data_19083 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for Mutant SENP1 C603S Catalytic Domain ; _BMRB_accession_number 19083 _BMRB_flat_file_name bmr19083.str _Entry_type original _Submission_date 2013-03-10 _Accession_date 2013-03-10 _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 Namanja Andrew T. . 2 Chen Chih-Hong . . 3 Chen Yuan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 275 "13C chemical shifts" 447 "15N chemical shifts" 216 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-02 update BMRB 'add related entry loop' 2014-02-07 update BMRB 'update entry citation' 2013-06-04 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19885 'Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23614497 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Madu Ikenna G. . 2 Namanja Andrew T. . 3 Su Yang . . 4 Wong Steven . . 5 Li Yi-Jia . . 6 Chen Yuan . . stop_ _Journal_abbreviation 'ACS Chem. Biol.' _Journal_name_full 'ACS chemical biology' _Journal_volume 8 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1435 _Page_last 1441 _Year 2013 _Details . loop_ _Keyword 'Enzyme kinetics' Inhibitor NMR SENP SUMO stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SENP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SENP1 $SENP1 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_SENP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SENP1 _Molecular_mass 28608 _Mol_thiol_state 'all free' loop_ _Biological_function 'SUMO1/sentrin specific peptidase 1' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 240 _Mol_residue_sequence ; MHHHHHHENLYFQGEFPEIT EEMEKEIKNVFRNGNQDEVL SEAFRLTITRKDIQTLNHLN WLNDEIINFYMNMLMERSKE KGLPSVHAFNTFFFTKLKTA GYQAVKRWTKKVDVFSVDIL LVPIHLGVHWCLAVVDFRKK NITYYDSMGGINNEACRILL QYLKQESIDKKRKEFDTNGW QLFSKKSQEIPQQMNGSDSG MFACKYADCITKDRPINFTQ QHMPYFRKRMVWEILHRKLL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 405 MET 2 406 HIS 3 407 HIS 4 408 HIS 5 409 HIS 6 410 HIS 7 411 HIS 8 412 GLU 9 413 ASN 10 414 LEU 11 415 TYR 12 416 PHE 13 417 GLN 14 418 GLY 15 419 GLU 16 420 PHE 17 421 PRO 18 422 GLU 19 423 ILE 20 424 THR 21 425 GLU 22 426 GLU 23 427 MET 24 428 GLU 25 429 LYS 26 430 GLU 27 431 ILE 28 432 LYS 29 433 ASN 30 434 VAL 31 435 PHE 32 436 ARG 33 437 ASN 34 438 GLY 35 439 ASN 36 440 GLN 37 441 ASP 38 442 GLU 39 443 VAL 40 444 LEU 41 445 SER 42 446 GLU 43 447 ALA 44 448 PHE 45 449 ARG 46 450 LEU 47 451 THR 48 452 ILE 49 453 THR 50 454 ARG 51 455 LYS 52 456 ASP 53 457 ILE 54 458 GLN 55 459 THR 56 460 LEU 57 461 ASN 58 462 HIS 59 463 LEU 60 464 ASN 61 465 TRP 62 466 LEU 63 467 ASN 64 468 ASP 65 469 GLU 66 470 ILE 67 471 ILE 68 472 ASN 69 473 PHE 70 474 TYR 71 475 MET 72 476 ASN 73 477 MET 74 478 LEU 75 479 MET 76 480 GLU 77 481 ARG 78 482 SER 79 483 LYS 80 484 GLU 81 485 LYS 82 486 GLY 83 487 LEU 84 488 PRO 85 489 SER 86 490 VAL 87 491 HIS 88 492 ALA 89 493 PHE 90 494 ASN 91 495 THR 92 496 PHE 93 497 PHE 94 498 PHE 95 499 THR 96 500 LYS 97 501 LEU 98 502 LYS 99 503 THR 100 504 ALA 101 505 GLY 102 506 TYR 103 507 GLN 104 508 ALA 105 509 VAL 106 510 LYS 107 511 ARG 108 512 TRP 109 513 THR 110 514 LYS 111 515 LYS 112 516 VAL 113 517 ASP 114 518 VAL 115 519 PHE 116 520 SER 117 521 VAL 118 522 ASP 119 523 ILE 120 524 LEU 121 525 LEU 122 526 VAL 123 527 PRO 124 528 ILE 125 529 HIS 126 530 LEU 127 531 GLY 128 532 VAL 129 533 HIS 130 534 TRP 131 535 CYS 132 536 LEU 133 537 ALA 134 538 VAL 135 539 VAL 136 540 ASP 137 541 PHE 138 542 ARG 139 543 LYS 140 544 LYS 141 545 ASN 142 546 ILE 143 547 THR 144 548 TYR 145 549 TYR 146 550 ASP 147 551 SER 148 552 MET 149 553 GLY 150 554 GLY 151 555 ILE 152 556 ASN 153 557 ASN 154 558 GLU 155 559 ALA 156 560 CYS 157 561 ARG 158 562 ILE 159 563 LEU 160 564 LEU 161 565 GLN 162 566 TYR 163 567 LEU 164 568 LYS 165 569 GLN 166 570 GLU 167 571 SER 168 572 ILE 169 573 ASP 170 574 LYS 171 575 LYS 172 576 ARG 173 577 LYS 174 578 GLU 175 579 PHE 176 580 ASP 177 581 THR 178 582 ASN 179 583 GLY 180 584 TRP 181 585 GLN 182 586 LEU 183 587 PHE 184 588 SER 185 589 LYS 186 590 LYS 187 591 SER 188 592 GLN 189 593 GLU 190 594 ILE 191 595 PRO 192 596 GLN 193 597 GLN 194 598 MET 195 599 ASN 196 600 GLY 197 601 SER 198 602 ASP 199 603 SER 200 604 GLY 201 605 MET 202 606 PHE 203 607 ALA 204 608 CYS 205 609 LYS 206 610 TYR 207 611 ALA 208 612 ASP 209 613 CYS 210 614 ILE 211 615 THR 212 616 LYS 213 617 ASP 214 618 ARG 215 619 PRO 216 620 ILE 217 621 ASN 218 622 PHE 219 623 THR 220 624 GLN 221 625 GLN 222 626 HIS 223 627 MET 224 628 PRO 225 629 TYR 226 630 PHE 227 631 ARG 228 632 LYS 229 633 ARG 230 634 MET 231 635 VAL 232 636 TRP 233 637 GLU 234 638 ILE 235 639 LEU 236 640 HIS 237 641 ARG 238 642 LYS 239 643 LEU 240 644 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 19885 SENP1 100.00 240 99.58 99.58 1.13e-178 PDB 2CKG "The Structure Of Senp1 Sumo-2 Co-Complex Suggests A Structural Basis For Discrimination Between Sumo Paralogues During Processi" 94.17 225 99.12 99.12 7.69e-164 PDB 2CKH "Senp1-sumo2 Complex" 94.17 225 99.12 99.12 7.69e-164 PDB 2G4D "Crystal Structure Of Human Senp1 Mutant (C603s) In Complex With Sumo-1" 85.42 205 100.00 100.00 9.56e-151 PDB 2IY0 "Senp1 (Mutant) Sumo1 Rangap" 94.17 226 99.56 100.00 6.16e-167 PDB 2IY1 "Senp1 (Mutant) Full Length Sumo1" 