data_15753 ####################### # 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 15753 _BMRB_flat_file_name bmr15753.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" 276 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 15752 'ILTat1.24 C2' 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 C1 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 46 _Mol_residue_sequence ; GKSPEAECNKITEEPKCSEE KICSWHKEVKAGEKNCQFNS TKASKS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 382 GLY 2 383 LYS 3 384 SER 4 385 PRO 5 386 GLU 6 387 ALA 7 388 GLU 8 389 CYS 9 390 ASN 10 391 LYS 11 392 ILE 12 393 THR 13 394 GLU 14 395 GLU 15 396 PRO 16 397 LYS 17 398 CYS 18 399 SER 19 400 GLU 20 401 GLU 21 402 LYS 22 403 ILE 23 404 CYS 24 405 SER 25 406 TRP 26 407 HIS 27 408 LYS 28 409 GLU 29 410 VAL 30 411 LYS 31 412 ALA 32 413 GLY 33 414 GLU 34 415 LYS 35 416 ASN 36 417 CYS 37 418 GLN 38 419 PHE 39 420 ASN 40 421 SER 41 422 THR 42 423 LYS 43 424 ALA 44 425 SER 45 426 LYS 46 427 SER 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 2JWG "Structure Of A Glycosylphosphatidylinositol-Anchored Domain From A Trypanosome Variant Surface Glycoprotein" 100.00 46 100.00 100.00 7.39e-22 EMBL CAA40086 "variant surface glycoprotein ILTat 1.24 [Trypanosoma brucei]" 100.00 514 100.00 100.00 8.57e-22 GB AGH61239 "variant surface glycoprotein 785 [Trypanosoma brucei]" 93.48 551 100.00 100.00 4.78e-20 SP P26329 "RecName: Full=Variant surface glycoprotein ILTAT 1.24; Short=VSG; Flags: Precursor" 100.00 514 100.00 100.00 8.57e-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 . 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 800 _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 1 383 2 LYS HA H 4.311 0.0 . 2 383 2 LYS HB2 H 1.757387 0.0 . 3 383 2 LYS HB3 H 1.661 0.0 . 4 383 2 LYS HD2 H 1.590968 0.0 . 5 383 2 LYS HD3 H 1.590968 0.0 . 6 383 2 LYS HE2 H 2.909 0.0 . 7 383 2 LYS HE3 H 2.909 0.0 . 8 383 2 LYS HG2 H 1.362 0.0 . 9 383 2 LYS HG3 H 1.362 0.0 . 10 384 3 SER H H 8.487 0.0 . 11 384 3 SER HA H 4.723366 0.0 . 12 385 4 PRO HA H 4.165 0.0 . 13 385 4 PRO HB2 H 1.935 0.0 . 14 385 4 PRO HB3 H 1.207 0.0 . 15 385 4 PRO HD2 H 3.61 0.0 . 16 385 4 PRO HD3 H 3.556 0.0 . 17 385 4 PRO HG2 H 1.633 0.0 . 18 385 4 PRO HG3 H 1.535 0.0 . 19 386 5 GLU H H 8.077374 0.0 . 20 386 5 GLU HA H 3.987 0.0 . 21 386 5 GLU HB2 H 1.917522 0.0 . 22 386 5 GLU HB3 H 1.814499 0.0 . 23 386 5 GLU HG2 H 2.29 0.0 . 24 386 5 GLU HG3 H 2.155542 0.0 . 25 387 6 ALA H H 7.642 0.0 . 26 387 6 ALA HA H 3.988 0.0 . 27 387 6 ALA HB H 1.382 0.0 . 28 388 7 GLU H H 8.004 0.0 . 29 388 7 GLU HA H 4.091 0.0 . 30 388 7 GLU HB2 H 2.018825 0.0 . 31 388 7 GLU HB3 H 2.018825 0.0 . 