data_15722 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Resonance Assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase ; _BMRB_accession_number 15722 _BMRB_flat_file_name bmr15722.str _Entry_type original _Submission_date 2008-04-08 _Accession_date 2008-04-08 _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 Philominathan 'Sagaya T. Leena' . . 2 Matsushita Osamu . . 3 Jordan 'J. Brad' . . 4 Sakon Joshua . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 525 "13C chemical shifts" 420 "15N chemical shifts" 105 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-13 update BMRB 'added PubMed ID' 2008-12-02 update BMRB 'complete entry citation' 2008-08-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '1H, 13C and 15N resonance assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636886 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Philominathan 'Sagaya Theresa Leena' . . 2 Matsushita Osamu . . 3 Jordan 'John Brad' . . 4 Sakon Joshua . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR Assignments' _Journal_volume 2 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 127 _Page_last 129 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ca2+ bound Collagen binding domain derived from Clostridium Histolyticum' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Collagen binding domain derived from Clostridium Histolyticum' $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 'Calcium ion, 2+' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function collagenase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Collagen_binding_domain_derived_from_Clostridium_Histolyticum _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Collagen_binding_domain_derived_from_Clostridium_Histolyticum _Molecular_mass 13786 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; GSPGIPGNEKLKEKENNDSS DKATVIPNFNTTMQGSLLGD DSRDYYSFEVKEEGEVNIEL DKKDEFGVTWTLHPESNIND RITYGQVDGNKVSNKVKLRP GKYYLLVYKYSGSGNYELRV NK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 887 GLY 2 888 SER 3 889 PRO 4 890 GLY 5 891 ILE 6 892 PRO 7 893 GLY 8 894 ASN 9 895 GLU 10 896 LYS 11 897 LEU 12 898 LYS 13 899 GLU 14 900 LYS 15 901 GLU 16 902 ASN 17 903 ASN 18 904 ASP 19 905 SER 20 906 SER 21 907 ASP 22 908 LYS 23 909 ALA 24 910 THR 25 911 VAL 26 912 ILE 27 913 PRO 28 914 ASN 29 915 PHE 30 916 ASN 31 917 THR 32 918 THR 33 919 MET 34 920 GLN 35 921 GLY 36 922 SER 37 923 LEU 38 924 LEU 39 925 GLY 40 926 ASP 41 927 ASP 42 928 SER 43 929 ARG 44 930 ASP 45 931 TYR 46 932 TYR 47 933 SER 48 934 PHE 49 935 GLU 50 936 VAL 51 937 LYS 52 938 GLU 53 939 GLU 54 940 GLY 55 941 GLU 56 942 VAL 57 943 ASN 58 944 ILE 59 945 GLU 60 946 LEU 61 947 ASP 62 948 LYS 63 949 LYS 64 950 ASP 65 951 GLU 66 952 PHE 67 953 GLY 68 954 VAL 69 955 THR 70 956 TRP 71 957 THR 72 958 LEU 73 959 HIS 74 960 PRO 75 961 GLU 76 962 SER 77 963 ASN 78 964 ILE 79 965 ASN 80 966 ASP 81 967 ARG 82 968 ILE 83 969 THR 84 970 TYR 85 971 GLY 86 972 GLN 87 973 VAL 88 974 ASP 89 975 GLY 90 976 ASN 91 977 LYS 92 978 VAL 93 979 SER 94 980 ASN 95 981 LYS 96 982 VAL 97 983 LYS 98 984 LEU 99 985 ARG 100 986 PRO 101 987 GLY 102 988 LYS 103 989 TYR 104 990 TYR 105 991 LEU 106 992 LEU 107 993 VAL 108 994 TYR 109 995 LYS 110 996 TYR 111 997 SER 112 998 GLY 113 999 SER 114 1000 GLY 115 1001 ASN 116 1002 TYR 117 1003 GLU 118 1004 LEU 119 1005 ARG 120 1006 VAL 121 1007 ASN 122 1008 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 1NQD "Crystal Structure Of Clostridium Histolyticum Colg Collagenase Collagen-Binding Domain 3b At 1.65 Angstrom Resolution In Presen" 100.00 122 100.00 100.00 7.63e-81 PDB 1NQJ "Crystal Structure Of Clostridium Histolyticum Colg Collagenase Collagen-Binding Domain 3b At 1.0 Angstrom Resolution In Absence" 97.54 119 99.16 99.16 4.34e-77 PDB 2O8O "Crystal Structure Of Clostridium Histolyticum Colg Collagenase Collagen-Binding Domain 3b At 1.35 Angstrom Resolution In Presen" 100.00 122 100.00 100.00 7.63e-81 PDB 4HPK "Crystal Structure Of Clostridium Histolyticum Colg Collagenase Collagen-binding Domain 3b At 1.35 Angstrom Resolution In Presen" 96.72 118 100.00 100.00 1.05e-77 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 Fri Feb 15 18:14:40 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA N 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 _Strain _Gene_mnemonic _Details $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 'Bacillus histolyticus' 1498 Eubacteria . Clostridium histolyticum BL21 'Clostridium Histolyticum' 'Monomeric CBD derived from the Clostridium histolyticum class I collagenase (ColG)' 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 $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 'recombinant technology' . Escherichia coli . pGEX-4T-2 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 $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 0.75 mM '[U-100% 13C; U-100% 15N]' $CA 20 mM 'natural abundance' TRIS 50 mM '[U-100% 2H]' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.3 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 0.75 mM '[U-99% 15N]' $CA 20 mM 'natural abundance' TRIS 50 mM '[U-100% 2H]' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.3 