data_15752 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface Glycoprotein ; _BMRB_accession_number 15752 _BMRB_flat_file_name bmr15752.str _Entry_type original _Submission_date 2008-05-05 _Accession_date 2008-05-05 _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 Jones Nicola G. . 2 Nietlispach Daniel . . 3 Sharma Reuben . . 4 Burke David F. . 5 Eyres Isobel . . 6 Mues Marsilius . . 7 Mott Helen R. . 8 Carrington Mark . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 252 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 15753 'ILTat1.24 C1' stop_ _Original_release_date 2008-11-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18003615 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jones Nicola G. . 2 Nietlispach Daniel . . 3 Sharma Reuben . . 4 Burke David F. . 5 Eyres Isobel . . 6 Mues Marsilius . . 7 Mott Helen R. . 8 Carrington Mark . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 283 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3584 _Page_last 3593 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ILTat1.24 C2 domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $Variant_Surface_Glycoprotein_ILTat1.24 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Variant_Surface_Glycoprotein_ILTat1.24 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Variant_Surface_Glycoprotein_ILTat1.24 _Molecular_mass 5141.820 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 48 _Mol_residue_sequence ; GTKASKSGVPVTQTQTAGAD TTAEKCKGKGEKDCKSPDCK WEGGTCKD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 421 GLY 2 422 THR 3 423 LYS 4 424 ALA 5 425 SER 6 426 LYS 7 427 SER 8 428 GLY 9 429 VAL 10 430 PRO 11 431 VAL 12 432 THR 13 433 GLN 14 434 THR 15 435 GLN 16 436 THR 17 437 ALA 18 438 GLY 19 439 ALA 20 440 ASP 21 441 THR 22 442 THR 23 443 ALA 24 444 GLU 25 445 LYS 26 446 CYS 27 447 LYS 28 448 GLY 29 449 LYS 30 450 GLY 31 451 GLU 32 452 LYS 33 453 ASP 34 454 CYS 35 455 LYS 36 456 SER 37 457 PRO 38 458 ASP 39 459 CYS 40 460 LYS 41 461 TRP 42 462 GLU 43 463 GLY 44 464 GLY 45 465 THR 46 466 CYS 47 467 LYS 48 468 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 2JWH "Structure Of A Glycosylphosphatidylinositol-Anchored Domain From A Trypanosome Variant Surface Glycoprotein" 100.00 48 100.00 100.00 1.23e-22 EMBL CAA39964 "Variant Surface Glycoprotein [Trypanosoma brucei]" 97.92 510 100.00 100.00 7.85e-22 EMBL CAA40086 "variant surface glycoprotein ILTat 1.24 [Trypanosoma brucei]" 97.92 514 100.00 100.00 3.90e-22 SP P26329 "RecName: Full=Variant surface glycoprotein ILTAT 1.24; Short=VSG; Flags: Precursor" 97.92 514 100.00 100.00 3.90e-22 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Variant_Surface_Glycoprotein_ILTat1.24 'Trypanosoma brucei' 5691 Eukaryota . Trypanosoma brucei 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 $Variant_Surface_Glycoprotein_ILTat1.24 'recombinant technology' . Escherichia