data_11471 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS ; _BMRB_accession_number 11471 _BMRB_flat_file_name bmr11471.str _Entry_type original _Submission_date 2012-01-24 _Accession_date 2012-01-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'PCS-based rigid body docking structure' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kobashigawa Yoshihiro . . 2 Ushio Masahiro . . 3 Saio Tomohide . . 4 Inagaki Fuyuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 647 "13C chemical shifts" 535 "15N chemical shifts" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-01 original author . stop_ _Original_release_date 2012-06-01 save_ ############################# # Citation for this entry # ############################# save_Citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22487935 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kobashigawa Yoshihiro . . 2 Saio Tomohide . . 3 Ushio Masahiro . . 4 Inagaki Fuyuhiko . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 53 _Journal_issue . _Journal_ASTM JBNME9 _Journal_ISSN 0925-2738 _Journal_CSD 0800 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 53 _Page_last 63 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'FKBP12-mTOR FRB domain-rapamycin complex structure' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_2 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 11836.611 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; GVQVETISPGDGRTFPKRGQ TCVVHYTGMLEDGKKFDSSR DRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFD VELLKLE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 902 GLY 2 903 VAL 3 904 GLN 4 905 VAL 5 906 GLU 6 907 THR 7 908 ILE 8 909 SER 9 910 PRO 10 911 GLY 11 912 ASP 12 913 GLY 13 914 ARG 14 915 THR 15 916 PHE 16 917 PRO 17 918 LYS 18 919 ARG 19 920 GLY 20 921 GLN 21 922 THR 22 923 CYS 23 924 VAL 24 925 VAL 25 926 HIS 26 927 TYR 27 928 THR 28 929 GLY 29 930 MET 30 931 LEU 31 932 GLU 32 933 ASP 33 934 GLY 34 935 LYS 35 936 LYS 36 937 PHE 37 938 ASP 38 939 SER 39 940 SER 40 941 ARG 41 942 ASP 42 943 ARG 43 944 ASN 44 945 LYS 45 946 PRO 46 947 PHE 47 948 LYS 48 949 PHE 49 950 MET 50 951 LEU 51 952 GLY 52 953 LYS 53 954 GLN 54 955 GLU 55 956 VAL 56 957 ILE 57 958 ARG 58 959 GLY 59 960 TRP 60 961 GLU 61 962 GLU 62 963 GLY 63 964 VAL 64 965 ALA 65 966 GLN 66 967 MET 67 968 SER 68 969 VAL 69 970 GLY 70 971 GLN 71 972 ARG 72 973 ALA 73 974 LYS 74 975 LEU 75 976 THR 76 977 ILE 77 978 SER 78 979 PRO 79 980 ASP 80 981 TYR 81 982 ALA 82 983 TYR 83 984 GLY 84 985 ALA 85 986 THR 86 987 GLY 87 988 HIS 88 989 PRO 89 990 GLY 90 991 ILE 91 992 ILE 92 993 PRO 93 994 PRO 94 995 HIS 95 996 ALA 96 997 THR 97 998 LEU 98 999 VAL 99 1000 PHE 100 1001 ASP 101 1002 VAL 102 1003 GLU 103 1004 LEU 104 1005 LEU 105 1006 LYS 106 1007 LEU 107 1008 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-23 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 16925 FKBP12 100.00 107 100.00 100.00 3.08e-72 BMRB 16931 FKBP12 100.00 107 100.00 100.00 3.08e-72 BMRB 16933 FKBP12 100.00 107 100.00 100.00 3.08e-72 BMRB 19240 FKBP12 100.00 107 100.00 100.00 3.08e-72 BMRB 19241 FKBP12 100.00 107 100.00 100.00 3.08e-72 PDB 1A7X "Fkbp12-Fk1012 Complex" 100.00 107 100.00 100.00 3.08e-72 PDB 1B6C "Crystal Structure Of The Cytoplasmic Domain Of The Type I Tgf-Beta Receptor In Complex With Fkbp12" 100.00 107 100.00 100.00 3.08e-72 PDB 1BKF "Fk506 Binding Protein Fkbp Mutant R42kH87V COMPLEX WITH Immunosuppressant Fk506" 100.00 107 98.13 99.07 3.33e-70 PDB 1BL4 "Fkbp Mutant F36v Complexed With Remodeled Synthetic Ligand" 100.00 107 99.07 99.07 3.05e-71 PDB 1D6O "Native Fkbp" 100.00 107 100.00 100.00 3.08e-72 PDB 1D7H "Fkbp Complexed With Dmso" 100.00 107 100.00 100.00 3.08e-72 PDB 1D7I "Fkbp Complexed With Methyl Methylsulfinylmethyl Sulfide (Dss)" 100.00 107 100.00 100.00 3.08e-72 PDB 1D7J "Fkbp Complexed With 4-Hydroxy-2-Butanone" 100.00 107 100.00 100.00 3.08e-72 PDB 1EYM "Fk506 Binding Protein Mutant, Homodimeric Complex" 100.00 107 99.07 99.07 2.32e-71 PDB 1F40 "Solution Structure Of Fkbp12 Complexed With Gpi-1046, A Neurotrophic Ligand" 100.00 107 100.00 100.00 3.08e-72 PDB 1FAP "The Structure Of The Immunophilin-Immunosuppressant Fkbp12- Rapamycin Complex Interacting With Human Frap" 99.07 107 100.00 100.00 1.44e-71 PDB 1FKB "Atomic Structure Of The Rapamycin Human Immunophilin Fkbp- 12 Complex" 99.07 107 100.00 100.00 1.44e-71 PDB 1FKD "Fk-506 Binding Protein: Three-Dimensional Structure Of The Complex With The Antagonist L-685,818" 100.00 107 100.00 100.00 3.08e-72 PDB 1FKF "Atomic Structure Of Fkbp-Fk506, An Immunophilin-Immunosuppressant Complex" 100.00 107 100.00 100.00 3.08e-72 PDB 1FKG "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.44e-71 PDB 1FKH "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.44e-71 PDB 1FKI "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.44e-71 PDB 1FKJ "Atomic Structure Of Fkbp12-Fk506, An Immunophilin Immunosuppressant Complex" 100.00 107 100.00 100.00 3.08e-72 PDB 1FKK "Atomic Structure Of Fkbp12, An Immunophilin Binding Protein" 100.00 107 97.20 100.00 1.77e-70 PDB 1FKL "Atomic Structure Of Fkbp12-Rapaymycin, An Immunophilin- Immunosuppressant Complex" 100.00 107 97.20 100.00 1.77e-70 PDB 1FKR "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.08e-72 PDB 1FKS "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.08e-72 PDB 1FKT "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.08e-72 PDB 1J4H "Crystal Structure Analysis Of The Fkbp12 Complexed With 000107 Small Molecule" 100.00 107 100.00 100.00 3.08e-72 PDB 1J4I "Crystal Structure Analysis Of The Fkbp12 Complexed With 000308 Small Molecule" 100.00 107 100.00 100.00 3.08e-72 PDB 1J4R "Fk506 Binding Protein Complexed With Fkb-001" 100.00 107 100.00 100.00 3.08e-72 PDB 1NSG "The Structure Of The Immunophilin-immunosuppressant Fkbp12-rapamycin Complex Interacting With Human Frap" 100.00 107 100.00 100.00 3.08e-72 PDB 1QPF "Fk506 Binding Protein (12 Kda, Human) Complex With L-709,858" 100.00 107 100.00 100.00 3.08e-72 PDB 1QPL "Fk506 Binding Protein (12 Kda, Human) Complex With L-707,587" 100.00 107 100.00 100.00 3.08e-72 PDB 1TCO "Ternary Complex Of A Calcineurin A Fragment, Calcineurin B, Fkbp12 And The Immunosuppressant Drug Fk506 (tacrolimus)" 100.00 107 99.07 99.07 2.65e-71 PDB 2DG3 "Wildtype Fk506-Binding Protein Complexed With Rapamycin" 100.00 107 100.00 100.00 3.08e-72 PDB 2DG4 "Fk506-Binding Protein Mutant Wf59 Complexed With Rapamycin" 100.00 107 99.07 100.00 3.92e-71 PDB 2DG9 "Fk506-Binding Protein Mutant Wl59 Complexed With Rapamycin" 100.00 107 99.07 99.07 7.22e-71 PDB 2FAP "The Structure Of The Immunophilin-immunosuppressant Fkbp12-(c16)- Ethoxy Rapamycin Complex Interacting With Huma" 100.00 107 100.00 100.00 3.08e-72 PDB 2FKE "Fk-506-Binding Protein: Three-Dimensional Structure Of The Complex With The Antagonist L-685,818" 100.00 107 100.00 100.00 3.08e-72 PDB 2PPN "Crystal Structure Of Fkbp12" 100.00 107 100.00 100.00 3.08e-72 PDB 2PPO "Crystal Structure Of E60a Mutant Of Fkbp12" 100.00 107 99.07 99.07 1.59e-71 PDB 2PPP "Crystal Structure Of E60q Mutant Of Fkbp12" 100.00 107 99.07 100.00 8.89e-72 PDB 2RSE "Nmr Structure Of Fkbp12-Mtor Frb Domain-Rapamycin Complex Structure Determined Based On Pcs" 100.00 107 100.00 100.00 3.08e-72 PDB 3FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 107 100.00 100.00 3.08e-72 PDB 3H9R "Crystal Structure Of The Kinase Domain Of Type I Activin Receptor (Acvr1) In Complex With Fkbp12 And Dorsomorphin" 100.00 109 100.00 100.00 2.12e-72 PDB 3MDY "Crystal Structure Of The Cytoplasmic Domain Of The Bone Morp Protein Receptor Type-1b (Bmpr1b) In Complex With Fkbp12 An 193189" 100.00 109 100.00 100.00 2.12e-72 PDB 4DH0 "X-Ray Crystal Structure Of 28-O-Methylrapamycin Complexed With Fkbp12: Is The Cyclohexyl Moiety Part Of The Effector Domain Of " 100.00 107 100.00 100.00 3.08e-72 PDB 4FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 107 100.00 100.00 3.08e-72 PDB 4IPX "Analyzing The Visible Conformational Substates Of The Fk506 Binding Protein Fkbp12" 100.00 107 98.13 98.13 2.01e-69 PDB 4N19 "Structural Basis Of Conformational Transitions In The Active Site And 80 S Loop In The Fk506 Binding Protein Fkbp12" 100.00 107 98.13 98.13 9.38e-70 DBJ BAB22351 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 DBJ BAB27125 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 DBJ BAB31680 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 DBJ BAE32804 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 DBJ BAE40271 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 EMBL CAA36462 "FK-506 binding protein [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 EMBL CAA39272 "FKBP [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 EMBL CAA42762 "FK506-binding protein [Mus musculus]" 100.00 108 97.20 97.20 1.14e-69 EMBL CAG28541 "FKBP1A [Homo sapiens]" 100.00 108 98.13 99.07 2.08e-70 EMBL CAG46965 "FKBP1A [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 GB AAA19163 "immunophilin FKBP12 [Rattus norvegicus]" 100.00 108 97.20 97.20 1.14e-69 GB AAA31252 "binding protein [Oryctolagus cuniculus]" 100.00 108 100.00 100.00 3.36e-72 GB AAA35844 "FK506-binding protein (FKBP) [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 GB AAA58472 "FKBP-12 protein [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 GB AAA58476 "FK506-binding protein 12 [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 PRF 1613455A "FK506 binding protein FKBP" 100.00 108 100.00 100.00 3.36e-72 REF NP_000792 "peptidyl-prolyl cis-trans isomerase FKBP1A isoform a [Homo sapiens]" 100.00 108 100.00 100.00 3.36e-72 REF NP_001030533 "peptidyl-prolyl cis-trans isomerase FKBP1A [Bos taurus]" 100.00 108 97.20 100.00 1.53e-70 REF NP_001033089 "peptidyl-prolyl cis-trans isomerase FKBP1A [Sus scrofa]" 100.00 108 98.13 100.00 1.08e-70 REF NP_001164597 "peptidyl-prolyl cis-trans isomerase FKBP1A [Oryctolagus cuniculus]" 100.00 108 100.00 100.00 3.36e-72 REF NP_001239119 "peptidyl-prolyl cis-trans isomerase FKBP1A [Canis lupus familiaris]" 100.00 108 99.07 100.00 1.80e-71 SP P18203 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 100.00 1.53e-70 SP P26883 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 97.20 1.14e-69 SP P62942 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 100.00 100.00 3.36e-72 SP P62943 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 100.00 100.00 3.36e-72 SP Q62658 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 97.20 1.14e-69 TPG DAA23300 "TPA: peptidyl-prolyl cis-trans isomerase FKBP1A [Bos taurus]" 100.00 108 97.20 100.00 1.53e-70 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 11332.021 _Mol_thiol_state . _Details . _Residue_count 94 _Mol_residue_sequence ; VAILWHEMWHEGLEEASRLY FGERNVKGMFEVLEPLHAMM ERGPQTLKETSFNQAYGRDL MEAQEWCRKYMKSGNVKDLT QAWDLYYHVFRRIS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1009 VAL 2 1010 ALA 3 1011 ILE 4 1012 LEU 5 1013 TRP 6 1014 HIS 7 1015 GLU 8 1016 MET 9 1017 TRP 10 1018 HIS 11 1019 GLU 12 1020 GLY 13 1021 LEU 14 1022 GLU 15 1023 GLU 16 1024 ALA 17 1025 SER 18 1026 ARG 19 1027 LEU 20 1028 TYR 21 1029 PHE 22 1030 GLY 23 1031 GLU 24 1032 ARG 25 1033 ASN 26 1034 VAL 27 1035 LYS 28 1036 GLY 29 1037 MET 30 1038 PHE 31 1039 GLU 32 1040 VAL 33 1041 LEU 34 1042 GLU 35 1043 PRO 36 1044 LEU 37 1045 HIS 38 1046 ALA 39 1047 MET 40 1048 MET 41 1049 GLU 42 1050 ARG 43 1051 GLY 44 1052 PRO 45 1053 GLN 46 1054 THR 47 1055 LEU 48 1056 LYS 49 1057 GLU 50 1058 THR 51 1059 SER 52 1060 PHE 53 1061 ASN 54 1062 GLN 55 1063 ALA 56 1064 TYR 57 1065 GLY 58 1066 ARG 59 1067 ASP 60 1068 LEU 61 1069 MET 62 1070 GLU 63 1071 ALA 64 1072 GLN 65 1073 GLU 66 1074 TRP 67 1075 CYS 68 1076 ARG 69 1077 LYS 70 1078 TYR 71 1079 MET 72 1080 LYS 73 1081 SER 74 1082 GLY 75 1083 ASN 76 1084 VAL 77 1085 LYS 78 1086 ASP 79 1087 LEU 80 1088 THR 81 1089 GLN 82 1090 ALA 83 1091 TRP 84 1092 ASP 85 1093 LEU 86 1094 TYR 87 1095 TYR 88 1096 HIS 89 1097 VAL 90 1098 PHE 91 1099 ARG 92 1100 ARG 93 1101 ILE 94 1102 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-31 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 16933 FRB 100.00 102 100.00 100.00 1.69e-63 BMRB 6760 FRB_domain_polypeptide 100.00 126 98.94 98.94 1.92e-62 PDB 1AUE "Fkbp-Rapamycin Binding Domain (Frb) Of The Fkbp-Rapamycin Associated Protein" 100.00 100 100.00 100.00 1.68e-63 PDB 1FAP "The Structure Of The Immunophilin-Immunosuppressant Fkbp12- Rapamycin Complex Interacting With Human Frap" 100.00 95 100.00 100.00 1.96e-63 PDB 1NSG "The Structure Of The Immunophilin-immunosuppressant Fkbp12-rapamycin Complex Interacting With Human Frap" 100.00 94 100.00 100.00 1.90e-63 PDB 2FAP "The Structure Of The Immunophilin-immunosuppressant Fkbp12-(c16)- Ethoxy Rapamycin Complex Interacting With Huma" 100.00 94 100.00 100.00 1.90e-63 PDB 2GAQ "Nmr Solution Structure Of The Frb Domain Of Mtor" 100.00 100 100.00 100.00 1.68e-63 PDB 2NPU "The Solution Structure Of The Rapamycin-Binding Domain Of Mtor (Frb)" 100.00 126 98.94 98.94 1.92e-62 PDB 2RSE "Nmr Structure Of Fkbp12-Mtor Frb Domain-Rapamycin Complex Structure Determined Based On Pcs" 100.00 94 100.00 100.00 1.90e-63 PDB 3FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 94 100.00 100.00 1.90e-63 PDB 4DRH "Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor At Low Ph" 93.62 98 100.00 100.00 1.74e-58 PDB 4DRI "Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor" 93.62 98 100.00 100.00 1.74e-58 PDB 4DRJ "O-crystal Structure Of The Ppiase Domain Of Fkbp52, Rapamycin And The Frb Fragment Of Mtor" 93.62 98 100.00 100.00 1.74e-58 PDB 4FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 94 100.00 100.00 1.90e-63 PDB 4JSN "Structure Of Mtordeltan-mlst8 Complex" 100.00 1174 100.00 100.00 3.78e-58 PDB 4JSP "Structure Of Mtordeltan-mlst8-atpgammas-mg Complex" 100.00 1174 100.00 100.00 3.78e-58 PDB 4JSV "Mtor Kinase Structure, Mechanism And Regulation." 100.00 1174 100.00 100.00 3.78e-58 PDB 4JSX "Structure Of Mtordeltan-mlst8-torin2 Complex" 100.00 1174 100.00 100.00 3.78e-58 PDB 4JT5 "Mtordeltan-mlst8-pp242 Complex" 100.00 1174 100.00 100.00 3.78e-58 PDB 4JT6 "Structure Of Mtordeltan-mlst8-pi-103 Complex" 100.00 1174 100.00 100.00 3.78e-58 DBJ BAE06077 "FRAP1 variant protein [Homo sapiens]" 100.00 2583 100.00 100.00 2.92e-58 DBJ BAG10549 "FKBP12-rapamycin complex-associated protein [synthetic construct]" 100.00 2549 100.00 100.00 2.41e-58 DBJ BAG54371 "unnamed protein product [Homo sapiens]" 100.00 754 100.00 100.00 1.23e-59 EMBL CAC15570 "rapamycin associated protein FRAP2 [Homo sapiens]" 100.00 1188 100.00 100.00 3.68e-58 EMBL CAC42395 "dJ576K7.1 (FK506 binding protein 12-rapamycin associated protein 1) [Homo sapiens]" 100.00 895 100.00 100.00 7.91e-59 GB AAA20091 "rapamycin and FKBP12 target-1 protein [Rattus norvegicus]" 100.00 2549 100.00 100.00 2.21e-58 GB AAA58486 "FKBP-rapamycin associated protein [Homo sapiens]" 100.00 2549 100.00 100.00 2.46e-58 GB AAA65929 "rapamycin target [Rattus norvegicus]" 100.00 2549 100.00 100.00 2.21e-58 GB AAB32957 "RAPT1=putative novel phosphatidylinositol 3-kinase {N terminal} [human, Peptide Partial, 160 aa]" 100.00 160 100.00 100.00 9.51e-64 GB AAC39933 "rapamycin associated protein FRAP2 [Homo sapiens]" 100.00 2548 100.00 100.00 2.61e-58 PRF 2014422A "FKBP-rapamycin-associated protein" 100.00 2549 100.00 100.00 2.68e-58 REF NP_001138927 "serine/threonine-protein kinase mTOR [Ovis aries]" 100.00 2550 100.00 100.00 2.53e-58 REF NP_001272677 "mechanistic target of rapamycin (serine/threonine kinase) [Capra hircus]" 100.00 2549 100.00 100.00 2.51e-58 REF NP_004949 "serine/threonine-protein kinase mTOR [Homo sapiens]" 100.00 2549 100.00 100.00 2.46e-58 REF NP_063971 "serine/threonine-protein kinase mTOR [Rattus norvegicus]" 100.00 2549 