data_4572 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Conformational changes in the PBX Homeodomain and C-terminal Extension upon Binding DNA and HOX-derived YPWM Peptides ; _BMRB_accession_number 4572 _BMRB_flat_file_name bmr4572.str _Entry_type original _Submission_date 2000-01-14 _Accession_date 2000-01-14 _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 Sprules Tara . . 2 Green Nancy . . 3 Featherstone Mark . . 4 Gehring Kalle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 400 "13C chemical shifts" 244 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-10-23 original author . stop_ _Original_release_date 2000-10-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformational changes in the PBX Homeodomain and C-terminal Extension upon Binding DNA and HOX-derived YPWM Peptides ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20393887 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sprules Tara . . 2 Green Nancy . . 3 Featherstone Mark . . 4 Gehring Kalle . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full 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 9943 _Page_last 9950 _Year 2000 _Details . loop_ _Keyword homeodomain TALE stop_ save_ ################################## # Molecular system description # ################################## save_PBX_HD _Saveframe_category molecular_system _Mol_system_name 'PBX homeodomain' _Abbreviation_common 'PBX HD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PBX HD' $PBX1_HD 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_PBX1_HD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PBX1 homeodomain' _Abbreviation_common 'PBX1 HD' _Molecular_mass 8874 _Mol_thiol_state 'all free' _Details '21 residue his tag followed by residues 241-294 of murine PBX1' ############################## # Polymer residue sequence # ############################## _Residue_count 75 _Mol_residue_sequence ; GHHHHHHHHHHSSGHIEGRH MNKQATEILNEYFYSHLSNP YPSEEAKEELAKKCGITVSQ VSNWFGNKRIRYKKN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -21 GLY 2 -20 HIS 3 -19 HIS 4 -18 HIS 5 -17 HIS 6 -16 HIS 7 -15 HIS 8 -14 HIS 9 -13 HIS 10 -12 HIS 11 -11 HIS 12 -10 SER 13 -9 SER 14 -8 GLY 15 -7 HIS 16 -6 ILE 17 -5 GLU 18 -4 GLY 19 -3 ARG 20 -2 HIS 21 -1 MET 22 241 ASN 23 242 LYS 24 243 GLN 25 244 ALA 26 245 THR 27 246 GLU 28 247 ILE 29 248 LEU 30 249 ASN 31 250 GLU 32 251 TYR 33 252 PHE 34 253 TYR 35 254 SER 36 255 HIS 37 256 LEU 38 257 SER 39 258 ASN 40 259 PRO 41 260 TYR 42 261 PRO 43 262 SER 44 263 GLU 45 264 GLU 46 265 ALA 47 266 LYS 48 267 GLU 49 268 GLU 50 269 LEU 51 270 ALA 52 271 LYS 53 272 LYS 54 273 CYS 55 274 GLY 56 275 ILE 57 276 THR 58 277 VAL 59 278 SER 60 279 GLN 61 280 VAL 62 281 SER 63 282 ASN 64 283 TRP 65 284 PHE 66 285 GLY 67 286 ASN 68 287 LYS 69 288 ARG 70 289 ILE 71 290 ARG 72 291 TYR 73 292 LYS 74 293 LYS 75 294 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-14 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 1DU6 "Solution Structure Of The Truncated Pbx Homeodomain" 85.33 64 100.00 100.00 5.81e-39 GB AAP95000 "homeobox PBX2 [Macaca fascicularis]" 68.00 59 98.04 100.00 8.07e-29 GB AAP95001 "homeobox PBX2 [Aotus azarai]" 68.00 59 98.04 100.00 8.07e-29 GB AAP95002 "homeobox PBX2 [Tarsius syrichta]" 