data_4270 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignment of Ca2+/calmodulin (1H, 13C, and 15N) Complexed with Its Binding Domain from Rat Ca2+/calmodulin Dependent Protein Kinase Kinase (1H). ; _BMRB_accession_number 4270 _BMRB_flat_file_name bmr4270.str _Entry_type original _Submission_date 1998-11-18 _Accession_date 1998-11-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Ca2+/calmodulin - 26-residue-peptide complex' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Osawa Masanori . . 2 Tokumitsu Hiroshi . . 3 Swindells Mark B . 4 Kurihara Hiroyuki . . 5 Orita Masaya . . 6 Shibanuma Tadao . . 7 Furuya Toshio . . 8 Ikura Mitsuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 947 "13C chemical shifts" 601 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-07-13 original author . stop_ _Original_release_date 2007-07-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Osawa, M., Tokumitsu, H., Swindells, M.B., Kurihara, H., Orita, M., Shibanuma, T., Furuya, T., Ikura, M., "A Novel Target Recognition Revealed by Calmodulin in Complex with Ca2+-calmodulin-dependent Kinase Kinase," Nat. Struct. Biol. 6, 819-824 (1999). ; _Citation_title 'A Novel Target Recognition Revealed by Calmodulin in Complex with Ca2+-calmodulin-dependent Kinase Kinase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99396734 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Osawa Masanori . . 2 Tokumitsu Hiroshi . . 3 Swindells Mark B . 4 Kurihara Hiroyuki . . 5 Orita Masaya . . 6 Shibanuma Tadao . . 7 Furuya Toshio . . 8 Ikura Mitsuhiko . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 6 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 819 _Page_last 824 _Year 1999 _Details . loop_ _Keyword 'calmodulin dependent protein kinase kinase' 'calmodulin target peptide complex' stop_ save_ ################################## # Molecular system description # ################################## save_system_CaM-CaMKK _Saveframe_category molecular_system _Mol_system_name 'Ca2+/calmodulin - 26-residue peptide from rat Ca2+/calmodulin dependent protein kinase kinase complex' _Abbreviation_common 'Ca2+/CaM - CaMKK complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label calmodulin $cam camkk $camkk stop_ _System_molecular_weight 20000 _System_physical_state native _System_oligomer_state monomeric _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cam _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common calmodulin _Abbreviation_common Cam _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_author_seq_code _Residue_label 1 1 ALA 2 2 ASP 3 3 GLN 4 4 LEU 5 5 THR 6 6 GLU 7 7 GLU 8 8 GLN 9 9 ILE 10 10 ALA 11 11 GLU 12 12 PHE 13 13 LYS 14 14 GLU 15 15 ALA 16 16 PHE 17 17 SER 18 18 LEU 19 19 PHE 20 20 ASP 21 21 LYS 22 22 ASP 23 23 GLY 24 24 ASP 25 25 GLY 26 26 THR 27 27 ILE 28 28 THR 29 29 THR 30 30 LYS 31 31 GLU 32 32 LEU 33 33 GLY 34 34 THR 35 35 VAL 36 36 MET 37 37 ARG 38 38 SER 39 39 LEU 40 40 GLY 41 41 GLN 42 42 ASN 43 43 PRO 44 44 THR 45 45 GLU 46 46 ALA 47 47 GLU 48 48 LEU 49 49 GLN 50 50 ASP 51 51 MET 52 52 ILE 53 53 ASN 54 54 GLU 55 55 VAL 56 56 ASP 57 57 ALA 58 58 ASP 59 59 GLY 60 60 ASN 61 61 GLY 62 62 THR 63 63 ILE 64 64 ASP 65 65 PHE 66 66 PRO 67 67 GLU 68 68 PHE 69 69 LEU 70 70 THR 71 71 MET 72 72 MET 73 73 ALA 74 74 ARG 75 75 LYS 76 76 MET 77 77 LYS 78 78 ASP 79 79 THR 80 80 ASP 81 81 SER 82 82 GLU 83 83 GLU 84 84 GLU 85 85 ILE 86 86 ARG 87 87 GLU 88 88 ALA 89 89 PHE 90 90 ARG 91 91 VAL 92 92 PHE 93 93 ASP 94 94 LYS 95 95 ASP 96 96 GLY 97 97 ASN 98 98 GLY 99 99 TYR 100 100 ILE 101 101 SER 102 102 ALA 103 103 ALA 104 104 GLU 105 105 LEU 106 106 ARG 107 107 HIS 108 108 VAL 109 109 MET 110 110 THR 111 111 ASN 112 112 LEU 113 113 GLY 114 114 GLU 115 115 LYS 116 116 LEU 117 117 THR 118 118 ASP 119 119 GLU 120 120 GLU 121 121 VAL 122 122 ASP 123 123 GLU 124 124 MET 125 125 ILE 126 126 ARG 127 127 GLU 128 128 ALA 129 129 ASP 130 130 ILE 131 131 ASP 132 132 GLY 133 133 ASP 134 134 GLY 135 135 GLN 136 136 VAL 137 137 ASN 138 138 TYR 139 139 GLU 140 140 GLU 141 141 PHE 142 142 VAL 143 143 GLN 144 144 MET 145 145 MET 146 146 THR 147 147 ALA 148 148 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 15184 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15185 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15186 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15187 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15188 calmodulin 100.00 148 99.32 100.00 9.29e-100 BMRB 15191 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15470 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15624 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15650 calmodulin 100.00 148 99.32 100.00 3.16e-99 BMRB 15852 calmodulin 100.00 148 99.32 100.00 3.16e-99 BMRB 1634 calmodulin 100.00 148 97.30 99.32 2.41e-97 BMRB 16418 apoCaM 100.00 148 100.00 100.00 4.67e-100 BMRB 16465 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 1648 calmodulin 100.00 148 97.30 99.32 2.41e-97 BMRB 16764 CALMODULIN 100.00 150 100.00 100.00 4.99e-100 BMRB 17264 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 17360 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 17771 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 17807 Calmodulin 99.32 147 100.00 100.00 2.43e-99 BMRB 18027 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 18028 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 18556 Calmodulin 100.00 148 98.65 99.32 2.52e-98 BMRB 19036 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 19238 Calmodulin_prototypical_calcium_sensor 100.00 148 100.00 100.00 4.67e-100 BMRB 19586 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 19604 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 25253 CaM 100.00 148 98.65 99.32 1.16e-97 BMRB 25257 CaM 100.00 148 98.65 99.32 1.16e-97 BMRB 26503 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 26626 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 26627 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 4056 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 4284 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 4310 calmodulin 100.00 148 100.00 100.00 4.67e-100 PDB 1A29 "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" 100.00 148 100.00 100.00 4.67e-100 PDB 1CFC "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1CFD "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 4.67e-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 4.67e-100 PDB 1CKK "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" 100.00 148 100.00 100.00 4.67e-100 PDB 1CLL "Calmodulin Structure Refined At 1.7 Angstroms Resolution" 100.00 148 100.00 100.00 4.67e-100 PDB 1CM1 "Motions Of Calmodulin-Single-Conformer Refinement" 100.00 148 100.00 100.00 4.67e-100 PDB 1CM4 "Motions Of Calmodulin-four-conformer Refinement" 100.00 148 100.00 100.00 4.67e-100 PDB 1CTR "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 1DMO "Calmodulin, Nmr, 30 Structures" 100.00 148 99.32 100.00 1.91e-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 4.67e-100 PDB 1IQ5 "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" 100.00 149 100.00 100.00 4.88e-100 PDB 1IWQ "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" 100.00 148 100.00 100.00 4.67e-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 4.67e-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 4.20e-97 PDB 1L7Z "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 1LIN "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" 100.00 148 100.00 100.00 4.67e-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 4.88e-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 4.67e-100 PDB 1MXE "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" 100.00 148 97.97 99.32 6.44e-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 4.67e-100 PDB 1OOJ "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" 100.00 149 97.97 98.65 1.21e-97 PDB 1PRW "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" 100.00 149 99.32 99.32 4.06e-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 4.67e-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 4.67e-100 PDB 1QX5 "Crystal Structure Of Apocalmodulin" 100.00 148 100.00 100.00 4.67e-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 4.67e-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 4.67e-100 PDB 1SY9 "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" 100.00 148 100.00 100.00 4.67e-100 PDB 1UP5 "Chicken Calmodulin" 100.00 148 99.32 99.32 3.93e-99 PDB 1WRZ "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" 100.00 149 100.00 100.00 4.88e-100 PDB 1X02 "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1XA5 "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" 100.00 148 100.00 100.00 4.67e-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 1.16e-99 PDB 1XFV "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 149 99.32 100.00 1.16e-99 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 1.16e-99 PDB 1XFY "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 100.00 149 99.32 