data_25425 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and side-chain 13C, 15N resonance assignments of artificially disordered FAS 1-4 A546T domain of TGFBIp dissolved in 95 % of DMSO in presence of water ; _BMRB_accession_number 25425 _BMRB_flat_file_name bmr25425.str _Entry_type original _Submission_date 2015-01-12 _Accession_date 2015-01-12 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; we report complete backbone and aliphatic side chain 13C and 15N resonance assignments of FAS1-4 A546T at pH 2.9 and 25 C in its unfolded state ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kulminskaya Natalia V. . 2 Yoshimura Yuichi . . 3 Runager Kasper S. . 4 Sorensen Charlotte . . 5 Bjerring Morten . . 6 Mulder Frans . . 7 Nielsen Niels Chr. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 148 "13C chemical shifts" 540 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-30 update BMRB 'update entry citation' 2015-04-16 original author 'original release' stop_ _Original_release_date 2015-04-16 save_ ############################# # Citation for this entry # ############################# save_7 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Near-complete 1H, 13C, 15N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26275916 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kulminskaya Natalia V. . 2 Yoshimura Yuichi . . 3 Runager Kasper . . 4 Sorensen Charlotte S. . 5 Bjerring Morten . . 6 Andreasen Maria . . 7 Otzen Daniel E. . 8 Enghild Jan J. . 9 Nielsen Niels C. . 10 Mulder Frans A.A. . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 25 _Page_last 29 _Year 2016 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_1 _Saveframe_category citation _Citation_full . _Citation_title ; cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is preferentially expressed as an extracellular protein in the corneal epithelium. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Escribano J. . . stop_ _Journal_abbreviation 'J. Cell Physiol.' _Journal_name_full . _Journal_volume 160 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 511 _Page_last 521 _Year 1994 _Details . save_ save_2 _Saveframe_category citation _Citation_full . _Citation_title ; Polymorphic fibrillation of the destabilised fourth fascilin-1 domain mutant A546T of the Transforming growth factor-beta-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Andreasen Maria . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full . _Journal_volume 287 _Journal_issue 41 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 34730 _Page_last 34742 _Year 2012 _Details . save_ save_3 _Saveframe_category citation _Citation_full . _Citation_title ; A new mutation (A546T) of the betaig-h3 gene responsible for a French lattice corneal dystrophy type ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dighiero P. . . stop_ _Journal_abbreviation 'American J. Ophthalmology' _Journal_name_full . _Journal_volume 129 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 248 _Page_last 251 _Year 2000 _Details . save_ save_4 _Saveframe_category citation _Citation_full . _Citation_title ; Focus on molecules: Transforming growth factor beta induced protein (TGFBIp) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Runager Kasper S. . stop_ _Journal_abbreviation 'Exp. Eye Res.' _Journal_name_full . _Journal_volume 87 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 298 _Page_last 299 _Year 2008 _Details . save_ save_5 _Saveframe_category citation _Citation_full . _Citation_title ; Purification and structural characterisation of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Andersen R.B. . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full . _Journal_volume 43 _Journal_issue 51 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 16374 _Page_last 16384 _Year 2004 _Details . save_ save_6 _Saveframe_category citation _Citation_full . _Citation_title ; Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1-4 domain of TGFBIp ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Runager Kasper . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full . _Journal_volume 286 _Journal_issue 7 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 4951 _Page_last 4958 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'transforming growth factor beta induced protein (TGFBIp)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'fourth fascilin domain (FAS1-4)' $FAS1-4_domain_of_TGFBIp stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FAS1-4_domain_of_TGFBIp _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FAS1-4_domain_of_TGFBIp _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function ; TGFBIp has been found to be a major protein in the human cornea. Mutations occurring in TGFBIp may cause the eye dystrophies, which lead to blindness. The majority of the diseases causing mutations are located in the last domain of TGFBIp, named fourth fascilin-1 (FAS1-4) domain. ; stop_ _Details ; The FAS1-4 domain contains the naturally occurring C-terminal of corneal TGFBIp and two additional