32 388 7 GLU HG2 H 2.228983 0.0 . 33 388 7 GLU HG3 H 2.228983 0.0 . 34 389 8 CYS H H 7.809 0.0 . 35 389 8 CYS HA H 4.357 0.0 . 36 389 8 CYS HB2 H 2.773 0.0 . 37 389 8 CYS HB3 H 2.386 0.0 . 38 390 9 ASN H H 8.314 0.0 . 39 390 9 ASN HA H 4.618 0.0 . 40 390 9 ASN HB2 H 2.803 0.0 . 41 390 9 ASN HB3 H 2.672 0.0 . 42 390 9 ASN HD21 H 7.639 0.0 . 43 390 9 ASN HD22 H 8.099 0.0 . 44 391 10 LYS H H 7.248 0.0 . 45 391 10 LYS HA H 4.11 0.0 . 46 391 10 LYS HB2 H 1.935 0.0 . 47 391 10 LYS HB3 H 1.857 0.0 . 48 391 10 LYS HD2 H 1.655 0.0 . 49 391 10 LYS HD3 H 1.655 0.0 . 50 391 10 LYS HE2 H 2.883633 0.0 . 51 391 10 LYS HE3 H 2.883633 0.0 . 52 391 10 LYS HG2 H 1.538 0.0 . 53 391 10 LYS HG3 H 1.484 0.0 . 54 392 11 ILE H H 7.776 0.0 . 55 392 11 ILE HA H 4.045 0.0 . 56 392 11 ILE HB H 2.518 0.0 . 57 392 11 ILE HD1 H 1.841 0.0 . 58 392 11 ILE HG12 H 1.034 0.0 . 59 392 11 ILE HG13 H 0.932 0.0 . 60 392 11 ILE HG2 H 0.999 0.0 . 61 393 12 THR H H 8.578 0.0 . 62 393 12 THR HA H 4.655 0.0 . 63 393 12 THR HB H 4.690211 0.0 . 64 393 12 THR HG2 H 1.219 0.0 . 65 394 13 GLU H H 7.056443 0.0 . 66 394 13 GLU HA H 4.494 0.0 . 67 394 13 GLU HB2 H 1.939034 0.0 . 68 394 13 GLU HB3 H 1.743 0.0 . 69 394 13 GLU HG2 H 2.16 0.0 . 70 394 13 GLU HG3 H 2.16 0.0 . 71 395 14 GLU H H 8.237 0.0 . 72 395 14 GLU HA H 2.582 0.0 . 73 395 14 GLU HB2 H 1.333 0.0 . 74 395 14 GLU HB3 H -0.269 0.0 . 75 395 14 GLU HG2 H 1.274 0.0 . 76 395 14 GLU HG3 H 1.274 0.0 . 77 396 15 PRO HA H 3.987 0.0 . 78 396 15 PRO HB2 H 2.141 0.0 . 79 396 15 PRO HB3 H 1.699 0.0 . 80 396 15 PRO HD2 H 3.437 0.0 . 81 396 15 PRO HD3 H 3.386 0.0 . 82 396 15 PRO HG2 H 1.866 0.0 . 83 396 15 PRO HG3 H 1.784 0.0 . 84 397 16 LYS H H 6.354903 0.0 . 85 397 16 LYS HA H 4.02 0.0 . 86 397 16 LYS HB2 H 1.745 0.0 . 87 397 16 LYS HD2 H 1.636394 0.0 . 88 397 16 LYS HD3 H 1.636394 0.0 . 89 397 16 LYS HE2 H 2.914 0.0 . 90 397 16 LYS HE3 H 2.914 0.0 . 91 397 16 LYS HG2 H 1.455 0.0 . 92 397 16 LYS HG3 H 1.377 0.0 . 93 398 17 CYS H H 7.834466 0.0 . 94 398 17 CYS HA H 4.106006 0.0 . 95 398 17 CYS HB2 H 3.463 0.0 . 96 398 17 CYS HB3 H 2.993 0.0 . 97 399 18 SER H H 8.361 0.0 . 98 399 18 SER HA H 4.09 0.0 . 99 399 18 SER HB2 H 3.837978 0.0 . 100 399 18 SER HB3 H 3.837978 0.0 . 101 400 19 GLU H H 7.37 0.0 . 102 400 19 GLU HA H 4.016 0.0 . 103 400 19 GLU HB2 H 2.022 0.0 . 104 400 19 GLU HB3 H 2.022 0.0 . 105 400 19 GLU HG2 H 2.339 0.0 . 106 400 19 GLU HG3 H 2.272 0.0 . 107 401 20 GLU H H 7.303 0.0 . 108 401 20 GLU HA H 4.25 0.0 . 109 401 20 GLU HB2 H 2.044 0.0 . 110 401 20 GLU HB3 H 1.985 0.0 . 111 401 20 GLU HG2 H 2.436 0.0 . 112 401 20 GLU HG3 H 2.237 0.0 . 113 402 21 LYS H H 8.526 0.0 . 114 402 21 LYS HA H 4.086 0.0 . 