94.17 226 99.56 100.00 6.16e-167 PDB 2IYC "Senp1 Native Structure" 94.17 226 99.56 99.56 1.90e-166 PDB 2IYD "Senp1 Covalent Complex With Sumo-2" 94.17 226 99.56 99.56 1.90e-166 PDB 2XPH "Crystal Structure Of Human Senp1 With The Bound Cobalt" 95.00 238 98.68 99.12 1.44e-166 PDB 2XRE "Detection Of Cobalt In Previously Unassigned Human Senp1 Structure" 95.00 230 98.68 99.12 2.08e-166 DBJ BAC26011 "unnamed protein product [Mus musculus]" 95.00 640 96.93 98.68 7.98e-162 DBJ BAC26106 "unnamed protein product [Mus musculus]" 95.00 319 96.93 98.68 3.11e-165 DBJ BAF84749 "unnamed protein product [Homo sapiens]" 95.00 644 98.68 99.12 1.63e-164 EMBL CAH90949 "hypothetical protein [Pongo abelii]" 95.00 645 98.68 99.12 1.56e-164 GB AAF31171 "sentrin/SUMO-specific protease [Homo sapiens]" 95.00 643 98.25 98.68 5.49e-162 GB AAH23129 "SUMO1/sentrin specific peptidase 1 [Mus musculus]" 95.00 640 96.93 98.68 7.98e-162 GB AAH45639 "SUMO1/sentrin specific peptidase 1 [Homo sapiens]" 95.00 644 98.68 99.12 1.35e-164 GB AIC60034 "SENP1, partial [synthetic construct]" 95.00 644 98.68 99.12 1.35e-164 GB EAW57971 "SUMO1/sentrin specific peptidase 1, isoform CRA_a [Homo sapiens]" 95.00 675 98.25 98.68 1.79e-161 REF NP_001129011 "sentrin-specific protease 1 [Pongo abelii]" 95.00 645 98.68 99.12 1.56e-164 REF NP_001193805 "sentrin-specific protease 1 [Bos taurus]" 95.00 645 97.81 98.68 3.96e-163 REF NP_001254523 "sentrin-specific protease 1 [Homo sapiens]" 95.00 644 98.68 99.12 1.63e-164 REF NP_001254524 "sentrin-specific protease 1 [Homo sapiens]" 95.00 644 98.68 99.12 1.63e-164 REF NP_659100 "sentrin-specific protease 1 [Mus musculus]" 95.00 640 96.93 98.68 7.98e-162 SP P59110 "RecName: Full=Sentrin-specific protease 1; AltName: Full=SUMO-1 protease 2; Short=SuPr-2; AltName: Full=Sentrin/SUMO-specific p" 95.00 640 96.93 98.68 7.98e-162 SP Q5RBB1 "RecName: Full=Sentrin-specific protease 1; AltName: Full=Sentrin/SUMO-specific protease SENP1" 95.00 645 98.68 99.12 1.56e-164 SP Q9P0U3 "RecName: Full=Sentrin-specific protease 1; AltName: Full=Sentrin/SUMO-specific protease SENP1" 95.00 644 98.68 99.12 1.63e-164 TPG DAA29877 "TPA: SUMO1/sentrin specific peptidase 1 [Bos taurus]" 95.00 646 97.81 98.68 3.54e-163 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SENP1 Humans 9606 Eukaryota Metazoa Homo sapiens 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 _Details $SENP1 'recombinant technology' . Escherichia coli BL21(DE3) pET11 'C603S mutant' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'For stereospecific assignments of Val/Leu methyls' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 20 mM 'natural abundance' DTT 5 mM 'natural abundance' NaN3 0.03 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' $SENP1 . mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'TXI cryoprobe' 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_ save_3D_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_2D_HMCM-VAL_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HMCM-VAL' _Sample_label $sample_1 save_ save_2D_HMCM-LEU_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HMCM-LEU' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20mM Sodium Phosphate pH 6.8, 5mM DTT, 0.03% NaN3' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 pH pressure 1 . atm temperature 295 0.1 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HN(COCA)CB' '3D HNCA' '3D HN(CO)CA' '3D H(CCO)NH' '2D 1H-13C HSQC' '3D HCCH-TOCSY' '2D HMCM-VAL' '2D HMCM-LEU' 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 SENP1 _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 1 419 15 GLU H H 8.050 0.006 . 2 419 15 GLU CA C 56.645 0.087 . 3 419 15 GLU CB C 29.358 0.060 . 4 419 15 GLU N N 120.259 0.050 . 5 420 16 PHE H H 8.022 0.003 . 6 420 16 PHE CA C 54.895 0.060 . 7 420 16 PHE CB C 37.877 0.060 . 8 420 16 PHE N N 118.721 0.024 . 9 422 18 GLU H H 8.630 0.008 . 10 422 18 GLU CB C 29.492 0.060 . 11 422 18 GLU N N 124.101 0.049 . 12 423 19 ILE H H 8.517 0.004 . 13 423 19 ILE CA C 60.796 0.063 . 14 423 19 ILE CB C 35.409 0.060 . 15 423 19 ILE N N 122.103 0.023 . 16 424 20 THR H H 7.625 0.007 . 17 424 20 THR CB C 70.306 0.060 . 18 424 20 THR N N 121.249 0.039 . 19 425 21 GLU H H 8.912 0.010 . 20 425 21 GLU CA C 59.684 0.060 . 21 425 21 GLU CB C 28.421 0.060 . 22 425 21 GLU N N 120.991 0.049 . 23 426 22 GLU H H 8.420 0.009 . 24 426 22 GLU CA C 59.444 0.060 . 25 426 22 GLU N N 118.167 0.038 . 26 427 23 MET H H 7.356 0.002 . 27 427 23 MET CB C 33.322 0.060 . 28 427 23 MET N N 119.294 0.014 . 29 428 24 GLU H H 8.594 0.008 . 30 428 24 GLU CA C 59.192 0.060 . 31 428 24 GLU CB C 28.381 0.060 . 32 428 24 GLU N N 118.656 0.063 . 33 429 25 LYS H H 7.859 0.006 . 34 429 25 LYS CA C 59.593 0.073 . 35 429 25 LYS CB C 31.424 0.060 . 36 429 25 LYS N N 118.262 0.021 . 37 430 26 GLU H H 7.327 0.006 . 38 430 26 GLU CA C 59.460 0.030 . 39 430 26 GLU CB C 29.610 0.060 . 40 430 26 GLU N N 119.083 0.074 . 41 431 27 ILE H H 8.080 0.004 . 42 431 27 ILE CA C 64.619 0.016 . 43 431 27 ILE CB C 38.119 0.060 . 44 431 27 ILE N N 119.848 0.051 . 45 432 28 LYS H H 8.329 0.014 . 46 432 28 LYS CA C 59.437 0.029 . 47 432 28 LYS CB C 31.305 0.060 . 48 432 28 LYS N N 116.341 0.037 . 49 433 29 ASN H H 7.621 0.004 . 