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Collagen_binding_domain_derived_from_Clostridium_Histolyticum 0.75 mM '[U-100% 13C]' $CA 20 mM 'natural abundance' TRIS 50 mM '[U-100% 2H]' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.3 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_3 save_ save_3D_1H-15N_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N 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' 100 1 mM pH 7.5 0.1 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 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_ _Software_label $xwinnmr $SPARKY stop_ loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HBHA(CO)NH' '3D 1H-15N NOESY' '3D H(CCO)NH' '3D HCCH-TOCSY' '3D 1H-15N TOCSY' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Collagen binding domain derived from Clostridium Histolyticum' _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 1 893 7 GLY H H 8.38 0.01 1 2 893 7 GLY C C 172.294 0.05 1 3 893 7 GLY CA C 42.45 0.05 1 4 893 7 GLY N N 109.22 0.1 1 5 894 8 ASN H H 8.18 0.01 1 6 894 8 ASN HA H 4.97 0.01 1 7 894 8 ASN HB2 H 2.63 0.01 2 8 894 8 ASN HB3 H 2.63 0.01 2 9 894 8 ASN C C 173.40 0.05 1 10 894 8 ASN CA C 50.38 0.05 1 11 894 8 ASN CB C 36.35 0.05 1 12 894 8 ASN N N 118.77 0.05 1 13 895 9 GLU H H 8.288 0.01 1 14 895 9 GLU CA C 53.897 0.05 1 15 895 9 GLU CB C 26.925 0.05 1 16 895 9 GLU N N 121.203 0.05 1 17 896 10 LYS HA H 4.90 0.01 1 18 896 10 LYS HB2 H 1.55 0.01 2 19 896 10 LYS HB3 H 1.55 0.01 2 20 896 10 LYS HD2 H 1.39 0.01 2 21 896 10 LYS HD3 H 1.39 0.01 2 22 896 10 LYS HE2 H 2.49 0.01 2 23 896 10 LYS HE3 H 2.49 0.01 2 24 896 10 LYS HG2 H 1.14 0.01 2 25 896 10 LYS HG3 H 1.14 0.01 2 26 896 10 LYS CA C 52.50 0.05 1 27 896 10 LYS CB C 31.45 0.05 1 28 896 10 LYS CD C 26.85 0.05 1 29 896 10 LYS CE C 39.43 0.05 1 30 896 10 LYS CG C 22.74 0.05 1 31 897 11 LEU H H 8.587 0.01 1 32 897 11 LEU HA H 4.599 0.01 1 33 897 11 LEU HB2 H 1.639 0.01 2 34 897 11 LEU HB3 H 1.475 0.01 2 35 897 11 LEU HG H 0.837 0.01 1 36 897 11 LEU C C 172.36 0.05 1 37 897 11 LEU CA C 50.97 0.05 1 38 897 11 LEU CB C 42.14 0.05 1 39 897 11 LEU N N 124.67 0.1 1 40 898 12 LYS H H 8.278 0.01 1 41 898 12 LYS HA H 4.905 0.01 1 42 898 12 LYS HB2 H 1.90 0.01 2 43 898 12 LYS HB3 H 1.90 0.01 2 44 898 12 LYS HD2 H 1.534 0.01 2 45 898 12 LYS HD3 H 1.534 0.01 2 46 898 12 LYS HG2 H 1.347 0.01 2 47 898 12 LYS HG3 H 1.347 0.01 2 48 898 12 LYS C C 173.900 0.05 1 49 898 12 LYS CA C 52.84 0.05 1 50 898 12 LYS CB C 31.883 0.05 1 51 898 12 LYS CD C 26.537 0.05 1 52 898 12 LYS CG C 22.562 0.05 1 53 898 12 LYS N N 121.7 0.1 1 54 899 13 GLU H H 7.834 0.01 1 55 899 13 GLU HA H 4.277 0.01 1 56 899 13 GLU HB2 H 2.729 0.01 2 57 899 13 GLU HB3 H 2.612 0.01 2 58 899 13 GLU HG2 H 1.94 0.01 2 59 899 13 GLU HG3 H 1.94 0.01 2 60 899 13 GLU C C 170.759 0.05 1 61 899 13 GLU CA C 53.848 0.05 1 62 899 13 GLU CB C 25.521 0.05 1 63 899 13 GLU CG C 31.092 0.05 1 64 899 13 GLU N N 117.6 0.1 1 65 900 14 LYS H H 7.325 0.01 1 66 900 14 LYS HA H 4.63 0.01 1 67 900 14 LYS HB2 H 1.658 0.01 2 68 900 14 LYS HB3 H 1.658 0.01 2 69 900 14 LYS HD2 H 1.543 0.01 2 70 900 14 LYS HD3 H 1.543 0.01 2 71 900 14 LYS HE2 H 2.605 0.01 2 72 900 14 LYS HE3 H 2.605 0.01 2 73 900 14 LYS HG2 H 1.303 0.01 2 74 900 14 LYS HG3 H 1.303 0.01 2 75 900 14 LYS C C 173.2 0.05 1 76 900 14 LYS CA C 51.84 0.05 1 77 900 14 LYS CB C 30.994 0.05 1 78 900 14 LYS CD C 26.402 0.05 1 79 900 14 LYS CE C 39.571 0.05 1 80 900 14 LYS CG C 21.734 0.05 1 81 900 14 LYS N N 121.502 0.1 1 82 901 15 GLU H H 8.494 0.01 1 83 901 15 GLU HA H 4.692 0.01 1 84 901 15 GLU HG2 H 1.633 0.01 2 85 901 15 GLU HG3 H 1.633 0.01 2 86 901 15 GLU C C 173.056 0.05 1 87 901 15 GLU CA C 51.204 0.05 1 88 901 15 GLU CB C 25.102 0.05 1 89 901 15 GLU N N 124.008 0.1 1 90 902 16 ASN H H 7.676 0.01 1 91 902 16 ASN HA H 5.099 0.01 1 92 902 16 ASN HB2 H 2.731 0.01 2 93 902 16 ASN HB3 H 2.647 0.01 2 94 902 16 ASN C C 171.864 0.05 1 95 902 16 ASN CA C 51.904 0.05 1 96 902 16 ASN CB C 38.002 0.05 1 97 902 16 ASN N N 122.0 0.1 1 98 903 17 ASN H H 7.773 0.01 1 99 903 17 ASN HA H 5.223 0.01 1 100 903 17 ASN HB2 H 2.831 0.01 2 101 903 17 ASN HB3 H 3.714 0.01 2 102 903 17 ASN C C 174.229 0.05 1 103 903 17 ASN CA C 48.725 0.05 1 104 903 17 ASN CB C 35.64 0.05 1 105 903 17 ASN N N 125.123 0.01 1 106 904 18 ASP H H 8.365 0.01 1 107 904 18 ASP HA H 4.383 0.01 1 108 904 18 ASP HB2 H 2.881 0.01 2 109 904 18 ASP HB3 H 2.881 0.01 2 110 904 18 ASP C C 171.411 0.05 1 111 904 18 ASP CA C 53.601 0.05 1 112 904 18 ASP CB C 37.084 0.05 1 113 904 18 ASP N N 117.44 0.1 1 114 905 19 SER H H 7.216 0.01 1 115 905 19 SER HA H 4.361 0.01 1 116 905 19 SER HB2 H 3.49 0.01 2 117 905 19 SER HB3 H 3.732 0.01 2 118 905 19 SER C C 172.350 0.05 1 119 905 19 SER CA C 53.451 0.05 1 120 905 19 SER CB C 62.63 0.05 1 121 905 19 SER N N 110.38 0.1 1 122 906 20 SER H H 8.037 0.01 1 123 906 20 SER HB2 H 2.397 0.01 2 124 906 20 SER HB3 H 2.397 0.01 2 125 906 20 SER C C 172.335 0.05 1 126 906 20 SER CA C 59.3 0.05 1 127 906 20 SER CB C 57.94 0.05 1 128 906 20 SER N N 117.96 0.1 1 129 907 21 ASP H H 8.256 0.01 1 130 907 21 ASP HA H 4.176 0.01 1 131 907 21 ASP HB2 H 2.454 0.01 2 132 907 21 ASP HB3 H 2.454 0.01 2 133 907 21 ASP C C 