data_17931 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; biphosphorylated (747pY, 759pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions ; _BMRB_accession_number 17931 _BMRB_flat_file_name bmr17931.str _Entry_type original _Submission_date 2011-09-11 _Accession_date 2011-09-11 _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 Deshmukh Lalit . . 2 Vinogradova Olga . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 281 "13C chemical shifts" 213 "15N chemical shifts" 48 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-14 update BMRB 'update entry citation' 2011-10-20 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17930 'monophosphorylated (747pY) beta3 integrin cytoplasmic tail under membrane mimetic conditions' 17932 'monophosphorylated (747pY) beta3 integrin cytoplasmic tail under aqueous conditions' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Tyrosine phosphorylation as a conformational switch: a case study of integrin 3 cytoplasmic tail.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21956114 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deshmukh Lalit . . 2 Meller Nahum . . 3 Alder Nathan . . 4 Byzova Tatiana . . 5 Vinogradova Olga . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 47 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 40943 _Page_last 40953 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'biphosphorylated (747pY, 759pY) beta3 integrin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'biphosphorylated (747pY, 759pY) beta3 integrin' $biphosphorylated_beta3_integrin 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_biphosphorylated_beta3_integrin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common biphosphorylated_beta3_integrin _Molecular_mass 5746.294 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; GSSHHHHHHSSGLVPRGSHM KLLITIHDRKEFAKFEEERA RAKWDTANNPLXKEATSTFT NITXRGT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 696 GLY 2 697 SER 3 698 SER 4 699 HIS 5 700 HIS 6 701 HIS 7 702 HIS 8 703 HIS 9 704 HIS 10 705 SER 11 706 SER 12 707 GLY 13 708 LEU 14 709 VAL 15 710 PRO 16 711 ARG 17 712 GLY 18 713 SER 19 714 HIS 20 715 MET 21 716 LYS 22 717 LEU 23 718 LEU 24 719 ILE 25 720 THR 26 721 ILE 27 722 HIS 28 723 ASP 29 724 ARG 30 725 LYS 31 726 GLU 32 727 PHE 33 728 ALA 34 729 LYS 35 730 PHE 36 731 GLU 37 732 GLU 38 733 GLU 39 734 ARG 40 735 ALA 41 736 ARG 42 737 ALA 43 738 LYS 44 739 TRP 45 740 ASP 46 741 THR 47 742 ALA 48 743 ASN 49 744 ASN 50 745 PRO 51 746 LEU 52 747 PTR 53 748 LYS 54 749 GLU 55 750 ALA 56 751 THR 57 752 SER 58 753 THR 59 754 PHE 60 755 THR 61 756 ASN 62 757 ILE 63 758 THR 64 759 PTR 65 760 ARG 66 761 GLY 67 762 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-04 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 17930 entity 100.00 67 98.51 98.51 1.85e-38 BMRB 17932 monophosphorylated_(747pY)_beta3_integrin 100.00 67 98.51 98.51 1.85e-38 PDB 1S4X "Nmr Structure Of The Integrin B3 Cytoplasmic Domain In Dpc Micelles" 100.00 67 97.01 97.01 1.12e-30 PDB 2LJD "Monophosphorylated (747py) Beta3 Integrin Cytoplasmic Tail Under Membrane Mimetic Conditions" 100.00 67 98.51 98.51 1.85e-38 PDB 2LJE "Biphosphorylated (747py, 759py) Beta3 Integrin Cytoplasmic Tail Under Membrane Mimetic Conditions" 100.00 67 100.00 100.00 2.29e-38 PDB 2LJF "Monophosphorylated (747py) Beta3 Integrin Cytoplasmic Tail Under Aqueous Conditions" 100.00 67 98.51 98.51 1.85e-38 GB AAB27097 "beta 3 integrin, GPIIIA [mice, Peptide Partial, 680 aa]" 64.18 680 97.67 97.67 1.23e-19 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code . _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Sep 20 15:52:49 2011 ; 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 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P 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 H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $biphosphorylated_beta3_integrin 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 $biphosphorylated_beta3_integrin 'recombinant technology' . Escherichia coli . pET16b 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $biphosphorylated_beta3_integrin 0.2 mM . . '[U-100% 13C; U-100% 15N]' DSS 1 mM . . 'natural abundance' DPC . mM 150 300 '[U-100% 2H]' 'sodium phosphate' 20 mM . . 'natural abundance' D2O 95 % . . 'natural abundance' H2O 5 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version 1.21 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_PSVS _Saveframe_category software _Name PSVS _Version . loop_ _Vendor _Address _Electronic_address 'Bhattacharya and Montelione' . . stop_ loop_ _Task validation stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model compact _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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 pH 5.9 . pH pressure 1 . atm temperature 273 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0 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' '2D 1H-13C HSQC' '3D HNCO' '3D 1H-15N NOESY' 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 'biphosphorylated (747pY, 759pY) beta3 integrin' _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 1 716 21 LYS HA H 3.975 0.02 1 2 716 21 LYS HB2 H 1.747 0.02 2 3 716 21 LYS HB3 H 1.635 0.02 2 4 716 21 LYS HG2 H 1.425 0.02 2 5 716 21 LYS HG3 H 1.425 0.02 2 6 716 21 LYS HD2 H 1.661 0.02 2 7 716 21 LYS HD3 H 1.661 0.02 2 8 716 21 LYS HE2 H 2.952 0.02 2 9 716 21 LYS HE3 H 2.952 0.02 2 10 716 21 LYS H H 8.031 0.02 1 11 716 21 LYS C C 178.066 0.02 1 12 716 21 LYS CA C 57.786 0.02 1 13 716 21 LYS CB C 30.045 0.02 1 14 716 21 LYS CG C 25.056 0.02 1 15 716 21 LYS CD C 29.335 0.02 1 16 716 21 LYS CE C 38.525 0.02 1 17 716 21 LYS N N 119.867 0.02 1 18 717 22 LEU H H 7.866 0.02 1 19 717 22 LEU HA H 4.130 0.02 1 20 717 22 LEU HB2 H 1.664 0.02 2 21 717 22 LEU HB3 H 1.768 0.02 2 22 717 22 LEU HG H 1.661 0.02 