100.00 100.00 2.21e-58 REF NP_064393 "serine/threonine-protein kinase mTOR [Mus musculus]" 100.00 2549 100.00 100.00 2.26e-58 SP P42345 "RecName: Full=Serine/threonine-protein kinase mTOR; AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein" 100.00 2549 100.00 100.00 2.46e-58 SP P42346 "RecName: Full=Serine/threonine-protein kinase mTOR; AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein" 100.00 2549 100.00 100.00 2.21e-58 SP Q9JLN9 "RecName: Full=Serine/threonine-protein kinase mTOR; AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein" 100.00 2549 100.00 100.00 2.26e-58 TPG DAA21300 "TPA: mechanistic target of rapamycin (serine/threonine kinase) [Bos taurus]" 100.00 2551 100.00 100.00 2.42e-58 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens $entity_2 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 $entity_1 'recombinant technology' E.coli Escherichia coli . pGBHPS $entity_2 'recombinant technology' E.coli Escherichia coli . pGBHPS 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 $entity_1 0.3 mM 'natural abundance' $entity_2 0.3 mM '[U-98% 15N]' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl carbons' ppm 0 internal indirect . . . 0.251449530 DSS H 1 protons ppm 0 internal direct . . . 1 DSS N 15 nitrogen ppm 0 internal 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N 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 entity_1 _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 1 902 1 GLY HA2 H 2.776 0.007 . 2 902 1 GLY HA3 H 2.776 0.007 . 3 902 1 GLY H H 8.289 0.012 . 4 902 1 GLY CA C 45.279 0.083 . 5 902 1 GLY N N 111.899 0.038 . 6 903 2 VAL H H 7.656 0.004 . 7 903 2 VAL HA H 5.049 0.011 . 8 903 2 VAL HB H 1.901 0.002 . 9 903 2 VAL HG1 H 0.787 0 . 10 903 2 VAL HG2 H 0.884 0 . 11 903 2 VAL CA C 59.111 0.114 . 12 903 2 VAL CB C 34.611 0.098 . 13 903 2 VAL CG1 C 22.274 0 . 14 903 2 VAL CG2 C 18.76 0 . 15 903 2 VAL N N 117.489 0.019 . 16 904 3 GLN H H 8.573 0.006 . 17 904 3 GLN HA H 4.683 0.015 . 18 904 3 GLN HB2 H 2.066 0 . 19 904 3 GLN HB3 H 1.92 0 . 20 904 3 GLN HG2 H 2.307 0 . 21 904 3 GLN HG3 H 2.247 0 . 22 904 3 GLN HE21 H 6.796 0.005 . 23 904 3 GLN HE22 H 7.429 0.004 . 24 904 3 GLN CA C 54.174 0.146 . 25 904 3 GLN CB C 31.767 0.058 . 26 904 3 GLN CG C 33.96 0.039 . 27 904 3 GLN N N 127.217 0.021 . 28 904 3 GLN NE2 N 111.583 0.001 . 29 905 4 VAL H H 8.824 0.005 . 30 905 4 VAL HA H 4.511 0 . 31 905 4 VAL HB H 2.004 0.023 . 32 905 4 VAL HG1 H 0.617 0 . 33 905 4 VAL HG2 H 0.76 0 . 34 905 4 VAL CA C 61.924 0.083 . 35 905 4 VAL CB C 33.102 0.042 . 36 905 4 VAL CG1 C 20.591 0 . 37 905 4 VAL CG2 C 21.095 0 . 38 905 4 VAL N N 125.529 0.019 . 39 906 5 GLU H H 8.987 0.004 . 40 906 5 GLU CA C 54.396 0 . 41 906 5 GLU N N 128.79 0.02 . 42 907 6 THR HA H 3.893 0.004 . 43 907 6 THR HB H 4.069 0.012 . 44 907 6 THR HG2 H 1.096 0.015 . 45 907 6 THR CA C 66.845 0.075 . 46 907 6 THR CB C 68.882 0.081 . 47 907 6 THR CG2 C 22.372 0.085 . 48 908 7 ILE H H 9.371 0.004 . 49 908 7 ILE HA H 4.071 0.002 . 50 908 7 ILE HB H 1.304 0.008 . 51 908 7 ILE HG12 H 1.054 0 . 52 908 7 ILE HG13 H 1.554 0 . 53 908 7 ILE HG2 H 0.868 0 . 54 908 7 ILE HD1 H 0.707 0 . 55 908 7 ILE CA C 63.213 0.122 . 56 908 7 ILE CB C 39.554 0.046 . 57 908 7 ILE CG1 C 27.964 0 . 58 908 7 ILE CG2 C 16.488 0 . 59 908 7 ILE CD1 C 13.352 0 . 60 908 7 ILE N N 129.743 0.017 . 61 909 8 SER H H 8.307 0.004 . 62 909 8 SER CA C 55.592 0 . 63 909 8 SER CB C 64.363 0 . 64 909 8 SER N N 114.787 0.033 . 65 910 9 PRO HA H 4.336 0.007 . 66 910 9 PRO HB2 H 2.128 0.002 . 67 910 9 PRO HB3 H 2.295 0 . 68 910 9 PRO HG2 H 2.058 0 . 69 910 9 PRO HG3 H 1.987 0 . 70 910 9 PRO HD2 H 3.724 0 . 71 910 9 PRO HD3 H 3.82 0 . 72 910 9 PRO CA C 63.657 0.185 . 73 910 9 PRO CB C 32.869 0.052 . 74 910 9 PRO CG C 27.074 0 . 75 910 9 PRO CD C 51.188 0 . 76 911 10 GLY H H 8.488 0.005 . 77 911 10 GLY HA2 H 3.524 0.004 . 78 911 10 GLY HA3 H 4.141 0.011 . 79 911 10 GLY CA C 44.098 0.072 . 80 911 10 GLY N N 107.868 0.014 . 81 912 11 ASP H H 8.054 0.007 . 82 912 11 ASP HA H 4.302 0.009 . 83 912 11 ASP HB2 H 2.761 0.022 . 84 912 11 ASP HB3 H 2.983 0.022 . 85 912 11 ASP CA C 54.54 0.03 . 86 912 11 ASP CB C 39.425 0.062 . 87 912 11 ASP N N 118.804 0.01 . 88 913 12 GLY H H 8.715 0.004 . 89 913 12 GLY HA2 H 4.015 0.001 . 90 913 12 GLY HA3 H 3.477 0.01 . 91 913 12 GLY CA C 45.994 0.031 . 92 913 12 GLY N N 108.265 0.019 . 93 914 13 ARG H H 8.543 0.008 . 94 914 13 ARG HA H 4.728 0.008 . 95 914 13 ARG HB2 H 1.729 0.001 . 96 914 13 ARG HB3 H 1.542 0 . 97 914 13 ARG HG2 H 1.554 0 . 98 914 13 ARG HG3 H 1.436 0 . 99 914 13 ARG HD2 H 3.159 0 . 100 914 13 ARG HD3 H 3.159 0 . 101 914 13 ARG CA C 56.86 0.052 . 102 914 13 ARG CB C 34.458 0.102 . 103 914 13 ARG CG C 26.759 0 . 104 914 13 ARG CD C 43.281 0 . 105 914 13 ARG N N 117.666 0.011 . 106 915 14 THR H H 10.245 0.005 . 107 915 14 THR HA H 4.211 0 . 108 915 14 THR HB H 4.22 0.009 . 109 915 14 THR HG2 H 1.105 0 . 110 915 14 THR CA C 61.965 0.023 . 111 915 14 THR CB C 66.423 0.095 . 112 915 14 THR CG2 C 22.586 0 . 113 915 14 THR N N 125.413 0.021 . 114 916 15 PHE H H 8.134 0.004 . 115 916 15 PHE HA H 5.214 0.002 . 116 916 15 PHE HB2 H 2.603 0.023 . 117 916 15 PHE HB3 H 3.089 0.02 . 118 916 15 PHE HD1 H 7.046 0 . 119 916 15 PHE HD2 H 7.046 0 . 120 916 15 PHE CA C 54.454 0.065 . 121 916 15 PHE CB C 39.727 0.113 . 122 916 15 PHE N N 124.947 0.015 . 123 917 16 PRO HA H 4.371 0.002 . 124 917 16 PRO HB2 H 1.674 0.018 . 125 917 16 PRO HB3 H 2.044 0.003 . 126 917 16 PRO HG2 H 2.105 0 . 127 917 16 PRO HG3 H 1.825 0 . 128 917 16 PRO HD2 H 4.066 0.013 . 129 917 16 PRO HD3 H 4.218 0 . 130 917 16 PRO CA C 62.797 0.145 . 131 917 16 PRO CB C 33.307 0.035 . 132 917 16 PRO CG C 28.284 0 . 133 917 16 PRO CD C 51.556 0.051 . 134 918 17 LYS H H 8.538 0.005 . 135 918 17 LYS HA H 4.599 0.009 . 136 918 17 LYS HB2 H 1.821 0.003 . 137 918 17 LYS HB3 H 1.538 0.006 . 138 918 17 LYS HG2 H 1.511 0 . 139 918 17 LYS HG3 H 1.446 0 . 140 918 17 LYS HD2 H 1.681 0 . 141 918 17 LYS HD3 H 1.617 0 . 142 918 17 LYS HE2 H 3.007 0.015 . 143 918 17 LYS HE3 H 3.007 0.015 . 144 918 17 LYS CA C 53.497 0.084 . 145 918 17 LYS CB C 34.884 0.104 . 146 918 17 LYS CG C 24.604 0 . 147 918 17 LYS CD C 28.862 0 . 148 918 17 LYS CE C 42.309 0.336 . 149 918 17 LYS N N 121.492 0.033 . 150 919 18 ARG H H 8.457 0.003 . 151 919 18 ARG HA H 3.657 0.003 . 152 919 18 ARG HB2 H 1.77 0.024 . 153 919 18 ARG HB3 H 1.77 0.024 . 154 919 18 ARG HG2 H 1.503 0 . 155 919 18 ARG HG3 H 1.503 0 . 156 919 18 ARG HD2 H 3.241 0 . 157 919 18 ARG HD3 H 3.241 0 . 158 919 18 ARG CA C 58.693 0.046 . 159 919 18 ARG CB C 29.62 0.1 . 160 919 18 ARG CG C 27.998 0 . 161 919 18 ARG CD C 43.372 0 . 162 919 18 ARG N N 120.319 0.021 . 163 920 19 GLY H H 8.928 0.005 . 164 920 19 GLY HA2 H 4.379 0.011 . 165 920 19 GLY HA3 H 3.593 0.03 . 166 920 19 GLY CA C 44.909 0.06 . 167 920 19 GLY N N 113.107 0.022 . 168 921 20 GLN H H 8.103 0.007 . 169 921 20 GLN HA H 4.497 0.011 . 170 921 20 GLN HB2 H 2.241 0.004 . 171 921 20 GLN HB3 H 1.903 0 . 172 921 20 GLN HG2 H 2.355 0 . 173 921 20 GLN HG3 H 2.276 0 . 174 921 20 GLN HE21 H 6.479 0 . 175 921 20 GLN HE22 H 7.612 0 . 176 921 20 GLN CA C 56.326 0.065 . 177 921 20 GLN CB C 30.757 0.052 . 178 921 20 GLN CG C 35.815 0.073 . 179 921 20 GLN N N 118.965 0.038 . 180 921 20 GLN NE2 N 110.835 0.001 . 181 922 21 THR H H 8.67 0.004 . 182 922 21 THR HA H 4.502 0.002 . 183 922 21 THR HB H 3.914 0.003 . 184 922 21 THR HG2 H 0.846 0 . 185 922 21 THR CA C 63.046 0.024 . 186 922 21 THR CB C 68.81 0.076 . 187 922 21 THR CG2 C 21.457 0 . 188 922 21 THR N N 119.874 0.02 . 189 923 22 CYS H H 8.833 0.001 . 190 923 22 CYS HA H 4.382 0 . 191 923 22 CYS HB2 H 2.158 0.001 . 192 923 22 CYS HB3 H 1.994 0.002 . 193 923 22 CYS CA C 58.061 0.021 . 194 923 22 CYS CB C 29.251 0.047 . 195 923 22 CYS N N 126.056 0.068 . 196 924 23 VAL H H 8.147 0.002 . 197 924 23 VAL HA H 4.738 0 . 198 924 23 VAL HB H 2.039 0.001 . 