50 433 29 ASN CA C 55.826 0.005 . 51 433 29 ASN CB C 37.892 0.060 . 52 433 29 ASN N N 115.069 0.034 . 53 434 30 VAL H H 7.542 0.002 . 54 434 30 VAL HG1 H 0.784 0.004 . 55 434 30 VAL HG2 H 0.780 0.003 . 56 434 30 VAL CA C 64.195 0.085 . 57 434 30 VAL CB C 30.394 0.060 . 58 434 30 VAL CG1 C 22.397 0.011 . 59 434 30 VAL CG2 C 21.363 0.007 . 60 434 30 VAL N N 114.652 0.088 . 61 435 31 PHE H H 7.306 0.005 . 62 435 31 PHE CA C 55.273 0.060 . 63 435 31 PHE CB C 37.593 0.060 . 64 435 31 PHE N N 117.539 0.072 . 65 436 32 ARG H H 7.166 0.003 . 66 436 32 ARG CA C 56.392 0.029 . 67 436 32 ARG CB C 29.955 0.060 . 68 436 32 ARG N N 118.922 0.051 . 69 437 33 ASN H H 8.296 0.006 . 70 437 33 ASN CA C 53.644 0.060 . 71 437 33 ASN CB C 38.023 0.060 . 72 437 33 ASN N N 119.873 0.080 . 73 438 34 GLY H H 8.073 0.004 . 74 438 34 GLY CA C 44.853 0.060 . 75 438 34 GLY N N 109.616 0.053 . 76 439 35 ASN H H 8.740 0.006 . 77 439 35 ASN CB C 37.071 0.060 . 78 439 35 ASN N N 120.513 0.039 . 79 440 36 GLN H H 9.025 0.009 . 80 440 36 GLN CA C 58.099 0.060 . 81 440 36 GLN CB C 28.525 0.060 . 82 440 36 GLN N N 125.695 0.098 . 83 441 37 ASP H H 7.962 0.003 . 84 441 37 ASP CA C 53.379 0.069 . 85 441 37 ASP CB C 40.388 0.060 . 86 441 37 ASP N N 114.906 0.049 . 87 442 38 GLU H H 7.141 0.008 . 88 442 38 GLU CA C 56.512 0.009 . 89 442 38 GLU CB C 30.045 0.060 . 90 442 38 GLU N N 121.603 0.059 . 91 443 39 VAL H H 8.650 0.008 . 92 443 39 VAL HG1 H 0.772 0.007 . 93 443 39 VAL HG2 H 0.935 0.007 . 94 443 39 VAL CA C 64.084 0.018 . 95 443 39 VAL CB C 31.124 0.060 . 96 443 39 VAL CG1 C 21.422 0.060 . 97 443 39 VAL CG2 C 21.771 0.009 . 98 443 39 VAL N N 127.143 0.094 . 99 444 40 LEU H H 9.001 0.004 . 100 444 40 LEU HD1 H 0.641 0.007 . 101 444 40 LEU HD2 H 0.646 0.007 . 102 444 40 LEU CA C 54.052 0.030 . 103 444 40 LEU CB C 43.292 0.060 . 104 444 40 LEU CD1 C 26.889 0.010 . 105 444 40 LEU CD2 C 21.681 0.039 . 106 444 40 LEU N N 127.324 0.066 . 107 445 41 SER H H 7.404 0.009 . 108 445 41 SER CA C 57.490 0.024 . 109 445 41 SER CB C 64.097 0.060 . 110 445 41 SER N N 111.731 0.040 . 111 446 42 GLU H H 7.934 0.003 . 112 446 42 GLU CA C 55.344 0.047 . 113 446 42 GLU CB C 31.951 0.060 . 114 446 42 GLU N N 125.108 0.029 . 115 447 43 ALA H H 8.277 0.006 . 116 447 43 ALA CA C 51.883 0.025 . 117 447 43 ALA CB C 18.964 0.060 . 118 447 43 ALA N N 124.329 0.085 . 119 448 44 PHE H H 8.606 0.009 . 120 448 44 PHE CA C 56.361 0.030 . 121 448 44 PHE CB C 36.055 0.060 . 122 448 44 PHE N N 115.358 0.074 . 123 449 45 ARG H H 8.483 0.010 . 124 449 45 ARG CA C 57.728 0.048 . 125 449 45 ARG N N 110.856 0.082 . 126 450 46 LEU H H 8.383 0.008 . 127 450 46 LEU HD1 H 0.929 0.007 . 128 450 46 LEU HD2 H 0.997 0.007 . 129 450 46 LEU CA C 53.752 0.084 . 130 450 46 LEU CB C 43.999 0.060 . 131 450 46 LEU CD1 C 25.720 0.034 . 132 450 46 LEU CD2 C 22.320 0.083 . 133 450 46 LEU N N 121.619 0.055 . 134 451 47 THR H H 8.313 0.006 . 135 451 47 THR CA C 60.849 0.068 . 136 451 47 THR CB C 71.194 0.060 . 137 451 47 THR N N 113.226 0.070 . 138 452 48 ILE H H 8.503 0.003 . 139 452 48 ILE CA C 57.907 1.960 . 140 452 48 ILE CB C 36.141 0.060 . 141 452 48 ILE N N 124.128 0.052 . 142 453 49 THR H H 9.775 0.006 . 143 453 49 THR CA C 59.683 0.053 . 144 453 49 THR CB C 72.918 0.060 . 145 453 49 THR N N 119.821 0.022 . 146 454 50 ARG H H 8.209 0.005 . 147 454 50 ARG CA C 60.286 0.060 . 148 454 50 ARG CB C 28.933 0.060 . 149 454 50 ARG N N 122.141 0.043 . 150 455 51 LYS H H 8.497 0.005 . 151 455 51 LYS CA C 59.288 0.011 . 152 455 51 LYS CB C 31.083 0.060 . 153 455 51 LYS N N 119.120 0.034 . 154 456 52 ASP H H 7.261 0.005 . 155 456 52 ASP CA C 57.437 0.054 . 156 456 52 ASP CB C 40.888 0.060 . 157 456 52 ASP N N 117.782 0.062 . 158 457 53 ILE H H 8.169 0.012 . 159 457 53 ILE CA C 62.447 0.011 . 160 457 53 ILE CB C 37.077 0.060 . 161 457 53 ILE N N 121.587 0.038 . 162 458 54 GLN H H 7.895 0.004 . 163 458 54 GLN CA C 57.909 0.016 . 164 458 54 GLN CB C 26.433 0.060 . 165 458 54 GLN N N 117.962 0.064 . 166 459 55 THR H H 7.881 0.008 . 167 459 55 THR CA C 65.088 0.013 . 168 459 55 THR CB C 67.592 0.060 . 169 459 55 THR N N 113.413 0.034 . 170 460 56 LEU H H 7.257 0.003 . 171 460 56 LEU HD1 H 0.869 0.001 . 172 460 56 LEU HD2 H 0.974 0.001 . 173 460 56 LEU CA C 54.903 0.077 . 174 460 56 LEU CB C 41.520 0.060 . 175 460 56 LEU CD1 C 25.829 0.008 . 176 460 56 LEU CD2 C 25.682 0.007 . 177 460 56 LEU N N 115.361 0.047 . 178 461 57 ASN H H 7.438 0.004 . 179 461 57 ASN CA C 51.816 0.097 . 180 461 57 ASN CB C 37.102 0.060 . 181 461 57 ASN N N 120.260 0.067 . 182 462 58 HIS H H 7.717 0.006 . 183 462 58 HIS CA C 57.014 0.060 . 184 462 58 HIS CB C 29.037 0.060 . 185 462 58 HIS N N 119.708 0.064 . 186 465 61 TRP H H 8.319 0.006 . 187 465 61 TRP HE1 H 10.078 0.007 . 188 465 61 TRP CA C 56.901 0.084 . 189 465 61 TRP CB C 27.801 0.060 . 190 465 61 TRP N N 120.321 0.056 . 191 465 61 TRP NE1 N 129.591 0.060 . 192 466 62 LEU H H 7.644 0.005 . 193 466 62 LEU HD1 H 0.729 0.002 . 194 466 62 LEU HD2 H 0.685 0.001 . 195 466 62 LEU CA C 57.740 0.060 . 196 466 62 LEU CB C 41.916 0.060 . 197 466 62 LEU CD1 C 25.344 0.073 . 198 466 62 LEU CD2 C 23.439 0.044 . 199 466 62 LEU N N 125.508 0.071 . 200 467 63 ASN H H 7.039 0.005 . 201 467 63 ASN CA C 50.169 0.092 . 