1 23 717 22 LEU HD1 H 0.904 0.02 2 24 717 22 LEU HD2 H 0.813 0.02 2 25 717 22 LEU C C 177.505 0.02 1 26 717 22 LEU CA C 56.674 0.02 1 27 717 22 LEU CB C 41.853 0.002 1 28 717 22 LEU CG C 28.994 0.02 1 29 717 22 LEU CD1 C 24.646 0.02 2 30 717 22 LEU CD2 C 23.700 0.02 2 31 717 22 LEU N N 120.100 0.02 1 32 718 23 LEU H H 7.746 0.02 1 33 718 23 LEU HA H 4.057 0.02 1 34 718 23 LEU HB2 H 1.795 0.02 2 35 718 23 LEU HB3 H 1.795 0.02 2 36 718 23 LEU HG H 1.671 0.02 1 37 718 23 LEU HD1 H 0.867 0.02 2 38 718 23 LEU HD2 H 0.854 0.02 2 39 718 23 LEU C C 177.643 0.02 1 40 718 23 LEU CA C 56.943 0.02 1 41 718 23 LEU CB C 41.735 0.001 1 42 718 23 LEU CG C 27.185 0.02 1 43 718 23 LEU CD1 C 24.909 0.02 2 44 718 23 LEU CD2 C 24.233 0.02 2 45 718 23 LEU N N 118.481 0.02 1 46 719 24 ILE H H 7.724 0.02 1 47 719 24 ILE HA H 3.911 0.02 1 48 719 24 ILE HB H 1.896 0.02 1 49 719 24 ILE HG12 H 1.541 0.02 2 50 719 24 ILE HG13 H 1.195 0.02 2 51 719 24 ILE HG2 H 0.913 0.02 1 52 719 24 ILE HD1 H 0.732 0.02 1 53 719 24 ILE C C 176.774 0.02 1 54 719 24 ILE CA C 62.960 0.02 1 55 719 24 ILE CB C 38.219 0.02 1 56 719 24 ILE CG1 C 28.147 0.008 1 57 719 24 ILE CG2 C 17.632 0.02 1 58 719 24 ILE CD1 C 13.328 0.02 1 59 719 24 ILE N N 116.207 0.02 1 60 720 25 THR H H 7.802 0.02 1 61 720 25 THR HA H 4.161 0.02 1 62 720 25 THR HB H 4.291 0.02 1 63 720 25 THR HG2 H 1.195 0.02 1 64 720 25 THR C C 175.458 0.02 1 65 720 25 THR CA C 64.390 0.02 1 66 720 25 THR CB C 69.052 0.02 1 67 720 25 THR CG2 C 21.601 0.02 1 68 720 25 THR N N 114.581 0.02 1 69 721 26 ILE H H 7.751 0.02 1 70 721 26 ILE HA H 3.909 0.02 1 71 721 26 ILE HB H 1.941 0.02 1 72 721 26 ILE HG12 H 1.113 0.02 2 73 721 26 ILE HG13 H 1.500 0.02 2 74 721 26 ILE HG2 H 0.791 0.02 1 75 721 26 ILE HD1 H 0.809 0.02 1 76 721 26 ILE C C 176.102 0.02 1 77 721 26 ILE CA C 63.025 0.02 1 78 721 26 ILE CB C 38.104 0.02 1 79 721 26 ILE CG1 C 27.851 0.001 1 80 721 26 ILE CG2 C 17.583 0.02 1 81 721 26 ILE CD1 C 13.157 0.02 1 82 721 26 ILE N N 119.805 0.02 1 83 722 27 HIS H H 8.097 0.02 1 84 722 27 HIS HA H 4.615 0.02 1 85 722 27 HIS HB2 H 3.096 0.02 2 86 722 27 HIS HB3 H 3.267 0.02 2 87 722 27 HIS HD2 H 7.120 0.02 1 88 722 27 HIS C C 174.538 0.02 1 89 722 27 HIS CA C 57.344 0.02 1 90 722 27 HIS CB C 29.375 0.02 1 91 722 27 HIS CD2 C 120.340 0.02 1 92 722 27 HIS N N 118.760 0.02 1 93 723 28 ASP H H 7.969 0.02 1 94 723 28 ASP HA H 4.594 0.02 1 95 723 28 ASP HB2 H 2.728 0.02 2 96 723 28 ASP HB3 H 2.697 0.02 2 97 723 28 ASP C C 176.829 0.02 1 98 723 28 ASP CA C 54.176 0.02 1 99 723 28 ASP CB C 41.500 0.020 1 100 723 28 ASP N N 117.884 0.02 1 101 724 29 ARG H H 8.216 0.02 1 102 724 29 ARG HA H 4.204 0.02 1 103 724 29 ARG HB2 H 1.742 0.02 2 104 724 29 ARG HB3 H 1.656 0.02 2 105 724 29 ARG HD2 H 3.159 0.02 2 106 724 29 ARG HD3 H 3.159 0.02 2 107 724 29 ARG C C 177.662 0.02 1 108 724 29 ARG CA C 56.819 0.02 1 109 724 29 ARG CB C 32.703 0.02 1 110 724 29 ARG CD C 39.026 0.02 1 111 724 29 ARG