data_6541 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignments for stereo array isotope labeled (SAIL) calmodulin ; _BMRB_accession_number 6541 _BMRB_flat_file_name bmr6541.str _Entry_type original _Submission_date 2005-03-09 _Accession_date 2005-03-09 _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 Kainosho Masatsune . . 2 Torizawa Takuya . . 3 Terauchi Tsutomu . . 4 Ono 'Akira Mei' . . 5 Guntert Peter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 623 "13C chemical shifts" 591 "15N chemical shifts" 158 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-25 original author . stop_ _Original_release_date 2006-04-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Optimal isotope labelling for NMR protein structure determinations' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16511487 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kainosho Masatsune . . 2 Torizawa Takuya . . 3 Iwashita Yuki . . 4 Terauchi Tsutomu . . 5 Ono 'Akira Mei' . . 6 Guntert Peter . . stop_ _Journal_abbreviation Nature _Journal_volume 440 _Journal_issue 7080 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 52 _Page_last 57 _Year 2006 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title 'Efficient production of isotopically labeled proteins by cell-free synthesis: A practical protocol' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15754057 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Torizawa Takuya . . 2 Shimizu Masato . . 3 Taoka Masato . . 4 Miyano Hiroshi . . 5 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 30 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 311 _Page_last 325 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ca-bound calmodulin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label calmodulin $calmodulin 'Ca ion, 1' $CA 'Ca ion, 2' $CA 'Ca ion, 3' $CA 'Ca ion, 4' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_calmodulin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common calmodulin _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 GLN 4 LEU 5 THR 6 GLU 7 GLU 8 GLN 9 ILE 10 ALA 11 GLU 12 PHE 13 LYS 14 GLU 15 ALA 16 PHE 17 SER 18 LEU 19 PHE 20 ASP 21 LYS 22 ASP 23 GLY 24 ASP 25 GLY 26 THR 27 ILE 28 THR 29 THR 30 LYS 31 GLU 32 LEU 33 GLY 34 THR 35 VAL 36 MET 37 ARG 38 SER 39 LEU 40 GLY 41 GLN 42 ASN 43 PRO 44 THR 45 GLU 46 ALA 47 GLU 48 LEU 49 GLN 50 ASP 51 MET 52 ILE 53 ASN 54 GLU 55 VAL 56 ASP 57 ALA 58 ASP 59 GLY 60 ASN 61 GLY 62 THR 63 ILE 64 ASP 65 PHE 66 PRO 67 GLU 68 PHE 69 LEU 70 THR 71 MET 72 MET 73 ALA 74 ARG 75 LYS 76 MET 77 LYS 78 ASP 79 THR 80 ASP 81 SER 82 GLU 83 GLU 84 GLU 85 ILE 86 ARG 87 GLU 88 ALA 89 PHE 90 ARG 91 VAL 92 PHE 93 ASP 94 LYS 95 ASP 96 GLY 97 ASN 98 GLY 99 TYR 100 ILE 101 SER 102 ALA 103 ALA 104 GLU 105 LEU 106 ARG 107 HIS 108 VAL 109 MET 110 THR 111 ASN 112 LEU 113 GLY 114 GLU 115 LYS 116 LEU 117 THR 118 ASP 119 GLU 120 GLU 121 VAL 122 ASP 123 GLU 124 MET 125 ILE 126 ARG 127 GLU 128 ALA 129 ASP 130 ILE 131 ASP 132 GLY 133 ASP 134 GLY 135 GLN 136 VAL 137 ASN 138 TYR 139 GLU 140 GLU 141 PHE 142 VAL 143 GLN 144 MET 145 MET 146 THR 147 ALA 148 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 15183 calmodulin 100.00 149 98.65 100.00 2.21e-99 BMRB 15184 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 15185 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 15186 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 15187 calmodulin 100.00 149 98.65 100.00 2.21e-99 BMRB 15188 calmodulin 100.00 148 99.32 100.00 6.65e-100 BMRB 15191 Calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 15470 calmodulin 100.00 148 99.32 100.00 1.37e-99 BMRB 15624 Calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 15650 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 15852 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 1634 calmodulin 100.00 148 97.30 99.32 1.73e-97 BMRB 16418 apoCaM 100.00 148 100.00 100.00 3.34e-100 BMRB 16465 entity_1 100.00 148 100.00 100.00 3.34e-100 BMRB 1648 calmodulin 100.00 148 97.30 99.32 1.73e-97 BMRB 16764 CALMODULIN 100.00 150 100.00 100.00 3.57e-100 BMRB 17264 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 17360 entity_1 100.00 148 100.00 100.00 3.34e-100 BMRB 17771 Calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 17807 Calmodulin 99.32 147 100.00 100.00 1.74e-99 BMRB 18027 CaM 100.00 148 100.00 100.00 3.34e-100 BMRB 18028 CaM 100.00 148 100.00 100.00 3.34e-100 BMRB 18556 Calmodulin 100.00 148 98.65 99.32 1.80e-98 BMRB 19036 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 19238 Calmodulin_prototypical_calcium_sensor 100.00 148 100.00 100.00 3.34e-100 BMRB 19586 entity_1 100.00 148 100.00 100.00 3.34e-100 BMRB 19604 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 26503 Calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 4056 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 5227 CaM 100.00 148 100.00 100.00 3.34e-100 BMRB 547 calmodulin 100.00 148 97.30 99.32 1.73e-97 BMRB 6778 calmodulin 100.00 148 97.30 99.32 1.73e-97 BMRB 6798 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 6802 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 6825 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 6830 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 6831 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 7018 calmodulin 100.00 148 100.00 100.00 3.34e-100 BMRB 7028 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 7029 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 7030 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 7031 calmodulin 100.00 148 98.65 99.32 2.39e-98 BMRB 7416 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 7417 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 7418 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 7423 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 7424 calmodulin 100.00 148 99.32 100.00 2.26e-99 BMRB 7425 calmodulin 100.00 148 99.32 100.00 2.26e-99 PDB 1A29 "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" 100.00 148 100.00 100.00 3.34e-100 PDB 1CFC "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 1CFD "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 1CFF "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" 100.00 148 100.00 100.00 3.34e-100 PDB 1CKK "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" 100.00 148 100.00 100.00 3.34e-100 PDB 1CLL "Calmodulin Structure Refined At 1.7 Angstroms Resolution" 100.00 148 100.00 100.00 3.34e-100 PDB 1CM1 "Motions Of Calmodulin-Single-Conformer Refinement" 100.00 148 100.00 100.00 3.34e-100 PDB 1CM4 "Motions Of Calmodulin-four-conformer Refinement" 100.00 148 100.00 100.00 3.34e-100 PDB 1CTR "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 1DMO "Calmodulin, Nmr, 30 Structures" 100.00 148 99.32 100.00 1.37e-99 PDB 1G4Y "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 1IQ5 "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" 100.00 149 100.00 100.00 3.49e-100 PDB 1IWQ "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" 100.00 148 100.00 100.00 3.34e-100 PDB 1K90 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 148 100.00 100.00 3.34e-100 PDB 1K93 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 97.30 144 100.00 100.00 3.01e-97 PDB 1L7Z "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" 100.00 148 100.00 100.00 3.34e-100 PDB 1LIN "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" 100.00 148 100.00 100.00 3.34e-100 PDB 1LVC "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 2' Deoxy, 3' Anthr" 100.00 149 100.00 100.00 3.49e-100 PDB 1MUX "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" 100.00 148 100.00 100.00 3.34e-100 PDB 1MXE "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" 100.00 148 97.97 99.32 4.61e-98 PDB 1NWD "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" 100.00 148 100.00 100.00 3.34e-100 PDB 1OOJ "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" 100.00 149 97.97 98.65 8.69e-98 PDB 1PRW "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" 100.00 149 99.32 99.32 2.91e-99 PDB 1QIV "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 1QIW "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" 100.00 148 100.00 100.00 3.34e-100 PDB 1QX5 "Crystal Structure Of Apocalmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 1S26 "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" 100.00 148 100.00 100.00 3.34e-100 PDB 1SK6 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" 100.00 148 100.00 100.00 3.34e-100 PDB 1SY9 "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" 100.00 148 100.00 100.00 3.34e-100 PDB 1UP5 "Chicken Calmodulin" 100.00 148 99.32 99.32 2.81e-99 PDB 1WRZ "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" 100.00 149 100.00 100.00 3.49e-100 PDB 1X02 "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 1XA5 "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" 100.00 148 100.00 100.00 3.34e-100 PDB 1XFU "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" 