202 467 63 ASN CB C 39.809 0.060 . 203 467 63 ASN N N 117.210 0.084 . 204 468 64 ASP H H 8.129 0.005 . 205 468 64 ASP CA C 57.483 0.060 . 206 468 64 ASP CB C 40.674 0.060 . 207 468 64 ASP N N 114.915 0.099 . 208 469 65 GLU H H 9.005 0.004 . 209 469 65 GLU CA C 60.759 0.060 . 210 469 65 GLU CB C 27.420 0.060 . 211 469 65 GLU N N 118.847 0.027 . 212 470 66 ILE H H 7.730 0.005 . 213 470 66 ILE CA C 61.202 0.036 . 214 470 66 ILE CB C 34.813 0.060 . 215 470 66 ILE N N 117.722 0.019 . 216 471 67 ILE H H 6.968 0.007 . 217 471 67 ILE CA C 64.433 0.025 . 218 471 67 ILE N N 117.835 0.051 . 219 472 68 ASN H H 9.045 0.009 . 220 472 68 ASN CA C 55.986 0.060 . 221 472 68 ASN CB C 37.424 0.060 . 222 472 68 ASN N N 115.402 0.104 . 223 473 69 PHE H H 8.249 0.007 . 224 473 69 PHE CA C 62.588 0.006 . 225 473 69 PHE CB C 39.685 0.060 . 226 473 69 PHE N N 123.668 0.059 . 227 474 70 TYR H H 8.748 0.007 . 228 474 70 TYR CA C 62.864 0.060 . 229 474 70 TYR N N 120.505 0.060 . 230 475 71 MET H H 8.754 0.007 . 231 475 71 MET CA C 57.276 0.014 . 232 475 71 MET CB C 30.994 0.060 . 233 475 71 MET N N 115.316 0.050 . 234 476 72 ASN H H 7.361 0.004 . 235 476 72 ASN CA C 56.285 0.009 . 236 476 72 ASN CB C 37.889 0.060 . 237 476 72 ASN N N 117.161 0.096 . 238 477 73 MET H H 7.638 0.008 . 239 477 73 MET CA C 60.009 0.060 . 240 477 73 MET CB C 31.373 0.060 . 241 477 73 MET N N 121.431 0.049 . 242 478 74 LEU H H 7.754 0.008 . 243 478 74 LEU HD1 H 0.719 0.001 . 244 478 74 LEU HD2 H 0.475 0.002 . 245 478 74 LEU CA C 57.631 0.060 . 246 478 74 LEU CB C 39.857 0.060 . 247 478 74 LEU CD1 C 27.251 0.030 . 248 478 74 LEU CD2 C 22.008 0.078 . 249 478 74 LEU N N 120.016 0.065 . 250 479 75 MET H H 7.624 0.006 . 251 479 75 MET CA C 59.483 0.021 . 252 479 75 MET CB C 32.446 0.060 . 253 479 75 MET N N 119.020 0.072 . 254 480 76 GLU H H 8.055 0.006 . 255 480 76 GLU CA C 59.178 0.038 . 256 480 76 GLU CB C 28.394 0.060 . 257 480 76 GLU N N 122.941 0.037 . 258 481 77 ARG H H 7.908 0.007 . 259 481 77 ARG N N 120.673 0.035 . 260 482 78 SER H H 7.200 0.005 . 261 482 78 SER CA C 60.285 0.024 . 262 482 78 SER CB C 63.121 0.060 . 263 482 78 SER N N 113.341 0.055 . 264 483 79 LYS H H 6.963 0.008 . 265 483 79 LYS CA C 56.765 0.042 . 266 483 79 LYS CB C 31.668 0.060 . 267 483 79 LYS N N 118.812 0.036 . 268 484 80 GLU H H 8.106 0.005 . 269 484 80 GLU CA C 56.608 0.060 . 270 484 80 GLU CB C 29.038 0.060 . 271 484 80 GLU N N 121.040 0.037 . 272 485 81 LYS H H 8.263 0.009 . 273 485 81 LYS CA C 57.556 0.019 . 274 485 81 LYS CB C 31.136 0.060 . 275 485 81 LYS N N 121.732 0.045 . 276 486 82 GLY H H 8.736 0.010 . 277 486 82 GLY CA C 44.760 0.025 . 278 486 82 GLY N N 111.456 0.033 . 279 487 83 LEU H H 7.345 0.004 . 280 487 83 LEU HD1 H 0.814 0.001 . 281 487 83 LEU HD2 H 0.894 0.001 . 282 487 83 LEU CA C 52.234 0.048 . 283 487 83 LEU CB C 40.050 0.060 . 284 487 83 LEU CD1 C 25.653 0.017 . 285 487 83 LEU CD2 C 23.235 0.015 . 286 487 83 LEU N N 121.670 0.032 . 287 489 85 SER H H 9.139 0.004 . 288 489 85 SER CA C 57.760 0.027 . 289 489 85 SER CB C 64.008 0.060 . 290 489 85 SER N N 118.002 0.026 . 291 490 86 VAL H H 7.361 0.007 . 292 490 86 VAL HG1 H 0.603 0.001 . 293 490 86 VAL HG2 H 0.941 0.003 . 294 490 86 VAL CA C 55.387 0.060 . 295 490 86 VAL CB C 36.642 0.060 . 296 490 86 VAL CG1 C 20.944 0.023 . 297 490 86 VAL CG2 C 22.949 0.021 . 298 490 86 VAL N N 118.590 0.045 . 299 491 87 HIS H H 8.806 0.005 . 300 491 87 HIS CA C 56.454 0.036 . 301 491 87 HIS CB C 33.187 0.060 . 302 491 87 HIS N N 124.169 0.059 . 303 492 88 ALA H H 7.452 0.003 . 304 492 88 ALA CA C 48.953 0.027 . 305 492 88 ALA CB C 20.656 0.060 . 306 492 88 ALA N N 129.640 0.066 . 307 493 89 PHE H H 8.060 0.006 . 308 493 89 PHE CA C 57.442 0.018 . 309 493 89 PHE CB C 40.031 0.060 . 310 493 89 PHE N N 120.359 0.036 . 311 494 90 ASN H H 8.607 0.004 . 312 494 90 ASN CA C 52.520 0.059 . 313 494 90 ASN CB C 38.851 0.060 . 314 494 90 ASN N N 116.372 0.023 . 315 495 91 THR H H 8.710 0.008 . 316 495 91 THR CA C 65.105 0.014 . 317 495 91 THR CB C 67.827 0.060 . 318 495 91 THR N N 111.803 0.132 . 319 496 92 PHE H H 8.395 0.008 . 320 496 92 PHE CA C 57.585 0.038 . 321 496 92 PHE CB C 38.578 0.060 . 322 496 92 PHE N N 120.587 0.073 . 323 497 93 PHE H H 7.946 0.008 . 324 497 93 PHE CA C 61.499 0.015 . 325 497 93 PHE CB C 38.408 0.060 . 326 497 93 PHE N N 121.390 0.054 . 327 498 94 PHE H H 10.086 0.012 . 328 498 94 PHE CA C 62.544 0.019 . 329 498 94 PHE CB C 37.745 0.060 . 330 498 94 PHE N N 120.564 0.031 . 331 499 95 THR H H 7.077 0.007 . 332 499 95 THR CA C 65.828 0.022 . 333 499 95 THR CB C 68.658 0.060 . 334 499 95 THR N N 111.855 0.047 . 335 500 96 LYS H H 7.799 0.011 . 336 500 96 LYS CA C 58.148 0.015 . 337 500 96 LYS CB C 30.294 0.060 . 338 500 96 LYS N N 122.895 0.044 . 339 501 97 LEU H H 8.046 0.006 . 340 501 97 LEU HD1 H 0.659 0.002 . 341 501 97 LEU HD2 H 0.319 0.001 . 342 501 97 LEU CD1 C 21.250 0.028 . 343 501 97 LEU CD2 C 26.080 0.033 . 344 501 97 LEU N N 120.681 0.056 . 345 502 98 LYS H H 8.096 0.009 . 346 502 98 LYS CA C 58.412 0.060 . 347 502 98 LYS CB C 31.075 0.060 . 348 502 98 LYS N N 117.076 0.091 . 349 503 99 THR H H 7.507 0.008 . 350 503 99 THR CA C 63.680 0.060 . 351 503 99 THR CB C 69.640 0.060 . 352 503 99 THR N N 108.648 0.028 . 