data_16191 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR-Assignments of a Cytosolic Domain of the C-Terminus of Polycystin-2 ; _BMRB_accession_number 16191 _BMRB_flat_file_name bmr16191.str _Entry_type original _Submission_date 2009-03-02 _Accession_date 2009-03-02 _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 Kalbitzer 'Hans Robert' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 499 "13C chemical shifts" 348 "15N chemical shifts" 100 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-04-15 update BMRB 'add related PDB ID' 2009-08-20 update BMRB 'added PubMed ID' 2009-07-17 update author 'update chemical shifts' 2009-06-05 update BMRB 'completed entry citation' 2009-04-16 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636966 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schumann Frank H. . 2 Hoffmeister Helen . . 3 Schmidt Maren . . 4 Bader Reto . . 5 Besl Elisabeth . . 6 Witzgall Ralph . . 7 Kalbitzer 'Hans Robert' . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR Assignments' _Journal_volume 3 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 141 _Page_last 144 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Polycystin-2 Polypeptide' $Polycystin-2_Polypeptide Calcium $CA 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_Polycystin-2_Polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Polycystin-2_Polypeptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; GSTAIGINDTYSEVKSDLAQ QKAEMELSDLIRKGYHKALV KLKLKKNTVDDISESLRQGG GKLNFDELRQDLKGKGHTDA EIEAIFTKYDQDGDQELTEH EHQQMRDDLEKEREDLDLDH SSL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 674 GLY 2 675 SER 3 676 THR 4 677 ALA 5 678 ILE 6 679 GLY 7 680 ILE 8 681 ASN 9 682 ASP 10 683 THR 11 684 TYR 12 685 SER 13 686 GLU 14 687 VAL 15 688 LYS 16 689 SER 17 690 ASP 18 691 LEU 19 692 ALA 20 693 GLN 21 694 GLN 22 695 LYS 23 696 ALA 24 697 GLU 25 698 MET 26 699 GLU 27 700 LEU 28 701 SER 29 702 ASP 30 703 LEU 31 704 ILE 32 705 ARG 33 706 LYS 34 707 GLY 35 708 TYR 36 709 HIS 37 710 LYS 38 711 ALA 39 712 LEU 40 713 VAL 41 714 LYS 42 715 LEU 43 716 LYS 44 717 LEU 45 718 LYS 46 719 LYS 47 720 ASN 48 721 THR 49 722 VAL 50 723 ASP 51 724 ASP 52 725 ILE 53 726 SER 54 727 GLU 55 728 SER 56 729 LEU 57 730 ARG 58 731 GLN 59 732 GLY 60 733 GLY 61 734 GLY 62 735 LYS 63 736 LEU 64 737 ASN 65 738 PHE 66 739 ASP 67 740 GLU 68 741 LEU 69 742 ARG 70 743 GLN 71 744 ASP 72 745 LEU 73 746 LYS 74 747 GLY 75 748 LYS 76 749 GLY 77 750 HIS 78 751 THR 79 752 ASP 80 753 ALA 81 754 GLU 82 755 ILE 83 756 GLU 84 757 ALA 85 758 ILE 86 759 PHE 87 760 THR 88 761 LYS 89 762 TYR 90 763 ASP 91 764 GLN 92 765 ASP 93 766 GLY 94 767 ASP 95 768 GLN 96 769 GLU 97 770 LEU 98 771 THR 99 772 GLU 100 773 HIS 101 774 GLU 102 775 HIS 103 776 GLN 104 777 GLN 105 778 MET 106 779 ARG 107 780 ASP 108 781 ASP 109 782 LEU 110 783 GLU 111 784 LYS 112 785 GLU 113 786 ARG 114 787 GLU 115 788 ASP 116 789 LEU 117 790 ASP 118 791 LEU 119 792 ASP 120 793 HIS 121 794 SER 122 795 SER 123 796 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 16590 "EF-hand domain of polycystin-2" 62.60 78 100.00 100.00 3.73e-45 BMRB 17621 POLYCYSTIN-2 61.79 79 100.00 100.00 6.83e-44 BMRB 18268 EF-hand_domain_of_polycystin-2 62.60 78 100.00 100.00 3.73e-45 PDB 2KLD "Solution Structure Of The Calcium Binding Domain Of The C- Terminal Cytosolic Domain Of Polycystin-2" 100.00 123 100.00 100.00 9.39e-80 PDB 2KLE "Isic Refined Solution Structure Of The Calcium Binding Domain Of The C-Terminal Cytosolic Domain Of Polycystin-2" 100.00 123 100.00 100.00 9.39e-80 PDB 2KQ6 "The Structure Of The Ef-Hand Domain Of Polycystin-2 Suggests Mechanism For Ca2+-Dependent Regulation Of Polycystin-2 Cha Activi" 62.60 78 100.00 100.00 3.73e-45 PDB 2Y4Q "Solution Structure Of The Ef-hand Domain Of Human Polycystin 2" 61.79 79 100.00 100.00 6.83e-44 DBJ BAG56956 "unnamed protein product [Homo sapiens]" 95.12 294 100.00 100.00 5.86e-74 DBJ BAG57494 "unnamed protein product [Homo sapiens]" 95.12 386 100.00 100.00 5.52e-73 EMBL CAI38797 "polycystic kidney disease 2 membrane protein [Bos taurus]" 95.12 970 99.15 100.00 2.98e-69 GB AAC16004 "autosomal dominant polycystic kidney disease type II protein [Homo sapiens]" 95.12 968 100.00 100.00 3.47e-70 GB AAC50520 "autosomal dominant polycystic kidney disease type II [Homo sapiens]" 95.12 968 100.00 100.00 3.47e-70 GB AAC50933 "polycystwin, partial [Homo sapiens]" 95.12 608 100.00 100.00 5.39e-72 GB AAI11455 "PKD2 protein, partial [synthetic construct]" 95.12 968 100.00 100.00 3.47e-70 GB AAI12262 "Polycystin 2 [Homo sapiens]" 95.12 968 100.00 100.00 2.53e-70 REF NP_000288 "polycystin-2 [Homo sapiens]" 95.12 968 100.00 100.00 3.47e-70 REF NP_001039777 "polycystin-2 [Bos taurus]" 95.12 970 99.15 100.00 2.98e-69 REF NP_001232908 "polycystin-2 [Sus scrofa]" 95.12 970 98.29 99.15 1.95e-67 REF XP_001099242 "PREDICTED: polycystin-2 [Macaca mulatta]" 95.12 969 100.00 100.00 1.52e-69 REF XP_002717056 "PREDICTED: polycystin-2 [Oryctolagus cuniculus]" 95.12 970 100.00 100.00 2.29e-69 SP Q13563 "RecName: Full=Polycystin-2; AltName: Full=Autosomal dominant polycystic kidney disease type II protein; AltName: Full=Polycysti" 95.12 968 100.00 100.00 3.47e-70 SP Q4GZT3 "RecName: Full=Polycystin-2; AltName: Full=Polycystic kidney disease 2 protein homolog; AltName: Full=Transient receptor potenti" 95.12 970 99.15 100.00 2.98e-69 TPG DAA28806 "TPA: polycystin-2 [Bos taurus]" 95.12 970 99.15 100.00 2.98e-69 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Nov 18 18:34:14 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? 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 $Polycystin-2_Polypeptide Human 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 $Polycystin-2_Polypeptide 'recombinant technology' . Escherichia coli . pET41a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Polycystin-2_Polypeptide 0.5 mM '[U-100% 13C; U-100% 15N]' Ca2 5 mM 'natural abundance' DSS 0.1 mM 'natural abundance' 'potassium phosphate buffer' 10 mM 'natural abundance' NaCl 500 mM 'natural abundance' DTE 2 mM 'natural abundance' H20 90 % 'natural abundance' D20 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Auremol _Saveframe_category software _Name AUREMOL _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . 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 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_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_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCANNH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCANNH' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_15N-TOCSY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-TOCSY-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_1H-1H_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N-NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N-NOESY-HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.51 . M pH 6.8 . pH pressure 1 . atm temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCANNH' '3D HNCO' '2D 15N-TOCSY-HSQC' '3D HCCH-TOCSY' '2D 1H-1H NOESY' '3D 1H-15N-NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Polycystin-2 Polypeptide' _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 1 676 3 THR H H 8.34 0.01 1 2 676 3 THR HA H 4.24 0.01 1 3 676 3 THR HB H 4.14 0.01 1 4 676 3 THR C C 174.1 0.1 1 5 676 3 THR CA C 61.75 0.1 1 6 676 3 THR CB C 69.73 0.1 1 7 676 3 THR N N 116.48 0.1 1 8 677 4 ALA H H 8.39 0.01 1 9 677 4 ALA HA H 4.33 0.01 1 10 677 4 ALA HB H 1.36 0.01 1 11 677 4 ALA C C 177.4 0.1 1 12 677 4 ALA CA C 52.24 0.1 1 13 677 4 ALA CB C 19.11 0.1 1 14 677 4 ALA N N 127.04 0.1 1 15 678 5 ILE H H 8.16 0.01 1 16 678 5 ILE HA H 4.12 0.01 1 17 678 5 ILE HB H 1.85 0.01 1 18 678 5 ILE HD1 H 0.85 0.01 1 19 678 5 ILE HG12 H 1.11 0.01 2 20 678 5 ILE HG13 H 0.9 0.01 2 21 678 5 ILE C C 176.8 0.1 1 22 678 5 ILE CA C 61.09 0.1 1 23 678 5 ILE CB C 38.6 0.1 1 24 678 5 ILE CD1 C 13.09 0.1 1 25 678 5 ILE CG1 C 27.46 0.1 1 26 678 5 ILE CG2 C 17.61 0.1 1 27 678 5 ILE N N 120.55 0.1 1 28 679 6 GLY H H 8.55 0.01 1 29 679 6 GLY HA2 H 3.92 0.01 2 30 679 6 GLY HA3 H 3.99 0.01 2 31 679 6 GLY C C 174.2 0.1 1 32 679 6 GLY CA C 45.24 0.1 1 33 679 6 GLY N N 113.33 0.1 1 34 680 7 ILE H H 7.99 0.01 1 35 680 7 ILE HA H 4.14 0.01 1 36 680 7 ILE HB H 1.85 0.01 1 37 680 7 ILE HD1 H 0.86 0.01 1 38 680 7 ILE HG12 H 1.19 0.01 1 39 680 7 ILE HG13 H 1.19 0.01 1 40 680 7 ILE HG2 H 0.86 0.01 1 41 680 7 ILE C C 176.1 0.1 1 42 680 7 ILE CA C 61.18 0.1 1 43 680 7 ILE CB C 38.56 0.1 1 44 680 7 ILE CG1 C 27.41 0.1 1 45 680 7 ILE N N 119.93 0.1 1 46 681 8 ASN H H 8.55 0.01 1 47 681 8 ASN HA H 4.75 0.01 1 48 681 8 ASN HB2 H 2.76 0.01 1 49 681 8 ASN HB3 H 2.76 0.01 1 50 681 8 ASN HD21 H 7.54 0.01 2 51 681 8 ASN HD22 H 6.86 0.01 2 52 681 8 ASN C C 174.8 0.1 1 53 681 8 ASN CA C 53.21 0.1 1 54 681 8 ASN CB C 38.35 0.1 1 55 681 8 ASN N N 121.94 0.1 1 56 681 8 ASN ND2 N 112.31 0.1 1 57 682 9 ASP H H 8.27 0.01 1 58 682 9 ASP HA H 4.61 0.01 1 59 682 9 ASP HB2 H 2.62 0.01 1 60 682 9 ASP HB3 H 2.62 0.01 1 61 682 9 ASP C C 176.4 0.1 1 62 682 9 ASP CA C 54.23 0.1 1 63 682 9 ASP CB C 41.08 0.1 1 64 682 9 ASP N N 121.16 0.1 1 65 683 10 THR H H 8.08 0.01 1 66 683 10 THR HA H 4.37 0.01 1 67 683 10 THR HB H 4.23 0.01 1 68 683 10 THR HG2 H 1.08 0.01 1 69 683 10 THR C C 174.4 0.1 1 70 683 10 THR CA C 62.04 0.1 1 71 683 10 THR CB C 69.73 0.1 1 72 683 10 THR N N 114.02 0.1 1 73 684 11 TYR H H 8.23 0.01 