data_15986 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I Collagen Peptide ; _BMRB_accession_number 15986 _BMRB_flat_file_name bmr15986.str _Entry_type original _Submission_date 2008-10-15 _Accession_date 2008-10-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone chemical shift assignments of the fibronectin 8-9FnI domain pair in complex with a type-I collagen peptide' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Erat Michele C. . 2 Vakonakis Ioannis . . 3 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 174 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-20 update BMRB 'update entry citation' 2009-02-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15447 '8F19F1 module pair from Fibronectin' stop_ _Original_release_date 2015-07-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification and structural analysis of type-I collagen sites in complex with fibronectin fragments ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19251642 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Erat Michele C. . 2 Slatte David A. . 3 Lowe Edward D. . 4 Millard Christopher J. . 5 Farndale Richard W. . 6 Campbell Iain D. . 7 Vakonakis Ioannis . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci., U.S.A.' _Journal_volume 106 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4195 _Page_last 4200 _Year 2009 _Details . loop_ _Keyword complex 'extracellular matrix' 'fibronectin-collagen interaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name '89FnI-collagen complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 89FnI $89FnI 'collagen peptide' $collagen_peptide NAG $entity_NAG stop_ _System_molecular_weight 13462.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 89FnI 2 'collagen peptide' 3 NAG stop_ loop_ _Biological_function 'Cell adhesion' 'Cell migration' 'Matrix structure' stop_ _Database_query_date . _Details ; complex between the module pair 8-9FnI of fibronectin and a 23 aminoacid long peptide C-terminal of the collagenase cleavage site in the collagen I alpha1 chain ; save_ ######################## # Monomeric polymers # ######################## save_89FnI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 89FnI _Molecular_mass 10829.9 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'cell adhesion' 'collagen binding' development 'matrix protein' 'motogenic activity' 'structural protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; DQCIVDDITYNVQDTFHKKH EEGHMLNCTCFGQGRGRWKC DPVDQCQDSETGTFYQIGDS WEKYVHGVRYQCYCYGRGIG EWHCQPLQTYPSS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 516 ASP 2 517 GLN 3 518 CYS 4 519 ILE 5 520 VAL 6 521 ASP 7 522 ASP 8 523 ILE 9 524 THR 10 525 TYR 11 526 ASN 12 527 VAL 13 528 GLN 14 529 