residues added to N-terminus due to the expression and purification protocol, which are not part of the native TGFBIp sequence. They are denominated as A and G in the beginning of the sequence and A500 G501 in the uploaded assignments file. ; ############################## # Polymer residue sequence # ############################## _Residue_count 158 _Mol_residue_sequence ; AGMGTVMDVLKGDNRFSMLV AAIQSAGLTETLNREGVYTV FAPTNETFRALPPRERSRLL GDAKELANILKYHIGDEILV SGGIGALVRLKSLQGDKLEV SLKNNVVSVNKEPVAEPDIM ATNGVVHVITNVLQPPANRP QERGDELADSALEIFKQA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 500 ALA 2 501 GLY 3 502 MET 4 503 GLY 5 504 THR 6 505 VAL 7 506 MET 8 507 ASP 9 508 VAL 10 509 LEU 11 510 LYS 12 511 GLY 13 512 ASP 14 513 ASN 15 514 ARG 16 515 PHE 17 516 SER 18 517 MET 19 518 LEU 20 519 VAL 21 520 ALA 22 521 ALA 23 522 ILE 24 523 GLN 25 524 SER 26 525 ALA 27 526 GLY 28 527 LEU 29 528 THR 30 529 GLU 31 530 THR 32 531 LEU 33 532 ASN 34 533 ARG 35 534 GLU 36 535 GLY 37 536 VAL 38 537 TYR 39 538 THR 40 539 VAL 41 540 PHE 42 541 ALA 43 542 PRO 44 543 THR 45 544 ASN 46 545 GLU 47 546 THR 48 547 PHE 49 548 ARG 50 549 ALA 51 550 LEU 52 551 PRO 53 552 PRO 54 553 ARG 55 554 GLU 56 555 ARG 57 556 SER 58 557 ARG 59 558 LEU 60 559 LEU 61 560 GLY 62 561 ASP 63 562 ALA 64 563 LYS 65 564 GLU 66 565 LEU 67 566 ALA 68 567 ASN 69 568 ILE 70 569 LEU 71 570 LYS 72 571 TYR 73 572 HIS 74 573 ILE 75 574 GLY 76 575 ASP 77 576 GLU 78 577 ILE 79 578 LEU 80 579 VAL 81 580 SER 82 581 GLY 83 582 GLY 84 583 ILE 85 584 GLY 86 585 ALA 87 586 LEU 88 587 VAL 89 588 ARG 90 589 LEU 91 590 LYS 92 591 SER 93 592 LEU 94 593 GLN 95 594 GLY 96 595 ASP 97 596 LYS 98 597 LEU 99 598 GLU 100 599 VAL 101 600 SER 102 601 LEU 103 602 LYS 104 603 ASN 105 604 ASN 106 605 VAL 107 606 VAL 108 607 SER 109 608 VAL 110 609 ASN 111 610 LYS 112 611 GLU 113 612 PRO 114 613 VAL 115 614 ALA 116 615 GLU 117 616 PRO 118 617 ASP 119 618 ILE 120 619 MET 121 620 ALA 122 621 THR 123 622 ASN 124 623 GLY 125 624 VAL 126 625 VAL 127 626 HIS 128 627 VAL 129 628 ILE 130 629 THR 131 630 ASN 132 631 VAL 133 632 LEU 134 633 GLN 135 634 PRO 136 635 PRO 137 636 ALA 138 637 ASN 139 638 ARG 140 639 PRO 141 640 GLN 142 641 GLU 143 642 ARG 144 643 GLY 145 644 ASP 146 645 GLU 147 646 LEU 148 647 ALA 149 648 ASP 150 649 SER 151 650 ALA 152 651 LEU 153 652 GLU 154 653 ILE 155 654 PHE 156 655 LYS 157 656 GLN 158 657 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $FAS1-4_domain_of_TGFBIp Human 9606 Eukaryota Metazoa Homo sapiens TGFBI 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 $FAS1-4_domain_of_TGFBIp 'recombinant technology' . Escherichia coli BL21(DE3) 'ChampionTM pET SUMO Protein Expression System' ; The mutant FAS1-4 domain (residues 502 657) was constructed from the corresponding TGFBI clones using the following primers: 5-gcaggtatggggactgtcatggatgtcct-3 (for- ward) and 5-tcatgcttgtttgaagatctcaagcgca-3 (reverse), which add two additional amino acids (Ala-Gly) at the N terminus of FAS1-4 domain compared with the native TGFBIp amino acid sequence (SwissProt accession number Q15582) and include the authentic C terminus of corneal TGFBIp. PCR products were subsequently cloned into the ChampionTM pET SUMO Protein Expression System (Invitrogen) according to the manufacturer s instructions. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_FAS1-4 _Saveframe_category sample _Sample_type solution _Details 'Fibrillated FAS1-4 sample was fully denatured in 95% DMSO, 4% water and 1% TFA' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling H2O 4 % 'natural abundance' DMSO 95 % 'natural abundance' TFA 1 % 'natural abundance' $FAS1-4_domain_of_TGFBIp 3.3 mg/mL '[U-100% 13C; U-100% 15N]' 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $FAS1-4 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $FAS1-4 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $FAS1-4 save_ save_3D_HNCOCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCO' _Sample_label $FAS1-4 save_ save_(H)CC(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH _Sample_label $FAS1-4 save_ save_(HN)CO(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name (HN)CO(CO)NH _Sample_label $FAS1-4 save_ save_(H)N(COCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (H)N(COCO)NH _Sample_label $FAS1-4 save_ save_3D_HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details ; In order to improve the resolution of the 13C and 15N dimensions relative to existing pulse schemes, both t1 and t2 were implemented as semi-constant time chemical shift evolution periods (Ref.7) ; save_ save_3D_HNCOCO _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCOCO _BMRB_pulse_sequence_accession_number . _Details ; In order to improve the resolution of the 13C and 15N dimensions relative to existing pulse schemes, both t1 and t2 were implemented as semi-constant time chemical shift evolution periods (Ref.7) ; save_ save_3D_(H)CC(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D_(H)CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details ; In order to improve the resolution of the 