173.02 0.05 1 134 907 21 ASP CA C 52.384 0.05 1 135 907 21 ASP CB C 36.542 0.05 1 136 907 21 ASP N N 118.987 0.1 1 137 908 22 LYS H H 7.198 0.01 1 138 908 22 LYS HA H 4.414 0.01 1 139 908 22 LYS HB2 H 1.142 0.01 2 140 908 22 LYS HB3 H 1.142 0.01 2 141 908 22 LYS HD2 H 1.502 0.01 2 142 908 22 LYS HD3 H 1.502 0.01 2 143 908 22 LYS HE2 H 2.424 0.01 2 144 908 22 LYS HE3 H 2.424 0.01 2 145 908 22 LYS HG2 H 1.057 0.01 2 146 908 22 LYS HG3 H 1.057 0.01 2 147 908 22 LYS C C 172.068 0.05 1 148 908 22 LYS CA C 51.964 0.05 1 149 908 22 LYS CB C 29.902 0.05 1 150 908 22 LYS CD C 26.155 0.05 1 151 908 22 LYS CE C 39.603 0.05 1 152 908 22 LYS CG C 22.199 0.05 1 153 908 22 LYS N N 120.122 0.1 1 154 909 23 ALA H H 6.848 0.01 1 155 909 23 ALA HA H 3.85 0.01 1 156 909 23 ALA HB H 1.243 0.01 1 157 909 23 ALA C C 175.246 0.05 1 158 909 23 ALA CA C 49.934 0.05 1 159 909 23 ALA CB C 16.858 0.05 1 160 909 23 ALA N N 120.7 0.1 1 161 910 24 THR H H 9.152 0.01 1 162 910 24 THR HA H 4.399 0.01 1 163 910 24 THR HB H 3.98 0.01 1 164 910 24 THR HG2 H 1.333 0.01 1 165 910 24 THR C C 171.133 0.01 1 166 910 24 THR CA C 60.42 0.05 1 167 910 24 THR CB C 67.32 0.05 1 168 910 24 THR CG2 C 21.47 0.05 1 169 910 24 THR N N 121.1 0.1 1 170 911 25 VAL H H 8.735 0.01 1 171 911 25 VAL HA H 3.977 0.01 1 172 911 25 VAL HB H 1.852 0.01 1 173 911 25 VAL HG1 H 0.639 0.01 2 174 911 25 VAL HG2 H 0.883 0.01 2 175 911 25 VAL CA C 60.904 0.05 1 176 911 25 VAL CB C 29.984 0.05 1 177 911 25 VAL CG1 C 19.708 0.05 2 178 911 25 VAL CG2 C 19.708 0.05 2 179 911 25 VAL N N 130.6 0.1 1 180 912 26 ILE H H 9.070 0.01 1 181 912 26 ILE HA H 4.525 0.01 1 182 912 26 ILE HB H 2.037 0.01 1 183 912 26 ILE HG12 H 1.330 0.01 2 184 912 26 ILE HG13 H 1.330 0.01 2 185 912 26 ILE HG2 H 0.478 0.01 1 186 912 26 ILE CA C 56.252 0.05 1 187 912 26 ILE CB C 35.375 0.05 1 188 912 26 ILE N N 129 0.1 1 189 913 27 PRO HA H 4.705 0.01 1 190 913 27 PRO HB2 H 2.170 0.01 2 191 913 27 PRO HB3 H 1.854 0.01 2 192 913 27 PRO HD2 H 3.50 0.01 2 193 913 27 PRO HD3 H 3.50 0.01 2 194 913 27 PRO C C 173.026 0.05 1 195 913 27 PRO CA C 61.943 0.05 1 196 913 27 PRO CB C 29.901 0.05 1 197 913 27 PRO CD C 48.361 0.05 1 198 913 27 PRO CG C 24.637 0.05 1 199 914 28 ASN H H 6.893 0.01 1 200 914 28 ASN HA H 4.473 0.01 1 201 914 28 ASN HB2 H 2.186 0.01 2 202 914 28 ASN HB3 H 2.186 0.01 2 203 914 28 ASN C C 171.689 0.05 1 204 914 28 ASN CA C 49.013 0.05 1 205 914 28 ASN CB C 37.815 0.05 1 206 914 28 ASN N N 109.954 0.1 1 207 915 29 PHE H H 8.327 0.01 1 208 915 29 PHE HA H 4.742 0.01 1 209 915 29 PHE HB2 H 2.745 0.01 2 210 915 29 PHE HB3 H 2.745 0.01 2 211 915 29 PHE C C 173.007 0.05 1 212 915 29 PHE CA C 55.215 0.05 1 213 915 29 PHE CB C 35.987 0.05 1 214 915 29 PHE N N 116.861 0.1 1 215 916 30 ASN H H 9.003 0.01 1 216 916 30 ASN HA H 4.717 0.01 1 217 916 30 ASN HB2 H 2.636 0.01 2 218 916 30 ASN HB3 H 2.834 0.01 2 219 916 30 ASN C C 171.776 0.01 1 220 916 30 ASN CA C 51.022 0.05 1 221 916 30 ASN CB C 35.916 0.05 1 222 916 30 ASN N N 117.165 0.1 1 223 917 31 THR H H 7.708 0.01 1 224 917 31 THR HA H 4.508 0.01 1 225 917 31 THR HB H 3.633 0.01 1 226 917 31 THR HG2 H 1.026 0.01 1 227 917 31 THR C C 173.503 0.01 1 228 917 31 THR CA C 59.671 0.05 1 229 917 31 THR CB C 68.813 0.05 1 230 917 31 THR CG2 C 19.036 0.05 1 231 917 31 THR N N 114.664 0.1 1 232 918 32 THR H H 8.936 0.01 1 233 918 32 THR HA H 4.323 0.01 1 234 918 32 THR HB H 3.852 0.01 1 235 918 32 THR HG2 H 0.93 0.01 1 236 918 32 THR C C 171.976 0.01 1 237 918 32 THR CA C 60.237 0.05 1 238 918 32 THR CB C 67.259 0.05 1 239 918 32 THR CG2 C 19.241 0.05 1 240 918 32 THR N N 124.903 0.1 1 241 919 33 MET H H 9.226 0.01 1 242 919 33 MET HA H 5.304 0.01 1 243 919 33 MET HB2 H 1.763 0.01 2 244 919 33 MET HB3 H 1.763 0.01 2 245 919 33 MET HE H 1.365 0.01 1 246 919 33 MET HG2 H 2.33 0.01 2 247 919 33 MET HG3 H 2.33 0.01 2 248 919 33 MET C C 174.813 0.05 1 249 919 33 MET CA C 49.257 0.05 1 250 919 33 MET CB C 28.131 0.05 1 251 919 33 MET N N 124.97 0.1 1 252 920 34 GLN H H 9.007 0.01 1 253 920 34 GLN HA H 4.584 0.01 1 254 920 34 GLN HB2 H 2.133 0.01 2 255 920 34 GLN HB3 H 1.946 0.01 2 256 920 34 GLN C C 171.890 0.05 1 257 920 34 GLN CA C 52.333 0.05 1 258 920 34 GLN CB C 28.82 0.05 1 259 920 34 GLN CG C 31.893 0.05 1 260 920 34 GLN N N 122.56 0.1 1 261 921 35 GLY H H 7.628 0.01 1 262 921 35 GLY HA2 H 4.525 0.01 2 263 921 35 GLY HA3 H 4.525 0.01 2 264 921 35 GLY C C 168.300 0.05 1 265 921 35 GLY CA C 41.366 0.05 1 266 921 35 GLY N N 109.301 0.1 1 267 922 36 SER H H 8.854 0.01 1 268 922 36 SER HA H 4.805 0.01 1 269 922 36 SER HB2 H 3.463 0.01 2 270 922 36 SER HB3 H 3.831 0.01 2 271 922 36 SER C C 173.136 0.01 1 272 922 36 SER CA C 54.659 0.05 1 273 922 36 SER CB C 64.429 0.05 1 274 922 36 SER N N 112.501 0.1 1 275 923 37 LEU H H 8.918 0.01 1 276 923 37 LEU HA H 4.86 0.01 1 277 923 37 LEU HB2 H 1.655 0.01 2 278 923 37 LEU HB3 H 1.655 0.01 2 279 923 37 LEU HD1 H 0.45 0.01 2 280 923 37 LEU HD2 H 0.45 0.01 2 281 923 37 LEU HG H 0.689 0.01 1 282 923 37 LEU C C 173.612 0.05 1 283 923 37 LEU CA C 51.5 0.05 1 284 923 37 LEU CB C 41.309 0.05 1 285 923 37 LEU CD1 C 26.859 0.05 2 286 923 37 LEU CD2 C 25.919 0.05 2 287 923 37 LEU CG C 22.973 0.05 1 288 923 37 LEU N