353 504 100 ALA H H 8.417 0.006 . 354 504 100 ALA CA C 51.699 0.030 . 355 504 100 ALA CB C 19.982 0.060 . 356 504 100 ALA N N 124.292 0.046 . 357 505 101 GLY H H 7.402 0.004 . 358 505 101 GLY CA C 44.107 0.060 . 359 505 101 GLY N N 108.222 0.028 . 360 506 102 TYR H H 8.500 0.006 . 361 506 102 TYR CA C 61.401 0.022 . 362 506 102 TYR CB C 38.182 0.060 . 363 506 102 TYR N N 118.007 0.021 . 364 507 103 GLN H H 8.673 0.007 . 365 507 103 GLN CA C 58.137 0.038 . 366 507 103 GLN N N 113.988 0.032 . 367 508 104 ALA H H 7.187 0.008 . 368 508 104 ALA CA C 53.100 0.032 . 369 508 104 ALA CB C 19.382 0.060 . 370 508 104 ALA N N 117.877 0.061 . 371 509 105 VAL H H 6.979 0.005 . 372 509 105 VAL HG1 H 0.194 0.005 . 373 509 105 VAL HG2 H 0.551 0.001 . 374 509 105 VAL CA C 59.562 0.097 . 375 509 105 VAL CB C 32.569 0.060 . 376 509 105 VAL CG1 C 19.015 0.211 . 377 509 105 VAL CG2 C 20.041 0.175 . 378 509 105 VAL N N 104.885 0.073 . 379 510 106 LYS H H 7.245 0.005 . 380 510 106 LYS CA C 59.303 0.040 . 381 510 106 LYS CB C 30.389 0.060 . 382 510 106 LYS N N 126.600 0.075 . 383 511 107 ARG H H 8.596 0.004 . 384 511 107 ARG CA C 57.186 0.132 . 385 511 107 ARG CB C 28.322 0.060 . 386 511 107 ARG N N 116.249 0.050 . 387 512 108 TRP H H 8.479 0.007 . 388 512 108 TRP HE1 H 10.279 0.007 . 389 512 108 TRP CA C 59.233 0.060 . 390 512 108 TRP CB C 27.794 0.060 . 391 512 108 TRP N N 120.166 0.058 . 392 512 108 TRP NE1 N 129.360 0.060 . 393 513 109 THR H H 7.348 0.004 . 394 513 109 THR CA C 60.062 0.060 . 395 513 109 THR CB C 65.670 0.060 . 396 513 109 THR N N 105.793 0.068 . 397 514 110 LYS H H 7.181 0.007 . 398 514 110 LYS CA C 59.308 0.027 . 399 514 110 LYS CB C 31.470 0.060 . 400 514 110 LYS N N 120.810 0.032 . 401 515 111 LYS H H 8.518 0.008 . 402 515 111 LYS CA C 55.039 0.068 . 403 515 111 LYS CB C 31.329 0.060 . 404 515 111 LYS N N 115.255 0.032 . 405 516 112 VAL H H 7.335 0.003 . 406 516 112 VAL HG1 H 1.087 0.001 . 407 516 112 VAL HG2 H 0.878 0.007 . 408 516 112 VAL CA C 60.288 0.010 . 409 516 112 VAL CB C 34.823 0.060 . 410 516 112 VAL CG1 C 22.040 0.061 . 411 516 112 VAL CG2 C 19.472 0.218 . 412 516 112 VAL N N 118.566 0.023 . 413 517 113 ASP H H 8.503 0.007 . 414 517 113 ASP CA C 50.718 0.027 . 415 517 113 ASP CB C 39.298 0.060 . 416 517 113 ASP N N 124.287 0.118 . 417 518 114 VAL H H 8.897 0.005 . 418 518 114 VAL HG1 H 0.762 0.007 . 419 518 114 VAL HG2 H 0.303 0.002 . 420 518 114 VAL CA C 64.159 0.042 . 421 518 114 VAL CB C 30.530 0.060 . 422 518 114 VAL CG1 C 21.894 0.047 . 423 518 114 VAL CG2 C 17.668 0.035 . 424 518 114 VAL N N 121.428 0.042 . 425 519 115 PHE H H 7.216 0.006 . 426 519 115 PHE CA C 57.895 0.001 . 427 519 115 PHE CB C 36.838 0.060 . 428 519 115 PHE N N 110.893 0.043 . 429 520 116 SER H H 7.446 0.004 . 430 520 116 SER CA C 58.090 0.018 . 431 520 116 SER CB C 64.114 0.060 . 432 520 116 SER N N 113.545 0.026 . 433 521 117 VAL H H 6.664 0.005 . 434 521 117 VAL HG1 H 0.730 0.001 . 435 521 117 VAL HG2 H 0.789 0.003 . 436 521 117 VAL CA C 58.659 0.338 . 437 521 117 VAL CB C 33.064 0.060 . 438 521 117 VAL CG1 C 21.360 0.036 . 439 521 117 VAL CG2 C 19.096 0.065 . 440 521 117 VAL N N 114.181 0.034 . 441 522 118 ASP H H 8.176 0.005 . 442 522 118 ASP CA C 57.705 0.060 . 443 522 118 ASP CB C 42.255 0.060 . 444 522 118 ASP N N 120.158 0.121 . 445 523 119 ILE H H 8.186 0.003 . 446 523 119 ILE CA C 59.151 0.077 . 447 523 119 ILE N N 117.387 0.025 . 448 524 120 LEU H H 9.337 0.006 . 449 524 120 LEU HD1 H 0.881 0.007 . 450 524 120 LEU HD2 H 0.873 0.007 . 451 524 120 LEU CA C 51.718 0.060 . 452 524 120 LEU CD1 C 24.261 0.001 . 453 524 120 LEU CD2 C 24.508 0.018 . 454 524 120 LEU N N 122.128 0.092 . 455 525 121 LEU H H 8.703 0.007 . 456 525 121 LEU HD1 H 0.788 0.003 . 457 525 121 LEU HD2 H 0.766 0.007 . 458 525 121 LEU CA C 53.081 0.068 . 459 525 121 LEU CB C 43.595 0.060 . 460 525 121 LEU CD1 C 27.441 0.008 . 461 525 121 LEU CD2 C 23.515 0.059 . 462 525 121 LEU N N 120.635 0.088 . 463 526 122 VAL H H 8.905 0.007 . 464 526 122 VAL HG1 H -0.207 0.007 . 465 526 122 VAL HG2 H 0.520 0.006 . 466 526 122 VAL CA C 58.856 0.060 . 467 526 122 VAL CB C 32.266 0.060 . 468 526 122 VAL CG1 C 20.530 0.044 . 469 526 122 VAL CG2 C 19.241 0.048 . 470 526 122 VAL N N 121.007 0.052 . 471 528 124 ILE H H 8.695 0.004 . 472 528 124 ILE CA C 60.843 0.055 . 473 528 124 ILE CB C 39.908 0.060 . 474 528 124 ILE N N 124.930 0.045 . 475 529 125 HIS H H 9.105 0.009 . 476 529 125 HIS CA C 51.146 0.052 . 477 529 125 HIS CB C 29.604 0.060 . 478 529 125 HIS N N 129.310 0.094 . 479 530 126 LEU H H 8.699 0.004 . 480 530 126 LEU HD1 H 0.897 0.002 . 481 530 126 LEU HD2 H 0.802 0.001 . 482 530 126 LEU CA C 52.741 0.047 . 483 530 126 LEU CB C 40.918 0.060 . 484 530 126 LEU CD1 C 25.636 0.036 . 485 530 126 LEU CD2 C 23.628 0.040 . 486 530 126 LEU N N 130.938 0.062 . 487 531 127 GLY H H 8.114 0.010 . 488 531 127 GLY CA C 46.077 0.060 . 489 531 127 GLY N N 115.062 0.092 . 490 532 128 VAL H H 8.105 0.007 . 491 532 128 VAL HG1 H 0.529 0.004 . 492 532 128 VAL HG2 H 0.449 0.001 . 493 532 128 VAL CA C 60.956 0.040 . 494 532 128 VAL CB C 30.595 0.060 . 495 532 128 VAL CG1 C 20.748 0.028 . 496 532 128 VAL CG2 C 17.722 0.051 . 497 532 128 VAL N N 119.606 0.037 . 498 533 129 HIS H H 7.749 0.005 . 