data_16393 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Evidence for differential phosphorylation-dependent interactions in WT and deltaF508 CFTR ; _BMRB_accession_number 16393 _BMRB_flat_file_name bmr16393.str _Entry_type original _Submission_date 2009-07-03 _Accession_date 2009-07-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts for wild type (WT) murine CFTR NBD1 (389-673)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kanelis Voula . . 2 Hudson Rhea P. . 3 Thibodeau Patrick H. . 4 Thomas Philip J. . 5 Forman-Kay Julie D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 170 "13C chemical shifts" 166 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-28 update BMRB 'edit entity name' 2010-01-21 update BMRB 'complete entry citation' 2009-12-11 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16394 'deltaF508 CFTR NBD1-RE' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19927121 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kanelis Voula . . 2 Hudson Rhea P. . 3 Thibodeau Patrick H. . 4 Thomas Philip J. . 5 Forman-Kay Julie D. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 263 _Page_last 277 _Year 2010 _Details . loop_ _Keyword CFTR ICL NBD1 'NMR spectroscopy' phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'CFTR NBD1-RE monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CFTR NBD1-RE' $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CFTR NBD1-RE' _Molecular_mass 31994.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'chloride channel' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 285 _Mol_residue_sequence ; TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIF GVSYDEYRYKSVVKACQLQQ DITKFAEQDNTVLGEGGVTL SGGQRARISLARAVYKDADL YLLDSPFGYLDVFTEEQVFE SCVCKLMANKTRILVTSKME HLRKADKILILHQGSSYFYG TFSELQSLRPDFSSKLMGYD TFDQFTEERRSSILTETLRR FSVDD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 389 THR 2 390 THR 3 391 GLY 4 392 ILE 5 393 ILE 6 394 MET 7 395 GLU 8 396 ASN 9 397 VAL 10 398 THR 11 399 ALA 12 400 PHE 13 401 TRP 14 402 GLU 15 403 GLU 16 404 GLY 17 405 PHE 18 406 GLY 19 407 GLU 20 408 LEU 21 409 LEU 22 410 GLU 23 411 LYS 24 412 VAL 25 413 GLN 26 414 GLN 27 415 SER 28 416 ASN 29 417 GLY 30 418 ASP 31 419 ARG 32 420 LYS 33 421 HIS 34 422 SER 35 423 SER 36 424 ASP 37 425 GLU 38 426 ASN 39 427 ASN 40 428 VAL 41 429 SER 42 430 PHE 43 431 SER 44 432 HIS 45 433 LEU 46 434 CYS 47 435 LEU 48 436 VAL 49 437 GLY 50 438 ASN 51 439 PRO 52 440 VAL 53 441 LEU 54 442 LYS 55 443 ASN 56 444 ILE 57 445 ASN 58 446 LEU 59 447 ASN 60 448 ILE 61 449 GLU 62 450 LYS 63 451 GLY 64 452 GLU 65 453 MET 66 454 LEU 67 455 ALA 68 456 ILE 69 457 THR 70 458 GLY 71 459 SER 72 460 THR 73 461 GLY 74 462 SER 75 463 GLY 76 464 LYS 77 465 THR 78 466 SER 79 467 LEU 80 468 LEU 81 469 MET 82 470 LEU 83 471 ILE 84 472 LEU 85 473 GLY 86 474 GLU 87 475 LEU 88 476 GLU 89 477 ALA 90 478 SER 91 479 GLU 92 480 GLY 93 481 ILE 94 482 ILE 95 483 LYS 96 484 HIS 97 485 SER 98 486 GLY 99 487 ARG 100 488 VAL 101 489 SER 102 490 