100.00 1.16e-99 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 1.16e-99 PDB 1Y0V "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" 97.30 146 100.00 100.00 3.61e-97 PDB 1YR5 "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" 100.00 148 100.00 100.00 4.67e-100 PDB 2BBM "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 6.44e-98 PDB 2BBN "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 6.44e-98 PDB 2BCX "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2BKH "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 2BKI "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" 100.00 149 100.00 100.00 4.88e-100 PDB 2DFS "3-D Structure Of Myosin-V Inhibited State" 100.00 148 100.00 100.00 4.67e-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 7.52e-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 7.52e-100 PDB 2F3Y "CalmodulinIQ DOMAIN COMPLEX" 100.00 148 100.00 100.00 4.67e-100 PDB 2F3Z "CalmodulinIQ-Aa Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2FOT "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" 100.00 148 100.00 100.00 4.67e-100 PDB 2HQW "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2JZI "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0E "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0F "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0J "Solution Structure Of Cam Complexed To Drp1p" 100.00 148 99.32 100.00 3.16e-99 PDB 2K61 "Solution Structure Of Cam Complexed To Dapk Peptide" 100.00 148 99.32 100.00 3.16e-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 4.67e-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 4.67e-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 4.67e-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 4.67e-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 1.01e-98 PDB 2LL6 "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2LL7 "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 4.67e-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 2.52e-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 4.67e-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 4.67e-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 4.67e-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 4.67e-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 4.67e-100 PDB 2O5G "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2O60 "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" 100.00 148 100.00 100.00 4.67e-100 PDB 2R28 "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" 100.00 149 100.00 100.00 4.88e-100 PDB 2V01 "Recombinant Vertebrate Calmodulin Complexed With Pb" 100.00 149 100.00 100.00 4.88e-100 PDB 2V02 "Recombinant Vertebrate Calmodulin Complexed With Ba" 100.00 149 100.00 100.00 4.88e-100 PDB 2VAS "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" 100.00 149 97.97 99.32 4.90e-98 PDB 2VAY "Calmodulin Complexed With Cav1.1 Iq Peptide" 98.65 146 100.00 100.00 1.01e-98 PDB 2VB6 "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" 100.00 149 97.30 99.32 1.19e-97 PDB 2W73 "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" 100.00 149 100.00 100.00 4.88e-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 4.52e-100 PDB 2X0G "X-ray Structure Of A Dap-kinase Calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2X51 "M6 Delta Insert1" 100.00 149 97.97 99.32 4.90e-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 4.88e-100 PDB 2YGG "Complex Of Cambr And Cam" 100.00 150 100.00 100.00 5.33e-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 4.67e-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 4.67e-100 PDB 3BYA "Structure Of A Calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3CLN "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" 100.00 148 99.32 100.00 1.91e-99 PDB 3DVE "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-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 4.67e-100 PDB 3DVK "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3DVM "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3EK4 "Calcium-saturated Gcamp2 Monomer" 99.32 449 100.00 100.00 8.93e-96 PDB 3EK7 "Calcium-Saturated Gcamp2 Dimer" 99.32 449 100.00 100.00 8.93e-96 PDB 3EK8 "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" 99.32 449 100.00 100.00 1.26e-95 PDB 3EKH "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" 99.32 449 99.32 99.32 8.65e-95 PDB 3EVU "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" 99.32 449 100.00 100.00 8.93e-96 PDB 3EVV "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" 99.32 449 100.00 100.00 8.93e-96 PDB 3EWT "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.96e-100 PDB 3EWV "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.96e-100 PDB 3G43 "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" 100.00 148 100.00 100.00 4.67e-100 PDB 3GN4 "Myosin Lever Arm" 100.00 149 97.97 99.32 4.90e-98 PDB 3GOF "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" 100.00 148 100.00 100.00 4.67e-100 PDB 3HR4 "Human Inos Reductase And Calmodulin Complex" 100.00 149 100.00 100.00 4.88e-100 PDB 3IF7 "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" 100.00 148 100.00 100.00 4.67e-100 PDB 3J41 "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" 100.00 149 100.00 100.00 4.88e-100 PDB 3L9I "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 3O77 "The Structure Of Ca2+ Sensor (Case-16)" 99.32 415 100.00 100.00 4.01e-96 PDB 3O78 "The Structure Of Ca2+ Sensor (Case-12)" 99.32 415 100.00 100.00 4.42e-96 PDB 3OXQ "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" 100.00 149 100.00 100.00 4.88e-100 PDB 3SG2 "Crystal Structure Of Gcamp2-t116v,d381y" 99.32 449 99.32 99.32 1.28e-94 PDB 3SG3 "Crystal Structure Of Gcamp3-d380y" 99.32 449 98.64 99.32 1.62e-93 PDB 3SG4 "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" 100.00 448 97.97 98.65 1.11e-93 PDB 3SG5 "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" 100.00 448 97.97 98.65 9.15e-94 PDB 3SG6 "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" 99.32 450 100.00 100.00 1.14e-95 PDB 3SG7 "Crystal Structure Of Gcamp3-kf(linker 1)" 99.32 448 99.32 100.00 7.62e-95 PDB 3SJQ "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 3SUI "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" 100.00 149 100.00 100.00 4.88e-100 PDB 3U0K "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" 99.32 440 98.64 99.32 2.73e-94 PDB 3WFN "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" 100.00 182 100.00 100.00 5.62e-100 PDB 4ANJ "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" 100.00 149 97.97 99.32 4.90e-98 PDB 4BW7 "Calmodulin In Complex With Strontium" 100.00 149 100.00 100.00 4.88e-100 PDB 4BW8 "Calmodulin With Small Bend In Central Helix" 100.00 149 100.00 100.00 4.88e-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 4.88e-100 PDB 4CLN "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" 100.00 148 97.97 99.32 6.44e-98 PDB 4DBP "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 4DBQ "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" 100.00 149 97.97 99.32 4.90e-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 4.88e-100 PDB 4DJC "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" 100.00 152 100.00 100.00 3.41e-100 PDB 4E50 "Calmodulin And Ng Peptide Complex" 100.00 185 100.00 100.00 2.54e-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 4.67e-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 4.88e-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 4.88e-100 PDB 4HEX "A Novel Conformation Of Calmodulin" 100.00 156 100.00 100.00 2.09e-100 PDB 4IK1 "High Resolution Structure Of Gcampj At Ph 8.5" 99.32 448 98.64 99.32 1.39e-93 PDB 4IK3 "High Resolution Structure Of Gcamp3 At Ph 8.5" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK4 "High Resolution Structure Of Gcamp3 At Ph 5.0" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK5 "High Resolution Structure Of Delta-rest-gcamp3" 99.32 414 99.32 100.00 3.55e-95 PDB 4IK8 "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK9 "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" 99.32 448 99.32 100.00 9.06e-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 4.88e-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 4.88e-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 4.88e-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 4.88e-100 PDB 4L79 "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4LZX "Complex Of Iqcg And Ca2+-free Cam" 100.00 148 100.00 100.00 4.67e-100 PDB 4M1L "Complex Of Iqcg And Ca2+-bound Cam" 100.00 148 100.00 100.00 4.67e-100 PDB 4PJJ "Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4" 100.00 149 97.30 99.32 1.19e-97 PDB 4Q5U "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" 100.00 149 100.00 100.00 4.88e-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 5.95e-99 PDB 4R8G "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 4UMO "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4UPU "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 4V0C "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA08302 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA11896 "calmodulin [Anas platyrhynchos]" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA19786 "calmodulin [Branchiostoma lanceolatum]" 100.00 149 97.97 99.32 4.90e-98 DBJ BAA19787 "calmodulin [Branchiostoma floridae]" 100.00 149 97.97 99.32 4.90e-98 DBJ BAA19788 "calmodulin [Halocynthia roretzi]" 100.00 149 97.97 99.32 4.90e-98 EMBL CAA10601 "calmodulin [Caenorhabditis elegans]" 100.00 149 97.97 98.65 1.21e-97 EMBL CAA32050 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32062 "calmodulin II [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32119 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32120 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA35635 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 GB AAA35641 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 GB AAA37365 "calmodulin synthesis [Mus musculus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA40862 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA40863 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 PIR JC1305 "calmodulin - Japanese medaka" 100.00 149 100.00 100.00 4.88e-100 PIR MCON "calmodulin - salmon" 100.00 148 100.00 100.00 4.67e-100 PRF 0409298A "troponin C-like protein" 100.00 148 97.30 100.00 2.41e-98 PRF 0608335A calmodulin 100.00 148 97.97 99.32 3.31e-97 REF NP_001008160 "calmodulin [Xenopus (Silurana) tropicalis]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001009759 "calmodulin [Ovis aries]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001027633 "calmodulin [Ciona intestinalis]" 100.00 149 97.30 98.65 3.17e-97 REF NP_001039714 "calmodulin [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001040234 "calmodulin [Bombyx mori]" 100.00 149 97.97 99.32 4.90e-98 SP O02367 "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM" 100.00 149 97.30 98.65 3.17e-97 SP O16305 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 97.97 98.65 1.21e-97 SP O96081 "RecName: Full=Calmodulin-B; Short=CaM B" 100.00 149 97.30 98.65 3.58e-97 SP P02594 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 99.32 100.00 1.57e-99 SP P05932 "RecName: Full=Calmodulin-beta; Short=Cam B" 93.24 138 97.10 99.28 5.00e-90 TPG DAA13808 "TPA: calmodulin 2-like [Bos taurus]" 100.00 216 98.65 98.65 2.37e-98 TPG DAA18029 "TPA: calmodulin [Bos taurus]" 100.00 149 98.65 99.32 7.17e-99 TPG DAA19590 "TPA: calmodulin 3 [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 TPG DAA24777 "TPA: calmodulin 2-like [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 TPG DAA24988 "TPA: calmodulin 2-like isoform 1 [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 stop_ save_ save_camkk _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ca2+/calmodulin dependent protein kinase kinase complex' _Abbreviation_common Camkk _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 26 _Mol_residue_sequence ; VKLIPSWTTVILVKSMLRKR SFGNPF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 LYS 3 3 LEU 4 4 ILE 5 5 PRO 6 6 SER 7 7 TRP 8 8 THR 9 9 THR 10 10 VAL 11 11 ILE 12 12 LEU 13 13 VAL 14 14 LYS 15 15 SER 16 16 MET 17 17 LEU 18 18 ARG 19 19 LYS 20 20 ARG 21 21 SER 22 22 PHE 23 23 GLY 24 24 ASN 25 25 PRO 26 26 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic no _Mol_aromatic . _Details . 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 'not present' _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 $cam 'African clawed frog' 8355 Eukaryota Metazoa Xenopus laevis $camkk rat 10116 Eukaryota Metazoa Rattus norvegicus 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 _Details $cam 'recombinant technology' 'E. coli' . . . . 'Xenopus laevis' $camkk 'chemical synthesis' . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cam 1.5 mM '[U-13C, U-15N]' $camkk 1.875 mM . 'potassium chloride' 100 mM . 'calcium chloride' 10.6 mM . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_one loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $cam 95 % 'SDS gel electrophoresis' $camkk 95 % HPLC stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.1 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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_citation_label _Correction_value_citation_label TSP C 13 'methyl protons' . . external indirect . 'external to the sample' parallel $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.0 external direct . 'external to the sample' parallel $entry_citation $entry_citation TSP N 15 'methyl protons' . . external indirect . 'external to the sample' parallel $entry_citation $entry_citation 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _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 . 2 ASP HA H 4.58 0.02 1 2 . 2 ASP HB2 H 2.52 0.02 2 3 . 2 ASP HB3 H 2.61 0.02 2 4 . 2 ASP C C 175.55 0.30 1 5 . 2 ASP CA C 54.81 0.30 1 6 . 2 ASP CB C 41.36 0.30 1 7 . 3 GLN H H 8.23 0.02 1 8 . 3 GLN HA H 4.35 0.02 1 9 . 3 GLN HB2 H 1.95 0.02 2 10 . 3 GLN HB3 H 2.08 0.02 2 11 . 3 GLN HG2 H 2.33 0.02 1 12 . 3 GLN HG3 H 2.33 0.02 1 13 . 3 GLN C C 175.64 0.30 1 14 . 3 GLN CA C 55.40 0.30 1 15 . 3 GLN CB C 30.11 0.30 1 16 . 3 GLN CG C 33.72 0.30 1 17 . 3 GLN N N 119.14 0.20 1 18 . 4 LEU H H 8.24 0.02 1 19 . 4 LEU HA H 4.61 0.02 1 20 . 4 LEU HB2 H 1.52 0.02 2 21 . 4 LEU HB3 H 1.68 0.02 2 22 . 4 LEU HG H 1.70 0.02 1 23 . 4 LEU HD1 H 0.91 0.02 1 24 . 4 LEU HD2 H 0.87 0.02 1 25 . 4 LEU C C 177.46 0.30 1 26 . 4 LEU CA C 54.42 0.30 1 27 . 4 LEU CB C 43.47 0.30 1 28 . 4 LEU CG C 27.21 0.30 1 29 . 4 LEU CD1 C 26.87 0.30 1 30 . 4 LEU CD2 C 24.00 0.30 1 31 . 4 LEU N N 122.60 0.20 1 32 . 5 THR H H 8.56 0.02 1 33 . 5 THR HA H 4.43 0.02 1 34 . 5 THR HB H 4.76 0.02 1 35 . 5 THR HG2 H 1.31 0.02 1 36 . 5 THR C C 175.42 0.30 1 37 . 5 THR CA C 60.33 0.30 1 38 . 5 THR CB C 71.66 0.30 1 39 . 5 THR CG2 C 21.65 0.30 1 40 . 5 THR N N 112.54 0.20 1 41 . 6 GLU H H 8.98 0.02 1 42 . 6 GLU HA H 3.93 0.02 1 43 . 6 GLU HB2 H 2.01 0.02 1 44 . 6 GLU HB3 H 2.01 0.02 1 45 . 6 GLU HG2 H 2.35 0.02 1 46 . 6 GLU HG3 H 2.35 0.02 1 47 . 6 GLU C C 179.54 0.30 1 48 . 6 GLU CA C 60.15 0.30 1 49 . 6 GLU CB C 29.24 0.30 1 50 . 6 GLU CG C 36.62 0.30 1 51 . 6 GLU N N 120.30 0.20 1 52 . 7 GLU H H 8.68 0.02 1 53 . 7 GLU HA H 4.06 0.02 1 54 . 7 GLU HB2 H 1.94 0.02 1 55 . 7 GLU HB3 H 1.94 0.02 1 56 . 7 GLU HG2 H 2.33 0.02 1 57 . 7 GLU HG3 H 2.33 0.02 1 58 . 7 GLU C C 179.06 0.30 1 59 . 7 GLU CA C 59.86 0.30 1 60 . 7 GLU CB C 29.12 0.30 1 61 . 7 GLU CG C 36.90 0.30 1 62 . 7 GLU N N 119.27 0.20 1 63 . 8 GLN H H 7.70 0.02 1 64 . 8 GLN HA H 3.78 0.02 1 65 . 8 GLN HB2 H 1.56 0.02 2 66 . 8 GLN HB3 H 2.33 0.02 2 67 . 8 GLN HG2 H 2.48 0.02 1 68 . 8 GLN HG3 H 2.48 0.02 1 69 . 8 GLN C C 178.02 0.30 1 70 . 8 GLN CA C 58.82 0.30 1 71 . 8 GLN CB C 30.48 0.30 1 72 . 8 GLN CG C 34.80 0.30 1 73 . 8 GLN N N 120.37 0.20 1 74 . 9 ILE H H 8.38 0.02 1 75 . 9 ILE HA H 3.59 0.02 1 76 . 9 ILE HB H 1.87 0.02 1 77 . 9 ILE HG12 H 1.01 0.02 2 78 . 9 ILE HG13 H 1.82 0.02 2 79 . 9 ILE HG2 H 1.14 0.02 1 80 . 9 ILE HD1 H 0.83 0.02 1 81 . 9 ILE C C 177.80 0.30 1 82 . 9 ILE CA C 66.62 0.30 1 83 . 9 ILE CB C 37.92 0.30 1 84 . 9 ILE CG1 C 30.42 0.30 1 85 . 9 ILE CG2 C 17.34 0.30 1 86 . 9 ILE CD1 C 13.09 0.30 1 87 . 9 ILE N N 119.44 0.20 1 88 . 10 ALA H H 7.93 0.02 1 89 . 10 ALA HA H 4.12 0.02 1 90 . 10 ALA HB H 1.49 0.02 1 91 . 10 ALA C C 181.13 0.30 1 92 . 10 ALA CA C 55.42 0.30 1 93 . 10 ALA CB C 17.82 0.30 1 94 . 10 ALA N N 120.80 0.20 1 95 . 11 GLU H H 7.82 0.02 1 96 . 11 GLU HA H 4.05 0.02 1 97 . 11 GLU HB2 H 1.88 0.02 1 98 . 11 GLU HB3 H 1.88 0.02 1 99 . 11 GLU HG2 H 2.25 0.02 1 100 . 11 GLU HG3 H 2.25 0.02 1 101 . 11 GLU C C 180.54 0.30 1 102 . 11 GLU CA C 59.18 0.30 1 103 . 11 GLU CB C 29.13 0.30 1 104 . 11 GLU CG C 35.97 0.30 1 105 . 11 GLU N N 119.43 0.20 1 106 . 12 PHE H H 8.67 0.02 1 107 . 12 PHE HA H 5.07 0.02 1 108 . 12 PHE HB2 H 3.45 0.02 1 109 . 12 PHE HB3 H 3.45 0.02 1 110 . 12 PHE HD1 H 7.06 0.02 3 111 . 12 PHE HE1 H 6.77 0.02 3 112 . 12 PHE C C 178.70 0.30 1 113 . 12 PHE CA C 58.70 0.30 1 114 . 12 PHE CB C 37.09 0.30 1 115 . 12 PHE CD1 C 129.79 0.30 3 116 . 12 PHE CE1 C 129.70 0.30 3 117 . 12 PHE N N 120.04 0.20 1 118 . 13 LYS H H 9.21 0.02 1 119 . 13 LYS HA H 3.97 0.02 1 120 . 13 LYS HB2 H 1.88 0.02 2 121 . 13 LYS HB3 H 1.97 0.02 2 122 . 13 LYS HG2 H 1.07 0.02 1 123 . 13 LYS HG3 H 1.07 0.02 1 124 . 13 LYS HD2 H 1.18 0.02 2 125 . 13 LYS HD3 H 1.31 0.02 2 126 . 13 LYS HE2 H 2.57 0.02 1 127 . 13 LYS HE3 H 2.57 0.02 1 128 . 13 LYS C C 179.27 0.30 1 129 . 13 LYS CA C 60.10 0.30 1 130 . 13 LYS CB C 31.57 0.30 1 131 . 13 LYS CG C 25.33 0.30 1 132 . 13 LYS CD C 28.66 0.30 1 133 . 13 LYS CE C 41.85 0.30 1 134 . 13 LYS N N 124.60 0.20 1 135 . 14 GLU H H 7.66 0.02 1 136 . 14 GLU HA H 4.19 0.02 1 137 . 14 GLU HB2 H 2.17 0.02 1 138 . 14 GLU HB3 H 2.17 0.02 1 139 . 14 GLU HG2 H 2.40 0.02 1 140 . 14 GLU HG3 H 2.40 0.02 1 141 . 14 GLU C C 179.96 0.30 1 142 . 14 GLU CA C 59.19 0.30 1 143 . 14 GLU CB C 28.86 0.30 1 144 . 14 GLU CG C 36.13 0.30 1 145 . 14 GLU N N 119.17 0.20 1 146 . 15 ALA H H 7.98 0.02 1 147 . 