coli 'BL21 trxB' pET15b 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 $Variant_Surface_Glycoprotein_ILTat1.24 0.5 mM 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'sodium azide' 0.05 % 'natural abundance' D2O 10 % . H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version . loop_ _Vendor _Address _Electronic_address Boucher . . stop_ loop_ _Task processing stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _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 1 423 3 LYS H H 8.388445 0.0 . 2 423 3 LYS HA H 4.225 0.0 . 3 423 3 LYS HB2 H 1.7319 0.0 . 4 423 3 LYS HB3 H 1.654 0.0 . 5 423 3 LYS HD2 H 1.582225 0.0 . 6 423 3 LYS HD3 H 1.582225 0.0 . 7 423 3 LYS HE2 H 2.899219 0.0 . 8 423 3 LYS HE3 H 2.899219 0.0 . 9 423 3 LYS HG2 H 1.347677 0.0 . 10 423 3 LYS HG3 H 1.347677 0.0 . 11 425 5 SER H H 8.21991 0.0 . 12 425 5 SER HA H 4.336339 0.0 . 13 425 5 SER HB2 H 3.768259 0.0 . 14 425 5 SER HB3 H 3.768259 0.0 . 15 426 6 LYS H H 8.327222 0.0 . 16 426 6 LYS HA H 4.269 0.0 . 17 426 6 LYS HB2 H 1.775753 0.0 . 18 426 6 LYS HB3 H 1.775753 0.0 . 19 426 6 LYS HD2 H 1.653044 0.0 . 20 426 6 LYS HD3 H 1.653044 0.0 . 21 426 6 LYS HE2 H 2.89487 0.0 . 22 426 6 LYS HE3 H 2.89487 0.0 . 23 426 6 LYS HG2 H 1.330447 0.0 . 24 426 6 LYS HG3 H 1.330447 0.0 . 25 427 7 SER H H 8.235 0.0 . 26 427 7 SER HA H 4.342647 0.0 . 27 427 7 SER HB2 H 3.772052 0.0 . 28 427 7 SER HB3 H 3.772052 0.0 . 29 428 8 GLY H H 8.296894 0.0 . 30 428 8 GLY HA2 H 3.857 0.0 . 31 428 8 GLY HA3 H 3.857 0.0 . 32 429 9 VAL H H 7.813 0.0 . 33 429 9 VAL HA H 4.322 0.0 . 34 429 9 VAL HB H 1.955 0.0 . 35 429 9 VAL HG1 H 0.865 0.0 . 36 429 9 VAL HG2 H 0.804 0.0 . 37 430 10 PRO HA H 4.351 0.0 . 38 430 10 PRO HB2 H 2.185 0.0 . 39 430 10 PRO HB3 H 1.758 0.0 . 40 430 10 PRO HD2 H 3.783 0.0 . 41 430 10 PRO HD3 H 3.571 0.0 . 42 430 10 PRO HG2 H 1.919 0.0 . 43 430 10 PRO HG3 H 1.919 0.0 . 44 431 11 VAL H H 8.213 0.0 . 45 431 11 VAL HA H 4.019 0.0 . 46 431 11 VAL HB H 1.974 0.0 . 47 431 11 VAL HG2 H 0.857 0.0 . 48 432 12 THR H H 8.064 0.0 . 49 432 12 THR HA H 4.222106 0.0 . 50 432 12 THR HB H 4.087 0.0 . 51 432 12 THR HG2 H 1.091841 0.0 . 52 433 13 GLN H H 8.337 0.0 . 53 433 13 GLN HA H 4.332642 0.0 . 54 433 13 GLN HB2 H 2.006 0.0 . 55 433 13 GLN HB3 H 1.89192 0.0 . 56 433 13 GLN HE21 H 7.425764 0.0 . 57 433 13 GLN HE22 H 6.755024 0.0 . 58 433 13 GLN HG2 H 2.263255 0.0 . 59 433 13 GLN HG3 H 2.263255 0.0 . 60 434 14 THR H H 8.134 0.0 . 61 434 14 THR HA H 4.198 0.0 . 62 434 14 THR HB H 4.09 0.0 . 63 434 14 THR HG2 H 1.08 0.0 . 64 435 15 GLN H H 8.373 0.0 . 65 435 15 GLN HA H 4.332 0.0 . 66 435 15 GLN HB2 H 2.004 0.0 . 67 435 15 GLN HB3 H 1.921 0.0 . 68 435 15 GLN HE21 H 7.424142 0.0 . 69 435 15 GLN HE22 H 6.752135 0.0 . 70 435 15 GLN HG2 H 2.269866 0.0 . 71 435 15 GLN HG3 H 2.269866 0.0 . 72 436 16 THR H H 8.127364 0.0 . 73 436 16 THR HA H 4.206944 0.0 . 74 436 16 THR HB H 4.096 0.0 . 