PHE 103 491 CYS 104 492 SER 105 493 GLN 106 494 PHE 107 495 SER 108 496 TRP 109 497 ILE 110 498 MET 111 499 PRO 112 500 GLY 113 501 THR 114 502 ILE 115 503 LYS 116 504 GLU 117 505 ASN 118 506 ILE 119 507 ILE 120 508 PHE 121 509 GLY 122 510 VAL 123 511 SER 124 512 TYR 125 513 ASP 126 514 GLU 127 515 TYR 128 516 ARG 129 517 TYR 130 518 LYS 131 519 SER 132 520 VAL 133 521 VAL 134 522 LYS 135 523 ALA 136 524 CYS 137 525 GLN 138 526 LEU 139 527 GLN 140 528 GLN 141 529 ASP 142 530 ILE 143 531 THR 144 532 LYS 145 533 PHE 146 534 ALA 147 535 GLU 148 536 GLN 149 537 ASP 150 538 ASN 151 539 THR 152 540 VAL 153 541 LEU 154 542 GLY 155 543 GLU 156 544 GLY 157 545 GLY 158 546 VAL 159 547 THR 160 548 LEU 161 549 SER 162 550 GLY 163 551 GLY 164 552 GLN 165 553 ARG 166 554 ALA 167 555 ARG 168 556 ILE 169 557 SER 170 558 LEU 171 559 ALA 172 560 ARG 173 561 ALA 174 562 VAL 175 563 TYR 176 564 LYS 177 565 ASP 178 566 ALA 179 567 ASP 180 568 LEU 181 569 TYR 182 570 LEU 183 571 LEU 184 572 ASP 185 573 SER 186 574 PRO 187 575 PHE 188 576 GLY 189 577 TYR 190 578 LEU 191 579 ASP 192 580 VAL 193 581 PHE 194 582 THR 195 583 GLU 196 584 GLU 197 585 GLN 198 586 VAL 199 587 PHE 200 588 GLU 201 589 SER 202 590 CYS 203 591 VAL 204 592 CYS 205 593 LYS 206 594 LEU 207 595 MET 208 596 ALA 209 597 ASN 210 598 LYS 211 599 THR 212 600 ARG 213 601 ILE 214 602 LEU 215 603 VAL 216 604 THR 217 605 SER 218 606 LYS 219 607 MET 220 608 GLU 221 609 HIS 222 610 LEU 223 611 ARG 224 612 LYS 225 613 ALA 226 614 ASP 227 615 LYS 228 616 ILE 229 617 LEU 230 618 ILE 231 619 LEU 232 620 HIS 233 621 GLN 234 622 GLY 235 623 SER 236 624 SER 237 625 TYR 238 626 PHE 239 627 TYR 240 628 GLY 241 629 THR 242 630 PHE 243 631 SER 244 632 GLU 245 633 LEU 246 634 GLN 247 635 SER 248 636 LEU 249 637 ARG 250 638 PRO 251 639 ASP 252 640 PHE 253 641 SER 254 642 SER 255 643 LYS 256 644 LEU 257 645 MET 258 646 GLY 259 647 TYR 260 648 ASP 261 649 THR 262 650 PHE 263 651 ASP 264 652 GLN 265 653 PHE 266 654 THR 267 655 GLU 268 656 GLU 269 657 ARG 270 658 ARG 271 659 SER 272 660 SER 273 661 ILE 274 662 LEU 275 663 THR 276 664 GLU 277 665 THR 278 666 LEU 279 667 ARG 280 668 ARG 281 669 PHE 282 670 SER 283 671 VAL 284 672 ASP 285 673 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 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 BMRB 16367 CFTR_NBD1-RE_G550E/R553M/R555K 100.00 285 98.95 99.30 0.00e+00 BMRB 16394 "deltaF508 CFTR NBD1-RE" 100.00 284 99.65 99.65 0.00e+00 PDB 1Q3H "Mouse Cftr Nbd1 With Amp.Pnp" 100.00 286 100.00 100.00 0.00e+00 PDB 1R0W "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) Apo" 100.00 286 100.00 100.00 0.00e+00 PDB 1R0X "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp" 100.00 286 100.00 100.00 0.00e+00 PDB 1R0Y "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Adp" 100.00 286 100.00 100.00 0.00e+00 PDB 1R0Z "Phosphorylated Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide-Binding Domain One (Nbd1) With Atp" 100.00 286 98.60 98.60 0.00e+00 PDB 1R10 "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp, I4122 Space Group" 100.00 286 100.00 100.00 0.00e+00 PDB 1XF9 "Structure Of Nbd1 From Murine Cftr- F508s Mutant" 98.95 283 99.65 99.65 0.00e+00 PDB 1XFA "Structure Of Nbd1 From Murine Cftr- F508r Mutant" 98.95 283 99.65 99.65 0.00e+00 PDB 3SI7 "The Crystal Structure Of The Nbd1 Domain Of The Mouse Cftr Protein, Deltaf508 Mutant" 100.00 285 99.65 99.65 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 $entity 'recombinant technology' 'E. coli' Escherichia coli . pET-His-SUMO 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 $entity 400 uM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' ATP 5 mM 'natural abundance' DTT 5 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 500 mM '[U-100% 13C; U-100% 15N; 50% 2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' ATP 5 mM 'natural abundance' DTT 5 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 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' 170 . mM pH 7 . pH pressure 1 . atm temperature 293 . 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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal 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 'The 1H and 15N shifts reported are from a protonated sample. The 13C shifts reported are from a sample that was 50% deuterated.' loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'CFTR NBD1-RE' _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 1 390 2 THR H H 8.21 0.02 1 2 390 2 THR CA C 61.55 0.30 1 3 390 2 THR N N 117.10 0.30 1 4 391 3 GLY H H 8.62 0.02 1 5 391 3 GLY CA C 44.67 0.30 1 6 391 3 GLY N N 114.41 0.30 1 7 392 4 ILE H H 8.58 0.02 1 8 392 4 ILE CA C 59.80 0.30 1 9 392 4 ILE N N 120.38 0.30 1 10 393 5 ILE H H 8.55 0.02 1 11 393 5 ILE CA C 59.30 0.30 1 12 393 5 ILE N N 126.60 0.30 1 13 394 6 MET H H 8.91 0.02 1 14 394 6 MET CA C 55.15 0.30 1 15 394 6 MET N N 124.25 0.30 1 16 395 7 GLU H H 9.20 0.02 1 17 395 7 GLU CA C 54.26 0.30 1 18 395 7 GLU N N 125.22 0.30 1 19 396 8 ASN H H 8.90 0.02 1 20 396 8 ASN CA C 53.77 0.30 1 21 396 8 ASN N N 124.97 0.30 1 22 397 9 VAL H H 8.55 0.02 1 23 397 9 VAL CA C 63.04 0.30 1 24 397 9 VAL N N 121.16 0.30 1 25 398 10 THR H H 7.83 0.02 1 26 398 10 THR CA C 60.57 0.30 1 27 398 10 THR N N 124.69 0.30 1 28 399 11 ALA H H 8.68 0.02 1 29 399 11 ALA CA C 50.77 0.30 1 30 399 11 ALA N N 127.77 0.30 1 31 400 12 PHE H H 9.09 0.02 1 32 400 12 PHE CA C 56.35 0.30 1 33 400 12 PHE N N 120.81 0.30 1 34 401 13 TRP H H 8.79 0.02 1 35 401 13 TRP CA C 58.06 0.30 1 36 401 13 TRP N N 122.38 0.30 1 37 423 35 SER H H 8.49 0.02 1 38 423 35 SER CA C 58.35 0.30 1 39 423 35 SER N N 118.75 0.30 1 40 424 36 ASP H H 8.29 0.02 1 41 424 36 ASP CA C 54.29 0.30 1 42 424 36 ASP N N 122.87 0.30 1 43 425 37 GLU H H 8.30 0.02 1 44 425 37 GLU CA C 56.73 0.30 1 45 425 37 GLU N N 121.56 0.30 1 46 426 38 ASN H H 8.36 0.02 1 47 426 38 ASN CA C 53.18 0.30 1 48 426 38 ASN N N 119.28 0.30 1 49 427 39 ASN H H 8.22 0.02 1 50 427 39 ASN CA C 53.16 0.30 1 51 427 39 ASN N N 