15 ALA HA H 4.12 0.02 1 148 . 15 ALA HB H 2.08 0.02 1 149 . 15 ALA C C 177.99 0.30 1 150 . 15 ALA CA C 55.67 0.30 1 151 . 15 ALA CB C 18.30 0.30 1 152 . 15 ALA N N 121.81 0.20 1 153 . 16 PHE H H 8.81 0.02 1 154 . 16 PHE HA H 3.39 0.02 1 155 . 16 PHE HB2 H 2.66 0.02 2 156 . 16 PHE HB3 H 3.18 0.02 2 157 . 16 PHE HD1 H 6.74 0.02 3 158 . 16 PHE HE1 H 7.04 0.02 3 159 . 16 PHE HZ H 7.24 0.02 1 160 . 16 PHE C C 177.90 0.30 1 161 . 16 PHE CA C 62.22 0.30 1 162 . 16 PHE CB C 39.76 0.30 1 163 . 16 PHE CD1 C 131.89 0.30 3 164 . 16 PHE CE1 C 131.28 0.30 3 165 . 16 PHE N N 119.23 0.20 1 166 . 17 SER H H 8.20 0.02 1 167 . 17 SER HA H 4.11 0.02 1 168 . 17 SER HB2 H 4.00 0.02 2 169 . 17 SER C C 174.53 0.30 1 170 . 17 SER CA C 61.62 0.30 1 171 . 17 SER CB C 63.21 0.30 1 172 . 17 SER N N 113.52 0.20 1 173 . 18 LEU H H 7.21 0.02 1 174 . 18 LEU HA H 3.93 0.02 1 175 . 18 LEU HB2 H 1.38 0.02 2 176 . 18 LEU HB3 H 1.99 0.02 2 177 . 18 LEU HG H 0.96 0.02 1 178 . 18 LEU HD1 H 0.67 0.02 1 179 . 18 LEU HD2 H 0.58 0.02 1 180 . 18 LEU C C 176.61 0.30 1 181 . 18 LEU CA C 57.38 0.30 1 182 . 18 LEU CB C 41.31 0.30 1 183 . 18 LEU CG C 25.84 0.30 1 184 . 18 LEU CD1 C 22.92 0.30 1 185 . 18 LEU CD2 C 25.86 0.30 1 186 . 18 LEU N N 120.49 0.20 1 187 . 19 PHE H H 6.88 0.02 1 188 . 19 PHE HA H 4.10 0.02 1 189 . 19 PHE HB2 H 2.83 0.02 1 190 . 19 PHE HB3 H 2.83 0.02 1 191 . 19 PHE HD1 H 7.52 0.02 3 192 . 19 PHE HE1 H 7.26 0.02 3 193 . 19 PHE C C 176.32 0.30 1 194 . 19 PHE CA C 59.35 0.30 1 195 . 19 PHE CB C 41.33 0.30 1 196 . 19 PHE CD1 C 133.23 0.30 3 197 . 19 PHE CE1 C 131.15 0.30 3 198 . 19 PHE N N 111.67 0.20 1 199 . 20 ASP H H 7.85 0.02 1 200 . 20 ASP HA H 4.61 0.02 1 201 . 20 ASP HB2 H 1.61 0.02 2 202 . 20 ASP HB3 H 2.42 0.02 2 203 . 20 ASP C C 177.22 0.30 1 204 . 20 ASP CA C 52.44 0.30 1 205 . 20 ASP CB C 39.20 0.30 1 206 . 20 ASP N N 117.14 0.20 1 207 . 21 LYS H H 7.79 0.02 1 208 . 21 LYS HA H 3.97 0.02 1 209 . 21 LYS HB2 H 1.86 0.02 1 210 . 21 LYS HB3 H 1.86 0.02 1 211 . 21 LYS HG2 H 1.53 0.02 1 212 . 21 LYS HG3 H 1.53 0.02 1 213 . 21 LYS HD2 H 1.66 0.02 1 214 . 21 LYS HD3 H 1.66 0.02 1 215 . 21 LYS HE2 H 3.01 0.02 1 216 . 21 LYS HE3 H 3.01 0.02 1 217 . 21 LYS C C 178.30 0.30 1 218 . 21 LYS CA C 58.24 0.30 1 219 . 21 LYS CB C 32.63 0.30 1 220 . 21 LYS CG C 24.35 0.30 1 221 . 21 LYS CD C 28.54 0.30 1 222 . 21 LYS CE C 41.74 0.30 1 223 . 21 LYS N N 124.18 0.20 1 224 . 22 ASP H H 8.09 0.02 1 225 . 22 ASP HA H 4.59 0.02 1 226 . 22 ASP HB2 H 2.62 0.02 2 227 . 22 ASP HB3 H 3.04 0.02 2 228 . 22 ASP C C 177.72 0.30 1 229 . 22 ASP CA C 52.86 0.30 1 230 . 22 ASP CB C 39.53 0.30 1 231 . 22 ASP N N 113.94 0.20 1 232 . 23 GLY H H 7.66 0.02 1 233 . 23 GLY HA2 H 3.84 0.02 1 234 . 23 GLY HA3 H 3.84 0.02 1 235 . 23 GLY C C 175.17 0.30 1 236 . 23 GLY CA C 47.22 0.30 1 237 . 23 GLY N N 109.05 0.20 1 238 . 24 ASP H H 8.44 0.02 1 239 . 24 ASP HA H 4.49 0.02 1 240 . 24 ASP HB2 H 2.45 0.02 2 241 . 24 ASP HB3 H 3.05 0.02 2 242 . 24 ASP C C 177.43 0.30 1 243 . 24 ASP CA C 53.73 0.30 1 244 . 24 ASP CB C 40.45 0.30 1 245 . 24 ASP N N 120.62 0.20 1 246 . 25 GLY H H 10.52 0.02 1 247 . 25 GLY HA2 H 3.70 0.02 1 248 . 25 GLY HA3 H 4.35 0.02 1 249 . 25 GLY C C 173.91 0.30 1 250 . 25 GLY CA C 45.40 0.30 1 251 . 25 GLY N N 112.63 0.20 1 252 . 26 THR H H 8.23 0.02 1 253 . 26 THR HA H 5.41 0.02 1 254 . 26 THR HB H 3.87 0.02 1 255 . 26 THR HG2 H 1.05 0.02 1 256 . 26 THR C C 173.32 0.30 1 257 . 26 THR CA C 59.49 0.30 1 258 . 26 THR CB C 72.59 0.30 1 259 . 26 THR CG2 C 22.03 0.30 1 260 . 26 THR N N 112.13 0.20 1 261 . 27 ILE H H 9.94 0.02 1 262 . 27 ILE HA H 4.87 0.02 1 263 . 27 ILE HB H 1.80 0.02 1 264 . 27 ILE HG12 H 1.18 0.02 2 265 . 27 ILE HG13 H 1.21 0.02 2 266 . 27 ILE HG2 H 0.98 0.02 1 267 . 27 ILE HD1 H 0.39 0.02 1 268 . 27 ILE C C 176.07 0.30 1 269 . 27 ILE CA C 61.01 0.30 1 270 . 27 ILE CB C 40.31 0.30 1 271 . 27 ILE CG1 C 27.28 0.30 1 272 . 27 ILE CG2 C 17.69 0.30 1 273 . 27 ILE CD1 C 16.04 0.30 1 274 . 27 ILE N N 126.74 0.20 1 275 . 28 THR H H 8.27 0.02 1 276 . 28 THR HA H 4.92 0.02 1 277 . 28 THR HB H 4.81 0.02 1 278 . 28 THR HG2 H 1.26 0.02 1 279 . 28 THR C C 176.56 0.30 1 280 . 28 THR CA C 59.03 0.30 1 281 . 28 THR CB C 73.09 0.30 1 282 . 28 THR CG2 C 21.64 0.30 1 283 . 28 THR N N 116.08 0.20 1 284 . 29 THR H H 9.09 0.02 1 285 . 29 THR HA H 3.67 0.02 1 286 . 29 THR HB H 4.16 0.02 1 287 . 29 THR HG2 H 1.22 0.02 1 288 . 29 THR C C 177.22 0.30 1 289 . 29 THR CA C 66.14 0.30 1 290 . 29 THR CB C 67.84 0.30 1 291 . 29 THR CG2 C 23.40 0.30 1 292 . 29 THR N N 112.66 0.20 1 293 . 30 LYS H H 7.59 0.02 1 294 . 30 LYS HA H 4.08 0.02 1 295 . 30 LYS HB2 H 1.78 0.02 1 296 . 30 LYS HB3 H 1.78 0.02 1 297 . 30 LYS HG2 H 1.45 0.02 1 298 . 30 LYS HG3 H 1.45 0.02 1 299 . 30 LYS HD2 H 1.66 0.02 1 300 . 30 LYS HD3 H 1.66 0.02 1 301 . 30 LYS HE2 H 2.96 0.02 1 302 . 30 LYS HE3 H 2.96 0.02 1 303 . 30 LYS C C 179.87 0.30 1 304 . 30 LYS CA C 59.12 0.30 1 305 . 30 LYS CB C 32.44 0.30 1 306 . 30 LYS CG C 24.95 0.30 1 307 . 30 LYS CD C 29.25 0.30 1 308 . 30 LYS CE C 42.03 0.30 1 309 . 30 LYS N N 120.59 0.20 1 310 . 31 GLU H H 7.72 0.02 1 311 . 31 GLU HA H 3.98 0.02 1 312 . 31 GLU HB2 H 2.35 0.02 1 313 . 31 GLU HB3 H 2.35 0.02 1 314 . 31 GLU HG2 H 2.52 0.02 1 315 . 31 GLU HG3 H 2.52 0.02 1 316 . 31 GLU C C 179.50 0.30 1 317 . 31 GLU CA C 59.57 0.30 1 318 . 31 GLU CB C 29.32 0.30 1 319 . 31 GLU CG C 38.70 0.30 1 320 . 31 GLU N N 122.03 0.20 1 321 . 32 LEU H H 8.35 0.02 1 322 . 32 LEU HA H 4.06 0.02 1 323 . 32 LEU HB2 H 1.01 0.02 2 324 . 32 LEU HB3 H 1.74 0.02 2 325 . 32 LEU HG H 1.10 0.02 1 326 . 32 LEU HD1 H -0.04 0.02 1 327 . 32 LEU HD2 H 0.29 0.02 1 328 . 32 LEU C C 179.08 0.30 1 329 . 32 LEU CA C 58.46 0.30 1 330 . 32 LEU CB C 42.19 0.30 1 331 . 32 LEU CG C 26.43 0.30 1 332 . 32 LEU CD1 C 22.47 0.30 1 333 . 32 LEU CD2 C 25.87 0.30 1 334 . 32 LEU N N 120.36 0.20 1 335 . 33 GLY H H 8.72 0.02 1 336 . 33 GLY HA2 H 3.43 0.02 2 337 . 33 GLY HA3 H 3.91 0.02 2 338 . 33 GLY C C 174.97 0.30 1 339 . 33 GLY CA C 48.57 0.30 1 340 . 33 GLY N N 105.57 0.20 1 341 . 34 THR H H 8.12 0.02 1 342 . 34 THR HA H 3.92 0.02 1 343 . 34 THR HB H 4.35 0.02 1 344 . 34 THR HG2 H 1.27 0.02 1 345 . 34 THR C C 177.09 0.30 1 346 . 34 THR CA C 67.02 0.30 1 347 . 34 THR CB C 68.08 0.30 1 348 . 34 THR CG2 C 21.33 0.30 1 349 . 34 THR N N 118.39 0.20 1 350 . 35 VAL H H 7.37 0.02 1 351 . 35 VAL HA H 3.70 0.02 1 352 . 35 VAL HB H 2.01 0.02 1 353 . 35 VAL HG1 H 0.58 0.02 1 354 . 35 VAL HG2 H 0.77 0.02 1 355 . 35 VAL C C 179.06 0.30 1 356 . 35 VAL CA C 66.19 0.30 1 357 . 35 VAL CB C 31.62 0.30 1 358 . 35 VAL CG1 C 20.27 0.30 1 359 . 35 VAL CG2 C 22.86 0.30 1 360 . 35 VAL N N 121.16 0.20 1 361 . 36 MET H H 8.30 0.02 1 362 . 36 MET HA H 4.13 0.02 1 363 . 36 MET HB2 H 1.61 0.02 2 364 . 36 MET HB3 H 2.12 0.02 2 365 . 36 MET HG2 H 2.29 0.02 2 366 . 36 MET HG3 H 2.68 0.02 2 367 . 36 MET HE H 1.86 0.02 1 368 . 36 MET C C 178.95 0.30 1 369 . 36 MET CA C 57.69 0.30 1 370 . 36 MET CB C 31.30 0.30 1 371 . 36 MET CG C 33.28 0.30 1 372 . 36 MET CE C 17.80 0.30 1 373 . 36 MET N N 117.18 0.20 1 374 . 37 ARG H H 8.75 0.02 1 375 . 37 ARG HA H 4.75 0.02 1 376 . 37 ARG HB2 H 2.31 0.02 1 377 . 37 ARG HB3 H 2.31 0.02 1 378 . 37 ARG HD2 H 3.26 0.02 1 379 . 37 ARG HD3 H 3.26 0.02 1 380 . 37 ARG C C 181.18 0.30 1 381 . 37 ARG CA C 59.18 0.30 1 382 . 37 ARG CB C 29.94 0.30 1 383 . 37 ARG CG C 29.71 0.30 1 384 . 37 ARG CD C 29.71 0.30 1 385 . 37 ARG N N 118.61 0.20 1 386 . 38 SER H H 7.91 0.02 1 387 . 38 SER HA H 4.34 0.02 1 388 . 38 SER HB2 H 4.04 0.02 2 389 . 38 SER HB3 H 4.11 0.02 2 390 . 38 SER C C 174.86 0.30 1 391 . 38 SER CA C 61.57 0.30 1 392 . 38 SER CB C 62.63 0.30 1 393 . 38 SER N N 119.21 0.20 1 394 . 39 LEU H H 7.22 0.02 1 395 . 39 LEU HA H 4.38 0.02 1 396 . 39 LEU HB2 H 1.87 0.02 2 397 . 39 LEU HB3 H 1.83 0.02 2 398 . 39 LEU HG H 1.83 0.02 1 399 . 39 LEU HD1 H 0.83 0.02 1 400 . 39 LEU HD2 H 0.76 0.02 1 401 . 39 LEU C C 177.36 0.30 1 402 . 39 LEU CA C 54.60 0.30 1 403 . 39 LEU CB C 42.05 0.30 1 404 . 39 LEU CG C 26.29 0.30 1 405 . 39 LEU CD1 C 26.24 0.30 1 406 . 39 LEU CD2 C 22.57 0.30 1 407 . 39 LEU N N 119.20 0.20 1 408 . 40 GLY H H 7.92 0.02 1 409 . 40 GLY HA2 H 3.79 0.02 2 410 . 40 GLY HA3 H 4.25 0.02 2 411 . 40 GLY C C 174.25 0.30 1 412 . 40 GLY CA C 45.50 0.30 1 413 . 40 GLY N N 106.91 0.20 1 414 . 41 GLN H H 7.55 0.02 1 415 . 41 GLN HA H 4.42 0.02 1 416 . 41 GLN HB2 H 1.54 0.02 2 417 . 41 GLN HB3 H 2.07 0.02 2 418 . 41 GLN HG2 H 2.18 0.02 1 419 . 41 GLN HG3 H 2.18 0.02 1 420 . 41 GLN HE21 H 6.65 0.02 9 421 . 41 GLN HE22 H 7.39 0.02 9 422 . 41 GLN C C 174.33 0.30 1 423 . 41 GLN CA C 53.37 0.30 1 424 . 41 GLN CB C 29.79 0.30 1 425 . 41 GLN CG C 33.01 0.30 1 426 . 41 GLN N N 116.77 0.20 1 427 . 41 GLN NE2 N 111.93 0.20 1 428 . 42 ASN H H 8.75 0.02 1 429 . 42 ASN HA H 5.20 0.02 1 430 . 42 ASN HB2 H 2.52 0.02 2 431 . 42 ASN HB3 H 2.77 0.02 2 432 . 42 ASN HD21 H 6.70 0.02 9 433 . 42 ASN HD22 H 7.49 0.02 9 434 . 42 ASN C C 173.08 0.30 1 435 . 42 ASN CA C 51.11 0.30 1 436 . 42 ASN CB C 39.20 0.30 1 437 . 42 ASN N N 116.78 0.20 1 438 . 42 ASN ND2 N 112.15 0.20 1 439 . 43 PRO HA H 4.74 0.02 1 440 . 