N 128.996 0.1 1 289 924 38 LEU H H 10.001 0.01 1 290 924 38 LEU HA H 4.699 0.01 1 291 924 38 LEU HB2 H 1.391 0.01 2 292 924 38 LEU HB3 H 1.391 0.01 2 293 924 38 LEU CA C 50.74 0.05 1 294 924 38 LEU CB C 39.022 0.05 1 295 924 38 LEU N N 127.39 0.1 1 296 926 40 ASP HA H 4.342 0.01 1 297 926 40 ASP HB2 H 2.726 0.01 2 298 926 40 ASP HB3 H 2.505 0.01 2 299 926 40 ASP C C 173.102 0.05 1 300 926 40 ASP CA C 52.247 0.05 1 301 926 40 ASP CB C 37.726 0.05 1 302 927 41 ASP H H 7.616 0.01 1 303 927 41 ASP HA H 4.791 0.01 1 304 927 41 ASP HB2 H 3.015 0.01 2 305 927 41 ASP HB3 H 2.429 0.01 2 306 927 41 ASP C C 170.202 0.05 1 307 927 41 ASP CA C 51.283 0.05 1 308 927 41 ASP CB C 37.854 0.05 1 309 927 41 ASP N N 121.945 0.1 1 310 928 42 SER H H 8.640 0.1 1 311 928 42 SER HA H 4.512 0.01 1 312 928 42 SER HB2 H 3.977 0.01 2 313 928 42 SER HB3 H 3.701 0.01 2 314 928 42 SER C C 171.990 0.05 1 315 928 42 SER CA C 55.548 0.05 1 316 928 42 SER CB C 62.64 0.05 1 317 928 42 SER N N 118.056 0.1 1 318 929 43 ARG H H 7.610 0.01 1 319 929 43 ARG HA H 5.021 0.01 1 320 929 43 ARG HB2 H 1.655 0.01 2 321 929 43 ARG HB3 H 1.502 0.01 2 322 929 43 ARG HD2 H 3.092 0.01 2 323 929 43 ARG HD3 H 3.092 0.01 2 324 929 43 ARG HG2 H 2.50 0.01 2 325 929 43 ARG HG3 H 2.50 0.01 2 326 929 43 ARG C C 171.995 0.05 1 327 929 43 ARG CA C 52.247 0.05 1 328 929 43 ARG CB C 31.354 0.05 1 329 929 43 ARG CD C 41.016 0.05 1 330 929 43 ARG CG C 24.213 0.05 1 331 929 43 ARG N N 118.995 0.1 1 332 930 44 ASP H H 9.658 0.01 1 333 930 44 ASP HA H 4.678 0.01 1 334 930 44 ASP HB2 H 2.773 0.01 2 335 930 44 ASP HB3 H 2.303 0.01 2 336 930 44 ASP C C 170.020 0.05 1 337 930 44 ASP CA C 50.149 0.05 1 338 930 44 ASP CB C 40.652 0.05 1 339 930 44 ASP N N 127.057 0.1 1 340 931 45 TYR H H 8.626 0.01 1 341 931 45 TYR HA H 5.141 0.01 1 342 931 45 TYR HB2 H 2.906 0.01 2 343 931 45 TYR HB3 H 2.379 0.01 2 344 931 45 TYR HD1 H 6.436 0.01 3 345 931 45 TYR HE1 H 6.798 0.01 3 346 931 45 TYR C C 173.156 0.05 1 347 931 45 TYR CA C 56.448 0.05 1 348 931 45 TYR CB C 36.748 0.05 1 349 931 45 TYR N N 120.936 0.1 1 350 932 46 TYR H H 9.422 0.1 1 351 932 46 TYR HA H 5.875 0.01 1 352 932 46 TYR HB2 H 3.091 0.01 2 353 932 46 TYR HB3 H 2.782 0.01 2 354 932 46 TYR HD1 H 6.786 0.01 3 355 932 46 TYR HE1 H 6.964 0.01 3 356 932 46 TYR C C 173.312 0.05 1 357 932 46 TYR CA C 53.629 0.05 1 358 932 46 TYR CB C 40.307 0.05 1 359 932 46 TYR N N 117.658 0.1 1 360 933 47 SER H H 8.861 0.01 1 361 933 47 SER HA H 5.638 0.01 1 362 933 47 SER HB2 H 3.41 0.01 2 363 933 47 SER HB3 H 3.309 0.01 2 364 933 47 SER C C 169.40 0.01 1 365 933 47 SER CA C 53.307 0.05 1 366 933 47 SER CB C 64.305 0.05 1 367 933 47 SER N N 115.586 0.1 1 368 934 48 PHE H H 8.241 0.1 1 369 934 48 PHE HA H 4.978 0.01 1 370 934 48 PHE HB2 H 3.062 0.01 2 371 934 48 PHE HB3 H 2.892 0.01 2 372 934 48 PHE HD1 H 6.486 0.01 3 373 934 48 PHE HE1 H 6.751 0.01 3 374 934 48 PHE C C 169.481 0.05 1 375 934 48 PHE CA C 53.636 0.05 1 376 934 48 PHE CB C 38.722 0.05 1 377 934 48 PHE N N 114.245 0.1 1 378 935 49 GLU H H 8.293 0.01 1 379 935 49 GLU HA H 5.034 0.01 1 380 935 49 GLU HB2 H 1.719 0.01 2 381 935 49 GLU HB3 H 1.719 0.01 2 382 935 49 GLU HG2 H 1.974 0.01 2 383 935 49 GLU HG3 H 1.974 0.01 2 384 935 49 GLU C C 172.711 0.05 1 385 935 49 GLU CA C 51.797 0.05 1 386 935 49 GLU CB C 30.229 0.05 1 387 935 49 GLU CG C 33.830 0.05 1 388 935 49 GLU N N 119.015 0.1 1 389 936 50 VAL H H 9.092 0.01 1 390 936 50 VAL HA H 4.663 0.01 1 391 936 50 VAL HB H 2.236 0.01 1 392 936 50 VAL HG1 H 1.321 0.01 2 393 936 50 VAL HG2 H 1.081 0.01 2 394 936 50 VAL CA C 59.139 0.05 1 395 936 50 VAL CB C 31.268 0.05 1 396 936 50 VAL N N 123.894 0.1 1 397 937 51 LYS HA H 4.368 0.01 1 398 937 51 LYS HB2 H 1.793 0.01 2 399 937 51 LYS HB3 H 1.793 0.01 2 400 937 51 LYS HD2 H 1.541 0.01 2 401 937 51 LYS HD3 H 1.541 0.01 2 402 937 51 LYS HE2 H 2.847 0.01 2 403 937 51 LYS HE3 H 2.847 0.01 2 404 937 51 LYS HG2 H 1.309 0.01 2 405 937 51 LYS HG3 H 1.309 0.01 2 406 937 51 LYS CA C 54.099 0.05 1 407 937 51 LYS CB C 30.737 0.05 1 408 937 51 LYS CD C 25.784 0.05 1 409 937 51 LYS CG C 22.145 0.05 1 410 938 52 GLU H H 7.462 0.01 1 411 938 52 GLU HA H 4.435 0.01 1 412 938 52 GLU HB2 H 1.849 0.01 2 413 938 52 GLU HB3 H 1.697 0.01 2 414 938 52 GLU C C 171.764 0.05 1 415 938 52 GLU CA C 51.83 0.05 1 416 938 52 GLU CB C 29.692 0.05 1 417 938 52 GLU CG C 32.918 0.05 1 418 938 52 GLU N N 117.946 0.1 1 419 939 53 GLU H H 8.807 0.01 1 420 939 53 GLU HA H 4.504 0.01 1 421 939 53 GLU HB2 H 1.918 0.01 2 422 939 53 GLU HB3 H 1.918 0.01 2 423 939 53 GLU HG2 H 1.954 0.01 2 424 939 53 GLU HG3 H 1.954 0.01 2 425 939 53 GLU C C 173.641 0.05 1 426 939 53 GLU CA C 53.297 0.05 1 427 939 53 GLU CB C 27.671 0.05 1 428 939 53 GLU CG C 33.024 0.05 1 429 939 53 GLU N N 123.812 0.1 1 430 940 54 GLY H H 7.993 0.01 1 431 940 54 GLY HA2 H 4.067 0.01 2 432 940 54 GLY HA3 H 3.897 0.01 2 433 940 54 GLY C C 168.641 0.05 1 434 940 54 GLY CA C 42.323 0.01 1 435 940 54 GLY N N 110.65 0.1 1 436 941 55 GLU H H 8.547 0.01 1 437 941 55 GLU HA H 4.464 0.01 1 438 941 55 GLU HB2 H 1.675 0.01 2 439 941 55 GLU HB3 H 1.675 0.01 2 440 941 55 GLU HG2 H 1.784 0.01 2 441 941 55 GLU HG3 H 1.784 0.01 2 442 941 55 GLU C C 173.171 0.05 1 