ASP 15 530 THR 16 531 PHE 17 532 HIS 18 533 LYS 19 534 LYS 20 535 HIS 21 536 GLU 22 537 GLU 23 538 GLY 24 539 HIS 25 540 MET 26 541 LEU 27 542 ASN 28 543 CYS 29 544 THR 30 545 CYS 31 546 PHE 32 547 GLY 33 548 GLN 34 549 GLY 35 550 ARG 36 551 GLY 37 552 ARG 38 553 TRP 39 554 LYS 40 555 CYS 41 556 ASP 42 557 PRO 43 558 VAL 44 559 ASP 45 560 GLN 46 561 CYS 47 562 GLN 48 563 ASP 49 564 SER 50 565 GLU 51 566 THR 52 567 GLY 53 568 THR 54 569 PHE 55 570 TYR 56 571 GLN 57 572 ILE 58 573 GLY 59 574 ASP 60 575 SER 61 576 TRP 62 577 GLU 63 578 LYS 64 579 TYR 65 580 VAL 66 581 HIS 67 582 GLY 68 583 VAL 69 584 ARG 70 585 TYR 71 586 GLN 72 587 CYS 73 588 TYR 74 589 CYS 75 590 TYR 76 591 GLY 77 592 ARG 78 593 GLY 79 594 ILE 80 595 GLY 81 596 GLU 82 597 TRP 83 598 HIS 84 599 CYS 85 600 GLN 86 601 PRO 87 602 LEU 88 603 GLN 89 604 THR 90 605 TYR 91 606 PRO 92 607 SER 93 608 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-29 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 15447 8F19F1 94.62 88 98.86 98.86 3.77e-57 PDB 3EJH "Crystal Structure Of The Fibronectin 8-9fni Domain Pair In Complex With A Type-I Collagen Peptide" 100.00 93 100.00 100.00 9.90e-62 PDB 3GXE "Complex Of A Low Affinity Collagen Site With The Fibronectin 8-9fni Domain Pair" 100.00 93 100.00 100.00 9.90e-62 PDB 3M7P "Fibronectin Fragment" 95.70 308 97.75 98.88 1.01e-55 stop_ save_ save_collagen_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common collagen_peptide _Molecular_mass 2366.69 _Mol_thiol_state 'not present' loop_ _Biological_function 'cell migration' 'collagen cleavage' development 'matrix protein' 'structural protein' stop_ _Details . _Residue_count 23 _Mol_residue_sequence ; IAGQRGVVGLXGQRGERGFX GLX ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 ALA 3 GLY 4 GLN 5 ARG 6 GLY 7 VAL 8 VAL 9 GLY 10 LEU 11 HYP 12 GLY 13 GLN 14 ARG 15 GLY 16 GLU 17 ARG 18 GLY 19 PHE 20 HYP 21 GLY 22 LEU 23 HYP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 3EJH 'collagen peptide' . . . . . UNP P02452 a1(I) . . . . . stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_HYP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 4-HYDROXYPROLINE _BMRB_code HYP _PDB_code HYP _Standard_residue_derivative . _Molecular_mass 131.130 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OD1 OD1 O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG HG H . 0 . ? HD22 HD22 H . 0 . ? HD23 HD23 H . 0 . ? HD1 HD1 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG OD1 ? ? SING CG HG ? ? SING CD HD22 ? ? SING CD HD23 ? ? SING OD1 HD1 ? ? SING OXT HXT ? ? stop_ save_ ############# # Ligands # ############# save_NAG _Saveframe_category ligand _Mol_type "non-polymer (D-SACCHARIDE)" _Name_common N-ACETYL-D-GLUCOSAMINE _BMRB_code NAG _PDB_code NAG _Molecular_mass 221.208 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? N2 N2 N . 