43 PRO HB2 H 1.97 0.02 1 441 . 43 PRO HB3 H 1.97 0.02 1 442 . 43 PRO HG2 H 1.66 0.02 1 443 . 43 PRO HG3 H 1.66 0.02 1 444 . 43 PRO HD2 H 3.23 0.02 2 445 . 43 PRO HD3 H 3.67 0.02 2 446 . 43 PRO C C 177.24 0.30 1 447 . 43 PRO CA C 61.99 0.30 1 448 . 43 PRO CB C 32.09 0.30 1 449 . 43 PRO CG C 27.54 0.30 1 450 . 43 PRO CD C 49.88 0.30 1 451 . 44 THR H H 9.27 0.02 1 452 . 44 THR HA H 4.42 0.02 1 453 . 44 THR HB H 4.68 0.02 1 454 . 44 THR HG2 H 1.32 0.02 1 455 . 44 THR C C 175.25 0.30 1 456 . 44 THR CA C 60.47 0.30 1 457 . 44 THR CB C 71.66 0.30 1 458 . 44 THR CG2 C 21.89 0.30 1 459 . 44 THR N N 113.96 0.20 1 460 . 45 GLU H H 8.76 0.02 1 461 . 45 GLU HA H 3.94 0.02 1 462 . 45 GLU HB2 H 1.99 0.02 1 463 . 45 GLU HB3 H 1.99 0.02 1 464 . 45 GLU HG2 H 2.32 0.02 1 465 . 45 GLU HG3 H 2.32 0.02 1 466 . 45 GLU C C 178.89 0.30 1 467 . 45 GLU CA C 59.88 0.30 1 468 . 45 GLU CB C 28.92 0.30 1 469 . 45 GLU CG C 36.10 0.30 1 470 . 45 GLU N N 120.59 0.20 1 471 . 46 ALA H H 8.18 0.02 1 472 . 46 ALA HA H 4.08 0.02 1 473 . 46 ALA HB H 1.39 0.02 1 474 . 46 ALA C C 180.17 0.30 1 475 . 46 ALA CA C 55.02 0.30 1 476 . 46 ALA CB C 18.08 0.30 1 477 . 46 ALA N N 120.40 0.20 1 478 . 47 GLU H H 7.68 0.02 1 479 . 47 GLU HA H 3.97 0.02 1 480 . 47 GLU HB2 H 1.72 0.02 1 481 . 47 GLU HB3 H 1.72 0.02 1 482 . 47 GLU HG2 H 2.28 0.02 2 483 . 47 GLU HG3 H 2.33 0.02 2 484 . 47 GLU C C 180.24 0.30 1 485 . 47 GLU CA C 59.07 0.30 1 486 . 47 GLU CB C 29.77 0.30 1 487 . 47 GLU CG C 37.72 0.30 1 488 . 47 GLU N N 118.18 0.20 1 489 . 48 LEU H H 7.91 0.02 1 490 . 48 LEU HA H 3.94 0.02 1 491 . 48 LEU HB2 H 1.16 0.02 2 492 . 48 LEU HB3 H 2.05 0.02 2 493 . 48 LEU HG H 1.75 0.02 1 494 . 48 LEU HD1 H 0.82 0.02 1 495 . 48 LEU HD2 H 0.65 0.02 1 496 . 48 LEU C C 178.49 0.30 1 497 . 48 LEU CA C 57.55 0.30 1 498 . 48 LEU CB C 42.27 0.30 1 499 . 48 LEU CG C 26.56 0.30 1 500 . 48 LEU CD1 C 25.93 0.30 1 501 . 48 LEU CD2 C 22.43 0.30 1 502 . 48 LEU N N 119.21 0.20 1 503 . 49 GLN H H 8.43 0.02 1 504 . 49 GLN HA H 3.74 0.02 1 505 . 49 GLN HB2 H 2.14 0.02 2 506 . 49 GLN HB3 H 2.17 0.02 2 507 . 49 GLN HG2 H 2.42 0.02 1 508 . 49 GLN HG3 H 2.42 0.02 1 509 . 49 GLN HE21 H 6.95 0.02 9 510 . 49 GLN HE22 H 7.51 0.02 9 511 . 49 GLN C C 178.48 0.30 1 512 . 49 GLN CA C 58.49 0.30 1 513 . 49 GLN CB C 28.25 0.30 1 514 . 49 GLN CG C 34.10 0.30 1 515 . 49 GLN N N 118.79 0.20 1 516 . 49 GLN NE2 N 113.17 0.20 1 517 . 50 ASP H H 8.15 0.02 1 518 . 50 ASP HA H 4.41 0.02 1 519 . 50 ASP HB2 H 2.67 0.02 2 520 . 50 ASP HB3 H 2.77 0.02 2 521 . 50 ASP C C 178.76 0.30 1 522 . 50 ASP CA C 57.62 0.30 1 523 . 50 ASP CB C 40.31 0.30 1 524 . 50 ASP N N 119.52 0.20 1 525 . 51 MET H H 7.60 0.02 1 526 . 51 MET HA H 4.18 0.02 1 527 . 51 MET HB2 H 1.95 0.02 1 528 . 51 MET HB3 H 1.95 0.02 1 529 . 51 MET HG2 H 2.53 0.02 2 530 . 51 MET HG3 H 2.82 0.02 2 531 . 51 MET HE H 1.72 0.02 1 532 . 51 MET C C 179.30 0.30 1 533 . 51 MET CA C 59.71 0.30 1 534 . 51 MET CB C 31.70 0.30 1 535 . 51 MET CG C 33.24 0.30 1 536 . 51 MET CE C 16.89 0.30 1 537 . 51 MET N N 118.89 0.20 1 538 . 52 ILE H H 7.70 0.02 1 539 . 52 ILE HA H 3.85 0.02 1 540 . 52 ILE HB H 2.12 0.02 1 541 . 52 ILE HG12 H 1.43 0.02 2 542 . 52 ILE HG13 H 1.47 0.02 2 543 . 52 ILE HG2 H 0.78 0.02 1 544 . 52 ILE HD1 H 0.64 0.02 1 545 . 52 ILE C C 178.20 0.30 1 546 . 52 ILE CA C 63.16 0.30 1 547 . 52 ILE CB C 36.62 0.30 1 548 . 52 ILE CG1 C 28.50 0.30 1 549 . 52 ILE CG2 C 16.04 0.30 1 550 . 52 ILE CD1 C 10.97 0.30 1 551 . 52 ILE N N 118.94 0.20 1 552 . 53 ASN H H 8.88 0.02 1 553 . 53 ASN HA H 4.38 0.02 1 554 . 53 ASN HB2 H 2.89 0.02 2 555 . 53 ASN HB3 H 3.03 0.02 2 556 . 53 ASN HD21 H 6.96 0.02 9 557 . 53 ASN HD22 H 7.85 0.02 9 558 . 53 ASN C C 177.58 0.30 1 559 . 53 ASN CA C 55.90 0.30 1 560 . 53 ASN CB C 37.89 0.30 1 561 . 53 ASN N N 118.19 0.20 1 562 . 53 ASN ND2 N 111.40 0.20 1 563 . 54 GLU H H 7.59 0.02 1 564 . 54 GLU HA H 4.02 0.02 1 565 . 54 GLU HB2 H 2.06 0.02 2 566 . 54 GLU HB3 H 2.21 0.02 2 567 . 54 GLU HG2 H 2.32 0.02 2 568 . 54 GLU HG3 H 2.50 0.02 2 569 . 54 GLU C C 177.19 0.30 1 570 . 54 GLU CA C 58.89 0.30 1 571 . 54 GLU CB C 30.48 0.30 1 572 . 54 GLU CG C 36.23 0.30 1 573 . 54 GLU N N 116.17 0.20 1 574 . 55 VAL H H 7.14 0.02 1 575 . 55 VAL HA H 4.24 0.02 1 576 . 55 VAL HB H 2.11 0.02 1 577 . 55 VAL HG1 H 0.81 0.02 1 578 . 55 VAL HG2 H 0.88 0.02 1 579 . 55 VAL C C 175.21 0.30 1 580 . 55 VAL CA C 60.60 0.30 1 581 . 55 VAL CB C 33.02 0.30 1 582 . 55 VAL CG1 C 22.85 0.30 1 583 . 55 VAL CG2 C 20.27 0.30 1 584 . 55 VAL N N 110.76 0.20 1 585 . 56 ASP H H 7.44 0.02 1 586 . 56 ASP HA H 4.48 0.02 1 587 . 56 ASP HB2 H 2.54 0.02 2 588 . 56 ASP HB3 H 2.78 0.02 2 589 . 56 ASP C C 176.09 0.30 1 590 . 56 ASP CA C 53.62 0.30 1 591 . 56 ASP CB C 40.11 0.30 1 592 . 56 ASP N N 121.16 0.20 1 593 . 57 ALA H H 7.98 0.02 1 594 . 57 ALA HA H 4.18 0.02 1 595 . 57 ALA HB H 1.53 0.02 1 596 . 57 ALA C C 178.80 0.30 1 597 . 57 ALA CA C 54.55 0.30 1 598 . 57 ALA CB C 19.84 0.30 1 599 . 57 ALA N N 131.09 0.20 1 600 . 58 ASP H H 8.20 0.02 1 601 . 58 ASP HA H 4.63 0.02 1 602 . 58 ASP HB2 H 2.67 0.02 2 603 . 58 ASP HB3 H 3.04 0.02 2 604 . 58 ASP C C 178.01 0.30 1 605 . 58 ASP CA C 52.79 0.30 1 606 . 58 ASP CB C 39.93 0.30 1 607 . 58 ASP N N 113.52 0.20 1 608 . 59 GLY H H 7.55 0.02 1 609 . 59 GLY HA2 H 3.76 0.02 2 610 . 59 GLY HA3 H 3.92 0.02 2 611 . 59 GLY C C 174.97 0.30 1 612 . 59 GLY CA C 47.15 0.30 1 613 . 59 GLY N N 108.17 0.20 1 614 . 60 ASN H H 8.13 0.02 1 615 . 60 ASN HA H 4.58 0.02 1 616 . 60 ASN HB2 H 2.62 0.02 2 617 . 60 ASN HB3 H 3.29 0.02 2 618 . 60 ASN HD21 H 6.89 0.02 9 619 . 60 ASN HD22 H 7.76 0.02 9 620 . 60 ASN C C 176.85 0.30 1 621 . 60 ASN CA C 52.81 0.30 1 622 . 60 ASN CB C 37.55 0.30 1 623 . 60 ASN N N 118.63 0.20 1 624 . 60 ASN ND2 N 114.84 0.20 1 625 . 61 GLY H H 10.61 0.02 1 626 . 61 GLY HA2 H 3.48 0.02 2 627 . 61 GLY HA3 H 4.28 0.02 2 628 . 61 GLY C C 173.25 0.30 1 629 . 61 GLY CA C 45.54 0.30 1 630 . 61 GLY N N 113.51 0.20 1 631 . 62 THR H H 7.63 0.02 1 632 . 62 THR HA H 4.82 0.02 1 633 . 62 THR HB H 4.00 0.02 1 634 . 62 THR HG2 H 1.12 0.02 1 635 . 62 THR C C 173.18 0.30 1 636 . 62 THR CA C 59.26 0.30 1 637 . 62 THR CB C 72.25 0.30 1 638 . 62 THR CG2 C 22.34 0.30 1 639 . 62 THR N N 107.96 0.20 1 640 . 63 ILE H H 8.81 0.02 1 641 . 63 ILE HA H 5.37 0.02 1 642 . 63 ILE HB H 2.32 0.02 1 643 . 63 ILE HG12 H 1.57 0.02 2 644 . 63 ILE HG13 H 1.63 0.02 2 645 . 63 ILE HG2 H 1.25 0.02 1 646 . 63 ILE HD1 H 0.88 0.02 1 647 . 63 ILE C C 175.77 0.30 1 648 . 63 ILE CA C 57.90 0.30 1 649 . 63 ILE CB C 38.31 0.30 1 650 . 63 ILE CG2 C 18.00 0.30 1 651 . 63 ILE CD1 C 11.15 0.30 1 652 . 63 ILE N N 124.31 0.20 1 653 . 64 ASP H H 8.78 0.02 1 654 . 64 ASP HA H 5.53 0.02 1 655 . 64 ASP HB2 H 2.79 0.02 2 656 . 64 ASP HB3 H 3.16 0.02 2 657 . 64 ASP C C 176.02 0.30 1 658 . 64 ASP CA C 51.92 0.30 1 659 . 64 ASP CB C 42.44 0.30 1 660 . 64 ASP N N 127.90 0.20 1 661 . 65 PHE H H 8.96 0.02 1 662 . 65 PHE HA H 4.05 0.02 1 663 . 65 PHE HB2 H 1.97 0.02 2 664 . 65 PHE HB3 H 2.79 0.02 2 665 . 65 PHE HD1 H 6.73 0.02 3 666 . 65 PHE HE1 H 7.14 0.02 3 667 . 65 PHE HZ H 7.36 0.02 1 668 . 65 PHE C C 174.88 0.30 1 669 . 65 PHE CA C 62.50 0.30 1 670 . 65 PHE CB C 35.84 0.30 1 671 . 65 PHE CD1 C 131.89 0.30 3 672 . 65 PHE CE1 C 130.56 0.30 3 673 . 65 PHE N N 118.49 0.20 1 674 . 66 PRO HA H 3.85 0.02 1 675 . 66 PRO HD2 H 3.05 0.02 1 676 . 66 PRO HD3 H 3.05 0.02 1 677 . 66 PRO C C 180.15 0.30 1 678 . 66 PRO CA C 66.90 0.30 1 679 . 66 PRO CB C 28.54 0.30 1 680 . 67 GLU H H 8.37 0.02 1 681 . 67 GLU HA H 3.97 0.02 1 682 . 67 GLU HB2 H 2.11 0.02 2 683 . 67 GLU HB3 H 2.70 0.02 2 684 . 67 GLU HG2 H 2.30 0.02 2 685 . 67 GLU HG3 H 3.05 0.02 2 686 . 67 GLU C C 179.42 0.30 1 687 . 67 GLU CA C 59.28 0.30 1 688 . 67 GLU CB C 30.09 0.30 1 689 . 67 GLU CG C 37.68 0.30 1 690 . 67 GLU N N 118.14 0.20 1 691 . 68 PHE H H 8.54 0.02 1 692 . 68 PHE HA H 3.60 0.02 1 693 . 68 PHE HB2 H 3.06 0.02 2 694 . 68 PHE HB3 H 3.51 0.02 2 695 . 68 PHE HD1 H 6.72 0.02 3 696 . 68 PHE HE1 H 7.11 0.02 3 697 . 68 PHE C C 176.56 0.30 1 698 . 68 PHE CA C 61.15 0.30 1 699 . 68 PHE CB C 40.84 0.30 1 700 . 68 PHE N N 123.98 0.20 1 701 . 69 LEU H H 8.84 0.02 1 702 . 69 LEU HA H 3.41 0.02 1 703 . 69 LEU HB2 H 1.18 0.02 2 704 . 69 LEU HB3 H 1.25 0.02 2 705 . 69 LEU HG H 0.95 0.02 1 706 . 69 LEU HD1 H 0.59 0.02 1 707 . 69 LEU HD2 H 0.74 0.02 1 708 . 69 LEU C C 178.99 0.30 1 709 . 69 LEU CA C 57.54 0.30 1 710 . 69 LEU CB C 41.27 0.30 1 711 . 69 LEU CG C 26.70 0.30 1 712 . 69 LEU CD1 C 25.31 0.30 1 713 . 69 LEU CD2 C 24.36 0.30 1 714 . 69 LEU N N 118.96 0.20 1 715 . 70 THR H H 7.91 0.02 1 716 . 70 THR HA H 3.66 0.02 1 717 . 70 THR HB H 4.09 0.02 1 718 . 70 THR HG2 H 1.14 0.02 1 719 . 70 THR C C 176.19 0.30 1 720 . 70 THR CA C 66.68 0.30 1 721 . 70 THR CB C 68.14 0.30 1 722 . 70 THR CG2 C 21.65 0.30 1 723 . 70 THR N N 115.93 0.20 1 724 . 71 MET H H 7.35 0.02 1 725 . 71 MET HA H 3.84 0.02 1 726 . 71 MET HB2 H 1.96 0.02 1 727 . 71 MET HB3 H 1.96 0.02 1 728 . 71 MET HG2 H 2.13 0.02 1 729 . 71 MET HG3 H 2.13 0.02 1 730 . 71 MET HE H 0.58 0.02 1 731 . 71 MET C C 178.04 0.30 1 732 . 71 MET CA C 58.45 0.30 1 733 . 71 MET CB C 31.30 0.30 1 734 . 