data_50221 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Staphylococcus aureus EF-GC3 methyl side chain chemical shifts ; _BMRB_accession_number 50221 _BMRB_flat_file_name bmr50221.str _Entry_type original _Submission_date 2020-04-01 _Accession_date 2020-04-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Assigned chemical shifts for the side chains of methyl containing ILVA residues in a truncated form of Staphylococcus aureus EF-G comprising domains III-V. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomlinson Jennifer H. . 2 Kalverda Arnout P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 133 "13C chemical shifts" 265 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-10-07 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25368 'Backbone assignments for the same protein system' 50220 'EF-GC3 from Staphylococcus aureus in complex with FusB' stop_ _Original_release_date 2020-04-09 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Fusidic acid resistance through changes in the dynamics of the drug target ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32999060 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomlinson Jennifer H. . 2 Kalverda Arnout P. . 3 Calabrese Antonio N. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details 'Manuscript to be submitted shortly. Full details of the citation to follow after acceptance' loop_ _Keyword 'antibiotic resistance, Elongation Factor G, NMR, FusB, conformational flexibility' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'EF-GC3 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EF-GC3 $entity_1 stop_ _System_molecular_weight 33424.6284 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Translocation factor for bacterial protein synthesis' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 33424.6284 _Mol_thiol_state 'all free' loop_ _Biological_function 'Translocation factor for bacterial protein sysnthesis' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 301 _Mol_residue_sequence ; MEFPEPVIHLSVEPKSKADQ DKMTQALVKLQEEDPTFHAH TDEETGQVIIGGMGELHLDI LVDRMKKEFNVECNVGAPMV SYRETFKSSAQVQGKFSRQS GGRGQYGDVHIEFTPNETGA GFEFENAIVGGVVPREYIPS VEAGLKDAMENGVLAGYPLI DVKAKLYDGSYHDVDSSEMA FKIAASLALKEAAKKCDPVI LEPMMKVTIEMPEEYMGDIM GDVTSRRGRVDGMEPRGNAQ VVNAYVPLSEMFGYATSLRS NTQGRGTYTMYFDHYAEVPK SIAEDIIKKNKGELEHHHHH H ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 401 MET 2 402 GLU 3 403 PHE 4 404 PRO 5 405 GLU 6 406 PRO 7 407 VAL 8 408 ILE 9 409 HIS 10 410 LEU 11 411 SER 12 412 VAL 13 413 GLU 14 414 PRO 15 415 LYS 16 416 SER 17 417 LYS 18 418 ALA 19 419 ASP 20 420 GLN 21 421 ASP 22 422 LYS 23 