data_25481 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N chemical shift assignment for perforin C2 quad mutant ; _BMRB_accession_number 25481 _BMRB_flat_file_name bmr25481.str _Entry_type original _Submission_date 2015-02-09 _Accession_date 2015-02-09 _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 Yagi Hiromasa . . 2 Conroy Paul J. . 3 Leung Eleanor W.W. . 4 Law Ruby H. . 5 Whisstock James C. . 6 Norton Raymond S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 "13C chemical shifts" 211 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-11-02 original BMRB . stop_ _Original_release_date 2016-11-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Basis for Ca2+-mediated Interaction of the Perforin C2 Domain with Lipid Membranes ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26306037 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yagi Hiromasa . . 2 Conroy Paul J. . 3 Leung Eleanor W.W. . 4 Law Ruby H. . 5 Whisstock James C. . 6 Norton Raymond S. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 290 _Journal_issue 42 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 25213 _Page_last 25226 _Year 2015 _Details . loop_ _Keyword 'Ca2+-binding protein' 'Multisite ligand-binding' 'NMR spectroscopy' 'Protein-membrane interaction' 'X-ray crystallography' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'perforin C2 quad mutant' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'perforin C2 quad mutant' $perforin_C2_domain stop_ _System_molecular_weight 14300 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'perforin C2 quad mutant' stop_ loop_ _Biological_function 'membrane binding domain of a perforin' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_perforin_C2_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common perforin_C2_domain _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'immune protein; membrane binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 125 _Mol_residue_sequence ; AQRGLAHLVVSNFRAEHLAG DATTATDAYLKVFFGGQEFR TGVVWNNNNPRWTDKMDFEN VLLSTGGPLRVQVWDADAGA DDDLLGSCDRSPHSGFHEVT CELNHGRVKFSYHAKSLPGH HHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 409 ALA 2 410 GLN 3 411 ARG 4 412 GLY 5 413 LEU 6 414 ALA 7 415 HIS 8 416 LEU 9 417 VAL 10 418 VAL 11 419 SER 12 420 ASN 13 421 PHE 14 422 ARG 15 423 ALA 16 424 GLU 17 425 HIS 18 426 LEU 19 427 ALA 20 428 GLY 21 429 ASP 22 430 ALA 23 431 THR 24 432 THR 25 433 ALA 26 434 THR 27 435 ASP 28 436 ALA 29 437 TYR 30 438 LEU 31 439 LYS 32 440 VAL 33 441 PHE 34 442 PHE 35 