data_4758 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A novel killer toxin-like protein, SKLP, is a member of the single-domain beta-gamma crystallin family proteins ; _BMRB_accession_number 4758 _BMRB_flat_file_name bmr4758.str _Entry_type original _Submission_date 2000-06-12 _Accession_date 2000-06-12 _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 Ohki Shin-ya . . 2 Kariya Eri . . 3 Hiraga Kazumi . . 4 Wakamiya Akiko . . 5 Isobe Toshiaki . . 6 Oda Kohei . . 7 Kainosho Masatsune . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 364 "13C chemical shifts" 254 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-01 original author . stop_ _Original_release_date 2001-05-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of Streptomyces Killer Toxin-like Protein, SKLP: Further Evidence for the Wide Distribution of Single-domain Betagamma-crystallin Superfamily Proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20566721 _PubMed_ID 11114251 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ohki Shin-ya . . 2 Kariya Eri . . 3 Hiraga Kazumi . . 4 Wakamiya Akiko . . 5 Isobe Toshiaki . . 6 Oda Kohei . . 7 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 305 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 109 _Page_last 120 _Year 2001 _Details . loop_ _Keyword 'killer toxin-like protein' stop_ save_ ################################## # Molecular system description # ################################## save_SKLP_system _Saveframe_category molecular_system _Mol_system_name SKLP _Abbreviation_common SKLP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SKLP monomer' $SKLP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SKLP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'yeast killer toxin-like protein' _Abbreviation_common SKLP _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 84 _Mol_residue_sequence ; IDHVPCRGGENFLKIWSHSG GQQSVDCYANRGRIDFGGWW VDKISTGNNDLIYYDANGDS VRVDRWHDITYPNRPPKVNS IEIL ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 ASP 3 HIS 4 VAL 5 PRO 6 CYS 7 ARG 8 GLY 9 GLY 10 GLU 11 ASN 12 PHE 13 LEU 14 LYS 15 ILE 16 TRP 17 SER 18 HIS 19 SER 20 GLY 21 GLY 22 GLN 23 GLN 24 SER 25 VAL 26 ASP 27 CYS 28 TYR 29 ALA 30 ASN 31 ARG 32 GLY 33 ARG 34 ILE 35 ASP 36 PHE 37 GLY 38 GLY 39 TRP 40 TRP 41 VAL 42 ASP 43 LYS 44 ILE 45 SER 46 THR 47 GLY 48 ASN 49 ASN 50 ASP 51 LEU 52 ILE 53 TYR 54 TYR 55 ASP 56 ALA 57 ASN 58 GLY 59 ASP 60 SER 61 VAL 62 ARG 63 VAL 64 ASP 65 ARG 66 TRP 67 HIS 68 ASP 69 ILE 70 THR 71 TYR 72 PRO 73 ASN 74 ARG 75 PRO 76 PRO 77 LYS 78 VAL 79 ASN 80 SER 81 ILE 82 GLU 83 ILE 84 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 1F53 "Nmr Structure Of Killer Toxin-Like Protein Sklp" 100.00 84 100.00 100.00 4.47e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SKLP 'Streptomyces sp. F-287' 1883 Eubacteria . Streptomyces 'sp. F-287' 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 $SKLP 'purified from the natural source' . . . . . 