13C and 15N dimensions relative to existing pulse schemes, both t1 and t2 were implemented as semi-constant time chemical shift evolution periods (Ref.7) ; save_ save_3D_(HN)CO(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D_(HN)CO(CO)NH _BMRB_pulse_sequence_accession_number . _Details ; In order to improve the resolution of the 13C and 15N dimensions relative to existing pulse schemes, both t1 and t2 were implemented as semi-constant time chemical shift evolution periods (Ref.7) ; save_ save_3D_(H)N(COCO)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D_(H)N(COCO)NH _BMRB_pulse_sequence_accession_number . _Details ; In order to improve the resolution of the 13C and 15N dimensions relative to existing pulse schemes, both t1 and t2 were implemented as semi-constant time chemical shift evolution periods (Ref.7) ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.9 . pH temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCOCO' (H)CC(CO)NH (HN)CO(CO)NH (H)N(COCO)NH stop_ loop_ _Sample_label $FAS1-4 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'fourth fascilin domain (FAS1-4)' _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 1 500 1 ALA C C 174.108 0.500 1 2 501 2 GLY H H 8.615 0.010 1 3 501 2 GLY C C 172.711 0.500 1 4 501 2 GLY N N 107.742 0.086 1 5 502 3 MET H H 8.252 0.010 1 6 502 3 MET C C 175.806 0.500 1 7 502 3 MET CA C 56.224 0.500 1 8 502 3 MET CB C 33.659 0.500 1 9 502 3 MET N N 118.342 0.086 1 10 503 4 GLY H H 8.300 0.010 1 11 503 4 GLY C C 173.133 0.500 1 12 503 4 GLY CA C 46.189 0.500 1 13 503 4 GLY N N 107.903 0.086 1 14 504 5 THR H H 7.772 0.010 1 15 504 5 THR C C 174.299 0.500 1 16 504 5 THR CA C 62.172 0.500 1 17 504 5 THR CG2 C 23.664 0.500 1 18 504 5 THR N N 112.113 0.086 1 19 505 6 VAL H H 7.814 0.010 1 20 505 6 VAL C C 175.244 0.500 1 21 505 6 VAL CA C 62.105 0.500 1 22 505 6 VAL CB C 34.583 0.500 1 23 505 6 VAL CG1 C 23.553 0.500 2 24 505 6 VAL CG2 C 22.437 0.500 2 25 505 6 VAL N N 117.818 0.086 1 26 506 7 MET H H 8.092 0.010 1 27 506 7 MET C C 175.507 0.500 1 28 506 7 MET CA C 56.102 0.500 1 29 506 7 MET CB C 36.615 0.500 1 30 506 7 MET CG C 33.631 0.500 1 31 506 7 MET N N 120.548 0.086 1 32 507 8 ASP H H 8.268 0.010 1 33 507 8 ASP C C 174.736 0.500 1 34 507 8 ASP CA C 53.855 0.500 1 35 507 8 ASP CB C 39.729 0.500 1 36 507 8 ASP N N 119.485 0.086 1 37 508 9 VAL H H 7.678 0.010 1 38 508 9 VAL C C 175.085 0.500 1 39 508 9 VAL CA C 61.917 0.500 1 40 508 9 VAL CB C 34.828 0.500 1 41 508 9 VAL CG1 C 23.432 0.500 2 42 508 9 VAL CG2 C 22.195 0.500 2 43 508 9 VAL N N 115.716 0.086 1 44 509 10 LEU H H 7.972 0.010 1 45 509 10 LEU C C 176.353 0.500 1 46 509 10 LEU CA C 55.239 0.500 1 47 509 10 LEU CB C 44.510 0.500 1 48 509 10 LEU CG C 28.267 0.500 1 49 509 10 LEU CD1 C 27.368 0.500 2 50 509 10 LEU CD2 C 25.611 0.500 2 51 509 10 LEU N N 122.360 0.086 1 52 510 11 LYS H H 7.939 0.010 1 53 510 11 LYS C C 176.159 0.500 1 54 510 11 LYS CD C 28.640 0.500 1 55 510 11 LYS CE C 43.053 0.500 1 56 510 11 LYS N N 119.339 0.086 1 57 511 12 GLY H H 8.107 0.010 1 58 511 12 GLY C C 173.184 0.500 1 59 511 12 GLY CA C 46.033 0.500 1 60 511 12 GLY N N 107.105 0.086 1 61 512 13 ASP H H 8.261 0.010 1 62 512 13 ASP C C 174.880 0.500 1 63 512 13 ASP CA C 53.674 0.500 1 64 512 13 ASP CB C 40.270 0.500 1 65 512 13 ASP N N 118.073 0.086 1 66 513 14 ASN H H 8.164 0.010 1 67 513 14 ASN C C 175.486 0.500 1 68 513 14 ASN N N 117.961 0.086 1 69 514 15 ARG H H 8.046 0.010 1 70 514 15 ARG C C 175.720 0.500 1 71 514 15 ARG CA C 57.195 0.500 1 72 514 15 ARG CB C 32.812 0.500 1 73 514 15 ARG CG C 28.662 0.500 1 74 514 15 ARG CD C 44.730 0.500 1 75 514 15 ARG N N 119.458 0.086 1 76 515 16 PHE H H 8.060 0.010 1 77 515 16 PHE C C 175.697 0.500 1 78 515 16 PHE CA C 58.517 0.500 1 79 515 16 PHE CB C 41.322 0.500 1 80 515 16 PHE N N 117.451 0.086 1 81 516 17 SER H H 8.103 0.010 1 82 516 17 SER C C 174.515 0.500 1 83 516 17 SER CA C 59.750 0.500 1 84 516 17 SER CB C 66.256 0.500 1 85 516 17 SER N N 115.036 0.086 1 86 517 18 MET H H 7.996 0.010 1 87 517 18 MET C C 175.412 0.500 1 88 517 18 MET CA C 56.460 0.500 1 89 517 18 MET CG C 33.592 0.500 1 90 517 18 MET N N 119.668 0.086 1 91 518 19 LEU H H 8.017 0.010 1 92 518 19 LEU C C 176.376 0.500 1 93 518 19 LEU N N 120.332 0.086 1 94 519 20 VAL H H 7.749 0.010 1 95 519 20 VAL C C 175.065 0.500 1 96 519 20 VAL CA C 62.208 0.500 1 97 519 20 VAL CB C 34.725 0.500 1 98 519 20 VAL CG1 C 23.455 0.500 2 99 519 20 VAL CG2 C 22.504 0.500 2 100 519 20 VAL N N 116.272 0.086 1 101 520 21 ALA H H 8.038 0.010 1 102 520 21 ALA C C 176.469 0.500 1 103 520 21 ALA CA C 52.607 0.500 1 104 520 21 ALA CB C 22.080 0.500 1 105 520 21 ALA N N 123.872 0.086 1 106 521 22 ALA H H 8.001 0.010 1 107 521 22 ALA C C 176.654 0.500 1 108 521 22 ALA CA C 52.763 0.500 1 109 521 22 ALA CB C 21.936 0.500 1 110 521 22 ALA N N 120.999 0.086 1 111 522 23 ILE H H 7.766 0.010 1 112 522 23 ILE C C 175.464 0.500 1 113 522 23 ILE N N 116.139 0.086 1 114 523 24 GLN H H 8.100 0.010 1 115 523 24 GLN C C 175.694 0.500 1 116 523 24 GLN CA C 56.698 0.500 1 117 523 24 GLN CB C 31.46 