443 941 55 GLU CA C 53.779 0.05 1 444 941 55 GLU CB C 28.68 0.05 1 445 941 55 GLU CG C 35.057 0.05 1 446 941 55 GLU N N 120.733 0.1 1 447 942 56 VAL H H 8.755 0.01 1 448 942 56 VAL HA H 4.446 0.01 1 449 942 56 VAL HB H 1.626 0.01 1 450 942 56 VAL HG1 H 0.547 0.01 2 451 942 56 VAL HG2 H 0.360 0.01 2 452 942 56 VAL C C 170.838 0.05 1 453 942 56 VAL CA C 57.384 0.05 1 454 942 56 VAL CB C 31.549 0.05 1 455 942 56 VAL CG1 C 18.150 0.05 2 456 942 56 VAL CG2 C 17.780 0.05 2 457 942 56 VAL N N 122.893 0.05 1 458 943 57 ASN H H 8.745 0.01 1 459 943 57 ASN HA H 5.028 0.01 1 460 943 57 ASN HB2 H 2.550 0.01 2 461 943 57 ASN HB3 H 2.389 0.01 2 462 943 57 ASN C C 171.218 0.05 1 463 943 57 ASN CA C 49.352 0.05 1 464 943 57 ASN CB C 38.558 0.05 1 465 943 57 ASN N N 122.909 0.1 1 466 944 58 ILE H H 8.467 0.01 1 467 944 58 ILE HA H 4.093 0.01 1 468 944 58 ILE HB H 1.28 0.01 1 469 944 58 ILE HG2 H 0.299 0.01 1 470 944 58 ILE C C 171.219 0.05 1 471 944 58 ILE CA C 58.486 0.05 1 472 944 58 ILE CB C 35.898 0.05 1 473 944 58 ILE CD1 C 12.111 0.05 1 474 944 58 ILE CG2 C 14.13 0.05 1 475 944 58 ILE N N 126.083 0.1 1 476 945 59 GLU H H 8.460 0.01 1 477 945 59 GLU HA H 4.655 0.01 1 478 945 59 GLU HB2 H 1.697 0.01 2 479 945 59 GLU HB3 H 1.697 0.01 2 480 945 59 GLU HG2 H 1.944 0.01 2 481 945 59 GLU HG3 H 1.944 0.01 2 482 945 59 GLU C C 170.314 0.05 1 483 945 59 GLU CA C 52.556 0.05 1 484 945 59 GLU CB C 31.183 0.05 1 485 945 59 GLU CG C 33.883 0.05 1 486 945 59 GLU N N 124.77 0.01 1 487 946 60 LEU H H 8.571 0.01 1 488 946 60 LEU HA H 5.185 0.01 1 489 946 60 LEU HB2 H 1.293 0.01 2 490 946 60 LEU HB3 H 1.293 0.01 2 491 946 60 LEU HD1 H 0.552 0.01 2 492 946 60 LEU HD2 H 0.379 0.01 2 493 946 60 LEU HG H 2.116 0.01 1 494 946 60 LEU C C 171.369 0.05 1 495 946 60 LEU CA C 50.874 0.05 1 496 946 60 LEU CB C 42.144 0.05 1 497 946 60 LEU CD1 C 23.495 0.05 2 498 946 60 LEU CD2 C 23.495 0.05 2 499 946 60 LEU CG C 27.199 0.05 1 500 946 60 LEU N N 129.087 0.1 1 501 947 61 ASP H H 9.458 0.01 1 502 947 61 ASP HA H 4.183 0.01 1 503 947 61 ASP HB2 H 2.559 0.01 2 504 947 61 ASP HB3 H 2.369 0.01 2 505 947 61 ASP C C 170.491 0.05 1 506 947 61 ASP CA C 50.34 0.05 1 507 947 61 ASP CB C 40.756 0.05 1 508 947 61 ASP N N 127.634 0.1 1 509 948 62 LYS H H 8.833 0.01 1 510 948 62 LYS HA H 4.199 0.01 1 511 948 62 LYS HB2 H 1.921 0.01 2 512 948 62 LYS HB3 H 1.921 0.01 2 513 948 62 LYS HD2 H 2.160 0.01 2 514 948 62 LYS HD3 H 2.160 0.01 2 515 948 62 LYS HE2 H 2.656 0.01 2 516 948 62 LYS HE3 H 2.656 0.01 2 517 948 62 LYS HG2 H 1.521 0.01 2 518 948 62 LYS HG3 H 1.521 0.01 2 519 948 62 LYS C C 173.940 0.05 1 520 948 62 LYS CA C 54.908 0.01 1 521 948 62 LYS CB C 33.507 0.01 1 522 948 62 LYS CD C 29.253 0.05 1 523 948 62 LYS CE C 39.090 0.05 1 524 948 62 LYS CG C 27.867 0.05 1 525 948 62 LYS N N 124.7 0.1 1 526 949 63 LYS H H 8.285 0.01 1 527 949 63 LYS HA H 4.306 0.01 1 528 949 63 LYS HB2 H 1.895 0.01 2 529 949 63 LYS HB3 H 1.360 0.01 2 530 949 63 LYS HD2 H 1.554 0.01 2 531 949 63 LYS HD3 H 1.554 0.01 2 532 949 63 LYS HE2 H 2.512 0.01 2 533 949 63 LYS HE3 H 2.512 0.01 2 534 949 63 LYS HG2 H 1.184 0.01 2 535 949 63 LYS HG3 H 1.184 0.01 2 536 949 63 LYS C C 172.088 0.05 1 537 949 63 LYS CA C 51.971 0.05 1 538 949 63 LYS CB C 28.256 0.05 1 539 949 63 LYS CD C 24.390 0.05 1 540 949 63 LYS CE C 38.949 0.05 1 541 949 63 LYS CG C 20.974 0.05 1 542 949 63 LYS N N 122.522 0.1 1 543 950 64 ASP H H 7.556 0.01 1 544 950 64 ASP HA H 4.797 0.01 1 545 950 64 ASP HB2 H 2.932 0.01 2 546 950 64 ASP HB3 H 2.692 0.01 2 547 950 64 ASP C C 171.566 0.05 1 548 950 64 ASP CA C 49.671 0.01 1 549 950 64 ASP CB C 44.14 0.01 1 550 950 64 ASP N N 115.758 0.1 1 551 951 65 GLU H H 8.726 0.01 1 552 951 65 GLU HA H 4.482 0.01 1 553 951 65 GLU HB2 H 1.903 0.01 2 554 951 65 GLU HB3 H 1.903 0.01 2 555 951 65 GLU HG2 H 2.199 0.01 2 556 951 65 GLU HG3 H 2.199 0.01 2 557 951 65 GLU C C 172.088 0.05 1 558 951 65 GLU CA C 53.646 0.05 1 559 951 65 GLU CB C 25.764 0.05 1 560 951 65 GLU CG C 32.232 0.05 1 561 951 65 GLU N N 119.744 0.01 1 562 952 66 PHE H H 7.531 0.01 1 563 952 66 PHE HA H 4.652 0.01 1 564 952 66 PHE HB2 H 3.313 0.01 2 565 952 66 PHE HB3 H 3.313 0.01 2 566 952 66 PHE HD1 H 7.028 0.01 3 567 952 66 PHE C C 175.954 0.05 1 568 952 66 PHE CA C 52.217 0.05 1 569 952 66 PHE CB C 34.983 0.05 1 570 952 66 PHE N N 125.105 0.1 1 571 953 67 GLY H H 7.770 0.01 1 572 953 67 GLY HA2 H 3.617 0.01 2 573 953 67 GLY HA3 H 3.617 0.01 2 574 953 67 GLY C C 167.926 0.05 1 575 953 67 GLY CA C 43.45 0.05 1 576 953 67 GLY N N 109.048 0.1 1 577 954 68 VAL H H 7.061 0.01 1 578 954 68 VAL HA H 4.459 0.01 1 579 954 68 VAL HB H 0.631 0.01 1 580 954 68 VAL HG1 H 0.229 0.01 2 581 954 68 VAL C C 169.061 0.05 1 582 954 68 VAL CA C 55.059 0.05 1 583 954 68 VAL CB C 30.001 0.05 1 584 954 68 VAL CG1 C 19.689 0.05 2 585 954 68 VAL CG2 C 16.538 0.05 2 586 954 68 VAL N N 123.678 0.1 1 587 955 69 THR H H 8.197 0.01 1 588 955 69 THR HA H 4.247 0.01 1 589 955 69 THR HB H 3.904 0.01 1 590 955 69 THR HG2 H 0.555 0.01 1 591 955 69 THR C C 167.278 0.05 1 592 955 69 THR CA C 56.037 0.05 1 593 955 69 THR CB C 65.739 0.05 1 594 955 69 THR CG2 C 16.229 0.05 1 595 955 69 THR N N 120.961 0.1 1 596 956 70 TRP H H 7.943 0.01 1 597 956 