100.00 149 99.32 100.00 8.28e-100 PDB 1XFV "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 149 99.32 100.00 8.28e-100 PDB 1XFW "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" 100.00 149 99.32 100.00 8.28e-100 PDB 1XFY "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 100.00 149 99.32 100.00 8.28e-100 PDB 1XFZ "Crystal Structure Of Anthrax Edema Factor (ef) In Complex With Calmodulin In The Presence Of 1 Millimolar Exogenously Added Cal" 100.00 149 99.32 100.00 8.28e-100 PDB 1Y0V "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" 97.30 146 100.00 100.00 2.59e-97 PDB 1YR5 "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" 100.00 148 100.00 100.00 3.34e-100 PDB 2BBM "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 4.61e-98 PDB 2BBN "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 4.61e-98 PDB 2BCX "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" 100.00 148 100.00 100.00 3.34e-100 PDB 2BKH "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" 100.00 149 97.97 99.32 3.51e-98 PDB 2BKI "Myosin Vi Nucleotide-Free (Mdinsert2-Iq) Crystal Structure" 100.00 149 100.00 100.00 3.49e-100 PDB 2DFS "3-D Structure Of Myosin-V Inhibited State" 100.00 148 100.00 100.00 3.34e-100 PDB 2F2O "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 100.00 100.00 5.38e-100 PDB 2F2P "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 100.00 100.00 5.38e-100 PDB 2F3Y "CalmodulinIQ DOMAIN COMPLEX" 100.00 148 100.00 100.00 3.34e-100 PDB 2F3Z "CalmodulinIQ-Aa Domain Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 2FOT "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" 100.00 148 100.00 100.00 3.34e-100 PDB 2HQW "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" 100.00 148 100.00 100.00 3.34e-100 PDB 2JZI "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" 100.00 148 100.00 100.00 3.34e-100 PDB 2K0E "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" 100.00 148 100.00 100.00 3.34e-100 PDB 2K0F "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" 100.00 148 100.00 100.00 3.34e-100 PDB 2K0J "Solution Structure Of Cam Complexed To Drp1p" 100.00 148 99.32 100.00 2.26e-99 PDB 2K61 "Solution Structure Of Cam Complexed To Dapk Peptide" 100.00 148 99.32 100.00 2.26e-99 PDB 2KDU "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" 100.00 148 100.00 100.00 3.34e-100 PDB 2KNE "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" 100.00 148 100.00 100.00 3.34e-100 PDB 2L53 "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" 100.00 148 100.00 100.00 3.34e-100 PDB 2L7L "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" 100.00 148 100.00 100.00 3.34e-100 PDB 2LGF "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" 98.65 146 100.00 100.00 7.26e-99 PDB 2LL6 "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 3.34e-100 PDB 2LL7 "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 3.34e-100 PDB 2LV6 "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" 100.00 148 98.65 99.32 1.80e-98 PDB 2M0J "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 2M0K "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" 100.00 148 100.00 100.00 3.34e-100 PDB 2M55 "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 2MG5 "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" 100.00 148 100.00 100.00 3.34e-100 PDB 2MGU "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" 100.00 148 100.00 100.00 3.34e-100 PDB 2O5G "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 2O60 "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" 100.00 148 100.00 100.00 3.34e-100 PDB 2R28 "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" 100.00 149 100.00 100.00 3.49e-100 PDB 2V01 "Recombinant Vertebrate Calmodulin Complexed With Pb" 100.00 149 100.00 100.00 3.49e-100 PDB 2V02 "Recombinant Vertebrate Calmodulin Complexed With Ba" 100.00 149 100.00 100.00 3.49e-100 PDB 2VAS "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" 100.00 149 97.97 99.32 3.51e-98 PDB 2VAY "Calmodulin Complexed With Cav1.1 Iq Peptide" 98.65 146 100.00 100.00 7.26e-99 PDB 2VB6 "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" 100.00 149 97.30 99.32 8.50e-98 PDB 2W73 "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" 100.00 149 100.00 100.00 3.49e-100 PDB 2WEL "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" 100.00 150 100.00 100.00 3.24e-100 PDB 2X0G "X-ray Structure Of A Dap-kinase Calmodulin Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 2X51 "M6 Delta Insert1" 100.00 149 97.97 99.32 3.51e-98 PDB 2Y4V "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" 100.00 149 100.00 100.00 3.49e-100 PDB 2YGG "Complex Of Cambr And Cam" 100.00 150 100.00 100.00 3.81e-100 PDB 3BXK "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3BXL "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3BYA "Structure Of A Calmodulin Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3CLN "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" 100.00 148 99.32 100.00 1.37e-99 PDB 3DVE "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3DVJ "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3DVK "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3DVM "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" 100.00 148 100.00 100.00 3.34e-100 PDB 3EK4 "Calcium-saturated Gcamp2 Monomer" 99.32 449 100.00 100.00 6.40e-96 PDB 3EK7 "Calcium-Saturated Gcamp2 Dimer" 99.32 449 100.00 100.00 6.40e-96 PDB 3EK8 "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" 99.32 449 100.00 100.00 9.04e-96 PDB 3EKH "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" 99.32 449 99.32 99.32 6.19e-95 PDB 3EVU "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" 99.32 449 100.00 100.00 6.40e-96 PDB 3EVV "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" 99.32 449 100.00 100.00 6.40e-96 PDB 3EWT "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.40e-100 PDB 3EWV "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.40e-100 PDB 3G43 "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" 100.00 148 100.00 100.00 3.34e-100 PDB 3GN4 "Myosin Lever Arm" 100.00 149 97.97 99.32 3.51e-98 PDB 3GOF "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" 100.00 148 100.00 100.00 3.34e-100 PDB 3HR4 "Human Inos Reductase And Calmodulin Complex" 100.00 149 100.00 100.00 3.49e-100 PDB 3IF7 "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" 100.00 148 100.00 100.00 3.34e-100 PDB 3J41 "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" 100.00 149 100.00 100.00 3.49e-100 PDB 3L9I "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" 100.00 149 97.97 99.32 3.51e-98 PDB 3O77 "The Structure Of Ca2+ Sensor (Case-16)" 99.32 415 100.00 100.00 2.87e-96 PDB 3O78 "The Structure Of Ca2+ Sensor (Case-12)" 99.32 415 100.00 100.00 3.16e-96 PDB 3OXQ "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" 100.00 149 100.00 100.00 3.49e-100 PDB 3SG2 "Crystal Structure Of Gcamp2-t116v,d381y" 99.32 449 99.32 99.32 9.13e-95 PDB 3SG3 "Crystal Structure Of Gcamp3-d380y" 99.32 449 98.64 99.32 1.16e-93 PDB 3SG4 "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" 100.00 448 97.97 98.65 7.96e-94 PDB 3SG5 "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" 100.00 448 97.97 98.65 6.55e-94 PDB 3SG6 "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" 99.32 450 100.00 100.00 8.17e-96 PDB 3SG7 "Crystal Structure Of Gcamp3-kf(linker 1)" 99.32 448 99.32 100.00 5.46e-95 PDB 3SJQ "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" 100.00 149 100.00 100.00 3.49e-100 PDB 3SUI "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" 100.00 149 100.00 100.00 3.49e-100 PDB 3U0K "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" 99.32 440 98.64 99.32 1.95e-94 PDB 3WFN "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" 100.00 182 100.00 100.00 4.02e-100 PDB 4ANJ "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" 100.00 149 97.97 99.32 3.51e-98 PDB 4BW7 "Calmodulin In Complex With Strontium" 100.00 149 100.00 100.00 3.49e-100 PDB 4BW8 "Calmodulin With Small Bend In Central Helix" 100.00 149 100.00 100.00 3.49e-100 PDB 4BYF "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" 100.00 149 100.00 100.00 3.49e-100 PDB 4CLN "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" 100.00 148 97.97 99.32 4.61e-98 PDB 4DBP "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" 100.00 149 97.97 99.32 3.51e-98 PDB 4DBQ "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" 100.00 149 97.97 99.32 3.51e-98 PDB 4DCK "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" 100.00 149 100.00 100.00 3.49e-100 PDB 4DJC "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" 100.00 152 100.00 100.00 2.44e-100 PDB 4E50 "Calmodulin And Ng Peptide Complex" 100.00 185 100.00 100.00 1.82e-100 PDB 4EHQ "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" 100.00 148 100.00 100.00 3.34e-100 PDB 4G27 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" 100.00 149 100.00 100.00 3.49e-100 PDB 4G28 