499 533 129 HIS CA C 55.451 0.071 . 500 533 129 HIS CB C 33.098 0.060 . 501 533 129 HIS N N 123.099 0.059 . 502 534 130 TRP H H 7.914 0.006 . 503 534 130 TRP HE1 H 9.422 0.007 . 504 534 130 TRP CB C 31.151 0.060 . 505 534 130 TRP N N 124.529 0.075 . 506 534 130 TRP NE1 N 127.379 0.060 . 507 535 131 CYS H H 9.472 0.004 . 508 535 131 CYS CA C 56.515 0.025 . 509 535 131 CYS CB C 30.317 0.060 . 510 535 131 CYS N N 117.423 0.070 . 511 536 132 LEU H H 7.881 0.004 . 512 536 132 LEU HD1 H 0.734 0.001 . 513 536 132 LEU HD2 H 0.642 0.002 . 514 536 132 LEU CA C 54.050 0.077 . 515 536 132 LEU CB C 46.509 0.060 . 516 536 132 LEU CD1 C 23.499 1.789 . 517 536 132 LEU CD2 C 25.134 1.765 . 518 536 132 LEU N N 120.669 0.048 . 519 537 133 ALA H H 8.834 0.012 . 520 537 133 ALA CA C 49.512 0.043 . 521 537 133 ALA CB C 20.885 0.060 . 522 537 133 ALA N N 126.923 0.116 . 523 538 134 VAL H H 9.057 0.005 . 524 538 134 VAL HG1 H 0.922 0.002 . 525 538 134 VAL HG2 H 0.857 0.001 . 526 538 134 VAL CA C 60.400 0.064 . 527 538 134 VAL CB C 35.415 0.060 . 528 538 134 VAL CG1 C 21.593 0.024 . 529 538 134 VAL CG2 C 21.801 0.017 . 530 538 134 VAL N N 119.568 0.019 . 531 539 135 VAL H H 9.399 0.009 . 532 539 135 VAL HG1 H 0.490 0.060 . 533 539 135 VAL HG2 H 0.929 0.002 . 534 539 135 VAL CA C 60.864 0.014 . 535 539 135 VAL CB C 32.034 0.060 . 536 539 135 VAL CG1 C 20.367 0.033 . 537 539 135 VAL CG2 C 19.356 0.025 . 538 539 135 VAL N N 130.616 0.062 . 539 540 136 ASP H H 8.936 0.006 . 540 540 136 ASP CA C 51.892 0.041 . 541 540 136 ASP CB C 41.795 0.060 . 542 540 136 ASP N N 126.599 0.051 . 543 541 137 PHE H H 9.460 0.005 . 544 541 137 PHE CA C 61.930 0.008 . 545 541 137 PHE CB C 39.228 0.060 . 546 541 137 PHE N N 124.047 0.058 . 547 542 138 ARG H H 8.703 0.006 . 548 542 138 ARG CA C 57.336 0.053 . 549 542 138 ARG CB C 28.583 0.060 . 550 542 138 ARG N N 117.505 0.044 . 551 543 139 LYS H H 6.738 0.003 . 552 543 139 LYS CA C 54.788 0.059 . 553 543 139 LYS CB C 33.252 0.060 . 554 543 139 LYS N N 114.215 0.032 . 555 544 140 LYS H H 7.415 0.004 . 556 544 140 LYS CA C 55.498 0.055 . 557 544 140 LYS CB C 27.557 0.060 . 558 544 140 LYS N N 115.819 0.035 . 559 545 141 ASN H H 7.219 0.004 . 560 545 141 ASN CA C 50.992 0.056 . 561 545 141 ASN CB C 42.131 0.060 . 562 545 141 ASN N N 113.582 0.071 . 563 546 142 ILE H H 8.432 0.005 . 564 546 142 ILE CA C 61.554 0.003 . 565 546 142 ILE CB C 38.765 0.060 . 566 546 142 ILE N N 120.310 0.041 . 567 547 143 THR H H 8.774 0.004 . 568 547 143 THR CA C 60.640 0.060 . 569 547 143 THR CB C 70.491 0.060 . 570 547 143 THR N N 121.479 0.058 . 571 548 144 TYR H H 8.698 0.009 . 572 548 144 TYR CA C 57.162 0.062 . 573 548 144 TYR CB C 40.702 0.060 . 574 548 144 TYR N N 128.870 0.054 . 575 549 145 TYR H H 9.090 0.005 . 576 549 145 TYR CA C 57.412 0.006 . 577 549 145 TYR CB C 39.999 0.060 . 578 549 145 TYR N N 125.877 0.035 . 579 550 146 ASP H H 8.073 0.003 . 580 550 146 ASP CA C 52.672 0.034 . 581 550 146 ASP CB C 44.004 0.060 . 582 550 146 ASP N N 123.203 0.040 . 583 551 147 SER H H 9.360 0.009 . 584 551 147 SER CA C 60.193 0.067 . 585 551 147 SER CB C 63.004 0.060 . 586 551 147 SER N N 122.514 0.129 . 587 552 148 MET H H 9.193 0.003 . 588 552 148 MET CA C 54.633 0.062 . 589 552 148 MET CB C 33.278 0.060 . 590 552 148 MET N N 121.989 0.053 . 591 553 149 GLY H H 7.838 0.007 . 592 553 149 GLY CA C 46.506 0.025 . 593 553 149 GLY N N 109.682 0.018 . 594 554 150 GLY H H 7.654 0.011 . 595 554 150 GLY CA C 45.002 0.021 . 596 554 150 GLY N N 107.999 0.029 . 597 555 151 ILE H H 8.058 0.003 . 598 555 151 ILE CA C 59.373 0.022 . 599 555 151 ILE CB C 38.565 0.060 . 600 555 151 ILE N N 118.298 0.051 . 601 556 152 ASN H H 7.761 0.005 . 602 556 152 ASN CA C 50.779 0.092 . 603 556 152 ASN CB C 36.162 0.060 . 604 556 152 ASN N N 124.223 0.057 . 605 557 153 ASN H H 8.311 0.006 . 606 557 153 ASN CA C 55.658 0.060 . 607 557 153 ASN CB C 37.255 0.060 . 608 557 153 ASN N N 121.145 0.058 . 609 558 154 GLU H H 8.525 0.009 . 610 558 154 GLU CA C 59.166 0.060 . 611 558 154 GLU CB C 28.321 0.060 . 612 558 154 GLU N N 120.798 0.060 . 613 559 155 ALA H H 7.509 0.003 . 614 559 155 ALA CA C 55.133 0.001 . 615 559 155 ALA CB C 17.162 0.060 . 616 559 155 ALA N N 120.631 0.058 . 617 560 156 CYS H H 6.838 0.003 . 618 560 156 CYS CA C 61.861 0.042 . 619 560 156 CYS CB C 26.352 0.060 . 620 560 156 CYS N N 111.967 0.043 . 621 561 157 ARG H H 8.006 0.005 . 622 561 157 ARG CA C 59.799 0.032 . 623 561 157 ARG N N 120.225 0.052 . 624 562 158 ILE H H 8.585 0.005 . 625 562 158 ILE CA C 64.838 0.018 . 626 562 158 ILE CB C 36.988 0.060 . 627 562 158 ILE N N 120.618 0.049 . 628 563 159 LEU H H 7.591 0.008 . 629 563 159 LEU HD1 H 0.764 0.001 . 630 563 159 LEU HD2 H 0.839 0.001 . 631 563 159 LEU CA C 57.016 0.037 . 632 563 159 LEU CB C 41.100 0.060 . 633 563 159 LEU CD1 C 26.019 0.022 . 634 563 159 LEU CD2 C 22.708 0.007 . 635 563 159 LEU N N 120.748 0.051 . 636 564 160 LEU H H 8.000 0.008 . 637 564 160 LEU HD1 H 0.556 0.002 . 638 564 160 LEU HD2 H 0.899 0.007 . 639 564 160 LEU CA C 57.945 0.060 . 640 564 160 LEU CB C 40.588 0.060 . 641 564 160 LEU CD1 C 23.761 1.261 . 642 564 160 LEU CD2 C 24.175 1.339 . 643 564 160 LEU N N 122.371 0.078 . 644 565 161 GLN H H 7.918 0.007 . 645 565 161 GLN CB C 26.983 0.060 . 