199 924 23 VAL HG1 H 0.651 0 . 200 924 23 VAL HG2 H 0.781 0 . 201 924 23 VAL CA C 61.419 0.09 . 202 924 23 VAL CB C 31.329 0.083 . 203 924 23 VAL CG1 C 19.904 0 . 204 924 23 VAL CG2 C 21.326 0 . 205 924 23 VAL N N 123.623 0.015 . 206 925 24 VAL H H 9.799 0.003 . 207 925 24 VAL HA H 5.912 0 . 208 925 24 VAL HB H 2.483 0 . 209 925 24 VAL HG1 H 1.486 0 . 210 925 24 VAL HG2 H 1.007 0 . 211 925 24 VAL CA C 58.15 0.04 . 212 925 24 VAL CB C 35.953 0.074 . 213 925 24 VAL CG1 C 21.011 0 . 214 925 24 VAL CG2 C 21.491 0 . 215 925 24 VAL N N 119.1 0.013 . 216 926 25 HIS H H 8.498 0.002 . 217 926 25 HIS HA H 3.742 0 . 218 926 25 HIS HB2 H 2.851 0 . 219 926 25 HIS HB3 H 2.719 0 . 220 926 25 HIS CA C 54.919 0.032 . 221 926 25 HIS CB C 35.66 0.045 . 222 926 25 HIS N N 117.791 0.027 . 223 927 26 TYR H H 10.025 0.005 . 224 927 26 TYR HB2 H 3.27 0 . 225 927 26 TYR HB3 H 3.135 0 . 226 927 26 TYR HE1 H 6.189 0.008 . 227 927 26 TYR HE2 H 6.189 0.008 . 228 927 26 TYR CA C 55.707 0.042 . 229 927 26 TYR CB C 44.864 0.075 . 230 927 26 TYR CE1 C 112.292 0 . 231 927 26 TYR CE2 C 112.292 0 . 232 927 26 TYR N N 118.552 0.019 . 233 928 27 THR H H 8.926 0.002 . 234 928 27 THR HA H 4.045 0.012 . 235 928 27 THR HB H 4.061 0 . 236 928 27 THR HG2 H 1.256 0 . 237 928 27 THR CA C 62.89 0.194 . 238 928 27 THR CB C 72.235 0.044 . 239 928 27 THR N N 116.977 0.027 . 240 929 28 GLY H H 9.325 0.004 . 241 929 28 GLY HA2 H 4.152 0.009 . 242 929 28 GLY HA3 H 2.37 0.003 . 243 929 28 GLY CA C 45.52 0.036 . 244 929 28 GLY N N 115.078 0.011 . 245 930 29 MET H H 8.998 0.003 . 246 930 29 MET HA H 5.094 0.016 . 247 930 29 MET HB2 H 1.903 0 . 248 930 29 MET HB3 H 1.792 0.001 . 249 930 29 MET HG2 H 2.356 0 . 250 930 29 MET HG3 H 2.041 0.068 . 251 930 29 MET CA C 54.204 0.047 . 252 930 29 MET CB C 37.825 0.075 . 253 930 29 MET CG C 31.559 0.159 . 254 930 29 MET N N 124.963 0.01 . 255 931 30 LEU H H 8.392 0.004 . 256 931 30 LEU HA H 4.81 0.003 . 257 931 30 LEU HB2 H 2.23 0.036 . 258 931 30 LEU HB3 H 1.932 0.009 . 259 931 30 LEU HG H 1.983 0 . 260 931 30 LEU HD1 H 1.072 0.012 . 261 931 30 LEU HD2 H 0.931 0 . 262 931 30 LEU CA C 54.237 0.066 . 263 931 30 LEU CB C 41.7 0.09 . 264 931 30 LEU CG C 27.753 0 . 265 931 30 LEU CD1 C 25.688 0.014 . 266 931 30 LEU CD2 C 22.864 0 . 267 931 30 LEU N N 119.51 0.011 . 268 932 31 GLU H H 8.979 0.004 . 269 932 31 GLU HA H 3.825 0.001 . 270 932 31 GLU HB2 H 2.092 0.001 . 271 932 31 GLU HB3 H 2.092 0.001 . 272 932 31 GLU HG2 H 2.254 0 . 273 932 31 GLU HG3 H 2.254 0 . 274 932 31 GLU CA C 59.584 0.044 . 275 932 31 GLU CB C 29.899 0.129 . 276 932 31 GLU CG C 36.544 0 . 277 932 31 GLU N N 120.698 0.021 . 278 933 32 ASP H H 7.884 0.006 . 279 933 32 ASP HA H 4.426 0.01 . 280 933 32 ASP HB2 H 2.602 0.002 . 281 933 32 ASP HB3 H 2.997 0.001 . 282 933 32 ASP CA C 53.589 0.052 . 283 933 32 ASP CB C 40.058 0.036 . 284 933 32 ASP N N 115.563 0.029 . 285 934 33 GLY H H 8.232 0.005 . 286 934 33 GLY HA2 H 4.293 0.017 . 287 934 33 GLY HA3 H 3.681 0.01 . 288 934 33 GLY CA C 44.917 0.037 . 289 934 33 GLY N N 108.513 0.027 . 290 935 34 LYS H H 7.876 0.009 . 291 935 34 LYS HA H 4.113 0.009 . 292 935 34 LYS HB2 H 1.933 0.021 . 293 935 34 LYS HB3 H 1.815 0.001 . 294 935 34 LYS HG2 H 1.467 0 . 295 935 34 LYS HG3 H 1.324 0 . 296 935 34 LYS HD2 H 1.673 0 . 297 935 34 LYS HD3 H 1.746 0.006 . 298 935 34 LYS HE2 H 3.06 0 . 299 935 34 LYS HE3 H 2.993 0 . 300 935 34 LYS CA C 57.38 0.069 . 301 935 34 LYS CB C 32.614 0.038 . 302 935 34 LYS CG C 24.972 0 . 303 935 34 LYS CD C 29.144 0.065 . 304 935 34 LYS CE C 42.309 0 . 305 935 34 LYS N N 121.819 0.046 . 306 936 35 LYS H H 8.569 0.004 . 307 936 35 LYS HA H 4.485 0.012 . 308 936 35 LYS HB2 H 1.738 0.021 . 309 936 35 LYS HB3 H 1.698 0.002 . 310 936 35 LYS HG2 H 1.424 0 . 311 936 35 LYS HG3 H 1.117 0 . 312 936 35 LYS HD2 H 1.518 0 . 313 936 35 LYS HD3 H 1.439 0 . 314 936 35 LYS HE2 H 2.926 0 . 315 936 35 LYS HE3 H 2.822 0 . 316 936 35 LYS CA C 56.385 0.019 . 317 936 35 LYS CB C 33.061 0.096 . 318 936 35 LYS CG C 24.753 0 . 319 936 35 LYS CD C 29.798 0 . 320 936 35 LYS CE C 41.379 0 . 321 936 35 LYS N N 128.078 0.008 . 322 937 36 PHE H H 8.346 0.002 . 323 937 36 PHE HA H 5.139 0 . 324 937 36 PHE HB2 H 2.743 0 . 325 937 36 PHE HB3 H 3.262 0 . 326 937 36 PHE HD1 H 6.948 0.005 . 327 937 36 PHE HD2 H 6.948 0.005 . 328 937 36 PHE CA C 56.288 0.01 . 329 937 36 PHE CB C 40.788 0.023 . 330 937 36 PHE CD1 C 132.499 0 . 331 937 36 PHE CD2 C 132.499 0 . 332 937 36 PHE N N 120.67 0.019 . 333 938 37 ASP H H 7.015 0.006 . 334 938 37 ASP HA H 4.942 0.016 . 335 938 37 ASP HB2 H 3.59 0.017 . 336 938 37 ASP HB3 H 2.864 0.011 . 337 938 37 ASP CA C 54.538 0.035 . 338 938 37 ASP CB C 43.094 0.085 . 339 938 37 ASP N N 118.405 0.046 . 340 939 38 SER H H 8.501 0.005 . 341 939 38 SER HA H 4.779 0 . 342 939 38 SER HB2 H 4.041 0 . 343 939 38 SER HB3 H 3.645 0.013 . 344 939 38 SER CA C 56.937 0.035 . 345 939 38 SER CB C 65.05 0.067 . 346 939 38 SER N N 118.647 0.038 . 347 940 39 SER H H 8.414 0.002 . 348 940 39 SER HA H 4.973 0.014 . 349 940 39 SER HB2 H 4.087 0.034 . 350 940 39 SER HB3 H 3.627 0.038 . 351 940 39 SER CA C 61.705 0.047 . 352 940 39 SER CB C 61.821 0.083 . 353 940 39 SER N N 125.661 0.026 . 354 941 40 ARG H H 7.685 0 . 355 941 40 ARG HA H 4.072 0 . 356 941 40 ARG HG2 H 1.063 0 . 357 941 40 ARG HG3 H 1.063 0 . 358 941 40 ARG HD2 H 3.516 0 . 359 941 40 ARG HD3 H 3.516 0 . 360 941 40 ARG CA C 58.861 0.079 . 361 941 40 ARG CB C 28.85 0.059 . 362 941 40 ARG N N 123.447 0.013 . 363 942 41 ASP H H 7.138 0.002 . 364 942 41 ASP HB2 H 2.789 0.013 . 365 942 41 ASP HB3 H 2.69 0.011 . 366 942 41 ASP CA C 56.411 0.002 . 367 942 41 ASP CB C 40.192 0.088 . 368 942 41 ASP N N 118.529 0.027 . 369 943 42 ARG H H 6.882 0.002 . 370 943 42 ARG HA H 4.505 0.012 . 371 943 42 ARG HB2 H 1.963 0 . 372 943 42 ARG HB3 H 1.963 0 . 373 943 42 ARG HG2 H 1.745 0.041 . 374 943 42 ARG HG3 H 1.745 0.041 . 375 943 42 ARG HD2 H 2.88 0 . 376 943 42 ARG HD3 H 2.88 0 . 377 943 42 ARG CA C 55.684 0.062 . 378 943 42 ARG CB C 31.269 0.046 . 379 943 42 ARG CG C 28.364 0.511 . 380 943 42 ARG CD C 43.055 0 . 381 943 42 ARG N N 114.112 0.013 . 382 944 43 ASN H H 7.808 0.001 . 383 944 43 ASN HA H 4.394 0.008 . 384 944 43 ASN HB2 H 3.187 0.018 . 385 944 43 ASN HB3 H 2.697 0 . 386 944 43 ASN HD21 H 6.861 0.004 . 387 944 43 ASN HD22 H 7.61 0.006 . 388 944 43 ASN CA C 54.05 0.035 . 389 944 43 ASN CB C 37.614 0.067 . 390 944 43 ASN N N 116.253 0.013 . 391 944 43 ASN ND2 N 112.457 0.003 . 392 945 44 LYS H H 7.425 0.005 . 393 945 44 LYS HA H 4.935 0 . 394 945 44 LYS HG2 H 1.464 0 . 395 945 44 LYS HG3 H 1.464 0 . 396 945 44 LYS HD2 H 1.733 0 . 397 945 44 LYS HD3 H 1.733 0 . 398 945 44 LYS CA C 53.293 0.096 . 399 945 44 LYS CB C 35.403 0 . 400 945 44 LYS N N 115.872 0.026 . 401 946 45 PRO HA H 3.978 0.012 . 402 946 45 PRO HB2 H 1.456 0.007 . 403 946 45 PRO HB3 H 1.456 0.007 . 404 946 45 PRO HG2 H 1.744 0 . 405 946 45 PRO HG3 H 1.303 0 . 406 946 45 PRO HD2 H 3.623 0.004 . 407 946 45 PRO HD3 H 3.623 0.004 . 408 946 45 PRO CA C 63.098 0.056 . 409 946 45 PRO CB C 32.425 0.022 . 410 946 45 PRO CG C 26.771 0 . 411 946 45 PRO CD C 50.59 0 . 412 947 46 PHE H H 9.246 0.003 . 413 947 46 PHE HA H 4.816 0.015 . 414 947 46 PHE HB2 H 3.518 0.015 . 415 947 46 PHE HB3 H 3.236 0.017 . 416 947 46 PHE CA C 57.284 0.129 . 417 947 46 PHE CB C 42.395 0.104 . 418 947 46 PHE N N 124.896 0.029 . 419 948 47 LYS H H 7.313 0.005 . 420 948 47 LYS HA H 5.698 0.005 . 421 948 47 LYS HB2 H 1.513 0.001 . 422 948 47 LYS HB3 H 1.291 0 . 423 948 47 LYS HG2 H 1.26 0 . 424 948 47 LYS HG3 H 1.132 0 . 425 948 47 LYS HD2 H 1.615 0 . 426 948 47 LYS HD3 H 1.587 0 . 427 948 47 LYS HE2 H 2.839 0 . 428 948 47 LYS HE3 H 2.839 0 . 429 948 47 LYS CA C 54.171 0.124 . 430 948 47 LYS CB C 35.741 0.037 . 431 948 47 LYS CG C 25.519 0 . 432 948 47 LYS CD C 29.6 0 . 433 948 47 LYS CE C 41.892 0 . 434 948 47 LYS N N 124.366 0.027 . 435 949 48 PHE H H 8.108 0.003 . 