0 . ? O1 O1 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? O7 O7 O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H83 H83 H . 0 . ? HN2 HN2 H . 0 . ? HO1 HO1 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 N2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 N2 ? ? DOUB C7 O7 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C8 H83 ? ? SING N2 HN2 ? ? SING O1 HO1 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_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 $89FnI Human 9606 Eukaryota Metazoa Homo sapiens FN1 $collagen_peptide Human 9606 Eukaryota Metazoa Homo sapiens COL1A1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $89FnI 'recombinant technology' . . . X-33 'not applicable' 'Genomic integration' 'Integrated in the AOX1 locus' $collagen_peptide 'chemical synthesis' . . . . plasmid . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '89FnI in a 1:1 complex with collagen peptide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $89FnI 1.4 mM '[U-100% 13C; U-100% 15N]' $collagen_peptide 1.5 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 5 % [U-2H] H2O 95 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '89FnI in a 1:1 complex with collagen peptide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $89FnI 1.1 mM [U-15N] $collagen_peptide 1.2 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 5 % [U-2H] H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version '2.4 Rev 2006.095.11.35' loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.3.7 loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_Omega_Spectrometer_Operating_Software _Saveframe_category software _Name 'Omega Spectrometer Operating Software' _Version 'Beta 6.03b2' loop_ _Vendor _Address _Electronic_address GE/Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer 'home built' _Model OMEGA _Field_strength 950 _Details 'Oxford supercon magnets, home built consoles controlled by GE omega computers' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer 'home built' _Model OMEGA _Field_strength 600 _Details 'Oxford supercon magnets, home built consoles controlled by GE omega computers' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'Oxford supercon magnets, Bruker console' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.255 . M pH 7.2 . pH pressure 1 . atm 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_ _Software_label $PIPP $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D CBCA(CO)NH' '3D CBCANH' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 89FnI _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 1 516 