N N 121.014 0.02 1 112 725 30 LYS HA H 4.135 0.02 1 113 725 30 LYS HB2 H 1.850 0.02 2 114 725 30 LYS HB3 H 1.850 0.02 2 115 725 30 LYS HG2 H 1.432 0.02 2 116 725 30 LYS HG3 H 1.432 0.02 2 117 725 30 LYS HE2 H 3.213 0.02 2 118 725 30 LYS HE3 H 3.213 0.02 2 119 725 30 LYS C C 178.127 0.02 1 120 725 30 LYS CA C 57.747 0.02 1 121 725 30 LYS CB C 32.190 0.02 1 122 725 30 LYS CG C 24.793 0.02 1 123 725 30 LYS CE C 42.918 0.02 1 124 726 31 GLU HA H 4.096 0.02 1 125 726 31 GLU HB2 H 1.902 0.02 2 126 726 31 GLU HB3 H 1.937 0.02 2 127 726 31 GLU HG2 H 2.238 0.02 2 128 726 31 GLU HG3 H 2.238 0.02 2 129 726 31 GLU C C 177.791 0.02 1 130 726 31 GLU CA C 58.406 0.02 1 131 726 31 GLU CB C 29.340 0.02 1 132 726 31 GLU CG C 36.199 0.02 1 133 727 32 PHE H H 7.922 0.02 1 134 727 32 PHE HA H 4.378 0.02 1 135 727 32 PHE HB2 H 3.153 0.02 2 136 727 32 PHE HB3 H 3.153 0.02 2 137 727 32 PHE HD1 H 7.176 0.02 3 138 727 32 PHE HD2 H 7.176 0.02 3 139 727 32 PHE HE1 H 7.215 0.02 3 140 727 32 PHE HE2 H 7.215 0.02 3 141 727 32 PHE C C 176.439 0.02 1 142 727 32 PHE CA C 59.332 0.02 1 143 727 32 PHE CB C 39.160 0.02 1 144 727 32 PHE CD1 C 131.605 0.02 3 145 727 32 PHE CD2 C 131.605 0.02 3 146 727 32 PHE CE1 C 131.660 0.02 3 147 727 32 PHE CE2 C 131.660 0.02 3 148 727 32 PHE N N 118.859 0.02 1 149 728 33 ALA H H 7.970 0.02 1 150 728 33 ALA HA H 4.158 0.02 1 151 728 33 ALA HB H 1.449 0.02 1 152 728 33 ALA C C 178.542 0.02 1 153 728 33 ALA CA C 54.083 0.02 1 154 728 33 ALA CB C 18.409 0.02 1 155 728 33 ALA N N 122.111 0.02 1 156 729 34 LYS H H 7.792 0.02 1 157 729 34 LYS HA H 4.096 0.02 1 158 729 34 LYS HB2 H 1.767 0.02 2 159 729 34 LYS HB3 H 1.767 0.02 2 160 729 34 LYS HG2 H 1.340 0.02 2 161 729 34 LYS HG3 H 1.340 0.02 2 162 729 34 LYS HD2 H 1.584 0.02 2 163 729 34 LYS HD3 H 1.584 0.02 2 164 729 34 LYS HE2 H 3.077 0.02 2 165 729 34 LYS HE3 H 3.077 0.02 2 166 729 34 LYS C C 177.664 0.02 1 167 729 34 LYS CA C 56.930 0.02 1 168 729 34 LYS CB C 30.515 0.02 1 169 729 34 LYS CG C 24.787 0.02 1 170 729 34 LYS CD C 27.056 0.02 1 171 729 34 LYS CE C 38.870 0.02 1 172 729 34 LYS N N 117.588 0.02 1 173 730 35 PHE H H 7.874 0.02 1 174 730 35 PHE HA H 4.379 0.02 1 175 730 35 PHE HB2 H 3.106 0.02 2 176 730 35 PHE HB3 H 3.220 0.02 2 177 730 35 PHE HD1 H 7.213 0.02 3 178 730 35 PHE HD2 H 7.213 0.02 3 179 730 35 PHE HE1 H 7.165 0.02 3 180 730 35 PHE HE2 H 7.165 0.02 3 181 730 35 PHE C C 176.732 0.02 1 182 730 35 PHE CA C 59.753 0.02 1 183 730 35 PHE CB C 39.010 0.02 1 184 730 35 PHE CD1 C 131.233 0.02 3 185 730 35 PHE CD2 C 131.233 0.02 3 186 730 35 PHE CE1 C 132.178 0.02 3 187 730 35 PHE CE2 C 132.178 0.02 3 188 730 35 PHE N N 119.916 0.02 1 189 731 36 GLU H H 8.178 0.02 1 190 731 36 GLU HA H 4.065 0.02 1 191 731 36 GLU HB2 H 1.989 0.02 2 192 731 36 GLU HB3 H 1.989 0.02 2 193 731 36 GLU HG2 H 2.205 0.02 2 194 731 36 GLU HG3 H 2.307 0.02 2 195 731 36 GLU C C 177.920 0.02 1 196 731 36 GLU CA C 57.825 0.02 1 197 731 36 GLU CB C 