0.500 1 118 523 24 GLN CG C 35.612 0.500 1 119 523 24 GLN N N 121.632 0.086 1 120 524 25 SER H H 7.900 0.010 1 121 524 25 SER C C 174.358 0.500 1 122 524 25 SER N N 114.811 0.086 1 123 525 26 ALA H H 8.128 0.010 1 124 525 26 ALA C C 177.065 0.500 1 125 525 26 ALA CA C 53.030 0.500 1 126 525 26 ALA CB C 22.033 0.500 1 127 525 26 ALA N N 123.585 0.086 1 128 526 27 GLY H H 8.128 0.010 1 129 526 27 GLY C C 172.966 0.500 1 130 526 27 GLY N N 105.430 0.086 1 131 527 28 LEU H H 7.930 0.010 1 132 527 28 LEU C C 176.652 0.500 1 133 527 28 LEU CA C 55.406 0.500 1 134 527 28 LEU CB C 44.972 0.500 1 135 527 28 LEU CG C 28.359 0.500 1 136 527 28 LEU CD1 C 27.334 0.500 2 137 527 28 LEU CD2 C 25.899 0.500 2 138 527 28 LEU N N 119.433 0.086 1 139 528 29 THR H H 7.916 0.010 1 140 528 29 THR C C 174.423 0.500 1 141 528 29 THR CA C 62.836 0.500 1 142 528 29 THR CB C 70.811 0.500 1 143 528 29 THR CG2 C 23.990 0.500 1 144 528 29 THR N N 113.131 0.086 1 145 529 30 GLU H H 7.905 0.010 1 146 529 30 GLU C C 175.519 0.500 1 147 529 30 GLU CA C 56.225 0.500 1 148 529 30 GLU CB C 34.286 0.500 1 149 529 30 GLU N N 119.995 0.086 1 150 530 31 THR H H 7.815 0.010 1 151 530 31 THR C C 174.191 0.500 1 152 530 31 THR CA C 62.432 0.500 1 153 530 31 THR CB C 71.129 0.500 1 154 530 31 THR CG2 C 23.843 0.500 1 155 530 31 THR N N 113.520 0.086 1 156 531 32 LEU H H 7.937 0.010 1 157 531 32 LEU C C 176.428 0.500 1 158 531 32 LEU CA C 55.385 0.500 1 159 531 32 LEU CB C 44.848 0.500 1 160 531 32 LEU CG C 28.279 0.500 1 161 531 32 LEU CD1 C 27.300 0.500 2 162 531 32 LEU CD2 C 25.726 0.500 2 163 531 32 LEU N N 121.428 0.086 1 164 532 33 ASN H H 8.133 0.010 1 165 532 33 ASN C C 175.410 0.500 1 166 532 33 ASN CA C 57.928 0.500 1 167 532 33 ASN CB C 41.408 0.500 1 168 532 33 ASN N N 118.673 0.086 1 169 533 34 ARG H H 8.024 0.010 1 170 533 34 ARG C C 175.607 0.500 1 171 533 34 ARG CA C 56.639 0.500 1 172 533 34 ARG CB C 32.960 0.500 1 173 533 34 ARG CG C 28.709 0.500 1 174 533 34 ARG CD C 44.745 0.500 1 175 533 34 ARG N N 119.361 0.086 1 176 534 35 GLU H H 8.037 0.010 1 177 534 35 GLU C C 175.785 0.500 1 178 534 35 GLU CA C 56.453 0.500 1 179 534 35 GLU CB C 30.892 0.500 1 180 534 35 GLU CG C 34.427 0.500 1 181 534 35 GLU N N 117.940 0.086 1 182 535 36 GLY H H 8.065 0.010 1 183 535 36 GLY C C 172.839 0.500 1 184 535 36 GLY CA C 46.198 0.500 1 185 535 36 GLY N N 107.370 0.086 1 186 536 37 VAL H H 7.710 0.010 1 187 536 37 VAL C C 175.169 0.500 1 188 536 37 VAL CA C 61.565 0.500 1 189 536 37 VAL CB C 35.024 0.500 1 190 536 37 VAL CG1 C 23.518 0.500 2 191 536 37 VAL CG2 C 22.255 0.500 2 192 536 37 VAL N N 115.139 0.086 1 193 537 38 TYR H H 8.123 0.010 1 194 537 38 TYR C C 175.662 0.500 1 195 537 38 TYR CA C 58.490 0.500 1 196 537 38 TYR CB C 40.786 0.500 1 197 537 38 TYR N N 121.248 0.086 1 198 538 39 THR H H 7.914 0.010 1 199 538 39 THR C C 173.915 0.500 1 200 538 39 THR CA C 62.097 0.500 1 201 538 39 THR CG2 C 23.615 0.500 1 202 538 39 THR N N 112.962 0.086 1 203 539 40 VAL H H 7.595 0.010 1 204 539 40 VAL C C 174.944 0.500 1 205 539 40 VAL CA C 61.675 0.500 1 206 539 40 VAL CB C 34.897 0.500 1 207 539 40 VAL CG1 C 23.432 0.500 2 208 539 40 VAL CG2 C 21.932 0.500 2 209 539 40 VAL N N 116.715 0.086 1 210 540 41 PHE H H 8.050 0.010 1 211 540 41 PHE C C 174.738 0.500 1 212 540 41 PHE CA C 57.765 0.500 1 213 540 41 PHE CB C 41.579 0.500 1 214 540 41 PHE N N 120.555 0.086 1 215 541 42 ALA H H 8.184 0.010 1 216 541 42 ALA C C 174.858 0.500 1 217 541 42 ALA N N 123.120 0.086 1 218 542 43 PRO C C 176.308 0.500 1 219 542 43 PRO CA C 63.643 0.500 1 220 542 43 PRO CB C 33.101 0.500 1 221 542 43 PRO CG C 28.735 0.500 1 222 542 43 PRO CD C 50.978 0.500 1 223 543 44 THR H H 7.847 0.010 1 224 543 44 THR C C 174.279 0.500 1 225 543 44 THR CA C 62.577 0.500 1 226 543 44 THR CG2 C 23.628 0.500 1 227 543 44 THR N N 111.389 0.086 1 228 544 45 ASN H H 8.067 0.010 1 229 544 45 ASN C C 175.376 0.500 1 230 544 45 ASN CA C 54.078 0.500 1 231 544 45 ASN CB C 40.904 0.500 1 232 544 45 ASN N N 119.114 0.086 1 233 545 46 GLU H H 7.935 0.010 1 234 545 46 GLU C C 175.457 0.500 1 235 545 46 GLU CA C 56.366 0.500 1 236 545 46 GLU CB C 30.786 0.500 1 237 545 46 GLU CG C 34.329 0.500 1 238 545 46 GLU N N 118.472 0.086 1 239 546 47 THR H H 7.700 0.010 1 240 546 47 THR C C 174.138 0.500 1 241 546 47 THR CA C 62.669 0.500 1 242 546 47 THR CG2 C 23.557 0.500 1 243 546 47 THR N N 112.820 0.086 1 244 547 48 PHE H H 7.946 0.010 1 245 547 48 PHE C C 175.264 0.500 1 246 547 48 PHE CA C 58.203 0.500 1 247 547 48 PHE CB C 41.411 0.500 1 248 547 48 PHE N N 119.506 0.086 1 249 548 49 ARG H H 8.141 0.010 1 250 548 49 ARG C C 174.986 0.500 1 251 548 49 ARG CA C 56.434 0.500 1 252 548 49 ARG CB C 33.212 0.500 1 253 548 49 ARG CG C 28.898 0.500 1 254 548 49 ARG CD C 44.745 0.500 1 255 548 49 ARG N N 119.561 0.086 1 256 549 50 ALA H H 7.918 0.010 1 257 549 50 ALA C C 176.251 0.500 1 258 549 50 ALA CA C 51.985 0.500 1 259 549 50 ALA CB C 22.480 0.500 1 260 549 50 ALA N N 122.147 0.086 1 261 550 51 LEU H H 8.010 0.010 1 262 550 51 LEU C C 174.356 0.500 1 263 550 51 LEU N N 