70 TRP HA H 6.196 0.01 1 598 956 70 TRP HB2 H 2.883 0.01 2 599 956 70 TRP HB3 H 3.150 0.01 2 600 956 70 TRP HD1 H 6.527 0.01 1 601 956 70 TRP HE3 H 6.828 0.01 1 602 956 70 TRP C C 172.769 0.05 1 603 956 70 TRP CA C 51.262 0.05 1 604 956 70 TRP CB C 30.862 0.05 1 605 956 70 TRP N N 114.326 0.1 1 606 957 71 THR H H 9.360 0.01 1 607 957 71 THR CA C 58.84 0.05 1 608 957 71 THR CB C 68.694 0.05 1 609 957 71 THR N N 110.865 0.01 1 610 958 72 LEU HA H 5.530 0.01 1 611 958 72 LEU HB2 H 1.683 0.01 2 612 958 72 LEU HB3 H 1.263 0.01 2 613 958 72 LEU HD1 H 0.927 0.01 2 614 958 72 LEU HD2 H 0.642 0.01 2 615 958 72 LEU HG H 1.558 0.01 1 616 958 72 LEU C C 171.806 0.05 1 617 958 72 LEU CA C 50.582 0.05 1 618 958 72 LEU CB C 44.420 0.05 1 619 958 72 LEU CD1 C 22.453 0.05 2 620 958 72 LEU CD2 C 22.453 0.05 2 621 958 72 LEU CG C 25.097 0.05 1 622 959 73 HIS H H 9.560 0.01 1 623 959 73 HIS CA C 50.850 0.05 1 624 959 73 HIS CB C 29.390 0.05 1 625 959 73 HIS N N 126.087 0.1 1 626 960 74 PRO HA H 4.644 0.01 1 627 960 74 PRO HB2 H 2.299 0.01 2 628 960 74 PRO HB3 H 2.137 0.01 2 629 960 74 PRO C C 173.780 0.05 1 630 960 74 PRO CA C 59.646 0.05 1 631 960 74 PRO CB C 28.856 0.05 1 632 960 74 PRO CD C 47.556 0.05 1 633 961 75 GLU H H 7.474 0.01 1 634 961 75 GLU HA H 3.826 0.01 1 635 961 75 GLU HB2 H 1.63 0.01 2 636 961 75 GLU HB3 H 1.63 0.01 2 637 961 75 GLU HG2 H 2.083 0.01 2 638 961 75 GLU HG3 H 1.990 0.01 2 639 961 75 GLU C C 172.711 0.01 1 640 961 75 GLU CA C 55.869 0.01 1 641 961 75 GLU CB C 26.416 0.01 1 642 961 75 GLU CG C 32.251 0.01 1 643 961 75 GLU N N 119.233 0.1 1 644 962 76 SER H H 7.904 0.01 1 645 962 76 SER HA H 3.988 0.01 1 646 962 76 SER HB2 H 3.796 0.01 2 647 962 76 SER HB3 H 3.796 0.01 2 648 962 76 SER C C 172.344 0.05 1 649 962 76 SER CA C 56.815 0.05 1 650 962 76 SER CB C 60.412 0.05 1 651 962 76 SER N N 109.19 0.1 1 652 963 77 ASN H H 7.026 0.01 1 653 963 77 ASN HA H 4.587 0.01 1 654 963 77 ASN HB2 H 2.895 0.01 2 655 963 77 ASN HB3 H 2.895 0.01 2 656 963 77 ASN C C 171.905 0.05 1 657 963 77 ASN CA C 50.711 0.05 1 658 963 77 ASN CB C 35.529 0.05 1 659 963 77 ASN N N 116.977 0.1 1 660 964 78 ILE H H 8.474 0.01 1 661 964 78 ILE HA H 4.078 0.01 1 662 964 78 ILE HB H 1.687 0.01 1 663 964 78 ILE HD1 H 0.429 0.01 1 664 964 78 ILE HG12 H 0.641 0.01 2 665 964 78 ILE HG13 H 0.641 0.01 2 666 964 78 ILE C C 172.288 0.05 1 667 964 78 ILE CA C 59.417 0.05 1 668 964 78 ILE CB C 35.687 0.05 1 669 964 78 ILE CD1 C 15.276 0.05 1 670 964 78 ILE CG1 C 25.165 0.05 1 671 964 78 ILE CG2 C 17.028 0.05 1 672 964 78 ILE N N 123.121 0.1 1 673 965 79 ASN H H 7.806 0.01 1 674 965 79 ASN HA H 4.469 0.01 1 675 965 79 ASN HB2 H 2.649 0.01 2 676 965 79 ASN HB3 H 2.649 0.01 2 677 965 79 ASN C C 173.432 0.05 1 678 965 79 ASN CA C 51.321 0.05 1 679 965 79 ASN CB C 36.145 0.05 1 680 965 79 ASN N N 115.452 0.1 1 681 966 80 ASP H H 7.854 0.01 1 682 966 80 ASP CA C 51.445 0.05 1 683 966 80 ASP CB C 38.78 0.05 1 684 966 80 ASP N N 122.416 0.1 1 685 968 82 ILE HA H 3.640 0.01 1 686 968 82 ILE C C 170.276 0.05 1 687 968 82 ILE CB C 34.659 0.05 1 688 968 82 ILE CD1 C 12.752 0.05 1 689 968 82 ILE CG2 C 17.405 0.05 1 690 969 83 THR H H 7.966 0.01 1 691 969 83 THR CA C 53.394 0.05 1 692 969 83 THR CB C 60.861 0.05 1 693 969 83 THR N N 115.607 0.1 1 694 970 84 TYR HA H 5.357 0.01 1 695 970 84 TYR C C 170.601 0.05 1 696 970 84 TYR CB C 38.476 0.05 1 697 971 85 GLY H H 6.656 0.01 1 698 971 85 GLY C C 168.541 0.05 1 699 971 85 GLY CA C 42.902 0.05 1 700 971 85 GLY N N 104.154 0.1 1 701 972 86 GLN H H 7.930 0.01 1 702 972 86 GLN HA H 4.499 0.01 1 703 972 86 GLN HB2 H 1.999 0.01 2 704 972 86 GLN HB3 H 1.999 0.01 2 705 972 86 GLN HG2 H 2.132 0.01 2 706 972 86 GLN HG3 H 2.132 0.01 2 707 972 86 GLN C C 172.887 0.05 1 708 972 86 GLN CA C 51.549 0.05 1 709 972 86 GLN CB C 27.286 0.05 1 710 972 86 GLN CG C 30.865 0.05 1 711 972 86 GLN N N 122.323 0.1 1 712 973 87 VAL H H 8.717 0.01 1 713 973 87 VAL HA H 4.091 0.01 1 714 973 87 VAL HB H 1.943 0.01 1 715 973 87 VAL HG1 H 0.939 0.01 2 716 973 87 VAL HG2 H 0.939 0.01 2 717 973 87 VAL C C 169.457 0.05 1 718 973 87 VAL CA C 60.998 0.05 1 719 973 87 VAL CB C 29.558 0.05 1 720 973 87 VAL CG1 C 19.050 0.05 2 721 973 87 VAL CG2 C 19.050 0.05 2 722 973 87 VAL N N 126.67 0.1 1 723 974 88 ASP H H 8.885 0.01 1 724 974 88 ASP HA H 4.697 0.01 1 725 974 88 ASP HB2 H 2.365 0.01 2 726 974 88 ASP HB3 H 2.365 0.01 2 727 974 88 ASP C C 173.480 0.05 1 728 974 88 ASP CA C 50.697 0.05 1 729 974 88 ASP CB C 38.853 0.05 1 730 974 88 ASP N N 129.326 0.1 1 731 975 89 GLY H H 8.851 0.01 1 732 975 89 GLY C C 170.970 0.05 1 733 975 89 GLY CA C 44.616 0.01 1 734 975 89 GLY N N 115.484 0.1 1 735 976 90 ASN H H 8.745 0.01 1 736 976 90 ASN HA H 4.695 0.01 1 737 976 90 ASN HB2 H 2.874 0.01 2 738 976 90 ASN HB3 H 2.663 0.01 2 739 976 90 ASN C C 170.359 0.05 1 740 976 90 ASN CA C 50.861 0.05 1 741 976 90 ASN CB C 35.866 0.05 1 742 976 90 ASN N N 125.32 0.1 1 743 977 91 LYS H H 7.828 0.01 1 744 977 91 LYS HA H 5.139 0.01 1 745 977 91 LYS HB2 H 1.888 0.01 2 746 977 91 LYS HB3 H 1.675 0.01 2 747 977 91 LYS HG2 H 1.38 0.01 2 748 977 91 LYS HG3 H 1.38 0.01 2 749 977 91 LYS C C 173.232 0.05 1 750 977 91 LYS CA C 51.734 0.05 1 751 977 91 LYS