data_16394 ####################### # 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 16394 _BMRB_flat_file_name bmr16394.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 delta F508 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" 114 "15N chemical shifts" 114 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' 2009-12-14 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16393 '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 'deltaF508 CFTR NBD1-RE monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'deltaF508 CFTR NBD1-RE' $entity stop_ _System_molecular_weight 31847.3 _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 'deltaF508 CFTR NBD1-RE' _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'chloride channel' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 284 _Mol_residue_sequence ; TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIG VSYDEYRYKSVVKACQLQQD ITKFAEQDNTVLGEGGVTLS GGQRARISLARAVYKDADLY LLDSPFGYLDVFTEEQVFES CVCKLMANKTRILVTSKMEH LRKADKILILHQGSSYFYGT FSELQSLRPDFSSKLMGYDT FDQFTEERRSSILTETLRRF SVDD ; 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 120 509 GLY 121 510 VAL 122 511 SER 123 512 TYR 124 513 ASP 125 514 GLU 126 515 TYR 127 516 ARG 128 517 TYR 129 518 LYS 130 519 SER 131 520 VAL 132 521 VAL 133 522 LYS 134 523 ALA 135 524 CYS 136 525 GLN 137 526 LEU 138 527 GLN 139 528 GLN 140 529 ASP 141 530 ILE 142 531 THR 143 532 LYS 144 533 PHE 145 534 ALA 146 535 GLU 147 536 GLN 148 537 ASP 149 538 ASN 150 539 THR 151 540 VAL 152 541 LEU 153 542 GLY 154 543 GLU 155 544 GLY 156 545 GLY 157 546 VAL 158 547 THR 159 548 LEU 160 549 SER 161 550 GLY 162 551 GLY 163 552 GLN 164 553 ARG 165 554 ALA 166 555 ARG 167 556 ILE 168 557 SER 169 558 LEU 170 559 ALA 171 560 ARG 172 561 ALA 173 562 VAL 174 563 TYR 175 564 LYS 176 565 ASP 177 566 ALA 178 567 ASP 179 568 LEU 180 569 TYR 181 570 LEU 182 571 LEU 183 572 ASP 184 573 SER 185 574 PRO 186 575 PHE 187 576 GLY 188 577 TYR 189 578 LEU 190 579 ASP 191 580 VAL 192 581 PHE 193 582 THR 194 583 GLU 195 584 GLU 196 585 GLN 197 586 VAL 198 587 PHE 199 588 GLU 200 589 SER 201 590 CYS 202 591 VAL 203 592 CYS 204 593 LYS 205 594 LEU 206 595 MET 207 596 ALA 208 597 ASN 209 598 LYS 210 599 THR 211 600 ARG 212 601 ILE 213 602 LEU 214 603 VAL 215 604 THR 216 605 SER 217 606 LYS 218 607 MET 219 608 GLU 220 609 HIS 221 610 LEU 222 611 ARG 223 612 LYS 224 613 ALA 225 614 ASP 226 615 LYS 227 616 ILE 228 617 LEU 229 618 ILE 230 619 LEU 231 620 HIS 232 621 GLN 233 622 GLY 234 623 SER 235 624 SER 236 625 TYR 237 626 PHE 238 627 TYR 239 628 GLY 240 629 THR 241 630 PHE 242 631 SER 243 632 GLU 244 633 LEU 245 634 GLN 246 635 SER 247 636 LEU 248 637 ARG 249 638 PRO 250 639 ASP 251 640 PHE 252 641 SER 253 642 SER 254 643 LYS 255 644 LEU 256 645 MET 257 646 GLY 258 647 TYR 259 648 ASP 260 649 THR 261 650 PHE 262 651 ASP 263 652 GLN 264 653 PHE 265 654 THR 266 655 GLU 267 656 GLU 268 657 ARG 269 658 ARG 270 659 SER 271 660 SER 272 661 ILE 273 662 LEU 274 663 THR 275 664 GLU 276 665 THR 277 666 LEU 278 667 ARG 279 668 ARG 280 