119.96 0.30 1 52 428 40 VAL H H 8.04 0.02 1 53 428 40 VAL CA C 62.14 0.30 1 54 428 40 VAL N N 120.92 0.30 1 55 429 41 SER H H 8.27 0.02 1 56 429 41 SER CA C 58.04 0.30 1 57 429 41 SER N N 119.65 0.30 1 58 430 42 PHE H H 8.19 0.02 1 59 430 42 PHE CA C 57.69 0.30 1 60 430 42 PHE N N 122.83 0.30 1 61 431 43 SER H H 8.18 0.02 1 62 431 43 SER CA C 58.63 0.30 1 63 431 43 SER N N 117.43 0.30 1 64 434 46 CYS H H 8.34 0.02 1 65 434 46 CYS CA C 58.73 0.30 1 66 434 46 CYS N N 120.67 0.30 1 67 435 47 LEU H H 8.05 0.02 1 68 435 47 LEU CA C 54.56 0.30 1 69 435 47 LEU N N 124.61 0.30 1 70 436 48 VAL H H 8.01 0.02 1 71 436 48 VAL CA C 62.38 0.30 1 72 436 48 VAL N N 120.21 0.30 1 73 437 49 GLY H H 8.37 0.02 1 74 437 49 GLY CA C 44.66 0.30 1 75 437 49 GLY N N 112.28 0.30 1 76 438 50 ASN H H 8.42 0.02 1 77 438 50 ASN CA C 50.48 0.30 1 78 438 50 ASN N N 120.05 0.30 1 79 441 53 LEU H H 6.94 0.02 1 80 441 53 LEU CA C 52.74 0.30 1 81 441 53 LEU N N 119.98 0.30 1 82 442 54 LYS H H 8.60 0.02 1 83 442 54 LYS CA C 54.57 0.30 1 84 442 54 LYS N N 121.67 0.30 1 85 443 55 ASN H H 7.90 0.02 1 86 443 55 ASN CA C 53.80 0.30 1 87 443 55 ASN N N 122.72 0.30 1 88 444 56 ILE H H 9.39 0.02 1 89 444 56 ILE CA C 59.49 0.30 1 90 444 56 ILE N N 120.31 0.30 1 91 445 57 ASN H H 7.42 0.02 1 92 445 57 ASN CA C 51.69 0.30 1 93 445 57 ASN N N 123.45 0.30 1 94 446 58 LEU H H 8.71 0.02 1 95 446 58 LEU CA C 55.20 0.30 1 96 446 58 LEU N N 117.16 0.30 1 97 447 59 ASN H H 7.96 0.02 1 98 447 59 ASN CA C 53.88 0.30 1 99 447 59 ASN N N 120.01 0.30 1 100 448 60 ILE H H 8.90 0.02 1 101 448 60 ILE CA C 57.75 0.30 1 102 448 60 ILE N N 124.97 0.30 1 103 449 61 GLU H H 9.06 0.02 1 104 449 61 GLU CA C 54.73 0.30 1 105 449 61 GLU N N 128.81 0.30 1 106 450 62 LYS H H 8.34 0.02 1 107 450 62 LYS CA C 57.45 0.30 1 108 450 62 LYS N N 120.67 0.30 1 109 451 63 GLY H H 8.81 0.02 1 110 451 63 GLY CA C 44.56 0.30 1 111 451 63 GLY N N 115.02 0.30 1 112 452 64 GLU H H 7.96 0.02 1 113 452 64 GLU CA C 56.05 0.30 1 114 452 64 GLU N N 120.71 0.30 1 115 453 65 MET H H 9.71 0.02 1 116 453 65 MET CA C 53.54 0.30 1 117 453 65 MET N N 119.15 0.30 1 118 454 66 LEU H H 9.05 0.02 1 119 454 66 LEU CA C 52.03 0.30 1 120 454 66 LEU N N 131.06 0.30 1 121 455 67 ALA H H 8.95 0.02 1 122 455 67 ALA CA C 49.26 0.30 1 123 455 67 ALA N N 130.33 0.30 1 124 456 68 ILE H H 9.35 0.02 1 125 456 68 ILE CA C 59.10 0.30 1 126 456 68 ILE N N 122.92 0.30 1 127 457 69 THR H H 9.09 0.02 1 128 457 69 THR CA C 62.20 0.30 1 129 457 69 THR N N 120.81 0.30 1 130 466 78 SER CA C 64.20 0.30 1 131 467 79 LEU H H 8.18 0.02 1 132 467 79 LEU CA C 58.69 0.30 1 133 467 79 LEU N N 124.33 0.30 1 134 468 80 LEU H H 7.26 0.02 1 135 468 80 LEU CA C 57.93 0.30 1 136 468 80 LEU N N 118.64 0.30 1 137 469 81 MET H H 8.35 0.02 1 138 469 81 MET CA C 56.56 0.30 1 139 469 81 MET N N 118.14 0.30 1 140 470 82 LEU H H 7.94 0.02 1 141 470 82 LEU CA C 56.80 0.30 1 142 470 82 LEU N N 123.97 0.30 1 143 471 83 ILE H H 7.35 0.02 1 144 471 83 ILE CA C 64.90 0.30 1 145 471 83 ILE N N 122.44 0.30 