CB C 32.731 0.05 1 752 977 91 LYS CD C 26.252 0.05 1 753 977 91 LYS CE C 43.542 0.05 1 754 977 91 LYS CG C 22.134 0.05 1 755 977 91 LYS N N 119.275 0.1 1 756 978 92 VAL H H 9.369 0.01 1 757 978 92 VAL HA H 4.728 0.01 1 758 978 92 VAL HB H 2.164 0.01 1 759 978 92 VAL HG1 H 0.854 0.01 2 760 978 92 VAL HG2 H 0.598 0.01 2 761 978 92 VAL C C 175.649 0.05 1 762 978 92 VAL CA C 58.944 0.05 1 763 978 92 VAL CB C 30.26 0.05 1 764 978 92 VAL CG1 C 19.196 0.05 2 765 978 92 VAL CG2 C 19.196 0.05 2 766 978 92 VAL N N 123.247 0.1 1 767 979 93 SER H H 9.154 0.01 1 768 979 93 SER HA H 6.443 0.01 1 769 979 93 SER HB2 H 3.991 0.01 2 770 979 93 SER HB3 H 3.795 0.01 2 771 979 93 SER C C 171.806 0.05 1 772 979 93 SER CA C 55.15 0.05 1 773 979 93 SER CB C 65.698 0.05 1 774 979 93 SER N N 124.416 0.1 1 775 980 94 ASN H H 8.940 0.01 1 776 980 94 ASN HA H 4.698 0.01 1 777 980 94 ASN HB2 H 3.106 0.01 2 778 980 94 ASN HB3 H 2.359 0.01 2 779 980 94 ASN C C 170.327 0.05 1 780 980 94 ASN CA C 50.53 0.05 1 781 980 94 ASN CB C 39.05 0.05 1 782 980 94 ASN N N 117.556 0.05 1 783 981 95 LYS H H 8.451 0.01 1 784 981 95 LYS HA H 5.375 0.01 1 785 981 95 LYS HB2 H 1.55 0.01 2 786 981 95 LYS HB3 H 1.55 0.01 2 787 981 95 LYS HG2 H 1.152 0.01 2 788 981 95 LYS HG3 H 1.152 0.01 2 789 981 95 LYS C C 172.602 0.05 1 790 981 95 LYS CA C 52.16 0.05 1 791 981 95 LYS CB C 32.65 0.05 1 792 981 95 LYS CD C 26.665 0.05 1 793 981 95 LYS CE C 39.275 0.05 1 794 981 95 LYS CG C 21.936 0.05 1 795 981 95 LYS N N 119.183 0.01 1 796 982 96 VAL H H 8.681 0.01 1 797 982 96 VAL HA H 4.424 0.01 1 798 982 96 VAL HB H 1.876 0.01 1 799 982 96 VAL HG1 H 0.719 0.01 2 800 982 96 VAL HG2 H 0.575 0.01 2 801 982 96 VAL C C 169.302 0.01 1 802 982 96 VAL CA C 56.899 0.05 1 803 982 96 VAL CB C 32.37 0.05 1 804 982 96 VAL CG1 C 18.173 0.05 2 805 982 96 VAL CG2 C 15.950 0.05 2 806 982 96 VAL N N 121.046 0.01 1 807 983 97 LYS H H 8.488 0.01 1 808 983 97 LYS HA H 4.308 0.01 1 809 983 97 LYS HB2 H 1.673 0.01 2 810 983 97 LYS HB3 H 1.524 0.01 2 811 983 97 LYS HE2 H 2.738 0.01 2 812 983 97 LYS HE3 H 2.738 0.01 2 813 983 97 LYS HG2 H 1.014 0.01 2 814 983 97 LYS HG3 H 1.014 0.01 2 815 983 97 LYS C C 172.247 0.05 1 816 983 97 LYS CA C 53.51 0.05 1 817 983 97 LYS CB C 29.33 0.05 1 818 983 97 LYS CD C 26.462 0.05 1 819 983 97 LYS CE C 38.979 0.05 1 820 983 97 LYS CG C 22.628 0.05 1 821 983 97 LYS N N 128.123 0.1 1 822 984 98 LEU H H 8.116 0.01 1 823 984 98 LEU HA H 4.707 0.01 1 824 984 98 LEU HB2 H 1.358 0.01 2 825 984 98 LEU HB3 H 1.138 0.01 2 826 984 98 LEU HD1 H 0.0952 0.01 2 827 984 98 LEU HD2 H 0.0952 0.01 2 828 984 98 LEU HG H 0.3722 0.01 1 829 984 98 LEU C C 172.947 0.05 1 830 984 98 LEU CA C 50.31 0.05 1 831 984 98 LEU CB C 42.05 0.05 1 832 984 98 LEU CD1 C 20.081 0.05 2 833 984 98 LEU CD2 C 20.081 0.05 2 834 984 98 LEU CG C 22.684 0.05 1 835 984 98 LEU N N 126.294 0.1 1 836 985 99 ARG H H 7.872 0.01 1 837 985 99 ARG C C 171.623 0.05 1 838 985 99 ARG CA C 51.51 0.01 1 839 985 99 ARG CB C 26.08 0.01 1 840 985 99 ARG N N 118.403 0.1 1 841 986 100 PRO HA H 4.043 0.01 1 842 986 100 PRO HB2 H 2.036 0.01 2 843 986 100 PRO HB3 H 1.762 0.01 2 844 986 100 PRO C C 172.905 0.05 1 845 986 100 PRO CA C 61.31 0.05 1 846 986 100 PRO CB C 29.084 0.05 1 847 986 100 PRO CD C 47.579 0.05 1 848 986 100 PRO CG C 25.294 0.05 1 849 987 101 GLY H H 8.535 0.01 1 850 987 101 GLY HA2 H 4.043 0.01 2 851 987 101 GLY HA3 H 3.702 0.01 2 852 987 101 GLY C C 172.714 0.05 1 853 987 101 GLY CA C 41.579 0.05 1 854 987 101 GLY N N 110.632 0.1 1 855 988 102 LYS H H 8.001 0.01 1 856 988 102 LYS HA H 4.661 0.01 1 857 988 102 LYS HB2 H 1.305 0.01 2 858 988 102 LYS HB3 H 1.305 0.01 2 859 988 102 LYS HD2 H 0.947 0.01 2 860 988 102 LYS HD3 H 0.947 0.01 2 861 988 102 LYS HE2 H 2.302 0.01 2 862 988 102 LYS HE3 H 2.302 0.01 2 863 988 102 LYS HG2 H 0.543 0.01 2 864 988 102 LYS HG3 H 0.543 0.01 2 865 988 102 LYS C C 171.581 0.05 1 866 988 102 LYS CA C 52.32 0.05 1 867 988 102 LYS CB C 30.95 0.05 1 868 988 102 LYS CD C 26.656 0.05 1 869 988 102 LYS CE C 39.188 0.05 1 870 988 102 LYS CG C 22.639 0.05 1 871 988 102 LYS N N 120.133 0.1 1 872 989 103 TYR H H 8.275 0.01 1 873 989 103 TYR HA H 4.476 0.01 1 874 989 103 TYR HB2 H 2.325 0.01 2 875 989 103 TYR HD1 H 6.584 0.01 3 876 989 103 TYR HE1 H 6.817 0.01 3 877 989 103 TYR C C 170.770 0.05 1 878 989 103 TYR CA C 54.37 0.05 1 879 989 103 TYR CB C 39.79 0.05 1 880 989 103 TYR N N 122.5 0.1 1 881 990 104 TYR H H 9.180 0.01 1 882 990 104 TYR HA H 5.385 0.01 1 883 990 104 TYR HB2 H 2.928 0.01 2 884 990 104 TYR HB3 H 2.637 0.01 2 885 990 104 TYR C C 171.386 0.05 1 886 990 104 TYR CA C 54.12 0.05 1 887 990 104 TYR CB C 39.023 0.05 1 888 990 104 TYR N N 116.25 0.1 1 889 991 105 LEU H H 9.463 0.01 1 890 991 105 LEU HA H 5.275 0.01 1 891 991 105 LEU HB2 H 1.669 0.01 2 892 991 105 LEU HB3 H 1.267 0.01 2 893 991 105 LEU C C 171.269 0.05 1 894 991 105 LEU CA C 50.37 0.05 1 895 991 105 LEU CB C 43.49 0.05 1 896 991 105 LEU CD1 C 23.315 0.05 2 897 991 105 LEU CD2 C 23.315 0.05 2 898 991 105 LEU CG C 24.472 0.05 1 899 991 105 LEU N N 126.8 0.1 1 900 992 106 LEU H H 9.375 0.01 1 901 992 106 LEU HA H 4.409 0.01 1 902 992 106 LEU HB2 H 2.279 0.01 2 903 992 106 LEU HB3 H 2.279 0.01 2 904 