1 74 684 11 TYR HA H 4.56 0.01 1 75 684 11 TYR HB2 H 2.98 0.01 2 76 684 11 TYR HB3 H 3.06 0.01 2 77 684 11 TYR HD1 H 7.18 0.01 3 78 684 11 TYR HD2 H 7.18 0.01 3 79 684 11 TYR HE1 H 6.77 0.01 3 80 684 11 TYR HE2 H 6.77 0.01 3 81 684 11 TYR C C 175.7 0.1 1 82 684 11 TYR CA C 58.17 0.1 1 83 684 11 TYR CB C 38.56 0.1 1 84 684 11 TYR CD1 C 133.22 0.1 3 85 684 11 TYR CD2 C 133.22 0.1 3 86 684 11 TYR CE1 C 118.18 0.1 3 87 684 11 TYR CE2 C 118.18 0.1 3 88 684 11 TYR N N 122.63 0.1 1 89 685 12 SER H H 8.07 0.01 1 90 685 12 SER HA H 4.37 0.01 1 91 685 12 SER HB2 H 3.9 0.01 2 92 685 12 SER HB3 H 3.77 0.01 2 93 685 12 SER C C 174 0.1 1 94 685 12 SER CA C 58.13 0.1 1 95 685 12 SER CB C 63.87 0.1 1 96 685 12 SER N N 117.81 0.1 1 97 686 13 GLU H H 8.38 0.01 1 98 686 13 GLU HA H 4.24 0.01 1 99 686 13 GLU HB2 H 1.95 0.01 1 100 686 13 GLU HB3 H 1.95 0.01 1 101 686 13 GLU HG2 H 2.21 0.01 1 102 686 13 GLU HG3 H 2.21 0.01 1 103 686 13 GLU C C 176.4 0.1 1 104 686 13 GLU CA C 56.41 0.1 1 105 686 13 GLU CB C 30.12 0.1 1 106 686 13 GLU N N 123.31 0.1 1 107 687 14 VAL H H 8.17 0.01 1 108 687 14 VAL HA H 4.05 0.01 1 109 687 14 VAL HB H 2.03 0.01 1 110 687 14 VAL HG1 H 0.91 0.01 1 111 687 14 VAL HG2 H 0.91 0.01 1 112 687 14 VAL C C 176.3 0.1 1 113 687 14 VAL CA C 62.48 0.1 1 114 687 14 VAL CB C 32.57 0.1 1 115 687 14 VAL CG1 C 21.1 0.1 1 116 687 14 VAL CG2 C 21.1 0.1 1 117 687 14 VAL N N 121.88 0.1 1 118 688 15 LYS H H 8.44 0.01 1 119 688 15 LYS HA H 4.32 0.01 1 120 688 15 LYS HB2 H 1.77 0.01 1 121 688 15 LYS HB3 H 1.77 0.01 1 122 688 15 LYS HD2 H 1.58 0.01 1 123 688 15 LYS HD3 H 1.58 0.01 1 124 688 15 LYS HE2 H 2.95 0.01 1 125 688 15 LYS HE3 H 2.95 0.01 1 126 688 15 LYS HG2 H 1.41 0.01 1 127 688 15 LYS HG3 H 1.41 0.01 1 128 688 15 LYS C C 176.8 0.1 1 129 688 15 LYS CA C 56.3 0.1 1 130 688 15 LYS CB C 32.9 0.1 1 131 688 15 LYS N N 125.67 0.1 1 132 689 16 SER H H 8.37 0.01 1 133 689 16 SER HA H 4.41 0.01 1 134 689 16 SER HB2 H 3.83 0.01 1 135 689 16 SER HB3 H 3.83 0.01 1 136 689 16 SER C C 174.5 0.1 1 137 689 16 SER CA C 58.48 0.1 1 138 689 16 SER CB C 63.75 0.1 1 139 689 16 SER N N 117.33 0.1 1 140 690 17 ASP H H 8.47 0.01 1 141 690 17 ASP HA H 4.57 0.01 1 142 690 17 ASP HB2 H 2.67 0.01 1 143 690 17 ASP HB3 H 2.67 0.01 1 144 690 17 ASP C C 176.8 0.1 1 145 690 17 ASP CA C 54.59 0.1 1 146 690 17 ASP CB C 40.77 0.1 1 147 690 17 ASP N N 122.87 0.1 1 148 691 18 LEU H H 8.16 0.01 1 149 691 18 LEU HA H 4.12 0.01 1 150 691 18 LEU HB2 H 1.63 0.01 1 151 691 18 LEU HB3 H 1.63 0.01 1 152 691 18 LEU C C 178.1 0.1 1 153 691 18 LEU CA C 56.15 0.1 1 154 691 18 LEU CB C 42.15 0.1 1 155 691 18 LEU CD1 C 24.17 0.1 1 156 691 18 LEU CD2 C 24.17 0.1 1 157 691 18 LEU CG C 27.07 0.1 1 158 691 18 LEU N N 122.15 0.1 1 159 692 19 ALA H H 8.19 0.01 1 160 692 19 ALA HA H 4.2 0.01 1 161 692 19 ALA HB H 1.32 0.01 1 162 692 19 ALA C C 178.7 0.1 1 163 692 19 ALA CA C 53.67 0.1 1 164 692 19 ALA CB C 18.52 0.1 1 165 692 19 ALA N N 123.18 0.1 1 166 693 20 GLN H H 8.19 0.01 1 167 693 20 GLN HA H 4.19 0.01 1 168 693 20 GLN HB2 H 2.06 0.01 1 169 693 20 GLN HB3 H 2.06 0.01 1 170 693 20 GLN HG2 H 2.42 0.01 1 171 693 20 GLN HG3 H 2.42 0.01 1 172 693 20 GLN C C 176.8 0.1 1 173 693 20 GLN CA C 56.76 0.1 1 174 693 20 GLN CB C 28.77 0.1 1 175 693 20 GLN CG C 34.19 0.1 1 176 693 20 GLN N N 119.11 0.1 1 177 694 21 GLN H H 8.26 0.01 1 178 694 21 GLN HA H 4.19 0.01 1 179 694 21 GLN HB2 H 2.04 0.01 1 180 694 21 GLN HB3 H 2.04 0.01 1 181 694 21 GLN HG2 H 2.38 0.01 1 182 694 21 GLN HG3 H 2.38 0.01 1 183 694 21 GLN C C 177.1 0.1 1 184 694 21 GLN CA C 56.92 0.1 1 185 694 21 GLN CB C 28.98 0.1 1 186 694 21 GLN N N 120.72 0.1 1 187 695 22 LYS H H 8.29 0.01 1 188 695 22 LYS HA H 4.14 0.01 1 189 695 22 LYS HB2 H 1.81 0.01 1 190 695 22 LYS HB3 H 1.81 0.01 1 191 695 22 LYS HE2 H 2.77 0.01 1 192 695 22 LYS HE3 H 2.77 0.01 1 193 695 22 LYS HG2 H 1.46 0.01 1 194 695 22 LYS HG3 H 1.46 0.01 1 195 695 22 LYS C C 177.1 0.1 1 196 695 22 LYS CA C 57.41 0.1 1 197 695 22 LYS CB C 32.46 0.1 1 198 695 22 LYS N N 121.84 0.1 1 199 696 23 ALA H H 8.11 0.01 1 200 696 23 ALA HA H 4.25 0.01 1 201 696 23 ALA HB H 1.43 0.01 1 202 696 23 ALA C C 178.9 0.1 1 203 696 23 ALA CA C 53.44 0.1 1 204 696 23 ALA CB C 18.52 0.1 1 205 696 23 ALA N N 123.86 0.1 1 206 697 24 GLU H H 8.29 0.01 1 207 697 24 GLU HA H 4.18 0.01 1 208 697 24 GLU HB2 H 2.05 0.01 1 209 697 24 GLU HB3 H 2.05 0.01 1 210 697 24 GLU HG2 H 2.25 0.01 1 211 697 24 GLU HG3 H 2.25 0.01 1 212 697 24 GLU C C 177.5 0.1 1 213 697 24 GLU CA C 57.37 0.1 1 214 697 24 GLU CB C 29.87 0.1 1 215 697 24 GLU CG C 36.47 0.1 1 216 697 24 GLU N N 119.15 0.1 1 217 698 25 MET H H 8.2 0.01 1 218 698 25 MET HA H 4.36 0.01 1 219 698 25 MET HB2 H 1.8 0.01 2 220 698 25 MET HB3 H 1.57 0.01 