1 146 472 84 LEU H H 7.81 0.02 1 147 472 84 LEU CA C 55.62 0.30 1 148 472 84 LEU N N 117.56 0.30 1 149 473 85 GLY H H 7.48 0.02 1 150 473 85 GLY CA C 44.48 0.30 1 151 473 85 GLY N N 105.55 0.30 1 152 474 86 GLU H H 7.56 0.02 1 153 474 86 GLU CA C 56.56 0.30 1 154 474 86 GLU N N 119.50 0.30 1 155 475 87 LEU H H 6.67 0.02 1 156 475 87 LEU CA C 52.59 0.30 1 157 475 87 LEU N N 119.23 0.30 1 158 476 88 GLU H H 8.19 0.02 1 159 476 88 GLU CA C 54.54 0.30 1 160 476 88 GLU N N 123.46 0.30 1 161 477 89 ALA H H 8.79 0.02 1 162 477 89 ALA CA C 51.50 0.30 1 163 477 89 ALA N N 126.14 0.30 1 164 478 90 SER H H 8.84 0.02 1 165 478 90 SER CA C 59.92 0.30 1 166 478 90 SER N N 120.72 0.30 1 167 479 91 GLU H H 7.84 0.02 1 168 479 91 GLU CA C 54.88 0.30 1 169 479 91 GLU N N 119.92 0.30 1 170 480 92 GLY H H 8.28 0.02 1 171 480 92 GLY CA C 44.45 0.30 1 172 480 92 GLY N N 108.94 0.30 1 173 481 93 ILE H H 7.99 0.02 1 174 481 93 ILE CA C 59.37 0.30 1 175 481 93 ILE N N 118.07 0.30 1 176 482 94 ILE H H 8.28 0.02 1 177 482 94 ILE CA C 59.68 0.30 1 178 482 94 ILE N N 125.46 0.30 1 179 483 95 LYS H H 9.10 0.02 1 180 483 95 LYS CA C 54.89 0.30 1 181 483 95 LYS N N 127.46 0.30 1 182 484 96 HIS H H 7.94 0.02 1 183 484 96 HIS CA C 55.96 0.30 1 184 484 96 HIS N N 118.91 0.30 1 185 486 98 GLY CA C 45.03 0.30 1 186 487 99 ARG H H 8.42 0.02 1 187 487 99 ARG CA C 55.30 0.30 1 188 487 99 ARG N N 122.66 0.30 1 189 488 100 VAL H H 8.50 0.02 1 190 488 100 VAL CA C 59.81 0.30 1 191 488 100 VAL N N 125.03 0.30 1 192 489 101 SER H H 8.12 0.02 1 193 489 101 SER CA C 55.48 0.30 1 194 489 101 SER N N 119.24 0.30 1 195 490 102 PHE H H 8.87 0.02 1 196 490 102 PHE CA C 54.97 0.30 1 197 490 102 PHE N N 130.32 0.30 1 198 491 103 CYS H H 8.78 0.02 1 199 491 103 CYS CA C 56.53 0.30 1 200 491 103 CYS N N 130.59 0.30 1 201 492 104 SER H H 8.02 0.02 1 202 492 104 SER CA C 56.82 0.30 1 203 492 104 SER N N 121.64 0.30 1 204 493 105 GLN H H 9.13 0.02 1 205 493 105 GLN N N 123.92 0.30 1 206 494 106 PHE H H 7.88 0.02 1 207 494 106 PHE CA C 55.76 0.30 1 208 494 106 PHE N N 118.61 0.30 1 209 496 108 TRP CA C 55.17 0.30 1 210 497 109 ILE H H 8.71 0.02 1 211 497 109 ILE N N 117.16 0.30 1 212 499 111 PRO CA C 63.01 0.30 1 213 500 112 GLY H H 7.85 0.02 1 214 500 112 GLY CA C 43.55 0.30 1 215 500 112 GLY N N 113.48 0.30 1 216 501 113 THR H H 9.08 0.02 1 217 501 113 THR CA C 60.97 0.30 1 218 501 113 THR N N 111.71 0.30 1 219 502 114 ILE H H 7.75 0.02 1 220 502 114 ILE CA C 66.80 0.30 1 221 502 114 ILE N N 123.00 0.30 1 222 503 115 LYS H H 8.27 0.02 1 223 503 115 LYS CA C 59.81 0.30 1 224 503 115 LYS N N 119.65 0.30 1 225 504 116 GLU H H 8.14 0.02 1 226 504 116 GLU CA C 58.69 0.30 1 227 504 116 GLU N N 117.61 0.30 1 228 505 117 ASN H H 8.22 0.02 1 229 505 117 ASN CA C 57.52 0.30 1 230 505 117 ASN N N 118.19 0.30 1 231 506 118 ILE H H 7.70 0.02 1 232 506 118 ILE CA C 65.19 0.30 1 233 506 118 ILE N N 119.52 0.30 1 234 507 119 ILE H H 8.00 0.02 1 235 507 119 ILE CA C 62.26 0.30 1 236 507 119 ILE N N 111.86 0.30 1 237 508 