29.349 0.02 1 198 731 36 GLU CG C 36.187 0.02 1 199 731 36 GLU N N 119.398 0.02 1 200 732 37 GLU H H 8.117 0.02 1 201 732 37 GLU HA H 4.050 0.02 1 202 732 37 GLU HB2 H 2.043 0.02 2 203 732 37 GLU HB3 H 2.043 0.02 2 204 732 37 GLU HG2 H 2.213 0.02 2 205 732 37 GLU HG3 H 2.213 0.02 2 206 732 37 GLU C C 178.097 0.02 1 207 732 37 GLU CA C 58.307 0.02 1 208 732 37 GLU CB C 29.388 0.02 1 209 732 37 GLU CG C 35.693 0.02 1 210 732 37 GLU N N 120.386 0.02 1 211 733 38 GLU H H 8.130 0.02 1 212 733 38 GLU HA H 4.056 0.02 1 213 733 38 GLU HB2 H 2.028 0.02 2 214 733 38 GLU HB3 H 2.028 0.02 2 215 733 38 GLU HG2 H 2.295 0.02 2 216 733 38 GLU HG3 H 2.295 0.02 2 217 733 38 GLU C C 177.228 0.02 1 218 733 38 GLU CA C 58.298 0.02 1 219 733 38 GLU CB C 29.447 0.02 1 220 733 38 GLU CG C 35.870 0.02 1 221 733 38 GLU N N 119.473 0.02 1 222 734 39 ARG H H 8.032 0.02 1 223 734 39 ARG HA H 4.029 0.02 1 224 734 39 ARG HB2 H 1.851 0.02 2 225 734 39 ARG HB3 H 1.851 0.02 2 226 734 39 ARG HG2 H 1.463 0.02 2 227 734 39 ARG HG3 H 1.463 0.02 2 228 734 39 ARG HD2 H 3.130 0.02 2 229 734 39 ARG HD3 H 3.130 0.02 2 230 734 39 ARG C C 177.402 0.02 1 231 734 39 ARG CA C 58.400 0.02 1 232 734 39 ARG CB C 32.170 0.02 1 233 734 39 ARG CG C 27.052 0.02 1 234 734 39 ARG CD C 43.342 0.02 1 235 734 39 ARG N N 118.929 0.02 1 236 735 40 ALA H H 7.853 0.02 1 237 735 40 ALA HA H 4.129 0.02 1 238 735 40 ALA HB H 1.402 0.02 1 239 735 40 ALA C C 179.108 0.02 1 240 735 40 ALA CA C 53.559 0.02 1 241 735 40 ALA CB C 18.561 0.02 1 242 735 40 ALA N N 121.514 0.02 1 243 736 41 ARG H H 7.850 0.02 1 244 736 41 ARG HA H 4.110 0.02 1 245 736 41 ARG HB2 H 1.828 0.02 2 246 736 41 ARG HB3 H 1.828 0.02 2 247 736 41 ARG HG2 H 1.660 0.02 2 248 736 41 ARG HG3 H 1.660 0.02 2 249 736 41 ARG HD2 H 3.145 0.02 2 250 736 41 ARG HD3 H 3.145 0.02 2 251 736 41 ARG C C 176.643 0.02 1 252 736 41 ARG CA C 56.737 0.02 1 253 736 41 ARG CB C 30.573 0.02 1 254 736 41 ARG CG C 27.114 0.02 1 255 736 41 ARG CD C 42.796 0.02 1 256 736 41 ARG N N 117.944 0.02 1 257 737 42 ALA H H 7.776 0.02 1 258 737 42 ALA HA H 4.151 0.02 1 259 737 42 ALA HB H 1.247 0.02 1 260 737 42 ALA C C 177.640 0.02 1 261 737 42 ALA CA C 52.770 0.02 1 262 737 42 ALA CB C 18.747 0.02 1 263 737 42 ALA N N 122.381 0.02 1 264 738 43 LYS H H 7.838 0.02 1 265 738 43 LYS HA H 4.159 0.02 1 266 738 43 LYS HB2 H 1.674 0.02 2 267 738 43 LYS HB3 H 1.674 0.02 2 268 738 43 LYS HG2 H 1.279 0.02 2 269 738 43 LYS HG3 H 1.279 0.02 2 270 738 43 LYS HE2 H 3.144 0.02 2 271 738 43 LYS HE3 H 3.144 0.02 2 272 738 43 LYS C C 176.483 0.02 1 273 738 43 LYS CA C 56.468 0.02 1 274 738 43 LYS CB C 32.526 0.007 1 275 738 43 LYS CG C 24.501 0.02 1 276 738 43 LYS CE C 39.506 0.02 1 277 738 43 LYS N N 118.327 0.02 1 278 739 44 TRP H H 7.958 0.02 1 279 739 44 TRP HA H 4.601 0.02 1 280 739 44 TRP HB2 H 3.275 0.02 2 281 739 44 TRP HB3 H 3.164 0.02 2 282 739 44 TRP HD1 H 7.198 0.02 1 283 739 44 TRP HE1 H 10.306 0.02 1 284 739 44 TRP HE3 