423 MET 24 424 THR 25 425 GLN 26 426 ALA 27 427 LEU 28 428 VAL 29 429 LYS 30 430 LEU 31 431 GLN 32 432 GLU 33 433 GLU 34 434 ASP 35 435 PRO 36 436 THR 37 437 PHE 38 438 HIS 39 439 ALA 40 440 HIS 41 441 THR 42 442 ASP 43 443 GLU 44 444 GLU 45 445 THR 46 446 GLY 47 447 GLN 48 448 VAL 49 449 ILE 50 450 ILE 51 451 GLY 52 452 GLY 53 453 MET 54 454 GLY 55 455 GLU 56 456 LEU 57 457 HIS 58 458 LEU 59 459 ASP 60 460 ILE 61 461 LEU 62 462 VAL 63 463 ASP 64 464 ARG 65 465 MET 66 466 LYS 67 467 LYS 68 468 GLU 69 469 PHE 70 470 ASN 71 471 VAL 72 472 GLU 73 473 CYS 74 474 ASN 75 475 VAL 76 476 GLY 77 477 ALA 78 478 PRO 79 479 MET 80 480 VAL 81 481 SER 82 482 TYR 83 483 ARG 84 484 GLU 85 485 THR 86 486 PHE 87 487 LYS 88 488 SER 89 489 SER 90 490 ALA 91 491 GLN 92 492 VAL 93 493 GLN 94 494 GLY 95 495 LYS 96 496 PHE 97 497 SER 98 498 ARG 99 499 GLN 100 500 SER 101 501 GLY 102 502 GLY 103 503 ARG 104 504 GLY 105 505 GLN 106 506 TYR 107 507 GLY 108 508 ASP 109 509 VAL 110 510 HIS 111 511 ILE 112 512 GLU 113 513 PHE 114 514 THR 115 515 PRO 116 516 ASN 117 517 GLU 118 518 THR 119 519 GLY 120 520 ALA 121 521 GLY 122 522 PHE 123 523 GLU 124 524 PHE 125 525 GLU 126 526 ASN 127 527 ALA 128 528 ILE 129 529 VAL 130 530 GLY 131 531 GLY 132 532 VAL 133 533 VAL 134 534 PRO 135 535 ARG 136 536 GLU 137 537 TYR 138 538 ILE 139 539 PRO 140 540 SER 141 541 VAL 142 542 GLU 143 543 ALA 144 544 GLY 145 545 LEU 146 546 LYS 147 547 ASP 148 548 ALA 149 549 MET 150 550 GLU 151 551 ASN 152 552 GLY 153 553 VAL 154 554 LEU 155 555 ALA 156 556 GLY 157 557 TYR 158 558 PRO 159 559 LEU 160 560 ILE 161 561 ASP 162 562 VAL 163 563 LYS 164 564 ALA 165 565 LYS 166 566 LEU 167 567 TYR 168 568 ASP 169 569 GLY 170 570 SER 171 571 TYR 172 572 HIS 173 573 ASP 174 574 VAL 175 575 ASP 176 576 SER 177 577 SER 178 578 GLU 179 579 MET 180 580 ALA 181 581 PHE 182 582 LYS 183 583 ILE 184 584 ALA 185 585 ALA 186 586 SER 187 587 LEU 188 588 ALA 189 589 LEU 190 590 LYS 191 591 GLU 192 592 ALA 193 593 ALA 194 594 LYS 195 595 LYS 196 596 CYS 197 597 ASP 198 598 PRO 199 599 VAL 200 600 ILE 201 601 LEU 202 602 GLU 203 603 PRO 204 604 MET 205 605 MET 206 606 LYS 207 607 VAL 208 608 THR 209 609 ILE 210 610 GLU 211 611 MET 212 612 PRO 213 613 GLU 214 614 GLU 215 615 TYR 216 616 MET 217 617 GLY 218 618 ASP 219 619 ILE 220 620 MET 221 621 GLY 222 622 ASP 223 623 VAL 224 624 THR 225 625 SER 226 626 ARG 227 627 ARG 228 628 GLY 229 629 ARG 230 630 VAL 231 631 ASP 232 632 GLY 233 633 MET 234 634 GLU 235 635 PRO 236 636 ARG 237 637 GLY 238 638 ASN 239 639 ALA 240 640 GLN 241 641 VAL 242 642 VAL 243 643 ASN 244 644 ALA 245 645 TYR 246 646 VAL 247 647 PRO 248 648 