120 PHE H H 7.56 0.02 1 238 508 120 PHE CA C 58.92 0.30 1 239 508 120 PHE N N 122.22 0.30 1 240 509 121 GLY H H 8.33 0.02 1 241 509 121 GLY N N 109.71 0.30 1 242 510 122 VAL H H 8.17 0.02 1 243 510 122 VAL CA C 60.90 0.30 1 244 510 122 VAL N N 121.88 0.30 1 245 511 123 SER H H 8.22 0.02 1 246 511 123 SER CA C 59.15 0.30 1 247 511 123 SER N N 118.19 0.30 1 248 523 135 ALA CA C 54.95 0.30 1 249 524 136 CYS H H 7.86 0.02 1 250 524 136 CYS CA C 60.68 0.30 1 251 524 136 CYS N N 112.26 0.30 1 252 525 137 GLN H H 7.74 0.02 1 253 525 137 GLN N N 110.28 0.30 1 254 527 139 GLN H H 7.89 0.02 1 255 527 139 GLN N N 123.17 0.30 1 256 528 140 GLN CA C 58.15 0.30 1 257 529 141 ASP H H 7.60 0.02 1 258 529 141 ASP CA C 56.58 0.30 1 259 529 141 ASP N N 118.98 0.30 1 260 531 143 THR H H 7.67 0.02 1 261 531 143 THR CA C 64.43 0.30 1 262 531 143 THR N N 110.31 0.30 1 263 532 144 LYS H H 7.01 0.02 1 264 532 144 LYS CA C 56.57 0.30 1 265 532 144 LYS N N 118.97 0.30 1 266 533 145 PHE H H 7.32 0.02 1 267 533 145 PHE CA C 56.70 0.30 1 268 533 145 PHE N N 120.20 0.30 1 269 534 146 ALA H H 9.25 0.02 1 270 534 146 ALA CA C 55.76 0.30 1 271 534 146 ALA N N 128.90 0.30 1 272 535 147 GLU H H 8.10 0.02 1 273 535 147 GLU CA C 54.61 0.30 1 274 535 147 GLU N N 112.86 0.30 1 275 536 148 GLN H H 8.00 0.02 1 276 536 148 GLN CA C 57.09 0.30 1 277 536 148 GLN N N 116.62 0.30 1 278 537 149 ASP H H 9.03 0.02 1 279 537 149 ASP CA C 55.34 0.30 1 280 537 149 ASP N N 122.40 0.30 1 281 538 150 ASN H H 8.13 0.02 1 282 538 150 ASN CA C 52.40 0.30 1 283 538 150 ASN N N 114.49 0.30 1 284 539 151 THR H H 7.33 0.02 1 285 539 151 THR CA C 64.59 0.30 1 286 539 151 THR N N 119.87 0.30 1 287 540 152 VAL H H 8.47 0.02 1 288 540 152 VAL CA C 63.78 0.30 1 289 540 152 VAL N N 128.97 0.30 1 290 541 153 LEU H H 8.60 0.02 1 291 541 153 LEU CA C 52.66 0.30 1 292 541 153 LEU N N 127.91 0.30 1 293 542 154 GLY H H 8.33 0.02 1 294 542 154 GLY CA C 43.49 0.30 1 295 542 154 GLY N N 108.76 0.30 1 296 545 157 GLY H H 8.22 0.02 1 297 545 157 GLY CA C 44.70 0.30 1 298 545 157 GLY N N 111.11 0.30 1 299 547 159 THR H H 8.39 0.02 1 300 547 159 THR N N 120.99 0.30 1 301 561 173 ALA H H 7.32 0.02 1 302 561 173 ALA CA C 53.96 0.30 1 303 561 173 ALA N N 120.20 0.30 1 304 562 174 VAL H H 8.34 0.02 1 305 562 174 VAL CA C 63.67 0.30 1 306 562 174 VAL N N 116.09 0.30 1 307 563 175 TYR H H 8.76 0.02 1 308 563 175 TYR CA C 61.63 0.30 1 309 563 175 TYR N N 121.62 0.30 1 310 564 176 LYS H H 6.83 0.02 1 311 564 176 LYS CA C 56.70 0.30 1 312 564 176 LYS N N 119.12 0.30 1 313 565 177 ASP H H 8.83 0.02 1 314 565 177 ASP CA C 54.56 0.30 1 315 565 177 ASP N N 127.77 0.30 1 316 566 178 ALA H H 7.82 0.02 1 317 566 178 ALA CA C 49.89 0.30 1 318 566 178 ALA N N 128.51 0.30 1 319 567 179 ASP H H 7.81 0.02 1 320 567 179 ASP N N 117.56 0.30 1 321 570 182 LEU H H 9.17 0.02 1 322 570 182 LEU CA C 52.38 0.30 1 323 570 182 LEU N N 123.99 0.30 1 324 571 183 LEU H H 9.49 0.02 1 325 571 183 LEU CA C 52.66 0.30 1 326 571 183 LEU N N 125.37 0.30 1 327 572 