68.00 59 98.04 100.00 8.07e-29 GB AAP95003 "homeobox PBX2 [Lemur catta]" 68.00 59 98.04 100.00 8.07e-29 GB AAP95004 "homeobox PBX2, partial [Galeopterus variegatus]" 68.00 59 98.04 100.00 8.07e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $PBX1_HD mouse 10090 Eukaryota . Mus musculus PBX1 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 $PBX1_HD 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET16b 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 $PBX1_HD 1.0 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HMQC_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HMQC NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H COSY' _Sample_label . save_ save_13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_TOCSY(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HMQC NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.8 0.05 n/a temperature 303 0.1 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_cs1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PBX HD' _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 . 12 SER H H 8.49 0.01 1 2 . 12 SER CA C 56.5 0.20 1 3 . 12 SER HA H 4.54 0.01 1 4 . 12 SER HB2 H 3.88 0.01 1 5 . 12 SER HB3 H 3.88 0.01 1 6 . 12 SER C C 174.4 0.20 1 7 . 13 SER N N 118.4 0.25 1 8 . 13 SER H H 8.60 0.01 1 9 . 13 SER CA C 56.8 0.20 1 10 . 13 SER HA H 4.50 0.01 1 11 . 13 SER CB C 62.1 0.20 1 12 . 13 SER HB2 H 3.92 0.01 1 13 . 13 SER HB3 H 3.92 0.01 1 14 . 13 SER C C 175.0 0.20 1 15 . 14 GLY N N 110.4 0.25 1 16 . 14 GLY H H 8.45 0.01 1 17 . 14 GLY CA C 43.5 0.20 1 18 . 14 GLY HA2 H 3.97 0.01 1 19 . 14 GLY HA3 H 3.97 0.01 1 20 . 14 GLY C C 173.8 0.20 1 21 . 15 HIS HA H 4.74 0.01 1 22 . 15 HIS HB2 H 3.20 0.01 1 23 . 15 HIS HB3 H 3.20 0.01 1 24 . 15 HIS C C 174.4 0.20 1 25 . 16 ILE N N 123.6 0.25 1 26 . 16 ILE H H 8.33 0.01 1 27 . 16 ILE CA C 59.3 0.20 1 28 . 16 ILE HA H 4.18 0.01 1 29 . 16 ILE CB C 36.9 0.20 1 30 . 16 ILE HB H 1.84 0.01 1 31 . 16 ILE HG2 H 0.93 0.01 1 32 . 16 ILE CG2 C 15.7 0.20 1 33 . 16 ILE CG1 C 25.5 0.20 1 34 . 16 ILE HG12 H 1.46 0.01 2 35 . 16 ILE HG13 H 1.19 0.01 2 36 . 16 ILE HD1 H 0.93 0.01 1 37 . 16 ILE CD1 C 11.4 0.20 1 38 . 16 ILE C C 176.1 0.20 1 39 . 17 GLU N N 126.1 0.25 1 40 . 17 GLU H H 8.64 0.01 1 41 . 17 GLU CA C 54.7 0.20 1 42 . 17 GLU HA H 4.32 0.01 1 43 . 17 GLU CB C 28.3 0.20 1 44 . 17 GLU HB2 H 2.10 0.01 2 45 . 17 GLU HB3 H 2.01 0.01 2 46 . 17 GLU CG C 33.6 0.20 1 47 . 17 GLU HG2 H 2.39 0.01 1 48 . 17 GLU HG3 H 2.39 0.01 1 49 . 17 GLU C C 176.7 0.20 1 50 . 18 GLY N N 110.4 0.25 1 51 . 18 GLY H H 8.48 0.01 1 52 . 18 GLY CA C 43.5 0.20 1 53 . 18 GLY HA2 H 4.02 0.01 2 54 . 18 GLY HA3 H 3.90 0.01 2 55 . 18 GLY C C 174.0 0.20 1 56 . 19 ARG N N 120.3 0.25 1 57 . 19 ARG H H 8.28 0.01 1 58 . 19 ARG CA C 54.3 0.20 1 59 . 19 ARG HA H 4.35 0.01 1 60 . 19 ARG CB C 29.1 0.20 1 61 . 19 ARG HB2 H 1.82 0.01 2 62 . 19 ARG HB3 H 1.77 0.01 2 63 . 19 ARG CG C 25.3 0.20 1 64 . 19 ARG HG2 H 1.62 0.01 1 65 . 19 ARG HG3 H 1.62 0.01 1 66 . 19 ARG CD C 41.6 0.20 1 67 . 19 ARG HD2 H 3.20 0.01 1 68 . 19 ARG HD3 H 3.20 0.01 1 69 . 19 ARG NE N 117.3 0.25 1 70 . 19 ARG HE H 7.23 0.01 1 71 . 19 ARG C C 176.3 0.20 1 72 . 20 HIS N N 120.0 0.25 1 73 . 20 HIS H H 8.61 0.01 1 74 . 20 HIS HB2 H 3.22 0.01 1 75 . 