443 GLY 36 444 GLY 37 445 GLN 38 446 GLU 39 447 PHE 40 448 ARG 41 449 THR 42 450 GLY 43 451 VAL 44 452 VAL 45 453 TRP 46 454 ASN 47 455 ASN 48 456 ASN 49 457 ASN 50 458 PRO 51 459 ARG 52 460 TRP 53 461 THR 54 462 ASP 55 463 LYS 56 464 MET 57 465 ASP 58 466 PHE 59 467 GLU 60 468 ASN 61 469 VAL 62 470 LEU 63 471 LEU 64 472 SER 65 473 THR 66 474 GLY 67 475 GLY 68 476 PRO 69 477 LEU 70 478 ARG 71 479 VAL 72 480 GLN 73 481 VAL 74 482 TRP 75 483 ASP 76 484 ALA 77 485 ASP 78 486 ALA 79 487 GLY 80 488 ALA 81 489 ASP 82 490 ASP 83 491 ASP 84 492 LEU 85 493 LEU 86 494 GLY 87 495 SER 88 496 CYS 89 497 ASP 90 498 ARG 91 499 SER 92 500 PRO 93 501 HIS 94 502 SER 95 503 GLY 96 504 PHE 97 505 HIS 98 506 GLU 99 507 VAL 100 508 THR 101 509 CYS 102 510 GLU 103 511 LEU 104 512 ASN 105 513 HIS 106 514 GLY 107 515 ARG 108 516 VAL 109 517 LYS 110 518 PHE 111 519 SER 112 520 TYR 113 521 HIS 114 522 ALA 115 523 LYS 116 524 SER 117 525 LEU 118 526 PRO 119 527 GLY 120 528 HIS 121 529 HIS 122 530 HIS 123 531 HIS 124 532 HIS 125 533 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $perforin_C2_domain 'house mouse' 10090 Eukaryota Metazoa Mus musculus 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 $perforin_C2_domain 'recombinant technology' . Escherichia coli Top10F' pComb3X 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 $perforin_C2_domain 0.5 mM '[U-99% 13C; U-99% 15N]' HEPES 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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 'ionic strength' 150 . mM pH 7.0 . 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 'perforin C2 quad mutant' _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 1 411 3 ARG CA C 53.41 0.4 1 2 412 4 GLY H H 8.05 0.02 1 3 412 4 GLY CA C 42.57 0.4 1 4 412 4 GLY N N 109.77 0.4 1 5 413 5 LEU H H 7.98 0.02 1 6 413 5 LEU CA C 50.94 0.4 1 7 413 5 LEU N N 123.71 0.4 1 8 414 6 ALA H H 8.06 0.02 1 9 414 6 ALA CA C 46.88 0.4 1 10 414 6 ALA CB C 20.83 0.4 1 11 414 6 ALA N N 124.40 0.4 1 12 415 7 HIS H H 8.26 0.02 1 13 415 7 HIS CA C 51.96 0.4 1 14 415 7 HIS CB C 29.14 0.4 1 15 415 7 HIS N N 122.78 0.4 1 16 416 8 LEU H H 8.35 0.02 1 17 416 8 LEU CA C 50.16 0.4 1 18 416 8 LEU CB C 40.90 0.4 1 19 416 8 LEU N N 121.76 0.4 1 20 417 9 VAL H H 8.32 0.02 1 21 417 9 VAL CA C 59.25 0.4 1 22 417 9 VAL CB C 31.31 0.4 1 23 417 9 VAL N N 127.19 0.4 1 24 418 10 VAL H H 8.95 0.02 1 25 418 10 VAL CA C 58.26 0.4 1 26 418 10 VAL CB C 30.67 0.4 1 27 418 10 VAL N N 130.16 0.4 1 28 419 11 SER H H 8.63 0.02 1 29 419 11 SER CA C 54.79 0.4 1 30 