992 106 LEU HD2 H 0.46 0.01 2 905 992 106 LEU HG H 1.311 0.01 1 906 992 106 LEU C C 171.932 0.05 1 907 992 106 LEU CA C 51.03 0.05 1 908 992 106 LEU CB C 39.02 0.05 1 909 992 106 LEU CD1 C 22.653 0.05 2 910 992 106 LEU CD2 C 22.653 0.05 2 911 992 106 LEU CG C 24.341 0.05 1 912 992 106 LEU N N 128.5 0.01 1 913 993 107 VAL H H 8.750 0.01 1 914 993 107 VAL HA H 4.543 0.01 1 915 993 107 VAL HB H 2.21 0.01 1 916 993 107 VAL HG1 H 0.757 0.01 2 917 993 107 VAL HG2 H 0.095 0.01 2 918 993 107 VAL C C 171.806 0.05 1 919 993 107 VAL CA C 58.875 0.05 1 920 993 107 VAL CB C 29.565 0.05 1 921 993 107 VAL CG1 C 19.043 0.05 2 922 993 107 VAL CG2 C 19.053 0.05 2 923 993 107 VAL N N 128.173 0.1 1 924 994 108 TYR H H 8.581 0.01 1 925 994 108 TYR HA H 5.516 0.01 1 926 994 108 TYR HB2 H 3.130 0.01 2 927 994 108 TYR HB3 H 2.524 0.01 2 928 994 108 TYR C C 169.228 0.05 1 929 994 108 TYR CA C 52.501 0.05 1 930 994 108 TYR CB C 38.438 0.05 1 931 994 108 TYR N N 123.406 0.1 1 932 995 109 LYS H H 8.026 0.01 1 933 995 109 LYS HA H 5.263 0.01 1 934 995 109 LYS HB2 H 1.920 0.01 2 935 995 109 LYS HB3 H 1.665 0.01 2 936 995 109 LYS HG2 H 1.332 0.01 2 937 995 109 LYS HG3 H 1.332 0.01 2 938 995 109 LYS C C 172.234 0.05 1 939 995 109 LYS CA C 49.91 0.05 1 940 995 109 LYS CB C 33.82 0.05 1 941 995 109 LYS CD C 27.091 0.05 1 942 995 109 LYS CG C 20.944 0.05 1 943 995 109 LYS N N 115.629 0.1 1 944 996 110 TYR H H 8.195 0.01 1 945 996 110 TYR HA H 4.878 0.01 1 946 996 110 TYR HB2 H 3.256 0.01 2 947 996 110 TYR HB3 H 2.626 0.01 2 948 996 110 TYR C C 172.777 0.05 1 949 996 110 TYR CA C 52.834 0.05 1 950 996 110 TYR CB C 36.995 0.05 1 951 996 110 TYR N N 116.424 0.1 1 952 997 111 SER H H 7.337 0.01 1 953 997 111 SER HA H 4.51 0.01 1 954 997 111 SER HB2 H 3.856 0.01 2 955 997 111 SER HB3 H 3.856 0.01 2 956 997 111 SER C C 171.294 0.05 1 957 997 111 SER CA C 56.11 0.05 1 958 997 111 SER CB C 61.77 0.05 1 959 997 111 SER N N 116.664 0.1 1 960 998 112 GLY H H 8.667 0.01 1 961 998 112 GLY HA2 H 4.209 0.01 2 962 998 112 GLY HA3 H 3.81 0.01 2 963 998 112 GLY C C 170.280 0.05 1 964 998 112 GLY CA C 43.26 0.05 1 965 998 112 GLY N N 109.961 0.1 1 966 999 113 SER H H 7.907 0.01 1 967 999 113 SER HA H 4.257 0.01 1 968 999 113 SER HB2 H 3.711 0.01 2 969 999 113 SER HB3 H 3.553 0.01 2 970 999 113 SER C C 167.888 0.05 1 971 999 113 SER CA C 56.26 0.05 1 972 999 113 SER CB C 65.838 0.05 1 973 999 113 SER N N 115.066 0.1 1 974 1000 114 GLY H H 5.904 0.01 1 975 1000 114 GLY HA2 H 3.229 0.01 2 976 1000 114 GLY HA3 H 2.952 0.01 2 977 1000 114 GLY C C 167.047 0.05 1 978 1000 114 GLY CA C 42.787 0.05 1 979 1000 114 GLY N N 105.718 0.1 1 980 1001 115 ASN H H 9.322 0.01 1 981 1001 115 ASN HA H 4.994 0.01 1 982 1001 115 ASN HB2 H 2.654 0.01 2 983 1001 115 ASN HB3 H 2.552 0.01 2 984 1001 115 ASN C C 171.262 0.05 1 985 1001 115 ASN CA C 49.895 0.05 1 986 1001 115 ASN CB C 38.83 0.05 1 987 1001 115 ASN N N 119.078 0.1 1 988 1002 116 TYR H H 8.528 0.01 1 989 1002 116 TYR HA H 5.463 0.01 1 990 1002 116 TYR HB2 H 2.912 0.01 2 991 1002 116 TYR HB3 H 2.763 0.01 2 992 1002 116 TYR HD1 H 6.449 0.01 3 993 1002 116 TYR HE2 H 6.629 0.01 3 994 1002 116 TYR C C 170.654 0.05 1 995 1002 116 TYR CA C 54.19 0.05 1 996 1002 116 TYR CB C 39.094 0.05 1 997 1002 116 TYR N N 115.2 0.1 1 998 1003 117 GLU H H 8.895 0.01 1 999 1003 117 GLU HA H 5.196 0.01 1 1000 1003 117 GLU HB2 H 1.791 0.01 2 1001 1003 117 GLU HB3 H 1.791 0.01 2 1002 1003 117 GLU HG2 H 2.13 0.01 2 1003 1003 117 GLU C C 171.970 0.05 1 1004 1003 117 GLU CA C 51.89 0.05 1 1005 1003 117 GLU CB C 31.468 0.05 1 1006 1003 117 GLU CG C 34.975 0.05 1 1007 1003 117 GLU N N 119.3 0.1 1 1008 1004 118 LEU H H 9.283 0.01 1 1009 1004 118 LEU HA H 5.196 0.01 1 1010 1004 118 LEU HB2 H 1.329 0.01 2 1011 1004 118 LEU HB3 H 0.937 0.01 2 1012 1004 118 LEU C C 171.832 0.05 1 1013 1004 118 LEU CA C 51.05 0.05 1 1014 1004 118 LEU CB C 44.8 0.05 1 1015 1004 118 LEU CD1 C 19.920 0.05 2 1016 1004 118 LEU CD2 C 19.920 0.05 2 1017 1004 118 LEU CG C 23.492 0.05 1 1018 1004 118 LEU N N 124.9 0.1 1 1019 1005 119 ARG H H 8.835 0.01 1 1020 1005 119 ARG HA H 4.48 0.01 1 1021 1005 119 ARG HB2 H 1.603 0.01 2 1022 1005 119 ARG HB3 H 1.603 0.01 2 1023 1005 119 ARG C C 170.649 0.05 1 1024 1005 119 ARG CA C 52.23 0.05 1 1025 1005 119 ARG CB C 31.57 0.05 1 1026 1005 119 ARG CD C 40.456 0.05 1 1027 1005 119 ARG CG C 24.884 0.05 1 1028 1005 119 ARG N N 125.6 0.1 1 1029 1006 120 VAL H H 8.185 0.01 1 1030 1006 120 VAL HA H 5.101 0.01 1 1031 1006 120 VAL HB H 1.401 0.01 1 1032 1006 120 VAL HG2 H 0.015 0.01 2 1033 1006 120 VAL C C 171.121 0.05 1 1034 1006 120 VAL CA C 58.62 0.05 1 1035 1006 120 VAL CB C 29.09 0.05 1 1036 1006 120 VAL CG1 C 17.445 0.05 2 1037 1006 120 VAL CG2 C 17.445 0.05 2 1038 1006 120 VAL N N 123.7 0.1 1 1039 1007 121 ASN H H 8.30 0.01 1 1040 1007 121 ASN HA H 5.105 0.01 1 1041 1007 121 ASN HB2 H 2.296 0.01 2 1042 1007 121 ASN HB3 H 2.296 0.01 2 1043 1007 121 ASN C C 170.495 0.05 1 1044 1007 121 ASN CA C 49.74 0.05 1 1045 1007 121 ASN CB C 39.04 0.05 1 1046 1007 121 ASN N N 124.5 0.1 1 1047 1008 122 LYS H H 8.183 0.01 1 1048 1008 122 LYS CA C 55.14 0.05 1 1049 1008 122 LYS CB C 32.19 0.05 1 1050 1008 122 LYS N N 124.9 0.1 1 stop_ save_