LEU 249 649 SER 250 650 GLU 251 651 MET 252 652 PHE 253 653 GLY 254 654 TYR 255 655 ALA 256 656 THR 257 657 SER 258 658 LEU 259 659 ARG 260 660 SER 261 661 ASN 262 662 THR 263 663 GLN 264 664 GLY 265 665 ARG 266 666 GLY 267 667 THR 268 668 TYR 269 669 THR 270 670 MET 271 671 TYR 272 672 PHE 273 673 ASP 274 674 HIS 275 675 TYR 276 676 ALA 277 677 GLU 278 678 VAL 279 679 PRO 280 680 LYS 281 681 SER 282 682 ILE 283 683 ALA 284 684 GLU 285 685 ASP 286 686 ILE 287 687 ILE 288 688 LYS 289 689 LYS 290 690 ASN 291 691 LYS 292 692 GLY 293 693 GLU 294 694 LEU 295 695 GLU 296 696 HIS 297 697 HIS 298 698 HIS 299 699 HIS 300 700 HIS 301 701 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 NCBI P68790 EF-G . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $entity_1 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus fusA 'Truncated version of EF-G comprising domains III-V' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli 'BL21 Gold' plasmid pET-29b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '300 uM 15N 13C partially 2H (expressed in D2O with 1H glucose) EF-GC3 in 20 mM TrisHCl, 300 mM NaCl, 1 mM DTT, pH 8.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.25 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' TrisHCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNmr_Analysis _Version 2.1 loop_ _Task assignment stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details 'Bruker Avance console and cryoprobe with Varian magnet' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CCH-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCH-TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM TrisHCl, 300 mM NaCl, 1 mM DTT, 10 % D2O, pH 8.0' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.310 0.002 M pH 8.000 0.01 pH pressure 1.000 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 internal indirect . . . . DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ loop_ _Experiment_label '2D 1H-13C HSQC' '3D CCH-TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name EF-GC3 _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 1 408 8 ILE HG2 H 0.563 0.036 1 2 408 8 ILE HD1 H 0.659 0.027 1 3 408 8 ILE CA C 58.443 . 1 4 408 8 ILE CB C 40.280 . 1 5 408 8 ILE CG1 C 26.316 0.088 1 6 408 8 ILE CG2 C 14.754 0.115 1 7 408 8 ILE CD1 C 13.275 0.121 1 8 410 10 LEU HD1 H 0.592 0.0 1 9 410 10 LEU CB C 45.240 . 1 10 410 10 LEU CD1 C 21.327 0.045 1 11 412 12 VAL HG1 H 0.770 0.034 1 12 412 12 VAL CA C 60.268 . 1 13 412 12 VAL CB C 33.599 . 1 14 412 12 VAL CG1 C 20.572 0.129 1 15 418 18 ALA HB H 1.356 0.0 1 16 418 18 ALA CA C 54.310 . 