436 949 48 PHE HA H 4.746 0.004 . 437 949 48 PHE HB2 H 3.092 0.039 . 438 949 48 PHE HB3 H 2.917 0.019 . 439 949 48 PHE CA C 55.699 0.051 . 440 949 48 PHE CB C 41.241 0.056 . 441 949 48 PHE N N 116.166 0.057 . 442 950 49 MET H H 9.102 0.005 . 443 950 49 MET HA H 4.625 0 . 444 950 49 MET HB2 H 1.863 0 . 445 950 49 MET HB3 H 1.808 0 . 446 950 49 MET HG2 H 2.109 0 . 447 950 49 MET HG3 H 2.109 0 . 448 950 49 MET CA C 54.399 0.052 . 449 950 49 MET CB C 33.741 0.057 . 450 950 49 MET CG C 31.786 0 . 451 950 49 MET N N 123.253 0.013 . 452 951 50 LEU H H 8.338 0.004 . 453 951 50 LEU HA H 4.254 0.009 . 454 951 50 LEU HB2 H 1.914 0.011 . 455 951 50 LEU HB3 H 1.914 0.011 . 456 951 50 LEU HG H 1.642 0 . 457 951 50 LEU HD1 H 0.707 0 . 458 951 50 LEU HD2 H 1.196 0 . 459 951 50 LEU CA C 56.806 0.051 . 460 951 50 LEU CB C 42.302 0.026 . 461 951 50 LEU CG C 25.683 0 . 462 951 50 LEU CD1 C 26.113 0 . 463 951 50 LEU CD2 C 24.638 0 . 464 951 50 LEU N N 130.901 0.058 . 465 952 51 GLY H H 10.366 0.005 . 466 952 51 GLY HA2 H 4.222 0.023 . 467 952 51 GLY HA3 H 3.83 0.011 . 468 952 51 GLY CA C 45.843 0.043 . 469 952 51 GLY N N 118.516 0.01 . 470 953 52 LYS H H 7.691 0.006 . 471 953 52 LYS HA H 4.514 0 . 472 953 52 LYS HB2 H 2.099 0.009 . 473 953 52 LYS HB3 H 1.702 0.001 . 474 953 52 LYS HG2 H 1.432 0 . 475 953 52 LYS HG3 H 1.33 0 . 476 953 52 LYS HD2 H 1.75 0 . 477 953 52 LYS HD3 H 1.507 0 . 478 953 52 LYS HE2 H 2.999 0 . 479 953 52 LYS HE3 H 2.999 0 . 480 953 52 LYS CA C 54.401 0.042 . 481 953 52 LYS CB C 33.188 0.035 . 482 953 52 LYS CG C 24.629 0 . 483 953 52 LYS CD C 28.196 0 . 484 953 52 LYS CE C 41.955 0 . 485 953 52 LYS N N 119.202 0.085 . 486 954 53 GLN H H 9.084 0.004 . 487 954 53 GLN HA H 3.885 0 . 488 954 53 GLN HB2 H 2.333 0.002 . 489 954 53 GLN HB3 H 2.102 0.003 . 490 954 53 GLN HG2 H 2.285 0 . 491 954 53 GLN HG3 H 2.194 0 . 492 954 53 GLN HE21 H 6.631 0.004 . 493 954 53 GLN HE22 H 7.57 0.003 . 494 954 53 GLN CA C 57.475 0.063 . 495 954 53 GLN CB C 25.954 0.055 . 496 954 53 GLN CG C 34.874 0.018 . 497 954 53 GLN N N 116.196 0.014 . 498 954 53 GLN NE2 N 112.171 0 . 499 955 54 GLU H H 9.614 0.002 . 500 955 54 GLU CA C 57.678 0 . 501 955 54 GLU CB C 31.212 0 . 502 955 54 GLU N N 119.317 0.006 . 503 956 55 VAL H H 6.533 0.005 . 504 956 55 VAL HA H 4.57 0.015 . 505 956 55 VAL HB H 1.308 0 . 506 956 55 VAL HG1 H 0.486 0 . 507 956 55 VAL HG2 H 0.345 0 . 508 956 55 VAL CA C 56.543 0.025 . 509 956 55 VAL CB C 36.101 0 . 510 956 55 VAL CG1 C 19.481 0 . 511 956 55 VAL CG2 C 21.26 0 . 512 956 55 VAL N N 138.355 0.02 . 513 957 56 ILE H H 7.098 0.001 . 514 957 56 ILE HA H 3.875 0 . 515 957 56 ILE HB H 2.283 0 . 516 957 56 ILE HG12 H 1.339 0 . 517 957 56 ILE HG13 H 1.339 0 . 518 957 56 ILE HG2 H 0.262 0 . 519 957 56 ILE HD1 H 0.782 0 . 520 957 56 ILE CA C 61.854 0.107 . 521 957 56 ILE CB C 38.515 0.054 . 522 957 56 ILE CG1 C 25.459 0 . 523 957 56 ILE CG2 C 18.507 0 . 524 957 56 ILE CD1 C 13.831 0 . 525 957 56 ILE N N 108.717 0.035 . 526 958 57 ARG H H 8.726 0.002 . 527 958 57 ARG HA H 4.011 0 . 528 958 57 ARG HB2 H 1.781 0 . 529 958 57 ARG HB3 H 1.43 0 . 530 958 57 ARG HG2 H 1.613 0 . 531 958 57 ARG HG3 H 1.155 0 . 532 958 57 ARG HD2 H 2.83 0 . 533 958 57 ARG HD3 H 2.22 0 . 534 958 57 ARG CA C 59.972 0.05 . 535 958 57 ARG CB C 30.545 0.063 . 536 958 57 ARG CG C 26.897 0 . 537 958 57 ARG CD C 43.52 0 . 538 958 57 ARG N N 125.386 0.021 . 539 959 58 GLY H H 9.714 0.002 . 540 959 58 GLY HA2 H 3.953 0 . 541 959 58 GLY HA3 H 3.824 0 . 542 959 58 GLY CA C 47.762 0.1 . 543 959 58 GLY N N 101.643 0.002 . 544 960 59 TRP H H 7.738 0.001 . 545 960 59 TRP HA H 4.048 0 . 546 960 59 TRP HB2 H 3.002 0 . 547 960 59 TRP HB3 H 2.62 0 . 548 960 59 TRP HE1 H 10.179 0 . 549 960 59 TRP CA C 62.02 0.028 . 550 960 59 TRP CB C 28.168 0.043 . 551 960 59 TRP N N 119.555 0.018 . 552 960 59 TRP NE1 N 129.939 0 . 553 961 60 GLU H H 7.521 0.004 . 554 961 60 GLU HA H 4.239 0.013 . 555 961 60 GLU HB2 H 2.129 0.01 . 556 961 60 GLU HB3 H 2.26 0.002 . 557 961 60 GLU HG2 H 2.266 0.014 . 558 961 60 GLU HG3 H 2.391 0.004 . 559 961 60 GLU CA C 60.363 0.036 . 560 961 60 GLU CB C 29.873 0.06 . 561 961 60 GLU CG C 36.692 0.103 . 562 961 60 GLU N N 118.467 0.021 . 563 962 61 GLU H H 8.333 0.004 . 564 962 61 GLU HA H 4.264 0 . 565 962 61 GLU HB2 H 1.841 0 . 566 962 61 GLU HB3 H 2.153 0 . 567 962 61 GLU HG2 H 2.258 0 . 568 962 61 GLU HG3 H 2.388 0 . 569 962 61 GLU CA C 58.06 0.032 . 570 962 61 GLU CB C 30.117 0.009 . 571 962 61 GLU CG C 36.817 0 . 572 962 61 GLU N N 112.49 0.03 . 573 963 62 GLY H H 7.782 0.003 . 574 963 62 GLY HA2 H 3.695 0 . 575 963 62 GLY HA3 H 3.572 0 . 576 963 62 GLY CA C 47.028 0.049 . 577 963 62 GLY N N 107.837 0.017 . 578 964 63 VAL H H 8.909 0.007 . 579 964 63 VAL HA H 3.701 0.003 . 580 964 63 VAL HB H 2.219 0.004 . 581 964 63 VAL HG1 H 1.062 0.023 . 582 964 63 VAL HG2 H 0.681 0.003 . 583 964 63 VAL CA C 65.648 0.039 . 584 964 63 VAL CB C 30.764 0.036 . 585 964 63 VAL CG1 C 22.341 0.038 . 586 964 63 VAL CG2 C 23.153 0.046 . 587 964 63 VAL N N 120.937 0.043 . 588 965 64 ALA H H 6.543 0.002 . 589 965 64 ALA HA H 4.022 0.004 . 590 965 64 ALA HB H 1.587 0 . 591 965 64 ALA CA C 54.531 0.043 . 592 965 64 ALA CB C 18.939 0.072 . 593 965 64 ALA N N 115.471 0.005 . 594 966 65 GLN H H 7.067 0.009 . 595 966 65 GLN HA H 4.316 0.003 . 596 966 65 GLN HB2 H 2.367 0.016 . 597 966 65 GLN HB3 H 2.101 0.001 . 598 966 65 GLN HG2 H 2.541 0.004 . 599 966 65 GLN HG3 H 2.356 0.002 . 600 966 65 GLN HE21 H 7.061 0.001 . 601 966 65 GLN HE22 H 7.224 0.006 . 602 966 65 GLN CA C 55.603 0.036 . 603 966 65 GLN CB C 29.978 0.04 . 604 966 65 GLN CG C 34.373 0.05 . 605 966 65 GLN N N 111.968 0.034 . 606 966 65 GLN NE2 N 111.351 0.001 . 607 967 66 MET H H 7.887 0.003 . 608 967 66 MET HA H 4.777 0.006 . 609 967 66 MET HB2 H 2.103 0.003 . 610 967 66 MET HB3 H 2.103 0.003 . 611 967 66 MET HG2 H 2.683 0 . 612 967 66 MET HG3 H 1.875 0 . 613 967 66 MET HE H 1.816 0 . 614 967 66 MET CA C 55.07 0.036 . 615 967 66 MET CB C 35.386 0.029 . 616 967 66 MET CG C 31.432 0 . 617 967 66 MET CE C 17.497 0 . 618 967 66 MET N N 122.161 0.007 . 619 968 67 SER H H 8.188 0.002 . 620 968 67 SER HA H 4.819 0 . 621 968 67 SER HB2 H 3.683 0 . 622 968 67 SER HB3 H 2.364 0 . 623 968 67 SER CA C 54.426 0.068 . 624 968 67 SER CB C 65.997 0.048 . 625 968 67 SER N N 107.731 0.028 . 626 969 68 VAL H H 7.692 0.015 . 627 969 68 VAL HA H 3.116 0.009 . 628 969 68 VAL HB H 1.814 0 . 629 969 68 VAL HG1 H 0.837 0 . 630 969 68 VAL HG2 H 0.876 0 . 631 969 68 VAL CA C 66.889 0.055 . 632 969 68 VAL CB C 31.481 0.06 . 633 969 68 VAL CG1 C 21.463 0.01 . 634 969 68 VAL CG2 C 23.271 0 . 635 969 68 VAL N N 119.333 0.006 . 636 970 69 GLY H H 8.846 0.006 . 637 970 69 GLY HA2 H 4.402 0.018 . 638 970 69 GLY HA3 H 3.859 0 . 639 970 69 GLY CA C 44.401 0.035 . 640 970 69 GLY N N 116.982 0.036 . 641 971 70 GLN H H 8.637 0.004 . 642 971 70 GLN HA H 4.058 0.012 . 643 971 70 GLN HB2 H 2.182 0 . 644 971 70 GLN HB3 H 2.182 0 . 645 971 70 GLN HG2 H 2.931 0 . 646 971 70 GLN HG3 H 2.151 0 . 647 971 70 GLN HE21 H 6.47 0 . 648 971 70 GLN HE22 H 7.613 0 . 649 971 70 GLN CA C 55.728 0.028 . 650 971 70 GLN CB C 30.593 0.027 . 651 971 70 GLN CG C 33.408 0 . 652 971 70 GLN N N 123.175 0.037 . 653 971 70 GLN NE2 N 108.553 0.001 . 654 972 71 ARG H H 8.84 0.007 . 655 972 71 ARG HA H 5.626 0.009 . 656 972 71 ARG HB2 H 1.543 0 . 657 972 71 ARG HB3 H 1.86 0.039 . 658 972 71 ARG HG2 H 1.517 0 . 659 972 71 ARG HG3 H 1.423 0 . 660 972 71 ARG HD2 H 2.982 0 . 661 972 71 ARG HD3 H 2.907 0 . 662 972 71 ARG CA C 53.937 0.072 . 663 972 71 ARG CB C 33.754 0.084 . 664 972 71 ARG CG C 26.947 0 . 665 972 71 ARG CD C 44.327 0 . 666 972 71 ARG N N 124.835 0.036 . 667 973 72 ALA H H 9.962 0.004 . 668 973 72 ALA HA H 5.131 0.023 . 669 973 72 ALA HB H 1.246 0.012 . 670 973 72 ALA CA C 50.984 0.023 . 671 973 72 ALA CB C 23.539 0.095 . 672 973 72 ALA N N 131.232 0.02 . 673 974 73 LYS H H 9.213 0.008 . 