20 HIS HB3 H 3.22 0.01 1 76 . 20 HIS C C 174.2 0.20 1 77 . 21 MET N N 122.5 0.25 1 78 . 21 MET H H 8.55 0.01 1 79 . 21 MET CA C 53.4 0.20 1 80 . 21 MET HA H 4.53 0.01 1 81 . 21 MET CB C 31.9 0.20 1 82 . 21 MET HB2 H 2.03 0.01 1 83 . 21 MET HB3 H 2.03 0.01 1 84 . 21 MET CG C 30.2 0.20 1 85 . 21 MET HG2 H 2.55 0.01 1 86 . 21 MET HG3 H 2.55 0.01 1 87 . 21 MET HE H 1.94 0.01 1 88 . 21 MET CE C 15.5 0.20 1 89 . 21 MET C C 175.5 0.20 1 90 . 22 ASN N N 122.0 0.25 1 91 . 22 ASN H H 8.46 0.01 1 92 . 22 ASN CA C 50.9 0.20 1 93 . 22 ASN HA H 4.75 0.01 1 94 . 22 ASN CB C 37.3 0.20 1 95 . 22 ASN HB2 H 3.13 0.01 2 96 . 22 ASN HB3 H 3.04 0.01 2 97 . 22 ASN ND2 N 112.6 0.25 1 98 . 22 ASN HD21 H 7.65 0.01 2 99 . 22 ASN HD22 H 7.04 0.01 2 100 . 22 ASN C C 175.8 0.20 1 101 . 23 LYS N N 122.0 0.25 1 102 . 23 LYS H H 8.64 0.01 1 103 . 23 LYS CA C 57.7 0.20 1 104 . 23 LYS HA H 4.18 0.01 1 105 . 23 LYS CB C 30.8 0.20 1 106 . 23 LYS HB2 H 1.94 0.01 2 107 . 23 LYS HB3 H 1.88 0.01 2 108 . 23 LYS HG2 H 1.49 0.01 1 109 . 23 LYS HG3 H 1.49 0.01 1 110 . 23 LYS CE C 40.2 0.20 1 111 . 23 LYS HE2 H 3.01 0.01 1 112 . 23 LYS HE3 H 3.01 0.01 1 113 . 23 LYS C C 178.4 0.20 1 114 . 24 GLN N N 119.5 0.25 1 115 . 24 GLN H H 8.52 0.01 1 116 . 24 GLN CA C 57.1 0.20 1 117 . 24 GLN HA H 4.18 0.01 1 118 . 24 GLN CB C 26.4 0.20 1 119 . 24 GLN HB2 H 2.17 0.01 1 120 . 24 GLN HB3 H 2.17 0.01 1 121 . 24 GLN CG C 32.6 0.20 1 122 . 24 GLN HG2 H 2.48 0.01 1 123 . 24 GLN HG3 H 2.48 0.01 1 124 . 24 GLN NE2 N 112.1 0.25 1 125 . 24 GLN HE21 H 7.56 0.01 1 126 . 24 GLN HE22 H 6.92 0.01 1 127 . 24 GLN C C 178.0 0.20 1 128 . 25 ALA N N 122.0 0.25 1 129 . 25 ALA H H 8.20 0.01 1 130 . 25 ALA CA C 53.3 0.20 1 131 . 25 ALA HA H 4.18 0.01 1 132 . 25 ALA HB H 1.51 0.01 1 133 . 25 ALA CB C 16.8 0.20 1 134 . 25 ALA C C 178.7 0.20 1 135 . 26 THR N N 111.2 0.25 1 136 . 26 THR H H 8.00 0.01 1 137 . 26 THR CA C 65.2 0.20 1 138 . 26 THR HA H 3.47 0.01 1 139 . 26 THR CB C 66.8 0.20 1 140 . 26 THR HB H 4.32 0.01 1 141 . 26 THR HG2 H 1.36 0.01 1 142 . 26 THR CG2 C 20.7 0.20 1 143 . 26 THR C C 175.9 0.20 1 144 . 27 GLU N N 120.9 0.25 1 145 . 27 GLU H H 7.86 0.01 1 146 . 27 GLU CA C 57.7 0.20 1 147 . 27 GLU HA H 4.23 0.01 1 148 . 27 GLU CB C 26.8 0.20 1 149 . 27 GLU HB2 H 2.29 0.01 2 150 . 27 GLU HB3 H 2.19 0.01 2 151 . 27 GLU CG C 33.1 0.20 1 152 . 27 GLU HG2 H 2.48 0.01 1 153 . 27 GLU HG3 H 2.48 0.01 1 154 . 27 GLU C C 178.9 0.20 1 155 . 28 ILE N N 121.7 0.25 1 156 . 28 ILE H H 7.79 0.01 1 157 . 28 ILE CA C 63.3 0.20 1 158 . 28 ILE HA H 3.70 0.01 1 159 . 28 ILE CB C 36.1 0.20 1 160 . 28 ILE HB H 2.01 0.01 1 161 . 28 ILE HG2 H 0.78 0.01 1 162 . 28 ILE CG2 C 16.0 0.20 1 163 . 28 ILE CG1 C 27.7 0.20 1 164 . 28 ILE HG12 H 1.84 0.01 2 165 . 28 ILE HG13 H 1.14 0.01 2 166 . 28 ILE HD1 H 0.84 0.01 1 167 . 28 ILE CD1 C 12.0 0.20 1 168 . 28 ILE C C 179.3 0.20 1 169 . 29 LEU N N 121.7 0.25 1 170 . 29 LEU H H 8.03 0.01 1 171 . 29 LEU CA C 56.6 0.20 1 172 . 29 LEU HA H 3.61 0.01 1 173 . 29 LEU CB C 35.6 0.20 1 174 . 29 LEU HB2 H 0.43 0.01 2 175 . 29 LEU HB3 H -0.86 0.01 2 176 . 29 LEU CG C 23.9 0.20 1 177 . 29 LEU HG H 1.45 0.01 1 178 . 29 LEU HD1 H -0.25 0.01 1 179 . 29 LEU HD2 H 0.48 0.01 1 180 . 29 LEU CD1 C 22.4 0.20 2 181 . 29 LEU CD2 C 22.0 0.20 2 182 . 29 LEU C C 178.5 0.20 1 183 . 