419 11 SER CB C 62.50 0.4 1 31 419 11 SER N N 120.10 0.4 1 32 420 12 ASN H H 8.17 0.02 1 33 420 12 ASN CA C 50.76 0.4 1 34 420 12 ASN CB C 34.03 0.4 1 35 420 12 ASN N N 115.21 0.4 1 36 421 13 PHE H H 8.43 0.02 1 37 421 13 PHE CA C 55.90 0.4 1 38 421 13 PHE CB C 38.88 0.4 1 39 421 13 PHE N N 117.07 0.4 1 40 422 14 ARG H H 9.38 0.02 1 41 422 14 ARG CA C 53.67 0.4 1 42 422 14 ARG CB C 29.22 0.4 1 43 422 14 ARG N N 122.13 0.4 1 44 423 15 ALA H H 8.96 0.02 1 45 423 15 ALA CA C 47.53 0.4 1 46 423 15 ALA CB C 20.28 0.4 1 47 423 15 ALA N N 122.53 0.4 1 48 424 16 GLU H H 8.31 0.02 1 49 424 16 GLU CA C 50.88 0.4 1 50 424 16 GLU CB C 31.09 0.4 1 51 424 16 GLU N N 115.20 0.4 1 52 425 17 HIS H H 8.19 0.02 1 53 425 17 HIS CA C 53.07 0.4 1 54 425 17 HIS CB C 25.92 0.4 1 55 425 17 HIS N N 116.88 0.4 1 56 426 18 LEU H H 8.12 0.02 1 57 426 18 LEU CA C 52.95 0.4 1 58 426 18 LEU CB C 37.35 0.4 1 59 426 18 LEU N N 114.08 0.4 1 60 427 19 ALA H H 7.39 0.02 1 61 427 19 ALA CA C 48.87 0.4 1 62 427 19 ALA CB C 17.47 0.4 1 63 427 19 ALA N N 117.71 0.4 1 64 428 20 GLY H H 7.62 0.02 1 65 428 20 GLY CA C 42.46 0.4 1 66 428 20 GLY N N 108.16 0.4 1 67 429 21 ASP H H 7.78 0.02 1 68 429 21 ASP CA C 51.24 0.4 1 69 429 21 ASP CB C 38.65 0.4 1 70 429 21 ASP N N 121.00 0.4 1 71 430 22 ALA H H 7.78 0.02 1 72 430 22 ALA CA C 50.16 0.4 1 73 430 22 ALA CB C 16.60 0.4 1 74 430 22 ALA N N 122.20 0.4 1 75 431 23 THR H H 7.82 0.02 1 76 431 23 THR CA C 59.41 0.4 1 77 431 23 THR CB C 66.85 0.4 1 78 431 23 THR N N 109.96 0.4 1 79 432 24 THR H H 7.32 0.02 1 80 432 24 THR CA C 59.14 0.4 1 81 432 24 THR CB C 67.37 0.4 1 82 432 24 THR N N 116.46 0.4 1 83 433 25 ALA H H 7.99 0.02 1 84 433 25 ALA CA C 48.60 0.4 1 85 433 25 ALA CB C 17.02 0.4 1 86 433 25 ALA N N 126.49 0.4 1 87 434 26 THR H H 7.35 0.02 1 88 434 26 THR CA C 60.32 0.4 1 89 434 26 THR CB C 68.03 0.4 1 90 434 26 THR N N 116.49 0.4 1 91 435 27 ASP H H 8.43 0.02 1 92 435 27 ASP CA C 48.91 0.4 1 93 435 27 ASP CB C 39.96 0.4 1 94 435 27 ASP N N 128.25 0.4 1 95 436 28 ALA H H 8.59 0.02 1 96 436 28 ALA CA C 49.68 0.4 1 97 436 28 ALA CB C 18.43 0.4 1 98 436 28 ALA N N 123.38 0.4 1 99 437 29 TYR H H 8.51 0.02 1 100 437 29 TYR CA C 53.27 0.4 1 101 437 29 TYR CB C 38.55 0.4 1 102 437 29 TYR N N 114.49 0.4 1 103 438 30 LEU H H 7.50 0.02 1 104 438 30 LEU CA C 53.70 0.4 1 105 438 30 LEU CB C 38.50 0.4 1 106 438 30 LEU N N 116.21 0.4 1 107 439 31 LYS H H 8.03 0.02 1 108 439 31 LYS CA C 52.91 0.4 1 109 439 31 LYS CB C 27.82 0.4 1 110 439 31 LYS N N 123.60 0.4 1 111 440 32 VAL H H 7.80 0.02 