1 17 418 18 ALA CB C 17.168 0.034 1 18 424 24 THR HG2 H 1.126 0.0 1 19 424 24 THR CA C 66.270 . 1 20 424 24 THR CB C 68.114 . 1 21 424 24 THR CG2 C 20.781 0.033 1 22 426 26 ALA H H 7.923 . 1 23 426 26 ALA HB H 0.750 0.026 1 24 426 26 ALA CA C 53.895 . 1 25 426 26 ALA CB C 17.720 0.024 1 26 427 27 LEU HD1 H 0.656 0.0 1 27 427 27 LEU CA C 57.612 . 1 28 427 27 LEU CB C 40.223 . 1 29 427 27 LEU CG C 25.238 . 1 30 427 27 LEU CD1 C 22.142 0.036 1 31 428 28 VAL HG1 H 0.962 0.0 2 32 428 28 VAL HG2 H 0.839 0.002 2 33 428 28 VAL CA C 65.767 0.033 1 34 428 28 VAL CB C 30.815 0.024 1 35 428 28 VAL CG1 C 21.327 0.035 2 36 428 28 VAL CG2 C 20.101 0.037 2 37 430 30 LEU HD1 H 0.449 0.0 2 38 430 30 LEU HD2 H 0.697 0.0 2 39 430 30 LEU CA C 57.576 0.035 1 40 430 30 LEU CB C 40.352 0.023 1 41 430 30 LEU CG C 25.838 0.103 1 42 430 30 LEU CD1 C 24.345 0.033 2 43 430 30 LEU CD2 C 21.442 0.042 2 44 436 36 THR HG2 H 0.915 0.001 1 45 436 36 THR CA C 61.430 . 1 46 436 36 THR CB C 68.726 . 1 47 436 36 THR CG2 C 16.987 0.037 1 48 439 39 ALA H H 7.845 . 1 49 439 39 ALA HB H 1.040 0.027 1 50 439 39 ALA CA C 50.266 . 1 51 439 39 ALA CB C 22.032 0.018 1 52 441 41 THR HG2 H 0.781 0.0 1 53 441 41 THR CA C 61.285 . 1 54 441 41 THR CB C 68.866 . 1 55 441 41 THR CG2 C 20.168 0.031 1 56 445 45 THR HG2 H 1.086 0.001 1 57 445 45 THR CA C 61.264 . 1 58 445 45 THR CB C 70.567 . 1 59 445 45 THR CG2 C 20.284 0.038 1 60 448 48 VAL HG1 H 0.871 0.001 2 61 448 48 VAL HG2 H 0.852 0.03 2 62 448 48 VAL CA C 60.417 0.005 1 63 448 48 VAL CB C 32.983 0.003 1 64 448 48 VAL CG1 C 19.497 0.1 2 65 448 48 VAL CG2 C 20.322 0.118 2 66 449 49 ILE HG2 H 0.667 0.0 1 67 449 49 ILE HD1 H 0.584 0.001 1 68 449 49 ILE CA C 58.466 0.046 1 69 449 49 ILE CB C 37.271 0.129 1 70 449 49 ILE CG1 C 25.826 . 1 71 449 49 ILE CG2 C 17.186 0.028 1 72 449 49 ILE CD1 C 10.801 0.073 1 73 450 50 ILE HG2 H 0.720 0.032 1 74 450 50 ILE HD1 H 0.572 0.001 1 75 450 50 ILE CA C 58.642 0.02 1 76 450 50 ILE CB C 38.765 0.029 1 77 450 50 ILE CG1 C 25.092 0.026 1 78 450 50 ILE CG2 C 17.223 0.122 1 79 450 50 ILE CD1 C 12.498 0.03 1 80 456 56 LEU HD1 H 0.741 0.001 2 81 456 56 LEU HD2 H 0.692 0.025 2 82 456 56 LEU CA C 54.671 0.012 1 83 456 56 LEU CG C 25.618 0.043 1 84 456 56 LEU CD1 C 23.907 0.059 2 85 456 56 LEU CD2 C 22.408 0.031 2 86 460 60 ILE HG2 H 0.829 0.03 1 87 460 60 ILE HD1 H 0.762 0.028 1 88 460 60 ILE CA C 63.888 0.061 1 89 460 60 ILE CB C 36.716 0.04 1 90 460 60 ILE CG1 C 27.506 . 1 91 460 60 ILE CG2 C 16.152 0.127 1 92 460 60 ILE CD1 C 12.144 0.132 1 93 461 61 LEU HD1 H -0.100 0.0 2 94 461 61 LEU HD2 H 0.325 0.001 2 95 461 61 LEU CB C 40.695 . 