30 ASN N N 118.1 0.25 1 184 . 30 ASN H H 8.39 0.01 1 185 . 30 ASN CA C 55.1 0.20 1 186 . 30 ASN HA H 4.76 0.01 1 187 . 30 ASN CB C 36.8 0.20 1 188 . 30 ASN HB2 H 2.98 0.01 2 189 . 30 ASN HB3 H 2.89 0.01 2 190 . 30 ASN ND2 N 111.8 0.25 1 191 . 30 ASN HD21 H 7.53 0.01 2 192 . 30 ASN HD22 H 7.17 0.01 2 193 . 30 ASN C C 177.7 0.20 1 194 . 31 GLU N N 119.2 0.25 1 195 . 31 GLU H H 8.39 0.01 1 196 . 31 GLU CA C 57.8 0.20 1 197 . 31 GLU HA H 4.21 0.01 1 198 . 31 GLU CB C 26.5 0.20 1 199 . 31 GLU HB2 H 2.29 0.01 1 200 . 31 GLU HB3 H 2.29 0.01 1 201 . 31 GLU CG C 33.5 0.20 1 202 . 31 GLU HG2 H 2.68 0.01 2 203 . 31 GLU HG3 H 2.49 0.01 2 204 . 31 GLU C C 180.2 0.20 1 205 . 32 TYR N N 120.9 0.25 1 206 . 32 TYR H H 8.18 0.01 1 207 . 32 TYR CA C 60.8 0.20 1 208 . 32 TYR HA H 4.17 0.01 1 209 . 32 TYR CB C 36.4 0.20 1 210 . 32 TYR HB2 H 3.42 0.01 2 211 . 32 TYR HB3 H 3.20 0.01 2 212 . 32 TYR HE1 H 6.43 0.01 1 213 . 32 TYR HE2 H 6.43 0.01 1 214 . 32 TYR HD1 H 7.07 0.01 1 215 . 32 TYR HD2 H 7.07 0.01 1 216 . 32 TYR C C 179.1 0.20 1 217 . 33 PHE N N 123.1 0.25 1 218 . 33 PHE H H 9.45 0.01 1 219 . 33 PHE CA C 61.5 0.20 1 220 . 33 PHE HA H 4.20 0.01 1 221 . 33 PHE CB C 37.9 0.20 1 222 . 33 PHE HB2 H 3.40 0.01 2 223 . 33 PHE HB3 H 3.35 0.01 2 224 . 33 PHE HD1 H 6.58 0.01 1 225 . 33 PHE HD2 H 6.58 0.01 1 226 . 33 PHE HE1 H 6.87 0.01 1 227 . 33 PHE HE2 H 6.87 0.01 1 228 . 33 PHE C C 177.4 0.20 1 229 . 34 TYR N N 113.2 0.25 1 230 . 34 TYR H H 8.85 0.01 1 231 . 34 TYR CA C 60.2 0.20 1 232 . 34 TYR HA H 4.20 0.01 1 233 . 34 TYR CB C 35.5 0.20 1 234 . 34 TYR HB2 H 3.34 0.01 2 235 . 34 TYR HB3 H 3.04 0.01 2 236 . 34 TYR HE1 H 7.05 0.01 1 237 . 34 TYR HE2 H 7.05 0.01 1 238 . 34 TYR HD1 H 7.50 0.01 1 239 . 34 TYR HD2 H 7.50 0.01 1 240 . 34 TYR C C 177.4 0.20 1 241 . 35 SER N N 112.6 0.25 1 242 . 35 SER H H 7.78 0.01 1 243 . 35 SER CA C 57.1 0.20 1 244 . 35 SER HA H 4.59 0.01 1 245 . 35 SER CB C 62.3 0.20 1 246 . 35 SER HB2 H 3.98 0.01 2 247 . 35 SER HB3 H 3.89 0.01 2 248 . 35 SER C C 174.3 0.20 1 249 . 36 HIS N N 121.1 0.25 1 250 . 36 HIS H H 7.57 0.01 1 251 . 36 HIS CA C 53.9 0.20 1 252 . 36 HIS HA H 4.78 0.01 1 253 . 36 HIS CB C 25.5 0.20 1 254 . 36 HIS HB2 H 3.51 0.01 2 255 . 36 HIS HB3 H 2.39 0.01 2 256 . 36 HIS HD2 H 8.07 0.01 1 257 . 36 HIS HE1 H 7.12 0.01 1 258 . 36 HIS C C 175.1 0.20 1 259 . 37 LEU N N 120.3 0.25 1 260 . 37 LEU H H 7.64 0.01 1 261 . 37 LEU CA C 55.9 0.20 1 262 . 37 LEU HA H 3.59 0.01 1 263 . 37 LEU CB C 40.1 0.20 1 264 . 37 LEU HB2 H 1.69 0.01 2 265 . 37 LEU HB3 H 1.46 0.01 2 266 . 37 LEU CG C 24.8 0.20 1 267 . 37 LEU HG H 1.63 0.01 1 268 . 37 LEU HD1 H 0.55 0.01 1 269 . 37 LEU HD2 H 0.91 0.01 1 270 . 37 LEU CD1 C 22.4 0.20 2 271 . 37 LEU CD2 C 23.6 0.20 2 272 . 37 LEU C C 178.4 0.20 1 273 . 38 SER N N 110.4 0.25 1 274 . 38 SER H H 8.17 0.01 1 275 . 38 SER CA C 58.0 0.20 1 276 . 38 SER HA H 4.01 0.01 1 277 . 38 SER CB C 61.0 0.20 1 278 . 38 SER HB2 H 3.99 0.01 2 279 . 38 SER HB3 H 3.87 0.01 2 280 . 38 SER C C 174.8 0.20 1 281 . 39 ASN N N 115.9 0.25 1 282 . 39 ASN H H 7.50 0.01 1 283 . 39 ASN CA C 50.1 0.20 1 284 . 39 ASN HA H 5.12 0.01 1 285 . 39 ASN CB C 37.0 0.20 1 286 . 39 ASN HB2 H 2.94 0.01 2 287 . 39 ASN HB3 H 2.82 0.01 2 288 . 39 ASN ND2 N 110.7 0.25 1 289 . 39 ASN HD21 H 7.55 0.01 2 290 . 