1 112 440 32 VAL CA C 58.03 0.4 1 113 440 32 VAL CB C 31.58 0.4 1 114 440 32 VAL N N 118.66 0.4 1 115 441 33 PHE H H 9.06 0.02 1 116 441 33 PHE CA C 53.75 0.4 1 117 441 33 PHE CB C 39.97 0.4 1 118 441 33 PHE N N 123.79 0.4 1 119 442 34 PHE H H 7.88 0.02 1 120 442 34 PHE CA C 57.53 0.4 1 121 442 34 PHE N N 119.53 0.4 1 122 443 35 GLY H H 7.57 0.02 1 123 443 35 GLY CA C 44.43 0.4 1 124 443 35 GLY N N 116.74 0.4 1 125 444 36 GLY H H 8.38 0.02 1 126 444 36 GLY CA C 42.21 0.4 1 127 444 36 GLY N N 108.46 0.4 1 128 445 37 GLN H H 7.81 0.02 1 129 445 37 GLN CA C 52.27 0.4 1 130 445 37 GLN CB C 29.11 0.4 1 131 445 37 GLN N N 121.03 0.4 1 132 446 38 GLU H H 7.70 0.02 1 133 446 38 GLU CA C 51.60 0.4 1 134 446 38 GLU CB C 30.78 0.4 1 135 446 38 GLU N N 122.78 0.4 1 136 447 39 PHE H H 8.62 0.02 1 137 447 39 PHE CA C 53.44 0.4 1 138 447 39 PHE CB C 39.99 0.4 1 139 447 39 PHE N N 123.37 0.4 1 140 448 40 ARG H H 8.25 0.02 1 141 448 40 ARG CA C 51.14 0.4 1 142 448 40 ARG CB C 31.23 0.4 1 143 448 40 ARG N N 119.07 0.4 1 144 449 41 THR H H 7.91 0.02 1 145 449 41 THR CA C 57.87 0.4 1 146 449 41 THR CB C 69.38 0.4 1 147 449 41 THR N N 113.24 0.4 1 148 450 42 GLY H H 8.49 0.02 1 149 450 42 GLY CA C 41.58 0.4 1 150 450 42 GLY N N 105.49 0.4 1 151 451 43 VAL H H 7.69 0.02 1 152 451 43 VAL CA C 58.93 0.4 1 153 451 43 VAL CB C 29.17 0.4 1 154 451 43 VAL N N 120.81 0.4 1 155 452 44 VAL H H 8.04 0.02 1 156 452 44 VAL CA C 58.92 0.4 1 157 452 44 VAL CB C 27.75 0.4 1 158 452 44 VAL N N 129.20 0.4 1 159 453 45 TRP H H 7.29 0.02 1 160 453 45 TRP CA C 55.06 0.4 1 161 453 45 TRP CB C 26.64 0.4 1 162 453 45 TRP N N 127.85 0.4 1 163 454 46 ASN H H 10.12 0.02 1 164 454 46 ASN CA C 50.82 0.4 1 165 454 46 ASN CB C 34.84 0.4 1 166 454 46 ASN N N 123.91 0.4 1 167 455 47 ASN H H 8.89 0.02 1 168 455 47 ASN CA C 50.54 0.4 1 169 455 47 ASN CB C 38.81 0.4 1 170 455 47 ASN N N 117.81 0.4 1 171 456 48 ASN H H 8.81 0.02 1 172 456 48 ASN CA C 51.14 0.4 1 173 456 48 ASN CB C 36.96 0.4 1 174 456 48 ASN N N 124.48 0.4 1 175 457 49 ASN H H 8.31 0.02 1 176 457 49 ASN CA C 48.41 0.4 1 177 457 49 ASN CB C 37.92 0.4 1 178 457 49 ASN N N 116.76 0.4 1 179 458 50 PRO CA C 60.65 0.4 1 180 458 50 PRO CB C 29.58 0.4 1 181 459 51 ARG H H 6.79 0.02 1 182 459 51 ARG CA C 52.52 0.4 1 183 459 51 ARG CB C 30.33 0.4 1 184 459 51 ARG N N 114.57 0.4 1 185 460 52 TRP H H 7.93 0.02 1 186 460 52 TRP CA C 55.69 0.4 1 187 460 52 TRP CB C 26.54 0.4 1 188 460 52 TRP N N 121.36 0.4 1 189 461 53 THR CA C 59.54 0.4 1 190 461 53 THR CB C 66.65 0.4 1 191 462 54 ASP H H 