1 96 461 61 LEU CG C 25.493 0.011 1 97 461 61 LEU CD1 C 23.875 0.052 2 98 461 61 LEU CD2 C 22.215 0.027 2 99 462 62 VAL HG1 H 0.809 0.001 2 100 462 62 VAL HG2 H 0.774 0.002 2 101 462 62 VAL CA C 66.042 0.052 1 102 462 62 VAL CB C 30.467 0.026 1 103 462 62 VAL CG1 C 22.107 0.023 2 104 462 62 VAL CG2 C 20.909 0.035 2 105 471 71 VAL HG1 H 0.674 0.029 2 106 471 71 VAL HG2 H 0.712 0.0 2 107 471 71 VAL CA C 62.232 0.05 1 108 471 71 VAL CB C 32.218 0.015 1 109 471 71 VAL CG1 C 20.874 0.112 2 110 471 71 VAL CG2 C 20.777 0.021 2 111 475 75 VAL HG1 H 0.816 0.029 2 112 475 75 VAL HG2 H 0.679 0.028 2 113 475 75 VAL CA C 60.654 0.018 1 114 475 75 VAL CB C 33.674 0.065 1 115 475 75 VAL CG1 C 18.474 0.106 2 116 475 75 VAL CG2 C 21.190 0.098 2 117 477 77 ALA H H 7.910 . 1 118 477 77 ALA HB H 1.246 0.035 1 119 477 77 ALA CA C 49.060 . 1 120 477 77 ALA CB C 17.376 0.038 1 121 485 85 THR HG2 H 0.995 0.0 1 122 485 85 THR CA C 61.136 . 1 123 485 85 THR CB C 69.317 . 1 124 485 85 THR CG2 C 21.014 0.021 1 125 490 90 ALA H H 8.490 . 1 126 490 90 ALA HB H 1.254 0.032 1 127 490 90 ALA CA C 52.314 . 1 128 490 90 ALA CB C 23.281 0.024 1 129 492 92 VAL HG1 H 1.134 0.029 2 130 492 92 VAL HG2 H 0.760 0.033 2 131 492 92 VAL CA C 58.796 0.03 1 132 492 92 VAL CB C 35.490 0.017 1 133 492 92 VAL CG1 C 18.641 0.099 2 134 492 92 VAL CG2 C 21.051 0.142 2 135 509 109 VAL HG1 H 1.218 0.03 2 136 509 109 VAL HG2 H 0.790 0.027 2 137 509 109 VAL CA C 57.780 0.026 1 138 509 109 VAL CB C 34.792 0.087 1 139 509 109 VAL CG1 C 23.245 0.098 2 140 509 109 VAL CG2 C 17.634 0.056 2 141 511 111 ILE HG2 H -0.211 0.032 1 142 511 111 ILE HD1 H 0.750 0.026 1 143 511 111 ILE CA C 57.774 0.007 1 144 511 111 ILE CB C 41.364 0.001 1 145 511 111 ILE CG1 C 27.276 0.029 1 146 511 111 ILE CG2 C 16.462 0.114 1 147 511 111 ILE CD1 C 12.795 0.082 1 148 514 114 THR HG2 H 1.166 0.0 1 149 514 114 THR CA C 58.364 . 1 150 514 114 THR CG2 C 20.372 0.036 1 151 518 118 THR HG2 H 1.302 0.0 1 152 518 118 THR CA C 63.748 . 1 153 518 118 THR CB C 68.543 . 1 154 518 118 THR CG2 C 20.897 0.035 1 155 520 120 ALA H H 8.145 . 1 156 520 120 ALA HB H 1.236 0.031 1 157 520 120 ALA CA C 52.524 . 1 158 520 120 ALA CB C 19.386 0.017 1 159 527 127 ALA H H 8.653 . 1 160 527 127 ALA HB H 1.167 0.033 1 161 527 127 ALA CA C 49.804 . 1 162 527 127 ALA CB C 18.536 0.02 1 163 528 128 ILE HG2 H 0.826 0.043 1 164 528 128 ILE HD1 H 0.350 0.029 1 165 528 128 ILE CA C 58.903 . 1 166 528 128 ILE CB C 34.436 . 1 167 528 128 ILE CG1 C 25.641 . 1 168 528 128 ILE CG2 C 16.646 0.101 1 169 528 128 ILE CD1 C 8.572 0.072 1 170 529 129 VAL HG1 H 0.588 0.032 1 171 529 129 VAL CA C 60.149 . 1 172 529 129 VAL CB C 33.455 . 