75 436 16 THR HG2 H 1.082 0.0 . 76 437 17 ALA H H 8.306 0.0 . 77 437 17 ALA HA H 4.239218 0.0 . 78 437 17 ALA HB H 1.296 0.0 . 79 438 18 GLY H H 8.284767 0.0 . 80 438 18 GLY HA2 H 3.839 0.0 . 81 438 18 GLY HA3 H 3.839 0.0 . 82 439 19 ALA H H 8.056 0.0 . 83 439 19 ALA HA H 4.227223 0.0 . 84 439 19 ALA HB H 1.272 0.0 . 85 440 20 ASP H H 8.325 0.0 . 86 440 20 ASP HA H 4.56707 0.0 . 87 440 20 ASP HB2 H 2.629 0.0 . 88 440 20 ASP HB3 H 2.557 0.0 . 89 441 21 THR H H 8.067 0.0 . 90 441 21 THR HA H 4.3 0.0 . 91 441 21 THR HB H 4.234752 0.0 . 92 441 21 THR HG2 H 1.101 0.0 . 93 442 22 THR H H 8.130549 0.0 . 94 442 22 THR HA H 4.176358 0.0 . 95 442 22 THR HB H 4.115011 0.0 . 96 442 22 THR HG2 H 1.124 0.0 . 97 443 23 ALA H H 8.147 0.0 . 98 443 23 ALA HA H 4.179 0.0 . 99 443 23 ALA HB H 1.282 0.0 . 100 444 24 GLU H H 8.193 0.0 . 101 444 24 GLU HA H 4.206 0.0 . 102 444 24 GLU HB2 H 1.974 0.0 . 103 444 24 GLU HB3 H 1.857 0.0 . 104 444 24 GLU HG2 H 2.196 0.0 . 105 444 24 GLU HG3 H 2.196 0.0 . 106 445 25 LYS H H 8.525 0.0 . 107 445 25 LYS HA H 4.088 0.0 . 108 445 25 LYS HB2 H 1.792 0.0 . 109 445 25 LYS HB3 H 1.792 0.0 . 110 445 25 LYS HD2 H 1.586 0.0 . 111 445 25 LYS HD3 H 1.586 0.0 . 112 445 25 LYS HE2 H 2.908164 0.0 . 113 445 25 LYS HE3 H 2.908164 0.0 . 114 445 25 LYS HG2 H 1.433 0.0 . 115 445 25 LYS HG3 H 1.368 0.0 . 116 446 26 CYS H H 8.624 0.0 . 117 446 26 CYS HA H 4.56 0.0 . 118 446 26 CYS HB2 H 2.939 0.0 . 119 446 26 CYS HB3 H 2.413 0.0 . 120 447 27 LYS H H 7.925 0.0 . 121 447 27 LYS HA H 4.019 0.0 . 122 447 27 LYS HB2 H 1.63 0.0 . 123 447 27 LYS HB3 H 1.586 0.0 . 124 447 27 LYS HD2 H 1.45 0.0 . 125 447 27 LYS HD3 H 1.45 0.0 . 126 447 27 LYS HE2 H 2.896 0.0 . 127 447 27 LYS HE3 H 2.896 0.0 . 128 447 27 LYS HG2 H 1.309 0.0 . 129 447 27 LYS HG3 H 1.309 0.0 . 130 448 28 GLY H H 8.873 0.0 . 131 448 28 GLY HA2 H 4.094 0.0 . 132 448 28 GLY HA3 H 3.665 0.0 . 133 449 29 LYS H H 7.462 0.0 . 134 449 29 LYS HA H 4.22 0.0 . 135 449 29 LYS HB2 H 2.121 0.0 . 136 449 29 LYS HB3 H 2.121 0.0 . 137 449 29 LYS HD2 H 1.453 0.0 . 138 449 29 LYS HD3 H 1.225 0.0 . 139 449 29 LYS HE2 H 2.942 0.0 . 140 449 29 LYS HE3 H 1.686 0.0 . 141 449 29 LYS HG2 H 1.542 0.0 . 142 449 29 LYS HG3 H 1.542 0.0 . 143 450 30 GLY H H 8.669 0.0 . 144 450 30 GLY HA2 H 4.212 0.0 . 145 450 30 GLY HA3 H 3.563 0.0 . 146 451 31 GLU H H 7.724 0.0 . 147 451 31 GLU HA H 1.968 0.0 . 148 451 31 GLU HB2 H 1.018 0.0 . 149 451 31 GLU HB3 H 0.556 0.0 . 150 451 31 GLU HG2 H 1.191 0.0 . 151 451 31 GLU HG3 H 1.191 0.0 . 152 452 32 LYS H H 8.012 0.0 . 153 452 32 LYS HA H 3.712 0.0 . 154 452 32 LYS HB2 H 1.543 0.0 . 155 452 32 LYS HB3 H 1.543 0.0 . 156 452 32 LYS HD2 H 1.435 0.0 . 157 452 32 LYS HD3 H 1.435 0.0 . 158 452 32 LYS HE2 H 2.810293 0.0 . 159 452 32 LYS HE3 H 2.810293 0.0 . 160 452 32 LYS HG2 H 1.192 0.0 . 161 452 32 LYS HG3 H 1.127 0.0 . 162 453 33 ASP H H 7.057 0.0 . 163 453 33 ASP HA H 4.67767 0.0 . 