1 ASP CA C 53.43 0.2 1 2 516 1 ASP CB C 42.45 0.2 1 3 517 2 GLN H H 8.496 0.01 1 4 517 2 GLN CA C 55.36 0.2 1 5 517 2 GLN CB C 32.48 0.2 1 6 517 2 GLN N N 117.59 0.1 1 7 518 3 CYS H H 8.922 0.01 1 8 518 3 CYS CA C 55.77 0.2 1 9 518 3 CYS CB C 43.76 0.2 1 10 518 3 CYS N N 115.35 0.1 1 11 519 4 ILE H H 8.717 0.01 1 12 519 4 ILE CA C 61.01 0.2 1 13 519 4 ILE CB C 38.7 0.2 1 14 519 4 ILE N N 124.07 0.1 1 15 520 5 VAL H H 8.558 0.01 1 16 520 5 VAL CA C 61.06 0.2 1 17 520 5 VAL CB C 33.56 0.2 1 18 520 5 VAL N N 127.64 0.1 1 19 521 6 ASP H H 9.162 0.01 1 20 521 6 ASP CA C 55.98 0.2 1 21 521 6 ASP CB C 39.04 0.2 1 22 521 6 ASP N N 129.79 0.1 1 23 522 7 ASP H H 8.242 0.01 1 24 522 7 ASP CA C 56.28 0.2 1 25 522 7 ASP CB C 39.79 0.2 1 26 522 7 ASP N N 108.32 0.1 1 27 523 8 ILE H H 7.678 0.01 1 28 523 8 ILE CA C 59.96 0.2 1 29 523 8 ILE CB C 38.05 0.2 1 30 523 8 ILE N N 123.76 0.1 1 31 524 9 THR H H 7.792 0.01 1 32 524 9 THR CA C 62 0.2 1 33 524 9 THR CB C 69.3 0.2 1 34 524 9 THR N N 120.72 0.1 1 35 525 10 TYR H H 9.251 0.01 1 36 525 10 TYR CA C 57.35 0.2 1 37 525 10 TYR CB C 41.93 0.2 1 38 525 10 TYR N N 125.69 0.1 1 39 526 11 ASN H H 9.141 0.01 1 40 526 11 ASN CA C 51.99 0.2 1 41 526 11 ASN CB C 40.33 0.2 1 42 526 11 ASN N N 119.44 0.1 1 43 527 12 VAL H H 8.593 0.01 1 44 527 12 VAL CA C 66.05 0.2 1 45 527 12 VAL CB C 31.24 0.2 1 46 527 12 VAL N N 120.59 0.1 1 47 528 13 GLN H H 9.171 0.01 1 48 528 13 GLN CA C 59.11 0.2 1 49 528 13 GLN CB C 26.72 0.2 1 50 528 13 GLN N N 118.66 0.1 1 51 529 14 ASP H H 8.307 0.01 1 52 529 14 ASP CA C 55.99 0.2 1 53 529 14 ASP CB C 41.41 0.2 1 54 529 14 ASP N N 121.34 0.1 1 55 530 15 THR H H 8.133 0.01 1 56 530 15 THR CA C 58.84 0.2 1 57 530 15 THR CB C 71.56 0.2 1 58 530 15 THR N N 109.56 0.1 1 59 531 16 PHE H H 7.699 0.01 1 60 531 16 PHE CA C 55.93 0.2 1 61 531 16 PHE CB C 39.11 0.2 1 62 531 16 PHE N N 115.41 0.1 1 63 532 17 HIS H H 8.798 0.01 1 64 532 17 HIS CA C 55.4 0.2 1 65 532 17 HIS CB C 33.09 0.2 1 66 532 17 HIS N N 119.69 0.1 1 67 533 18 LYS H H 8.255 0.01 1 68 533 18 LYS CA C 55.51 0.2 1 69 533 18 LYS CB C 37.46 0.2 1 70 533 18 LYS N N 120.46 0.1 1 71 534 19 LYS H H 8.756 0.01 1 72 534 19 LYS CA C 55.48 0.2 1 73 534 19 LYS CB C 33.53 0.2 1 74 534 19 LYS N N 125.57 0.1 1 75 535 20 HIS H H 9.095 0.01 1 76 535 20 HIS CA C 58.09 0.2 1 77 535 20 HIS CB C 30.75 0.2 1 78 535 20 HIS N N 128.89 0.1 1 79 536 21 GLU H H 8.559 0.01 1 80 536 21 GLU CA C 60.51 0.2 1 81 536 21 GLU CB C 28.96 0.2 1 82 536 21 GLU N N 131.29 0.1 1 83 537 22 GLU H H 11.614 0.01 1 84 537 22 GLU CA C 58.24 0.2 1 85 537 22 GLU CB C 29.49 0.2 1 86 537 22 GLU N N 120.87 0.1 1 87 538 23 GLY H H 8.161 0.01 1 88 538 23 GLY CA C 45.22 0.2 1 89 538 23 GLY N N 104.83 0.1 1 90 539 24 HIS H H 7.611 