646 565 161 GLN N N 116.230 0.093 . 647 566 162 TYR H H 8.129 0.008 . 648 566 162 TYR CA C 61.319 0.026 . 649 566 162 TYR CB C 36.819 0.060 . 650 566 162 TYR N N 121.493 0.037 . 651 567 163 LEU H H 7.760 0.009 . 652 567 163 LEU HD1 H 0.347 0.007 . 653 567 163 LEU HD2 H 0.639 0.007 . 654 567 163 LEU CA C 57.657 0.001 . 655 567 163 LEU CB C 39.783 0.060 . 656 567 163 LEU CD1 C 25.936 0.037 . 657 567 163 LEU CD2 C 21.550 0.059 . 658 567 163 LEU N N 119.034 0.056 . 659 568 164 LYS H H 7.433 0.012 . 660 568 164 LYS CA C 59.704 0.045 . 661 568 164 LYS CB C 31.079 0.060 . 662 568 164 LYS N N 116.350 0.069 . 663 569 165 GLN H H 7.695 0.009 . 664 569 165 GLN CA C 58.460 0.008 . 665 569 165 GLN CB C 26.791 0.060 . 666 569 165 GLN N N 119.295 0.053 . 667 570 166 GLU H H 8.869 0.003 . 668 570 166 GLU CA C 57.245 0.014 . 669 570 166 GLU CB C 27.853 0.060 . 670 570 166 GLU N N 123.828 0.026 . 671 571 167 SER H H 8.108 0.006 . 672 571 167 SER CA C 61.870 0.054 . 673 571 167 SER CB C 63.714 0.060 . 674 571 167 SER N N 113.091 0.021 . 675 572 168 ILE H H 7.079 0.007 . 676 572 168 ILE CA C 64.122 0.012 . 677 572 168 ILE CB C 36.740 0.060 . 678 572 168 ILE N N 120.026 0.028 . 679 573 169 ASP H H 8.267 0.008 . 680 573 169 ASP CA C 58.625 0.003 . 681 573 169 ASP CB C 45.354 0.060 . 682 573 169 ASP N N 119.683 0.043 . 683 574 170 LYS H H 8.536 0.003 . 684 574 170 LYS CA C 55.197 0.060 . 685 574 170 LYS N N 110.113 0.037 . 686 575 171 LYS H H 7.814 0.008 . 687 575 171 LYS CA C 53.600 0.060 . 688 575 171 LYS N N 114.921 0.066 . 689 580 176 ASP H H 8.008 0.004 . 690 580 176 ASP CA C 53.133 0.043 . 691 580 176 ASP N N 128.240 0.042 . 692 581 177 THR H H 7.997 0.003 . 693 581 177 THR CA C 61.623 0.030 . 694 581 177 THR CB C 67.989 0.060 . 695 581 177 THR N N 114.516 0.047 . 696 582 178 ASN H H 8.552 0.005 . 697 582 178 ASN CA C 55.614 0.058 . 698 582 178 ASN CB C 37.674 0.060 . 699 582 178 ASN N N 124.767 0.038 . 700 583 179 GLY H H 8.970 0.013 . 701 583 179 GLY CA C 44.988 0.017 . 702 583 179 GLY N N 113.047 0.055 . 703 584 180 TRP H H 7.883 0.003 . 704 584 180 TRP HE1 H 10.191 0.007 . 705 584 180 TRP CA C 58.705 0.060 . 706 584 180 TRP CB C 27.412 0.060 . 707 584 180 TRP N N 120.575 0.051 . 708 584 180 TRP NE1 N 130.090 0.060 . 709 585 181 GLN H H 8.302 0.004 . 710 585 181 GLN CA C 54.343 0.054 . 711 585 181 GLN CB C 32.640 0.060 . 712 585 181 GLN N N 120.499 0.055 . 713 586 182 LEU H H 8.246 0.007 . 714 586 182 LEU HD1 H 0.921 0.005 . 715 586 182 LEU HD2 H 1.106 0.002 . 716 586 182 LEU CA C 52.796 0.011 . 717 586 182 LEU CB C 41.618 0.060 . 718 586 182 LEU CD1 C 24.455 0.038 . 719 586 182 LEU CD2 C 24.100 0.004 . 720 586 182 LEU N N 122.565 0.100 . 721 587 183 PHE H H 9.004 0.005 . 722 587 183 PHE CA C 56.242 0.036 . 723 587 183 PHE CB C 42.072 0.060 . 724 587 183 PHE N N 119.629 0.055 . 725 588 184 SER H H 8.552 0.004 . 726 588 184 SER CA C 57.498 0.062 . 727 588 184 SER CB C 64.651 0.060 . 728 588 184 SER N N 115.738 0.030 . 729 589 185 LYS H H 8.359 0.007 . 730 589 185 LYS CA C 54.554 0.040 . 731 589 185 LYS CB C 30.741 0.060 . 732 589 185 LYS N N 124.102 0.081 . 733 590 186 LYS H H 9.141 0.007 . 734 590 186 LYS CA C 55.700 0.049 . 735 590 186 LYS CB C 32.576 0.060 . 736 590 186 LYS N N 124.690 0.039 . 737 591 187 SER H H 8.706 0.009 . 738 591 187 SER CA C 60.742 0.035 . 739 591 187 SER CB C 62.437 0.060 . 740 591 187 SER N N 117.012 0.069 . 741 592 188 GLN H H 7.792 0.006 . 742 592 188 GLN CA C 56.544 0.017 . 743 592 188 GLN CB C 27.273 0.060 . 744 593 189 GLU H H 8.133 0.004 . 745 593 189 GLU CA C 56.781 0.035 . 746 593 189 GLU CB C 31.403 0.060 . 747 593 189 GLU N N 116.615 0.027 . 748 594 190 ILE H H 7.107 0.007 . 749 594 190 ILE CA C 57.257 0.026 . 750 594 190 ILE CB C 39.407 0.060 . 751 594 190 ILE N N 111.854 0.025 . 752 596 192 GLN H H 8.537 0.004 . 753 596 192 GLN CA C 52.738 0.035 . 754 596 192 GLN CB C 31.474 0.060 . 755 596 192 GLN N N 119.737 0.052 . 756 597 193 GLN H H 8.656 0.007 . 757 597 193 GLN CA C 53.768 0.059 . 758 597 193 GLN CB C 29.186 0.060 . 759 597 193 GLN N N 118.854 0.041 . 760 598 194 MET H H 9.501 0.005 . 761 598 194 MET CA C 54.881 0.118 . 762 598 194 MET CB C 33.414 0.060 . 763 598 194 MET N N 119.234 0.032 . 764 599 195 ASN H H 7.426 0.005 . 765 599 195 ASN CA C 51.638 0.086 . 766 599 195 ASN CB C 39.541 0.060 . 767 599 195 ASN N N 115.946 0.052 . 768 602 198 ASP H H 7.471 0.003 . 769 602 198 ASP CA C 55.441 0.063 . 770 602 198 ASP CB C 41.257 0.060 . 771 602 198 ASP N N 118.797 0.048 . 772 603 199 SER H H 8.134 0.006 . 773 603 199 SER CA C 63.796 0.027 . 774 603 199 SER N N 120.851 0.089 . 775 604 200 GLY H H 8.802 0.005 . 776 604 200 GLY CA C 47.455 0.018 . 777 604 200 GLY N N 107.992 0.042 . 778 605 201 MET H H 6.928 0.004 . 779 605 201 MET CA C 54.362 0.007 . 780 605 201 MET CB C 28.918 0.060 . 781 605 201 MET N N 118.281 0.062 . 782 606 202 PHE H H 8.185 0.008 . 783 606 202 PHE CA C 63.162 0.013 . 784 606 202 PHE CB C 37.299 0.060 . 785 606 202 PHE N N 119.035 0.097 . 786 607 203 ALA H H 8.024 0.004 . 787 607 203 ALA CA C 55.879 0.060 . 788 607 203 ALA CB C 16.008 0.060 . 789 607 203 ALA N N 118.660 0.048 . 790 608 204 CYS H H 7.169 0.006 . 791 608 204 CYS CA C 64.702 0.020 . 792 608 204 CYS CB C 26.434 0.060 . 