H 7.089 0.02 1 285 739 44 TRP HZ2 H 7.407 0.02 1 286 739 44 TRP HH2 H 7.089 0.02 1 287 739 44 TRP C C 175.904 0.02 1 288 739 44 TRP CA C 56.947 0.02 1 289 739 44 TRP CB C 29.521 0.02 1 290 739 44 TRP CD1 C 127.324 0.02 1 291 739 44 TRP CE3 C 123.074 0.02 1 292 739 44 TRP CZ2 C 114.279 0.02 1 293 739 44 TRP CH2 C 124.126 0.02 1 294 739 44 TRP N N 120.598 0.02 1 295 739 44 TRP NE1 N 129.835 0.02 1 296 740 45 ASP H H 8.248 0.02 1 297 740 45 ASP HA H 4.151 0.02 1 298 740 45 ASP HB2 H 2.634 0.02 2 299 740 45 ASP HB3 H 2.555 0.02 2 300 740 45 ASP C C 176.626 0.02 1 301 740 45 ASP CA C 54.173 0.02 1 302 740 45 ASP CB C 40.971 0.007 1 303 740 45 ASP N N 121.214 0.02 1 304 741 46 THR H H 7.945 0.02 1 305 741 46 THR HA H 4.221 0.02 1 306 741 46 THR HB H 4.193 0.02 1 307 741 46 THR HG2 H 1.145 0.02 1 308 741 46 THR C C 174.851 0.02 1 309 741 46 THR CA C 62.439 0.02 1 310 741 46 THR CB C 69.255 0.02 1 311 741 46 THR CG2 C 21.642 0.02 1 312 741 46 THR N N 113.708 0.02 1 313 742 47 ALA H H 8.113 0.02 1 314 742 47 ALA HA H 4.196 0.02 1 315 742 47 ALA HB H 1.334 0.02 1 316 742 47 ALA C C 177.509 0.02 1 317 742 47 ALA CA C 52.953 0.02 1 318 742 47 ALA CB C 18.949 0.02 1 319 742 47 ALA N N 124.543 0.02 1 320 743 48 ASN H H 8.055 0.02 1 321 743 48 ASN HA H 4.599 0.02 1 322 743 48 ASN HB2 H 2.604 0.02 2 323 743 48 ASN HB3 H 2.604 0.02 2 324 743 48 ASN HD21 H 7.595 0.02 2 325 743 48 ASN HD22 H 6.775 0.02 2 326 743 48 ASN C C 174.330 0.02 1 327 743 48 ASN CA C 52.868 0.02 1 328 743 48 ASN CB C 38.995 0.02 1 329 743 48 ASN N N 116.039 0.02 1 330 743 48 ASN ND2 N 113.260 0.001 1 331 744 49 ASN H H 8.015 0.02 1 332 744 49 ASN HA H 4.608 0.02 1 333 744 49 ASN HB2 H 2.801 0.02 2 334 744 49 ASN HB3 H 2.643 0.02 2 335 744 49 ASN HD21 H 7.705 0.02 2 336 744 49 ASN HD22 H 6.645 0.02 2 337 744 49 ASN CA C 50.940 0.02 1 338 744 49 ASN CB C 38.798 0.02 1 339 744 49 ASN N N 119.625 0.02 1 340 744 49 ASN ND2 N 112.475 0.004 1 341 745 50 PRO HA H 4.372 0.02 1 342 745 50 PRO HB2 H 2.236 0.02 2 343 745 50 PRO HB3 H 1.856 0.02 2 344 745 50 PRO HG2 H 1.897 0.02 2 345 745 50 PRO HG3 H 1.973 0.02 2 346 745 50 PRO HD2 H 3.756 0.02 2 347 745 50 PRO HD3 H 3.662 0.02 2 348 745 50 PRO C C 177.196 0.02 1 349 745 50 PRO CA C 63.583 0.02 1 350 745 50 PRO CB C 31.888 0.013 1 351 745 50 PRO CG C 27.086 0.02 1 352 745 50 PRO CD C 50.594 0.02 1 353 746 51 LEU H H 8.085 0.02 1 354 746 51 LEU HA H 4.197 0.02 1 355 746 51 LEU HB2 H 1.442 0.02 2 356 746 51 LEU HB3 H 1.562 0.02 2 357 746 51 LEU HG H 1.537 0.02 1 358 746 51 LEU HD1 H 0.793 0.02 1 359 746 51 LEU HD2 H 0.793 0.02 1 360 746 51 LEU C C 177.480 0.02 1 361 746 51 LEU CA C 55.716 0.02 1 362 746 51 LEU CB C 41.683 0.022 1 363 746 51 LEU CG C 26.938 0.02 1 364 746 51 LEU CD1 C 23.336 0.02 2 365 746 51 LEU N N 119.443 0.02 1 366 747 52 PTR C C 175.836 0.02 1 367 747 52 PTR CA C 57.935 0.02 1 368 747 52 PTR CB C 38.424 0.02 1 369 747 52 PTR CD1 C 132.986 0.02 3 370 747 52 PTR CD2 C 