119.414 0.086 1 264 551 52 PRO C C 176.436 0.500 1 265 553 54 ARG H H 8.052 0.010 1 266 553 54 ARG C C 175.930 0.500 1 267 553 54 ARG N N 117.973 0.086 1 268 554 55 GLU H H 7.863 0.010 1 269 554 55 GLU C C 175.544 0.500 1 270 554 55 GLU N N 118.046 0.086 1 271 555 56 ARG H H 8.020 0.010 1 272 555 56 ARG C C 175.833 0.500 1 273 555 56 ARG N N 119.691 0.086 1 274 556 57 SER H H 8.013 0.010 1 275 556 57 SER C C 174.664 0.500 1 276 556 57 SER N N 115.094 0.086 1 277 557 58 ARG H H 8.162 0.010 1 278 557 58 ARG C C 175.726 0.500 1 279 557 58 ARG CA C 56.821 0.500 1 280 557 58 ARG CB C 33.186 0.500 1 281 557 58 ARG CG C 28.911 0.500 1 282 557 58 ARG CD C 44.826 0.500 1 283 557 58 ARG N N 121.123 0.086 1 284 558 59 LEU H H 7.956 0.010 1 285 558 59 LEU C C 176.454 0.500 1 286 558 59 LEU CA C 55.402 0.500 1 287 558 59 LEU CB C 44.659 0.500 1 288 558 59 LEU CD1 C 27.334 0.500 2 289 558 59 LEU CD2 C 25.633 0.500 2 290 558 59 LEU N N 120.011 0.086 1 291 559 60 LEU H H 7.953 0.010 1 292 559 60 LEU C C 176.926 0.500 1 293 559 60 LEU CA C 55.573 0.500 1 294 559 60 LEU CB C 45.038 0.500 1 295 559 60 LEU CG C 28.323 0.500 1 296 559 60 LEU CD1 C 27.242 0.500 2 297 559 60 LEU CD2 C 25.770 0.500 2 298 559 60 LEU N N 120.143 0.086 1 299 560 61 GLY H H 8.090 0.010 1 300 560 61 GLY C C 173.262 0.500 1 301 560 61 GLY N N 106.562 0.086 1 302 561 62 ASP H H 8.177 0.010 1 303 561 62 ASP C C 174.962 0.500 1 304 561 62 ASP CA C 53.681 0.500 1 305 561 62 ASP CB C 40.220 0.500 1 306 561 62 ASP N N 117.912 0.086 1 307 562 63 ALA H H 8.055 0.010 1 308 562 63 ALA C C 176.806 0.500 1 309 562 63 ALA CA C 53.116 0.500 1 310 562 63 ALA CB C 21.893 0.500 1 311 562 63 ALA N N 121.968 0.086 1 312 563 64 LYS H H 7.995 0.010 1 313 563 64 LYS C C 176.050 0.500 1 314 563 64 LYS N N 117.793 0.086 1 315 564 65 GLU H H 7.927 0.010 1 316 564 65 GLU C C 175.645 0.500 1 317 564 65 GLU CA C 56.318 0.500 1 318 564 65 GLU CG C 34.331 0.500 1 319 564 65 GLU N N 118.337 0.086 1 320 565 66 LEU H H 7.946 0.010 1 321 565 66 LEU C C 176.343 0.500 1 322 565 66 LEU CA C 55.367 0.500 1 323 565 66 LEU CB C 44.564 0.500 1 324 565 66 LEU CG C 28.245 0.500 1 325 565 66 LEU CD1 C 27.317 0.500 2 326 565 66 LEU CD2 C 25.662 0.500 2 327 565 66 LEU N N 120.504 0.086 1 328 566 67 ALA H H 8.073 0.010 1 329 566 67 ALA C C 176.867 0.500 1 330 566 67 ALA CA C 52.754 0.500 1 331 566 67 ALA CB C 22.078 0.500 1 332 566 67 ALA N N 121.521 0.086 1 333 567 68 ASN H H 8.129 0.010 1 334 567 68 ASN C C 175.642 0.500 1 335 567 68 ASN N N 117.571 0.086 1 336 568 69 ILE H H 7.751 0.010 1 337 568 69 ILE C C 175.605 0.500 1 338 568 69 ILE CA C 61.724 0.500 1 339 568 69 ILE CG2 C 19.642 0.500 1 340 568 69 ILE CD1 C 15.541 0.500 1 341 568 69 ILE N N 117.181 0.086 1 342 569 70 LEU H H 8.025 0.010 1 343 569 70 LEU C C 176.626 0.500 1 344 569 70 LEU CB C 44.182 0.500 1 345 569 70 LEU CG C 28.362 0.500 1 346 569 70 LEU CD1 C 27.234 0.500 2 347 569 70 LEU CD2 C 25.618 0.500 2 348 569 70 LEU N N 122.029 0.086 1 349 570 71 LYS H H 7.820 0.010 1 350 570 71 LYS C C 175.788 0.500 1 351 570 71 LYS CA C 56.858 0.500 1 352 570 71 LYS CB C 35.043 0.500 1 353 570 71 LYS CG C 26.481 0.500 1 354 570 71 LYS CD C 30.895 0.500 1 355 570 71 LYS N N 118.612 0.086 1 356 571 72 TYR H H 7.729 0.010 1 357 571 72 TYR C C 175.406 0.500 1 358 571 72 TYR CA C 58.383 0.500 1 359 571 72 TYR CB C 40.712 0.500 1 360 571 72 TYR N N 117.192 0.086 1 361 572 73 HIS H H 8.301 0.010 1 362 572 73 HIS C C 173.871 0.500 1 363 572 73 HIS CA C 55.698 0.500 1 364 572 73 HIS CB C 31.216 0.500 1 365 572 73 HIS N N 117.652 0.086 1 366 573 74 ILE H H 7.900 0.010 1 367 573 74 ILE C C 175.684 0.500 1 368 573 74 ILE CA C 61.483 0.500 1 369 573 74 ILE CB C 40.937 0.500 1 370 573 74 ILE CG1 C 28.322 0.500 1 371 573 74 ILE CG2 C 19.592 0.500 1 372 573 74 ILE CD1 C 15.376 0.500 1 373 573 74 ILE N N 119.140 0.086 1 374 574 75 GLY H H 8.332 0.010 1 375 574 75 GLY C C 173.051 0.500 1 376 574 75 GLY N N 110.787 0.086 1 377 575 76 ASP H H 8.243 0.010 1 378 575 76 ASP N N 118.258 0.086 1 379 576 77 GLU C C 174.925 0.500 1 380 577 78 ILE H H 8.046 0.010 1 381 577 78 ILE C C 175.149 0.500 1 382 577 78 ILE CA C 61.139 0.500 1 383 577 78 ILE CB C 40.726 0.500 1 384 577 78 ILE CG2 C 19.595 0.500 1 385 577 78 ILE CD1 C 15.167 0.500 1 386 577 78 ILE N N 118.230 0.086 1 387 578 79 LEU H H 8.138 0.010 1 388 578 79 LEU C C 176.192 0.500 1 389 578 79 LEU CA C 55.284 0.500 1 390 578 79 LEU CB C 44.831 0.500 1 391 578 79 LEU CG C 28.365 0.500 1 392 578 79 LEU CD1 C 27.282 0.500 2 393 578 79 LEU CD2 C 25.718 0.500 2 394 578 79 LEU N N 123.937 0.086 1 395 579 80 VAL H H 7.731 0.010 1 396 579 80 VAL C C 175.227 0.500 1 397 579 80 VAL CA C 61.693 0.500 1 398 579 80 VAL CB C 34.914 0.500 1 399 579 80 VAL CG1 C 23.398 0.500 2 400 579 80 VAL CG2 C 22.210 0.500 2 401 579 80 VAL N N 116.219 0.086 1 402 580 81 SER H H 8.015 0.010 1 403 580 81 SER C C 174.766 0.500 1 404 580 81 SER N N 117.057 0.086 1 405 581 82 GLY H H 8.193 0.010 1 406 581 82 GLY C C 173.570 0.500 1 407 581 82 GLY CA C 46.381 0.500 1 408 581 82 GLY N N 108.816 0.086 1 409 582 83 GLY