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" 100.00 149 100.00 100.00 3.49e-100 PDB 4HEX "A Novel Conformation Of Calmodulin" 100.00 156 100.00 100.00 1.50e-100 PDB 4IK1 "High Resolution Structure Of Gcampj At Ph 8.5" 99.32 448 98.64 99.32 9.99e-94 PDB 4IK3 "High Resolution Structure Of Gcamp3 At Ph 8.5" 99.32 448 99.32 100.00 6.49e-95 PDB 4IK4 "High Resolution Structure Of Gcamp3 At Ph 5.0" 99.32 448 99.32 100.00 6.49e-95 PDB 4IK5 "High Resolution Structure Of Delta-rest-gcamp3" 99.32 414 99.32 100.00 2.54e-95 PDB 4IK8 "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" 99.32 448 99.32 100.00 6.49e-95 PDB 4IK9 "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" 99.32 448 99.32 100.00 6.49e-95 PDB 4J9Y "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" 100.00 149 100.00 100.00 3.49e-100 PDB 4J9Z "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" 100.00 149 100.00 100.00 3.49e-100 PDB 4JPZ "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" 100.00 149 100.00 100.00 3.49e-100 PDB 4JQ0 "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" 100.00 149 100.00 100.00 3.49e-100 PDB 4L79 "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" 100.00 149 100.00 100.00 3.49e-100 PDB 4LZX "Complex Of Iqcg And Ca2+-free Cam" 100.00 148 100.00 100.00 3.34e-100 PDB 4M1L "Complex Of Iqcg And Ca2+-bound Cam" 100.00 148 100.00 100.00 3.34e-100 PDB 4Q5U "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" 100.00 149 100.00 100.00 3.49e-100 PDB 4QNH "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" 100.00 149 99.32 99.32 4.26e-99 PDB 4R8G "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 4UMO "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 3.49e-100 PDB 4UPU "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" 100.00 148 100.00 100.00 3.34e-100 PDB 4V0C "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 3.49e-100 DBJ BAA08302 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 3.49e-100 DBJ BAA11896 "calmodulin [Anas platyrhynchos]" 100.00 149 100.00 100.00 3.49e-100 DBJ BAA19786 "calmodulin [Branchiostoma lanceolatum]" 100.00 149 97.97 99.32 3.51e-98 DBJ BAA19787 "calmodulin [Branchiostoma floridae]" 100.00 149 97.97 99.32 3.51e-98 DBJ BAA19788 "calmodulin [Halocynthia roretzi]" 100.00 149 97.97 99.32 3.51e-98 EMBL CAA10601 "calmodulin [Caenorhabditis elegans]" 100.00 149 97.97 98.65 8.69e-98 EMBL CAA32050 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 EMBL CAA32062 "calmodulin II [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 EMBL CAA32119 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 EMBL CAA32120 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 GB AAA35635 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 3.49e-100 GB AAA35641 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 3.49e-100 GB AAA37365 "calmodulin synthesis [Mus musculus]" 100.00 149 100.00 100.00 3.49e-100 GB AAA40862 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 GB AAA40863 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 3.49e-100 PIR JC1305 "calmodulin - Japanese medaka" 100.00 149 100.00 100.00 3.49e-100 PIR MCON "calmodulin - salmon" 100.00 148 100.00 100.00 3.34e-100 PRF 0409298A "troponin C-like protein" 100.00 148 97.30 100.00 1.72e-98 PRF 0608335A calmodulin 100.00 148 97.97 99.32 2.37e-97 REF NP_001008160 "calmodulin 2 (phosphorylase kinase, delta) [Xenopus (Silurana) tropicalis]" 100.00 149 100.00 100.00 3.49e-100 REF NP_001009759 "calmodulin [Ovis aries]" 100.00 149 100.00 100.00 3.49e-100 REF NP_001027633 "calmodulin [Ciona intestinalis]" 100.00 149 97.30 98.65 2.27e-97 REF NP_001039714 "calmodulin [Bos taurus]" 100.00 149 100.00 100.00 3.49e-100 REF NP_001040234 "calmodulin [Bombyx mori]" 100.00 149 97.97 99.32 3.51e-98 SP O02367 "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM [Ciona intestinalis]" 100.00 149 97.30 98.65 2.27e-97 SP O16305 "RecName: Full=Calmodulin; Short=CaM [Caenorhabditis elegans]" 100.00 149 97.97 98.65 8.69e-98 SP O96081 "RecName: Full=Calmodulin-B; Short=CaM B [Halocynthia roretzi]" 100.00 149 97.30 98.65 2.56e-97 SP P02594 "RecName: Full=Calmodulin; Short=CaM [Electrophorus electricus]" 100.00 149 99.32 100.00 1.12e-99 SP P05932 "RecName: Full=Calmodulin-beta; Short=Cam B, partial [Arbacia punctulata]" 93.24 138 97.10 99.28 3.58e-90 TPG DAA13808 "TPA: calmodulin 2-like [Bos taurus]" 100.00 216 98.65 98.65 1.70e-98 TPG DAA18029 "TPA: calmodulin [Bos taurus]" 100.00 149 98.65 99.32 5.13e-99 TPG DAA19590 "TPA: calmodulin 3 [Bos taurus]" 100.00 149 100.00 100.00 3.49e-100 TPG DAA24777 "TPA: calmodulin 2-like [Bos taurus]" 100.00 149 100.00 100.00 3.49e-100 TPG DAA24988 "TPA: calmodulin 2-like isoform 1 [Bos taurus]" 100.00 149 100.00 100.00 3.49e-100 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 2 16:12:04 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $calmodulin 'clawed frog' 8355 Eukaryota Metazoa Xenopus laevis 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 $calmodulin 'chemical, enzymatic, and cell-free synthesis' 'E. coli' . . . . 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 $calmodulin 0.7 mM 'SAIL (stereo array isotope labeled)' MES-d13 5 mM . bis-Tris-d19 10 mM . CaCl2 5 mM . NaN3 0.1 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_[1H,15N]-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name [1H,15N]-HSQC _Sample_label $sample_1 save_ save_[1H,13C]-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name [1H,13C]-HSQC _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_CBCANH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HBHANH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHANH _Sample_label $sample_1 save_ save_HBHA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_1 save_ save_CBCGHE_11 _Saveframe_category NMR_applied_experiment _Experiment_name CBCGHE _Sample_label $sample_1 save_ save_HBCBCGHE_12 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCGHE _Sample_label $sample_1 save_ save_15N-resolved_[1H,1H]-NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-resolved [1H,1H]-NOESY' _Sample_label $sample_1 save_ save_13C-resolved_[1H,1H]-NOESY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-resolved [1H,1H]-NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 310 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name calmodulin _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 1 1 ALA H H 8.418 0.020 1 2 1 1 ALA HA H 4.143 0.020 1 3 1 1 ALA HB H 1.304 0.020 1 4 1 1 ALA C C 177.632 0.200 1 5 1 1 ALA CA C 53.218 0.200 1 6 1 1 ALA CB C 18.487 0.200 1 7 1 1 ALA N N 123.237 0.200 1 8 2 2 ASP H H 7.996 0.020 1 9 2 2 ASP HA H 4.498 0.020 1 10 2 2 ASP HB2 H 2.633 0.020 1 11 2 2 ASP C C 176.253 0.200 1 12 2 2 ASP CA C 54.926 0.200 1 13 2 2 ASP CB C 40.626 0.200 1 14 2 2 ASP N N 117.319 0.200 1 15 3 3 GLN H H 7.904 0.020 1 16 3 3 GLN HA H 4.352 0.020 1 17 3 3 GLN HB2 H 1.943 0.020 1 18 3 3 GLN HG2 H 2.309 0.020 1 19 3 3 GLN HE21 H 7.424 0.020 2 20 3 3 GLN HE22 H 6.744 0.020 2 21 3 3 GLN C C 175.715 0.200 1 22 3 3 GLN CA C 55.477 0.200 1 23 3 3 GLN CB C 29.296 0.200 1 24 3 3 GLN CG C 33.528 0.200 1 25 3 3 GLN N N 118.074 0.200 1 26 3 3 GLN NE2 N 112.266 0.200 1 27 4 4 LEU H H 7.809 0.020 1 28 4 4 LEU HA H 4.649 0.020 1 29 4 4 LEU HB3 H 1.481 0.020 1 30 4 4 LEU HG H 1.723 0.020 1 31 4 4 LEU HD1 H 0.876 0.020 1 32 4 4 LEU C C 177.533 0.200 1 33 4 4 LEU CA C 54.320 0.200 1 34 4 4 LEU CB C 43.137 0.200 1 35 4 4 LEU CG C 26.511 0.200 1 36 4 4 LEU CD1 C 26.252 0.200 1 37 4 4 LEU N N 121.727 0.200 1 38 5 5 THR H H 8.642 0.020 1 39 5 5 THR HA H 4.457 0.020 1 40 5 5 THR HB H 4.745 0.020 1 41 5 5 THR HG2 H 1.285 0.020 1 42 5 5 THR C C 175.564 0.200 1 43 5 5 THR CA C 60.506 0.200 1 44 5 5 THR CB C 71.149 0.200 1 45 5 5 THR CG2 C 21.336 0.200 1 46 5 5 THR N N 112.755 0.200 1 47 6 6 GLU H H 8.955 0.020 1 48 6 6 GLU HA H 3.958 0.020 1 49 6 6 GLU HB2 H 2.024 0.020 1 50 6 6 GLU HG2 H 2.288 0.020 1 51 6 6 GLU C C 179.446 0.200 1 52 6 6 GLU CA C 60.035 0.200 1 53 6 6 GLU CB C 28.894 0.200 1 54 6 6 GLU CG C 36.202 0.200 1 55 6 6 GLU N N 120.513 0.200 1 56 7 7 GLU H H 8.633 0.020 1 57 7 7 GLU HA H 4.052 0.020 1 58 7 7 GLU HB2 H 2.003 0.020 1 59 7 7 GLU HG2 H 2.314 0.020 1 60 7 7 GLU C C 179.110 0.200 1 61 7 7 GLU CA C 59.874 0.200 1 62 7 7 GLU CB C 28.736 0.200 1 63 7 7 GLU CG C 36.443 0.200 1 64 7 7 GLU N N 119.367 0.200 1 65 8 8 GLN H H 7.681 0.020 1 66 8 8 GLN HA H 3.854 0.020 1 67 8 8 GLN HB2 H 2.338 0.020 1 68 8 8 GLN HG2 H 2.259 0.020 1 69 8 8 GLN HE21 H 7.387 0.020 2 70 8 8 GLN HE22 H 6.704 0.020 2 71 8 8 GLN C C 178.344 0.200 1 72 8 8 GLN CA C 58.557 0.200 1 73 8 8 GLN CB C 28.957 0.200 1 74 8 8 GLN CG C 34.570 0.200 1 75 8 8 GLN N N 120.081 0.200 1 76 8 8 GLN NE2 N 111.230 0.200 1 77 9 9 ILE H H 8.361 0.020 1 78 9 9 ILE HA H 3.704 0.020 1 79 9 9 ILE HB H 1.938 0.020 1 80 9 9 ILE HG12 H 1.057 0.020 1 81 9 9 ILE HG2 H 1.056 0.020 1 82 9 9 ILE HD1 H 0.813 0.020 1 83 9 9 ILE C C 177.775 0.200 1 84 9 9 ILE CA C 