39 ASN HD22 H 6.85 0.01 2 291 . 40 PRO CD C 47.7 0.20 1 292 . 40 PRO CA C 61.9 0.20 1 293 . 40 PRO HA H 4.71 0.01 1 294 . 40 PRO CB C 28.3 0.20 1 295 . 40 PRO HB2 H 1.75 0.01 1 296 . 40 PRO HB3 H 1.75 0.01 1 297 . 40 PRO CG C 24.6 0.20 1 298 . 40 PRO HG2 H 1.93 0.01 2 299 . 40 PRO HG3 H 1.50 0.01 2 300 . 40 PRO HD2 H 3.73 0.01 2 301 . 40 PRO HD3 H 3.66 0.01 2 302 . 40 PRO C C 174.1 0.20 1 303 . 41 TYR N N 118.9 0.25 1 304 . 41 TYR H H 7.63 0.01 1 305 . 41 TYR CA C 53.6 0.20 1 306 . 41 TYR HA H 4.76 0.01 1 307 . 41 TYR CB C 36.3 0.20 1 308 . 41 TYR HB2 H 2.92 0.01 2 309 . 41 TYR HB3 H 2.85 0.01 2 310 . 41 TYR HE1 H 6.89 0.01 1 311 . 41 TYR HE2 H 6.89 0.01 1 312 . 41 TYR HD1 H 7.15 0.01 1 313 . 41 TYR HD2 H 7.15 0.01 1 314 . 42 PRO CD C 48.5 0.20 1 315 . 42 PRO CA C 60.4 0.20 1 316 . 42 PRO HA H 4.38 0.01 1 317 . 42 PRO CB C 29.4 0.20 1 318 . 42 PRO HB2 H 1.62 0.01 2 319 . 42 PRO HB3 H 1.50 0.01 2 320 . 42 PRO CG C 24.5 0.20 1 321 . 42 PRO HG2 H 0.88 0.01 2 322 . 42 PRO HG3 H 0.36 0.01 2 323 . 42 PRO HD2 H 3.18 0.01 2 324 . 42 PRO HD3 H 2.82 0.01 2 325 . 42 PRO C C 176.5 0.20 1 326 . 43 SER N N 117.6 0.25 1 327 . 43 SER H H 8.36 0.01 1 328 . 43 SER CA C 55.5 0.20 1 329 . 43 SER HA H 4.42 0.01 1 330 . 43 SER CB C 63.2 0.20 1 331 . 43 SER HB2 H 4.45 0.01 2 332 . 43 SER HB3 H 4.16 0.01 2 333 . 43 SER C C 174.2 0.20 1 334 . 44 GLU N N 120.6 0.25 1 335 . 44 GLU H H 9.02 0.01 1 336 . 44 GLU CA C 58.0 0.20 1 337 . 44 GLU HA H 3.90 0.01 1 338 . 44 GLU CB C 26.2 0.20 1 339 . 44 GLU HB2 H 2.05 0.01 1 340 . 44 GLU HB3 H 2.05 0.01 1 341 . 44 GLU CG C 32.5 0.20 1 342 . 44 GLU HG2 H 2.53 0.01 2 343 . 44 GLU HG3 H 2.43 0.01 2 344 . 44 GLU C C 178.5 0.20 1 345 . 45 GLU N N 118.4 0.25 1 346 . 45 GLU H H 8.73 0.01 1 347 . 45 GLU CA C 58.1 0.20 1 348 . 45 GLU HA H 4.00 0.01 1 349 . 45 GLU CB C 26.7 0.20 1 350 . 45 GLU HB2 H 2.12 0.01 2 351 . 45 GLU HB3 H 1.98 0.01 2 352 . 45 GLU CG C 33.8 0.20 1 353 . 45 GLU HG2 H 2.44 0.01 1 354 . 45 GLU HG3 H 2.44 0.01 1 355 . 45 GLU C C 178.8 0.20 1 356 . 46 ALA N N 123.6 0.25 1 357 . 46 ALA H H 7.92 0.01 1 358 . 46 ALA CA C 53.2 0.20 1 359 . 46 ALA HA H 4.11 0.01 1 360 . 46 ALA HB H 1.34 0.01 1 361 . 46 ALA CB C 16.3 0.20 1 362 . 46 ALA C C 180.7 0.20 1 363 . 47 LYS N N 117.0 0.25 1 364 . 47 LYS H H 8.52 0.01 1 365 . 47 LYS CA C 59.2 0.20 1 366 . 47 LYS HA H 3.68 0.01 1 367 . 47 LYS CB C 31.2 0.20 1 368 . 47 LYS HB2 H 2.05 0.01 1 369 . 47 LYS HB3 H 2.05 0.01 1 370 . 47 LYS CG C 25.0 0.20 1 371 . 47 LYS HG2 H 0.88 0.01 1 372 . 47 LYS HG3 H 0.88 0.01 1 373 . 47 LYS CD C 28.1 0.20 1 374 . 47 LYS HD2 H 1.60 0.01 1 375 . 47 LYS HD3 H 1.60 0.01 1 376 . 47 LYS CE C 40.0 0.20 1 377 . 47 LYS HE2 H 2.87 0.01 2 378 . 47 LYS HE3 H 2.67 0.01 2 379 . 47 LYS C C 178.4 0.20 1 380 . 48 GLU N N 118.7 0.25 1 381 . 48 GLU H H 8.15 0.01 1 382 . 48 GLU CA C 57.5 0.20 1 383 . 48 GLU HA H 3.92 0.01 1 384 . 48 GLU CB C 26.6 0.20 1 385 . 48 GLU HB2 H 2.22 0.01 2 386 . 48 GLU HB3 H 2.13 0.01 2 387 . 48 GLU CG C 33.3 0.20 1 388 . 48 GLU HG2 H 2.67 0.01 2 389 . 48 GLU HG3 H 2.39 0.01 2 390 . 48 GLU C C 179.1 0.20 1 391 . 49 GLU N N 120.6 0.25 1 392 . 49 GLU H H 7.84 0.01 1 393 . 49 GLU CA C 57.4 0.20 1 394 . 49 GLU HA H 4.11 0.01 1 395 . 49 GLU CB C 27.0 0.20 1 396 . 49 GLU HB2 H 2.22 0.01 2 397 . 