2 221 698 25 MET HG2 H 2.03 0.01 1 222 698 25 MET HG3 H 2.03 0.01 1 223 698 25 MET C C 176.9 0.1 1 224 698 25 MET CA C 56.58 0.1 1 225 698 25 MET CB C 32.86 0.1 1 226 698 25 MET N N 120.41 0.1 1 227 699 26 GLU H H 8.36 0.01 1 228 699 26 GLU HA H 4.33 0.01 1 229 699 26 GLU HB2 H 2.02 0.01 1 230 699 26 GLU HB3 H 2.02 0.01 1 231 699 26 GLU HG2 H 2.31 0.01 1 232 699 26 GLU HG3 H 2.31 0.01 1 233 699 26 GLU C C 177.5 0.1 1 234 699 26 GLU CA C 57.21 0.1 1 235 699 26 GLU CB C 29.83 0.1 1 236 699 26 GLU CG C 35.87 0.1 1 237 699 26 GLU N N 121.26 0.1 1 238 700 27 LEU H H 8.18 0.01 1 239 700 27 LEU HA H 4.22 0.01 1 240 700 27 LEU HB2 H 1.99 0.01 1 241 700 27 LEU HB3 H 1.99 0.01 1 242 700 27 LEU HD1 H 0.89 0.01 1 243 700 27 LEU HG H 1.61 0.01 1 244 700 27 LEU C C 178 0.1 1 245 700 27 LEU CA C 55.42 0.1 1 246 700 27 LEU N N 122.1 0.1 1 247 701 28 SER H H 8.22 0.01 1 248 701 28 SER HA H 4.25 0.01 1 249 701 28 SER HB2 H 3.89 0.01 1 250 701 28 SER HB3 H 3.89 0.01 1 251 701 28 SER C C 175.6 0.1 1 252 701 28 SER CA C 59.77 0.1 1 253 701 28 SER CB C 63.47 0.1 1 254 701 28 SER N N 115.01 0.1 1 255 702 29 ASP H H 8.23 0.01 1 256 702 29 ASP HA H 4.52 0.01 1 257 702 29 ASP HB2 H 2.69 0.01 1 258 702 29 ASP HB3 H 2.69 0.01 1 259 702 29 ASP C C 177.1 0.1 1 260 702 29 ASP CA C 55.9 0.1 1 261 702 29 ASP CB C 40.9 0.1 1 262 702 29 ASP N N 122.15 0.1 1 263 703 30 LEU H H 7.95 0.01 1 264 703 30 LEU HA H 4.1 0.01 1 265 703 30 LEU HB2 H 1.69 0.01 1 266 703 30 LEU HB3 H 1.69 0.01 1 267 703 30 LEU C C 178.9 0.1 1 268 703 30 LEU CA C 56.74 0.1 1 269 703 30 LEU CB C 42.15 0.1 1 270 703 30 LEU N N 120.61 0.1 1 271 704 31 ILE H H 7.99 0.01 1 272 704 31 ILE HA H 4.09 0.01 1 273 704 31 ILE HB H 1.91 0.01 1 274 704 31 ILE HD1 H 0.7 0.01 1 275 704 31 ILE HG12 H 1.55 0.01 2 276 704 31 ILE HG13 H 1.18 0.01 2 277 704 31 ILE HG2 H 0.75 0.01 1 278 704 31 ILE C C 177.8 0.1 1 279 704 31 ILE CA C 62.7 0.1 1 280 704 31 ILE CB C 37.8 0.1 1 281 704 31 ILE CD1 C 12.79 0.1 1 282 704 31 ILE CG1 C 28.3 0.1 1 283 704 31 ILE CG2 C 17.56 0.1 1 284 704 31 ILE N N 121.91 0.1 1 285 705 32 ARG H H 8.23 0.01 1 286 705 32 ARG HA H 4.21 0.01 1 287 705 32 ARG HB2 H 1.86 0.01 1 288 705 32 ARG HB3 H 1.86 0.01 1 289 705 32 ARG HD2 H 2.97 0.01 1 290 705 32 ARG HD3 H 2.97 0.01 1 291 705 32 ARG HE H 7.09 0.01 1 292 705 32 ARG HG2 H 1.48 0.01 2 293 705 32 ARG HG3 H 1.4 0.01 2 294 705 32 ARG CA C 57.69 0.1 1 295 705 32 ARG CB C 30.36 0.1 1 296 705 32 ARG CD C 43.46 0.1 1 297 705 32 ARG CG C 27.2 0.1 1 298 705 32 ARG N N 122.28 0.1 1 299 707 34 GLY N N 108.62 0.1 1 300 725 52 ILE H H 7.99 0.01 1 301 725 52 ILE HA H 3.45 0.01 1 302 725 52 ILE HB H 1.7 0.01 1 303 725 52 ILE HD1 H 0.74 0.01 1 304 725 52 ILE HG2 H 0.38 0.01 1 305 725 52 ILE CB C 37.81 0.1 1 306 725 52 ILE CD1 C 14.32 0.1 1 307 725 52 ILE CG1 C 31.15 0.1 1 308 725 52 ILE CG2 C 17.27 0.1 1 309 725 52 ILE N N 121.91 0.1 1 310 726 53 SER H H 8 0.01 1 311 726 53 SER HA H 4.33 0.01 1 312 726 53 SER HB2 H 3.75 0.01 1 313 726 53 SER HB3 H 3.75 0.01 1 314 726 53 SER N N 117.27 0.1 1 315 728 55 SER H H 8.02 0.01 1 316 728 55 SER HA H 4.38 0.01 1 317 728 55 SER C C 177.7 0.1 1 318 729 56 LEU H H 8.36 0.01 1 319 729 56 LEU HA H 4.24 0.01 1 320 729 56 LEU HB2 H 1.44 0.01 1 321 729 56 LEU HB3 H 1.44 0.01 1 322 729 56 LEU HD1 H 0.55 0.01 2 323 729 56 LEU HD2 H 0.46 0.01 2 324 729 56 LEU HG H 1.07 0.01 1 325 729 56 LEU C C 179.3 0.1 1 326 729 56 LEU CA C 58.01 0.1 1 327 729 56 LEU CB C 42.11 0.1 1 328 729 56 LEU CD1 C 23.21 0.1 1 329 729 56 LEU CD2 C 23.21 0.1 1 330 729 56 LEU CG C 26.32 0.1 1 331 729 56 LEU N N 121.43 0.1 1 332 730 57 ARG H H 8.02 0.01 1 333 730 57 ARG HA H 4 0.01 1 334 730 57 ARG HB2 H 1.87 0.01 1 335 730 57 ARG HB3 H 1.87 0.01 1 336 730 57 ARG HD2 H 3.26 0.01 2 337 730 57 ARG HD3 H 3.21 0.01 2 338 730 57 ARG HE H 7.2 0.01 1 339 730 57 ARG HG2 H 1.71 0.01 1 340 730 57 ARG HG3 H 1.71 0.01 1 341 730 57 ARG CA C 59.43 0.1 1 342 730 57 ARG CB C 29.9 0.1 1 343 730 57 ARG N N 120.61 0.1 1 344 731 58 GLN H H 8.08 0.01 1 345 731 58 GLN HA H 4.13 0.01 1 346 731 58 GLN HB2 H 2.14 0.01 2 347 731 58 GLN HB3 H 1.96 0.01 2 348 731 58 GLN HE21 H 7.65 0.01 2 349 731 58 GLN HE22 H 6.86 0.01 2 350 731 58 GLN HG2 H 2.46 0.01 1 351 731 58 GLN HG3 H 2.46 0.01 1 352 731 58 GLN C C 177.3 0.1 1 353 731 58 GLN CA C 58.4 0.1 1 354 731 58 GLN CB C 28.53 0.1 1 355 731 58 GLN CG C 34.09 0.1 1 356 731 58 GLN N N 118.84 0.1 1 357 731 58 GLN NE2 N 112.27 0.1 1 358 732 59 GLY H H 7.78 0.01 1 359 732 59 GLY HA2 H 4.42 0.01 2 360 732 59 GLY HA3 H 3.69 0.01 2 361 732 59 GLY C C 174 0.1 1 362 732 59 GLY CA C 44.88 0.1 1 363 732 59 GLY N N 105.81 0.1 1 364 733 60 GLY H H 7.62 0.01 1 365 733 60 GLY HA2 H 3.89 0.01 2 366 733 60 GLY HA3 H 3.69 0.01 2 367 733 60 GLY