71 MET CG C 32.95 0.30 1 735 . 71 MET CE C 15.76 0.30 1 736 . 71 MET N N 120.35 0.20 1 737 . 72 MET H H 7.48 0.02 1 738 . 72 MET HA H 4.05 0.02 1 739 . 72 MET HB2 H 1.09 0.02 1 740 . 72 MET HB3 H 1.09 0.02 1 741 . 72 MET HG2 H 2.46 0.02 1 742 . 72 MET HG3 H 2.46 0.02 1 743 . 72 MET HE H 1.33 0.02 1 744 . 72 MET C C 178.25 0.30 1 745 . 72 MET CA C 55.09 0.30 1 746 . 72 MET CB C 28.62 0.30 1 747 . 72 MET CG C 29.79 0.30 1 748 . 72 MET CE C 14.54 0.30 1 749 . 72 MET N N 116.57 0.20 1 750 . 73 ALA H H 8.50 0.02 1 751 . 73 ALA HA H 3.89 0.02 1 752 . 73 ALA HB H 1.32 0.02 1 753 . 73 ALA C C 180.20 0.30 1 754 . 73 ALA CA C 55.08 0.30 1 755 . 73 ALA CB C 17.84 0.30 1 756 . 73 ALA N N 122.09 0.20 1 757 . 74 ARG H H 7.41 0.02 1 758 . 74 ARG HA H 4.00 0.02 1 759 . 74 ARG HB2 H 1.83 0.02 1 760 . 74 ARG HB3 H 1.83 0.02 1 761 . 74 ARG HG2 H 1.58 0.02 2 762 . 74 ARG HG3 H 1.72 0.02 2 763 . 74 ARG HD2 H 3.15 0.02 1 764 . 74 ARG HD3 H 3.15 0.02 1 765 . 74 ARG C C 178.67 0.30 1 766 . 74 ARG CA C 58.59 0.30 1 767 . 74 ARG CB C 30.17 0.30 1 768 . 74 ARG CG C 27.47 0.30 1 769 . 74 ARG CD C 43.42 0.30 1 770 . 74 ARG N N 115.53 0.20 1 771 . 75 LYS H H 7.58 0.02 1 772 . 75 LYS HA H 4.19 0.02 1 773 . 75 LYS HB2 H 1.71 0.02 2 774 . 75 LYS HB3 H 1.84 0.02 2 775 . 75 LYS HG2 H 1.39 0.02 2 776 . 75 LYS HG3 H 1.60 0.02 2 777 . 75 LYS HE2 H 3.00 0.02 1 778 . 75 LYS HE3 H 3.00 0.02 1 779 . 75 LYS C C 178.55 0.30 1 780 . 75 LYS CA C 56.91 0.30 1 781 . 75 LYS CB C 31.70 0.30 1 782 . 75 LYS CG C 24.39 0.30 1 783 . 75 LYS CD C 28.15 0.30 1 784 . 75 LYS N N 118.95 0.20 1 785 . 76 MET H H 7.95 0.02 1 786 . 76 MET HA H 4.05 0.02 1 787 . 76 MET HB2 H 1.93 0.02 1 788 . 76 MET HB3 H 1.93 0.02 1 789 . 76 MET HG2 H 2.24 0.02 2 790 . 76 MET HG3 H 2.40 0.02 2 791 . 76 MET HE H 1.82 0.02 1 792 . 76 MET C C 177.10 0.30 1 793 . 76 MET CA C 57.74 0.30 1 794 . 76 MET CB C 32.78 0.30 1 795 . 76 MET CG C 31.76 0.30 1 796 . 76 MET CE C 16.68 0.30 1 797 . 76 MET N N 116.69 0.20 1 798 . 77 LYS H H 7.38 0.02 1 799 . 77 LYS HA H 4.29 0.02 1 800 . 77 LYS HB2 H 1.83 0.02 2 801 . 77 LYS HB3 H 1.95 0.02 2 802 . 77 LYS HG2 H 1.48 0.02 1 803 . 77 LYS HG3 H 1.48 0.02 1 804 . 77 LYS HD2 H 1.67 0.02 1 805 . 77 LYS HD3 H 1.67 0.02 1 806 . 77 LYS HE2 H 2.99 0.02 1 807 . 77 LYS HE3 H 2.99 0.02 1 808 . 77 LYS C C 176.52 0.30 1 809 . 77 LYS CA C 56.75 0.30 1 810 . 77 LYS CB C 32.58 0.30 1 811 . 77 LYS CG C 24.59 0.30 1 812 . 77 LYS CD C 28.91 0.30 1 813 . 77 LYS CE C 42.23 0.30 1 814 . 77 LYS N N 116.80 0.20 1 815 . 78 ASP H H 7.66 0.02 1 816 . 78 ASP HA H 4.80 0.02 1 817 . 78 ASP HB2 H 2.67 0.02 2 818 . 78 ASP HB3 H 2.84 0.02 2 819 . 78 ASP C C 176.37 0.30 1 820 . 78 ASP CA C 54.14 0.30 1 821 . 78 ASP CB C 41.70 0.30 1 822 . 78 ASP N N 119.81 0.20 1 823 . 79 THR H H 8.06 0.02 1 824 . 79 THR HA H 4.22 0.02 1 825 . 79 THR HB H 4.27 0.02 1 826 . 79 THR HG2 H 1.26 0.02 1 827 . 79 THR C C 173.91 0.30 1 828 . 79 THR CA C 62.60 0.30 1 829 . 79 THR CB C 69.54 0.30 1 830 . 79 THR CG2 C 22.06 0.30 1 831 . 79 THR N N 113.81 0.20 1 832 . 80 ASP H H 8.25 0.02 1 833 . 80 ASP HA H 4.68 0.02 1 834 . 80 ASP HB2 H 2.60 0.02 1 835 . 80 ASP HB3 H 2.60 0.02 1 836 . 80 ASP C C 175.96 0.30 1 837 . 80 ASP CA C 53.86 0.30 1 838 . 80 ASP CB C 40.85 0.30 1 839 . 80 ASP N N 121.50 0.20 1 840 . 81 SER H H 8.32 0.02 1 841 . 81 SER HA H 4.56 0.02 1 842 . 81 SER HB2 H 4.02 0.02 2 843 . 81 SER HB3 H 4.19 0.02 2 844 . 81 SER C C 175.01 0.30 1 845 . 81 SER CA C 57.69 0.30 1 846 . 81 SER CB C 64.89 0.30 1 847 . 81 SER N N 117.17 0.20 1 848 . 82 GLU H H 8.83 0.02 1 849 . 82 GLU HA H 3.96 0.02 1 850 . 82 GLU HB2 H 2.05 0.02 1 851 . 82 GLU HB3 H 2.05 0.02 1 852 . 82 GLU HG2 H 2.35 0.02 1 853 . 82 GLU HG3 H 2.35 0.02 1 854 . 82 GLU C C 178.29 0.30 1 855 . 82 GLU CA C 60.03 0.30 1 856 . 82 GLU CB C 29.33 0.30 1 857 . 82 GLU CG C 36.46 0.30 1 858 . 82 GLU N N 123.41 0.20 1 859 . 83 GLU H H 8.50 0.02 1 860 . 83 GLU HA H 3.99 0.02 1 861 . 83 GLU HB2 H 2.01 0.02 1 862 . 83 GLU HB3 H 2.01 0.02 1 863 . 83 GLU HG2 H 2.33 0.02 1 864 . 83 GLU HG3 H 2.33 0.02 1 865 . 83 GLU C C 178.92 0.30 1 866 . 83 GLU CA C 59.79 0.30 1 867 . 83 GLU CB C 29.31 0.30 1 868 . 83 GLU CG C 36.53 0.30 1 869 . 83 GLU N N 117.24 0.20 1 870 . 84 GLU H H 7.69 0.02 1 871 . 84 GLU HA H 4.04 0.02 1 872 . 84 GLU HB2 H 2.05 0.02 1 873 . 84 GLU HB3 H 2.05 0.02 1 874 . 84 GLU HG2 H 2.29 0.02 1 875 . 84 GLU HG3 H 2.29 0.02 1 876 . 84 GLU C C 179.01 0.30 1 877 . 84 GLU CA C 59.33 0.30 1 878 . 84 GLU CB C 29.33 0.30 1 879 . 84 GLU CG C 36.90 0.30 1 880 . 84 GLU N N 119.14 0.20 1 881 . 85 ILE H H 8.07 0.02 1 882 . 85 ILE HA H 3.80 0.02 1 883 . 85 ILE HB H 2.15 0.02 1 884 . 85 ILE HG12 H 1.04 0.02 2 885 . 85 ILE HG13 H 1.95 0.02 2 886 . 85 ILE HG2 H 1.17 0.02 1 887 . 85 ILE HD1 H 0.77 0.02 1 888 . 85 ILE C C 178.30 0.30 1 889 . 85 ILE CA C 66.19 0.30 1 890 . 85 ILE CB C 37.91 0.30 1 891 . 85 ILE CG1 C 29.16 0.30 1 892 . 85 ILE CG2 C 18.70 0.30 1 893 . 85 ILE CD1 C 13.72 0.30 1 894 . 85 ILE N N 121.66 0.20 1 895 . 86 ARG H H 8.39 0.02 1 896 . 86 ARG HA H 4.13 0.02 1 897 . 86 ARG HB2 H 1.88 0.02 2 898 . 86 ARG HB3 H 2.06 0.02 2 899 . 86 ARG HG2 H 1.60 0.02 2 900 . 86 ARG HG3 H 1.72 0.02 2 901 . 86 ARG HD2 H 2.97 0.02 1 902 . 86 ARG HD3 H 2.97 0.02 1 903 . 86 ARG C C 178.97 0.30 1 904 . 86 ARG CA C 59.90 0.30 1 905 . 86 ARG CB C 29.84 0.30 1 906 . 86 ARG CG C 27.57 0.30 1 907 . 86 ARG CD C 43.16 0.30 1 908 . 86 ARG N N 119.69 0.20 1 909 . 87 GLU H H 8.05 0.02 1 910 . 87 GLU HA H 3.94 0.02 1 911 . 87 GLU HB2 H 2.19 0.02 1 912 . 87 GLU HB3 H 2.19 0.02 1 913 . 87 GLU HG2 H 2.32 0.02 2 914 . 87 GLU HG3 H 2.52 0.02 2 915 . 87 GLU C C 178.60 0.30 1 916 . 87 GLU CA C 59.59 0.30 1 917 . 87 GLU CB C 30.54 0.30 1 918 . 87 GLU CG C 37.04 0.30 1 919 . 87 GLU N N 117.80 0.20 1 920 . 88 ALA H H 8.12 0.02 1 921 . 88 ALA HA H 3.85 0.02 1 922 . 88 ALA HB H 1.84 0.02 1 923 . 88 ALA C C 178.59 0.30 1 924 . 88 ALA CA C 55.40 0.30 1 925 . 88 ALA CB C 17.64 0.30 1 926 . 88 ALA N N 120.94 0.20 1 927 . 89 PHE H H 8.37 0.02 1 928 . 89 PHE HA H 3.17 0.02 1 929 . 89 PHE HB2 H 2.81 0.02 2 930 . 89 PHE HB3 H 3.14 0.02 2 931 . 89 PHE HD1 H 6.46 0.02 3 932 . 89 PHE HE1 H 6.92 0.02 3 933 . 89 PHE C C 176.81 0.30 1 934 . 89 PHE CA C 62.56 0.30 1 935 . 89 PHE CB C 39.07 0.30 1 936 . 89 PHE CE1 C 129.03 0.30 3 937 . 89 PHE N N 118.14 0.20 1 938 . 90 ARG H H 7.87 0.02 1 939 . 90 ARG HA H 3.84 0.02 1 940 . 90 ARG HB2 H 1.95 0.02 1 941 . 90 ARG HB3 H 1.95 0.02 1 942 . 90 ARG HG2 H 1.72 0.02 1 943 . 90 ARG HG3 H 1.72 0.02 1 944 . 90 ARG HD2 H 3.21 0.02 1 945 . 90 ARG HD3 H 3.21 0.02 1 946 . 90 ARG C C 177.80 0.30 1 947 . 90 ARG CA C 58.58 0.30 1 948 . 90 ARG CB C 30.52 0.30 1 949 . 90 ARG CG C 28.04 0.30 1 950 . 90 ARG CD C 43.71 0.30 1 951 . 90 ARG N N 114.89 0.20 1 952 . 91 VAL H H 7.34 0.02 1 953 . 91 VAL HA H 3.46 0.02 1 954 . 91 VAL HB H 2.09 0.02 1 955 . 91 VAL HG1 H 0.67 0.02 1 956 . 91 VAL HG2 H 0.96 0.02 1 957 . 91 VAL C C 176.58 0.30 1 958 . 91 VAL CA C 65.80 0.30 1 959 . 91 VAL CB C 30.83 0.30 1 960 . 91 VAL CG1 C 22.18 0.30 1 961 . 91 VAL CG2 C 23.33 0.30 1 962 . 91 VAL N N 117.81 0.20 1 963 . 92 PHE H H 6.79 0.02 1 964 . 92 PHE HA H 4.21 0.02 1 965 . 92 PHE HB2 H 2.54 0.02 2 966 . 92 PHE HB3 H 2.82 0.02 2 967 . 92 PHE HD1 H 7.29 0.02 3 968 . 92 PHE HE1 H 7.42 0.02 3 969 . 92 PHE C C 176.77 0.30 1 970 . 92 PHE CA C 61.34 0.30 1 971 . 92 PHE CB C 41.72 0.30 1 972 . 92 PHE CD1 C 132.32 0.30 3 973 . 92 PHE CE1 C 131.30 0.30 3 974 . 92 PHE N N 113.25 0.20 1 975 . 93 ASP H H 7.93 0.02 1 976 . 93 ASP HA H 4.55 0.02 1 977 . 93 ASP HB2 H 1.25 0.02 2 978 . 93 ASP HB3 H 2.18 0.02 2 979 . 93 ASP C C 177.49 0.30 1 980 . 93 ASP CA C 52.13 0.30 1 981 . 93 ASP CB C 38.78 0.30 1 982 . 93 ASP N N 115.12 0.20 1 983 . 94 LYS H H 7.78 0.02 1 984 . 94 LYS HA H 3.91 0.02 1 985 . 94 LYS HB2 H 1.85 0.02 2 986 . 94 LYS HB3 H 1.88 0.02 2 987 . 94 LYS HG2 H 1.46 0.02 2 988 . 94 LYS HG3 H 1.53 0.02 2 989 . 94 LYS HE2 H 2.64 0.02 1 990 . 94 LYS HE3 H 2.64 0.02 1 991 . 94 LYS C C 178.25 0.30 1 992 . 94 LYS CA C 59.24 0.30 1 993 . 94 LYS CB C 32.89 0.30 1 994 . 94 LYS CG C 23.73 0.30 1 995 . 94 LYS CD C 28.65 0.30 1 996 . 94 LYS CE C 41.44 0.30 1 997 . 94 LYS N N 126.35 0.20 1 998 . 95 ASP H H 8.39 0.02 1 999 . 95 ASP HA H 4.51 0.02 1 1000 . 95 ASP HB2 H 2.63 0.02 2 1001 . 95 ASP HB3 H 3.07 0.02 2 1002 . 95 ASP C C 177.83 0.30 1 1003 . 95 ASP CA C 53.15 0.30 1 1004 . 95 ASP CB C 39.66 0.30 1 1005 . 95 ASP N N 114.02 0.20 1 1006 . 96 GLY H H 7.87 0.02 1 1007 . 96 GLY HA2 H 3.85 0.02 1 1008 . 96 GLY HA3 H 3.85 0.02 1 1009 . 96 GLY C C 175.17 0.30 1 1010 . 96 GLY CA C 46.99 0.30 1 1011 . 96 GLY N N 109.27 0.20 1 1012 . 97 ASN H H 8.39 0.02 1 1013 . 97 ASN HA H 4.61 0.02 1 1014 . 97 ASN HB2 H 2.66 0.02 2 1015 . 97 ASN HB3 H 3.40 0.02 2 1016 . 97 ASN HD21 H 8.03 0.02 9 1017 . 97 ASN HD22 H 7.49 0.02 9 1018 . 97 ASN C C 176.22 0.30 1 1019 . 97 ASN CA C 52.68 0.30 1 1020 . 97 ASN CB C 38.25 0.30 1 1021 . 97 ASN N N 119.69 0.20 1 1022 . 97 ASN ND2 N 117.06 0.20 1 1023 . 98 GLY H H 10.67 0.02 1 1024 . 98 GLY HA2 H 3.45 0.02 2 1025 . 98 GLY HA3 H 4.11 0.02 2 1026 . 