115 402 21 LYS HB2 H 1.897 0.0 . 116 402 21 LYS HB3 H 1.897 0.0 . 117 402 21 LYS HD2 H 1.698 0.0 . 118 402 21 LYS HD3 H 1.698 0.0 . 119 402 21 LYS HE2 H 3.008 0.0 . 120 402 21 LYS HE3 H 3.008 0.0 . 121 402 21 LYS HG2 H 1.56 0.0 . 122 402 21 LYS HG3 H 1.503 0.0 . 123 403 22 ILE H H 7.324 0.0 . 124 403 22 ILE HA H 4.558 0.0 . 125 403 22 ILE HB H 2.463 0.0 . 126 403 22 ILE HD1 H 1.564 0.0 . 127 403 22 ILE HG2 H 1.323 0.0 . 128 404 23 CYS H H 7.211 0.0 . 129 404 23 CYS HA H 5.728 0.0 . 130 404 23 CYS HB2 H 3.359 0.0 . 131 404 23 CYS HB3 H 2.946 0.0 . 132 405 24 SER H H 9.201 0.0 . 133 405 24 SER HA H 4.628 0.0 . 134 405 24 SER HB2 H 3.745 0.0 . 135 405 24 SER HB3 H 3.686 0.0 . 136 406 25 TRP H H 9.257 0.0 . 137 406 25 TRP HA H 4.971 0.0 . 138 406 25 TRP HB2 H 3.16 0.0 . 139 406 25 TRP HB3 H 2.708 0.0 . 140 406 25 TRP HD1 H 6.817 0.0 . 141 406 25 TRP HE1 H 10.345 0.0 . 142 406 25 TRP HE3 H 7.444 0.0 . 143 406 25 TRP HH2 H 6.700042 0.0 . 144 406 25 TRP HZ2 H 7.419 0.0 . 145 406 25 TRP HZ3 H 7.051789 0.0 . 146 407 26 HIS H H 8.951 0.0 . 147 407 26 HIS HA H 4.456 0.0 . 148 407 26 HIS HB2 H 2.837 0.0 . 149 407 26 HIS HB3 H 2.742 0.0 . 150 407 26 HIS HD2 H 7.415 0.0 . 151 407 26 HIS HE1 H 6.611 0.0 . 152 408 27 LYS H H 8.673 0.0 . 153 408 27 LYS HA H 3.916 0.0 . 154 408 27 LYS HB2 H 1.883 0.0 . 155 408 27 LYS HB3 H 1.883 0.0 . 156 408 27 LYS HD2 H 1.758 0.0 . 157 408 27 LYS HD3 H 1.758 0.0 . 158 408 27 LYS HE2 H 3.045 0.0 . 159 408 27 LYS HE3 H 3.045 0.0 . 160 408 27 LYS HG2 H 1.619 0.0 . 161 408 27 LYS HG3 H 1.543 0.0 . 162 409 28 GLU H H 8.116 0.0 . 163 409 28 GLU HA H 4.506 0.0 . 164 409 28 GLU HB2 H 1.881 0.0 . 165 409 28 GLU HB3 H 1.838 0.0 . 166 409 28 GLU HG2 H 2.110892 0.0 . 167 409 28 GLU HG3 H 2.110892 0.0 . 168 410 29 VAL H H 7.897 0.0 . 169 410 29 VAL HA H 4.415 0.0 . 170 410 29 VAL HB H 2.109 0.0 . 171 410 29 VAL HG1 H 0.427 0.0 . 172 410 29 VAL HG2 H 0.427 0.0 . 173 411 30 LYS H H 8.377 0.0 . 174 411 30 LYS HA H 4.259 0.0 . 175 411 30 LYS HB2 H 1.791 0.0 . 176 411 30 LYS HB3 H 1.498 0.0 . 177 411 30 LYS HD2 H 1.584 0.0 . 178 411 30 LYS HD3 H 1.584 0.0 . 179 411 30 LYS HE2 H 2.92 0.0 . 180 411 30 LYS HE3 H 2.92 0.0 . 181 411 30 LYS HG2 H 1.379674 0.0 . 182 411 30 LYS HG3 H 1.379674 0.0 . 183 412 31 ALA H H 8.255 0.0 . 184 412 31 ALA HA H 4.041 0.0 . 185 412 31 ALA HB H 1.297 0.0 . 186 413 32 GLY H H 8.584894 0.0 . 187 413 32 GLY HA2 H 4.126215 0.0 . 188 413 32 GLY HA3 H 3.584078 0.0 . 189 414 33 GLU H H 7.889508 0.0 . 190 414 33 GLU HA H 4.316 0.0 . 191 414 33 GLU HB2 H 1.965 0.0 . 192 414 33 GLU HB3 H 1.789342 0.0 . 193 414 33 GLU HG2 H 2.058 0.0 . 194 414 33 GLU HG3 H 2.058 0.0 . 195 415 34 LYS H H 8.379 0.0 . 196 415 34 LYS HA H 4.381 0.0 . 