8.73 0.02 1 192 462 54 ASP CA C 53.03 0.4 1 193 462 54 ASP CB C 39.25 0.4 1 194 462 54 ASP N N 120.59 0.4 1 195 463 55 LYS H H 8.17 0.02 1 196 463 55 LYS CA C 52.90 0.4 1 197 463 55 LYS CB C 31.37 0.4 1 198 463 55 LYS N N 122.20 0.4 1 199 464 56 MET H H 8.78 0.02 1 200 464 56 MET CA C 52.06 0.4 1 201 464 56 MET CB C 31.17 0.4 1 202 464 56 MET N N 124.73 0.4 1 203 465 57 ASP H H 7.65 0.02 1 204 465 57 ASP CA C 50.49 0.4 1 205 465 57 ASP CB C 40.03 0.4 1 206 465 57 ASP N N 123.32 0.4 1 207 466 58 PHE H H 8.81 0.02 1 208 466 58 PHE CA C 50.44 0.4 1 209 466 58 PHE CB C 39.30 0.4 1 210 466 58 PHE N N 123.78 0.4 1 211 467 59 GLU H H 8.76 0.02 1 212 467 59 GLU CA C 50.47 0.4 1 213 467 59 GLU CB C 25.40 0.4 1 214 467 59 GLU N N 123.36 0.4 1 215 468 60 ASN H H 8.08 0.02 1 216 468 60 ASN CA C 53.32 0.4 1 217 468 60 ASN CB C 34.35 0.4 1 218 468 60 ASN N N 117.55 0.4 1 219 469 61 VAL H H 8.30 0.02 1 220 469 61 VAL CA C 58.07 0.4 1 221 469 61 VAL CB C 31.68 0.4 1 222 469 61 VAL N N 123.31 0.4 1 223 470 62 LEU H H 8.27 0.02 1 224 470 62 LEU CA C 50.14 0.4 1 225 470 62 LEU N N 126.59 0.4 1 226 473 65 THR H H 6.74 0.02 1 227 473 65 THR CA C 59.21 0.4 1 228 473 65 THR CB C 67.51 0.4 1 229 473 65 THR N N 108.72 0.4 1 230 474 66 GLY H H 7.58 0.02 1 231 474 66 GLY CA C 42.92 0.4 1 232 474 66 GLY N N 109.36 0.4 1 233 475 67 GLY H H 7.39 0.02 1 234 475 67 GLY CA C 41.63 0.4 1 235 475 67 GLY N N 106.89 0.4 1 236 476 68 PRO CA C 59.77 0.4 1 237 476 68 PRO CB C 31.69 0.4 1 238 477 69 LEU H H 8.35 0.02 1 239 477 69 LEU CA C 52.36 0.4 1 240 477 69 LEU CB C 41.82 0.4 1 241 477 69 LEU N N 120.10 0.4 1 242 478 70 ARG H H 8.69 0.02 1 243 478 70 ARG CA C 51.47 0.4 1 244 478 70 ARG CB C 30.65 0.4 1 245 478 70 ARG N N 131.46 0.4 1 246 479 71 VAL H H 8.55 0.02 1 247 479 71 VAL CA C 58.75 0.4 1 248 479 71 VAL CB C 31.11 0.4 1 249 479 71 VAL N N 125.73 0.4 1 250 480 72 GLN H H 9.03 0.02 1 251 480 72 GLN CA C 50.83 0.4 1 252 480 72 GLN CB C 30.11 0.4 1 253 480 72 GLN N N 123.02 0.4 1 254 481 73 VAL H H 7.93 0.02 1 255 481 73 VAL CA C 57.99 0.4 1 256 481 73 VAL CB C 29.76 0.4 1 257 481 73 VAL N N 121.36 0.4 1 258 482 74 TRP H H 8.63 0.02 1 259 482 74 TRP CA C 52.93 0.4 1 260 482 74 TRP CB C 29.23 0.4 1 261 482 74 TRP N N 128.99 0.4 1 262 483 75 ASP H H 8.98 0.02 1 263 483 75 ASP CA C 49.34 0.4 1 264 483 75 ASP CB C 40.50 0.4 1 265 483 75 ASP N N 118.74 0.4 1 266 484 76 ALA H H 9.33 0.02 1 267 484 76 ALA CA C 50.27 0.4 1 268 484 76 ALA CB C 16.65 0.4 1 269 484 76 ALA N N 130.04 0.4 1 270 485 77 ASP H H 8.27 0.02 1 271 485 