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 $SKLP 1.0 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.08 n/a temperature 303 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449519 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329112 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_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SKLP monomer' _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 ILE C C 167.00 . 1 2 . 1 ILE CA C 56.70 . 1 3 . 1 ILE HA H 4.26 . 1 4 . 1 ILE CB C 36.23 . 1 5 . 1 ILE HB H 1.56 . 1 6 . 1 ILE HG12 H 0.81 . 1 7 . 1 ILE HG13 H 1.90 . 1 8 . 1 ILE HG2 H 0.75 . 1 9 . 1 ILE HD1 H 0.66 . 1 10 . 2 ASP N N 126.55 . 1 11 . 2 ASP C C 171.52 . 1 12 . 2 ASP CA C 50.82 . 1 13 . 2 ASP HA H 5.06 . 1 14 . 2 ASP CB C 42.73 . 1 15 . 2 ASP HB2 H 2.47 . 1 16 . 2 ASP HB3 H 2.27 . 1 17 . 3 HIS N N 123.91 . 1 18 . 3 HIS C C 172.18 . 1 19 . 3 HIS CA C 52.17 . 1 20 . 3 HIS HA H 4.69 . 1 21 . 3 HIS CB C 27.14 . 1 22 . 3 HIS HB2 H 3.35 . 1 23 . 3 HIS HB3 H 2.83 . 1 24 . 4 VAL N N 121.81 . 1 25 . 4 VAL CA C 55.55 . 1 26 . 4 VAL HA H 4.63 . 1 27 . 4 VAL CB C 30.70 . 1 28 . 4 VAL HB H 1.77 . 1 29 . 4 VAL HG1 H 0.57 . 1 30 . 4 VAL HG2 H -0.26 . 1 31 . 4 VAL CG1 C 19.85 . 1 32 . 4 VAL CG2 C 14.85 . 1 33 . 5 PRO C C 175.60 . 1 34 . 5 PRO CA C 60.23 . 1 35 . 5 PRO HA H 4.17 . 1 36 . 5 PRO CB C 29.53 . 1 37 . 5 PRO HB2 H 2.21 . 1 38 . 5 PRO HB3 H 1.65 . 1 39 . 5 PRO HG2 H 1.99 . 1 40 . 5 PRO HG3 H 1.80 . 1 41 . 5 PRO HD2 H 1.80 . 1 42 . 5 PRO HD3 H 3.44 . 1 43 . 6 CYS N N 121.43 . 1 44 . 6 CYS C C 173.17 . 1 45 . 6 CYS CA C 52.10 . 1 46 . 6 CYS HA H 4.42 . 1 47 . 6 CYS CB C 38.04 . 1 48 . 6 CYS HB2 H 2.95 . 1 49 . 6 CYS HB3 H 2.71 . 1 50 . 7 ARG N N 120.16 . 1 51 . 7 ARG C C 173.92 . 1 52 . 7 ARG CA C 53.61 . 1 53 . 7 ARG HA H 4.45 . 1 54 . 7 ARG CB C 29.74 . 1 55 . 7 ARG HB2 H 1.82 . 1 56 . 7 ARG HB3 H 1.71 . 1 57 . 7 ARG HG2 H 1.53 . 1 58 . 7 ARG HG3 H 1.47 . 1 59 . 7 ARG HD2 H 3.14 . 1 60 . 7 ARG HD3 H 3.05 . 1 61 . 8 GLY N N 110.60 . 1 62 . 8 GLY C C 172.38 . 1 63 . 8 GLY CA C 43.82 . 1 64 . 8 GLY HA2 H 3.98 . 1 65 . 9 GLY N N 109.62 . 1 66 . 9 GLY C C 171.72 . 1 67 . 9 GLY CA C 43.36 . 1 68 . 9 GLY HA2 H 3.89 . 1 69 . 10 GLU N N 118.02 . 1 70 . 10 GLU C C 174.15 . 1 71 . 10 GLU CA C 53.48 . 1 72 . 10 GLU HA H 4.36 . 1 73 . 10 GLU CB C 28.22 . 1 74 . 10 GLU HB2 H 1.50 . 1 75 . 10 GLU HB3 H 1.45 . 1 76 . 10 GLU HG2 H 2.09 . 1 77 . 11 ASN N N 117.70 . 1 78 . 11 ASN C C 172.67 . 1 79 . 11 ASN CA C 51.05 . 1 80 . 11 ASN HA H 4.80 . 1 81 . 11 ASN CB C 36.66 . 1 82 . 11 ASN HB2 H 2.80 . 1 83 . 11 ASN HD21 H 7.94 . 1 84 . 11 ASN HD22 H 7.21 . 1 85 . 11 ASN ND2 N 113.67 . 1 86 . 12 PHE N N 117.41 . 1 87 . 12 PHE C C 173.32 . 1 88 . 12 PHE CA C 53.48 . 1 89 . 12 PHE HA H 4.95 . 1 90 . 