197 415 34 LYS HB2 H 1.548 0.0 . 198 415 34 LYS HB3 H 1.548 0.0 . 199 415 34 LYS HD2 H 1.86 0.0 . 200 415 34 LYS HD3 H 1.86 0.0 . 201 415 34 LYS HE2 H 2.871 0.0 . 202 415 34 LYS HE3 H 2.871 0.0 . 203 415 34 LYS HG2 H 1.39 0.0 . 204 415 34 LYS HG3 H 1.39 0.0 . 205 416 35 ASN H H 7.723 0.0 . 206 416 35 ASN HA H 3.810584 0.0 . 207 416 35 ASN HB2 H 0.738 0.0 . 208 416 35 ASN HB3 H 0.425 0.0 . 209 416 35 ASN HD21 H 6.92 0.0 . 210 416 35 ASN HD22 H 7.63 0.0 . 211 417 36 CYS H H 8.238 0.0 . 212 417 36 CYS HA H 5.087 0.0 . 213 417 36 CYS HB2 H 3.976 0.0 . 214 417 36 CYS HB3 H 2.952 0.0 . 215 418 37 GLN H H 8.638 0.0 . 216 418 37 GLN HA H 4.564 0.0 . 217 418 37 GLN HB2 H 2.008 0.0 . 218 418 37 GLN HB3 H 1.408516 0.0 . 219 418 37 GLN HE21 H 7.036 0.0 . 220 418 37 GLN HE22 H 8.296 0.0 . 221 418 37 GLN HG2 H 2.247 0.0 . 222 418 37 GLN HG3 H 2.12 0.0 . 223 419 38 PHE H H 9.014 0.0 . 224 419 38 PHE HA H 5.193 0.0 . 225 419 38 PHE HB2 H 2.983 0.0 . 226 419 38 PHE HB3 H 2.882 0.0 . 227 419 38 PHE HD1 H 7.329 0.0 . 228 419 38 PHE HD2 H 7.329 0.0 . 229 419 38 PHE HE1 H 7.299339 0.0 . 230 419 38 PHE HE2 H 7.299339 0.0 . 231 419 38 PHE HZ H 7.296885 0.0 . 232 420 39 ASN H H 8.451 0.0 . 233 420 39 ASN HA H 4.623 0.0 . 234 420 39 ASN HB2 H 2.580427 0.0 . 235 420 39 ASN HB3 H 2.49 0.0 . 236 420 39 ASN HD21 H 6.762 0.0 . 237 420 39 ASN HD22 H 7.638 0.0 . 238 421 40 SER H H 8.005003 0.0 . 239 421 40 SER HA H 3.893 0.0 . 240 421 40 SER HB2 H 3.723458 0.0 . 241 421 40 SER HB3 H 3.723458 0.0 . 242 422 41 THR H H 7.952 0.0 . 243 422 41 THR HA H 4.182 0.0 . 244 422 41 THR HB H 4.204 0.0 . 245 422 41 THR HG2 H 1.144 0.0 . 246 423 42 LYS H H 7.815 0.0 . 247 423 42 LYS HA H 4.084 0.0 . 248 423 42 LYS HB2 H 1.768421 0.0 . 249 423 42 LYS HB3 H 1.622 0.0 . 250 423 42 LYS HD2 H 1.518329 0.0 . 251 423 42 LYS HD3 H 1.518329 0.0 . 252 423 42 LYS HE2 H 2.94 0.0 . 253 423 42 LYS HE3 H 2.94 0.0 . 254 423 42 LYS HG2 H 1.356 0.0 . 255 423 42 LYS HG3 H 1.356 0.0 . 256 424 43 ALA H H 8.182 0.0 . 257 424 43 ALA HA H 4.238 0.0 . 258 424 43 ALA HB H 1.402 0.0 . 259 425 44 SER H H 7.993 0.0 . 260 425 44 SER HA H 4.394 0.0 . 261 425 44 SER HB2 H 3.884 0.0 . 262 425 44 SER HB3 H 3.884 0.0 . 263 426 45 LYS H H 8.077 0.0 . 264 426 45 LYS HA H 4.37 0.0 . 265 426 45 LYS HB2 H 1.880706 0.0 . 266 426 45 LYS HB3 H 1.759195 0.0 . 267 426 45 LYS HD2 H 1.643 0.0 . 268 426 45 LYS HD3 H 1.643 0.0 . 269 426 45 LYS HE2 H 2.942 0.0 . 270 426 45 LYS HE3 H 2.942 0.0 . 271 426 45 LYS HG2 H 1.43886 0.0 . 272 426 45 LYS HG3 H 1.43886 0.0 . 273 427 46 SER H H 7.924 0.0 . 274 427 46 SER HA H 4.228 0.0 . 275 427 46 SER HB2 H 3.806 0.0 . 276 427 46 SER HB3 H 3.806 0.0 . stop_ save_