184 ASP H H 8.50 0.02 1 328 572 184 ASP CA C 52.38 0.30 1 329 572 184 ASP N N 127.04 0.30 1 330 581 193 PHE H H 8.02 0.02 1 331 581 193 PHE CA C 60.43 0.30 1 332 581 193 PHE N N 121.64 0.30 1 333 586 198 VAL H H 8.69 0.02 1 334 586 198 VAL N N 120.60 0.30 1 335 588 200 GLU H H 7.81 0.02 1 336 588 200 GLU CA C 58.71 0.30 1 337 588 200 GLU N N 117.65 0.30 1 338 589 201 SER H H 8.71 0.02 1 339 589 201 SER CA C 61.87 0.30 1 340 589 201 SER N N 112.45 0.30 1 341 590 202 CYS H H 9.02 0.02 1 342 590 202 CYS CA C 60.39 0.30 1 343 590 202 CYS N N 121.97 0.30 1 344 591 203 VAL H H 6.97 0.02 1 345 591 203 VAL CA C 66.04 0.30 1 346 591 203 VAL N N 116.88 0.30 1 347 592 204 CYS H H 7.29 0.02 1 348 592 204 CYS CA C 61.15 0.30 1 349 592 204 CYS N N 113.17 0.30 1 350 593 205 LYS H H 6.81 0.02 1 351 593 205 LYS CA C 58.06 0.30 1 352 593 205 LYS N N 117.48 0.30 1 353 594 206 LEU H H 7.89 0.02 1 354 594 206 LEU CA C 58.71 0.30 1 355 594 206 LEU N N 123.17 0.30 1 356 595 207 MET H H 7.19 0.02 1 357 595 207 MET CA C 54.38 0.30 1 358 595 207 MET N N 112.51 0.30 1 359 596 208 ALA H H 6.75 0.02 1 360 596 208 ALA CA C 54.57 0.30 1 361 596 208 ALA N N 119.81 0.30 1 362 597 209 ASN H H 8.46 0.02 1 363 597 209 ASN CA C 52.77 0.30 1 364 597 209 ASN N N 111.45 0.30 1 365 598 210 LYS H H 7.90 0.02 1 366 598 210 LYS CA C 52.55 0.30 1 367 598 210 LYS N N 119.00 0.30 1 368 599 211 THR H H 8.58 0.02 1 369 599 211 THR CA C 63.25 0.30 1 370 599 211 THR N N 123.33 0.30 1 371 600 212 ARG H H 8.98 0.02 1 372 600 212 ARG N N 127.41 0.30 1 373 601 213 ILE H H 9.10 0.02 1 374 601 213 ILE CA C 59.92 0.30 1 375 601 213 ILE N N 122.68 0.30 1 376 602 214 LEU H H 9.24 0.02 1 377 602 214 LEU CA C 52.42 0.30 1 378 602 214 LEU N N 130.71 0.30 1 379 603 215 VAL H H 8.99 0.02 1 380 603 215 VAL CA C 61.27 0.30 1 381 603 215 VAL N N 129.86 0.30 1 382 604 216 THR H H 8.93 0.02 1 383 604 216 THR CA C 58.91 0.30 1 384 604 216 THR N N 122.44 0.30 1 385 611 223 ARG H H 7.72 0.02 1 386 611 223 ARG CA C 58.32 0.30 1 387 611 223 ARG N N 115.76 0.30 1 388 612 224 LYS H H 7.25 0.02 1 389 612 224 LYS CA C 55.54 0.30 1 390 612 224 LYS N N 116.98 0.30 1 391 613 225 ALA H H 7.34 0.02 1 392 613 225 ALA CA C 52.23 0.30 1 393 613 225 ALA N N 123.09 0.30 1 394 614 226 ASP H H 8.76 0.02 1 395 614 226 ASP CA C 57.58 0.30 1 396 614 226 ASP N N 121.09 0.30 1 397 615 227 LYS H H 8.06 0.02 1 398 615 227 LYS CA C 53.68 0.30 1 399 615 227 LYS N N 116.40 0.30 1 400 616 228 ILE H H 8.39 0.02 1 401 616 228 ILE CA C 56.71 0.30 1 402 616 228 ILE N N 123.92 0.30 1 403 618 230 ILE H H 9.39 0.02 1 404 618 230 ILE CA C 59.24 0.30 1 405 618 230 ILE N N 124.84 0.30 1 406 619 231 LEU H H 9.18 0.02 1 407 619 231 LEU CA C 53.15 0.30 1 408 619 231 LEU N N 129.40 0.30 1 409 620 232 HIS H H 8.87 0.02 1 410 620 232 HIS CA C 56.71 0.30 1 411 620 232 HIS N N 116.64 0.30 1 412 621 233 GLN H H 8.68 0.02 1 413 621 233 GLN CA C 56.12 0.30 1 414 621 233 GLN N N 126.41 0.30 1 415 622 234 GLY H H 7.69 0.02 1 416 622 234 GLY CA C 46.79 0.30 1 417 622 234 