98 GLY C C 173.11 0.30 1 1027 . 98 GLY CA C 45.06 0.30 1 1028 . 98 GLY N N 112.52 0.20 1 1029 . 99 TYR H H 7.70 0.02 1 1030 . 99 TYR HA H 4.86 0.02 1 1031 . 99 TYR HB2 H 2.47 0.02 2 1032 . 99 TYR HB3 H 2.58 0.02 2 1033 . 99 TYR HD1 H 6.77 0.02 3 1034 . 99 TYR HE1 H 6.89 0.02 3 1035 . 99 TYR C C 174.69 0.30 1 1036 . 99 TYR CA C 56.47 0.30 1 1037 . 99 TYR CB C 42.44 0.30 1 1038 . 99 TYR CD1 C 133.47 0.30 3 1039 . 99 TYR CE1 C 118.05 0.30 3 1040 . 99 TYR N N 116.74 0.20 1 1041 . 100 ILE H H 9.90 0.02 1 1042 . 100 ILE HA H 4.49 0.02 1 1043 . 100 ILE HB H 1.66 0.02 1 1044 . 100 ILE HG12 H 1.25 0.02 1 1045 . 100 ILE HG13 H 1.25 0.02 1 1046 . 100 ILE HG2 H 0.88 0.02 1 1047 . 100 ILE HD1 H 0.12 0.02 1 1048 . 100 ILE C C 175.28 0.30 1 1049 . 100 ILE CA C 61.73 0.30 1 1050 . 100 ILE CB C 39.15 0.30 1 1051 . 100 ILE CG1 C 26.53 0.30 1 1052 . 100 ILE CG2 C 16.96 0.30 1 1053 . 100 ILE CD1 C 15.52 0.30 1 1054 . 100 ILE N N 127.23 0.20 1 1055 . 101 SER H H 8.79 0.02 1 1056 . 101 SER HA H 5.00 0.02 1 1057 . 101 SER HB2 H 3.91 0.02 2 1058 . 101 SER HB3 H 4.44 0.02 2 1059 . 101 SER C C 175.42 0.30 1 1060 . 101 SER CA C 55.36 0.30 1 1061 . 101 SER CB C 67.27 0.30 1 1062 . 101 SER N N 122.95 0.20 1 1063 . 102 ALA H H 9.33 0.02 1 1064 . 102 ALA HA H 3.94 0.02 1 1065 . 102 ALA HB H 1.45 0.02 1 1066 . 102 ALA C C 179.46 0.30 1 1067 . 102 ALA CA C 55.56 0.30 1 1068 . 102 ALA CB C 18.20 0.30 1 1069 . 102 ALA N N 123.52 0.20 1 1070 . 103 ALA H H 8.22 0.02 1 1071 . 103 ALA HA H 4.07 0.02 1 1072 . 103 ALA HB H 1.41 0.02 1 1073 . 103 ALA C C 181.54 0.30 1 1074 . 103 ALA CA C 55.13 0.30 1 1075 . 103 ALA CB C 18.24 0.30 1 1076 . 103 ALA N N 118.10 0.20 1 1077 . 104 GLU H H 7.90 0.02 1 1078 . 104 GLU HA H 4.03 0.02 1 1079 . 104 GLU HB2 H 2.63 0.02 2 1080 . 104 GLU HB3 H 2.82 0.02 2 1081 . 104 GLU HG2 H 2.33 0.02 2 1082 . 104 GLU HG3 H 2.60 0.02 2 1083 . 104 GLU C C 179.28 0.30 1 1084 . 104 GLU CA C 59.82 0.30 1 1085 . 104 GLU CB C 28.50 0.30 1 1086 . 104 GLU CG C 38.71 0.30 1 1087 . 104 GLU N N 120.25 0.20 1 1088 . 105 LEU H H 8.26 0.02 1 1089 . 105 LEU HA H 4.23 0.02 1 1090 . 105 LEU HB2 H 1.83 0.02 1 1091 . 105 LEU HB3 H 1.83 0.02 1 1092 . 105 LEU HG H 1.74 0.02 1 1093 . 105 LEU HD1 H 1.02 0.02 1 1094 . 105 LEU HD2 H 0.98 0.02 1 1095 . 105 LEU C C 178.72 0.30 1 1096 . 105 LEU CA C 59.23 0.30 1 1097 . 105 LEU CB C 42.73 0.30 1 1098 . 105 LEU CG C 28.14 0.30 1 1099 . 105 LEU CD1 C 26.10 0.30 1 1100 . 105 LEU CD2 C 25.55 0.30 1 1101 . 105 LEU N N 121.76 0.20 1 1102 . 106 ARG H H 8.40 0.02 1 1103 . 106 ARG HA H 4.20 0.02 1 1104 . 106 ARG HB2 H 1.95 0.02 1 1105 . 106 ARG HB3 H 1.95 0.02 1 1106 . 106 ARG HG2 H 1.56 0.02 1 1107 . 106 ARG HG3 H 1.56 0.02 1 1108 . 106 ARG HD2 H 3.17 0.02 2 1109 . 106 ARG HD3 H 3.34 0.02 2 1110 . 106 ARG C C 178.76 0.30 1 1111 . 106 ARG CA C 59.09 0.30 1 1112 . 106 ARG CB C 30.59 0.30 1 1113 . 106 ARG CG C 29.57 0.30 1 1114 . 106 ARG CD C 43.50 0.30 1 1115 . 106 ARG N N 116.56 0.20 1 1116 . 107 HIS H H 8.05 0.02 1 1117 . 107 HIS HA H 4.34 0.02 1 1118 . 107 HIS HB2 H 3.26 0.02 2 1119 . 107 HIS HB3 H 3.42 0.02 2 1120 . 107 HIS C C 178.03 0.30 1 1121 . 107 HIS CA C 60.01 0.30 1 1122 . 107 HIS CB C 30.84 0.30 1 1123 . 107 HIS N N 119.99 0.20 1 1124 . 108 VAL H H 8.39 0.02 1 1125 . 108 VAL HA H 3.68 0.02 1 1126 . 108 VAL HB H 2.23 0.02 1 1127 . 108 VAL HG1 H 0.83 0.02 1 1128 . 108 VAL HG2 H 1.18 0.02 1 1129 . 108 VAL C C 177.96 0.30 1 1130 . 108 VAL CA C 66.18 0.30 1 1131 . 108 VAL CB C 31.84 0.30 1 1132 . 108 VAL CG1 C 21.99 0.30 1 1133 . 108 VAL CG2 C 23.83 0.30 1 1134 . 108 VAL N N 118.81 0.20 1 1135 . 109 MET H H 8.56 0.02 1 1136 . 109 MET HA H 3.92 0.02 1 1137 . 109 MET HB2 H 2.10 0.02 1 1138 . 109 MET HB3 H 2.10 0.02 1 1139 . 109 MET HG2 H 2.51 0.02 2 1140 . 109 MET HG3 H 3.14 0.02 2 1141 . 109 MET HE H 2.25 0.02 1 1142 . 109 MET C C 176.71 0.30 1 1143 . 109 MET CA C 59.37 0.30 1 1144 . 109 MET CB C 30.74 0.30 1 1145 . 109 MET CG C 32.22 0.30 1 1146 . 109 MET CE C 17.95 0.30 1 1147 . 109 MET N N 118.40 0.20 1 1148 . 110 THR H H 7.53 0.02 1 1149 . 110 THR HA H 4.09 0.02 1 1150 . 110 THR HB H 4.21 0.02 1 1151 . 110 THR HG2 H 1.26 0.02 1 1152 . 110 THR C C 177.68 0.30 1 1153 . 110 THR CA C 65.65 0.30 1 1154 . 110 THR CB C 68.74 0.30 1 1155 . 110 THR CG2 C 21.62 0.30 1 1156 . 110 THR N N 115.03 0.20 1 1157 . 111 ASN H H 7.46 0.02 1 1158 . 111 ASN HA H 4.50 0.02 1 1159 . 111 ASN HB2 H 2.53 0.02 2 1160 . 111 ASN HB3 H 2.61 0.02 2 1161 . 111 ASN C C 175.40 0.30 1 1162 . 111 ASN CA C 55.89 0.30 1 1163 . 111 ASN CB C 39.11 0.30 1 1164 . 111 ASN N N 120.06 0.20 1 1165 . 112 LEU H H 7.57 0.02 1 1166 . 112 LEU HA H 4.51 0.02 1 1167 . 112 LEU HB2 H 1.45 0.02 2 1168 . 112 LEU HB3 H 1.53 0.02 2 1169 . 112 LEU HG H 1.63 0.02 1 1170 . 112 LEU HD1 H 0.69 0.02 1 1171 . 112 LEU HD2 H 0.69 0.02 1 1172 . 112 LEU C C 176.23 0.30 1 1173 . 112 LEU CA C 53.38 0.30 1 1174 . 112 LEU CB C 41.33 0.30 1 1175 . 112 LEU CG C 26.53 0.30 1 1176 . 112 LEU CD1 C 26.87 0.30 1 1177 . 112 LEU CD2 C 23.22 0.30 1 1178 . 112 LEU N N 115.33 0.20 1 1179 . 113 GLY H H 7.58 0.02 1 1180 . 113 GLY HA2 H 3.76 0.02 2 1181 . 113 GLY HA3 H 3.90 0.02 2 1182 . 113 GLY C C 173.95 0.30 1 1183 . 113 GLY CA C 47.27 0.30 1 1184 . 113 GLY N N 107.75 0.20 1 1185 . 114 GLU H H 7.96 0.02 1 1186 . 114 GLU HA H 4.49 0.02 1 1187 . 114 GLU HB2 H 1.33 0.02 2 1188 . 114 GLU HB3 H 1.91 0.02 2 1189 . 114 GLU HG2 H 2.23 0.02 1 1190 . 114 GLU HG3 H 2.23 0.02 1 1191 . 114 GLU C C 174.50 0.30 1 1192 . 114 GLU CA C 54.03 0.30 1 1193 . 114 GLU CB C 32.43 0.30 1 1194 . 114 GLU CG C 35.47 0.30 1 1195 . 114 GLU N N 117.39 0.20 1 1196 . 115 LYS H H 8.89 0.02 1 1197 . 115 LYS HA H 4.27 0.02 1 1198 . 115 LYS HB2 H 1.58 0.02 2 1199 . 115 LYS HB3 H 1.75 0.02 2 1200 . 115 LYS HG2 H 1.24 0.02 2 1201 . 115 LYS HG3 H 1.19 0.02 2 1202 . 115 LYS HD2 H 1.54 0.02 1 1203 . 115 LYS HD3 H 1.54 0.02 1 1204 . 115 LYS HE2 H 2.93 0.02 1 1205 . 115 LYS HE3 H 2.93 0.02 1 1206 . 115 LYS C C 173.82 0.30 1 1207 . 115 LYS CA C 56.16 0.30 1 1208 . 115 LYS CB C 32.84 0.30 1 1209 . 115 LYS CG C 24.75 0.30 1 1210 . 115 LYS CD C 29.27 0.30 1 1211 . 115 LYS CE C 42.06 0.30 1 1212 . 115 LYS N N 121.76 0.20 1 1213 . 116 LEU H H 7.82 0.02 1 1214 . 116 LEU HA H 4.69 0.02 1 1215 . 116 LEU HB2 H 1.56 0.02 2 1216 . 116 LEU HB3 H 1.84 0.02 2 1217 . 116 LEU HG H 1.61 0.02 1 1218 . 116 LEU HD1 H 0.86 0.02 1 1219 . 116 LEU HD2 H 0.75 0.02 1 1220 . 116 LEU C C 178.25 0.30 1 1221 . 116 LEU CA C 55.92 0.30 1 1222 . 116 LEU CB C 42.96 0.30 1 1223 . 116 LEU CD1 C 24.60 0.30 1 1224 . 116 LEU CD2 C 26.66 0.30 1 1225 . 116 LEU N N 128.87 0.20 1 1226 . 117 THR H H 9.42 0.02 1 1227 . 117 THR HA H 4.34 0.02 1 1228 . 117 THR HB H 4.73 0.02 1 1229 . 117 THR HG2 H 1.32 0.02 1 1230 . 117 THR C C 175.40 0.30 1 1231 . 117 THR CA C 60.95 0.30 1 1232 . 117 THR CB C 71.37 0.30 1 1233 . 117 THR CG2 C 21.85 0.30 1 1234 . 117 THR N N 114.14 0.20 1 1235 . 118 ASP H H 8.92 0.02 1 1236 . 118 ASP HA H 4.23 0.02 1 1237 . 118 ASP HB2 H 2.54 0.02 2 1238 . 118 ASP HB3 H 2.74 0.02 2 1239 . 118 ASP C C 178.46 0.30 1 1240 . 118 ASP CA C 58.10 0.30 1 1241 . 118 ASP CB C 39.60 0.30 1 1242 . 118 ASP N N 120.90 0.20 1 1243 . 119 GLU H H 8.50 0.02 1 1244 . 119 GLU HA H 4.06 0.02 1 1245 . 119 GLU HB2 H 1.94 0.02 1 1246 . 119 GLU HB3 H 1.94 0.02 1 1247 . 119 GLU HG2 H 2.33 0.02 1 1248 . 119 GLU HG3 H 2.33 0.02 1 1249 . 119 GLU C C 179.06 0.30 1 1250 . 119 GLU CA C 59.95 0.30 1 1251 . 119 GLU CB C 29.19 0.30 1 1252 . 119 GLU CG C 36.90 0.30 1 1253 . 119 GLU N N 118.68 0.20 1 1254 . 120 GLU H H 7.70 0.02 1 1255 . 120 GLU HA H 3.94 0.02 1 1256 . 120 GLU HB2 H 1.68 0.02 1 1257 . 120 GLU HB3 H 1.68 0.02 1 1258 . 120 GLU HG2 H 2.21 0.02 2 1259 . 120 GLU HG3 H 2.49 0.02 2 1260 . 120 GLU C C 179.21 0.30 1 1261 . 120 GLU CA C 58.82 0.30 1 1262 . 120 GLU CB C 28.82 0.30 1 1263 . 120 GLU CG C 38.13 0.30 1 1264 . 120 GLU N N 120.37 0.20 1 1265 . 121 VAL H H 8.24 0.02 1 1266 . 121 VAL HA H 3.31 0.02 1 1267 . 121 VAL HB H 2.24 0.02 1 1268 . 121 VAL HG1 H 1.02 0.02 1 1269 . 121 VAL HG2 H 0.95 0.02 1 1270 . 121 VAL C C 177.00 0.30 1 1271 . 121 VAL CA C 67.12 0.30 1 1272 . 121 VAL CB C 31.99 0.30 1 1273 . 121 VAL CG1 C 21.80 0.30 1 1274 . 121 VAL CG2 C 23.93 0.30 1 1275 . 121 VAL N N 120.89 0.20 1 1276 . 122 ASP H H 7.74 0.02 1 1277 . 122 ASP HA H 4.31 0.02 1 1278 . 122 ASP HB2 H 2.64 0.02 2 1279 . 122 ASP HB3 H 2.73 0.02 2 1280 . 122 ASP C C 179.38 0.30 1 1281 . 122 ASP CA C 57.51 0.30 1 1282 . 122 ASP CB C 40.53 0.30 1 1283 . 122 ASP N N 117.08 0.20 1 1284 . 123 GLU H H 8.23 0.02 1 1285 . 123 GLU HA H 4.04 0.02 1 1286 . 123 GLU HB2 H 2.04 0.02 2 1287 . 123 GLU HB3 H 2.10 0.02 2 1288 . 123 GLU HG2 H 2.37 0.02 1 1289 . 123 GLU HG3 H 2.37 0.02 1 1290 . 123 GLU C C 177.59 0.30 1 1291 . 123 GLU CA C 58.91 0.30 1 1292 . 123 GLU CB C 29.27 0.30 1 1293 . 123 GLU CG C 35.65 0.30 1 1294 . 123 GLU N N 120.07 0.20 1 1295 . 124 MET H H 8.10 0.02 1 1296 . 124 MET HA H 3.98 0.02 1 1297 . 124 MET HB2 H 1.57 0.02 2 1298 . 124 MET HB3 H 1.90 0.02 2 1299 . 124 MET HG2 H 1.72 0.02 1 1300 . 124 MET HG3 H 1.72 0.02 1 1301 . 124 MET HE H 0.65 0.02 1 1302 . 124 MET C C 179.11 0.30 1 1303 . 