674 974 73 LYS HA H 5.098 0.005 . 675 974 73 LYS HB2 H 1.736 0.003 . 676 974 73 LYS HB3 H 1.607 0.001 . 677 974 73 LYS HG2 H 1.265 0 . 678 974 73 LYS HG3 H 1.123 0 . 679 974 73 LYS HD2 H 1.57 0 . 680 974 73 LYS HD3 H 1.57 0 . 681 974 73 LYS HE2 H 2.779 0 . 682 974 73 LYS HE3 H 2.779 0 . 683 974 73 LYS CA C 54.878 0.03 . 684 974 73 LYS CB C 34.403 0.083 . 685 974 73 LYS CG C 25.465 0 . 686 974 73 LYS CD C 29.41 0 . 687 974 73 LYS CE C 41.79 0 . 688 974 73 LYS N N 120.513 0.006 . 689 975 74 LEU H H 9.978 0.004 . 690 975 74 LEU HA H 5.385 0 . 691 975 74 LEU HB2 H 1.738 0 . 692 975 74 LEU HB3 H 1.234 0 . 693 975 74 LEU HG H 1.512 0 . 694 975 74 LEU HD1 H 0.446 0 . 695 975 74 LEU HD2 H 0.473 0 . 696 975 74 LEU CA C 53.43 0.082 . 697 975 74 LEU CB C 43.414 0.055 . 698 975 74 LEU CG C 28.486 0 . 699 975 74 LEU CD1 C 24.708 0 . 700 975 74 LEU CD2 C 25.308 0 . 701 975 74 LEU N N 130.561 0.018 . 702 976 75 THR H H 8.862 0.009 . 703 976 75 THR HA H 5.043 0.024 . 704 976 75 THR HB H 3.972 0.019 . 705 976 75 THR HG2 H 1.022 0 . 706 976 75 THR CA C 63.238 0.085 . 707 976 75 THR CB C 68.728 0.045 . 708 976 75 THR CG2 C 21.008 0 . 709 976 75 THR N N 122.018 0.017 . 710 977 76 ILE H H 9.925 0.004 . 711 977 76 ILE HA H 4.698 0 . 712 977 76 ILE HB H 1.852 0.001 . 713 977 76 ILE HG12 H 0.828 0 . 714 977 76 ILE HG13 H 1.823 0 . 715 977 76 ILE HG2 H 1.2 0 . 716 977 76 ILE HD1 H 1.007 0 . 717 977 76 ILE CA C 60.867 0.078 . 718 977 76 ILE CB C 41.376 0.03 . 719 977 76 ILE CG1 C 27.679 0 . 720 977 76 ILE CG2 C 20.833 0 . 721 977 76 ILE CD1 C 15.733 0 . 722 977 76 ILE N N 129.323 0.018 . 723 978 77 SER H H 8.692 0.003 . 724 978 77 SER HA H 4.699 0.011 . 725 978 77 SER HB2 H 4.23 0.02 . 726 978 77 SER HB3 H 4.017 0.008 . 727 978 77 SER CA C 57.643 0.06 . 728 978 77 SER CB C 62.564 0.018 . 729 978 77 SER N N 123.403 0.021 . 730 979 78 PRO HA H 4.523 0.002 . 731 979 78 PRO HB2 H 2.101 0 . 732 979 78 PRO HB3 H 2.101 0 . 733 979 78 PRO HG2 H 1.753 0 . 734 979 78 PRO HG3 H 1.753 0 . 735 979 78 PRO HD2 H 3.828 0.008 . 736 979 78 PRO HD3 H 3.828 0.008 . 737 979 78 PRO CA C 65.731 0 . 738 979 78 PRO CB C 30.837 0.033 . 739 979 78 PRO CG C 27.635 0 . 740 979 78 PRO CD C 49.868 0.056 . 741 980 79 ASP H H 8.786 0.01 . 742 980 79 ASP HA H 4.427 0.015 . 743 980 79 ASP HB2 H 2.713 0.067 . 744 980 79 ASP HB3 H 2.612 0.029 . 745 980 79 ASP CA C 56.325 0.049 . 746 980 79 ASP CB C 39.531 0.08 . 747 980 79 ASP N N 115.982 0.009 . 748 981 80 TYR H H 8.148 0.007 . 749 981 80 TYR HA H 4.445 0.009 . 750 981 80 TYR HB2 H 3.025 0.026 . 751 981 80 TYR HB3 H 2.795 0.01 . 752 981 80 TYR HD1 H 6.691 0.016 . 753 981 80 TYR HD2 H 6.691 0.016 . 754 981 80 TYR HE1 H 6.812 0 . 755 981 80 TYR HE2 H 6.812 0 . 756 981 80 TYR CA C 57.339 0.124 . 757 981 80 TYR CB C 38.829 0.02 . 758 981 80 TYR CD1 C 131.027 0 . 759 981 80 TYR CD2 C 131.027 0 . 760 981 80 TYR CE1 C 118.52 0 . 761 981 80 TYR CE2 C 118.52 0 . 762 981 80 TYR N N 121.664 0.039 . 763 982 81 ALA H H 7.838 0.006 . 764 982 81 ALA HA H 4.276 0.015 . 765 982 81 ALA HB H 1.374 0.019 . 766 982 81 ALA CA C 51.897 0.061 . 767 982 81 ALA CB C 19.069 0.048 . 768 982 81 ALA N N 125.598 0.005 . 769 983 82 TYR H H 9.178 0.003 . 770 983 82 TYR HA H 4.587 0.005 . 771 983 82 TYR HB2 H 3.235 0.013 . 772 983 82 TYR HB3 H 2.662 0.009 . 773 983 82 TYR HD1 H 7.107 0.011 . 774 983 82 TYR HD2 H 7.107 0.011 . 775 983 82 TYR CA C 58.808 0.071 . 776 983 82 TYR CB C 37.644 0.024 . 777 983 82 TYR N N 121.9 0.011 . 778 984 83 GLY H H 8.69 0.006 . 779 984 83 GLY CA C 46.905 0 . 780 984 83 GLY N N 108.661 0.02 . 781 985 84 ALA HA H 3.261 0 . 782 985 84 ALA HB H 1.46 0 . 783 985 84 ALA CA C 53.319 0.065 . 784 985 84 ALA CB C 19.278 0.035 . 785 986 85 THR H H 7.89 0.003 . 786 986 85 THR HA H 4.032 0 . 787 986 85 THR HB H 4.253 0 . 788 986 85 THR HG2 H 1.226 0 . 789 986 85 THR CA C 64.253 0.033 . 790 986 85 THR CB C 69.472 0.05 . 791 986 85 THR CG2 C 21.791 0 . 792 986 85 THR N N 109.798 0.012 . 793 987 86 GLY H H 7.354 0.004 . 794 987 86 GLY HA2 H 3.783 0.016 . 795 987 86 GLY HA3 H 3.466 0.019 . 796 987 86 GLY CA C 44.873 0.042 . 797 987 86 GLY N N 106.996 0.006 . 798 988 87 HIS H H 8.816 0.004 . 799 988 87 HIS HA H 4.841 0.002 . 800 988 87 HIS HB2 H 2.315 0.007 . 801 988 87 HIS HB3 H 1.472 0.002 . 802 988 87 HIS CA C 54.123 0.05 . 803 988 87 HIS CB C 32.011 0 . 804 988 87 HIS N N 121.569 0.016 . 805 990 89 GLY H H 8.232 0.004 . 806 990 89 GLY HA2 H 4.263 0.018 . 807 990 89 GLY HA3 H 3.659 0.038 . 808 990 89 GLY CA C 45.066 0.188 . 809 991 90 ILE H H 8.01 0.003 . 810 991 90 ILE HA H 4.275 0 . 811 991 90 ILE HB H 1.383 0.013 . 812 991 90 ILE HG12 H 1.535 0 . 813 991 90 ILE HG13 H 1.012 0 . 814 991 90 ILE HG2 H 0.762 0 . 815 991 90 ILE HD1 H 0.912 0 . 816 991 90 ILE CA C 63.132 0.136 . 817 991 90 ILE CB C 42.289 0.074 . 818 991 90 ILE CG1 C 27.215 0 . 819 991 90 ILE CG2 C 17.622 0 . 820 991 90 ILE CD1 C 13.222 0 . 821 991 90 ILE N N 117.725 0.009 . 822 992 91 ILE H H 8.222 0.003 . 823 992 91 ILE HA H 4.623 0.02 . 824 992 91 ILE HB H 1.472 0.017 . 825 992 91 ILE HG12 H 0.627 0 . 826 992 91 ILE HG13 H 0.627 0 . 827 992 91 ILE HD1 H -0.335 0.017 . 828 992 91 ILE CA C 55.235 0 . 829 992 91 ILE CB C 39.282 0.158 . 830 992 91 ILE CD1 C 9.811 0 . 831 992 91 ILE N N 119.077 0.011 . 832 993 92 PRO HA H 4.787 0 . 833 994 93 PRO HA H 3.598 0.005 . 834 994 93 PRO HB2 H 1.542 0.001 . 835 994 93 PRO HB3 H 2.173 0.004 . 836 994 93 PRO HG2 H 2.021 0 . 837 994 93 PRO HG3 H 1.657 0 . 838 994 93 PRO HD2 H 3.443 0 . 839 994 93 PRO HD3 H 3.748 0 . 840 994 93 PRO CA C 63.605 0.065 . 841 994 93 PRO CB C 33.23 0.023 . 842 994 93 PRO CG C 28.041 0 . 843 994 93 PRO CD C 50.905 0 . 844 995 94 HIS H H 8.001 0.003 . 845 995 94 HIS HA H 3.816 0 . 846 995 94 HIS HB2 H 3.246 0.037 . 847 995 94 HIS HB3 H 3.2 0.032 . 848 995 94 HIS HD2 H 6.908 0.002 . 849 995 94 HIS CA C 57.069 0.031 . 850 995 94 HIS CB C 27.943 0.039 . 851 995 94 HIS CD2 C 119.831 0 . 852 995 94 HIS N N 115.999 0.009 . 853 996 95 ALA H H 7.704 0.006 . 854 996 95 ALA HA H 4.508 0.001 . 855 996 95 ALA HB H 1.309 0.002 . 856 996 95 ALA CA C 52.655 0.014 . 857 996 95 ALA CB C 20.622 0.07 . 858 996 95 ALA N N 122.156 0.007 . 859 997 96 THR H H 8.483 0.003 . 860 997 96 THR HA H 4.711 0.006 . 861 997 96 THR HB H 3.989 0.003 . 862 997 96 THR HG2 H 1.036 0 . 863 997 96 THR CA C 63.7 0.035 . 864 997 96 THR CB C 69.506 0.075 . 865 997 96 THR CG2 C 21.066 0 . 866 997 96 THR N N 123.044 0.022 . 867 998 97 LEU H H 8.8 0.004 . 868 998 97 LEU HA H 5.104 0.009 . 869 998 97 LEU HB2 H 1.484 0.01 . 870 998 97 LEU HB3 H 1.811 0.02 . 871 998 97 LEU HG H 1.865 0 . 872 998 97 LEU HD1 H 1.225 0.019 . 873 998 97 LEU HD2 H 0.913 0 . 874 998 97 LEU CA C 52.749 0.094 . 875 998 97 LEU CB C 46.427 0.046 . 876 998 97 LEU CG C 27.063 0 . 877 998 97 LEU CD1 C 27.401 0.094 . 878 998 97 LEU CD2 C 23.892 0 . 879 998 97 LEU N N 124.741 0.011 . 880 999 98 VAL H H 8.74 0.004 . 881 999 98 VAL HA H 5.266 0 . 882 999 98 VAL HB H 1.763 0.024 . 883 999 98 VAL HG1 H 0.929 0.036 . 884 999 98 VAL HG2 H 0.837 0.042 . 885 999 98 VAL CA C 60.629 0.019 . 886 999 98 VAL CB C 34.322 0.099 . 887 999 98 VAL CG1 C 20.751 0 . 888 999 98 VAL CG2 C 21.219 0 . 889 999 98 VAL N N 121.317 0.007 . 890 1000 99 PHE H H 9.653 0.005 . 891 1000 99 PHE HA H 5.958 0.017 . 892 1000 99 PHE HB2 H 2.892 0 . 893 1000 99 PHE HB3 H 2.798 0.012 . 894 1000 99 PHE CA C 54.985 0.048 . 895 1000 99 PHE CB C 43.394 0.094 . 896 1000 99 PHE N N 122.315 0.031 . 897 1001 100 ASP H H 8.952 0 . 898 1001 100 ASP HA H 5.144 0 . 899 1001 100 ASP HB2 H 2.886 0 . 900 1001 100 ASP HB3 H 2.473 0 . 901 1001 100 ASP CA C 52.729 0.057 . 902 1001 100 ASP CB C 42.366 0.093 . 903 1001 100 ASP N N 125.175 0.019 . 904 1002 101 VAL H H 9.525 0.003 . 905 1002 101 VAL HA H 5.033 0 . 906 1002 101 VAL HB H 1.603 0 . 907 1002 101 VAL HG1 H 0.474 0 . 908 1002 101 VAL HG2 H 0.441 0 . 909 1002 101 VAL CA C 61.31 0.042 . 