C C 175.6 0.1 1 368 733 60 GLY CA C 45.71 0.1 1 369 733 60 GLY N N 106.53 0.1 1 370 734 61 GLY H H 8.74 0.01 1 371 734 61 GLY HA2 H 4.36 0.01 2 372 734 61 GLY HA3 H 3.44 0.01 2 373 734 61 GLY C C 172.7 0.1 1 374 734 61 GLY CA C 44.86 0.1 1 375 734 61 GLY N N 107.08 0.1 1 376 735 62 LYS H H 7.26 0.01 1 377 735 62 LYS HA H 5.19 0.01 1 378 735 62 LYS HB2 H 1.82 0.01 2 379 735 62 LYS HB3 H 1.68 0.01 2 380 735 62 LYS HD2 H 1.56 0.01 1 381 735 62 LYS HD3 H 1.56 0.01 1 382 735 62 LYS HE2 H 2.93 0.01 1 383 735 62 LYS HE3 H 2.93 0.01 1 384 735 62 LYS HG2 H 1.23 0.01 1 385 735 62 LYS HG3 H 1.23 0.01 1 386 735 62 LYS C C 173.8 0.1 1 387 735 62 LYS CA C 55.08 0.1 1 388 735 62 LYS CB C 35.05 0.1 1 389 735 62 LYS CD C 29.73 0.1 1 390 735 62 LYS CE C 42.2 0.1 1 391 735 62 LYS CG C 23.21 0.1 1 392 735 62 LYS N N 117.4 0.1 1 393 736 63 LEU H H 8.28 0.01 1 394 736 63 LEU HA H 4.86 0.01 1 395 736 63 LEU HB2 H 1.64 0.01 2 396 736 63 LEU HB3 H 1.43 0.01 2 397 736 63 LEU HD1 H 0.93 0.01 1 398 736 63 LEU HD2 H 0.93 0.01 1 399 736 63 LEU HG H 0.76 0.01 1 400 736 63 LEU C C 175.7 0.1 1 401 736 63 LEU CA C 54.1 0.1 1 402 736 63 LEU CB C 48.4 0.1 1 403 736 63 LEU CD1 C 24.82 0.1 1 404 736 63 LEU CD2 C 24.82 0.1 1 405 736 63 LEU CG C 27.16 0.1 1 406 736 63 LEU N N 119.9 0.1 1 407 737 64 ASN H H 9.04 0.01 1 408 737 64 ASN HA H 5.15 0.01 1 409 737 64 ASN HB2 H 3.28 0.01 2 410 737 64 ASN HB3 H 2.92 0.01 2 411 737 64 ASN C C 175 0.1 1 412 737 64 ASN CA C 52.03 0.1 1 413 737 64 ASN CB C 38.89 0.1 1 414 737 64 ASN N N 120.68 0.1 1 415 737 64 ASN ND2 N 112.28 0.1 1 416 738 65 PHE H H 8.38 0.01 1 417 738 65 PHE HA H 3.66 0.01 1 418 738 65 PHE HB2 H 2.77 0.01 2 419 738 65 PHE HB3 H 2.53 0.01 2 420 738 65 PHE HD1 H 6.49 0.01 3 421 738 65 PHE HD2 H 6.49 0.01 3 422 738 65 PHE HE1 H 7 0.01 3 423 738 65 PHE HE2 H 7 0.01 3 424 738 65 PHE HZ H 7.21 0.01 1 425 738 65 PHE CA C 60.3 0.1 1 426 738 65 PHE CB C 38.45 0.1 1 427 738 65 PHE CD1 C 131.07 0.1 3 428 738 65 PHE CD2 C 131.07 0.1 3 429 738 65 PHE CE1 C 130.4 0.1 3 430 738 65 PHE CE2 C 130.4 0.1 3 431 738 65 PHE CZ C 133.53 0.1 1 432 738 65 PHE N N 118.94 0.1 1 433 739 66 ASP H H 7.37 0.01 1 434 739 66 ASP C C 177.3 0.1 1 435 739 66 ASP CA C 59.66 0.1 1 436 739 66 ASP CB C 40.9 0.1 1 437 739 66 ASP N N 117.76 0.1 1 438 740 67 GLU H H 6.9 0.01 1 439 740 67 GLU HA H 4.15 0.01 1 440 740 67 GLU HB2 H 2.08 0.01 2 441 740 67 GLU HB3 H 1.97 0.01 2 442 740 67 GLU C C 179.3 0.1 1 443 740 67 GLU CA C 59.02 0.1 1 444 740 67 GLU CB C 28.23 0.1 1 445 740 67 GLU N N 119.15 0.1 1 446 741 68 LEU H H 8.38 0.01 1 447 741 68 LEU HA H 4.05 0.01 1 448 741 68 LEU HB2 H 1.92 0.01 2 449 741 68 LEU HB3 H 1.54 0.01 2 450 741 68 LEU HD1 H 0.59 0.01 2 451 741 68 LEU HD2 H 0.55 0.01 2 452 741 68 LEU HG H 1.89 0.01 1 453 741 68 LEU C C 178 0.1 1 454 741 68 LEU CA C 57.63 0.1 1 455 741 68 LEU CB C 41.7 0.1 1 456 741 68 LEU CD1 C 25.99 0.1 2 457 741 68 LEU CD2 C 22.19 0.1 2 458 741 68 LEU CG C 27.09 0.1 1 459 741 68 LEU N N 120.99 0.1 1 460 742 69 ARG H H 9.03 0.01 1 461 742 69 ARG HA H 3.72 0.01 1 462 742 69 ARG HB2 H 1.97 0.01 1 463 742 69 ARG HB3 H 1.97 0.01 1 464 742 69 ARG HD2 H 3.1 0.01 1 465 742 69 ARG HD3 H 3.1 0.01 1 466 742 69 ARG HE H 6.96 0.01 1 467 742 69 ARG HG2 H 1.73 0.01 2 468 742 69 ARG HG3 H 1.55 0.01 2 469 742 69 ARG C C 177.7 0.1 1 470 742 69 ARG CA C 60 0.1 1 471 742 69 ARG CB C 29.84 0.1 1 472 742 69 ARG CD C 43.81 0.1 1 473 742 69 ARG CG C 27.51 0.1 1 474 742 69 ARG N N 119.21 0.1 1 475 743 70 GLN H H 7.71 0.01 1 476 743 70 GLN HA H 3.92 0.01 1 477 743 70 GLN HB2 H 2.14 0.01 1 478 743 70 GLN HB3 H 2.14 0.01 1 479 743 70 GLN HE21 H 7.83 0.01 2 480 743 70 GLN HE22 H 7.1 0.01 2 481 743 70 GLN HG2 H 2.54 0.01 1 482 743 70 GLN HG3 H 2.54 0.01 1 483 743 70 GLN C C 179 0.1 1 484 743 70 GLN CA C 58.91 0.1 1 485 743 70 GLN CB C 28.21 0.1 1 486 743 70 GLN CG C 34.12 0.1 1 487 743 70 GLN N N 116.65 0.1 1 488 743 70 GLN NE2 N 116.58 0.1 1 489 744 71 ASP H H 7.78 0.01 1 490 744 71 ASP HA H 4.43 0.01 1 491 744 71 ASP HB2 H 2.71 0.01 1 492 744 71 ASP HB3 H 2.71 0.01 1 493 744 71 ASP C C 179.3 0.1 1 494 744 71 ASP CA C 56.95 0.1 1 495 744 71 ASP CB C 41.19 0.1 1 496 744 71 ASP N N 120.03 0.1 1 497 745 72 LEU H H 8.61 0.01 1 498 745 72 LEU HA H 4.09 0.01 1 499 745 72 LEU HB2 H 1.77 0.01 1 500 745 72 LEU HB3 H 1.77 0.01 1 501 745 72 LEU HD1 H 0.91 0.01 2 502 745 72 LEU HD2 H 0.62 0.01 2 503 745 72 LEU C C 178.7 0.1 1 504 745 72 LEU CA C 57.06 0.1 1 505 745 72 LEU CB C 42.29 0.1 1 506 745 72 LEU CD1 C 25.53 0.1 2 507 745 72 LEU CD2 C 23.89 0.1 2 508 745 72 LEU CG C 27.01 0.1 1 509 745 72 LEU N N 116.34 0.1 1 510 746 73 LYS H H 8.86 0.01 1 511 746 73 LYS HA H 4.45 0.01 1 512 746 73 LYS HB2 H 1.8 0.01 1 513 746 73 LYS HB3 H 1.8 0.01 