132.986 0.02 3 371 747 52 PTR CE1 C 118.110 0.02 3 372 747 52 PTR CE2 C 118.110 0.02 3 373 747 52 PTR H H 7.789 0.02 1 374 747 52 PTR HA H 4.452 0.02 1 375 747 52 PTR HB2 H 2.994 0.02 2 376 747 52 PTR HB3 H 3.087 0.02 2 377 747 52 PTR N N 119.182 0.02 1 378 747 52 PTR HD1 H 7.089 0.02 3 379 747 52 PTR HD2 H 7.089 0.02 3 380 747 52 PTR HE1 H 6.770 0.02 3 381 747 52 PTR HE2 H 6.770 0.02 3 382 748 53 LYS H H 7.880 0.02 1 383 748 53 LYS HA H 4.124 0.02 1 384 748 53 LYS HB2 H 1.738 0.02 2 385 748 53 LYS HB3 H 1.671 0.02 2 386 748 53 LYS HG2 H 1.297 0.02 2 387 748 53 LYS HG3 H 1.297 0.02 2 388 748 53 LYS HD2 H 1.594 0.02 2 389 748 53 LYS HD3 H 1.594 0.02 2 390 748 53 LYS C C 176.606 0.02 1 391 748 53 LYS CA C 56.448 0.02 1 392 748 53 LYS CB C 32.831 0.02 1 393 748 53 LYS CG C 24.553 0.02 1 394 748 53 LYS CD C 28.858 0.02 1 395 748 53 LYS N N 121.752 0.02 1 396 749 54 GLU H H 8.215 0.02 1 397 749 54 GLU HA H 4.206 0.02 1 398 749 54 GLU HB2 H 1.946 0.02 2 399 749 54 GLU HB3 H 2.041 0.02 2 400 749 54 GLU HG2 H 2.271 0.02 2 401 749 54 GLU HG3 H 2.271 0.02 2 402 749 54 GLU C C 176.764 0.02 1 403 749 54 GLU CA C 56.698 0.02 1 404 749 54 GLU CB C 29.784 0.02 1 405 749 54 GLU CG C 35.777 0.003 1 406 749 54 GLU N N 121.140 0.02 1 407 750 55 ALA H H 8.335 0.02 1 408 750 55 ALA HA H 4.276 0.02 1 409 750 55 ALA HB H 1.387 0.02 1 410 750 55 ALA C C 178.054 0.02 1 411 750 55 ALA CA C 53.011 0.02 1 412 750 55 ALA CB C 19.021 0.02 1 413 750 55 ALA N N 124.506 0.02 1 414 751 56 THR H H 8.007 0.02 1 415 751 56 THR HA H 4.225 0.02 1 416 751 56 THR HB H 4.213 0.02 1 417 751 56 THR HG2 H 1.125 0.02 1 418 751 56 THR C C 175.137 0.02 1 419 751 56 THR CA C 62.508 0.02 1 420 751 56 THR CB C 69.600 0.02 1 421 751 56 THR CG2 C 21.881 0.02 1 422 751 56 THR N N 111.925 0.02 1 423 752 57 SER H H 8.156 0.02 1 424 752 57 SER HA H 4.567 0.02 1 425 752 57 SER HB2 H 3.868 0.02 2 426 752 57 SER HB3 H 3.803 0.02 2 427 752 57 SER C C 174.881 0.02 1 428 752 57 SER CA C 58.856 0.02 1 429 752 57 SER CB C 63.705 0.02 1 430 752 57 SER N N 117.676 0.02 1 431 753 58 THR H H 8.042 0.02 1 432 753 58 THR HA H 4.126 0.02 1 433 753 58 THR HB H 4.068 0.02 1 434 753 58 THR HG2 H 1.020 0.02 1 435 753 58 THR C C 174.555 0.02 1 436 753 58 THR CA C 62.889 0.02 1 437 753 58 THR CB C 69.292 0.02 1 438 753 58 THR CG2 C 21.497 0.02 1 439 753 58 THR N N 116.343 0.02 1 440 754 59 PHE H H 8.163 0.02 1 441 754 59 PHE HA H 4.567 0.02 1 442 754 59 PHE HB2 H 3.000 0.02 2 443 754 59 PHE HB3 H 3.154 0.02 2 444 754 59 PHE HD1 H 7.211 0.02 3 445 754 59 PHE HD2 H 7.211 0.02 3 446 754 59 PHE HE1 H 7.214 0.02 3 447 754 59 PHE HE2 H 7.214 0.02 3 448 754 59 PHE C C 175.956 0.02 1 449 754 59 PHE CA C 58.289 0.02 1 450 754 59 PHE CB C 39.222 0.011 1 451 754 59 PHE CD1 C 131.470 0.02 3 452 754 59 PHE CD2 C 131.470 0.02 3 453 754 59 PHE CE1 C 132.127 0.02 3 454 754 59 PHE CE2 C 132.127 0.02 3 455 754 59 PHE N N 120.983 0.02 1 456 755 60 THR H H 7.943 0.02 1 457 