910 1002 101 VAL CB C 35.113 0.067 . 911 1002 101 VAL CG1 C 20.759 0 . 912 1002 101 VAL CG2 C 22.485 0 . 913 1002 101 VAL N N 126.722 0.013 . 914 1003 102 GLU H H 9.132 0.004 . 915 1003 102 GLU HA H 5.405 0.001 . 916 1003 102 GLU HB2 H 1.858 0 . 917 1003 102 GLU HB3 H 2.032 0 . 918 1003 102 GLU HG2 H 1.831 0 . 919 1003 102 GLU HG3 H 1.977 0 . 920 1003 102 GLU CA C 53.778 0.017 . 921 1003 102 GLU CB C 33.797 0.011 . 922 1003 102 GLU CG C 35.707 0 . 923 1003 102 GLU N N 128.123 0.011 . 924 1004 103 LEU H H 8.668 0.005 . 925 1004 103 LEU HA H 4.666 0.007 . 926 1004 103 LEU HB2 H 1.033 0 . 927 1004 103 LEU HB3 H 2.255 0.002 . 928 1004 103 LEU HG H 1.325 0.009 . 929 1004 103 LEU HD1 H 0.638 0 . 930 1004 103 LEU HD2 H 0.805 0.009 . 931 1004 103 LEU CA C 54.244 0.105 . 932 1004 103 LEU CB C 41.454 0.045 . 933 1004 103 LEU CG C 28.401 0.035 . 934 1004 103 LEU CD1 C 26.044 0 . 935 1004 103 LEU CD2 C 23.389 0.08 . 936 1004 103 LEU N N 128.444 0.005 . 937 1005 104 LEU H H 9.139 0.002 . 938 1005 104 LEU HA H 4.212 0.01 . 939 1005 104 LEU HB2 H 1.515 0 . 940 1005 104 LEU HB3 H 1.447 0 . 941 1005 104 LEU HG H 1.366 0 . 942 1005 104 LEU HD1 H 0.653 0 . 943 1005 104 LEU HD2 H 0.805 0.01 . 944 1005 104 LEU CA C 57.083 0.048 . 945 1005 104 LEU CB C 42.828 0.03 . 946 1005 104 LEU CG C 26.672 0 . 947 1005 104 LEU CD1 C 25.84 0 . 948 1005 104 LEU CD2 C 22.29 0.041 . 949 1005 104 LEU N N 128.947 0.007 . 950 1006 105 LYS H H 7.728 0.005 . 951 1006 105 LYS HA H 4.359 0.011 . 952 1006 105 LYS HB2 H 1.798 0 . 953 1006 105 LYS HB3 H 1.704 0 . 954 1006 105 LYS HG2 H 1.227 0 . 955 1006 105 LYS HG3 H 1.148 0 . 956 1006 105 LYS HD2 H 1.579 0 . 957 1006 105 LYS HD3 H 1.579 0 . 958 1006 105 LYS HE2 H 2.92 0 . 959 1006 105 LYS HE3 H 2.859 0 . 960 1006 105 LYS CA C 55.565 0.038 . 961 1006 105 LYS CB C 35.152 0.046 . 962 1006 105 LYS CG C 23.9 0 . 963 1006 105 LYS CD C 29.319 0 . 964 1006 105 LYS CE C 42.049 0 . 965 1006 105 LYS N N 112.298 0.009 . 966 1007 106 LEU H H 8.244 0.003 . 967 1007 106 LEU HA H 5.245 0.014 . 968 1007 106 LEU HB2 H 1.558 0.013 . 969 1007 106 LEU HB3 H 1.213 0.003 . 970 1007 106 LEU HG H 1.353 0 . 971 1007 106 LEU HD1 H 0.876 0.018 . 972 1007 106 LEU HD2 H 0.644 0.013 . 973 1007 106 LEU CA C 53.063 0.129 . 974 1007 106 LEU CB C 44.088 0.02 . 975 1007 106 LEU CD1 C 25.927 0 . 976 1007 106 LEU CD2 C 25.762 0.003 . 977 1007 106 LEU N N 120.422 0.019 . 978 1008 107 GLU H H 9.007 0.005 . 979 1008 107 GLU CA C 56.713 0 . 980 1008 107 GLU CB C 32.509 0 . 981 1008 107 GLU N N 127.004 0.01 . stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N 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 entity_2 _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 1009 1 VAL H H 8.144 0.018 . 2 1009 1 VAL C C 175.531 0 . 3 1009 1 VAL CA C 62.13 0.008 . 4 1009 1 VAL N N 121.927 0.143 . 5 1010 2 ALA H H 8.351 0.03 . 6 1010 2 ALA C C 176.779 0 . 7 1010 2 ALA CA C 52.444 0.019 . 8 1010 2 ALA N N 127.8 0.039 . 9 1011 3 ILE H H 8.189 0.042 . 10 1011 3 ILE C C 176.12 0 . 11 1011 3 ILE CA C 61.011 0 . 12 1011 3 ILE N N 119.386 0.052 . 13 1012 4 LEU H H 8.457 0.014 . 14 1012 4 LEU C C 178.5 0 . 15 1012 4 LEU CA C 54.221 0 . 16 1012 4 LEU N N 125.839 0.254 . 17 1013 5 TRP H H 9.433 0.057 . 18 1013 5 TRP C C 178.127 0 . 19 1013 5 TRP CA C 60.265 0 . 20 1013 5 TRP N N 125.006 0.1 . 21 1014 6 HIS H H 8.56 0.088 . 22 1014 6 HIS C C 176.665 0 . 23 1014 6 HIS CA C 60.832 0.076 . 24 1014 6 HIS N N 114.451 0.122 . 25 1015 7 GLU H H 6.476 0.02 . 26 1015 7 GLU CA C 58.944 0.109 . 27 1015 7 GLU N N 120.182 0.151 . 28 1016 8 MET H H 8.262 0.01 . 29 1016 8 MET C C 180.249 0 . 30 1016 8 MET CA C 58.917 0.018 . 31 1016 8 MET N N 118.63 0.083 . 32 1017 9 TRP H H 8.452 0.009 . 33 1017 9 TRP C C 177.797 0 . 34 1017 9 TRP CA C 61.448 0.01 . 35 1017 9 TRP N N 118.249 0.039 . 36 1018 10 HIS H H 8.352 0.015 . 37 1018 10 HIS C C 176.521 0 . 38 1018 10 HIS CA C 62.177 0.015 . 39 1018 10 HIS N N 120.651 0.183 . 40 1019 11 GLU H H 8.161 0.011 . 41 1019 11 GLU C C 180.02 0 . 42 1019 11 GLU CA C 58.914 0 . 43 1019 11 GLU N N 116.102 0.268 . 44 1020 12 GLY H H 8.362 0.015 . 45 1020 12 GLY C C 175.202 0 . 46 1020 12 GLY CA C 46.888 0.013 . 47 1020 12 GLY N N 107.438 0.05 . 48 1021 13 LEU H H 8.919 0.035 . 49 1021 13 LEU C C 179.934 0 . 50 1021 13 LEU CA C 58.383 0 . 51 1021 13 LEU CB C 40.963 0 . 52 1021 13 LEU N N 120.376 0.136 . 53 1022 14 GLU H H 7.627 0.023 . 54 1022 14 GLU C C 179.193 0 . 55 1022 14 GLU CA C 61.424 0 . 56 1022 14 GLU N N 119.998 0.042 . 57 1023 15 GLU H H 8.168 0 . 58 1023 15 GLU C C 178.643 0 . 59 1023 15 GLU CA C 59.136 0 . 60 1023 15 GLU N N 120.862 0 . 61 1024 16 ALA H H 9.441 0.028 . 62 1024 16 ALA C C 179.661 0 . 63 1024 16 ALA CA C 55.706 0.048 . 64 1024 16 ALA CB C 17.967 0 . 65 1024 16 ALA N N 120.837 0.14 . 66 1025 17 SER H H 8.546 0.026 . 67 1025 17 SER C C 176.292 0 . 68 1025 17 SER CA C 61.751 0.058 . 69 1025 17 SER N N 113.136 0.062 . 70 1026 18 ARG H H 8.016 0.017 . 71 1026 18 ARG CA C 60.551 0 . 72 1026 18 ARG CB C 29.364 0 . 73 1026 18 ARG N N 128.65 0.172 . 74 1027 19 LEU C C 175.833 0 . 75 1027 19 LEU CA C 55.856 0 . 76 1028 20 TYR H H 8.186 0.007 . 77 1028 20 TYR CA C 62.04 0 . 78 1028 20 TYR N N 122.246 0.057 . 79 1030 22 GLY H H 7.796 0.035 . 80 1030 22 GLY C C 175.862 0 . 81 1030 22 GLY CA C 46.438 0.004 . 82 1030 22 GLY N N 105.781 0.074 . 83 1031 23 GLU H H 7.114 0.047 . 84 1031 23 GLU C C 179.877 0 . 85 1031 23 GLU CA C 55.832 0 . 86 1031 23 GLU CB C 29.954 0 . 87 1031 23 GLU N N 116.334 0.118 . 88 1032 24 ARG H H 7.134 0.039 . 89 1032 24 ARG C C 175.374 0 . 90 1032 24 ARG CA C 57.2 0 . 91 1032 24 ARG N N 116.67 0.077 . 92 1033 25 ASN H H 8.635 0.031 . 93 1033 25 ASN C C 175.002 0 . 94 1033 25 ASN CA C 51.081 0.056 . 95 1033 25 ASN CB C 37.911 0 . 96 1033 25 ASN N N 118.394 0.094 . 97 1034 26 VAL H H 8.293 0.029 . 98 1034 26 VAL C C 176.923 0 . 99 1034 26 VAL CA C 66.14 0.019 . 100 1034 26 VAL CB C 31.872 0 . 101 1034 26 VAL N N 124.215 0.141 . 102 1035 27 LYS H H 8.411 0.03 . 103 1035 27 LYS C C 179.905 0 . 104 1035 27 LYS CA C 60.048 0.024 . 105 1035 27 LYS CB C 31.843 0 . 106 1035 27 LYS N N 121.378 0.135 . 107 1036 28 GLY H H 8.283 0.01 . 108 1036 28 GLY C C 175.789 0 . 109 1036 28 GLY CA C 47.656 0.011 . 110 1036 28 GLY N N 106.352 0.039 . 111 1037 29 MET H H 7.558 0.016 . 112 1037 29 MET C C 177.955 0 . 113 1037 29 MET CA C 60.265 0 . 114 1037 29 MET CB C 32.337 0 . 115 1037 29 MET N N 121.861 0.171 . 116 1038 30 PHE H H 8.354 0.023 . 117 1038 30 PHE C C 179.045 0 . 118 1038 30 PHE CA C 61.448 0 . 119 1038 30 PHE N N 118.668 0.062 . 120 1039 31 GLU H H 8.094 0.038 . 121 1039 31 GLU C C 178.915 0 . 122 1039 31 GLU CA C 59.114 0.021 . 123 1039 31 GLU CB C 28.702 0 . 124 1039 31 GLU N N 120.857 0.118 . 125 1040 32 VAL H H 7.449 0.019 . 126 1040 32 VAL C C 177.668 0 . 127 1040 32 VAL CA C 65.074 0.006 . 128 1040 32 VAL N N 117.481 0.091 . 129 1041 33 LEU H H 7.649 0.026 . 130 1041 33 LEU C C 178.643 0 . 131 1041 33 LEU CA C 57.473 0.017 . 132 1041 33 LEU CB C 42.28 0 . 133 1041 33 LEU N N 116.834 0.13 . 134 1042 34 GLU H H 8.782 0.012 . 135 1042 34 GLU CA C 62.47 0 . 136 1042 34 GLU CB C 26.441 0 . 137 1042 34 GLU N N 119.109 0.102 . 138 1043 35 PRO C C 179.331 0 . 139 1043 35 PRO CA C 65.474 0 . 140 1044 36 LEU H H 6.686 0.04 . 141 1044 36 LEU C C 178.543 0 . 142 1044 36 LEU CA C 57.085 0.021 . 143 1044 36 LEU CB C 38.574 0 . 144 1044 36 LEU N N 119.43 0.125 . 145 1045 37 HIS H H 7.716 0.048 . 146 1045 37 HIS C C 179.331 0 . 147 1045 37 HIS CA C 60.797 0.038 . 148 1045 37 HIS CB C 28.513 0 . 149 1045 37 HIS N N 117.196 0.076 . 150 1046 38 ALA H H 8.505 0.032 . 151 1046 38 ALA C C 180.765 0 . 152 1046 38 ALA CA C 55.422 0.081 . 153 1046 38 ALA N N 122.694 0.046 . 154 1047 39 MET H H 7.638 0.041 . 155 1047 39 MET C C 177.353 0 . 156 1047 39 MET CA C 58.41 0.005 . 157 1047 39 MET N N 118.284 0.073 . 158 1048 40 MET H H 7.115 0.044 . 159 1048 40 MET C C 179.503 0 . 