12 PHE CB C 36.65 . 1 91 . 12 PHE HB2 H 3.38 . 1 92 . 12 PHE HB3 H 2.73 . 1 93 . 12 PHE HD1 H 7.24 . 1 94 . 12 PHE HE1 H 7.39 . 1 95 . 13 LEU N N 122.09 . 1 96 . 13 LEU C C 172.21 . 1 97 . 13 LEU CA C 53.33 . 1 98 . 13 LEU HA H 4.69 . 1 99 . 13 LEU CB C 40.49 . 1 100 . 13 LEU HB2 H 1.96 . 1 101 . 13 LEU HB3 H 1.39 . 1 102 . 13 LEU HG H 1.61 . 1 103 . 13 LEU HD1 H 0.98 . 1 104 . 13 LEU HD2 H 0.78 . 1 105 . 13 LEU CD1 C 24.68 . 1 106 . 13 LEU CD2 C 25.96 . 1 107 . 14 LYS N N 131.13 . 1 108 . 14 LYS C C 172.05 . 1 109 . 14 LYS CA C 53.35 . 1 110 . 14 LYS HA H 5.35 . 1 111 . 14 LYS CB C 35.06 . 1 112 . 14 LYS HB2 H 1.84 . 1 113 . 14 LYS HB3 H 1.54 . 1 114 . 14 LYS HG2 H 0.95 . 1 115 . 14 LYS HG3 H 0.12 . 1 116 . 14 LYS HD2 H 1.43 . 1 117 . 14 LYS HD3 H 0.96 . 1 118 . 14 LYS HE2 H 2.67 . 1 119 . 14 LYS HE3 H 2.30 . 1 120 . 15 ILE N N 123.57 . 1 121 . 15 ILE C C 173.39 . 1 122 . 15 ILE CA C 58.57 . 1 123 . 15 ILE HA H 5.15 . 1 124 . 15 ILE CB C 40.47 . 1 125 . 15 ILE HB H 1.90 . 1 126 . 15 ILE HG12 H 1.02 . 1 127 . 15 ILE HG13 H 1.67 . 1 128 . 15 ILE HG2 H 1.08 . 1 129 . 15 ILE HD1 H 0.54 . 1 130 . 16 TRP N N 134.50 . 1 131 . 16 TRP C C 173.23 . 1 132 . 16 TRP CA C 56.11 . 1 133 . 16 TRP HA H 5.60 . 1 134 . 16 TRP CB C 30.23 . 1 135 . 16 TRP HB2 H 3.75 . 1 136 . 16 TRP HB3 H 3.57 . 1 137 . 16 TRP HE3 H 7.74 . 1 138 . 16 TRP HZ2 H 7.27 . 1 139 . 16 TRP HZ3 H 6.99 . 1 140 . 16 TRP HH2 H 7.51 . 1 141 . 17 SER N N 118.77 . 1 142 . 17 SER C C 171.94 . 1 143 . 17 SER CA C 56.12 . 1 144 . 17 SER HA H 6.22 . 1 145 . 17 SER CB C 66.30 . 1 146 . 17 SER HB2 H 4.39 . 1 147 . 17 SER HB3 H 4.15 . 1 148 . 18 HIS N N 112.75 . 1 149 . 18 HIS C C 170.76 . 1 150 . 18 HIS CA C 54.36 . 1 151 . 18 HIS HA H 5.84 . 1 152 . 18 HIS CB C 30.52 . 1 153 . 18 HIS HB2 H 3.48 . 1 154 . 18 HIS HB3 H 3.32 . 1 155 . 19 SER N N 112.64 . 1 156 . 19 SER C C 173.75 . 1 157 . 19 SER CA C 55.89 . 1 158 . 19 SER HA H 4.25 . 1 159 . 19 SER CB C 58.89 . 1 160 . 19 SER HB2 H 2.27 . 1 161 . 19 SER HB3 H 1.80 . 1 162 . 20 GLY N N 118.80 . 1 163 . 20 GLY C C 172.98 . 1 164 . 20 GLY CA C 45.15 . 1 165 . 20 GLY HA2 H 3.92 . 1 166 . 20 GLY HA3 H 3.75 . 1 167 . 21 GLY N N 112.00 . 1 168 . 21 GLY C C 171.83 . 1 169 . 21 GLY CA C 43.22 . 1 170 . 21 GLY HA2 H 4.02 . 1 171 . 21 GLY HA3 H 3.90 . 1 172 . 22 GLN N N 119.69 . 1 173 . 22 GLN C C 172.65 . 1 174 . 22 GLN CA C 52.80 . 1 175 . 22 GLN HA H 4.69 . 1 176 . 22 GLN CB C 29.34 . 1 177 . 22 GLN HB2 H 2.34 . 1 178 . 22 GLN HB3 H 2.14 . 1 179 . 22 GLN HG2 H 2.49 . 1 180 . 23 GLN N N 119.84 . 1 181 . 23 GLN C C 173.56 . 1 182 . 23 GLN CA C 52.81 . 1 183 . 23 GLN HA H 5.52 . 1 184 . 23 GLN CB C 30.09 . 1 185 . 23 GLN HB2 H 2.53 . 1 186 . 23 GLN HB3 H 2.21 . 1 187 . 23 GLN HG2 H 2.48 . 1 188 . 24 SER N N 116.22 . 1 189 . 24 SER C C 170.94 . 1 190 . 24 SER CA C 55.67 . 1 191 . 24 SER HA H 4.77 . 1 192 . 24 SER CB C 62.98 . 1 193 . 