49 GLU HB3 H 2.13 0.01 2 398 . 49 GLU CG C 33.2 0.20 1 399 . 49 GLU HG2 H 2.53 0.01 2 400 . 49 GLU HG3 H 2.36 0.01 2 401 . 49 GLU C C 179.5 0.20 1 402 . 50 LEU N N 120.0 0.25 1 403 . 50 LEU H H 8.33 0.01 1 404 . 50 LEU CA C 56.1 0.20 1 405 . 50 LEU HA H 3.90 0.01 1 406 . 50 LEU CB C 40.6 0.20 1 407 . 50 LEU HB2 H 1.89 0.01 2 408 . 50 LEU HB3 H 1.10 0.01 2 409 . 50 LEU CG C 25.0 0.20 1 410 . 50 LEU HG H 1.56 0.01 1 411 . 50 LEU HD1 H 0.14 0.01 1 412 . 50 LEU HD2 H 0.67 0.01 1 413 . 50 LEU CD1 C 22.5 0.20 2 414 . 50 LEU CD2 C 20.8 0.20 2 415 . 50 LEU C C 178.5 0.20 1 416 . 51 ALA N N 122.8 0.25 1 417 . 51 ALA H H 8.66 0.01 1 418 . 51 ALA CA C 54.2 0.20 1 419 . 51 ALA HA H 3.54 0.01 1 420 . 51 ALA HB H 1.48 0.01 1 421 . 51 ALA CB C 15.9 0.20 1 422 . 51 ALA C C 179.7 0.20 1 423 . 52 LYS N N 116.7 0.25 1 424 . 52 LYS H H 7.64 0.01 1 425 . 52 LYS CA C 57.4 0.20 1 426 . 52 LYS HA H 4.10 0.01 1 427 . 52 LYS CB C 30.6 0.20 1 428 . 52 LYS HB2 H 1.98 0.01 1 429 . 52 LYS HB3 H 1.98 0.01 1 430 . 52 LYS CG C 23.3 0.20 1 431 . 52 LYS HG2 H 1.63 0.01 2 432 . 52 LYS HG3 H 1.50 0.01 2 433 . 52 LYS CD C 27.5 0.20 1 434 . 52 LYS HD2 H 1.75 0.01 1 435 . 52 LYS HD3 H 1.75 0.01 1 436 . 52 LYS CE C 40.3 0.20 1 437 . 52 LYS HE2 H 3.03 0.01 1 438 . 52 LYS HE3 H 3.03 0.01 1 439 . 52 LYS C C 179.9 0.20 1 440 . 53 LYS N N 118.9 0.25 1 441 . 53 LYS H H 8.06 0.01 1 442 . 53 LYS CA C 57.5 0.20 1 443 . 53 LYS HA H 4.10 0.01 1 444 . 53 LYS CB C 31.7 0.20 1 445 . 53 LYS HB2 H 2.02 0.01 2 446 . 53 LYS HB3 H 1.98 0.01 2 447 . 53 LYS CG C 23.9 0.20 1 448 . 53 LYS HG2 H 1.72 0.01 2 449 . 53 LYS HG3 H 1.58 0.01 2 450 . 53 LYS CD C 27.8 0.20 1 451 . 53 LYS HD2 H 1.72 0.01 1 452 . 53 LYS HD3 H 1.72 0.01 1 453 . 53 LYS CE C 40.3 0.20 1 454 . 53 LYS HE2 H 3.04 0.01 1 455 . 53 LYS HE3 H 3.04 0.01 1 456 . 53 LYS C C 178.6 0.20 1 457 . 54 CYS N N 112.9 0.25 1 458 . 54 CYS H H 8.22 0.01 1 459 . 54 CYS CA C 59.5 0.20 1 460 . 54 CYS HA H 4.16 0.01 1 461 . 54 CYS CB C 28.2 0.20 1 462 . 54 CYS HB2 H 2.91 0.01 2 463 . 54 CYS HB3 H 2.68 0.01 2 464 . 54 CYS C C 174.6 0.20 1 465 . 55 GLY N N 109.9 0.25 1 466 . 55 GLY H H 8.02 0.01 1 467 . 55 GLY CA C 45.0 0.20 1 468 . 55 GLY HA2 H 4.01 0.01 1 469 . 55 GLY HA3 H 4.01 0.01 1 470 . 55 GLY C C 174.8 0.20 1 471 . 56 ILE N N 112.1 0.25 1 472 . 56 ILE H H 7.78 0.01 1 473 . 56 ILE CA C 57.3 0.20 1 474 . 56 ILE HA H 4.97 0.01 1 475 . 56 ILE CB C 38.2 0.20 1 476 . 56 ILE HB H 2.25 0.01 1 477 . 56 ILE HG2 H 0.81 0.01 1 478 . 56 ILE CG2 C 15.4 0.20 1 479 . 56 ILE CG1 C 22.3 0.20 1 480 . 56 ILE HG12 H 1.48 0.01 2 481 . 56 ILE HG13 H 0.83 0.01 2 482 . 56 ILE HD1 H 0.67 0.01 1 483 . 56 ILE CD1 C 11.9 0.20 1 484 . 56 ILE C C 174.2 0.20 1 485 . 57 THR N N 108.2 0.25 1 486 . 57 THR H H 8.20 0.01 1 487 . 57 THR CA C 58.7 0.20 1 488 . 57 THR HA H 4.68 0.01 1 489 . 57 THR CB C 69.6 0.20 1 490 . 57 THR HB H 4.78 0.01 1 491 . 57 THR HG2 H 1.34 0.01 1 492 . 57 THR CG2 C 20.0 0.20 1 493 . 57 THR C C 176.7 0.20 1 494 . 58 VAL N N 120.6 0.25 1 495 . 58 VAL H H 8.99 0.01 1 496 . 58 VAL CA C 65.5 0.20 1 497 . 58 VAL HA H 3.54 0.01 1 498 . 58 VAL CB C 29.6 0.20 1 499 . 58 VAL HB H 2.12 0.01 1 500 . 58 VAL HG1 H 1.01 0.01 1 501 . 58 VAL HG2 H 1.05 0.01 1 502 . 58 VAL CG1 C 19.7 0.20 1 503 . 58 VAL CG2 C 21.8 0.20 1 504 . 