1 173 529 129 VAL CG1 C 20.412 0.108 1 174 532 132 VAL HG1 H 1.079 0.0 2 175 532 132 VAL HG2 H 1.068 0.004 2 176 532 132 VAL CA C 65.054 0.108 1 177 532 132 VAL CB C 30.091 0.053 1 178 532 132 VAL CG1 C 21.027 0.019 2 179 532 132 VAL CG2 C 18.898 0.031 2 180 533 133 VAL HG1 H 0.436 0.036 2 181 533 133 VAL HG2 H 0.955 0.03 2 182 533 133 VAL CA C 59.642 0.014 1 183 533 133 VAL CB C 33.769 0.086 1 184 533 133 VAL CG1 C 19.895 0.121 2 185 533 133 VAL CG2 C 21.042 0.107 2 186 538 138 ILE HG2 H 1.001 0.036 1 187 538 138 ILE HD1 H 0.616 0.027 1 188 538 138 ILE CA C 66.067 0.082 1 189 538 138 ILE CB C 33.485 0.101 1 190 538 138 ILE CG1 C 27.630 0.024 1 191 538 138 ILE CG2 C 16.086 0.117 1 192 538 138 ILE CD1 C 10.253 0.081 1 193 543 143 ALA H H 8.116 . 1 194 543 143 ALA HB H 1.366 0.032 1 195 543 143 ALA CA C 54.378 . 1 196 543 143 ALA CB C 17.773 0.029 1 197 545 145 LEU HD1 H 1.001 0.0 1 198 545 145 LEU CA C 57.149 . 1 199 545 145 LEU CB C 40.955 . 1 200 545 145 LEU CG C 25.525 . 1 201 545 145 LEU CD1 C 23.320 0.037 1 202 548 148 ALA H H 7.593 . 1 203 548 148 ALA HB H 1.365 0.035 1 204 548 148 ALA CA C 54.067 . 1 205 548 148 ALA CB C 17.582 0.027 1 206 555 155 ALA HB H 1.209 0.0 1 207 555 155 ALA CA C 50.003 . 1 208 555 155 ALA CB C 20.487 0.035 1 209 559 159 LEU HD1 H 0.333 0.0 2 210 559 159 LEU HD2 H 0.150 0.001 2 211 559 159 LEU CA C 53.353 0.113 1 212 559 159 LEU CB C 42.952 0.093 1 213 559 159 LEU CG C 25.759 . 1 214 559 159 LEU CD1 C 24.490 0.047 2 215 559 159 LEU CD2 C 25.574 0.016 2 216 560 160 ILE HG2 H 0.678 0.034 1 217 560 160 ILE HD1 H 0.360 0.026 1 218 560 160 ILE CA C 58.335 0.099 1 219 560 160 ILE CB C 41.968 0.109 1 220 560 160 ILE CG1 C 23.683 0.019 1 221 560 160 ILE CG2 C 16.841 0.117 1 222 560 160 ILE CD1 C 13.268 0.099 1 223 562 162 VAL HG1 H 0.988 0.001 2 224 562 162 VAL HG2 H 0.668 0.001 2 225 562 162 VAL CA C 60.629 0.03 1 226 562 162 VAL CB C 35.892 0.001 1 227 562 162 VAL CG1 C 21.704 0.136 2 228 562 162 VAL CG2 C 20.555 0.15 2 229 564 164 ALA H H 8.605 . 1 230 564 164 ALA HB H 1.186 0.032 1 231 564 164 ALA CA C 49.238 . 1 232 564 164 ALA CB C 23.039 0.042 1 233 574 174 VAL HG1 H 0.992 0.031 2 234 574 174 VAL HG2 H 0.969 0.034 2 235 574 174 VAL CA C 63.465 0.014 1 236 574 174 VAL CB C 33.135 0.038 1 237 574 174 VAL CG1 C 20.768 0.137 2 238 574 174 VAL CG2 C 20.525 0.138 2 239 583 183 ILE HG2 H -0.149 0.03 1 240 583 183 ILE HD1 H 0.140 0.026 1 241 583 183 ILE CA C 63.985 0.009 1 242 583 183 ILE CB C 36.191 0.048 1 243 583 183 ILE CG1 C 27.248 0.035 1 244 583 183 ILE CG2 C 15.933 0.11 1 245 583 183 ILE CD1 C 12.057 0.103 1 246 584 184 ALA H H 8.201 . 1 247 584 184 ALA HB H 1.252 0.035 1 248 584 184 ALA CA C 55.517 . 