164 453 33 ASP HB2 H 2.745 0.0 . 165 453 33 ASP HB3 H 2.252 0.0 . 166 454 34 CYS H H 7.329 0.0 . 167 454 34 CYS HA H 4.35 0.0 . 168 454 34 CYS HB2 H 3.218 0.0 . 169 454 34 CYS HB3 H 2.563 0.0 . 170 455 35 LYS H H 7.892 0.0 . 171 455 35 LYS HA H 4.457 0.0 . 172 455 35 LYS HB2 H 1.772 0.0 . 173 455 35 LYS HB3 H 1.772 0.0 . 174 455 35 LYS HD2 H 1.63 0.0 . 175 455 35 LYS HD3 H 1.63 0.0 . 176 455 35 LYS HE2 H 2.924427 0.0 . 177 455 35 LYS HE3 H 2.924427 0.0 . 178 455 35 LYS HG2 H 1.211 0.0 . 179 455 35 LYS HG3 H 1.211 0.0 . 180 456 36 SER H H 8.47 0.0 . 181 456 36 SER HA H 4.624 0.0 . 182 456 36 SER HB2 H 3.879 0.0 . 183 456 36 SER HB3 H 3.879 0.0 . 184 457 37 PRO HA H 4.723 0.0 . 185 457 37 PRO HB2 H 2.153 0.0 . 186 457 37 PRO HB3 H 2.153 0.0 . 187 457 37 PRO HD2 H 3.573 0.0 . 188 457 37 PRO HD3 H 3.42 0.0 . 189 457 37 PRO HG2 H 1.878 0.0 . 190 457 37 PRO HG3 H 1.696 0.0 . 191 458 38 ASP H H 8.115 0.0 . 192 458 38 ASP HA H 4.23 0.0 . 193 458 38 ASP HB2 H 2.676 0.0 . 194 458 38 ASP HB3 H 2.585 0.0 . 195 459 39 CYS H H 7.993 0.0 . 196 459 39 CYS HA H 5.259 0.0 . 197 459 39 CYS HB2 H 3.203 0.0 . 198 459 39 CYS HB3 H 2.317 0.0 . 199 460 40 LYS H H 9.018 0.0 . 200 460 40 LYS HA H 4.441 0.0 . 201 460 40 LYS HB2 H 1.57 0.0 . 202 460 40 LYS HB3 H 1.57 0.0 . 203 460 40 LYS HD2 H 1.49 0.0 . 204 460 40 LYS HD3 H 1.49 0.0 . 205 460 40 LYS HE2 H 2.76808 0.0 . 206 460 40 LYS HE3 H 2.76808 0.0 . 207 460 40 LYS HG2 H 1.188 0.0 . 208 460 40 LYS HG3 H 1.188 0.0 . 209 461 41 TRP H H 8.511 0.0 . 210 461 41 TRP HA H 5.205 0.0 . 211 461 41 TRP HB2 H 3.245 0.0 . 212 461 41 TRP HB3 H 2.814 0.0 . 213 461 41 TRP HD1 H 6.994 0.0 . 214 461 41 TRP HE1 H 9.737 0.0 . 215 461 41 TRP HE3 H 7.337 0.0 . 216 461 41 TRP HH2 H 7.01 0.0 . 217 461 41 TRP HZ2 H 7.234 0.0 . 218 461 41 TRP HZ3 H 7.107 0.0 . 219 462 42 GLU H H 8.31 0.0 . 220 462 42 GLU HA H 4.308 0.0 . 221 462 42 GLU HB2 H 1.601 0.0 . 222 462 42 GLU HB3 H 1.601 0.0 . 223 462 42 GLU HG2 H 1.959 0.0 . 224 462 42 GLU HG3 H 1.868702 0.0 . 225 463 43 GLY H H 8.73 0.0 . 226 463 43 GLY HA2 H 3.569 0.0 . 227 463 43 GLY HA3 H 3.569 0.0 . 228 464 44 GLY H H 7.73 0.0 . 229 464 44 GLY HA2 H 3.713 0.0 . 230 464 44 GLY HA3 H 3.139 0.0 . 231 465 45 THR H H 6.343 0.0 . 232 465 45 THR HA H 3.821 0.0 . 233 465 45 THR HB H 3.633 0.0 . 234 465 45 THR HG2 H 0.863 0.0 . 235 466 46 CYS H H 8.406 0.0 . 236 466 46 CYS HA H 5.281 0.0 . 237 466 46 CYS HB2 H 3.44 0.0 . 238 466 46 CYS HB3 H 3.08 0.0 . 239 467 47 LYS H H 9.363 0.0 . 240 467 47 LYS HA H 4.547 0.0 . 241 467 47 LYS HB2 H 1.816 0.0 . 242 467 47 LYS HB3 H 1.697 0.0 . 243 467 47 LYS HD2 H 1.484 0.0 . 244 467 47 LYS HD3 H 1.484 0.0 . 245 467 47 LYS HE2 H 2.745 0.0 . 246 467 47 LYS HE3 H 2.745 0.0 . 247 467 47 LYS HG2 H 1.335 0.0 . 248 467 47 LYS HG3 H 1.23 0.0 . 249 468 48 ASP H H 7.69 0.0 . 250 468 48 ASP HA H 4.626 0.0 . 251 468 48 ASP HB2 H 2.579 0.0 . 252 468 48 ASP HB3 H 2.446 0.0 . stop_ save_