160 1048 40 MET CA C 56.424 0.032 . 161 1048 40 MET N N 115.801 0.134 . 162 1049 41 GLU H H 7.799 0.035 . 163 1049 41 GLU C C 178.184 0 . 164 1049 41 GLU CA C 59.04 0.017 . 165 1049 41 GLU CB C 29.143 0 . 166 1049 41 GLU N N 120.239 0.1 . 167 1050 42 ARG H H 7.629 0.034 . 168 1050 42 ARG C C 177.611 0 . 169 1050 42 ARG CA C 58.145 0.01 . 170 1050 42 ARG CB C 29.426 0 . 171 1050 42 ARG N N 117.297 0.097 . 172 1051 43 GLY H H 7.599 0.039 . 173 1051 43 GLY CA C 43.991 0 . 174 1051 43 GLY N N 106.396 0.067 . 175 1052 44 PRO C C 177.812 0 . 176 1052 44 PRO CA C 62.857 0.01 . 177 1053 45 GLN H H 9.758 0.035 . 178 1053 45 GLN C C 175.763 0 . 179 1053 45 GLN CA C 55.756 0 . 180 1053 45 GLN CB C 30.364 0 . 181 1053 45 GLN N N 119.393 0.052 . 182 1054 46 THR H H 7.231 0.043 . 183 1054 46 THR CA C 58.998 0 . 184 1054 46 THR CB C 71.75 0 . 185 1054 46 THR N N 108.676 0.058 . 186 1056 48 LYS C C 180.134 0 . 187 1056 48 LYS CA C 59.62 0 . 188 1057 49 GLU H H 7.841 0.041 . 189 1057 49 GLU C C 178.729 0 . 190 1057 49 GLU CA C 59.374 0.074 . 191 1057 49 GLU N N 121.458 0.102 . 192 1058 50 THR H H 8.455 0.043 . 193 1058 50 THR C C 176.636 0 . 194 1058 50 THR CA C 67.497 0.049 . 195 1058 50 THR N N 118.911 0.067 . 196 1059 51 SER H H 8.465 0.016 . 197 1059 51 SER C C 177.123 0 . 198 1059 51 SER CA C 61.884 0.027 . 199 1059 51 SER N N 118.163 0.032 . 200 1060 52 PHE H H 8.175 0.053 . 201 1060 52 PHE C C 177.267 0 . 202 1060 52 PHE CA C 61.95 0.05 . 203 1060 52 PHE CB C 38.999 0 . 204 1060 52 PHE N N 124.08 0.073 . 205 1061 53 ASN H H 9.135 0.051 . 206 1061 53 ASN C C 178.787 0 . 207 1061 53 ASN CA C 57.269 0.055 . 208 1061 53 ASN CB C 39.734 0.033 . 209 1061 53 ASN N N 118.724 0.096 . 210 1062 54 GLN H H 8.634 0.052 . 211 1062 54 GLN C C 177.439 0 . 212 1062 54 GLN CA C 58.903 0.005 . 213 1062 54 GLN CB C 27.998 0 . 214 1062 54 GLN N N 118.906 0.1 . 215 1063 55 ALA H H 7.417 0.06 . 216 1063 55 ALA C C 179.721 0 . 217 1063 55 ALA CA C 54.454 0.006 . 218 1063 55 ALA N N 120.135 0.101 . 219 1064 56 TYR H H 7.826 0.064 . 220 1064 56 TYR C C 176.349 0 . 221 1064 56 TYR CA C 57.169 0.01 . 222 1064 56 TYR CB C 39.82 0 . 223 1064 56 TYR N N 112.882 0.072 . 224 1065 57 GLY H H 8.289 0.058 . 225 1065 57 GLY C C 176.407 0 . 226 1065 57 GLY CA C 48.079 0 . 227 1065 57 GLY N N 107.804 0.09 . 228 1066 58 ARG H H 8.51 0.012 . 229 1066 58 ARG C C 178.758 0 . 230 1066 58 ARG CA C 59.768 0.005 . 231 1066 58 ARG CB C 28.542 0 . 232 1066 58 ARG N N 122.605 0.066 . 233 1067 59 ASP H H 8.054 0.056 . 234 1067 59 ASP C C 178.5 0 . 235 1067 59 ASP CA C 57.696 0.006 . 236 1067 59 ASP CB C 40.674 0 . 237 1067 59 ASP N N 120.682 0.109 . 238 1068 60 LEU H H 8.081 0.053 . 239 1068 60 LEU C C 179.059 0 . 240 1068 60 LEU CA C 57.815 0.043 . 241 1068 60 LEU CB C 40.864 0 . 242 1068 60 LEU N N 117.792 0.094 . 243 1069 61 MET H H 8.33 0.059 . 244 1069 61 MET C C 179.561 0 . 245 1069 61 MET CA C 59.036 0.033 . 246 1069 61 MET CB C 32.876 0 . 247 1069 61 MET N N 120.209 0.091 . 248 1070 62 GLU H H 8.327 0.018 . 249 1070 62 GLU C C 178.672 0 . 250 1070 62 GLU CA C 59.469 0.024 . 251 1070 62 GLU CB C 28.497 0 . 252 1070 62 GLU N N 121.76 0.085 . 253 1071 63 ALA H H 8.36 0.047 . 254 1071 63 ALA C C 179.733 0 . 255 1071 63 ALA CA C 56.528 0.006 . 256 1071 63 ALA N N 123.741 0.052 . 257 1072 64 GLN H H 8.024 0.02 . 258 1072 64 GLN C C 178.184 0 . 259 1072 64 GLN CA C 59.539 0.005 . 260 1072 64 GLN CB C 27.325 0 . 261 1072 64 GLN N N 117.668 0.093 . 262 1073 65 GLU H H 7.954 0.018 . 263 1073 65 GLU C C 180.048 0 . 264 1073 65 GLU CA C 59.551 0.022 . 265 1073 65 GLU CB C 27.959 0 . 266 1073 65 GLU N N 120.797 0.14 . 267 1074 66 TRP H H 8.22 0.037 . 268 1074 66 TRP C C 178.93 0 . 269 1074 66 TRP CA C 61.692 0.004 . 270 1074 66 TRP CB C 28.702 0 . 271 1074 66 TRP N N 121.37 0.108 . 272 1075 67 CYS H H 8.176 0.042 . 273 1075 67 CYS C C 177.295 0 . 274 1075 67 CYS CA C 64.93 0.018 . 275 1075 67 CYS N N 118.469 0.105 . 276 1076 68 ARG H H 8.562 0.042 . 277 1076 68 ARG C C 180.048 0 . 278 1076 68 ARG CA C 59.869 0.036 . 279 1076 68 ARG CB C 29.174 0 . 280 1076 68 ARG N N 120.349 0.114 . 281 1077 69 LYS H H 8.356 0.045 . 282 1077 69 LYS C C 179.675 0 . 283 1077 69 LYS CA C 60.623 0.06 . 284 1077 69 LYS CB C 31.485 0 . 285 1077 69 LYS N N 122.159 0.05 . 286 1078 70 TYR H H 8.413 0.014 . 287 1078 70 TYR C C 177.984 0 . 288 1078 70 TYR CA C 60.971 0.043 . 289 1078 70 TYR CB C 37.329 0 . 290 1078 70 TYR N N 121.392 0.116 . 291 1079 71 MET H H 8.071 0.049 . 292 1079 71 MET C C 177.439 0 . 293 1079 71 MET CA C 58.165 0.005 . 294 1079 71 MET CB C 31.18 0 . 295 1079 71 MET N N 118.555 0.113 . 296 1080 72 LYS H H 7.246 0.052 . 297 1080 72 LYS C C 177.668 0 . 298 1080 72 LYS CA C 57.492 0.021 . 299 1080 72 LYS CB C 32.876 0.11 . 300 1080 72 LYS N N 115.953 0.053 . 301 1081 73 SER H H 9 0.057 . 302 1081 73 SER C C 176.751 0 . 303 1081 73 SER CA C 59.392 0.012 . 304 1081 73 SER CB C 63.92 0 . 305 1081 73 SER N N 116.007 0.063 . 306 1082 74 GLY H H 8.873 0.062 . 307 1082 74 GLY C C 173.568 0 . 308 1082 74 GLY CA C 46.247 0.044 . 309 1082 74 GLY N N 113.707 0.094 . 310 1083 75 ASN H H 8.951 0.079 . 311 1083 75 ASN C C 176.808 0 . 312 1083 75 ASN CA C 52.307 0.019 . 313 1083 75 ASN CB C 37.901 0 . 314 1083 75 ASN N N 119.463 0.135 . 315 1084 76 VAL H H 9.261 0.109 . 316 1084 76 VAL N N 128.268 0.113 . 317 1085 77 LYS C C 179.245 0 . 318 1085 77 LYS CA C 59.099 0 . 319 1085 77 LYS CB C 31.096 0 . 320 1086 78 ASP H H 8.095 0.097 . 321 1086 78 ASP C C 177.754 0 . 322 1086 78 ASP CA C 58.226 0.027 . 323 1086 78 ASP CB C 40.447 0 . 324 1086 78 ASP N N 120.311 0.148 . 325 1087 79 LEU H H 6.832 0.096 . 326 1087 79 LEU CA C 56.786 0 . 327 1087 79 LEU N N 118.682 0.089 . 328 1088 80 THR H H 8.632 0.118 . 329 1088 80 THR C C 178.914 0 . 330 1088 80 THR N N 115.18 0.112 . 331 1089 81 GLN H H 7.328 0 . 332 1089 81 GLN C C 178.959 0 . 333 1089 81 GLN CA C 58.622 0 . 334 1089 81 GLN N N 120.325 0 . 335 1090 82 ALA H H 7.217 0.085 . 336 1090 82 ALA C C 178.701 0 . 337 1090 82 ALA CA C 56.053 0.005 . 338 1090 82 ALA CB C 19.074 0 . 339 1090 82 ALA N N 120.36 0.109 . 340 1091 83 TRP H H 8.061 0.083 . 341 1091 83 TRP CA C 61.886 0 . 342 1091 83 TRP CB C 28.98 0 . 343 1091 83 TRP N N 114.619 0.071 . 344 1092 84 ASP C C 179.002 0 . 345 1092 84 ASP CA C 58.453 0 . 346 1093 85 LEU H H 6.911 0.082 . 347 1093 85 LEU C C 180.048 0 . 348 1093 85 LEU CA C 58.145 0.023 . 349 1093 85 LEU CB C 42.345 0 . 350 1093 85 LEU N N 119.975 0.085 . 351 1094 86 TYR H H 8.835 0.071 . 352 1094 86 TYR C C 179.217 0 . 353 1094 86 TYR CA C 60.584 0.081 . 354 1094 86 TYR N N 118.597 0.083 . 355 1095 87 TYR H H 9.326 0.076 . 356 1095 87 TYR C C 177.095 0 . 357 1095 87 TYR CA C 58.614 0.021 . 358 1095 87 TYR CB C 37.583 0 . 359 1095 87 TYR N N 118.857 0.059 . 360 1096 88 HIS H H 7.73 0.079 . 361 1096 88 HIS C C 179.145 0 . 362 1096 88 HIS CA C 59.982 0.002 . 363 1096 88 HIS CB C 30.207 0 . 364 1096 88 HIS N N 118.823 0.169 . 365 1097 89 VAL H H 7.996 0.073 . 366 1097 89 VAL C C 176.751 0 . 367 1097 89 VAL CA C 67.511 0.064 . 368 1097 89 VAL N N 119.577 0.102 . 369 1098 90 PHE H H 9.078 0.06 . 370 1098 90 PHE C C 178.184 0 . 371 1098 90 PHE CA C 62.586 0.024 . 372 1098 90 PHE CB C 39.881 0 . 373 1098 90 PHE N N 119.797 0.084 . 374 1099 91 ARG H H 8.644 0.072 . 375 1099 91 ARG C C 178.701 0 . 376 1099 91 ARG CA C 59.571 0.017 . 377 1099 91 ARG N N 117.128 0.127 . 378 1100 92 ARG H H 7.374 0.077 . 379 1100 92 ARG C C 178.959 0 . 380 1100 92 ARG CA C 58.955 0.036 . 381 1100 92 ARG CB C 30.232 0 . 382 1100 92 ARG N N 118.068 0.084 . 383 1101 93 ILE H H 7.99 0.093 . 384 1101 93 ILE C C 177.238 0 . 385 1101 93 ILE CA C 64.013 0.023 . 386 1101 93 ILE N N 116.399 0.22 . 387 1102 94 SER H H 7.521 0.078 . 388 1102 94 SER C C 173.74 0 . 389 1102 94 SER CA C 59.564 0.026 . 390 1102 94 SER CB C 63.304 0 . 391 1102 94 SER N N 115.276 0.192 . stop_ save_