1 249 584 184 ALA CB C 16.261 0.033 1 250 585 185 ALA H H 7.862 . 1 251 585 185 ALA HB H 1.592 0.03 1 252 585 185 ALA CA C 55.032 . 1 253 585 185 ALA CB C 18.613 0.061 1 254 587 187 LEU HD1 H 0.869 0.001 2 255 587 187 LEU HD2 H 0.801 0.0 2 256 587 187 LEU CA C 57.240 0.019 1 257 587 187 LEU CB C 39.833 0.002 1 258 587 187 LEU CG C 25.881 0.038 1 259 587 187 LEU CD1 C 23.199 0.027 2 260 587 187 LEU CD2 C 23.348 0.051 2 261 588 188 ALA H H 8.135 . 1 262 588 188 ALA HB H 1.467 0.032 1 263 588 188 ALA CA C 54.184 . 1 264 588 188 ALA CB C 16.524 0.049 1 265 589 189 LEU HD1 H 0.635 0.003 1 266 589 189 LEU CA C 56.963 . 1 267 589 189 LEU CD1 C 22.714 0.064 1 268 592 192 ALA H H 8.457 . 1 269 592 192 ALA HB H 1.036 0.031 1 270 592 192 ALA CA C 54.102 . 1 271 592 192 ALA CB C 17.842 0.036 1 272 593 193 ALA H H 7.967 . 1 273 593 193 ALA HB H 1.428 0.036 1 274 593 193 ALA CA C 54.249 . 1 275 593 193 ALA CB C 17.597 0.031 1 276 599 199 VAL HG1 H 0.618 0.037 2 277 599 199 VAL HG2 H 0.809 0.009 2 278 599 199 VAL CA C 58.373 . 1 279 599 199 VAL CB C 35.529 0.011 1 280 599 199 VAL CG1 C 17.480 0.116 2 281 599 199 VAL CG2 C 21.111 0.073 2 282 600 200 ILE HG2 H 0.752 0.027 1 283 600 200 ILE HD1 H 0.675 0.028 1 284 600 200 ILE CA C 59.720 0.047 1 285 600 200 ILE CB C 37.602 0.027 1 286 600 200 ILE CG1 C 27.153 0.108 1 287 600 200 ILE CG2 C 17.323 0.024 1 288 600 200 ILE CD1 C 12.825 0.102 1 289 601 201 LEU HD1 H 0.605 0.004 2 290 601 201 LEU HD2 H 0.555 0.038 2 291 601 201 LEU CB C 45.135 0.048 1 292 601 201 LEU CD1 C 23.768 0.025 2 293 601 201 LEU CD2 C 24.342 0.037 2 294 607 207 VAL HG1 H 0.746 0.029 1 295 607 207 VAL CA C 60.209 . 1 296 607 207 VAL CB C 33.459 . 1 297 607 207 VAL CG1 C 20.167 0.15 1 298 609 209 ILE HG2 H 0.972 0.03 1 299 609 209 ILE HD1 H 0.487 0.024 1 300 609 209 ILE CA C 60.107 0.059 1 301 609 209 ILE CB C 40.942 0.042 1 302 609 209 ILE CG1 C 27.403 0.022 1 303 609 209 ILE CG2 C 19.625 0.15 1 304 609 209 ILE CD1 C 14.301 0.132 1 305 619 219 ILE HG2 H 0.765 0.031 1 306 619 219 ILE HD1 H 0.585 0.03 1 307 619 219 ILE CA C 61.510 0.038 1 308 619 219 ILE CB C 34.936 0.013 1 309 619 219 ILE CG1 C 27.380 . 1 310 619 219 ILE CG2 C 17.430 0.118 1 311 619 219 ILE CD1 C 10.299 0.065 1 312 623 223 VAL HG1 H 0.725 0.035 2 313 623 223 VAL HG2 H 0.489 0.003 2 314 623 223 VAL CA C 67.042 0.013 1 315 623 223 VAL CB C 29.966 . 1 316 623 223 VAL CG1 C 21.959 0.096 2 317 623 223 VAL CG2 C 20.811 0.027 2 318 624 224 THR HG2 H 1.235 0.0 1 319 624 224 THR CA C 65.591 . 1 320 624 224 THR CB C 67.871 . 1 321 624 224 THR CG2 C 21.004 0.023 1 322 630 230 VAL HG1 H 0.345 0.032 1 323 630 230 VAL CA C 62.177 . 