24 SER HB2 H 3.58 . 1 194 . 24 SER HB3 H 3.47 . 1 195 . 25 VAL N N 127.53 . 1 196 . 25 VAL C C 172.90 . 1 197 . 25 VAL CA C 59.76 . 1 198 . 25 VAL HA H 4.79 . 1 199 . 25 VAL CB C 31.11 . 1 200 . 25 VAL HB H 1.72 . 1 201 . 25 VAL HG1 H 0.23 . 1 202 . 25 VAL HG2 H 0.71 . 1 203 . 25 VAL CG1 C 18.61 . 1 204 . 25 VAL CG2 C 18.99 . 1 205 . 26 ASP N N 125.18 . 1 206 . 26 ASP C C 171.00 . 1 207 . 26 ASP CA C 51.48 . 1 208 . 26 ASP HA H 5.21 . 1 209 . 26 ASP CB C 45.05 . 1 210 . 26 ASP HB2 H 2.53 . 1 211 . 26 ASP HB3 H 2.33 . 1 212 . 27 CYS N N 117.33 . 1 213 . 27 CYS C C 170.31 . 1 214 . 27 CYS CA C 54.82 . 1 215 . 27 CYS HA H 6.02 . 1 216 . 27 CYS CB C 44.79 . 1 217 . 27 CYS HB2 H 2.80 . 1 218 . 27 CYS HB3 H 2.72 . 1 219 . 28 TYR N N 116.77 . 1 220 . 28 TYR C C 171.28 . 1 221 . 28 TYR CA C 54.07 . 1 222 . 28 TYR HA H 5.48 . 1 223 . 28 TYR CB C 41.83 . 1 224 . 28 TYR HB2 H 2.79 . 1 225 . 28 TYR HB3 H 2.40 . 1 226 . 28 TYR HD1 H 6.63 . 1 227 . 28 TYR HE1 H 6.40 . 1 228 . 29 ALA N N 119.99 . 1 229 . 29 ALA C C 174.19 . 1 230 . 29 ALA CA C 49.04 . 1 231 . 29 ALA HA H 4.64 . 1 232 . 29 ALA CB C 21.85 . 1 233 . 29 ALA HB H 1.25 . 1 234 . 30 ASN N N 111.06 . 1 235 . 30 ASN C C 170.24 . 1 236 . 30 ASN CA C 53.19 . 1 237 . 30 ASN HA H 4.37 . 1 238 . 30 ASN CB C 36.00 . 1 239 . 30 ASN HB2 H 3.66 . 1 240 . 30 ASN HB3 H 2.80 . 1 241 . 30 ASN HD21 H 8.00 . 1 242 . 30 ASN HD22 H 7.15 . 1 243 . 30 ASN ND2 N 116.00 . 1 244 . 31 ARG N N 114.59 . 1 245 . 31 ARG C C 176.20 . 1 246 . 31 ARG CA C 54.87 . 1 247 . 31 ARG HA H 4.00 . 1 248 . 31 ARG CB C 29.39 . 1 249 . 31 ARG HB2 H 1.82 . 1 250 . 31 ARG HB3 H 1.70 . 1 251 . 31 ARG HG2 H 1.58 . 1 252 . 31 ARG HG3 H 1.74 . 1 253 . 31 ARG HD2 H 3.25 . 1 254 . 32 GLY N N 113.73 . 1 255 . 32 GLY C C 168.01 . 1 256 . 32 GLY CA C 42.11 . 1 257 . 32 GLY HA2 H 4.60 . 1 258 . 32 GLY HA3 H 3.90 . 1 259 . 33 ARG N N 119.86 . 1 260 . 33 ARG C C 172.58 . 1 261 . 33 ARG CA C 52.16 . 1 262 . 33 ARG HA H 5.59 . 1 263 . 33 ARG CB C 31.76 . 1 264 . 33 ARG HB2 H 1.74 . 1 265 . 33 ARG HB3 H 1.38 . 1 266 . 33 ARG HG2 H 1.50 . 1 267 . 33 ARG HG3 H 1.47 . 1 268 . 33 ARG HD2 H 2.90 . 1 269 . 33 ARG HD3 H 2.85 . 1 270 . 34 ILE N N 125.38 . 1 271 . 34 ILE C C 170.55 . 1 272 . 34 ILE CA C 57.57 . 1 273 . 34 ILE HA H 4.62 . 1 274 . 34 ILE CB C 40.51 . 1 275 . 34 ILE HB H 1.67 . 1 276 . 34 ILE HG12 H 1.46 . 1 277 . 34 ILE HG13 H 1.40 . 1 278 . 34 ILE HG2 H 0.66 . 1 279 . 34 ILE HD1 H 0.97 . 1 280 . 35 ASP N N 124.48 . 1 281 . 35 ASP C C 172.90 . 1 282 . 35 ASP CA C 53.23 . 1 283 . 35 ASP HA H 4.64 . 1 284 . 35 ASP CB C 39.17 . 1 285 . 35 ASP HB2 H 2.71 . 1 286 . 35 ASP HB3 H 2.60 . 1 287 . 36 PHE N N 125.16 . 1 288 . 36 PHE C C 174.49 . 1 289 . 36 PHE CA C 55.24 . 1 290 . 36 PHE HA H 4.47 . 1 291 . 36 PHE CB C 40.96 . 1 292 . 36 PHE HB2 H 2.75 . 1 293 . 36 PHE HB3 H 2.55 . 1 294 . 36 PHE HD1 H 7.14 . 1 295 . 36 PHE HE1 H 7.34 . 