66.109 0.200 1 85 9 9 ILE CB C 37.513 0.200 1 86 9 9 ILE CG1 C 29.619 0.200 1 87 9 9 ILE CG2 C 16.870 0.200 1 88 9 9 ILE CD1 C 12.272 0.200 1 89 9 9 ILE N N 119.556 0.200 1 90 10 10 ALA H H 7.960 0.020 1 91 10 10 ALA HA H 4.098 0.020 1 92 10 10 ALA HB H 1.485 0.020 1 93 10 10 ALA C C 180.987 0.200 1 94 10 10 ALA CA C 55.395 0.200 1 95 10 10 ALA CB C 17.418 0.200 1 96 10 10 ALA N N 121.255 0.200 1 97 11 11 GLU H H 7.754 0.020 1 98 11 11 GLU HA H 4.130 0.020 1 99 11 11 GLU HB2 H 1.994 0.020 1 100 11 11 GLU HG2 H 2.128 0.020 1 101 11 11 GLU C C 180.448 0.200 1 102 11 11 GLU CA C 59.271 0.200 1 103 11 11 GLU CB C 28.757 0.200 1 104 11 11 GLU CG C 35.633 0.200 1 105 11 11 GLU N N 119.513 0.200 1 106 12 12 PHE H H 8.527 0.020 1 107 12 12 PHE HA H 4.995 0.020 1 108 12 12 PHE HB3 H 3.414 0.020 1 109 12 12 PHE HE1 H 7.231 0.020 1 110 12 12 PHE HE2 H 7.231 0.020 1 111 12 12 PHE C C 178.741 0.200 1 112 12 12 PHE CA C 59.293 0.200 1 113 12 12 PHE CB C 37.526 0.200 1 114 12 12 PHE CE1 C 131.192 0.200 1 115 12 12 PHE N N 120.041 0.200 1 116 13 13 LYS H H 9.152 0.020 1 117 13 13 LYS HA H 4.012 0.020 1 118 13 13 LYS HB3 H 1.888 0.020 1 119 13 13 LYS HG3 H 1.187 0.020 1 120 13 13 LYS HD3 H 1.200 0.020 1 121 13 13 LYS HE2 H 2.530 0.020 1 122 13 13 LYS C C 179.355 0.200 1 123 13 13 LYS CA C 60.149 0.200 1 124 13 13 LYS CB C 31.517 0.200 1 125 13 13 LYS CG C 24.988 0.200 1 126 13 13 LYS CD C 28.288 0.200 1 127 13 13 LYS CE C 41.483 0.200 1 128 13 13 LYS N N 123.493 0.200 1 129 14 14 GLU H H 7.772 0.020 1 130 14 14 GLU HA H 4.119 0.020 1 131 14 14 GLU HB2 H 2.206 0.020 1 132 14 14 GLU HG2 H 2.257 0.020 1 133 14 14 GLU C C 179.455 0.200 1 134 14 14 GLU CA C 59.329 0.200 1 135 14 14 GLU CB C 28.783 0.200 1 136 14 14 GLU CG C 35.733 0.200 1 137 14 14 GLU N N 120.399 0.200 1 138 15 15 ALA H H 7.972 0.020 1 139 15 15 ALA HA H 4.262 0.020 1 140 15 15 ALA HB H 1.915 0.020 1 141 15 15 ALA C C 179.043 0.200 1 142 15 15 ALA CA C 55.215 0.200 1 143 15 15 ALA CB C 17.613 0.200 1 144 15 15 ALA N N 122.472 0.200 1 145 16 16 PHE H H 8.774 0.020 1 146 16 16 PHE HA H 3.206 0.020 1 147 16 16 PHE HB3 H 3.155 0.020 1 148 16 16 PHE HE1 H 7.003 0.020 1 149 16 16 PHE HE2 H 7.003 0.020 1 150 16 16 PHE C C 177.349 0.200 1 151 16 16 PHE CA C 61.958 0.200 1 152 16 16 PHE CB C 39.159 0.200 1 153 16 16 PHE CE1 C 130.872 0.200 1 154 16 16 PHE N N 119.346 0.200 1 155 17 17 SER H H 7.887 0.020 1 156 17 17 SER HA H 4.117 0.020 1 157 17 17 SER HB2 H 4.015 0.020 1 158 17 17 SER C C 174.991 0.200 1 159 17 17 SER CA C 61.421 0.200 1 160 17 17 SER CB C 63.033 0.200 1 161 17 17 SER N N 112.628 0.200 1 162 18 18 LEU H H 7.417 0.020 1 163 18 18 LEU HA H 3.980 0.020 1 164 18 18 LEU HB3 H 1.562 0.020 1 165 18 18 LEU HG H 1.437 0.020 1 166 18 18 LEU HD1 H 0.777 0.020 1 167 18 18 LEU C C 177.967 0.200 1 168 18 18 LEU CA C 57.142 0.200 1 169 18 18 LEU CB C 41.094 0.200 1 170 18 18 LEU CG C 26.260 0.200 1 171 18 18 LEU CD1 C 23.761 0.200 1 172 18 18 LEU N N 120.971 0.200 1 173 19 19 PHE H H 7.273 0.020 1 174 19 19 PHE HA H 4.216 0.020 1 175 19 19 PHE HB3 H 2.625 0.020 1 176 19 19 PHE HE1 H 7.353 0.020 1 177 19 19 PHE HE2 H 7.353 0.020 1 178 19 19 PHE C C 176.718 0.200 1 179 19 19 PHE CA C 59.312 0.200 1 180 19 19 PHE CB C 40.586 0.200 1 181 19 19 PHE CE1 C 130.874 0.200 1 182 19 19 PHE N N 114.999 0.200 1 183 20 20 ASP H H 7.793 0.020 1 184 20 20 ASP HA H 4.530 0.020 1 185 20 20 ASP HB2 H 1.477 0.020 1 186 20 20 ASP C C 177.179 0.200 1 187 20 20 ASP CA C 52.373 0.200 1 188 20 20 ASP CB C 38.632 0.200 1 189 20 20 ASP N N 117.590 0.200 1 190 21 21 LYS H H 7.652 0.020 1 191 21 21 LYS HA H 3.954 0.020 1 192 21 21 LYS HB3 H 1.835 0.020 1 193 21 21 LYS HG3 H 1.508 0.020 1 194 21 21 LYS HD3 H 1.665 0.020 1 195 21 21 LYS HE2 H 2.951 0.020 1 196 21 21 LYS C C 178.163 0.200 1 197 21 21 LYS CA C 58.400 0.200 1 198 21 21 LYS CB C 32.187 0.200 1 199 21 21 LYS CG C 23.956 0.200 1 200 21 21 LYS CD C 27.791 0.200 1 201 21 21 LYS CE C 41.779 0.200 1 202 21 21 LYS N N 124.427 0.200 1 203 22 22 ASP H H 8.044 0.020 1 204 22 22 ASP HA H 4.573 0.020 1 205 22 22 ASP HB2 H 3.030 0.020 1 206 22 22 ASP C C 177.716 0.200 1 207 22 22 ASP CA C 52.809 0.200 1 208 22 22 ASP CB C 39.349 0.200 1 209 22 22 ASP N N 113.971 0.200 1 210 23 23 GLY H H 7.645 0.020 1 211 23 23 GLY HA3 H 3.858 0.020 1 212 23 23 GLY C C 175.155 0.200 1 213 23 23 GLY CA C 47.040 0.200 1 214 23 23 GLY N N 109.138 0.200 1 215 24 24 ASP H H 8.355 0.020 1 216 24 24 ASP HA H 4.490 0.020 1 217 24 24 ASP HB2 H 3.017 0.020 1 218 24 24 ASP C C 177.492 0.200 1 219 24 24 ASP CA C 53.746 0.200 1 220 24 24 ASP CB C 40.180 0.200 1 221 24 24 ASP N N 120.669 0.200 1 222 25 25 GLY H H 10.569 0.020 1 223 25 25 GLY HA3 H 4.327 0.020 1 224 25 25 GLY C C 173.711 0.200 1 225 25 25 GLY CA C 45.294 0.200 1 226 25 25 GLY N N 113.169 0.200 1 227 26 26 THR H H 8.108 0.020 1 228 26 26 THR HA H 5.272 0.020 1 229 26 26 THR HB H 3.829 0.020 1 230 26 26 THR HG2 H 0.992 0.020 1 231 26 26 THR C C 172.956 0.200 1 232 26 26 THR CA C 59.885 0.200 1 233 26 26 THR CB C 72.585 0.200 1 234 26 26 THR CG2 C 21.100 0.200 1 235 26 26 THR N N 112.932 0.200 1 236 27 27 ILE H H 9.754 0.020 1 237 27 27 ILE HA H 4.946 0.020 1 238 27 27 ILE HB H 1.764 0.020 1 239 27 27 ILE HG12 H 0.252 0.020 1 240 27 27 ILE HG2 H 0.826 0.020 1 241 27 27 ILE HD1 H 0.190 0.020 1 242 27 27 ILE C C 176.112 0.200 1 243 27 27 ILE CA C 60.495 0.200 1 244 27 27 ILE CB C 39.409 0.200 1 245 27 27 ILE CG1 C 26.432 0.200 1 246 27 27 ILE CG2 C 17.126 0.200 1 247 27 27 ILE CD1 C 14.639 0.200 1 248 27 27 ILE N N 127.132 0.200 1 249 28 28 THR H H 8.457 0.020 1 250 28 28 THR HA H 4.806 0.020 1 251 28 28 THR HB H 4.782 0.020 1 252 28 28 THR HG2 H 1.258 0.020 1 253 28 28 THR C C 176.634 0.200 1 254 28 28 THR CA C 59.653 0.200 1 255 28 28 THR CB C 72.367 0.200 1 256 28 28 THR CG2 C 21.441 0.200 1 257 28 28 THR N N 116.595 0.200 1 258 29 29 THR H H 9.057 0.020 1 259 29 29 THR HA H 3.774 0.020 1 260 29 29 THR HB H 4.181 0.020 1 261 29 29 THR HG2 H 1.225 0.020 1 262 29 29 THR C C 177.225 0.200 1 263 29 29 THR CA C 66.511 0.200 1 264 29 29 THR CB C 67.912 0.200 1 265 29 29 THR CG2 C 22.809 0.200 1 266 29 29 THR N N 112.859 0.200 1 267 30 30 LYS H H 7.633 0.020 1 268 30 30 LYS HA H 4.107 0.020 1 269 30 30 LYS HB3 H 1.764 0.020 1 270 30 30 LYS HG3 H 1.456 0.020 1 271 30 30 LYS HD3 H 1.628 0.020 1 272 30 30 LYS HE2 H 2.951 0.020 1 273 30 30 LYS C C 179.894 0.200 1 274 30 30 LYS CA C 59.143 0.200 1 275 30 30 LYS CB C 32.046 0.200 1 276 30 30 LYS CG C 24.386 0.200 1 277 30 30 LYS CD C 28.531 0.200 1 278 30 30 LYS CE C 41.781 0.200 1 279 30 30 LYS N N 120.732 0.200 1 280 31 31 GLU H H 7.629 0.020 1 281 31 31 GLU HA H 4.031 0.020 1 282 31 31 GLU HB2 H 2.357 0.020 1 283 31 31 GLU HG2 H 2.288 0.020 1 284 31 31 GLU C C 179.102 0.200 1 285 31 31 GLU CA C 59.355 0.200 1 286 31 31 GLU CB C 29.507 0.200 1 287 31 31 GLU CG C 37.911 0.200 1 288 31 31 GLU N N 121.563 0.200 1 289 32 32 LEU H H 8.659 0.020 1 290 32 32 LEU HA H 4.078 0.020 1 291 32 32 LEU HB3 H 1.815 0.020 1 292 32 32 LEU HG H 1.557 0.020 1 293 32 32 LEU HD1 H 0.815 0.020 1 294 32 32 LEU C C 178.996 0.200 1 295 32 32 LEU CA C 58.097 0.200 1 296 32 32 LEU CB C 42.281 0.200 1 297 32 32 LEU CG C 26.106 0.200 1 298 32 32 LEU CD1 C 23.129 0.200 1 299 32 32 LEU N N 120.584 0.200 1 300 33 33 GLY H H 8.590 0.020 1 301 33 33 GLY HA3 H 3.947 0.020 1 302 33 33 GLY C C 175.255 0.200 1 303 33 33 GLY CA C 48.075 0.200 1 304 33 33 GLY N N 105.213 0.200 1 305 34 34 THR H H 7.874 0.020 1 306 34 34 THR HA H 3.920 0.020 1 307 34 34 THR HB H 4.300 0.020 1 308 34 34 THR HG2 H 1.233 0.020 1 309 34 34 THR C C 177.096 0.200 1 310 34 34 THR CA C 66.929 0.200 1 311 34 34 THR CB C 68.700 0.200 1 312 34 34 THR CG2 C 21.088 0.200 1 313 34 34 THR N N 117.984 0.200 1 314 35 35 VAL H H 7.609 0.020 1 315 35 35 VAL HA H 3.485 0.020 1 316 35 35 VAL HB H 1.929 0.020 1 317 35 35 VAL HG2 H 0.622 0.020 1 318 35 35 VAL C C 179.156 0.200 1 319 35 35 VAL CA C 66.301 0.200 1 320 35 35 VAL CB C 31.035 0.200 1 321 35 35 VAL CG2 C 22.234 0.200 1 322 35 35 VAL N N 122.184 0.200 1 323 36 36 MET H H 8.402 0.020 1 324 36 36 MET HA H 4.085 0.020 1 325 36 36 MET HB2 H 1.985 0.020 1 326 36 36 MET HG2 H 2.584 0.020 1 327 36 36 MET HE H 1.939 0.020 1 328 36 36 MET C C 179.128 0.200 1 329 36 36 MET CA C 59.088 0.200 1 330 36 36 MET CB C 31.130 0.200 1 331 36 36 MET CG C 32.469 0.200 1 332 36 36 MET CE C 16.952 0.200 1 333 36 36 MET N N 118.323 0.200 1 334 37 37 ARG H H 8.439 0.020 1 335 37 37 ARG HA H 4.777 0.020 1 336 37 37 ARG HB3 H 1.859 0.020 1 337 37 37 ARG HG3 H 1.860 0.020 1 338 37 37 ARG HD2 H 3.109 0.020 1 339 37 37 ARG C C 181.179 0.200 1 340 37 37 ARG CA C 59.068 0.200 1 341 37 37 ARG CB C 29.698 0.200 1 342 37 37 ARG CG C 28.688 0.200 1 343 37 37 ARG CD C 43.230 0.200 1 344 37 37 ARG N N 118.959 0.200 1 345 38 38 SER H H 7.887 0.020 1 346 38 38 SER HA H 4.383 0.020 1 347 38 38 SER HB2 H 4.091 0.020 1 348 38 38 SER C C 174.745 0.200 1 349 38 38 SER CA C 61.572 0.200 1 350 38 38 SER CB C 62.588 