58 VAL C C 178.4 0.20 1 505 . 59 SER N N 115.6 0.25 1 506 . 59 SER H H 8.42 0.01 1 507 . 59 SER CA C 60.4 0.20 1 508 . 59 SER HA H 4.37 0.01 1 509 . 59 SER CB C 60.7 0.20 1 510 . 59 SER HB2 H 3.96 0.01 1 511 . 59 SER HB3 H 3.96 0.01 1 512 . 59 SER C C 177.2 0.20 1 513 . 60 GLN N N 121.4 0.25 1 514 . 60 GLN H H 7.86 0.01 1 515 . 60 GLN CA C 57.7 0.20 1 516 . 60 GLN HA H 4.14 0.01 1 517 . 60 GLN CB C 27.5 0.20 1 518 . 60 GLN HB2 H 2.51 0.01 2 519 . 60 GLN HB3 H 2.01 0.01 2 520 . 60 GLN CG C 33.8 0.20 1 521 . 60 GLN HG2 H 2.51 0.01 1 522 . 60 GLN HG3 H 2.51 0.01 1 523 . 60 GLN NE2 N 112.1 0.25 1 524 . 60 GLN HE21 H 7.68 0.01 1 525 . 60 GLN HE22 H 7.00 0.01 1 526 . 60 GLN C C 179.8 0.20 1 527 . 61 VAL N N 122.0 0.25 1 528 . 61 VAL H H 8.19 0.01 1 529 . 61 VAL CA C 65.8 0.20 1 530 . 61 VAL HA H 3.63 0.01 1 531 . 61 VAL CB C 30.2 0.20 1 532 . 61 VAL HB H 2.54 0.01 1 533 . 61 VAL HG1 H 1.14 0.01 1 534 . 61 VAL HG2 H 1.07 0.01 1 535 . 61 VAL CG1 C 21.0 0.20 1 536 . 61 VAL CG2 C 20.9 0.20 1 537 . 61 VAL C C 178.1 0.20 1 538 . 62 SER N N 115.9 0.25 1 539 . 62 SER H H 9.08 0.01 1 540 . 62 SER CA C 61.0 0.20 1 541 . 62 SER HA H 4.14 0.01 1 542 . 62 SER CB C 60.9 0.20 1 543 . 62 SER HB2 H 4.21 0.01 1 544 . 62 SER HB3 H 4.21 0.01 1 545 . 62 SER C C 177.8 0.20 1 546 . 63 ASN N N 120.6 0.25 1 547 . 63 ASN H H 8.66 0.01 1 548 . 63 ASN CA C 54.3 0.20 1 549 . 63 ASN HA H 4.57 0.01 1 550 . 63 ASN CB C 36.7 0.20 1 551 . 63 ASN HB2 H 2.93 0.01 2 552 . 63 ASN HB3 H 2.86 0.01 2 553 . 63 ASN ND2 N 112.3 0.25 1 554 . 63 ASN HD21 H 7.68 0.01 2 555 . 63 ASN HD22 H 7.00 0.01 2 556 . 63 ASN C C 177.0 0.20 1 557 . 64 TRP N N 122.8 0.25 1 558 . 64 TRP H H 8.30 0.01 1 559 . 64 TRP CA C 61.0 0.20 1 560 . 64 TRP HA H 4.07 0.01 1 561 . 64 TRP HB2 H 3.52 0.01 2 562 . 64 TRP HB3 H 3.25 0.01 2 563 . 64 TRP NE1 N 128.6 0.25 1 564 . 64 TRP HD1 H 7.15 0.01 1 565 . 64 TRP HE3 H 6.28 0.01 1 566 . 64 TRP HE1 H 10.00 0.01 1 567 . 64 TRP HZ3 H 5.80 0.01 1 568 . 64 TRP HZ2 H 7.26 0.01 1 569 . 64 TRP HH2 H 6.59 0.01 1 570 . 64 TRP C C 179.9 0.20 1 571 . 65 PHE N N 117.6 0.25 1 572 . 65 PHE H H 8.63 0.01 1 573 . 65 PHE CA C 61.7 0.20 1 574 . 65 PHE HA H 3.90 0.01 1 575 . 65 PHE HB2 H 3.36 0.01 2 576 . 65 PHE HB3 H 3.25 0.01 2 577 . 65 PHE HZ H 7.39 0.01 1 578 . 65 PHE HD1 H 7.24 0.01 1 579 . 65 PHE HD2 H 7.24 0.01 1 580 . 65 PHE HE1 H 7.76 0.01 1 581 . 65 PHE HE2 H 7.76 0.01 1 582 . 65 PHE C C 178.3 0.20 1 583 . 66 GLY N N 106.3 0.25 1 584 . 66 GLY H H 8.39 0.01 1 585 . 66 GLY CA C 45.7 0.20 1 586 . 66 GLY HA2 H 4.08 0.01 2 587 . 66 GLY HA3 H 3.92 0.01 2 588 . 66 GLY C C 176.0 0.20 1 589 . 67 ASN N N 118.4 0.25 1 590 . 67 ASN H H 7.63 0.01 1 591 . 67 ASN CA C 53.4 0.20 1 592 . 67 ASN HA H 4.50 0.01 1 593 . 67 ASN CB C 37.0 0.20 1 594 . 67 ASN HB2 H 2.63 0.01 2 595 . 67 ASN HB3 H 2.56 0.01 2 596 . 67 ASN ND2 N 113.2 0.25 1 597 . 67 ASN HD21 H 7.43 0.01 2 598 . 67 ASN HD22 H 6.84 0.01 2 599 . 67 ASN C C 176.7 0.20 1 600 . 68 LYS N N 120.9 0.25 1 601 . 68 LYS H H 7.73 0.01 1 602 . 68 LYS CA C 54.9 0.20 1 603 . 68 LYS HA H 3.54 0.01 1 604 . 68 LYS CB C 29.8 0.20 1 605 . 68 LYS HB2 H 1.05 0.01 2 606 . 68 LYS HB3 H 0.40 0.01 2 607 . 68 LYS HG2 H -0.15 0.01 1 608 . 68 LYS HG3 H -0.15 0.01 1 609 . 68 LYS CD C 25.9 0.20 1 610 . 68 LYS HD2 H 0.98 0.01 2 611 . 