1 296 . 36 PHE HZ H 7.60 . 1 297 . 37 GLY N N 104.61 . 1 298 . 37 GLY C C 173.46 . 1 299 . 37 GLY CA C 43.90 . 1 300 . 37 GLY HA2 H 3.86 . 1 301 . 37 GLY HA3 H 3.77 . 1 302 . 38 GLY N N 107.20 . 1 303 . 38 GLY C C 172.55 . 1 304 . 38 GLY CA C 44.63 . 1 305 . 38 GLY HA2 H 3.87 . 1 306 . 38 GLY HA3 H 3.48 . 1 307 . 39 TRP N N 119.73 . 1 308 . 39 TRP C C 171.99 . 1 309 . 39 TRP CA C 56.23 . 1 310 . 39 TRP HA H 4.38 . 1 311 . 39 TRP CB C 27.34 . 1 312 . 39 TRP HB2 H 3.24 . 1 313 . 39 TRP HB3 H 2.84 . 1 314 . 39 TRP HE3 H 7.89 . 1 315 . 39 TRP HZ2 H 7.36 . 1 316 . 39 TRP HZ3 H 7.20 . 1 317 . 39 TRP HH2 H 7.55 . 1 318 . 40 TRP N N 120.45 . 1 319 . 40 TRP C C 174.22 . 1 320 . 40 TRP CA C 55.99 . 1 321 . 40 TRP HA H 5.08 . 1 322 . 40 TRP CB C 27.42 . 1 323 . 40 TRP HB2 H 2.45 . 1 324 . 40 TRP HB3 H 2.03 . 1 325 . 40 TRP HE3 H 7.41 . 1 326 . 40 TRP HZ2 H 6.69 . 1 327 . 40 TRP HH2 H 7.02 . 1 328 . 41 VAL N N 122.75 . 1 329 . 41 VAL C C 170.29 . 1 330 . 41 VAL CA C 61.26 . 1 331 . 41 VAL HA H 4.23 . 1 332 . 41 VAL CB C 31.13 . 1 333 . 41 VAL HB H 1.60 . 1 334 . 41 VAL HG1 H 0.90 . 1 335 . 41 VAL HG2 H 0.67 . 1 336 . 41 VAL CG1 C 19.97 . 1 337 . 41 VAL CG2 C 22.45 . 1 338 . 42 ASP N N 123.38 . 1 339 . 42 ASP C C 175.40 . 1 340 . 42 ASP CA C 54.36 . 1 341 . 42 ASP HA H 4.95 . 1 342 . 42 ASP CB C 42.01 . 1 343 . 42 ASP HB2 H 2.83 . 1 344 . 42 ASP HB3 H 2.43 . 1 345 . 43 LYS N N 119.85 . 1 346 . 43 LYS C C 171.52 . 1 347 . 43 LYS CA C 53.94 . 1 348 . 43 LYS HA H 5.33 . 1 349 . 43 LYS CB C 32.55 . 1 350 . 43 LYS HB2 H 1.73 . 1 351 . 43 LYS HB3 H 1.54 . 1 352 . 43 LYS HG2 H 0.74 . 1 353 . 43 LYS HG3 H -0.24 . 1 354 . 43 LYS HD2 H 1.19 . 1 355 . 43 LYS HD3 H 0.94 . 1 356 . 43 LYS HE2 H 2.10 . 1 357 . 43 LYS HE3 H 2.00 . 1 358 . 44 ILE N N 125.07 . 1 359 . 44 ILE C C 172.23 . 1 360 . 44 ILE CA C 58.94 . 1 361 . 44 ILE HA H 5.05 . 1 362 . 44 ILE CB C 41.35 . 1 363 . 44 ILE HB H 1.70 . 1 364 . 44 ILE HG12 H 0.90 . 1 365 . 44 ILE HD1 H 0.83 . 1 366 . 45 SER N N 122.66 . 1 367 . 45 SER C C 173.84 . 1 368 . 45 SER CA C 54.43 . 1 369 . 45 SER HA H 5.95 . 1 370 . 45 SER CB C 62.72 . 1 371 . 45 SER HB2 H 4.32 . 1 372 . 45 SER HB3 H 4.06 . 1 373 . 46 THR N N 116.63 . 1 374 . 46 THR C C 174.03 . 1 375 . 46 THR CA C 61.77 . 1 376 . 46 THR HA H 4.19 . 1 377 . 46 THR CB C 66.40 . 1 378 . 46 THR HB H 5.05 . 1 379 . 46 THR HG2 H 1.18 . 1 380 . 47 GLY N N 110.02 . 1 381 . 47 GLY C C 172.55 . 1 382 . 47 GLY CA C 43.23 . 1 383 . 47 GLY HA2 H 3.45 . 1 384 . 47 GLY HA3 H 3.19 . 1 385 . 48 ASN N N 123.08 . 1 386 . 48 ASN C C 172.03 . 1 387 . 48 ASN CA C 49.57 . 1 388 . 48 ASN HA H 3.91 . 1 389 . 48 ASN CB C 35.28 . 1 390 . 48 ASN HB2 H 2.79 . 1 391 . 48 ASN HB3 H 2.62 . 1 392 . 48 ASN HD21 H 7.67 . 1 393 . 48 ASN HD22 H 7.00 . 1 394 . 48 ASN ND2 N 109.49 . 1 395 . 49 ASN N N 115.44 . 1 396 . 49 ASN C C 169.75 . 1 397 . 49 ASN CA C 50.76 . 1 398 . 