H H 8.110 0.010 1 410 582 83 GLY C C 173.435 0.500 1 411 582 83 GLY CA C 46.175 0.500 1 412 582 83 GLY N N 106.586 0.086 1 413 583 84 ILE H H 7.996 0.010 1 414 583 84 ILE C C 176.069 0.500 1 415 583 84 ILE CA C 61.761 0.500 1 416 583 84 ILE CB C 40.534 0.500 1 417 583 84 ILE CG1 C 28.692 0.500 1 418 583 84 ILE CG2 C 19.668 0.500 1 419 583 84 ILE CD1 C 15.353 0.500 1 420 583 84 ILE N N 117.611 0.086 1 421 584 85 GLY H H 8.316 0.010 1 422 584 85 GLY C C 173.197 0.500 1 423 584 85 GLY CA C 46.468 0.500 1 424 584 85 GLY N N 110.441 0.086 1 425 585 86 ALA H H 7.925 0.010 1 426 585 86 ALA C C 177.060 0.500 1 427 585 86 ALA CA C 52.900 0.500 1 428 585 86 ALA CB C 22.148 0.500 1 429 585 86 ALA N N 121.250 0.086 1 430 586 87 LEU H H 8.038 0.010 1 431 586 87 LEU C C 176.662 0.500 1 432 586 87 LEU CB C 44.316 0.500 1 433 586 87 LEU CG C 28.348 0.500 1 434 586 87 LEU CD1 C 27.196 0.500 2 435 586 87 LEU CD2 C 25.787 0.500 2 436 586 87 LEU N N 119.049 0.086 1 437 587 88 VAL H H 7.664 0.010 1 438 587 88 VAL C C 175.576 0.500 1 439 587 88 VAL CA C 62.468 0.500 1 440 587 88 VAL CB C 34.616 0.500 1 441 587 88 VAL CG1 C 23.346 0.500 2 442 587 88 VAL CG2 C 22.590 0.500 2 443 587 88 VAL N N 115.944 0.086 1 444 588 89 ARG H H 8.045 0.010 1 445 588 89 ARG C C 175.874 0.500 1 446 588 89 ARG CA C 56.833 0.500 1 447 588 89 ARG CB C 33.143 0.500 1 448 588 89 ARG CG C 29.000 0.500 1 449 588 89 ARG CD C 44.667 0.500 1 450 588 89 ARG N N 121.869 0.086 1 451 589 90 LEU H H 7.919 0.010 1 452 589 90 LEU C C 176.730 0.500 1 453 589 90 LEU CA C 55.746 0.500 1 454 589 90 LEU CB C 44.842 0.500 1 455 589 90 LEU CG C 28.404 0.500 1 456 589 90 LEU CD1 C 27.341 0.500 2 457 589 90 LEU CD2 C 25.658 0.500 2 458 589 90 LEU N N 120.569 0.086 1 459 590 91 LYS H H 8.030 0.010 1 460 590 91 LYS C C 176.245 0.500 1 461 590 91 LYS CA C 57.052 0.500 1 462 590 91 LYS CB C 35.037 0.500 1 463 590 91 LYS CG C 26.476 0.500 1 464 590 91 LYS CD C 30.986 0.500 1 465 590 91 LYS CE C 43.112 0.500 1 466 590 91 LYS N N 118.902 0.086 1 467 591 92 SER H H 7.905 0.010 1 468 591 92 SER C C 174.593 0.500 1 469 591 92 SER CA C 59.475 0.500 1 470 591 92 SER CB C 65.715 0.500 1 471 591 92 SER N N 114.548 0.086 1 472 592 93 LEU H H 8.021 0.010 1 473 592 93 LEU C C 176.650 0.500 1 474 592 93 LEU CA C 55.591 0.500 1 475 592 93 LEU CB C 44.453 0.500 1 476 592 93 LEU CG C 28.314 0.500 1 477 592 93 LEU CD1 C 27.420 0.500 2 478 592 93 LEU CD2 C 25.602 0.500 2 479 592 93 LEU N N 121.693 0.086 1 480 593 94 GLN H H 7.969 0.010 1 481 593 94 GLN C C 176.066 0.500 1 482 593 94 GLN CA C 56.776 0.500 1 483 593 94 GLN CB C 32.41 0.500 1 484 593 94 GLN CG C 35.564 0.500 1 485 593 94 GLN N N 118.442 0.086 1 486 594 95 GLY H H 8.093 0.010 1 487 594 95 GLY C C 173.221 0.500 1 488 594 95 GLY CA C 46.103 0.500 1 489 594 95 GLY N N 107.114 0.086 1 490 595 96 ASP H H 8.186 0.010 1 491 595 96 ASP C C 174.986 0.500 1 492 595 96 ASP CA C 53.907 0.500 1 493 595 96 ASP CB C 40.243 0.500 1 494 595 96 ASP CG C 176.063 0.500 1 495 595 96 ASP N N 118.068 0.086 1 496 596 97 LYS H H 7.971 0.010 1 497 596 97 LYS C C 175.635 0.500 1 498 596 97 LYS CA C 56.631 0.500 1 499 596 97 LYS CB C 35.362 0.500 1 500 596 97 LYS CG C 26.349 0.500 1 501 596 97 LYS CD C 30.866 0.500 1 502 596 97 LYS CE C 43.148 0.500 1 503 596 97 LYS N N 118.789 0.086 1 504 597 98 LEU H H 7.906 0.010 1 505 597 98 LEU C C 176.512 0.500 1 506 597 98 LEU CA C 55.402 0.500 1 507 597 98 LEU CB C 44.893 0.500 1 508 597 98 LEU CG C 28.365 0.500 1 509 597 98 LEU CD1 C 27.273 0.500 2 510 597 98 LEU CD2 C 25.890 0.500 2 511 597 98 LEU N N 119.843 0.086 1 512 598 99 GLU H H 8.087 0.010 1 513 598 99 GLU C C 175.313 0.500 1 514 598 99 GLU CA C 56.209 0.500 1 515 598 99 GLU CG C 34.519 0.500 1 516 598 99 GLU N N 119.442 0.086 1 517 599 100 VAL H H 7.642 0.010 1 518 599 100 VAL C C 175.119 0.500 1 519 599 100 VAL CA C 61.538 0.500 1 520 599 100 VAL CB C 35.094 0.500 1 521 599 100 VAL CG1 C 23.372 0.500 2 522 599 100 VAL CG2 C 22.093 0.500 2 523 599 100 VAL N N 115.870 0.086 1 524 600 101 SER H H 8.068 0.010 1 525 600 101 SER C C 174.589 0.500 1 526 600 101 SER CA C 59.013 0.500 1 527 600 101 SER CB C 65.895 0.500 1 528 600 101 SER N N 117.377 0.086 1 529 601 102 LEU H H 8.072 0.010 1 530 601 102 LEU C C 176.401 0.500 1 531 601 102 LEU CA C 55.505 0.500 1 532 601 102 LEU CB C 44.600 0.500 1 533 601 102 LEU CG C 28.254 0.500 1 534 601 102 LEU CD1 C 27.415 0.500 2 535 601 102 LEU CD2 C 25.592 0.500 2 536 601 102 LEU N N 122.471 0.086 1 537 602 103 LYS H H 7.912 0.010 1 538 602 103 LYS C C 175.634 0.500 1 539 602 103 LYS CA C 56.514 0.500 1 540 602 103 LYS CB C 35.323 0.500 1 541 602 103 LYS CG C 26.133 0.500 1 542 602 103 LYS CD C 30.966 0.500 1 543 602 103 LYS CE C 43.079 0.500 1 544 602 103 LYS N N 118.330 0.086 1 545 603 104 ASN H H 8.080 0.010 1 546 603 104 ASN C C 175.197 0.500 1 547 603 104 ASN CA C 54.017 0.500 1 548 603 104 ASN CB C 41.563 0.500 1 549 603 104 ASN N N 118.434 0.086 1 550 604 105 ASN H H 8.135 0.010 1 551 604 105 ASN C C 175.061 0.500 1 552 604 105 ASN CA C 54.044 0.500 1 553 604 105 ASN CB C 41.133 0.500 