68 LYS HD3 H 0.52 0.01 2 612 . 68 LYS CE C 40.3 0.20 1 613 . 68 LYS HE2 H 2.15 0.01 1 614 . 68 LYS HE3 H 2.15 0.01 1 615 . 68 LYS C C 178.0 0.20 1 616 . 69 ARG N N 116.2 0.25 1 617 . 69 ARG H H 7.91 0.01 1 618 . 69 ARG CA C 57.4 0.20 1 619 . 69 ARG HA H 4.18 0.01 1 620 . 69 ARG CB C 29.6 0.20 1 621 . 69 ARG HB2 H 1.91 0.01 1 622 . 69 ARG HB3 H 1.91 0.01 1 623 . 69 ARG CG C 27.0 0.20 1 624 . 69 ARG HG2 H 1.82 0.01 1 625 . 69 ARG HG3 H 1.82 0.01 1 626 . 69 ARG CD C 41.6 0.20 1 627 . 69 ARG HD2 H 3.01 0.01 2 628 . 69 ARG HD3 H 2.89 0.01 2 629 . 69 ARG NE N 117.8 0.25 1 630 . 69 ARG HE H 7.35 0.01 1 631 . 69 ARG C C 178.0 0.20 1 632 . 70 ILE N N 118.1 0.25 1 633 . 70 ILE H H 7.45 0.01 1 634 . 70 ILE CA C 61.3 0.20 1 635 . 70 ILE HA H 4.04 0.01 1 636 . 70 ILE CB C 36.5 0.20 1 637 . 70 ILE HB H 1.98 0.01 1 638 . 70 ILE HG2 H 0.90 0.01 1 639 . 70 ILE CG2 C 15.8 0.20 1 640 . 70 ILE CG1 C 26.5 0.20 1 641 . 70 ILE HG12 H 1.67 0.01 2 642 . 70 ILE HG13 H 1.31 0.01 2 643 . 70 ILE HD1 H 0.86 0.01 1 644 . 70 ILE CD1 C 11.1 0.20 1 645 . 70 ILE C C 177.2 0.20 1 646 . 71 ARG N N 121.1 0.25 1 647 . 71 ARG H H 7.85 0.01 1 648 . 71 ARG CA C 55.0 0.20 1 649 . 71 ARG HA H 4.26 0.01 1 650 . 71 ARG CB C 28.8 0.20 1 651 . 71 ARG HB2 H 1.82 0.01 2 652 . 71 ARG HB3 H 1.74 0.01 2 653 . 71 ARG CG C 25.4 0.20 1 654 . 71 ARG HG2 H 1.58 0.01 1 655 . 71 ARG HG3 H 1.58 0.01 1 656 . 71 ARG CD C 41.4 0.20 1 657 . 71 ARG HD2 H 3.13 0.01 1 658 . 71 ARG HD3 H 3.13 0.01 1 659 . 71 ARG NE N 117.3 0.25 1 660 . 71 ARG HE H 7.19 0.01 1 661 . 71 ARG C C 176.7 0.20 1 662 . 72 TYR N N 120.9 0.25 1 663 . 72 TYR H H 8.08 0.01 1 664 . 72 TYR CA C 57.1 0.20 1 665 . 72 TYR HA H 4.50 0.01 1 666 . 72 TYR CB C 36.9 0.20 1 667 . 72 TYR HB2 H 3.11 0.01 2 668 . 72 TYR HB3 H 3.06 0.01 2 669 . 72 TYR HE1 H 6.93 0.01 1 670 . 72 TYR HE2 H 6.93 0.01 1 671 . 72 TYR HD1 H 7.26 0.01 1 672 . 72 TYR HD2 H 7.26 0.01 1 673 . 72 TYR C C 175.3 0.20 1 674 . 73 LYS N N 123.1 0.25 1 675 . 73 LYS H H 7.89 0.01 1 676 . 73 LYS CA C 54.3 0.20 1 677 . 73 LYS HA H 4.26 0.01 1 678 . 73 LYS CB C 31.4 0.20 1 679 . 73 LYS HB2 H 1.86 0.01 2 680 . 73 LYS HB3 H 1.79 0.01 2 681 . 73 LYS CG C 22.9 0.20 1 682 . 73 LYS HG2 H 1.41 0.01 1 683 . 73 LYS HG3 H 1.41 0.01 1 684 . 73 LYS CD C 27.4 0.20 1 685 . 73 LYS HD2 H 1.72 0.01 1 686 . 73 LYS HD3 H 1.72 0.01 1 687 . 73 LYS CE C 40.4 0.20 1 688 . 73 LYS HE2 H 3.06 0.01 1 689 . 73 LYS HE3 H 3.06 0.01 1 690 . 73 LYS C C 175.8 0.20 1 691 . 74 LYS N N 123.3 0.25 1 692 . 74 LYS H H 8.27 0.01 1 693 . 74 LYS CA C 54.7 0.20 1 694 . 74 LYS HA H 4.37 0.01 1 695 . 74 LYS CB C 31.3 0.20 1 696 . 74 LYS HB2 H 1.91 0.01 2 697 . 74 LYS CG C 22.9 0.20 1 698 . 74 LYS HG2 H 1.50 0.01 1 699 . 74 LYS HG3 H 1.50 0.01 1 700 . 74 LYS CD C 27.4 0.20 1 701 . 74 LYS HD2 H 1.75 0.01 1 702 . 74 LYS HD3 H 1.75 0.01 1 703 . 74 LYS CE C 40.4 0.20 1 704 . 74 LYS HE2 H 3.08 0.01 1 705 . 74 LYS HE3 H 3.08 0.01 1 706 . 74 LYS C C 175.5 0.20 1 707 . 75 ASN N N 125.3 0.25 1 708 . 75 ASN H H 8.06 0.01 1 709 . 75 ASN CA C 52.9 0.20 1 710 . 75 ASN HA H 4.50 0.01 1 711 . 75 ASN CB C 38.5 0.20 1 712 . 75 ASN HB2 H 2.80 0.01 2 713 . 75 ASN HB3 H 2.27 0.01 2 714 . 75 ASN ND2 N 112.3 0.25 1 715 . 75 ASN HD21 H 7.53 0.01 2 716 . 75 ASN HD22 H 6.88 0.01 2 stop_ save_