1 514 746 73 LYS HD2 H 1.61 0.01 1 515 746 73 LYS HD3 H 1.61 0.01 1 516 746 73 LYS HE2 H 2.74 0.01 1 517 746 73 LYS HE3 H 2.74 0.01 1 518 746 73 LYS HG2 H 1.45 0.01 1 519 746 73 LYS HG3 H 1.45 0.01 1 520 746 73 LYS CA C 57.39 0.1 1 521 746 73 LYS CB C 33.05 0.1 1 522 746 73 LYS CD C 29.5 0.1 1 523 746 73 LYS CE C 42.2 0.1 1 524 746 73 LYS CG C 25.7 0.1 1 525 746 73 LYS N N 121.65 0.1 1 526 747 74 GLY H H 7.94 0.01 1 527 747 74 GLY HA2 H 4.05 0.01 1 528 747 74 GLY HA3 H 4.05 0.01 1 529 747 74 GLY C C 175.5 0.1 1 530 747 74 GLY CA C 46.49 0.1 1 531 747 74 GLY N N 108.21 0.1 1 532 748 75 LYS H H 7.29 0.01 1 533 748 75 LYS HA H 4.43 0.01 1 534 748 75 LYS HB2 H 1.71 0.01 1 535 748 75 LYS HB3 H 1.71 0.01 1 536 748 75 LYS HD2 H 1.45 0.01 2 537 748 75 LYS HD3 H 1.38 0.01 2 538 748 75 LYS HE2 H 2.7 0.01 1 539 748 75 LYS HE3 H 2.7 0.01 1 540 748 75 LYS HG2 H 1.57 0.01 1 541 748 75 LYS HG3 H 1.57 0.01 1 542 748 75 LYS C C 175.2 0.1 1 543 748 75 LYS CA C 55.84 0.1 1 544 748 75 LYS CB C 33.89 0.1 1 545 748 75 LYS CD C 29.43 0.1 1 546 748 75 LYS CE C 42.42 0.1 1 547 748 75 LYS CG C 25.99 0.1 1 548 748 75 LYS N N 118.22 0.1 1 549 749 76 GLY H H 7.82 0.01 1 550 749 76 GLY HA2 H 4.22 0.01 2 551 749 76 GLY HA3 H 4.06 0.01 2 552 749 76 GLY C C 174.5 0.1 1 553 749 76 GLY CA C 45.94 0.1 1 554 749 76 GLY N N 106.56 0.1 1 555 750 77 HIS H H 7.76 0.01 1 556 750 77 HIS HA H 4.34 0.01 1 557 750 77 HIS HB2 H 3.06 0.01 1 558 750 77 HIS HB3 H 3.06 0.01 1 559 750 77 HIS HD2 H 7.3 0.01 1 560 750 77 HIS HE1 H 8.23 0.01 1 561 750 77 HIS C C 174.8 0.1 1 562 750 77 HIS CA C 55.04 0.1 1 563 750 77 HIS CB C 29.03 0.1 1 564 750 77 HIS CD2 C 122.98 0.1 1 565 750 77 HIS CE1 C 137.36 0.1 1 566 750 77 HIS N N 118.26 0.1 1 567 751 78 THR H H 9.02 0.01 1 568 751 78 THR HA H 4.44 0.01 1 569 751 78 THR HB H 4.73 0.01 1 570 751 78 THR HG2 H 1.21 0.01 1 571 751 78 THR C C 175 0.1 1 572 751 78 THR CA C 60.59 0.1 1 573 751 78 THR CB C 71.01 0.1 1 574 751 78 THR CG2 C 21.57 0.1 1 575 751 78 THR N N 113.85 0.1 1 576 752 79 ASP H H 8.84 0.01 1 577 752 79 ASP HA H 4.67 0.01 1 578 752 79 ASP HB2 H 2.7 0.01 2 579 752 79 ASP HB3 H 2.64 0.01 2 580 752 79 ASP C C 178.2 0.1 1 581 752 79 ASP CA C 58.13 0.1 1 582 752 79 ASP CB C 40.53 0.1 1 583 752 79 ASP N N 120.75 0.1 1 584 753 80 ALA H H 8.45 0.01 1 585 753 80 ALA HA H 4.13 0.01 1 586 753 80 ALA HB H 1.42 0.01 1 587 753 80 ALA C C 180.9 0.1 1 588 753 80 ALA CA C 55.08 0.1 1 589 753 80 ALA CB C 18.04 0.1 1 590 753 80 ALA N N 120.1 0.1 1 591 754 81 GLU H H 8.38 0.01 1 592 754 81 GLU HA H 4 0.01 1 593 754 81 GLU HB2 H 2.17 0.01 2 594 754 81 GLU HB3 H 2.32 0.01 2 595 754 81 GLU CA C 59.11 0.1 1 596 754 81 GLU CB C 29.79 0.1 1 597 754 81 GLU CG C 35.66 0.1 1 598 754 81 GLU N N 120.03 0.1 1 599 755 82 ILE H H 8.02 0.01 1 600 755 82 ILE HA H 3.24 0.01 1 601 755 82 ILE HB H 1.8 0.01 1 602 755 82 ILE HD1 H 0.72 0.01 1 603 755 82 ILE HG12 H 0.67 0.01 1 604 755 82 ILE HG13 H 0.67 0.01 1 605 755 82 ILE HG2 H 0.46 0.01 1 606 755 82 ILE C C 177.2 0.1 1 607 755 82 ILE CA C 65.51 0.1 1 608 755 82 ILE CB C 38.41 0.1 1 609 755 82 ILE CD1 C 15.16 0.1 1 610 755 82 ILE CG1 C 28.51 0.1 1 611 755 82 ILE CG2 C 17.5 0.1 1 612 755 82 ILE N N 118.53 0.1 1 613 756 83 GLU H H 8.62 0.01 1 614 756 83 GLU HA H 4.13 0.01 1 615 756 83 GLU HB2 H 2.05 0.01 1 616 756 83 GLU HB3 H 2.05 0.01 1 617 756 83 GLU HG2 H 2.27 0.01 1 618 756 83 GLU HG3 H 2.27 0.01 1 619 756 83 GLU C C 179 0.1 1 620 756 83 GLU CA C 59.56 0.1 1 621 756 83 GLU CB C 29.26 0.1 1 622 756 83 GLU CG C 36.83 0.1 1 623 756 83 GLU N N 117.98 0.1 1 624 757 84 ALA H H 7.71 0.01 1 625 757 84 ALA HA H 4.13 0.01 1 626 757 84 ALA HB H 1.54 0.01 1 627 757 84 ALA C C 178.5 0.1 1 628 757 84 ALA CA C 55.08 0.1 1 629 757 84 ALA CB C 18.52 0.1 1 630 757 84 ALA N N 121.37 0.1 1 631 758 85 ILE H H 7.95 0.01 1 632 758 85 ILE HA H 3.8 0.01 1 633 758 85 ILE HB H 1.97 0.01 1 634 758 85 ILE HD1 H 0.77 0.01 1 635 758 85 ILE HG12 H 1.12 0.01 1 636 758 85 ILE HG13 H 1.12 0.01 1 637 758 85 ILE HG2 H 0.92 0.01 1 638 758 85 ILE C C 177.4 0.1 1 639 758 85 ILE CA C 64.92 0.1 1 640 758 85 ILE CB C 38.56 0.1 1 641 758 85 ILE CD1 C 14.24 0.1 1 642 758 85 ILE CG1 C 29.95 0.1 1 643 758 85 ILE CG2 C 17.7 0.1 1 644 758 85 ILE N N 119.78 0.1 1 645 759 86 PHE H H 8.54 0.01 1 646 759 86 PHE HA H 4.15 0.01 1 647 759 86 PHE HB2 H 3.07 0.01 2 648 759 86 PHE HB3 H 3.07 0.01 2 649 759 86 PHE HD1 H 6.61 0.01 3 650 759 86 PHE HD2 H 6.61 0.01 3 651 759 86 PHE HE1 H 7.03 0.01 3 652 759 86 PHE HE2 H 7.03 0.01 3 653 759 86 PHE HZ H 7.16 0.01 1 654 759 86 PHE C C 177.4 0.1 1 655 759 86 PHE CA C 61.1 0.1 1 656 759 86 PHE CB C 38.84 0.1 1 657 759 86 PHE CD1 C 131.34 0.1 3 658 759 86 PHE CD2 C 131.34 0.1 3 659 759 86 PHE CE1 C 130.72 0.1 3 660 759 