1 554 604 105 ASN N N 118.391 0.086 1 555 605 106 VAL H H 7.707 0.010 1 556 605 106 VAL C C 175.174 0.500 1 557 605 106 VAL CA C 62.217 0.500 1 558 605 106 VAL CB C 34.533 0.500 1 559 605 106 VAL CG1 C 23.596 0.500 2 560 605 106 VAL CG2 C 22.341 0.500 2 561 605 106 VAL N N 115.258 0.086 1 562 606 107 VAL H H 7.842 0.010 1 563 606 107 VAL C C 175.296 0.500 1 564 606 107 VAL CA C 62.049 0.500 1 565 606 107 VAL CB C 34.670 0.500 1 566 606 107 VAL CG1 C 23.492 0.500 2 567 606 107 VAL CG2 C 22.461 0.500 2 568 606 107 VAL N N 118.360 0.086 1 569 607 108 SER H H 7.980 0.010 1 570 607 108 SER C C 174.401 0.500 1 571 607 108 SER CA C 59.080 0.500 1 572 607 108 SER CB C 65.809 0.500 1 573 607 108 SER N N 117.494 0.086 1 574 608 109 VAL H H 7.761 0.010 1 575 608 109 VAL C C 175.063 0.500 1 576 608 109 VAL CA C 61.791 0.500 1 577 608 109 VAL CB C 34.849 0.500 1 578 608 109 VAL CG1 C 23.372 0.500 2 579 608 109 VAL CG2 C 22.031 0.500 2 580 608 109 VAL N N 117.140 0.086 1 581 609 110 ASN H H 8.178 0.010 1 582 609 110 ASN C C 175.140 0.500 1 583 609 110 ASN CA C 56.347 0.500 1 584 609 110 ASN CB C 41.13 0.500 1 585 609 110 ASN N N 121.093 0.086 1 586 610 111 LYS H H 7.905 0.010 1 587 610 111 LYS C C 175.671 0.500 1 588 610 111 LYS CA C 56.254 0.500 1 589 610 111 LYS CB C 35.496 0.500 1 590 610 111 LYS CD C 26.331 0.500 1 591 610 111 LYS CE C 43.017 0.500 1 592 610 111 LYS N N 118.732 0.086 1 593 611 112 GLU H H 8.039 0.010 1 594 611 112 GLU C C 174.045 0.500 1 595 611 112 GLU N N 119.408 0.086 1 596 612 113 PRO C C 175.680 0.500 1 597 612 113 PRO CA C 63.472 0.500 1 598 612 113 PRO CB C 33.361 0.500 1 599 612 113 PRO CG C 28.821 0.500 1 600 612 113 PRO CD C 51.134 0.500 1 601 613 114 VAL H H 7.820 0.010 1 602 613 114 VAL C C 174.946 0.500 1 603 613 114 VAL CA C 61.664 0.500 1 604 613 114 VAL CB C 34.916 0.500 1 605 613 114 VAL CG1 C 22.496 0.500 1 606 613 114 VAL N N 115.436 0.086 1 607 614 115 ALA H H 8.013 0.010 1 608 614 115 ALA C C 176.410 0.500 1 609 614 115 ALA CA C 52.241 0.500 1 610 614 115 ALA CB C 22.276 0.500 1 611 614 115 ALA N N 124.166 0.086 1 612 615 116 GLU H H 8.030 0.010 1 613 615 116 GLU C C 173.973 0.500 1 614 615 116 GLU N N 118.261 0.086 1 615 616 117 PRO C C 176.105 0.500 1 616 616 117 PRO CA C 63.567 0.500 1 617 616 117 PRO CB C 33.479 0.500 1 618 616 117 PRO CG C 28.563 0.500 1 619 616 117 PRO CD C 51.097 0.500 1 620 617 118 ASP H H 8.290 0.010 1 621 617 118 ASP C C 174.769 0.500 1 622 617 118 ASP CA C 53.846 0.500 1 623 617 118 ASP CG C 176.103 0.500 1 624 617 118 ASP N N 117.427 0.086 1 625 618 119 ILE H H 7.524 0.010 1 626 618 119 ILE C C 175.070 0.500 1 627 618 119 ILE CA C 61.162 0.500 1 628 618 119 ILE CB C 41.028 0.500 1 629 618 119 ILE CG2 C 19.543 0.500 1 630 618 119 ILE CD1 C 15.368 0.500 1 631 618 119 ILE N N 116.389 0.086 1 632 619 120 MET H H 8.059 0.010 1 633 619 120 MET C C 175.036 0.500 1 634 619 120 MET CA C 56.081 0.500 1 635 619 120 MET CB C 33.743 0.500 1 636 619 120 MET N N 120.996 0.086 1 637 620 121 ALA H H 8.028 0.010 1 638 620 121 ALA C C 176.829 0.500 1 639 620 121 ALA CA C 52.545 0.500 1 640 620 121 ALA CB C 21.998 0.500 1 641 620 121 ALA N N 122.736 0.086 1 642 621 122 THR H H 7.796 0.010 1 643 621 122 THR C C 174.196 0.500 1 644 621 122 THR CA C 62.184 0.500 1 645 621 122 THR CG2 C 23.572 0.500 1 646 621 122 THR N N 110.873 0.086 1 647 622 123 ASN H H 8.110 0.010 1 648 622 123 ASN C C 175.509 0.500 1 649 622 123 ASN N N 119.257 0.086 1 650 623 124 GLY H H 8.079 0.010 1 651 623 124 GLY C C 172.893 0.500 1 652 623 124 GLY CA C 46.464 0.500 1 653 623 124 GLY N N 106.287 0.086 1 654 624 125 VAL H H 7.698 0.010 1 655 624 125 VAL C C 175.364 0.500 1 656 624 125 VAL CA C 61.999 0.500 1 657 624 125 VAL CB C 34.629 0.500 1 658 624 125 VAL CG1 C 23.372 0.500 1 659 624 125 VAL CG2 C 22.570 0.500 1 660 624 125 VAL N N 115.528 0.086 1 661 625 126 VAL H H 7.935 0.010 1 662 625 126 VAL C C 175.299 0.500 1 663 625 126 VAL CA C 62.363 0.500 1 664 625 126 VAL CB C 34.345 0.500 1 665 625 126 VAL CG1 C 23.389 0.500 2 666 625 126 VAL CG2 C 22.710 0.500 2 667 625 126 VAL N N 120.017 0.086 1 668 626 127 HIS H H 8.323 0.010 1 669 626 127 HIS C C 173.978 0.500 1 670 626 127 HIS CA C 55.416 0.500 1 671 626 127 HIS CB C 31.382 0.500 1 672 626 127 HIS N N 120.867 0.086 1 673 627 128 VAL H H 7.870 0.010 1 674 627 128 VAL C C 175.270 0.500 1 675 627 128 VAL CA C 62.019 0.500 1 676 627 128 VAL CB C 34.916 0.500 1 677 627 128 VAL CG1 C 23.381 0.500 2 678 627 128 VAL CG2 C 22.298 0.500 2 679 627 128 VAL N N 117.835 0.086 1 680 628 129 ILE H H 8.143 0.010 1 681 628 129 ILE C C 175.305 0.500 1 682 628 129 ILE CA C 61.403 0.500 1 683 628 129 ILE CB C 40.325 0.500 1 684 628 129 ILE CG1 C 28.740 0.500 1 685 628 129 ILE CG2 C 19.644 0.500 1 686 628 129 ILE CD1 C 15.238 0.500 1 687 628 129 ILE N N 121.601 0.086 1 688 629 130 THR H H 7.776 0.010 1 689 629 130 THR C C 173.947 0.500 1 690 629 130 THR CA C 62.012 0.500 1 691 629 130 THR CB C 71.550 0.500 1 692 629 130 THR CG2 C 23.380 0.500 1 693 629 130 THR N N 115.228 0.086 1 694 630 131 ASN H H 8.018 0.010 1 695 630 131 ASN C