GLY N N 105.86 0.30 1 418 623 235 SER H H 7.77 0.02 1 419 623 235 SER CA C 56.53 0.30 1 420 623 235 SER N N 113.90 0.30 1 421 624 236 SER H H 9.13 0.02 1 422 624 236 SER CA C 56.74 0.30 1 423 624 236 SER N N 117.07 0.30 1 424 625 237 TYR H H 9.49 0.02 1 425 625 237 TYR CA C 59.65 0.30 1 426 625 237 TYR N N 134.13 0.30 1 427 626 238 PHE H H 7.81 0.02 1 428 626 238 PHE CA C 58.71 0.30 1 429 626 238 PHE N N 117.56 0.30 1 430 627 239 TYR H H 7.02 0.02 1 431 627 239 TYR CA C 55.31 0.30 1 432 627 239 TYR N N 128.91 0.30 1 433 628 240 GLY H H 7.85 0.02 1 434 628 240 GLY CA C 44.89 0.30 1 435 628 240 GLY N N 116.02 0.30 1 436 629 241 THR H H 8.85 0.02 1 437 629 241 THR CA C 60.31 0.30 1 438 629 241 THR N N 114.38 0.30 1 439 630 242 PHE H H 9.29 0.02 1 440 630 242 PHE CA C 62.22 0.30 1 441 630 242 PHE N N 122.88 0.30 1 442 631 243 SER H H 8.65 0.02 1 443 631 243 SER CA C 61.31 0.30 1 444 631 243 SER N N 113.90 0.30 1 445 632 244 GLU H H 7.66 0.02 1 446 632 244 GLU CA C 58.09 0.30 1 447 632 244 GLU N N 122.89 0.30 1 448 633 245 LEU H H 7.97 0.02 1 449 633 245 LEU CA C 57.73 0.30 1 450 633 245 LEU N N 124.35 0.30 1 451 640 252 PHE H H 8.00 0.02 1 452 640 252 PHE CA C 60.68 0.30 1 453 640 252 PHE N N 123.38 0.30 1 454 641 253 SER H H 8.26 0.02 1 455 641 253 SER CA C 61.91 0.30 1 456 641 253 SER N N 113.24 0.30 1 457 642 254 SER H H 8.13 0.02 1 458 642 254 SER CA C 61.06 0.30 1 459 642 254 SER N N 116.58 0.30 1 460 643 255 LYS H H 7.34 0.02 1 461 643 255 LYS CA C 57.11 0.30 1 462 643 255 LYS N N 121.95 0.30 1 463 644 256 LEU H H 7.42 0.02 1 464 644 256 LEU CA C 56.87 0.30 1 465 644 256 LEU N N 119.52 0.30 1 466 645 257 MET H H 8.18 0.02 1 467 645 257 MET CA C 56.33 0.30 1 468 645 257 MET N N 114.91 0.30 1 469 646 258 GLY H H 7.44 0.02 1 470 646 258 GLY N N 106.54 0.30 1 471 647 259 TYR H H 7.21 0.02 1 472 647 259 TYR CA C 57.11 0.30 1 473 647 259 TYR N N 120.28 0.30 1 474 652 264 GLN H H 7.84 0.02 1 475 652 264 GLN CA C 55.37 0.30 1 476 652 264 GLN N N 116.47 0.30 1 477 653 265 PHE H H 7.35 0.02 1 478 653 265 PHE CA C 53.98 0.30 1 479 653 265 PHE N N 121.07 0.30 1 480 654 266 THR H H 8.22 0.02 1 481 654 266 THR CA C 61.19 0.30 1 482 654 266 THR N N 111.11 0.30 1 483 655 267 GLU H H 8.91 0.02 1 484 655 267 GLU CA C 59.48 0.30 1 485 655 267 GLU N N 123.10 0.30 1 486 656 268 GLU H H 8.72 0.02 1 487 656 268 GLU CA C 59.15 0.30 1 488 656 268 GLU N N 119.15 0.30 1 489 657 269 ARG H H 7.61 0.02 1 490 657 269 ARG CA C 58.07 0.30 1 491 657 269 ARG N N 122.95 0.30 1 492 669 281 PHE H H 7.59 0.02 1 493 669 281 PHE CA C 57.92 0.30 1 494 669 281 PHE N N 116.35 0.30 1 495 670 282 SER H H 7.79 0.02 1 496 670 282 SER CA C 58.43 0.30 1 497 670 282 SER N N 117.14 0.30 1 498 671 283 VAL H H 8.17 0.02 1 499 671 283 VAL CA C 61.66 0.30 1 500 671 283 VAL N N 121.88 0.30 1 501 672 284 ASP H H 8.40 0.02 1 502 672 284 ASP CA C 54.14 0.30 1 503 672 284 ASP N N 125.16 0.30 1 504 673 285 ASP H H 7.95 0.02 1 505 673 285 ASP CA C 55.61 0.30 1 506 673 285 ASP N N 127.25 0.30 1 stop_ save_