0.01 1 91 539 24 HIS CA C 55.01 0.2 1 92 539 24 HIS CB C 29.43 0.2 1 93 539 24 HIS N N 117.88 0.1 1 94 540 25 MET H H 9.277 0.01 1 95 540 25 MET CA C 54.3 0.2 1 96 540 25 MET CB C 31.88 0.2 1 97 540 25 MET N N 119.17 0.1 1 98 541 26 LEU H H 8.883 0.01 1 99 541 26 LEU CA C 53.29 0.2 1 100 541 26 LEU CB C 45.54 0.2 1 101 541 26 LEU N N 122.3 0.1 1 102 542 27 ASN H H 9.659 0.01 1 103 542 27 ASN CA C 52.89 0.2 1 104 542 27 ASN CB C 40.94 0.2 1 105 542 27 ASN N N 118.77 0.1 1 106 543 28 CYS H H 8.45 0.01 1 107 543 28 CYS CA C 55.47 0.2 1 108 543 28 CYS CB C 50.2 0.2 1 109 543 28 CYS N N 120.41 0.1 1 110 544 29 THR H H 8.362 0.01 1 111 544 29 THR CA C 62.29 0.2 1 112 544 29 THR CB C 72.99 0.2 1 113 544 29 THR N N 114.74 0.1 1 114 545 30 CYS H H 8.453 0.01 1 115 545 30 CYS CA C 54.49 0.2 1 116 545 30 CYS CB C 38.03 0.2 1 117 545 30 CYS N N 122.01 0.1 1 118 546 31 PHE H H 9.268 0.01 1 119 546 31 PHE CA C 60.22 0.2 1 120 546 31 PHE CB C 40.55 0.2 1 121 546 31 PHE N N 130.1 0.1 1 122 547 32 GLY H H 9.336 0.01 1 123 547 32 GLY CA C 48.61 0.2 1 124 547 32 GLY N N 107.13 0.1 1 125 548 33 GLN H H 8.995 0.01 1 126 548 33 GLN CA C 57.29 0.2 1 127 548 33 GLN CB C 25.48 0.2 1 128 548 33 GLN N N 123.35 0.1 1 129 549 34 GLY H H 8.81 0.01 1 130 549 34 GLY CA C 45.7 0.2 1 131 549 34 GLY N N 108.14 0.1 1 132 550 35 ARG H H 7.345 0.01 1 133 550 35 ARG CA C 54.27 0.2 1 134 550 35 ARG CB C 33.07 0.2 1 135 550 35 ARG N N 118.03 0.1 1 136 551 36 GLY H H 10.496 0.01 1 137 551 36 GLY CA C 49.33 0.2 1 138 551 36 GLY N N 117.02 0.1 1 139 552 37 ARG H H 9.085 0.01 1 140 552 37 ARG CA C 59.05 0.2 1 141 552 37 ARG CB C 30.97 0.2 1 142 552 37 ARG N N 118.56 0.1 1 143 553 38 TRP CA C 54.47 0.2 1 144 553 38 TRP CB C 33.38 0.2 1 145 554 39 LYS H H 8.432 0.01 1 146 554 39 LYS CA C 55.7 0.2 1 147 554 39 LYS CB C 37.75 0.2 1 148 554 39 LYS N N 118.46 0.1 1 149 555 40 CYS H H 9.272 0.01 1 150 555 40 CYS CA C 55.48 0.2 1 151 555 40 CYS CB C 49.55 0.2 1 152 555 40 CYS N N 119.77 0.1 1 153 556 41 ASP H H 9.363 0.01 1 154 556 41 ASP CA C 55.74 0.2 1 155 556 41 ASP CB C 43.78 0.2 1 156 556 41 ASP N N 124.58 0.1 1 157 557 42 PRO CA C 63.27 0.2 1 158 557 42 PRO CB C 33.98 0.2 1 159 558 43 VAL H H 8.078 0.01 1 160 558 43 VAL CA C 60.08 0.2 1 161 558 43 VAL CB C 34.01 0.2 1 162 558 43 VAL N N 122.21 0.1 1 163 559 44 ASP H H 8.844 0.01 1 164 559 44 ASP CA C 56.07 0.2 1 165 559 44 ASP CB C 40.69 0.2 1 166 559 44 ASP N N 124.76 0.1 1 167 560 45 GLN H H 7.784 0.01 1 168 560 45 GLN CA C 54.1 0.2 1 169 560 45 GLN CB C 29.75 0.2 1 170 560 45 GLN N N 121.12 0.1 1 171 561 46 CYS H H 9.511 0.01 1 172 561 46 CYS CA C 56.66 0.2 1 173 561 46 CYS CB C 45.27 0.2 1 174 561 46 CYS N N 115.88 0.1 1 175 562 47 GLN H H 8.935 0.01 1 176 562 47 GLN