669 PHE 281 670 SER 282 671 VAL 283 672 ASP 284 673 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-06 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 100.35 285 98.60 98.95 0.00e+00 BMRB 16393 "CFTR NBD1-RE" 100.35 285 99.65 99.65 0.00e+00 PDB 1Q3H "Mouse Cftr Nbd1 With Amp.Pnp" 100.35 286 99.65 99.65 0.00e+00 PDB 1R0W "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) Apo" 100.35 286 99.65 99.65 0.00e+00 PDB 1R0X "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp" 100.35 286 99.65 99.65 0.00e+00 PDB 1R0Y "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Adp" 100.35 286 99.65 99.65 0.00e+00 PDB 1R0Z "Phosphorylated Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide-Binding Domain One (Nbd1) With Atp" 100.35 286 98.25 98.25 0.00e+00 PDB 1R10 "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp, I4122 Space Group" 100.35 286 99.65 99.65 0.00e+00 PDB 1XF9 "Structure Of Nbd1 From Murine Cftr- F508s Mutant" 99.30 283 99.65 99.65 0.00e+00 PDB 1XFA "Structure Of Nbd1 From Murine Cftr- F508r Mutant" 99.30 283 99.65 99.65 0.00e+00 PDB 3SI7 "The Crystal Structure Of The Nbd1 Domain Of The Mouse Cftr Protein, Deltaf508 Mutant" 100.00 285 100.00 100.00 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' . 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 175 mM '[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' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_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_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_ ####################### # 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 H 1 'methyl protons' ppm 0 internal direct . . . 1.0000 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 . loop_ _Experiment_label '2D 1H-15N HSQC' 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 'deltaF508 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 N N 117.19 0.30 1 3 391 3 GLY H H 8.62 0.02 1 4 391 3 GLY N N 114.49 0.30 1 5 392 4 ILE H H 8.58 0.02 1 6 392 4 ILE N N 120.43 0.30 1 7 393 5 ILE H H 8.54 0.02 1 8 393 5 ILE N N 126.69 0.30 1 9 394 6 MET H H 8.90 0.02 1 10 394 6 MET N N 124.25 0.30 1 11 395 7 GLU H H 9.19 0.02 1 12 395 7 GLU N N 125.27 0.30 1 13 397 9 VAL H H 8.54 0.02 1 14 397 9 VAL N N 121.24 0.30 1 15 399 11 ALA H H 8.67 0.02 1 16 399 11 ALA N N 127.82 0.30 1 17 401 13 TRP H H 8.81 0.02 1 18 401 13 TRP N N 122.50 0.30 1 19 423 35 SER H H 8.48 0.02 1 20 423 35 SER N N 118.83 0.30 1 21 425 37 GLU H H 8.31 0.02 1 22 425 37 GLU N N 121.62 0.30 1 23 426 38 ASN H H 8.36 0.02 1 24 426 38 ASN N N 119.33 0.30 1 25 427 39 ASN H H 8.21 0.02 1 26 427 39 ASN N N 120.03 0.30 1 27 430 42 PHE H H 8.19 0.02 1 28 430 42 PHE N N 122.92 0.30 1 29 431 43 SER H H 8.18 0.02 1 30 431 43 SER N N 117.57 0.30 1 31 435 47 LEU H H 8.05 0.02 1 32 435 47 LEU N N 124.74 0.30 1 33 438 50 ASN H H 8.40 0.02 1 34 438 50 ASN N N 120.14 0.30 1 35 441 53 LEU H H 6.95 0.02 1 36 441 53 LEU N N 120.10 0.30 1 37 442 54 LYS H H 8.59 0.02 1 38 442 54 LYS N N 121.75 0.30 1 39 443 55 ASN H H 7.89 0.02 1 40 443 55 ASN N N 122.72 