755 60 THR HA H 4.159 0.02 1 458 755 60 THR HB H 4.166 0.02 1 459 755 60 THR HG2 H 1.189 0.02 1 460 755 60 THR C C 174.168 0.02 1 461 755 60 THR CA C 62.446 0.02 1 462 755 60 THR CB C 69.403 0.02 1 463 755 60 THR CG2 C 21.504 0.02 1 464 755 60 THR N N 114.474 0.02 1 465 756 61 ASN H H 8.254 0.02 1 466 756 61 ASN HA H 4.599 0.02 1 467 756 61 ASN HB2 H 2.740 0.02 2 468 756 61 ASN HB3 H 2.740 0.02 2 469 756 61 ASN HD21 H 6.832 0.02 2 470 756 61 ASN HD22 H 7.566 0.02 2 471 756 61 ASN C C 175.438 0.02 1 472 756 61 ASN CA C 53.625 0.02 1 473 756 61 ASN CB C 38.852 0.02 1 474 756 61 ASN N N 120.598 0.02 1 475 756 61 ASN ND2 N 112.493 0.001 1 476 757 62 ILE H H 7.988 0.02 1 477 757 62 ILE HA H 4.133 0.02 1 478 757 62 ILE HB H 1.869 0.02 1 479 757 62 ILE HG12 H 1.455 0.02 2 480 757 62 ILE HG13 H 1.162 0.02 2 481 757 62 ILE HG2 H 0.842 0.02 1 482 757 62 ILE HD1 H 0.809 0.02 1 483 757 62 ILE C C 176.180 0.02 1 484 757 62 ILE CA C 61.607 0.02 1 485 757 62 ILE CB C 38.526 0.02 1 486 757 62 ILE CG1 C 27.358 0.002 1 487 757 62 ILE CG2 C 17.552 0.02 1 488 757 62 ILE CD1 C 13.246 0.02 1 489 757 62 ILE N N 119.988 0.02 1 490 758 63 THR H H 7.963 0.02 1 491 758 63 THR HA H 4.276 0.02 1 492 758 63 THR HB H 4.112 0.02 1 493 758 63 THR HG2 H 1.125 0.02 1 494 758 63 THR C C 174.334 0.02 1 495 758 63 THR CA C 61.620 0.02 1 496 758 63 THR CB C 69.517 0.02 1 497 758 63 THR CG2 C 21.265 0.02 1 498 758 63 THR N N 115.445 0.02 1 499 759 64 PTR C C 175.431 0.02 1 500 759 64 PTR CA C 57.894 0.02 1 501 759 64 PTR CB C 38.782 0.02 1 502 759 64 PTR CD1 C 132.992 0.02 3 503 759 64 PTR CD2 C 132.992 0.02 3 504 759 64 PTR CE1 C 118.143 0.02 3 505 759 64 PTR CE2 C 118.143 0.02 3 506 759 64 PTR H H 8.037 0.02 1 507 759 64 PTR HA H 4.567 0.02 1 508 759 64 PTR N N 122.379 0.02 1 509 759 64 PTR HB2 H 3.036 0.02 2 510 759 64 PTR HB3 H 3.036 0.02 2 511 759 64 PTR HD1 H 7.064 0.02 3 512 759 64 PTR HD2 H 7.064 0.02 3 513 759 64 PTR HE1 H 6.771 0.02 3 514 759 64 PTR HE2 H 6.771 0.02 3 515 760 65 ARG H H 8.035 0.02 1 516 760 65 ARG HA H 4.266 0.02 1 517 760 65 ARG HB2 H 1.656 0.02 2 518 760 65 ARG HB3 H 1.832 0.02 2 519 760 65 ARG HG2 H 1.493 0.02 2 520 760 65 ARG HG3 H 1.493 0.02 2 521 760 65 ARG HD2 H 2.971 0.02 2 522 760 65 ARG HD3 H 2.919 0.02 2 523 760 65 ARG C C 176.189 0.02 1 524 760 65 ARG CA C 55.718 0.02 1 525 760 65 ARG CB C 30.827 0.02 1 526 760 65 ARG CG C 26.982 0.02 1 527 760 65 ARG CD C 41.901 0.003 1 528 760 65 ARG N N 122.859 0.02 1 529 761 66 GLY H H 8.038 0.02 1 530 761 66 GLY HA2 H 3.908 0.02 2 531 761 66 GLY HA3 H 3.952 0.02 2 532 761 66 GLY C C 173.400 0.02 1 533 761 66 GLY CA C 45.241 0.007 1 534 761 66 GLY N N 109.795 0.02 1 535 762 67 THR H H 7.638 0.02 1 536 762 67 THR HA H 4.160 0.02 1 537 762 67 THR HB H 4.212 0.02 1 538 762 67 THR HG2 H 1.063 0.02 1 539 762 67 THR CA C 62.990 0.02 1 540 762 67 THR CB C 70.610 0.02 1 541 762 67 THR CG2 C 21.481 0.02 1 542 762 67 THR N N 118.473 0.02 1 stop_ save_