0.200 1 351 38 38 SER N N 118.704 0.200 1 352 39 39 LEU H H 7.353 0.020 1 353 39 39 LEU HA H 4.473 0.020 1 354 39 39 LEU HB3 H 1.762 0.020 1 355 39 39 LEU HG H 1.761 0.020 1 356 39 39 LEU HD1 H 0.778 0.020 1 357 39 39 LEU C C 177.494 0.200 1 358 39 39 LEU CA C 54.524 0.200 1 359 39 39 LEU CB C 41.574 0.200 1 360 39 39 LEU CG C 25.763 0.200 1 361 39 39 LEU CD1 C 24.874 0.200 1 362 39 39 LEU N N 120.474 0.200 1 363 40 40 GLY H H 7.828 0.020 1 364 40 40 GLY HA3 H 4.231 0.020 1 365 40 40 GLY C C 174.426 0.200 1 366 40 40 GLY CA C 45.401 0.200 1 367 40 40 GLY N N 106.666 0.200 1 368 41 41 GLN H H 7.786 0.020 1 369 41 41 GLN HA H 4.460 0.020 1 370 41 41 GLN HB2 H 1.617 0.020 1 371 41 41 GLN HG2 H 2.215 0.020 1 372 41 41 GLN HE21 H 7.276 0.020 2 373 41 41 GLN HE22 H 6.678 0.020 2 374 41 41 GLN C C 174.170 0.200 1 375 41 41 GLN CA C 54.529 0.200 1 376 41 41 GLN CB C 30.257 0.200 1 377 41 41 GLN CG C 33.579 0.200 1 378 41 41 GLN N N 118.493 0.200 1 379 41 41 GLN NE2 N 111.095 0.200 1 380 42 42 ASN H H 8.638 0.020 1 381 42 42 ASN HA H 5.160 0.020 1 382 42 42 ASN HB2 H 2.488 0.020 1 383 42 42 ASN HD21 H 7.473 0.020 2 384 42 42 ASN HD22 H 6.667 0.020 2 385 42 42 ASN C C 169.309 0.200 1 386 42 42 ASN CA C 51.232 0.200 1 387 42 42 ASN CB C 39.026 0.200 1 388 42 42 ASN N N 116.363 0.200 1 389 42 42 ASN ND2 N 112.032 0.200 1 390 43 43 PRO HA H 4.732 0.020 1 391 43 43 PRO HB2 H 1.894 0.020 1 392 43 43 PRO HG2 H 1.895 0.020 1 393 43 43 PRO HD3 H 3.272 0.020 1 394 43 43 PRO C C 177.778 0.200 1 395 43 43 PRO CA C 62.412 0.200 1 396 43 43 PRO CB C 31.536 0.200 1 397 43 43 PRO CG C 27.044 0.200 1 398 43 43 PRO CD C 49.561 0.200 1 399 44 44 THR H H 8.669 0.020 1 400 44 44 THR HA H 4.434 0.020 1 401 44 44 THR HB H 4.689 0.020 1 402 44 44 THR HG2 H 1.316 0.020 1 403 44 44 THR C C 175.243 0.200 1 404 44 44 THR CA C 60.527 0.200 1 405 44 44 THR CB C 71.123 0.200 1 406 44 44 THR CG2 C 21.400 0.200 1 407 44 44 THR N N 112.931 0.200 1 408 45 45 GLU H H 8.756 0.020 1 409 45 45 GLU HA H 3.958 0.020 1 410 45 45 GLU HB2 H 2.014 0.020 1 411 45 45 GLU HG2 H 2.285 0.020 1 412 45 45 GLU C C 178.996 0.200 1 413 45 45 GLU CA C 60.041 0.200 1 414 45 45 GLU CB C 28.703 0.200 1 415 45 45 GLU CG C 35.937 0.200 1 416 45 45 GLU N N 120.670 0.200 1 417 46 46 ALA H H 8.200 0.020 1 418 46 46 ALA HA H 4.084 0.020 1 419 46 46 ALA HB H 1.349 0.020 1 420 46 46 ALA C C 180.252 0.200 1 421 46 46 ALA CA C 54.959 0.200 1 422 46 46 ALA CB C 17.737 0.200 1 423 46 46 ALA N N 120.626 0.200 1 424 47 47 GLU H H 7.654 0.020 1 425 47 47 GLU HA H 4.007 0.020 1 426 47 47 GLU HB2 H 2.277 0.020 1 427 47 47 GLU HG2 H 2.262 0.020 1 428 47 47 GLU C C 180.111 0.200 1 429 47 47 GLU CA C 59.046 0.200 1 430 47 47 GLU CB C 29.466 0.200 1 431 47 47 GLU CG C 37.016 0.200 1 432 47 47 GLU N N 118.826 0.200 1 433 48 48 LEU H H 8.113 0.020 1 434 48 48 LEU HA H 4.057 0.020 1 435 48 48 LEU HB3 H 1.237 0.020 1 436 48 48 LEU HG H 1.717 0.020 1 437 48 48 LEU HD1 H 0.807 0.020 1 438 48 48 LEU C C 178.538 0.200 1 439 48 48 LEU CA C 57.850 0.200 1 440 48 48 LEU CB C 41.940 0.200 1 441 48 48 LEU CG C 26.434 0.200 1 442 48 48 LEU CD1 C 25.124 0.200 1 443 48 48 LEU N N 120.375 0.200 1 444 49 49 GLN H H 8.148 0.020 1 445 49 49 GLN HA H 3.818 0.020 1 446 49 49 GLN HB2 H 2.167 0.020 1 447 49 49 GLN HG2 H 2.386 0.020 1 448 49 49 GLN HE21 H 7.432 0.020 2 449 49 49 GLN HE22 H 6.816 0.020 2 450 49 49 GLN C C 178.527 0.200 1 451 49 49 GLN CA C 58.558 0.200 1 452 49 49 GLN CB C 27.851 0.200 1 453 49 49 GLN CG C 33.792 0.200 1 454 49 49 GLN N N 118.217 0.200 1 455 49 49 GLN NE2 N 112.721 0.200 1 456 50 50 ASP H H 8.039 0.020 1 457 50 50 ASP HA H 4.399 0.020 1 458 50 50 ASP HB2 H 2.763 0.020 1 459 50 50 ASP C C 178.600 0.200 1 460 50 50 ASP CA C 57.544 0.200 1 461 50 50 ASP CB C 40.131 0.200 1 462 50 50 ASP N N 119.989 0.200 1 463 51 51 MET H H 7.828 0.020 1 464 51 51 MET HA H 4.017 0.020 1 465 51 51 MET HB2 H 2.250 0.020 1 466 51 51 MET HG2 H 2.492 0.020 1 467 51 51 MET HE H 2.003 0.020 1 468 51 51 MET C C 178.893 0.200 1 469 51 51 MET CA C 59.343 0.200 1 470 51 51 MET CB C 32.968 0.200 1 471 51 51 MET CG C 32.112 0.200 1 472 51 51 MET CE C 16.576 0.200 1 473 51 51 MET N N 119.264 0.200 1 474 52 52 ILE H H 7.680 0.020 1 475 52 52 ILE HA H 3.493 0.020 1 476 52 52 ILE HB H 1.901 0.020 1 477 52 52 ILE HG12 H 0.966 0.020 1 478 52 52 ILE HG2 H 0.642 0.020 1 479 52 52 ILE HD1 H 0.678 0.020 1 480 52 52 ILE C C 177.775 0.200 1 481 52 52 ILE CA C 64.843 0.200 1 482 52 52 ILE CB C 37.072 0.200 1 483 52 52 ILE CG1 C 28.498 0.200 1 484 52 52 ILE CG2 C 15.534 0.200 1 485 52 52 ILE CD1 C 12.297 0.200 1 486 52 52 ILE N N 118.167 0.200 1 487 53 53 ASN H H 8.524 0.020 1 488 53 53 ASN HA H 4.365 0.020 1 489 53 53 ASN HB2 H 2.959 0.020 1 490 53 53 ASN HD21 H 7.774 0.020 2 491 53 53 ASN HD22 H 6.876 0.020 2 492 53 53 ASN C C 177.429 0.200 1 493 53 53 ASN CA C 55.930 0.200 1 494 53 53 ASN CB C 37.863 0.200 1 495 53 53 ASN N N 117.725 0.200 1 496 53 53 ASN ND2 N 111.680 0.200 1 497 54 54 GLU H H 7.557 0.020 1 498 54 54 GLU HA H 4.020 0.020 1 499 54 54 GLU HB2 H 2.096 0.020 1 500 54 54 GLU HG2 H 2.226 0.020 1 501 54 54 GLU C C 177.599 0.200 1 502 54 54 GLU CA C 58.843 0.200 1 503 54 54 GLU CB C 30.030 0.200 1 504 54 54 GLU CG C 35.908 0.200 1 505 54 54 GLU N N 116.395 0.200 1 506 55 55 VAL H H 7.189 0.020 1 507 55 55 VAL HA H 4.446 0.020 1 508 55 55 VAL HB H 2.341 0.020 1 509 55 55 VAL HG2 H 0.853 0.020 1 510 55 55 VAL C C 175.808 0.200 1 511 55 55 VAL CA C 60.743 0.200 1 512 55 55 VAL CB C 32.387 0.200 1 513 55 55 VAL CG2 C 18.772 0.200 1 514 55 55 VAL N N 108.564 0.200 1 515 56 56 ASP H H 7.651 0.020 1 516 56 56 ASP HA H 4.617 0.020 1 517 56 56 ASP HB2 H 2.527 0.020 1 518 56 56 ASP C C 176.269 0.200 1 519 56 56 ASP CA C 53.794 0.200 1 520 56 56 ASP CB C 39.875 0.200 1 521 56 56 ASP N N 121.820 0.200 1 522 57 57 ALA H H 8.452 0.020 1 523 57 57 ALA HA H 4.182 0.020 1 524 57 57 ALA HB H 1.481 0.020 1 525 57 57 ALA C C 178.655 0.200 1 526 57 57 ALA CA C 54.203 0.200 1 527 57 57 ALA CB C 19.020 0.200 1 528 57 57 ALA N N 131.746 0.200 1 529 58 58 ASP H H 8.122 0.020 1 530 58 58 ASP HA H 4.621 0.020 1 531 58 58 ASP HB2 H 3.005 0.020 1 532 58 58 ASP C C 177.866 0.200 1 533 58 58 ASP CA C 52.648 0.200 1 534 58 58 ASP CB C 39.540 0.200 1 535 58 58 ASP N N 113.805 0.200 1 536 59 59 GLY H H 7.531 0.020 1 537 59 59 GLY HA3 H 3.866 0.020 1 538 59 59 GLY C C 174.962 0.200 1 539 59 59 GLY CA C 47.044 0.200 1 540 59 59 GLY N N 108.267 0.200 1 541 60 60 ASN H H 8.044 0.020 1 542 60 60 ASN HA H 4.624 0.020 1 543 60 60 ASN HB2 H 3.273 0.020 1 544 60 60 ASN HD21 H 7.679 0.020 2 545 60 60 ASN HD22 H 6.962 0.020 2 546 60 60 ASN C C 176.876 0.200 1 547 60 60 ASN CA C 52.580 0.200 1 548 60 60 ASN CB C 37.465 0.200 1 549 60 60 ASN N N 118.402 0.200 1 550 60 60 ASN ND2 N 115.193 0.200 1 551 61 61 GLY H H 10.540 0.020 1 552 61 61 GLY HA3 H 4.166 0.020 1 553 61 61 GLY C C 173.282 0.200 1 554 61 61 GLY CA C 45.520 0.200 1 555 61 61 GLY N N 113.357 0.200 1 556 62 62 THR H H 7.650 0.020 1 557 62 62 THR HA H 4.740 0.020 1 558 62 62 THR HB H 3.985 0.020 1 559 62 62 THR HG2 H 1.059 0.020 1 560 62 62 THR C C 173.236 0.200 1 561 62 62 THR CA C 59.535 0.200 1 562 62 62 THR CB C 71.882 0.200 1 563 62 62 THR CG2 C 21.856 0.200 1 564 62 62 THR N N 109.094 0.200 1 565 63 63 ILE H H 8.886 0.020 1 566 63 63 ILE HA H 5.159 0.020 1 567 63 63 ILE HB H 2.030 0.020 1 568 63 63 ILE HG12 H 0.949 0.020 1 569 63 63 ILE HG2 H 1.158 0.020 1 570 63 63 ILE HD1 H 0.740 0.020 1 571 63 63 ILE C C 175.567 0.200 1 572 63 63 ILE CA C 60.027 0.200 1 573 63 63 ILE CB C 39.468 0.200 1 574 63 63 ILE CG1 C 26.880 0.200 1 575 63 63 ILE CG2 C 17.779 0.200 1 576 63 63 ILE CD1 C 12.922 0.200 1 577 63 63 ILE N N 123.925 0.200 1 578 64 64 ASP H H 8.793 0.020 1 579 64 64 ASP HA H 5.340 0.020 1 580 64 64 ASP HB2 H 3.068 0.020 1 581 64 64 ASP C C 176.385 0.200 1 582 64 64 ASP CA C 52.174 0.200 1 583 64 64 ASP CB C 41.940 0.200 1 584 64 64 ASP N N 128.213 0.200 1 585 65 65 PHE H H 8.877 0.020 1 586 65 65 PHE HA H 3.997 0.020 1 587 65 65 PHE HB3 H 2.792 0.020 1 588 65 65 PHE HE1 H 7.177 0.020 1 589 65 65 PHE HE2 H 7.177 0.020 1 590 65 65 PHE C C 170.918 0.200 1 591 65 65 PHE CA C 63.585 0.200 1 592 65 65 PHE CB C 35.592 0.200 1 593 65 65 PHE CE1 C 130.445 0.200 1 594 65 65 PHE N N 118.730 0.200 1 595 66 66 PRO HA H 3.850 0.020 1 596 66 66 PRO HB2 H 1.866 0.020 1 597 66 66 PRO HG2 H 2.149 0.020 1 598 66 66 PRO HD3 H 3.719 0.020 1 599 66 66 PRO C C 180.059 0.200 1 600 66 66 PRO CA C 66.625 0.200 1 601 66 66 PRO CB C 30.301 0.200 1 602 66 66 PRO CG C 28.001 0.200 1 603 66 66 PRO CD C 48.770 0.200 1 604 67 67 GLU H H 7.900 0.020 1 605 67 67 GLU HA H 4.088 0.020 1 606 67 67 GLU HB2 H 2.550 0.020 1 607 67 67 GLU HG2 H 2.453 0.020 1 608 67 67 GLU C C 178.818 0.200 1 609 67 67 GLU CA C 58.723 0.200 1 610 67 67 GLU CB C 29.222 0.200 1 611 67 67 GLU CG C 36.621 0.200 1 612 67 67 GLU N N 117.607 0.200 1 613 68 68 PHE H H 8.820 0.020 1 614 68 68 PHE HA H 3.940 0.020 1 615 68 68 PHE HB3 H 3.472 