49 ASN HA H 4.76 . 1 399 . 49 ASN CB C 40.38 . 1 400 . 49 ASN HB2 H 2.79 . 1 401 . 49 ASN HB3 H 2.32 . 1 402 . 49 ASN HD21 H 7.77 . 1 403 . 49 ASN HD22 H 6.96 . 1 404 . 49 ASN ND2 N 116.35 . 1 405 . 50 ASP N N 120.45 . 1 406 . 50 ASP C C 171.42 . 1 407 . 50 ASP CA C 51.69 . 1 408 . 50 ASP HA H 4.99 . 1 409 . 50 ASP CB C 40.90 . 1 410 . 50 ASP HB2 H 2.56 . 1 411 . 51 LEU N N 124.62 . 1 412 . 51 LEU C C 173.60 . 1 413 . 51 LEU CA C 50.93 . 1 414 . 51 LEU HA H 5.34 . 1 415 . 51 LEU CB C 45.01 . 1 416 . 51 LEU HB2 H 2.07 . 1 417 . 51 LEU HB3 H 1.16 . 1 418 . 51 LEU HG H 1.45 . 1 419 . 51 LEU HD1 H 0.85 . 1 420 . 51 LEU HD2 H 0.93 . 1 421 . 51 LEU CD1 C 22.29 . 1 422 . 51 LEU CD2 C 26.18 . 1 423 . 52 ILE N N 123.85 . 1 424 . 52 ILE C C 172.77 . 1 425 . 52 ILE CA C 58.24 . 1 426 . 52 ILE HA H 4.88 . 1 427 . 52 ILE CB C 38.83 . 1 428 . 52 ILE HB H 1.44 . 1 429 . 52 ILE HG12 H 0.68 . 1 430 . 52 ILE HG2 H 0.23 . 1 431 . 52 ILE HD1 H 0.74 . 1 432 . 53 TYR N N 121.48 . 1 433 . 53 TYR C C 170.05 . 1 434 . 53 TYR CA C 52.06 . 1 435 . 53 TYR HA H 5.42 . 1 436 . 53 TYR CB C 39.43 . 1 437 . 53 TYR HB2 H 3.24 . 1 438 . 53 TYR HB3 H 2.36 . 1 439 . 53 TYR HD1 H 6.59 . 1 440 . 53 TYR HE1 H 6.45 . 1 441 . 54 TYR N N 119.12 . 1 442 . 54 TYR C C 174.33 . 1 443 . 54 TYR CA C 54.46 . 1 444 . 54 TYR HA H 5.17 . 1 445 . 54 TYR CB C 37.07 . 1 446 . 54 TYR HB2 H 2.93 . 1 447 . 54 TYR HB3 H 2.82 . 1 448 . 54 TYR HD1 H 6.85 . 1 449 . 54 TYR HE1 H 6.63 . 1 450 . 55 ASP N N 124.85 . 1 451 . 55 ASP C C 175.95 . 1 452 . 55 ASP CA C 50.65 . 1 453 . 55 ASP HA H 5.26 . 1 454 . 55 ASP CB C 40.65 . 1 455 . 55 ASP HB2 H 3.29 . 1 456 . 55 ASP HB3 H 2.69 . 1 457 . 56 ALA N N 122.43 . 1 458 . 56 ALA C C 175.96 . 1 459 . 56 ALA CA C 51.84 . 1 460 . 56 ALA HA H 4.15 . 1 461 . 56 ALA CB C 16.39 . 1 462 . 56 ALA HB H 1.33 . 1 463 . 57 ASN N N 115.94 . 1 464 . 57 ASN C C 173.71 . 1 465 . 57 ASN CA C 50.88 . 1 466 . 57 ASN HA H 4.79 . 1 467 . 57 ASN CB C 36.66 . 1 468 . 57 ASN HB2 H 3.03 . 1 469 . 57 ASN HB3 H 2.95 . 1 470 . 57 ASN HD21 H 8.10 . 1 471 . 57 ASN HD22 H 6.97 . 1 472 . 57 ASN ND2 N 113.37 . 1 473 . 58 GLY N N 108.07 . 1 474 . 58 GLY C C 172.32 . 1 475 . 58 GLY CA C 42.95 . 1 476 . 58 GLY HA2 H 4.36 . 1 477 . 58 GLY HA3 H 3.75 . 1 478 . 59 ASP N N 122.46 . 1 479 . 59 ASP C C 172.79 . 1 480 . 59 ASP CA C 52.37 . 1 481 . 59 ASP HA H 4.80 . 1 482 . 59 ASP CB C 39.24 . 1 483 . 59 ASP HB2 H 2.82 . 1 484 . 59 ASP HB3 H 2.56 . 1 485 . 60 SER N N 114.93 . 1 486 . 60 SER C C 171.69 . 1 487 . 60 SER CA C 53.53 . 1 488 . 60 SER HA H 5.06 . 1 489 . 60 SER CB C 63.72 . 1 490 . 60 SER HB2 H 3.44 . 1 491 . 60 SER HB3 H 3.27 . 1 492 . 61 VAL N N 124.37 . 1 493 . 61 VAL C C 170.86 . 1 494 . 61 VAL CA C 59.29 . 1 495 . 61 VAL HA H 3.77 . 1 496 . 61 VAL CB C 32.03 . 1 497 . 61 VAL HB H 0.05 . 1 498 . 61 VAL HG1 H 0.60 . 1 499 . 61 VAL HG2 H 0.52 . 1 500 . 61 VAL CG1 C 18.82 . 