH2 C 125.469 0.2 1 264 . 26 TRP HH2 H 7.166 0.02 1 265 . 26 TRP CZ3 C 122.902 0.2 2 266 . 26 TRP HZ3 H 7.073 0.02 2 267 . 26 TRP CE3 C 121.770 0.2 2 268 . 26 TRP HE3 H 7.457 0.02 2 269 . 27 VAL H H 7.665 0.02 1 270 . 27 VAL CA C 63.379 0.2 1 271 . 27 VAL HA H 3.964 0.02 1 272 . 27 VAL CB C 33.789 0.2 1 273 . 27 VAL HB H 1.953 0.02 1 274 . 27 VAL HG2 H 0.835 0.02 4 275 . 27 VAL CG1 C 21.680 0.2 2 276 . 27 VAL HG1 H 0.820 0.02 4 277 . 28 LYS H H 8.033 0.02 1 278 . 28 LYS CA C 57.411 0.2 1 279 . 28 LYS HA H 4.211 0.02 1 280 . 28 LYS CB C 33.869 0.2 1 281 . 28 LYS HB3 H 1.754 0.02 2 282 . 28 LYS HB2 H 1.676 0.02 2 283 . 28 LYS HG3 H 1.386 0.02 2 284 . 28 LYS HE2 H 2.932 0.02 2 285 . 29 VAL H H 7.948 0.02 1 286 . 29 VAL CA C 63.269 0.2 1 287 . 29 VAL HA H 4.039 0.02 1 288 . 29 VAL CB C 33.669 0.2 1 289 . 29 VAL HB H 2.000 0.02 1 290 . 29 VAL CG1 C 21.595 0.2 2 291 . 29 VAL HG1 H 0.865 0.02 4 292 . 30 GLN H H 8.280 0.02 1 293 . 30 GLN CA C 56.706 0.2 1 294 . 30 GLN HA H 4.317 0.02 1 295 . 30 GLN CB C 30.474 0.2 1 296 . 30 GLN HB3 H 2.052 0.02 2 297 . 30 GLN HB2 H 1.941 0.02 2 298 . 30 GLN CG C 34.627 0.2 1 299 . 30 GLN HG2 H 2.296 0.02 2 300 . 31 ARG H H 8.289 0.02 1 301 . 31 ARG CA C 56.941 0.2 1 302 . 31 ARG HA H 4.352 0.02 1 303 . 31 ARG CB C 31.910 0.2 1 304 . 31 ARG HB3 H 1.859 0.02 2 305 . 31 ARG HB2 H 1.756 0.02 2 306 . 31 ARG CG C 27.983 0.2 1 307 . 31 ARG HG2 H 1.627 0.02 2 308 . 31 ARG CD C 44.262 0.2 1 309 . 31 ARG HD2 H 3.170 0.02 2 310 . 31 ARG HE H 7.160 0.02 1 311 . 32 GLY H H 8.248 0.02 1 312 . 32 GLY CA C 45.172 0.2 1 313 . 32 GLY HA3 H 3.945 0.02 2 314 . 32 GLY HA2 H 3.948 0.02 2 stop_ save_