793 608 204 CYS N N 111.441 0.048 . 794 609 205 LYS H H 8.024 0.010 . 795 609 205 LYS CA C 56.088 0.025 . 796 609 205 LYS CB C 28.022 0.060 . 797 609 205 LYS N N 117.554 0.081 . 798 610 206 TYR H H 9.633 0.005 . 799 610 206 TYR CA C 58.091 0.005 . 800 610 206 TYR CB C 36.257 0.060 . 801 610 206 TYR N N 121.444 0.055 . 802 611 207 ALA H H 7.377 0.006 . 803 611 207 ALA CA C 55.331 0.060 . 804 611 207 ALA CB C 17.367 0.060 . 805 611 207 ALA N N 118.325 0.085 . 806 612 208 ASP H H 8.330 0.006 . 807 612 208 ASP CA C 57.478 0.009 . 808 612 208 ASP CB C 40.801 0.060 . 809 612 208 ASP N N 119.194 0.046 . 810 613 209 CYS H H 7.273 0.003 . 811 613 209 CYS CA C 64.358 0.012 . 812 613 209 CYS CB C 26.279 0.060 . 813 613 209 CYS N N 114.204 0.045 . 814 614 210 ILE H H 8.562 0.006 . 815 614 210 ILE CB C 38.381 0.060 . 816 614 210 ILE N N 119.260 0.039 . 817 615 211 THR H H 8.247 0.005 . 818 615 211 THR N N 108.254 0.018 . 819 616 212 LYS H H 7.185 0.007 . 820 616 212 LYS CA C 55.392 0.073 . 821 616 212 LYS N N 118.756 0.036 . 822 617 213 ASP H H 7.966 0.006 . 823 617 213 ASP CA C 55.029 0.060 . 824 617 213 ASP CB C 38.838 0.060 . 825 617 213 ASP N N 117.680 0.022 . 826 618 214 ARG H H 7.913 0.004 . 827 618 214 ARG CA C 51.941 0.080 . 828 618 214 ARG CB C 30.595 0.060 . 829 618 214 ARG N N 116.749 0.023 . 830 620 216 ILE H H 8.443 0.008 . 831 620 216 ILE CA C 62.265 0.060 . 832 620 216 ILE CB C 35.856 0.060 . 833 620 216 ILE N N 121.958 0.026 . 834 621 217 ASN H H 7.941 0.005 . 835 621 217 ASN CA C 52.331 0.009 . 836 621 217 ASN CB C 38.144 0.060 . 837 621 217 ASN N N 126.177 0.072 . 838 622 218 PHE H H 6.543 0.005 . 839 622 218 PHE CA C 54.419 0.070 . 840 622 218 PHE CB C 41.053 0.060 . 841 622 218 PHE N N 113.942 0.034 . 842 623 219 THR H H 10.992 0.006 . 843 623 219 THR CA C 59.947 0.044 . 844 623 219 THR CB C 73.269 0.060 . 845 623 219 THR N N 112.703 0.025 . 846 624 220 GLN H H 9.853 0.007 . 847 624 220 GLN CA C 58.030 0.001 . 848 624 220 GLN CB C 28.663 0.060 . 849 624 220 GLN N N 118.908 0.028 . 850 625 221 GLN H H 8.345 0.004 . 851 625 221 GLN CA C 57.772 0.060 . 852 625 221 GLN CB C 27.228 0.060 . 853 625 221 GLN N N 118.169 0.056 . 854 626 222 HIS H H 7.700 0.007 . 855 626 222 HIS CA C 58.981 0.052 . 856 626 222 HIS CB C 32.100 0.060 . 857 626 222 HIS N N 116.147 0.020 . 858 627 223 MET H H 7.630 0.010 . 859 627 223 MET CA C 58.625 0.034 . 860 627 223 MET CB C 29.346 0.060 . 861 627 223 MET N N 117.726 0.049 . 862 629 225 TYR H H 7.464 0.002 . 863 629 225 TYR CA C 59.858 0.006 . 864 629 225 TYR CB C 36.850 0.060 . 865 629 225 TYR N N 119.164 0.039 . 866 630 226 PHE H H 8.710 0.005 . 867 630 226 PHE CA C 57.735 0.017 . 868 630 226 PHE N N 118.767 0.058 . 869 631 227 ARG H H 8.819 0.010 . 870 631 227 ARG CA C 60.044 0.060 . 871 631 227 ARG CB C 29.797 0.060 . 872 631 227 ARG N N 121.584 0.085 . 873 632 228 LYS H H 7.023 0.007 . 874 632 228 LYS CA C 59.822 0.060 . 875 632 228 LYS CB C 31.995 0.060 . 876 632 228 LYS N N 115.504 0.036 . 877 633 229 ARG H H 8.492 0.009 . 878 633 229 ARG CA C 59.174 0.069 . 879 633 229 ARG CB C 30.402 0.060 . 880 633 229 ARG N N 116.645 0.040 . 881 634 230 MET H H 8.215 0.010 . 882 634 230 MET CA C 57.976 0.038 . 883 634 230 MET CB C 31.926 0.060 . 884 634 230 MET N N 117.035 0.030 . 885 635 231 VAL H H 7.385 0.003 . 886 635 231 VAL HG1 H 0.548 0.011 . 887 635 231 VAL HG2 H 1.123 0.001 . 888 635 231 VAL CA C 66.774 0.060 . 889 635 231 VAL CB C 30.902 0.060 . 890 635 231 VAL CG1 C 21.993 0.055 . 891 635 231 VAL CG2 C 24.171 0.081 . 892 635 231 VAL N N 117.802 0.057 . 893 636 232 TRP H H 6.936 0.007 . 894 636 232 TRP HE1 H 10.190 0.007 . 895 636 232 TRP CA C 63.059 0.046 . 896 636 232 TRP CB C 28.875 0.060 . 897 636 232 TRP N N 117.780 0.088 . 898 636 232 TRP NE1 N 131.268 0.060 . 899 637 233 GLU H H 8.916 0.004 . 900 637 233 GLU CA C 59.713 0.005 . 901 637 233 GLU CB C 29.523 0.060 . 902 637 233 GLU N N 118.361 0.044 . 903 638 234 ILE H H 8.497 0.006 . 904 638 234 ILE CA C 65.044 0.045 . 905 638 234 ILE CB C 36.562 0.060 . 906 638 234 ILE N N 118.104 0.051 . 907 639 235 LEU H H 8.015 0.008 . 908 639 235 LEU HD1 H 0.627 0.007 . 909 639 235 LEU HD2 H 0.547 0.001 . 910 639 235 LEU CA C 57.546 0.060 . 911 639 235 LEU CB C 40.763 0.060 . 912 639 235 LEU CD1 C 24.997 0.034 . 913 639 235 LEU CD2 C 22.659 0.077 . 914 639 235 LEU N N 119.918 0.096 . 915 640 236 HIS H H 7.751 0.005 . 916 640 236 HIS CA C 55.594 0.073 . 917 640 236 HIS CB C 26.881 0.060 . 918 640 236 HIS N N 112.266 0.063 . 919 641 237 ARG H H 7.868 0.005 . 920 641 237 ARG CA C 56.957 0.040 . 921 641 237 ARG CB C 25.976 0.060 . 922 641 237 ARG N N 122.591 0.040 . 923 642 238 LYS H H 8.226 0.007 . 924 642 238 LYS CA C 54.665 0.028 . 925 642 238 LYS CB C 34.896 0.060 . 926 642 238 LYS N N 121.200 0.041 . 927 643 239 LEU H H 8.125 0.005 . 928 643 239 LEU HD1 H 0.445 0.007 . 929 643 239 LEU HD2 H 0.605 0.001 . 930 643 239 LEU CA C 53.578 0.068 . 931 643 239 LEU CB C 41.226 0.060 . 932 643 239 LEU CD1 C 27.225 0.057 . 933 643 239 LEU CD2 C 24.320 0.049 . 934 643 239 LEU N N 122.338 0.051 . 935 644 240 LEU H H 8.829 0.008 . 936 644 240 LEU CA C 55.212 0.087 . 937 644 240 LEU CB C 41.636 0.060 . 938 644 240 LEU N N 130.191 0.067 . stop_ save_