0.30 1 41 444 56 ILE H H 9.38 0.02 1 42 444 56 ILE N N 120.37 0.30 1 43 445 57 ASN H H 7.42 0.02 1 44 445 57 ASN N N 123.51 0.30 1 45 449 61 GLU H H 9.06 0.02 1 46 449 61 GLU N N 128.89 0.30 1 47 451 63 GLY H H 8.81 0.02 1 48 451 63 GLY N N 114.96 0.30 1 49 452 64 GLU H H 7.95 0.02 1 50 452 64 GLU N N 120.73 0.30 1 51 453 65 MET H H 9.70 0.02 1 52 453 65 MET N N 119.15 0.30 1 53 454 66 LEU H H 9.04 0.02 1 54 454 66 LEU N N 131.11 0.30 1 55 455 67 ALA H H 8.95 0.02 1 56 455 67 ALA N N 130.40 0.30 1 57 456 68 ILE H H 9.34 0.02 1 58 456 68 ILE N N 122.93 0.30 1 59 467 79 LEU H H 8.18 0.02 1 60 467 79 LEU N N 124.31 0.30 1 61 468 80 LEU H H 7.24 0.02 1 62 468 80 LEU N N 118.65 0.30 1 63 469 81 MET H H 8.32 0.02 1 64 469 81 MET N N 118.07 0.30 1 65 470 82 LEU H H 7.92 0.02 1 66 470 82 LEU N N 124.03 0.30 1 67 471 83 ILE H H 7.34 0.02 1 68 471 83 ILE N N 122.47 0.30 1 69 473 85 GLY H H 7.47 0.02 1 70 473 85 GLY N N 105.74 0.30 1 71 474 86 GLU H H 7.56 0.02 1 72 474 86 GLU N N 119.47 0.30 1 73 475 87 LEU H H 6.67 0.02 1 74 475 87 LEU N N 119.17 0.30 1 75 476 88 GLU H H 8.16 0.02 1 76 476 88 GLU N N 123.51 0.30 1 77 477 89 ALA H H 8.79 0.02 1 78 477 89 ALA N N 126.22 0.30 1 79 478 90 SER H H 8.84 0.02 1 80 478 90 SER N N 120.82 0.30 1 81 479 91 GLU H H 7.83 0.02 1 82 479 91 GLU N N 119.94 0.30 1 83 480 92 GLY H H 8.28 0.02 1 84 480 92 GLY N N 109.00 0.30 1 85 481 93 ILE H H 8.00 0.02 1 86 481 93 ILE N N 118.19 0.30 1 87 482 94 ILE H H 8.28 0.02 1 88 482 94 ILE N N 125.60 0.30 1 89 483 95 LYS H H 9.09 0.02 1 90 483 95 LYS N N 127.55 0.30 1 91 487 99 ARG H H 8.42 0.02 1 92 487 99 ARG N N 122.69 0.30 1 93 488 100 VAL H H 8.50 0.02 1 94 488 100 VAL N N 125.31 0.30 1 95 490 102 PHE H H 8.90 0.02 1 96 490 102 PHE N N 130.39 0.30 1 97 494 106 PHE H H 7.86 0.02 1 98 494 106 PHE N N 118.68 0.30 1 99 500 112 GLY H H 7.85 0.02 1 100 500 112 GLY N N 113.28 0.30 1 101 501 113 THR H H 9.04 0.02 1 102 501 113 THR N N 111.75 0.30 1 103 502 114 ILE H H 7.76 0.02 1 104 502 114 ILE N N 122.99 0.30 1 105 529 140 ASP H H 7.55 0.02 1 106 529 140 ASP N N 119.00 0.30 1 107 532 143 LYS H H 7.03 0.02 1 108 532 143 LYS N N 119.14 0.30 1 109 534 145 ALA H H 9.25 0.02 1 110 534 145 ALA N N 129.10 0.30 1 111 535 146 GLU H H 8.09 0.02 1 112 535 146 GLU N N 113.09 0.30 1 113 536 147 GLN H H 7.98 0.02 1 114 536 147 GLN N N 116.65 0.30 1 115 538 149 ASN H H 8.09 0.02 1 116 538 149 ASN N N 114.72 0.30 1 117 539 150 THR H H 7.27 0.02 1 118 539 150 THR N N 119.77 0.30 1 119 540 151 VAL H H 8.47 0.02 1 120 540 151 VAL N N 129.19 0.30 1 121 542 153 GLY H H 8.34 0.02 1 122 542 153 GLY N N 108.85 0.30 1 123 566 177 ALA H H 7.76 0.02 1 124 566 177 ALA N N 128.84 0.30 1 125 570 181 LEU H H 9.19 0.02 1 126 570 181 LEU N N 123.97 0.30 1 127 571 182 LEU H H 9.51 0.02 1 128 571 182 LEU N N 125.52 0.30 1 129 572 183 ASP H H 8.52 0.02 1 130 572 183 ASP N N 127.10 0.30 1 131 586 197 VAL H H 8.70 0.02 1 132 586 197 VAL N N 120.63 0.30 1 133 589 200 SER H H 8.71 0.02 1 134 589 200 SER N N 112.58 0.30 1 135 590 201 CYS H H 9.02 0.02 1 136 590 201 CYS N N 121.86 