1 501 . 61 VAL CG2 C 18.76 . 1 502 . 62 ARG N N 125.88 . 1 503 . 62 ARG C C 174.14 . 1 504 . 62 ARG CA C 51.87 . 1 505 . 62 ARG HA H 5.17 . 1 506 . 62 ARG CB C 29.44 . 1 507 . 62 ARG HB2 H 1.70 . 1 508 . 62 ARG HB3 H 1.47 . 1 509 . 62 ARG HG2 H 1.29 . 1 510 . 62 ARG HG3 H 1.45 . 1 511 . 62 ARG HD2 H 3.03 . 1 512 . 62 ARG HD3 H 3.01 . 1 513 . 63 VAL N N 128.20 . 1 514 . 63 VAL C C 171.74 . 1 515 . 63 VAL CA C 59.54 . 1 516 . 63 VAL HA H 4.06 . 1 517 . 63 VAL CB C 31.45 . 1 518 . 63 VAL HB H 1.96 . 1 519 . 63 VAL HG1 H 1.06 . 1 520 . 63 VAL HG2 H 0.94 . 1 521 . 63 VAL CG1 C 20.53 . 1 522 . 63 VAL CG2 C 18.12 . 1 523 . 64 ASP N N 125.53 . 1 524 . 64 ASP C C 175.08 . 1 525 . 64 ASP CA C 52.44 . 1 526 . 64 ASP HA H 4.93 . 1 527 . 64 ASP CB C 40.81 . 1 528 . 64 ASP HB2 H 2.13 . 1 529 . 64 ASP HB3 H 2.81 . 1 530 . 65 ARG N N 118.66 . 1 531 . 65 ARG C C 175.17 . 1 532 . 65 ARG CA C 54.07 . 1 533 . 65 ARG HA H 4.46 . 1 534 . 65 ARG CB C 28.42 . 1 535 . 65 ARG HB2 H 1.45 . 1 536 . 65 ARG HB3 H 1.36 . 1 537 . 65 ARG HG2 H 1.60 . 1 538 . 65 ARG HG3 H 1.55 . 1 539 . 65 ARG HD2 H 3.30 . 1 540 . 65 ARG HD3 H 2.99 . 1 541 . 66 TRP N N 122.45 . 1 542 . 66 TRP C C 173.81 . 1 543 . 66 TRP CA C 54.27 . 1 544 . 66 TRP HA H 4.70 . 1 545 . 66 TRP CB C 24.29 . 1 546 . 66 TRP HB2 H 3.37 . 1 547 . 67 HIS N N 115.86 . 1 548 . 67 HIS C C 170.60 . 1 549 . 67 HIS CA C 53.71 . 1 550 . 67 HIS HA H 4.97 . 1 551 . 67 HIS CB C 29.90 . 1 552 . 67 HIS HB2 H 3.28 . 1 553 . 67 HIS HB3 H 2.95 . 1 554 . 68 ASP N N 122.49 . 1 555 . 68 ASP C C 172.99 . 1 556 . 68 ASP CA C 51.00 . 1 557 . 68 ASP HA H 5.96 . 1 558 . 68 ASP CB C 40.25 . 1 559 . 68 ASP HB2 H 2.66 . 1 560 . 68 ASP HB3 H 2.52 . 1 561 . 69 ILE N N 123.66 . 1 562 . 69 ILE C C 171.81 . 1 563 . 69 ILE CA C 56.95 . 1 564 . 69 ILE HA H 4.60 . 1 565 . 69 ILE CB C 39.06 . 1 566 . 69 ILE HB H 1.70 . 1 567 . 69 ILE HG12 H 1.40 . 1 568 . 69 ILE HG13 H 1.11 . 1 569 . 69 ILE HG2 H 0.66 . 1 570 . 69 ILE HD1 H 0.97 . 1 571 . 70 THR N N 116.02 . 1 572 . 70 THR C C 170.67 . 1 573 . 70 THR CA C 57.42 . 1 574 . 70 THR HA H 4.80 . 1 575 . 70 THR CB C 68.96 . 1 576 . 70 THR HB H 4.07 . 1 577 . 70 THR HG2 H 1.07 . 1 578 . 71 TYR N N 119.22 . 1 579 . 71 TYR CA C 52.78 . 1 580 . 71 TYR HA H 5.22 . 1 581 . 71 TYR CB C 36.63 . 1 582 . 71 TYR HB2 H 3.27 . 1 583 . 71 TYR HB3 H 3.03 . 1 584 . 71 TYR HD1 H 7.08 . 1 585 . 71 TYR HE1 H 6.63 . 1 586 . 72 PRO C C 174.85 . 1 587 . 72 PRO CA C 62.14 . 1 588 . 72 PRO HA H 4.38 . 1 589 . 72 PRO CB C 30.02 . 1 590 . 72 PRO HB2 H 2.30 . 1 591 . 72 PRO HB3 H 1.93 . 1 592 . 72 PRO HG2 H 2.28 . 1 593 . 72 PRO HG3 H 1.99 . 1 594 . 72 PRO HD2 H 3.44 . 1 595 . 73 ASN N N 113.69 . 1 596 . 73 ASN C C 172.07 . 1 597 . 73 ASN CA C 51.49 . 1 598 . 73 ASN HA H 4.90 . 1 599 . 73 ASN CB C 38.43 . 1 600 . 73 ASN HB2 H 2.82 . 1 601 . 73 ASN HD21 H 7.87 . 1 602 . 73 ASN HD22 H 7.19 . 1 603 . 