C 175.244 0.500 1 696 630 131 ASN CA C 53.965 0.500 1 697 630 131 ASN CB C 41.119 0.500 1 698 630 131 ASN N N 120.150 0.086 1 699 631 132 VAL H H 7.806 0.010 1 700 631 132 VAL C C 174.934 0.500 1 701 631 132 VAL CA C 62.260 0.500 1 702 631 132 VAL CB C 34.381 0.500 1 703 631 132 VAL CG1 C 23.501 0.500 2 704 631 132 VAL CG2 C 22.045 0.500 2 705 631 132 VAL N N 115.740 0.086 1 706 632 133 LEU H H 7.953 0.010 1 707 632 133 LEU C C 176.136 0.500 1 708 632 133 LEU CB C 44.625 0.500 1 709 632 133 LEU CG C 28.296 0.500 1 710 632 133 LEU CD1 C 27.420 0.500 2 711 632 133 LEU CD2 C 25.489 0.500 2 712 632 133 LEU N N 121.299 0.086 1 713 633 134 GLN H H 7.866 0.010 1 714 633 134 GLN C C 173.701 0.500 1 715 633 134 GLN N N 119.496 0.086 1 716 635 136 PRO C C 176.103 0.500 1 717 635 136 PRO CA C 63.573 0.500 1 718 635 136 PRO CB C 33.159 0.500 1 719 635 136 PRO CG C 28.760 0.500 1 720 635 136 PRO CD C 51.033 0.500 1 721 636 137 ALA H H 8.124 0.010 1 722 636 137 ALA C C 176.543 0.500 1 723 636 137 ALA CA C 52.840 0.500 1 724 636 137 ALA CB C 21.924 0.500 1 725 636 137 ALA N N 120.586 0.086 1 726 637 138 ASN H H 8.004 0.010 1 727 637 138 ASN C C 175.014 0.500 1 728 637 138 ASN CA C 53.603 0.500 1 729 637 138 ASN CB C 40.877 0.500 1 730 637 138 ASN N N 116.117 0.086 1 731 638 139 ARG H H 7.817 0.010 1 732 638 139 ARG N N 118.542 0.086 1 733 639 140 PRO C C 176.174 0.500 1 734 639 140 PRO CA C 63.817 0.500 1 735 639 140 PRO CB C 33.312 0.500 1 736 639 140 PRO CG C 28.787 0.500 1 737 639 140 PRO CD C 51.217 0.500 1 738 640 141 GLN H H 8.211 0.010 1 739 640 141 GLN C C 175.776 0.500 1 740 640 141 GLN CA C 56.583 0.500 1 741 640 141 GLN CG C 35.685 0.500 1 742 640 141 GLN N N 118.462 0.086 1 743 641 142 GLU H H 7.936 0.010 1 744 641 142 GLU C C 175.460 0.500 1 745 641 142 GLU CA C 56.135 0.500 1 746 641 142 GLU CB C 31.134 0.500 1 747 641 142 GLU CG C 34.369 0.500 1 748 641 142 GLU N N 118.736 0.086 1 749 642 143 ARG H H 8.039 0.010 1 750 642 143 ARG C C 175.950 0.500 1 751 642 143 ARG CA C 56.363 0.500 1 752 642 143 ARG CB C 33.359 0.500 1 753 642 143 ARG CG C 28.801 0.500 1 754 642 143 ARG N N 119.697 0.086 1 755 643 144 GLY H H 8.216 0.010 1 756 643 144 GLY C C 173.032 0.500 1 757 643 144 GLY CA C 45.997 0.500 1 758 643 144 GLY N N 107.583 0.086 1 759 644 145 ASP H H 8.265 0.010 1 760 644 145 ASP C C 175.029 0.500 1 761 644 145 ASP CA C 53.649 0.500 1 762 644 145 ASP CB C 40.612 0.500 1 763 644 145 ASP N N 117.928 0.086 1 764 645 146 GLU H H 8.051 0.010 1 765 645 146 GLU C C 175.291 0.500 1 766 645 146 GLU CA C 56.471 0.500 1 767 645 146 GLU CB C 30.910 0.500 1 768 645 146 GLU CG C 34.375 0.500 1 769 645 146 GLU N N 118.340 0.086 1 770 646 147 LEU H H 7.888 0.010 1 771 646 147 LEU C C 176.159 0.500 1 772 646 147 LEU CA C 55.187 0.500 1 773 646 147 LEU CB C 44.550 0.500 1 774 646 147 LEU CG C 28.271 0.500 1 775 646 147 LEU CD1 C 27.343 0.500 2 776 646 147 LEU CD2 C 25.710 0.500 2 777 646 147 LEU N N 119.904 0.086 1 778 647 148 ALA H H 8.019 0.010 1 779 647 148 ALA C C 176.817 0.500 1 780 647 148 ALA CA C 52.506 0.500 1 781 647 148 ALA CB C 22.148 0.500 1 782 647 148 ALA N N 121.735 0.086 1 783 648 149 ASP H H 8.197 0.010 1 784 648 149 ASP C C 175.088 0.500 1 785 648 149 ASP CA C 53.825 0.500 1 786 648 149 ASP CB C 40.062 0.500 1 787 648 149 ASP N N 117.232 0.086 1 788 649 150 SER H H 7.779 0.010 1 789 649 150 SER C C 174.186 0.500 1 790 649 150 SER CA C 59.436 0.500 1 791 649 150 SER CB C 65.775 0.500 1 792 649 150 SER N N 113.722 0.086 1 793 650 151 ALA H H 8.064 0.010 1 794 650 151 ALA C C 176.544 0.500 1 795 650 151 ALA CB C 21.930 0.500 1 796 650 151 ALA N N 123.290 0.086 1 797 651 152 LEU H H 7.853 0.010 1 798 651 152 LEU C C 176.471 0.500 1 799 651 152 LEU CB C 44.716 0.500 1 800 651 152 LEU CG C 28.354 0.500 1 801 651 152 LEU CD1 C 27.190 0.500 2 802 651 152 LEU CD2 C 25.778 0.500 2 803 651 152 LEU N N 117.895 0.086 1 804 652 153 GLU H H 7.907 0.010 1 805 652 153 GLU C C 175.083 0.500 1 806 652 153 GLU CA C 56.161 0.500 1 807 652 153 GLU CB C 30.783 0.500 1 808 652 153 GLU CG C 34.428 0.500 1 809 652 153 GLU N N 118.688 0.086 1 810 653 154 ILE H H 7.593 0.010 1 811 653 154 ILE C C 175.106 0.500 1 812 653 154 ILE CA C 61.268 0.500 1 813 653 154 ILE CB C 40.829 0.500 1 814 653 154 ILE CG2 C 19.553 0.500 1 815 653 154 ILE CD1 C 15.321 0.500 1 816 653 154 ILE N N 117.448 0.086 1 817 654 155 PHE H H 8.082 0.010 1 818 654 155 PHE C C 175.252 0.500 1 819 654 155 PHE N N 121.543 0.086 1 820 655 156 LYS H H 8.027 0.010 1 821 655 156 LYS C C 175.477 0.500 1 822 655 156 LYS CA C 56.535 0.500 1 823 655 156 LYS CB C 35.658 0.500 1 824 655 156 LYS CG C 26.277 0.500 1 825 655 156 LYS CD C 30.907 0.500 1 826 655 156 LYS CE C 43.099 0.500 1 827 655 156 LYS N N 119.392 0.086 1 828 656 157 GLN H H 7.990 0.010 1 829 656 157 GLN C C 175.370 0.500 1 830 656 157 GLN CA C 56.159 0.500 1 831 656 157 GLN CB C 32.052 0.500 1 832 656 157 GLN CG C 35.680 0.500 1 833 656 157 GLN N N 118.926 0.086 1 834 657 158 ALA H H 8.286 0.010 1 835 657 158 ALA C C 172.334 0.500 1 836 657 158 ALA N N 122.483 0.086 1 stop_ save_