0.30 1 137 591 202 VAL H H 6.99 0.02 1 138 591 202 VAL N N 117.06 0.30 1 139 592 203 CYS H H 7.28 0.02 1 140 592 203 CYS N N 113.23 0.30 1 141 593 204 LYS H H 6.82 0.02 1 142 593 204 LYS N N 117.58 0.30 1 143 595 206 MET H H 7.19 0.02 1 144 595 206 MET N N 112.61 0.30 1 145 596 207 ALA H H 6.74 0.02 1 146 596 207 ALA N N 119.90 0.30 1 147 597 208 ASN H H 8.44 0.02 1 148 597 208 ASN N N 111.47 0.30 1 149 599 210 THR H H 8.57 0.02 1 150 599 210 THR N N 123.33 0.30 1 151 601 212 ILE H H 9.10 0.02 1 152 601 212 ILE N N 122.63 0.30 1 153 602 213 LEU H H 9.23 0.02 1 154 602 213 LEU N N 130.75 0.30 1 155 603 214 VAL H H 8.99 0.02 1 156 603 214 VAL N N 129.91 0.30 1 157 604 215 THR H H 8.93 0.02 1 158 604 215 THR N N 122.61 0.30 1 159 611 222 ARG H H 7.72 0.02 1 160 611 222 ARG N N 115.88 0.30 1 161 612 223 LYS H H 7.25 0.02 1 162 612 223 LYS N N 117.06 0.30 1 163 613 224 ALA H H 7.32 0.02 1 164 613 224 ALA N N 123.11 0.30 1 165 614 225 ASP H H 8.75 0.02 1 166 614 225 ASP N N 121.00 0.30 1 167 615 226 LYS H H 8.06 0.02 1 168 615 226 LYS N N 116.46 0.30 1 169 618 229 ILE H H 8.88 0.02 1 170 618 229 ILE N N 124.47 0.30 1 171 619 230 LEU H H 9.17 0.02 1 172 619 230 LEU N N 129.40 0.30 1 173 620 231 HIS H H 8.86 0.02 1 174 620 231 HIS N N 116.67 0.30 1 175 621 232 GLN H H 8.66 0.02 1 176 621 232 GLN N N 126.50 0.30 1 177 622 233 GLY H H 7.74 0.02 1 178 622 233 GLY N N 106.02 0.30 1 179 623 234 SER H H 7.77 0.02 1 180 623 234 SER N N 114.00 0.30 1 181 624 235 SER H H 9.12 0.02 1 182 624 235 SER N N 117.14 0.30 1 183 625 236 TYR H H 9.47 0.02 1 184 625 236 TYR N N 134.14 0.30 1 185 627 238 TYR H H 7.01 0.02 1 186 627 238 TYR N N 129.00 0.30 1 187 628 239 GLY H H 7.84 0.02 1 188 628 239 GLY N N 116.06 0.30 1 189 629 240 THR H H 8.86 0.02 1 190 629 240 THR N N 114.42 0.30 1 191 630 241 PHE H H 9.28 0.02 1 192 630 241 PHE N N 122.94 0.30 1 193 631 242 SER H H 8.64 0.02 1 194 631 242 SER N N 113.97 0.30 1 195 632 243 GLU H H 7.66 0.02 1 196 632 243 GLU N N 122.94 0.30 1 197 633 244 LEU H H 7.97 0.02 1 198 633 244 LEU N N 124.41 0.30 1 199 640 251 PHE H H 7.99 0.02 1 200 640 251 PHE N N 123.38 0.30 1 201 641 252 SER H H 8.26 0.02 1 202 641 252 SER N N 113.30 0.30 1 203 642 253 SER H H 8.13 0.02 1 204 642 253 SER N N 116.69 0.30 1 205 643 254 LYS H H 7.33 0.02 1 206 643 254 LYS N N 122.02 0.30 1 207 644 255 LEU H H 7.42 0.02 1 208 644 255 LEU N N 119.57 0.30 1 209 645 256 MET H H 8.19 0.02 1 210 645 256 MET N N 114.99 0.30 1 211 646 257 GLY H H 7.42 0.02 1 212 646 257 GLY N N 106.58 0.30 1 213 652 263 GLN H H 7.83 0.02 1 214 652 263 GLN N N 116.54 0.30 1 215 653 264 PHE H H 7.33 0.02 1 216 653 264 PHE N N 121.16 0.30 1 217 655 266 GLU H H 8.91 0.02 1 218 655 266 GLU N N 123.17 0.30 1 219 656 267 GLU H H 8.74 0.02 1 220 656 267 GLU N N 119.16 0.30 1 221 657 268 ARG H H 7.62 0.02 1 222 657 268 ARG N N 123.09 0.30 1 223 669 280 PHE H H 7.57 0.02 1 224 669 280 PHE N N 116.34 0.30 1 225 672 283 ASP H H 8.40 0.02 1 226 672 283 ASP N N 125.25 0.30 1 227 673 284 ASP H H 7.94 0.02 1 228 673 284 ASP N N 127.33 0.30 1 stop_ save_