0.020 1 616 68 68 PHE HE1 H 7.111 0.020 1 617 68 68 PHE HE2 H 7.111 0.020 1 618 68 68 PHE C C 177.069 0.200 1 619 68 68 PHE CA C 61.214 0.200 1 620 68 68 PHE CB C 39.610 0.200 1 621 68 68 PHE CE1 C 131.320 0.200 1 622 68 68 PHE N N 123.570 0.200 1 623 69 69 LEU H H 8.329 0.020 1 624 69 69 LEU HA H 3.326 0.020 1 625 69 69 LEU HB3 H 1.091 0.020 1 626 69 69 LEU HG H 0.977 0.020 1 627 69 69 LEU HD1 H 0.542 0.020 1 628 69 69 LEU C C 179.051 0.200 1 629 69 69 LEU CA C 57.936 0.200 1 630 69 69 LEU CB C 40.617 0.200 1 631 69 69 LEU CG C 25.286 0.200 1 632 69 69 LEU CD1 C 24.813 0.200 1 633 69 69 LEU N N 118.916 0.200 1 634 70 70 THR H H 7.465 0.020 1 635 70 70 THR HA H 3.734 0.020 1 636 70 70 THR HB H 4.312 0.020 1 637 70 70 THR HG2 H 1.149 0.020 1 638 70 70 THR C C 175.958 0.200 1 639 70 70 THR CA C 66.554 0.200 1 640 70 70 THR CB C 68.331 0.200 1 641 70 70 THR CG2 C 21.616 0.200 1 642 70 70 THR N N 115.163 0.200 1 643 71 71 MET H H 7.746 0.020 1 644 71 71 MET HA H 3.740 0.020 1 645 71 71 MET HB2 H 1.924 0.020 1 646 71 71 MET HG2 H 2.073 0.020 1 647 71 71 MET HE H 1.714 0.020 1 648 71 71 MET C C 178.148 0.200 1 649 71 71 MET CA C 58.944 0.200 1 650 71 71 MET CB C 33.119 0.200 1 651 71 71 MET CG C 31.047 0.200 1 652 71 71 MET CE C 16.822 0.200 1 653 71 71 MET N N 121.605 0.200 1 654 72 72 MET H H 8.011 0.020 1 655 72 72 MET HA H 3.982 0.020 1 656 72 72 MET HB2 H 1.083 0.020 1 657 72 72 MET HG2 H 1.289 0.020 1 658 72 72 MET HE H 1.650 0.020 1 659 72 72 MET C C 178.525 0.200 1 660 72 72 MET CA C 55.773 0.200 1 661 72 72 MET CB C 30.767 0.200 1 662 72 72 MET CG C 31.735 0.200 1 663 72 72 MET CE C 17.097 0.200 1 664 72 72 MET N N 116.542 0.200 1 665 73 73 ALA H H 8.168 0.020 1 666 73 73 ALA HA H 4.063 0.020 1 667 73 73 ALA HB H 1.338 0.020 1 668 73 73 ALA C C 179.616 0.200 1 669 73 73 ALA CA C 54.434 0.200 1 670 73 73 ALA CB C 17.760 0.200 1 671 73 73 ALA N N 122.227 0.200 1 672 74 74 ARG H H 7.564 0.020 1 673 74 74 ARG HA H 4.063 0.020 1 674 74 74 ARG HB3 H 1.841 0.020 1 675 74 74 ARG HG3 H 1.713 0.020 1 676 74 74 ARG HD2 H 3.045 0.020 1 677 74 74 ARG C C 177.735 0.200 1 678 74 74 ARG CA C 58.102 0.200 1 679 74 74 ARG CB C 29.839 0.200 1 680 74 74 ARG CG C 26.945 0.200 1 681 74 74 ARG CD C 43.325 0.200 1 682 74 74 ARG N N 116.476 0.200 1 683 75 75 LYS H H 7.610 0.020 1 684 75 75 LYS HA H 4.200 0.020 1 685 75 75 LYS HB3 H 1.851 0.020 1 686 75 75 LYS HG3 H 1.443 0.020 1 687 75 75 LYS HD3 H 1.587 0.020 1 688 75 75 LYS HE2 H 2.878 0.020 1 689 75 75 LYS C C 177.611 0.200 1 690 75 75 LYS CA C 57.143 0.200 1 691 75 75 LYS CB C 32.103 0.200 1 692 75 75 LYS CG C 24.213 0.200 1 693 75 75 LYS CD C 28.339 0.200 1 694 75 75 LYS CE C 41.702 0.200 1 695 75 75 LYS N N 118.577 0.200 1 696 76 76 MET H H 7.800 0.020 1 697 76 76 MET HA H 4.325 0.020 1 698 76 76 MET HB2 H 2.061 0.020 1 699 76 76 MET HG2 H 2.574 0.020 1 700 76 76 MET HE H 2.053 0.020 1 701 76 76 MET C C 176.443 0.200 1 702 76 76 MET CA C 56.535 0.200 1 703 76 76 MET CB C 32.673 0.200 1 704 76 76 MET CG C 31.711 0.200 1 705 76 76 MET CE C 16.599 0.200 1 706 76 76 MET N N 118.509 0.200 1 707 77 77 LYS H H 7.817 0.020 1 708 77 77 LYS HA H 4.300 0.020 1 709 77 77 LYS HB3 H 1.837 0.020 1 710 77 77 LYS HG3 H 1.429 0.020 1 711 77 77 LYS HD3 H 1.632 0.020 1 712 77 77 LYS HE2 H 2.951 0.020 1 713 77 77 LYS C C 176.406 0.200 1 714 77 77 LYS CA C 56.527 0.200 1 715 77 77 LYS CB C 32.619 0.200 1 716 77 77 LYS CG C 24.029 0.200 1 717 77 77 LYS CD C 28.543 0.200 1 718 77 77 LYS CE C 41.771 0.200 1 719 77 77 LYS N N 120.357 0.200 1 720 78 78 ASP H H 8.218 0.020 1 721 78 78 ASP HA H 4.670 0.020 1 722 78 78 ASP HB2 H 2.642 0.020 1 723 78 78 ASP C C 176.590 0.200 1 724 78 78 ASP CA C 54.576 0.200 1 725 78 78 ASP CB C 40.895 0.200 1 726 78 78 ASP N N 121.572 0.200 1 727 79 79 THR H H 8.031 0.020 1 728 79 79 THR HA H 4.311 0.020 1 729 79 79 THR HB H 4.244 0.020 1 730 79 79 THR HG2 H 1.160 0.020 1 731 79 79 THR C C 174.547 0.200 1 732 79 79 THR CA C 62.160 0.200 1 733 79 79 THR CB C 69.695 0.200 1 734 79 79 THR CG2 C 21.138 0.200 1 735 79 79 THR N N 114.417 0.200 1 736 80 80 ASP H H 8.377 0.020 1 737 80 80 ASP HA H 4.694 0.020 1 738 80 80 ASP HB2 H 2.675 0.020 1 739 80 80 ASP C C 176.645 0.200 1 740 80 80 ASP CA C 54.614 0.200 1 741 80 80 ASP CB C 41.061 0.200 1 742 80 80 ASP N N 123.053 0.200 1 743 81 81 SER H H 8.324 0.020 1 744 81 81 SER HA H 4.462 0.020 1 745 81 81 SER HB2 H 4.030 0.020 1 746 81 81 SER C C 175.410 0.200 1 747 81 81 SER CA C 59.023 0.200 1 748 81 81 SER CB C 63.660 0.200 1 749 81 81 SER N N 116.800 0.200 1 750 82 82 GLU H H 8.499 0.020 1 751 82 82 GLU HA H 4.134 0.020 1 752 82 82 GLU HB2 H 2.070 0.020 1 753 82 82 GLU HG2 H 2.269 0.020 1 754 82 82 GLU C C 177.921 0.200 1 755 82 82 GLU CA C 58.786 0.200 1 756 82 82 GLU CB C 29.204 0.200 1 757 82 82 GLU CG C 36.143 0.200 1 758 82 82 GLU N N 122.704 0.200 1 759 83 83 GLU H H 8.309 0.020 1 760 83 83 GLU HA H 4.035 0.020 1 761 83 83 GLU HB2 H 2.065 0.020 1 762 83 83 GLU HG2 H 2.301 0.020 1 763 83 83 GLU C C 178.664 0.200 1 764 83 83 GLU CA C 59.475 0.200 1 765 83 83 GLU CB C 28.966 0.200 1 766 83 83 GLU CG C 35.830 0.200 1 767 83 83 GLU N N 119.473 0.200 1 768 84 84 GLU H H 8.076 0.020 1 769 84 84 GLU HA H 4.136 0.020 1 770 84 84 GLU HB2 H 2.162 0.020 1 771 84 84 GLU HG2 H 2.295 0.020 1 772 84 84 GLU C C 179.596 0.200 1 773 84 84 GLU CA C 59.298 0.200 1 774 84 84 GLU CB C 29.198 0.200 1 775 84 84 GLU CG C 36.236 0.200 1 776 84 84 GLU N N 118.827 0.200 1 777 85 85 ILE H H 7.994 0.020 1 778 85 85 ILE HA H 4.001 0.020 1 779 85 85 ILE HB H 2.128 0.020 1 780 85 85 ILE HG12 H 1.051 0.020 1 781 85 85 ILE HG2 H 1.056 0.020 1 782 85 85 ILE HD1 H 0.729 0.020 1 783 85 85 ILE C C 177.918 0.200 1 784 85 85 ILE CA C 64.705 0.200 1 785 85 85 ILE CB C 37.208 0.200 1 786 85 85 ILE CG1 C 28.599 0.200 1 787 85 85 ILE CG2 C 18.446 0.200 1 788 85 85 ILE CD1 C 12.474 0.200 1 789 85 85 ILE N N 122.006 0.200 1 790 86 86 ARG H H 8.370 0.020 1 791 86 86 ARG HA H 4.148 0.020 1 792 86 86 ARG HB3 H 1.828 0.020 1 793 86 86 ARG HG3 H 1.680 0.020 1 794 86 86 ARG HD2 H 2.964 0.020 1 795 86 86 ARG C C 179.336 0.200 1 796 86 86 ARG CA C 60.039 0.200 1 797 86 86 ARG CB C 29.488 0.200 1 798 86 86 ARG CG C 27.058 0.200 1 799 86 86 ARG CD C 42.885 0.200 1 800 86 86 ARG N N 121.659 0.200 1 801 87 87 GLU H H 8.047 0.020 1 802 87 87 GLU HA H 4.118 0.020 1 803 87 87 GLU HB2 H 2.124 0.020 1 804 87 87 GLU HG2 H 2.308 0.020 1 805 87 87 GLU C C 178.569 0.200 1 806 87 87 GLU CA C 58.973 0.200 1 807 87 87 GLU CB C 28.836 0.200 1 808 87 87 GLU CG C 35.552 0.200 1 809 87 87 GLU N N 118.625 0.200 1 810 88 88 ALA H H 7.934 0.020 1 811 88 88 ALA HA H 4.184 0.020 1 812 88 88 ALA HB H 1.744 0.020 1 813 88 88 ALA C C 179.220 0.200 1 814 88 88 ALA CA C 55.025 0.200 1 815 88 88 ALA CB C 17.253 0.200 1 816 88 88 ALA N N 121.901 0.200 1 817 89 89 PHE H H 8.519 0.020 1 818 89 89 PHE HA H 3.119 0.020 1 819 89 89 PHE HB3 H 3.189 0.020 1 820 89 89 PHE HE1 H 6.968 0.020 1 821 89 89 PHE HE2 H 6.968 0.020 1 822 89 89 PHE C C 176.480 0.200 1 823 89 89 PHE CA C 62.097 0.200 1 824 89 89 PHE CB C 38.698 0.200 1 825 89 89 PHE CE1 C 130.939 0.200 1 826 89 89 PHE N N 118.835 0.200 1 827 90 90 ARG H H 7.633 0.020 1 828 90 90 ARG HA H 3.869 0.020 1 829 90 90 ARG HB3 H 1.924 0.020 1 830 90 90 ARG HG3 H 1.860 0.020 1 831 90 90 ARG HD2 H 3.208 0.020 1 832 90 90 ARG C C 178.218 0.200 1 833 90 90 ARG CA C 58.780 0.200 1 834 90 90 ARG CB C 29.820 0.200 1 835 90 90 ARG CG C 27.313 0.200 1 836 90 90 ARG CD C 43.206 0.200 1 837 90 90 ARG N N 115.549 0.200 1 838 91 91 VAL H H 7.512 0.020 1 839 91 91 VAL HA H 3.495 0.020 1 840 91 91 VAL HB H 2.105 0.020 1 841 91 91 VAL HG2 H 0.945 0.020 1 842 91 91 VAL C C 177.398 0.200 1 843 91 91 VAL CA C 65.593 0.200 1 844 91 91 VAL CB C 31.260 0.200 1 845 91 91 VAL CG2 C 22.067 0.200 1 846 91 91 VAL N N 118.347 0.200 1 847 92 92 PHE H H 7.500 0.020 1 848 92 92 PHE HA H 4.222 0.020 1 849 92 92 PHE HB3 H 2.652 0.020 1 850 92 92 PHE HE1 H 7.351 0.020 1 851 92 92 PHE HE2 H 7.351 0.020 1 852 92 92 PHE C C 177.001 0.200 1 853 92 92 PHE CA C 59.911 0.200 1 854 92 92 PHE CB C 39.881 0.200 1 855 92 92 PHE CE1 C 130.846 0.200 1 856 92 92 PHE N N 116.488 0.200 1 857 93 93 ASP H H 7.791 0.020 1 858 93 93 ASP HA H 4.521 0.020 1 859 93 93 ASP HB2 H 1.356 0.020 1 860 93 93 ASP C C 177.491 0.200 1 861 93 93 ASP CA C 52.281 0.200 1 862 93 93 ASP CB C 38.005 0.200 1 863 93 93 ASP N N 117.006 0.200 1 864 94 94 LYS H H 7.677 0.020 1 865 94 94 LYS HA H 3.892 0.020 1 866 94 94 LYS HB3 H 1.798 0.020 1 867 94 94 LYS HG3 H 1.485 0.020 1 868 94 94 LYS HD3 H 1.598 0.020 1 869 94 94 LYS HE2 H 2.806 0.020 1 870 94 94 LYS C C 178.297 0.200 1 871 94 94 LYS CA C 58.920 0.200 1 872 94 94 LYS CB C 32.307 0.200 1 873 94 94 LYS CG C 23.748 0.200 1 874 94 94 LYS CD C 27.927 0.200 1 875 94 94 LYS CE C 41.405 0.200 1 876 94 94 LYS N N 125.892 0.200 1 877 95 95 ASP H H 8.176 0.020 1 878 95 95 ASP HA H 4.543 0.020 1 879 95 95 ASP HB2 H 3.046 0.020 1 880 95 95 ASP C C 177.734 0.200 1 881 95 95 