1 324 630 230 VAL CB C 31.708 . 1 325 630 230 VAL CG1 C 20.406 0.114 1 326 639 239 ALA H H 7.957 . 1 327 639 239 ALA HB H 1.318 0.033 1 328 639 239 ALA CA C 50.282 . 1 329 639 239 ALA CB C 20.828 0.033 1 330 641 241 VAL HG1 H 0.717 0.032 1 331 641 241 VAL CA C 60.001 . 1 332 641 241 VAL CB C 32.461 . 1 333 641 241 VAL CG1 C 20.551 0.111 1 334 644 244 ALA H H 9.303 . 1 335 644 244 ALA HB H 0.978 0.035 1 336 644 244 ALA CA C 49.518 . 1 337 644 244 ALA CB C 22.653 0.015 1 338 646 246 VAL HG1 H 0.529 0.037 1 339 646 246 VAL CA C 58.035 . 1 340 646 246 VAL CB C 36.571 . 1 341 646 246 VAL CG1 C 20.557 0.144 1 342 655 255 ALA H H 8.755 . 1 343 655 255 ALA HB H 1.596 0.035 1 344 655 255 ALA CA C 55.076 . 1 345 655 255 ALA CB C 17.463 0.055 1 346 656 256 THR HG2 H 1.108 0.001 1 347 656 256 THR CA C 65.262 . 1 348 656 256 THR CB C 67.810 . 1 349 656 256 THR CG2 C 20.943 0.025 1 350 658 258 LEU HD1 H 0.505 0.001 1 351 658 258 LEU CA C 56.727 . 1 352 658 258 LEU CB C 39.823 . 1 353 658 258 LEU CG C 25.529 . 1 354 658 258 LEU CD1 C 23.108 0.038 1 355 662 262 THR HG2 H 0.794 0.0 1 356 662 262 THR CA C 69.256 . 1 357 662 262 THR CG2 C 21.133 0.042 1 358 667 267 THR HG2 H 1.062 0.0 1 359 667 267 THR CA C 60.015 . 1 360 667 267 THR CG2 C 20.421 0.016 1 361 669 269 THR HG2 H 1.010 0.001 1 362 669 269 THR CA C 59.788 . 1 363 669 269 THR CG2 C 20.497 0.012 1 364 676 276 ALA H H 8.971 . 1 365 676 276 ALA HB H 1.518 0.03 1 366 676 276 ALA CA C 49.853 . 1 367 676 276 ALA CB C 23.395 0.028 1 368 678 278 VAL HG1 H 0.902 0.033 2 369 678 278 VAL HG2 H 0.941 0.001 2 370 678 278 VAL CA C 59.558 0.06 1 371 678 278 VAL CB C 31.481 0.043 1 372 678 278 VAL CG1 C 21.515 0.129 2 373 678 278 VAL CG2 C 20.937 0.018 2 374 682 282 ILE HG2 H 0.839 0.031 1 375 682 282 ILE HD1 H 0.782 0.034 1 376 682 282 ILE CA C 62.800 0.004 1 377 682 282 ILE CB C 36.914 0.059 1 378 682 282 ILE CG1 C 27.210 0.01 1 379 682 282 ILE CG2 C 16.070 0.112 1 380 682 282 ILE CD1 C 11.119 0.109 1 381 683 283 ALA H H 8.270 . 1 382 683 283 ALA HB H 1.381 0.032 1 383 683 283 ALA CA C 54.819 . 1 384 683 283 ALA CB C 17.536 0.039 1 385 686 286 ILE HG2 H 0.661 0.033 1 386 686 286 ILE HD1 H 0.216 0.026 1 387 686 286 ILE CA C 64.876 0.155 1 388 686 286 ILE CB C 37.575 0.003 1 389 686 286 ILE CG1 C 27.329 . 1 390 686 286 ILE CG2 C 16.855 0.12 1 391 686 286 ILE CD1 C 12.992 0.103 1 392 687 287 ILE HG2 H 0.838 0.034 1 393 687 287 ILE HD1 H 0.739 0.026 1 394 687 287 ILE CA C 65.086 0.001 1 395 687 287 ILE CB C 37.627 0.03 1 396 687 287 ILE CG1 C 28.671 . 1 397 687 287 ILE CG2 C 16.380 0.122 1 398 687 287 ILE CD1 C 13.047 0.121 1 stop_ save_