CA C 53.59 0.2 1 177 562 47 GLN CB C 31.15 0.2 1 178 562 47 GLN N N 123.18 0.1 1 179 563 48 ASP H H 8.08 0.01 1 180 563 48 ASP CA C 53.69 0.2 1 181 563 48 ASP CB C 42.14 0.2 1 182 563 48 ASP N N 126.67 0.1 1 183 564 49 SER H H 7.769 0.01 1 184 564 49 SER CA C 60.41 0.2 1 185 564 49 SER CB C 63.07 0.2 1 186 564 49 SER N N 121.77 0.1 1 187 565 50 GLU H H 8.723 0.01 1 188 565 50 GLU CA C 58.82 0.2 1 189 565 50 GLU CB C 30.46 0.2 1 190 565 50 GLU N N 121.58 0.1 1 191 566 51 THR H H 7.639 0.01 1 192 566 51 THR CA C 61.29 0.2 1 193 566 51 THR CB C 70.62 0.2 1 194 566 51 THR N N 105.89 0.1 1 195 567 52 GLY H H 8.052 0.01 1 196 567 52 GLY CA C 45.52 0.2 1 197 567 52 GLY N N 111.2 0.1 1 198 568 53 THR H H 7.471 0.01 1 199 568 53 THR CA C 63.42 0.2 1 200 568 53 THR CB C 69.46 0.2 1 201 568 53 THR N N 118.92 0.1 1 202 569 54 PHE H H 8.137 0.01 1 203 569 54 PHE CA C 58.02 0.2 1 204 569 54 PHE CB C 40.76 0.2 1 205 569 54 PHE N N 122.74 0.1 1 206 570 55 TYR H H 9.028 0.01 1 207 570 55 TYR CA C 57.53 0.2 1 208 570 55 TYR CB C 42.59 0.2 1 209 570 55 TYR N N 121.56 0.1 1 210 571 56 GLN H H 9.277 0.01 1 211 571 56 GLN CA C 52.42 0.2 1 212 571 56 GLN CB C 29.22 0.2 1 213 571 56 GLN N N 119.66 0.1 1 214 572 57 ILE H H 8.949 0.01 1 215 572 57 ILE CA C 64.67 0.2 1 216 572 57 ILE CB C 37.75 0.2 1 217 572 57 ILE N N 121.35 0.1 1 218 573 58 GLY H H 8.786 0.01 1 219 573 58 GLY CA C 44.32 0.2 1 220 573 58 GLY N N 116.69 0.1 1 221 574 59 ASP H H 8.411 0.01 1 222 574 59 ASP CA C 54.64 0.2 1 223 574 59 ASP CB C 42.13 0.2 1 224 574 59 ASP N N 121.82 0.1 1 225 575 60 SER H H 8.262 0.01 1 226 575 60 SER CA C 56.11 0.2 1 227 575 60 SER CB C 67.03 0.2 1 228 575 60 SER N N 111.75 0.1 1 229 576 61 TRP H H 8.316 0.01 1 230 576 61 TRP CA C 56.58 0.2 1 231 576 61 TRP CB C 31.75 0.2 1 232 576 61 TRP N N 122.05 0.1 1 233 577 62 GLU H H 8.519 0.01 1 234 577 62 GLU CA C 54.62 0.2 1 235 577 62 GLU CB C 33.14 0.2 1 236 577 62 GLU N N 119.74 0.1 1 237 578 63 LYS H H 8.462 0.01 1 238 578 63 LYS CA C 55.33 0.2 1 239 578 63 LYS CB C 36.49 0.2 1 240 578 63 LYS N N 120.1 0.1 1 241 579 64 TYR H H 8.973 0.01 1 242 579 64 TYR CA C 57.2 0.2 1 243 579 64 TYR CB C 40.24 0.2 1 244 579 64 TYR N N 123.01 0.1 1 245 580 65 VAL H H 8.986 0.01 1 246 580 65 VAL CA C 61.66 0.2 1 247 580 65 VAL CB C 33.59 0.2 1 248 580 65 VAL N N 124.19 0.1 1 249 581 66 HIS H H 9.516 0.01 1 250 581 66 HIS CA C 56.95 0.2 1 251 581 66 HIS CB C 28.76 0.2 1 252 581 66 HIS N N 127.72 0.1 1 253 582 67 GLY H H 8.453 0.01 1 254 582 67 GLY CA C 45.59 0.2 1 255 582 67 GLY N N 103.05 0.1 1 256 583 68 VAL H H 7.899 0.01 1 257 583 68 VAL CA C 61.79 0.2 1 258 583 68 VAL CB C 33.98 0.2 1 259 583 68 VAL N N 123.03 0.1 1 260 584 69 ARG H H 8.51 0.01 1 261 584 69 ARG CA C 56.69 