73 ASN ND2 N 113.70 . 1 604 . 74 ARG N N 119.83 . 1 605 . 74 ARG CA C 52.36 . 1 606 . 74 ARG HA H 4.51 . 1 607 . 74 ARG CB C 27.74 . 1 608 . 74 ARG HB2 H 1.92 . 1 609 . 74 ARG HB3 H 1.77 . 1 610 . 74 ARG HG2 H 1.60 . 1 611 . 74 ARG HD2 H 3.26 . 1 612 . 75 PRO HA H 4.80 . 1 613 . 75 PRO HB2 H 2.60 . 1 614 . 75 PRO HB3 H 2.13 . 1 615 . 75 PRO HG2 H 1.98 . 1 616 . 75 PRO HD2 H 3.68 . 1 617 . 75 PRO HD3 H 3.40 . 1 618 . 76 PRO C C 173.00 . 1 619 . 76 PRO CA C 59.83 . 1 620 . 76 PRO HA H 4.50 . 1 621 . 76 PRO CB C 29.61 . 1 622 . 76 PRO HB2 H 2.12 . 1 623 . 76 PRO HB3 H 1.46 . 1 624 . 76 PRO HG2 H 1.40 . 1 625 . 76 PRO HG3 H 1.36 . 1 626 . 76 PRO HD2 H 3.26 . 1 627 . 76 PRO HD3 H 2.86 . 1 628 . 77 LYS N N 124.16 . 1 629 . 77 LYS C C 173.55 . 1 630 . 77 LYS CA C 53.80 . 1 631 . 77 LYS HA H 3.75 . 1 632 . 77 LYS CB C 30.29 . 1 633 . 77 LYS HB2 H 1.47 . 1 634 . 77 LYS HB3 H 0.73 . 1 635 . 77 LYS HG2 H 0.26 . 1 636 . 77 LYS HG3 H -0.06 . 1 637 . 77 LYS HD2 H 1.19 . 1 638 . 77 LYS HD3 H 1.14 . 1 639 . 77 LYS HE2 H 2.56 . 1 640 . 77 LYS HE3 H 2.50 . 1 641 . 78 VAL N N 126.51 . 1 642 . 78 VAL C C 172.79 . 1 643 . 78 VAL CA C 62.01 . 1 644 . 78 VAL HA H 4.03 . 1 645 . 78 VAL CB C 30.62 . 1 646 . 78 VAL HB H 1.80 . 1 647 . 78 VAL HG1 H 0.56 . 1 648 . 78 VAL HG2 H 0.35 . 1 649 . 78 VAL CG1 C 21.07 . 1 650 . 78 VAL CG2 C 21.56 . 1 651 . 79 ASN N N 125.65 . 1 652 . 79 ASN C C 175.25 . 1 653 . 79 ASN CA C 51.78 . 1 654 . 79 ASN HA H 4.90 . 1 655 . 79 ASN CB C 37.46 . 1 656 . 79 ASN HB2 H 2.86 . 1 657 . 79 ASN HB3 H 2.56 . 1 658 . 79 ASN HD21 H 7.50 . 1 659 . 79 ASN HD22 H 6.99 . 1 660 . 79 ASN ND2 N 108.94 . 1 661 . 80 SER N N 113.69 . 1 662 . 80 SER C C 169.58 . 1 663 . 80 SER CA C 55.99 . 1 664 . 80 SER HA H 5.13 . 1 665 . 80 SER CB C 62.69 . 1 666 . 80 SER HB2 H 3.87 . 1 667 . 80 SER HB3 H 3.77 . 1 668 . 81 ILE N N 115.99 . 1 669 . 81 ILE C C 171.01 . 1 670 . 81 ILE CA C 57.61 . 1 671 . 81 ILE HA H 4.95 . 1 672 . 81 ILE CB C 40.32 . 1 673 . 81 ILE HB H 1.38 . 1 674 . 81 ILE HG12 H 1.14 . 1 675 . 81 ILE HG13 H 0.49 . 1 676 . 81 ILE HG2 H 0.31 . 1 677 . 81 ILE HD1 H -0.34 . 1 678 . 82 GLU N N 122.86 . 1 679 . 82 GLU C C 172.42 . 1 680 . 82 GLU CA C 52.09 . 1 681 . 82 GLU HA H 5.40 . 1 682 . 82 GLU CB C 32.12 . 1 683 . 82 GLU HB2 H 2.26 . 1 684 . 82 GLU HB3 H 1.85 . 1 685 . 82 GLU HG2 H 1.92 . 1 686 . 83 ILE N N 126.33 . 1 687 . 83 ILE C C 174.85 . 1 688 . 83 ILE CA C 59.29 . 1 689 . 83 ILE HA H 4.63 . 1 690 . 83 ILE CB C 36.00 . 1 691 . 83 ILE HB H 2.03 . 1 692 . 83 ILE HG12 H 1.57 . 1 693 . 83 ILE HG2 H 1.01 . 1 694 . 83 ILE HD1 H 0.76 . 1 695 . 84 LEU N N 135.64 . 1 696 . 84 LEU CA C 54.80 . 1 697 . 84 LEU HA H 4.15 . 1 698 . 84 LEU CB C 41.16 . 1 699 . 84 LEU HB2 H 1.62 . 1 700 . 84 LEU HB3 H 1.58 . 1 701 . 84 LEU HG H 1.48 . 1 702 . 84 LEU HD1 H 0.75 . 1 703 . 84 LEU CD1 C 22.98 . 1 704 . 84 LEU CD2 C 20.25 . 1 stop_ save_