86 PHE CE2 C 130.72 0.1 3 661 759 86 PHE CZ C 133.22 0.1 1 662 759 86 PHE N N 120.27 0.1 1 663 760 87 THR H H 8.41 0.01 1 664 760 87 THR HA H 3.95 0.01 1 665 760 87 THR HB H 4.19 0.01 1 666 760 87 THR HG2 H 1.31 0.01 1 667 760 87 THR C C 176.1 0.1 1 668 760 87 THR CA C 65.98 0.1 1 669 760 87 THR CB C 69.02 0.1 1 670 760 87 THR CG2 C 22.04 0.1 1 671 760 87 THR N N 111.79 0.1 1 672 761 88 LYS H H 7.46 0.01 1 673 761 88 LYS HA H 3.87 0.01 1 674 761 88 LYS HB2 H 1.59 0.01 2 675 761 88 LYS HB3 H 1.47 0.01 2 676 761 88 LYS HD2 H 1.45 0.01 2 677 761 88 LYS HD3 H 1.37 0.01 2 678 761 88 LYS HE2 H 2.62 0.01 1 679 761 88 LYS HE3 H 2.62 0.01 1 680 761 88 LYS HG2 H 0.16 0.01 1 681 761 88 LYS HG3 H 0.16 0.01 1 682 761 88 LYS C C 177.7 0.1 1 683 761 88 LYS CA C 58.65 0.1 1 684 761 88 LYS CB C 33.13 0.1 1 685 761 88 LYS CD C 29.36 0.1 1 686 761 88 LYS CE C 42.39 0.1 1 687 761 88 LYS CG C 24.96 0.1 1 688 761 88 LYS N N 119.31 0.1 1 689 762 89 TYR H H 7.93 0.01 1 690 762 89 TYR HA H 4.47 0.01 1 691 762 89 TYR HB2 H 3.06 0.01 2 692 762 89 TYR HB3 H 2.98 0.01 2 693 762 89 TYR HD1 H 7.49 0.01 3 694 762 89 TYR HD2 H 7.49 0.01 3 695 762 89 TYR HE1 H 6.64 0.01 3 696 762 89 TYR HE2 H 6.64 0.01 3 697 762 89 TYR C C 176.4 0.1 1 698 762 89 TYR CA C 60.84 0.1 1 699 762 89 TYR CB C 38.56 0.1 1 700 762 89 TYR CD1 C 133.65 0.1 3 701 762 89 TYR CD2 C 133.65 0.1 3 702 762 89 TYR CE1 C 117.36 0.1 3 703 762 89 TYR CE2 C 117.36 0.1 3 704 762 89 TYR N N 111.83 0.1 1 705 763 90 ASP H H 7.92 0.01 1 706 763 90 ASP HA H 4.97 0.01 1 707 763 90 ASP HB2 H 2.9 0.01 2 708 763 90 ASP HB3 H 2.74 0.01 2 709 763 90 ASP C C 177.8 0.1 1 710 763 90 ASP CA C 53.2 0.1 1 711 763 90 ASP CB C 39.17 0.1 1 712 763 90 ASP N N 120.72 0.1 1 713 764 91 GLN H H 7.89 0.01 1 714 764 91 GLN HA H 4.61 0.01 1 715 764 91 GLN HB2 H 2.1 0.01 1 716 764 91 GLN HB3 H 2.1 0.01 1 717 764 91 GLN HE21 H 7.86 0.01 2 718 764 91 GLN HE22 H 7 0.01 2 719 764 91 GLN HG2 H 2.5 0.01 1 720 764 91 GLN HG3 H 2.5 0.01 1 721 764 91 GLN C C 176.8 0.1 1 722 764 91 GLN CA C 58.92 0.1 1 723 764 91 GLN CB C 29.28 0.1 1 724 764 91 GLN CG C 34.19 0.1 1 725 764 91 GLN N N 125.88 0.1 1 726 764 91 GLN NE2 N 112.24 0.1 1 727 765 92 ASP H H 8.05 0.01 1 728 765 92 ASP HA H 4.61 0.01 1 729 765 92 ASP HB2 H 2.98 0.01 2 730 765 92 ASP HB3 H 2.65 0.01 2 731 765 92 ASP C C 177.6 0.1 1 732 765 92 ASP CA C 52.38 0.1 1 733 765 92 ASP CB C 39.42 0.1 1 734 765 92 ASP N N 114.26 0.1 1 735 766 93 GLY H H 7.62 0.01 1 736 766 93 GLY HA2 H 3.86 0.01 1 737 766 93 GLY HA3 H 3.86 0.01 1 738 766 93 GLY C C 174.7 0.1 1 739 766 93 GLY CA C 47.11 0.1 1 740 766 93 GLY N N 108.44 0.1 1 741 767 94 ASP H H 8.08 0.01 1 742 767 94 ASP HA H 4.49 0.01 1 743 767 94 ASP HB2 H 3 0.01 2 744 767 94 ASP HB3 H 2.32 0.01 2 745 767 94 ASP C C 176.5 0.1 1 746 767 94 ASP CA C 53.09 0.1 1 747 767 94 ASP N N 119.76 0.1 1 748 768 95 GLN H H 10.03 0.01 1 749 768 95 GLN HA H 4.28 0.01 1 750 768 95 GLN HB2 H 2.39 0.01 2 751 768 95 GLN HB3 H 2.11 0.01 2 752 768 95 GLN HE21 H 7.48 0.01 2 753 768 95 GLN HE22 H 6.67 0.01 2 754 768 95 GLN HG2 H 2.22 0.01 2 755 768 95 GLN HG3 H 2.07 0.01 2 756 768 95 GLN C C 174.2 0.1 1 757 768 95 GLN CA C 56.92 0.1 1 758 768 95 GLN CB C 26.05 0.1 1 759 768 95 GLN CG C 34.12 0.1 1 760 768 95 GLN N N 115.45 0.1 1 761 768 95 GLN NE2 N 112.75 0.1 1 762 769 96 GLU H H 7.98 0.01 1 763 769 96 GLU HA H 4.75 0.01 1 764 769 96 GLU HB2 H 1.82 0.01 1 765 769 96 GLU HB3 H 1.82 0.01 1 766 769 96 GLU HG2 H 2.35 0.01 1 767 769 96 GLU HG3 H 2.35 0.01 1 768 769 96 GLU C C 174.4 0.1 1 769 769 96 GLU CA C 54.88 0.1 1 770 769 96 GLU CB C 32.59 0.1 1 771 769 96 GLU CG C 37.41 0.1 1 772 769 96 GLU N N 118.12 0.1 1 773 770 97 LEU H H 9.31 0.01 1 774 770 97 LEU HA H 5.33 0.01 1 775 770 97 LEU HB2 H 1.73 0.01 1 776 770 97 LEU HB3 H 1.73 0.01 1 777 770 97 LEU HD1 H 1.1 0.01 1 778 770 97 LEU HD2 H 0.72 0.01 1 779 770 97 LEU HG H 1.55 0.01 1 780 770 97 LEU C C 175.7 0.1 1 781 770 97 LEU CA C 53.2 0.1 1 782 770 97 LEU CB C 44.42 0.1 1 783 770 97 LEU CD1 C 25.05 0.1 1 784 770 97 LEU CD2 C 24.5 0.1 1 785 770 97 LEU CG C 26.52 0.1 1 786 770 97 LEU N N 129.84 0.1 1 787 771 98 THR H H 8.46 0.01 1 788 771 98 THR HA H 5.11 0.01 1 789 771 98 THR HB H 3.69 0.01 1 790 771 98 THR HG2 H 1.38 0.01 1 791 771 98 THR C C 174.1 0.1 1 792 771 98 THR CA C 59.53 0.1 1 793 771 98 THR CB C 72.19 0.1 1 794 771 98 THR CG2 C 21.81 0.1 1 795 771 98 THR N N 114.02 0.1 1 796 772 99 GLU H H 8.29 0.01 1 797 772 99 GLU HA H 4.24 0.01 1 798 772 99 GLU C C 178.6 0.1 1 799 772 99 GLU CA C 58.78 0.1 1 800 772 99 GLU CB C 30.31 0.1 1 801 772 99 GLU N N 119.78 0.1 1 802 773 100 HIS H H 8.56 0.01 1 803 773 100 HIS HA H 4.5 0.01 1 804 773 100 HIS HB2 H 3.2 0.01 1 805 773 100 HIS HB3 H 3.2 0.01 1 806 773 