ASP CA C 53.000 0.200 1 882 95 95 ASP CB C 39.342 0.200 1 883 95 95 ASP N N 114.077 0.200 1 884 96 96 GLY H H 7.741 0.020 1 885 96 96 GLY HA3 H 3.825 0.020 1 886 96 96 GLY C C 175.116 0.200 1 887 96 96 GLY CA C 46.962 0.200 1 888 96 96 GLY N N 109.201 0.200 1 889 97 97 ASN H H 8.293 0.020 1 890 97 97 ASN HA H 4.632 0.020 1 891 97 97 ASN HB2 H 3.378 0.020 1 892 97 97 ASN HD21 H 7.986 0.020 2 893 97 97 ASN HD22 H 7.265 0.020 2 894 97 97 ASN C C 176.091 0.200 1 895 97 97 ASN CA C 52.671 0.200 1 896 97 97 ASN CB C 37.941 0.200 1 897 97 97 ASN N N 119.484 0.200 1 898 97 97 ASN ND2 N 116.156 0.200 1 899 98 98 GLY H H 10.590 0.020 1 900 98 98 GLY HA3 H 4.023 0.020 1 901 98 98 GLY C C 172.420 0.200 1 902 98 98 GLY CA C 44.926 0.200 1 903 98 98 GLY N N 112.901 0.200 1 904 99 99 TYR H H 7.581 0.020 1 905 99 99 TYR HA H 5.033 0.020 1 906 99 99 TYR HB3 H 2.497 0.020 1 907 99 99 TYR HE1 H 6.904 0.020 1 908 99 99 TYR HE2 H 6.904 0.020 1 909 99 99 TYR C C 174.588 0.200 1 910 99 99 TYR CA C 56.025 0.200 1 911 99 99 TYR CB C 42.751 0.200 1 912 99 99 TYR CE1 C 118.190 0.200 1 913 99 99 TYR N N 115.802 0.200 1 914 100 100 ILE H H 10.087 0.020 1 915 100 100 ILE HA H 4.816 0.020 1 916 100 100 ILE HB H 1.842 0.020 1 917 100 100 ILE HG12 H 0.325 0.020 1 918 100 100 ILE HG2 H 0.895 0.020 1 919 100 100 ILE HD1 H 0.206 0.020 1 920 100 100 ILE C C 175.576 0.200 1 921 100 100 ILE CA C 60.274 0.200 1 922 100 100 ILE CB C 38.387 0.200 1 923 100 100 ILE CG1 C 26.594 0.200 1 924 100 100 ILE CG2 C 17.308 0.200 1 925 100 100 ILE CD1 C 14.377 0.200 1 926 100 100 ILE N N 127.366 0.200 1 927 101 101 SER H H 8.947 0.020 1 928 101 101 SER HA H 4.829 0.020 1 929 101 101 SER HB2 H 4.393 0.020 1 930 101 101 SER C C 175.275 0.200 1 931 101 101 SER CA C 55.835 0.200 1 932 101 101 SER CB C 66.337 0.200 1 933 101 101 SER N N 123.769 0.200 1 934 102 102 ALA H H 9.156 0.020 1 935 102 102 ALA HA H 3.900 0.020 1 936 102 102 ALA HB H 1.434 0.020 1 937 102 102 ALA C C 179.352 0.200 1 938 102 102 ALA CA C 55.918 0.200 1 939 102 102 ALA CB C 17.514 0.200 1 940 102 102 ALA N N 122.942 0.200 1 941 103 103 ALA H H 8.178 0.020 1 942 103 103 ALA HA H 4.017 0.020 1 943 103 103 ALA HB H 1.378 0.020 1 944 103 103 ALA C C 181.339 0.200 1 945 103 103 ALA CA C 55.080 0.200 1 946 103 103 ALA CB C 17.907 0.200 1 947 103 103 ALA N N 118.263 0.200 1 948 104 104 GLU H H 7.801 0.020 1 949 104 104 GLU HA H 4.040 0.020 1 950 104 104 GLU HB2 H 2.507 0.020 1 951 104 104 GLU HG2 H 2.293 0.020 1 952 104 104 GLU C C 179.286 0.200 1 953 104 104 GLU CA C 59.265 0.200 1 954 104 104 GLU CB C 28.922 0.200 1 955 104 104 GLU CG C 37.571 0.200 1 956 104 104 GLU N N 119.679 0.200 1 957 105 105 LEU H H 8.547 0.020 1 958 105 105 LEU HA H 4.088 0.020 1 959 105 105 LEU HB3 H 1.827 0.020 1 960 105 105 LEU HG H 1.595 0.020 1 961 105 105 LEU HD1 H 0.827 0.020 1 962 105 105 LEU C C 178.530 0.200 1 963 105 105 LEU CA C 58.228 0.200 1 964 105 105 LEU CB C 41.671 0.200 1 965 105 105 LEU CG C 26.696 0.200 1 966 105 105 LEU CD1 C 23.814 0.200 1 967 105 105 LEU N N 121.039 0.200 1 968 106 106 ARG H H 8.490 0.020 1 969 106 106 ARG HA H 3.793 0.020 1 970 106 106 ARG HB3 H 1.900 0.020 1 971 106 106 ARG HG3 H 1.618 0.020 1 972 106 106 ARG HD2 H 3.114 0.020 1 973 106 106 ARG C C 178.659 0.200 1 974 106 106 ARG CA C 59.808 0.200 1 975 106 106 ARG CB C 30.068 0.200 1 976 106 106 ARG CG C 27.330 0.200 1 977 106 106 ARG CD C 43.361 0.200 1 978 106 106 ARG N N 117.424 0.200 1 979 107 107 HIS H H 7.871 0.020 1 980 107 107 HIS HA H 4.310 0.020 1 981 107 107 HIS HB3 H 3.301 0.020 1 982 107 107 HIS HD2 H 6.961 0.020 1 983 107 107 HIS HE1 H 7.850 0.020 1 984 107 107 HIS C C 177.407 0.200 1 985 107 107 HIS CA C 59.465 0.200 1 986 107 107 HIS CB C 30.259 0.200 1 987 107 107 HIS CD2 C 120.426 0.200 1 988 107 107 HIS CE1 C 138.686 0.200 1 989 107 107 HIS N N 118.677 0.200 1 990 108 108 VAL H H 7.887 0.020 1 991 108 108 VAL HA H 3.487 0.020 1 992 108 108 VAL HB H 1.937 0.020 1 993 108 108 VAL HG2 H 0.774 0.020 1 994 108 108 VAL C C 178.015 0.200 1 995 108 108 VAL CA C 65.963 0.200 1 996 108 108 VAL CB C 31.493 0.200 1 997 108 108 VAL CG2 C 22.339 0.200 1 998 108 108 VAL N N 118.754 0.200 1 999 109 109 MET H H 8.196 0.020 1 1000 109 109 MET HA H 4.328 0.020 1 1001 109 109 MET HB2 H 2.116 0.020 1 1002 109 109 MET HG2 H 2.717 0.020 1 1003 109 109 MET HE H 2.003 0.020 1 1004 109 109 MET C C 178.593 0.200 1 1005 109 109 MET CA C 57.539 0.200 1 1006 109 109 MET CB C 31.022 0.200 1 1007 109 109 MET CG C 32.644 0.200 1 1008 109 109 MET CE C 17.100 0.200 1 1009 109 109 MET N N 116.554 0.200 1 1010 110 110 THR H H 8.089 0.020 1 1011 110 110 THR HA H 4.180 0.020 1 1012 110 110 THR HB H 4.270 0.020 1 1013 110 110 THR HG2 H 1.198 0.020 1 1014 110 110 THR C C 177.450 0.200 1 1015 110 110 THR CA C 65.612 0.200 1 1016 110 110 THR CB C 68.998 0.200 1 1017 110 110 THR CG2 C 21.005 0.200 1 1018 110 110 THR N N 114.621 0.200 1 1019 111 111 ASN H H 7.869 0.020 1 1020 111 111 ASN HA H 4.496 0.020 1 1021 111 111 ASN HB2 H 2.779 0.020 1 1022 111 111 ASN HD21 H 7.390 0.020 2 1023 111 111 ASN HD22 H 6.549 0.020 2 1024 111 111 ASN C C 176.233 0.200 1 1025 111 111 ASN CA C 55.576 0.200 1 1026 111 111 ASN CB C 38.311 0.200 1 1027 111 111 ASN N N 122.005 0.200 1 1028 111 111 ASN ND2 N 111.589 0.200 1 1029 112 112 LEU H H 7.818 0.020 1 1030 112 112 LEU HA H 4.301 0.020 1 1031 112 112 LEU HB3 H 1.685 0.020 1 1032 112 112 LEU HG H 1.736 0.020 1 1033 112 112 LEU HD1 H 0.802 0.020 1 1034 112 112 LEU C C 177.371 0.200 1 1035 112 112 LEU CA C 55.353 0.200 1 1036 112 112 LEU CB C 41.698 0.200 1 1037 112 112 LEU CG C 26.074 0.200 1 1038 112 112 LEU CD1 C 24.825 0.200 1 1039 112 112 LEU N N 118.910 0.200 1 1040 113 113 GLY H H 7.817 0.020 1 1041 113 113 GLY HA3 H 4.190 0.020 1 1042 113 113 GLY C C 174.385 0.200 1 1043 113 113 GLY CA C 45.285 0.200 1 1044 113 113 GLY N N 106.632 0.200 1 1045 114 114 GLU H H 7.881 0.020 1 1046 114 114 GLU HA H 4.394 0.020 1 1047 114 114 GLU HB2 H 1.710 0.020 1 1048 114 114 GLU HG2 H 2.092 0.020 1 1049 114 114 GLU C C 175.571 0.200 1 1050 114 114 GLU CA C 55.399 0.200 1 1051 114 114 GLU CB C 30.113 0.200 1 1052 114 114 GLU CG C 35.121 0.200 1 1053 114 114 GLU N N 120.491 0.200 1 1054 115 115 LYS H H 8.462 0.020 1 1055 115 115 LYS HA H 4.353 0.020 1 1056 115 115 LYS HB3 H 1.748 0.020 1 1057 115 115 LYS HG3 H 1.359 0.020 1 1058 115 115 LYS HD3 H 1.619 0.020 1 1059 115 115 LYS HE2 H 2.944 0.020 1 1060 115 115 LYS C C 175.668 0.200 1 1061 115 115 LYS CA C 55.703 0.200 1 1062 115 115 LYS CB C 31.643 0.200 1 1063 115 115 LYS CG C 24.074 0.200 1 1064 115 115 LYS CD C 28.522 0.200 1 1065 115 115 LYS CE C 41.803 0.200 1 1066 115 115 LYS N N 123.688 0.200 1 1067 116 116 LEU H H 7.995 0.020 1 1068 116 116 LEU HA H 4.727 0.020 1 1069 116 116 LEU HB3 H 1.522 0.020 1 1070 116 116 LEU HG H 1.521 0.020 1 1071 116 116 LEU HD1 H 0.745 0.020 1 1072 116 116 LEU C C 177.962 0.200 1 1073 116 116 LEU CA C 54.156 0.200 1 1074 116 116 LEU CB C 44.267 0.200 1 1075 116 116 LEU CG C 26.984 0.200 1 1076 116 116 LEU CD1 C 25.878 0.200 1 1077 116 116 LEU N N 124.584 0.200 1 1078 117 117 THR H H 9.034 0.020 1 1079 117 117 THR HA H 4.457 0.020 1 1080 117 117 THR HB H 4.708 0.020 1 1081 117 117 THR HG2 H 1.286 0.020 1 1082 117 117 THR C C 175.534 0.200 1 1083 117 117 THR CA C 60.736 0.200 1 1084 117 117 THR CB C 71.198 0.200 1 1085 117 117 THR CG2 C 21.330 0.200 1 1086 117 117 THR N N 114.412 0.200 1 1087 118 118 ASP H H 8.807 0.020 1 1088 118 118 ASP HA H 4.196 0.020 1 1089 118 118 ASP HB2 H 2.554 0.020 1 1090 118 118 ASP C C 178.590 0.200 1 1091 118 118 ASP CA C 58.016 0.200 1 1092 118 118 ASP CB C 39.552 0.200 1 1093 118 118 ASP N N 120.966 0.200 1 1094 119 119 GLU H H 8.627 0.020 1 1095 119 119 GLU HA H 4.084 0.020 1 1096 119 119 GLU HB2 H 2.011 0.020 1 1097 119 119 GLU HG2 H 2.359 0.020 1 1098 119 119 GLU C C 179.183 0.200 1 1099 119 119 GLU CA C 59.870 0.200 1 1100 119 119 GLU CB C 28.763 0.200 1 1101 119 119 GLU CG C 36.415 0.200 1 1102 119 119 GLU N N 118.995 0.200 1 1103 120 120 GLU H H 7.702 0.020 1 1104 120 120 GLU HA H 3.999 0.020 1 1105 120 120 GLU HB2 H 2.339 0.020 1 1106 120 120 GLU HG2 H 2.228 0.020 1 1107 120 120 GLU C C 179.964 0.200 1 1108 120 120 GLU CA C 59.204 0.200 1 1109 120 120 GLU CB C 30.095 0.200 1 1110 120 120 GLU CG C 37.473 0.200 1 1111 120 120 GLU N N 120.439 0.200 1 1112 121 121 VAL H H 8.040 0.020 1 1113 121 121 VAL HA H 3.605 0.020 1 1114 121 121 VAL HB H 2.176 0.020 1 1115 121 121 VAL HG2 H 0.910 0.020 1 1116 121 121 VAL C C 177.264 0.200 1 1117 121 121 VAL CA C 66.879 0.200 1 1118 121 121 VAL CB C 31.024 0.200 1 1119 121 121 VAL CG2 C 23.172 0.200 1 1120 121 121 VAL N N 121.097 0.200 1 1121 122 122 ASP H H 8.000 0.020 1 1122 122 122 ASP HA H 4.315 0.020 1 1123 122 122 ASP HB2 H 2.735 0.020 1 1124 122 122 ASP C C 179.172 0.200 1 1125 122 122 ASP CA C 57.644 0.200 1 1126 122 122 ASP CB C 40.314 0.200 1 1127 122 122 ASP N N 119.691 0.200 1 1128 123 123 GLU H H 7.925 0.020 1 1129 123 123 GLU HA H 3.979 0.020 