77 ASP CA C 50.38 0.4 1 272 485 77 ASP CB C 41.34 0.4 1 273 485 77 ASP N N 121.56 0.4 1 274 486 78 ALA H H 8.46 0.02 1 275 486 78 ALA CA C 51.42 0.4 1 276 486 78 ALA CB C 15.70 0.4 1 277 486 78 ALA N N 127.33 0.4 1 278 487 79 GLY H H 8.23 0.02 1 279 487 79 GLY CA C 42.48 0.4 1 280 487 79 GLY N N 106.92 0.4 1 281 488 80 ALA H H 7.64 0.02 1 282 488 80 ALA CA C 49.46 0.4 1 283 488 80 ALA CB C 16.66 0.4 1 284 488 80 ALA N N 123.43 0.4 1 285 489 81 ASP H H 7.78 0.02 1 286 489 81 ASP CA C 51.28 0.4 1 287 489 81 ASP CB C 38.43 0.4 1 288 489 81 ASP N N 119.43 0.4 1 289 490 82 ASP H H 7.80 0.02 1 290 490 82 ASP CA C 52.28 0.4 1 291 490 82 ASP CB C 38.88 0.4 1 292 490 82 ASP N N 122.19 0.4 1 293 491 83 ASP H H 8.23 0.02 1 294 491 83 ASP CA C 50.66 0.4 1 295 491 83 ASP CB C 41.68 0.4 1 296 491 83 ASP N N 119.84 0.4 1 297 492 84 LEU H H 7.89 0.02 1 298 492 84 LEU CA C 50.62 0.4 1 299 492 84 LEU CB C 41.65 0.4 1 300 492 84 LEU N N 127.27 0.4 1 301 493 85 LEU H H 8.75 0.02 1 302 493 85 LEU CA C 51.58 0.4 1 303 493 85 LEU CB C 41.57 0.4 1 304 493 85 LEU N N 129.78 0.4 1 305 494 86 GLY H H 6.78 0.02 1 306 494 86 GLY CA C 42.62 0.4 1 307 494 86 GLY N N 103.24 0.4 1 308 495 87 SER H H 8.01 0.02 1 309 495 87 SER CA C 54.19 0.4 1 310 495 87 SER CB C 63.27 0.4 1 311 495 87 SER N N 112.56 0.4 1 312 496 88 CYS H H 8.59 0.02 1 313 496 88 CYS CA C 52.04 0.4 1 314 496 88 CYS CB C 41.68 0.4 1 315 496 88 CYS N N 118.86 0.4 1 316 497 89 ASP H H 8.31 0.02 1 317 497 89 ASP CA C 49.84 0.4 1 318 497 89 ASP CB C 40.03 0.4 1 319 497 89 ASP N N 122.39 0.4 1 320 498 90 ARG H H 8.94 0.02 1 321 498 90 ARG CA C 49.93 0.4 1 322 498 90 ARG CB C 31.47 0.4 1 323 498 90 ARG N N 121.55 0.4 1 324 499 91 SER H H 8.41 0.02 1 325 499 91 SER CA C 53.72 0.4 1 326 499 91 SER N N 121.06 0.4 1 327 500 92 PRO CA C 59.20 0.4 1 328 500 92 PRO CB C 27.79 0.4 1 329 501 93 HIS H H 7.80 0.02 1 330 501 93 HIS CA C 51.15 0.4 1 331 501 93 HIS CB C 29.25 0.4 1 332 501 93 HIS N N 121.53 0.4 1 333 502 94 SER H H 8.00 0.02 1 334 502 94 SER CA C 57.56 0.4 1 335 502 94 SER CB C 61.55 0.4 1 336 502 94 SER N N 112.24 0.4 1 337 503 95 GLY H H 8.93 0.02 1 338 503 95 GLY CA C 41.49 0.4 1 339 503 95 GLY N N 115.03 0.4 1 340 504 96 PHE H H 7.71 0.02 1 341 504 96 PHE CA C 53.90 0.4 1 342 504 96 PHE CB C 37.59 0.4 1 343 504 96 PHE N N 121.83 0.4 1 344 505 97 HIS H H 7.73 0.02 1 345 505 97 HIS CA C 51.96 0.4 1 346 505 97 HIS CB C 31.19 0.4 1 347 505 97 HIS N N 124.37 0.4 1 348 506 98 GLU H H 7.91 0.02 1 349 506 98 GLU CA C 52.57 0.4 1 350 506 98 GLU CB C 28.14 0.4 