100 HIS HD2 H 7.08 0.01 1 807 773 100 HIS HE1 H 7.92 0.01 1 808 773 100 HIS C C 177.9 0.1 1 809 773 100 HIS CA C 59.42 0.1 1 810 773 100 HIS CB C 30.07 0.1 1 811 773 100 HIS CD2 C 120.05 0.1 1 812 773 100 HIS CE1 C 138.1 0.1 1 813 773 100 HIS N N 118.22 0.1 1 814 774 101 GLU H H 7.86 0.01 1 815 774 101 GLU HA H 4.1 0.01 1 816 774 101 GLU HB2 H 2.04 0.01 1 817 774 101 GLU HB3 H 2.04 0.01 1 818 774 101 GLU HG2 H 2.44 0.01 1 819 774 101 GLU HG3 H 2.44 0.01 1 820 774 101 GLU C C 179.9 0.1 1 821 774 101 GLU CA C 59.1 0.1 1 822 774 101 GLU CB C 29.42 0.1 1 823 774 101 GLU N N 120.72 0.1 1 824 775 102 HIS H H 8.78 0.01 1 825 775 102 HIS HA H 4.09 0.01 1 826 775 102 HIS HB2 H 3.06 0.01 2 827 775 102 HIS HB3 H 2.73 0.01 2 828 775 102 HIS HD2 H 6.76 0.01 1 829 775 102 HIS HE1 H 7.65 0.01 1 830 775 102 HIS C C 176.7 0.1 1 831 775 102 HIS CA C 58.61 0.1 1 832 775 102 HIS CB C 29.8 0.1 1 833 775 102 HIS CD2 C 117.79 0.1 1 834 775 102 HIS CE1 C 138.22 0.1 1 835 775 102 HIS N N 119.9 0.1 1 836 776 103 GLN H H 8.06 0.01 1 837 776 103 GLN HA H 4.28 0.01 1 838 776 103 GLN HB2 H 2.22 0.01 1 839 776 103 GLN HB3 H 2.22 0.01 1 840 776 103 GLN HG2 H 2.45 0.01 1 841 776 103 GLN HG3 H 2.45 0.01 1 842 776 103 GLN C C 177.4 0.1 1 843 776 103 GLN CA C 58.46 0.1 1 844 776 103 GLN CB C 27.44 0.1 1 845 776 103 GLN CG C 33.31 0.1 1 846 776 103 GLN N N 119.35 0.1 1 847 777 104 GLN H H 7.19 0.01 1 848 777 104 GLN HA H 3.97 0.01 1 849 777 104 GLN HB2 H 2.1 0.01 1 850 777 104 GLN HB3 H 2.1 0.01 1 851 777 104 GLN HE21 H 7.81 0.01 2 852 777 104 GLN HE22 H 6.9 0.01 2 853 777 104 GLN HG2 H 2.32 0.01 1 854 777 104 GLN HG3 H 2.32 0.01 1 855 777 104 GLN C C 178.5 0.1 1 856 777 104 GLN CA C 58.01 0.1 1 857 777 104 GLN CB C 28.26 0.1 1 858 777 104 GLN CG C 33.63 0.1 1 859 777 104 GLN N N 116.03 0.1 1 860 777 104 GLN NE2 N 115.59 0.1 1 861 778 105 MET H H 8.12 0.01 1 862 778 105 MET HA H 4.32 0.01 1 863 778 105 MET HB2 H 1.8 0.01 1 864 778 105 MET HB3 H 1.8 0.01 1 865 778 105 MET HE H 1.51 0.01 1 866 778 105 MET HG2 H 2.02 0.01 1 867 778 105 MET HG3 H 2.02 0.01 1 868 778 105 MET CA C 55.62 0.1 1 869 778 105 MET N N 120.01 0.1 1 870 781 108 ASP H H 8.48 0.01 1 871 781 108 ASP C C 178.7 0.1 1 872 781 108 ASP CA C 56.6 0.1 1 873 781 108 ASP N N 121.54 0.1 1 874 782 109 LEU H H 7.92 0.01 1 875 782 109 LEU HA H 4.35 0.01 1 876 782 109 LEU HB2 H 1.58 0.01 1 877 782 109 LEU HB3 H 1.58 0.01 1 878 782 109 LEU HD1 H 0.85 0.01 1 879 782 109 LEU C C 178.6 0.1 1 880 782 109 LEU CA C 57.56 0.1 1 881 782 109 LEU CB C 41.5 0.1 1 882 782 109 LEU N N 121.54 0.1 1 883 783 110 GLU H H 7.8 0.01 1 884 783 110 GLU HA H 4.24 0.01 1 885 783 110 GLU HB2 H 2.07 0.01 1 886 783 110 GLU HB3 H 2.07 0.01 1 887 783 110 GLU HG2 H 2.33 0.01 1 888 783 110 GLU HG3 H 2.33 0.01 1 889 783 110 GLU CA C 58.49 0.1 1 890 783 110 GLU CB C 29 0.1 1 891 783 110 GLU CG C 36.24 0.1 1 892 783 110 GLU N N 118.26 0.1 1 893 789 116 LEU C C 178.8 0.1 1 894 790 117 ASP H H 8.56 0.01 1 895 790 117 ASP HA H 4.48 0.01 1 896 790 117 ASP HB2 H 2.75 0.01 1 897 790 117 ASP HB3 H 2.75 0.01 1 898 790 117 ASP C C 176.5 0.1 1 899 790 117 ASP CA C 54.45 0.1 1 900 790 117 ASP CB C 40.45 0.1 1 901 790 117 ASP N N 122.9 0.1 1 902 791 118 LEU H H 8.06 0.01 1 903 791 118 LEU HA H 4.23 0.01 1 904 791 118 LEU HB2 H 1.6 0.01 1 905 791 118 LEU HB3 H 1.6 0.01 1 906 791 118 LEU C C 177.5 0.1 1 907 791 118 LEU CA C 55.52 0.1 1 908 791 118 LEU CB C 42.44 0.1 1 909 791 118 LEU N N 121.54 0.1 1 910 792 119 ASP H H 8.28 0.01 1 911 792 119 ASP HA H 4.63 0.01 1 912 792 119 ASP C C 176.4 0.1 1 913 792 119 ASP CA C 54.88 0.1 1 914 792 119 ASP CB C 40.87 0.1 1 915 792 119 ASP N N 119.62 0.1 1 916 793 120 HIS H H 8.29 0.01 1 917 793 120 HIS HA H 4.59 0.01 1 918 793 120 HIS HB2 H 3.29 0.01 2 919 793 120 HIS HB3 H 3.11 0.01 2 920 793 120 HIS HD2 H 7.06 0.01 1 921 793 120 HIS HE1 H 7.83 0.01 1 922 793 120 HIS C C 174.9 0.1 1 923 793 120 HIS CA C 55.81 0.1 1 924 793 120 HIS CB C 29.19 0.1 1 925 793 120 HIS CD2 C 119.7 0.1 1 926 793 120 HIS CE1 C 138.61 0.1 1 927 793 120 HIS N N 119.25 0.1 1 928 794 121 SER C C 176.4 0.1 1 929 794 121 SER CA C 58.92 0.1 1 930 794 121 SER CB C 63.86 0.1 1 931 794 121 SER N N 116.61 0.1 1 932 795 122 SER H H 8.34 0.01 1 933 795 122 SER HA H 4.38 0.01 1 934 795 122 SER HB2 H 3.97 0.01 2 935 795 122 SER HB3 H 3.83 0.01 2 936 795 122 SER C C 173.5 0.1 1 937 795 122 SER CA C 58.04 0.1 1 938 795 122 SER CB C 63.86 0.1 1 939 795 122 SER N N 118.26 0.1 1 940 796 123 LEU H H 7.84 0.01 1 941 796 123 LEU HA H 4.35 0.01 1 942 796 123 LEU HB2 H 1.58 0.01 1 943 796 123 LEU HB3 H 1.58 0.01 1 944 796 123 LEU HG H 1.55 0.01 1 945 796 123 LEU CA C 56.74 0.1 1 946 796 123 LEU CB C 43.01 0.1 1 947 796 123 LEU N N 129.16 0.1 1 stop_ save_