0.2 1 262 584 69 ARG CB C 31.71 0.2 1 263 584 69 ARG N N 127.55 0.1 1 264 585 70 TYR H H 9.454 0.01 1 265 585 70 TYR CA C 56.7 0.2 1 266 585 70 TYR CB C 42.01 0.2 1 267 585 70 TYR N N 125.49 0.1 1 268 586 71 GLN H H 8.948 0.01 1 269 586 71 GLN CA C 54.64 0.2 1 270 586 71 GLN CB C 31.56 0.2 1 271 586 71 GLN N N 119.25 0.1 1 272 587 72 CYS H H 9.213 0.01 1 273 587 72 CYS CA C 54.69 0.2 1 274 587 72 CYS CB C 45.44 0.2 1 275 587 72 CYS N N 127.16 0.1 1 276 588 73 TYR H H 8.24 0.01 1 277 588 73 TYR CA C 56.6 0.2 1 278 588 73 TYR CB C 43 0.2 1 279 588 73 TYR N N 120.42 0.1 1 280 589 74 CYS H H 7.698 0.01 1 281 589 74 CYS CA C 54.03 0.2 1 282 589 74 CYS CB C 38.41 0.2 1 283 589 74 CYS N N 121.02 0.1 1 284 590 75 TYR H H 9.033 0.01 1 285 590 75 TYR CA C 60.34 0.2 1 286 590 75 TYR CB C 40.28 0.2 1 287 590 75 TYR N N 128.71 0.1 1 288 591 76 GLY H H 9.097 0.01 1 289 591 76 GLY CA C 48.08 0.2 1 290 591 76 GLY N N 106.79 0.1 1 291 592 77 ARG H H 8.628 0.01 1 292 592 77 ARG CA C 58.26 0.2 1 293 592 77 ARG CB C 27.11 0.2 1 294 592 77 ARG N N 121.87 0.1 1 295 593 78 GLY H H 9.885 0.01 1 296 593 78 GLY CA C 45.31 0.2 1 297 593 78 GLY N N 109.41 0.1 1 298 594 79 ILE H H 7.615 0.01 1 299 594 79 ILE CA C 60.31 0.2 1 300 594 79 ILE CB C 40.48 0.2 1 301 594 79 ILE N N 113.31 0.1 1 302 595 80 GLY H H 9.683 0.01 1 303 595 80 GLY CA C 49.46 0.2 1 304 595 80 GLY N N 117.95 0.1 1 305 596 81 GLU H H 9.336 0.01 1 306 596 81 GLU CA C 57.86 0.2 1 307 596 81 GLU N N 121.04 0.1 1 308 597 82 TRP CA C 54.45 0.2 1 309 597 82 TRP CB C 34.22 0.2 1 310 598 83 HIS H H 8.444 0.01 1 311 598 83 HIS CA C 55.23 0.2 1 312 598 83 HIS N N 114.65 0.1 1 313 599 84 CYS CA C 55.49 0.2 1 314 599 84 CYS CB C 49.56 0.2 1 315 600 85 GLN H H 9.042 0.01 1 316 600 85 GLN CA C 52.77 0.2 1 317 600 85 GLN CB C 30.99 0.2 1 318 600 85 GLN N N 120.47 0.1 1 319 601 86 PRO CA C 62.72 0.2 1 320 601 86 PRO CB C 31.49 0.2 1 321 602 87 LEU H H 8.399 0.01 1 322 602 87 LEU CA C 54.76 0.2 1 323 602 87 LEU CB C 43.09 0.2 1 324 602 87 LEU N N 124.63 0.1 1 325 603 88 GLN H H 8.416 0.01 1 326 603 88 GLN CA C 55.56 0.2 1 327 603 88 GLN CB C 29.91 0.2 1 328 603 88 GLN N N 122.35 0.1 1 329 604 89 THR H H 8.104 0.01 1 330 604 89 THR CA C 61.73 0.2 1 331 604 89 THR CB C 70.1 0.2 1 332 604 89 THR N N 115.72 0.1 1 333 605 90 TYR H H 8.294 0.01 1 334 605 90 TYR CA C 55.78 0.2 1 335 605 90 TYR CB C 38.47 0.2 1 336 605 90 TYR N N 123.31 0.1 1 337 606 91 PRO CA C 63.22 0.2 1 338 606 91 PRO CB C 32.11 0.2 1 339 607 92 SER H H 8.481 0.01 1 340 607 92 SER CA C 58.44 0.2 1 341 607 92 SER CB C 64.18 0.2 1 342 607 92 SER N N 116.82 0.1 1 343 608 93 SER H H 8.025 0.01 1 344 608 93 SER CA C 60.1 0.2 1 345 608 93 SER CB C 64.75 0.2 1 346 608 93 SER N N 122.96 0.1 1 stop_ save_