1 351 506 98 GLU N N 120.14 0.4 1 352 507 99 VAL H H 8.55 0.02 1 353 507 99 VAL CA C 58.72 0.4 1 354 507 99 VAL CB C 31.34 0.4 1 355 507 99 VAL N N 125.18 0.4 1 356 508 100 THR H H 7.78 0.02 1 357 508 100 THR CA C 59.13 0.4 1 358 508 100 THR CB C 68.15 0.4 1 359 508 100 THR N N 122.20 0.4 1 360 509 101 CYS H H 9.12 0.02 1 361 509 101 CYS CA C 51.52 0.4 1 362 509 101 CYS CB C 39.30 0.4 1 363 509 101 CYS N N 124.37 0.4 1 364 510 102 GLU H H 8.55 0.02 1 365 510 102 GLU CA C 54.14 0.4 1 366 510 102 GLU CB C 26.59 0.4 1 367 510 102 GLU N N 125.18 0.4 1 368 511 103 LEU H H 8.21 0.02 1 369 511 103 LEU CA C 51.01 0.4 1 370 511 103 LEU CB C 39.59 0.4 1 371 511 103 LEU N N 125.81 0.4 1 372 512 104 ASN H H 8.39 0.02 1 373 512 104 ASN CA C 53.96 0.4 1 374 512 104 ASN CB C 34.60 0.4 1 375 512 104 ASN N N 119.18 0.4 1 376 513 105 HIS H H 6.85 0.02 1 377 513 105 HIS CA C 52.86 0.4 1 378 513 105 HIS CB C 28.29 0.4 1 379 513 105 HIS N N 112.68 0.4 1 380 514 106 GLY H H 8.20 0.02 1 381 514 106 GLY CA C 43.15 0.4 1 382 514 106 GLY N N 111.62 0.4 1 383 515 107 ARG H H 8.04 0.02 1 384 515 107 ARG CA C 51.79 0.4 1 385 515 107 ARG CB C 29.27 0.4 1 386 515 107 ARG N N 112.97 0.4 1 387 516 108 VAL H H 8.42 0.02 1 388 516 108 VAL CA C 56.63 0.4 1 389 516 108 VAL CB C 32.98 0.4 1 390 516 108 VAL N N 117.97 0.4 1 391 517 109 LYS H H 9.16 0.02 1 392 517 109 LYS CA C 51.94 0.4 1 393 517 109 LYS CB C 34.11 0.4 1 394 517 109 LYS N N 127.51 0.4 1 395 518 110 PHE H H 7.89 0.02 1 396 518 110 PHE CA C 53.53 0.4 1 397 518 110 PHE CB C 36.97 0.4 1 398 518 110 PHE N N 113.25 0.4 1 399 519 111 SER H H 8.67 0.02 1 400 519 111 SER CA C 53.33 0.4 1 401 519 111 SER CB C 64.03 0.4 1 402 519 111 SER N N 114.62 0.4 1 403 520 112 TYR H H 8.29 0.02 1 404 520 112 TYR CA C 53.31 0.4 1 405 520 112 TYR CB C 39.95 0.4 1 406 520 112 TYR N N 115.94 0.4 1 407 521 113 HIS H H 8.79 0.02 1 408 521 113 HIS CA C 50.56 0.4 1 409 521 113 HIS CB C 31.13 0.4 1 410 521 113 HIS N N 119.90 0.4 1 411 522 114 ALA H H 8.82 0.02 1 412 522 114 ALA CA C 47.58 0.4 1 413 522 114 ALA CB C 17.58 0.4 1 414 522 114 ALA N N 130.67 0.4 1 415 523 115 LYS H H 8.38 0.02 1 416 523 115 LYS CA C 52.47 0.4 1 417 523 115 LYS CB C 32.04 0.4 1 418 523 115 LYS N N 125.10 0.4 1 419 524 116 SER H H 8.00 0.02 1 420 524 116 SER CA C 56.20 0.4 1 421 524 116 SER CB C 61.39 0.4 1 422 524 116 SER N N 125.33 0.4 1 423 525 117 LEU H H 7.98 0.02 1 424 525 117 LEU CA C 51.89 0.4 1 425 525 117 LEU CB C 39.19 0.4 1 426 525 117 LEU N N 125.54 0.4 1 427 526 118 PRO CA C 60.00 0.4 1 stop_ save_