1 1130 123 123 GLU HB2 H 2.087 0.020 1 1131 123 123 GLU HG2 H 2.237 0.020 1 1132 123 123 GLU C C 177.983 0.200 1 1133 123 123 GLU CA C 59.199 0.200 1 1134 123 123 GLU CB C 29.026 0.200 1 1135 123 123 GLU CG C 35.911 0.200 1 1136 123 123 GLU N N 119.419 0.200 1 1137 124 124 MET H H 7.793 0.020 1 1138 124 124 MET HA H 4.010 0.020 1 1139 124 124 MET HB2 H 2.235 0.020 1 1140 124 124 MET HG2 H 2.435 0.020 1 1141 124 124 MET HE H 1.829 0.020 1 1142 124 124 MET C C 179.275 0.200 1 1143 124 124 MET CA C 59.404 0.200 1 1144 124 124 MET CB C 32.960 0.200 1 1145 124 124 MET CG C 31.907 0.200 1 1146 124 124 MET CE C 16.602 0.200 1 1147 124 124 MET N N 119.476 0.200 1 1148 125 125 ILE H H 7.925 0.020 1 1149 125 125 ILE HA H 3.491 0.020 1 1150 125 125 ILE HB H 2.061 0.020 1 1151 125 125 ILE HG12 H 1.200 0.020 1 1152 125 125 ILE HG2 H 0.686 0.020 1 1153 125 125 ILE HD1 H 0.673 0.020 1 1154 125 125 ILE C C 177.140 0.200 1 1155 125 125 ILE CA C 63.973 0.200 1 1156 125 125 ILE CB C 36.283 0.200 1 1157 125 125 ILE CG1 C 27.821 0.200 1 1158 125 125 ILE CG2 C 15.809 0.200 1 1159 125 125 ILE CD1 C 10.521 0.200 1 1160 125 125 ILE N N 118.429 0.200 1 1161 126 126 ARG H H 8.131 0.020 1 1162 126 126 ARG HA H 3.998 0.020 1 1163 126 126 ARG HB3 H 1.830 0.020 1 1164 126 126 ARG HG3 H 1.729 0.020 1 1165 126 126 ARG HD2 H 3.176 0.020 1 1166 126 126 ARG C C 179.407 0.200 1 1167 126 126 ARG CA C 59.673 0.200 1 1168 126 126 ARG CB C 29.762 0.200 1 1169 126 126 ARG CG C 27.345 0.200 1 1170 126 126 ARG CD C 43.117 0.200 1 1171 126 126 ARG N N 118.442 0.200 1 1172 127 127 GLU H H 7.907 0.020 1 1173 127 127 GLU HA H 3.981 0.020 1 1174 127 127 GLU HB2 H 2.028 0.020 1 1175 127 127 GLU HG2 H 2.245 0.020 1 1176 127 127 GLU C C 177.300 0.200 1 1177 127 127 GLU CA C 58.393 0.200 1 1178 127 127 GLU CB C 29.252 0.200 1 1179 127 127 GLU CG C 35.455 0.200 1 1180 127 127 GLU N N 116.056 0.200 1 1181 128 128 ALA H H 7.352 0.020 1 1182 128 128 ALA HA H 4.390 0.020 1 1183 128 128 ALA HB H 1.383 0.020 1 1184 128 128 ALA C C 177.775 0.200 1 1185 128 128 ALA CA C 52.032 0.200 1 1186 128 128 ALA CB C 20.661 0.200 1 1187 128 128 ALA N N 119.117 0.200 1 1188 129 129 ASP H H 7.814 0.020 1 1189 129 129 ASP HA H 4.499 0.020 1 1190 129 129 ASP HB2 H 2.460 0.020 1 1191 129 129 ASP C C 176.121 0.200 1 1192 129 129 ASP CA C 54.011 0.200 1 1193 129 129 ASP CB C 40.061 0.200 1 1194 129 129 ASP N N 117.434 0.200 1 1195 130 130 ILE H H 8.384 0.020 1 1196 130 130 ILE HA H 3.907 0.020 1 1197 130 130 ILE HB H 1.969 0.020 1 1198 130 130 ILE HG12 H 1.285 0.020 1 1199 130 130 ILE HG2 H 0.897 0.020 1 1200 130 130 ILE HD1 H 0.834 0.020 1 1201 130 130 ILE C C 177.879 0.200 1 1202 130 130 ILE CA C 63.314 0.200 1 1203 130 130 ILE CB C 38.397 0.200 1 1204 130 130 ILE CG1 C 27.351 0.200 1 1205 130 130 ILE CG2 C 16.825 0.200 1 1206 130 130 ILE CD1 C 11.746 0.200 1 1207 130 130 ILE N N 127.886 0.200 1 1208 131 131 ASP H H 8.255 0.020 1 1209 131 131 ASP HA H 4.536 0.020 1 1210 131 131 ASP HB2 H 3.052 0.020 1 1211 131 131 ASP C C 178.314 0.200 1 1212 131 131 ASP CA C 53.769 0.200 1 1213 131 131 ASP CB C 39.680 0.200 1 1214 131 131 ASP N N 116.747 0.200 1 1215 132 132 GLY H H 7.548 0.020 1 1216 132 132 GLY HA3 H 3.947 0.020 1 1217 132 132 GLY C C 175.292 0.200 1 1218 132 132 GLY CA C 47.300 0.200 1 1219 132 132 GLY N N 108.436 0.200 1 1220 133 133 ASP H H 8.308 0.020 1 1221 133 133 ASP HA H 4.459 0.020 1 1222 133 133 ASP HB2 H 2.916 0.020 1 1223 133 133 ASP C C 177.639 0.200 1 1224 133 133 ASP CA C 53.633 0.200 1 1225 133 133 ASP CB C 39.965 0.200 1 1226 133 133 ASP N N 120.799 0.200 1 1227 134 134 GLY H H 10.304 0.020 1 1228 134 134 GLY HA3 H 4.010 0.020 1 1229 134 134 GLY C C 172.900 0.200 1 1230 134 134 GLY CA C 45.551 0.200 1 1231 134 134 GLY N N 112.879 0.200 1 1232 135 135 GLN H H 7.938 0.020 1 1233 135 135 GLN HA H 4.835 0.020 1 1234 135 135 GLN HB2 H 1.654 0.020 1 1235 135 135 GLN HG2 H 1.894 0.020 1 1236 135 135 GLN HE21 H 6.447 0.020 2 1237 135 135 GLN HE22 H 5.845 0.020 2 1238 135 135 GLN C C 174.755 0.200 1 1239 135 135 GLN CA C 53.124 0.200 1 1240 135 135 GLN CB C 31.956 0.200 1 1241 135 135 GLN CG C 32.727 0.200 1 1242 135 135 GLN N N 115.492 0.200 1 1243 135 135 GLN NE2 N 108.617 0.200 1 1244 136 136 VAL H H 9.106 0.020 1 1245 136 136 VAL HA H 5.184 0.020 1 1246 136 136 VAL HB H 2.262 0.020 1 1247 136 136 VAL HG2 H 0.852 0.020 1 1248 136 136 VAL C C 175.877 0.200 1 1249 136 136 VAL CA C 61.678 0.200 1 1250 136 136 VAL CB C 33.311 0.200 1 1251 136 136 VAL CG2 C 21.660 0.200 1 1252 136 136 VAL N N 125.413 0.200 1 1253 137 137 ASN H H 9.525 0.020 1 1254 137 137 ASN HA H 5.197 0.020 1 1255 137 137 ASN HB2 H 3.285 0.020 1 1256 137 137 ASN HD21 H 7.186 0.020 2 1257 137 137 ASN HD22 H 6.798 0.020 2 1258 137 137 ASN C C 174.926 0.200 1 1259 137 137 ASN CA C 51.139 0.200 1 1260 137 137 ASN CB C 38.031 0.200 1 1261 137 137 ASN N N 128.942 0.200 1 1262 137 137 ASN ND2 N 108.462 0.200 1 1263 138 138 TYR H H 8.402 0.020 1 1264 138 138 TYR HA H 3.423 0.020 1 1265 138 138 TYR HB3 H 2.378 0.020 1 1266 138 138 TYR HE1 H 6.496 0.020 1 1267 138 138 TYR HE2 H 6.496 0.020 1 1268 138 138 TYR C C 176.108 0.200 1 1269 138 138 TYR CA C 62.796 0.200 1 1270 138 138 TYR CB C 37.281 0.200 1 1271 138 138 TYR CE1 C 117.907 0.200 1 1272 138 138 TYR N N 118.326 0.200 1 1273 139 139 GLU H H 8.040 0.020 1 1274 139 139 GLU HA H 3.642 0.020 1 1275 139 139 GLU HB2 H 2.063 0.020 1 1276 139 139 GLU HG2 H 2.342 0.020 1 1277 139 139 GLU C C 180.590 0.200 1 1278 139 139 GLU CA C 60.352 0.200 1 1279 139 139 GLU CB C 28.566 0.200 1 1280 139 139 GLU CG C 36.774 0.200 1 1281 139 139 GLU N N 118.323 0.200 1 1282 140 140 GLU H H 8.712 0.020 1 1283 140 140 GLU HA H 4.014 0.020 1 1284 140 140 GLU HB2 H 2.531 0.020 1 1285 140 140 GLU HG2 H 2.425 0.020 1 1286 140 140 GLU C C 179.360 0.200 1 1287 140 140 GLU CA C 58.439 0.200 1 1288 140 140 GLU CB C 29.485 0.200 1 1289 140 140 GLU CG C 36.690 0.200 1 1290 140 140 GLU N N 119.793 0.200 1 1291 141 141 PHE H H 8.922 0.020 1 1292 141 141 PHE HA H 3.979 0.020 1 1293 141 141 PHE HB3 H 3.357 0.020 1 1294 141 141 PHE HE1 H 7.111 0.020 1 1295 141 141 PHE HE2 H 7.111 0.020 1 1296 141 141 PHE C C 176.828 0.200 1 1297 141 141 PHE CA C 61.555 0.200 1 1298 141 141 PHE CB C 39.434 0.200 1 1299 141 141 PHE CE1 C 131.328 0.200 1 1300 141 141 PHE N N 124.588 0.200 1 1301 142 142 VAL H H 8.487 0.020 1 1302 142 142 VAL HA H 3.119 0.020 1 1303 142 142 VAL HB H 1.843 0.020 1 1304 142 142 VAL HG2 H 0.478 0.020 1 1305 142 142 VAL C C 179.535 0.200 1 1306 142 142 VAL CA C 67.011 0.200 1 1307 142 142 VAL CB C 31.203 0.200 1 1308 142 142 VAL CG2 C 22.203 0.200 1 1309 142 142 VAL N N 119.468 0.200 1 1310 143 143 GLN H H 7.362 0.020 1 1311 143 143 GLN HA H 3.877 0.020 1 1312 143 143 GLN HB2 H 2.079 0.020 1 1313 143 143 GLN HG2 H 2.354 0.020 1 1314 143 143 GLN HE21 H 7.392 0.020 2 1315 143 143 GLN HE22 H 6.695 0.020 2 1316 143 143 GLN C C 177.899 0.200 1 1317 143 143 GLN CA C 58.794 0.200 1 1318 143 143 GLN CB C 27.800 0.200 1 1319 143 143 GLN CG C 33.637 0.200 1 1320 143 143 GLN N N 118.091 0.200 1 1321 143 143 GLN NE2 N 111.739 0.200 1 1322 144 144 MET H H 7.914 0.020 1 1323 144 144 MET HA H 4.076 0.020 1 1324 144 144 MET HB2 H 2.044 0.020 1 1325 144 144 MET HG2 H 2.295 0.020 1 1326 144 144 MET HE H 1.989 0.020 1 1327 144 144 MET C C 177.954 0.200 1 1328 144 144 MET CA C 58.343 0.200 1 1329 144 144 MET CB C 33.025 0.200 1 1330 144 144 MET CG C 30.975 0.200 1 1331 144 144 MET CE C 16.755 0.200 1 1332 144 144 MET N N 119.591 0.200 1 1333 145 145 MET H H 7.816 0.020 1 1334 145 145 MET HA H 4.280 0.020 1 1335 145 145 MET HB2 H 1.590 0.020 1 1336 145 145 MET HG2 H 1.635 0.020 1 1337 145 145 MET HE H 1.787 0.020 1 1338 145 145 MET C C 177.500 0.200 1 1339 145 145 MET CA C 55.285 0.200 1 1340 145 145 MET CB C 31.741 0.200 1 1341 145 145 MET CG C 31.767 0.200 1 1342 145 145 MET CE C 16.600 0.200 1 1343 145 145 MET N N 114.764 0.200 1 1344 146 146 THR H H 7.551 0.020 1 1345 146 146 THR HA H 4.291 0.020 1 1346 146 146 THR HB H 4.219 0.020 1 1347 146 146 THR HG2 H 1.124 0.020 1 1348 146 146 THR C C 174.272 0.200 1 1349 146 146 THR CA C 62.573 0.200 1 1350 146 146 THR CB C 70.160 0.200 1 1351 146 146 THR CG2 C 20.780 0.200 1 1352 146 146 THR N N 111.346 0.200 1 1353 147 147 ALA H H 7.697 0.020 1 1354 147 147 ALA HA H 4.291 0.020 1 1355 147 147 ALA HB H 1.354 0.020 1 1356 147 147 ALA C C 176.660 0.200 1 1357 147 147 ALA CA C 52.780 0.200 1 1358 147 147 ALA CB C 18.579 0.200 1 1359 147 147 ALA N N 126.416 0.200 1 1360 148 148 LYS H H 7.661 0.020 1 1361 148 148 LYS HA H 4.113 0.020 1 1362 148 148 LYS HB3 H 1.776 0.020 1 1363 148 148 LYS HG3 H 1.347 0.020 1 1364 148 148 LYS HD3 H 1.612 0.020 1 1365 148 148 LYS HE2 H 2.934 0.020 1 1366 148 148 LYS C C 178.918 0.200 1 1367 148 148 LYS CA C 57.478 0.200 1 1368 148 148 LYS CB C 33.235 0.200 1 1369 148 148 LYS CG C 24.110 0.200 1 1370 148 148 LYS CD C 28.510 0.200 1 1371 148 148 LYS CE C 41.935 0.200 1 1372 148 148 LYS N N 125.503 0.200 1 stop_ save_