124 MET CA C 59.62 0.30 1 1304 . 124 MET CB C 32.15 0.30 1 1305 . 124 MET CG C 33.03 0.30 1 1306 . 124 MET CE C 15.56 0.30 1 1307 . 124 MET N N 121.49 0.20 1 1308 . 125 ILE H H 7.57 0.02 1 1309 . 125 ILE HA H 3.70 0.02 1 1310 . 125 ILE HB H 2.02 0.02 1 1311 . 125 ILE HG12 H 1.09 0.02 2 1312 . 125 ILE HG13 H 1.79 0.02 2 1313 . 125 ILE HG2 H 0.72 0.02 1 1314 . 125 ILE HD1 H 0.86 0.02 1 1315 . 125 ILE C C 177.22 0.30 1 1316 . 125 ILE CA C 64.94 0.30 1 1317 . 125 ILE CB C 37.85 0.30 1 1318 . 125 ILE CG1 C 29.40 0.30 1 1319 . 125 ILE CG2 C 15.97 0.30 1 1320 . 125 ILE CD1 C 11.95 0.30 1 1321 . 125 ILE N N 116.46 0.20 1 1322 . 126 ARG H H 8.65 0.02 1 1323 . 126 ARG HA H 3.98 0.02 1 1324 . 126 ARG HB2 H 1.79 0.02 2 1325 . 126 ARG HB3 H 1.97 0.02 2 1326 . 126 ARG HG2 H 1.64 0.02 1 1327 . 126 ARG HG3 H 1.64 0.02 1 1328 . 126 ARG HD2 H 3.21 0.02 1 1329 . 126 ARG HD3 H 3.21 0.02 1 1330 . 126 ARG C C 178.92 0.30 1 1331 . 126 ARG CA C 59.86 0.30 1 1332 . 126 ARG CB C 30.45 0.30 1 1333 . 126 ARG CG C 27.44 0.30 1 1334 . 126 ARG CD C 43.32 0.30 1 1335 . 126 ARG N N 119.20 0.20 1 1336 . 127 GLU H H 8.03 0.02 1 1337 . 127 GLU HA H 3.85 0.02 1 1338 . 127 GLU HB2 H 2.09 0.02 1 1339 . 127 GLU HB3 H 2.09 0.02 1 1340 . 127 GLU HG2 H 2.34 0.02 1 1341 . 127 GLU HG3 H 2.34 0.02 1 1342 . 127 GLU C C 176.43 0.30 1 1343 . 127 GLU CA C 58.84 0.30 1 1344 . 127 GLU CB C 30.14 0.30 1 1345 . 127 GLU CG C 36.18 0.30 1 1346 . 127 GLU N N 116.20 0.20 1 1347 . 128 ALA H H 6.91 0.02 1 1348 . 128 ALA HA H 4.69 0.02 1 1349 . 128 ALA HB H 1.43 0.02 1 1350 . 128 ALA C C 177.43 0.30 1 1351 . 128 ALA CA C 51.75 0.30 1 1352 . 128 ALA CB C 22.42 0.30 1 1353 . 128 ALA N N 116.52 0.20 1 1354 . 129 ASP H H 7.74 0.02 1 1355 . 129 ASP HA H 4.47 0.02 1 1356 . 129 ASP HB2 H 2.46 0.02 2 1357 . 129 ASP HB3 H 2.82 0.02 2 1358 . 129 ASP C C 175.93 0.30 1 1359 . 129 ASP CA C 54.10 0.30 1 1360 . 129 ASP CB C 40.80 0.30 1 1361 . 129 ASP N N 118.26 0.20 1 1362 . 130 ILE H H 8.18 0.02 1 1363 . 130 ILE HA H 3.83 0.02 1 1364 . 130 ILE HB H 1.92 0.02 1 1365 . 130 ILE HG12 H 1.27 0.02 2 1366 . 130 ILE HG13 H 1.69 0.02 2 1367 . 130 ILE HG2 H 0.93 0.02 1 1368 . 130 ILE HD1 H 0.90 0.02 1 1369 . 130 ILE C C 178.06 0.30 1 1370 . 130 ILE CA C 63.61 0.30 1 1371 . 130 ILE CB C 38.64 0.30 1 1372 . 130 ILE CG1 C 27.86 0.30 1 1373 . 130 ILE CG2 C 17.23 0.30 1 1374 . 130 ILE CD1 C 12.52 0.30 1 1375 . 130 ILE N N 127.64 0.20 1 1376 . 131 ASP H H 8.27 0.02 1 1377 . 131 ASP HA H 4.50 0.02 1 1378 . 131 ASP HB2 H 2.63 0.02 2 1379 . 131 ASP HB3 H 3.04 0.02 2 1380 . 131 ASP C C 178.22 0.30 1 1381 . 131 ASP CA C 53.83 0.30 1 1382 . 131 ASP CB C 39.93 0.30 1 1383 . 131 ASP N N 116.08 0.20 1 1384 . 132 GLY H H 7.61 0.02 1 1385 . 132 GLY HA2 H 3.79 0.02 2 1386 . 132 GLY HA3 H 3.92 0.02 2 1387 . 132 GLY C C 175.33 0.30 1 1388 . 132 GLY CA C 47.40 0.30 1 1389 . 132 GLY N N 108.75 0.20 1 1390 . 133 ASP H H 8.38 0.02 1 1391 . 133 ASP HA H 4.45 0.02 1 1392 . 133 ASP HB2 H 2.47 0.02 2 1393 . 133 ASP HB3 H 2.95 0.02 2 1394 . 133 ASP C C 177.58 0.30 1 1395 . 133 ASP CA C 53.68 0.30 1 1396 . 133 ASP CB C 40.12 0.30 1 1397 . 133 ASP N N 120.66 0.20 1 1398 . 134 GLY H H 10.32 0.02 1 1399 . 134 GLY HA2 H 3.44 0.02 2 1400 . 134 GLY HA3 H 4.03 0.02 2 1401 . 134 GLY C C 172.95 0.30 1 1402 . 134 GLY CA C 45.87 0.30 1 1403 . 134 GLY N N 112.86 0.20 1 1404 . 135 GLN H H 8.02 0.02 1 1405 . 135 GLN HA H 4.95 0.02 1 1406 . 135 GLN HB2 H 1.77 0.02 2 1407 . 135 GLN HB3 H 1.93 0.02 2 1408 . 135 GLN HG2 H 2.06 0.02 2 1409 . 135 GLN HG3 H 2.26 0.02 2 1410 . 135 GLN HE21 H 6.73 0.02 9 1411 . 135 GLN HE22 H 7.30 0.02 9 1412 . 135 GLN C C 175.15 0.30 1 1413 . 135 GLN CA C 53.24 0.30 1 1414 . 135 GLN CB C 33.22 0.30 1 1415 . 135 GLN CG C 34.11 0.30 1 1416 . 135 GLN N N 115.71 0.20 1 1417 . 135 GLN NE2 N 110.86 0.20 1 1418 . 136 VAL H H 8.83 0.02 1 1419 . 136 VAL HA H 5.05 0.02 1 1420 . 136 VAL HB H 1.80 0.02 1 1421 . 136 VAL HG1 H 0.77 0.02 1 1422 . 136 VAL HG2 H 0.85 0.02 1 1423 . 136 VAL C C 175.81 0.30 1 1424 . 136 VAL CA C 61.41 0.30 1 1425 . 136 VAL CB C 33.46 0.30 1 1426 . 136 VAL CG1 C 21.14 0.30 1 1427 . 136 VAL CG2 C 23.17 0.30 1 1428 . 136 VAL N N 125.21 0.20 1 1429 . 137 ASN H H 9.46 0.02 1 1430 . 137 ASN HA H 5.35 0.02 1 1431 . 137 ASN HB2 H 2.97 0.02 1 1432 . 137 ASN HB3 H 2.97 0.02 1 1433 . 137 ASN HD21 H 6.79 0.02 9 1434 . 137 ASN HD22 H 7.00 0.02 9 1435 . 137 ASN C C 174.82 0.30 1 1436 . 137 ASN CA C 50.78 0.30 1 1437 . 137 ASN CB C 38.43 0.30 1 1438 . 137 ASN N N 129.02 0.20 1 1439 . 137 ASN ND2 N 108.26 0.20 1 1440 . 138 TYR H H 7.92 0.02 1 1441 . 138 TYR HA H 3.24 0.02 1 1442 . 138 TYR HB2 H 2.01 0.02 2 1443 . 138 TYR HB3 H 2.36 0.02 2 1444 . 138 TYR HD1 H 6.17 0.02 3 1445 . 138 TYR HE1 H 6.46 0.02 3 1446 . 138 TYR C C 176.16 0.30 1 1447 . 138 TYR CA C 62.26 0.30 1 1448 . 138 TYR CB C 38.06 0.30 1 1449 . 138 TYR CD1 C 132.39 0.30 3 1450 . 138 TYR CE1 C 117.86 0.30 3 1451 . 138 TYR N N 118.06 0.20 1 1452 . 139 GLU H H 7.97 0.02 1 1453 . 139 GLU HA H 3.63 0.02 1 1454 . 139 GLU HB2 H 1.94 0.02 2 1455 . 139 GLU HB3 H 2.04 0.02 2 1456 . 139 GLU HG2 H 2.29 0.02 1 1457 . 139 GLU HG3 H 2.29 0.02 1 1458 . 139 GLU C C 180.14 0.30 1 1459 . 139 GLU CA C 60.14 0.30 1 1460 . 139 GLU CB C 28.88 0.30 1 1461 . 139 GLU CG C 37.05 0.30 1 1462 . 139 GLU N N 118.14 0.20 1 1463 . 140 GLU H H 8.65 0.02 1 1464 . 140 GLU HA H 3.85 0.02 1 1465 . 140 GLU HB2 H 2.22 0.02 2 1466 . 140 GLU HB3 H 2.45 0.02 2 1467 . 140 GLU HG2 H 2.82 0.02 1 1468 . 140 GLU HG3 H 2.82 0.02 1 1469 . 140 GLU C C 179.36 0.30 1 1470 . 140 GLU CA C 58.70 0.30 1 1471 . 140 GLU CB C 29.46 0.30 1 1472 . 140 GLU CG C 37.26 0.30 1 1473 . 140 GLU N N 119.77 0.20 1 1474 . 141 PHE H H 8.36 0.02 1 1475 . 141 PHE HA H 3.59 0.02 1 1476 . 141 PHE HB2 H 2.86 0.02 2 1477 . 141 PHE HB3 H 3.19 0.02 2 1478 . 141 PHE HD1 H 6.62 0.02 3 1479 . 141 PHE HE1 H 7.64 0.02 3 1480 . 141 PHE HZ H 7.29 0.02 1 1481 . 141 PHE C C 176.79 0.30 1 1482 . 141 PHE CA C 62.17 0.30 1 1483 . 141 PHE CB C 40.36 0.30 1 1484 . 141 PHE CD1 C 131.52 0.30 3 1485 . 141 PHE CE1 C 132.26 0.30 3 1486 . 141 PHE CZ C 128.55 0.30 1 1487 . 141 PHE N N 123.27 0.20 1 1488 . 142 VAL H H 8.79 0.02 1 1489 . 142 VAL HA H 3.15 0.02 1 1490 . 142 VAL HB H 1.72 0.02 1 1491 . 142 VAL HG1 H 0.73 0.02 1 1492 . 142 VAL HG2 H 0.45 0.02 1 1493 . 142 VAL C C 179.55 0.30 1 1494 . 142 VAL CA C 66.92 0.30 1 1495 . 142 VAL CB C 31.47 0.30 1 1496 . 142 VAL CG1 C 21.39 0.30 1 1497 . 142 VAL CG2 C 23.21 0.30 1 1498 . 142 VAL N N 119.10 0.20 1 1499 . 143 GLN H H 7.83 0.02 1 1500 . 143 GLN HA H 3.82 0.02 1 1501 . 143 GLN HB2 H 2.04 0.02 1 1502 . 143 GLN HB3 H 2.04 0.02 1 1503 . 143 GLN HG2 H 2.38 0.02 1 1504 . 143 GLN HG3 H 2.38 0.02 1 1505 . 143 GLN HE21 H 6.72 0.02 9 1506 . 143 GLN HE22 H 7.37 0.02 9 1507 . 143 GLN C C 178.27 0.30 1 1508 . 143 GLN CA C 59.18 0.30 1 1509 . 143 GLN CB C 28.07 0.30 1 1510 . 143 GLN CG C 34.19 0.30 1 1511 . 143 GLN N N 119.30 0.20 1 1512 . 143 GLN NE2 N 111.61 0.20 1 1513 . 144 MET H H 7.27 0.02 1 1514 . 144 MET HA H 4.43 0.02 1 1515 . 144 MET HB2 H 1.62 0.02 2 1516 . 144 MET HB3 H 1.95 0.02 2 1517 . 144 MET HG2 H 2.36 0.02 2 1518 . 144 MET HG3 H 2.80 0.02 2 1519 . 144 MET HE H 1.91 0.02 1 1520 . 144 MET C C 178.71 0.30 1 1521 . 144 MET CA C 55.90 0.30 1 1522 . 144 MET CB C 30.12 0.30 1 1523 . 144 MET CG C 32.27 0.30 1 1524 . 144 MET CE C 15.89 0.30 1 1525 . 144 MET N N 115.96 0.20 1 1526 . 145 MET H H 7.95 0.02 1 1527 . 145 MET HA H 4.20 0.02 1 1528 . 145 MET HB2 H 1.82 0.02 1 1529 . 145 MET HB3 H 1.82 0.02 1 1530 . 145 MET HG2 H 2.01 0.02 2 1531 . 145 MET HG3 H 2.15 0.02 2 1532 . 145 MET HE H 1.92 0.02 1 1533 . 145 MET C C 177.31 0.30 1 1534 . 145 MET CA C 57.92 0.30 1 1535 . 145 MET CB C 33.00 0.30 1 1536 . 145 MET CG C 32.87 0.30 1 1537 . 145 MET CE C 16.94 0.30 1 1538 . 145 MET N N 117.84 0.20 1 1539 . 146 THR H H 7.65 0.02 1 1540 . 146 THR HA H 4.38 0.02 1 1541 . 146 THR HB H 4.34 0.02 1 1542 . 146 THR HG2 H 1.18 0.02 1 1543 . 146 THR C C 174.46 0.30 1 1544 . 146 THR CA C 61.84 0.30 1 1545 . 146 THR CB C 70.48 0.30 1 1546 . 146 THR CG2 C 21.54 0.30 1 1547 . 146 THR N N 107.57 0.20 1 1548 . 147 ALA H H 7.50 0.02 1 1549 . 147 ALA HA H 4.29 0.02 1 1550 . 147 ALA HB H 1.44 0.02 1 1551 . 147 ALA C C 176.88 0.30 1 1552 . 147 ALA CA C 53.29 0.30 1 1553 . 147 ALA CB C 19.09 0.30 1 1554 . 147 ALA N N 126.38 0.20 1 1555 . 148 LYS H H 7.87 0.02 1 1556 . 148 LYS HA H 4.20 0.02 1 1557 . 148 LYS HB2 H 1.70 0.02 2 1558 . 148 LYS HB3 H 1.84 0.02 2 1559 . 148 LYS HG2 H 1.41 0.02 1 1560 . 148 LYS HG3 H 1.41 0.02 1 1561 . 148 LYS HD2 H 2.91 0.02 1 1562 . 148 LYS HD3 H 2.91 0.02 1 1563 . 148 LYS HE2 H 3.00 0.02 1 1564 . 148 LYS HE3 H 3.00 0.02 1 1565 . 148 LYS CA C 57.49 0.30 1 1566 . 148 LYS CB C 33.93 0.30 1 1567 . 148 LYS N N 125.78 0.20 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name camkk _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 . 3 LEU H H 8.65 0.02 1 2 . 3 LEU HA H 4.32 0.02 1 3 . 3 LEU HB2 H 1.58 0.02 2 4 . 3 LEU HB3 H 1.66 0.02 2 5 . 3 LEU HG H 1.58 0.02 1 6 . 3 LEU HD1 H 0.88 0.02 1 7 . 3 LEU HD2 H 0.81 0.02 1 8 . 4 ILE H H 7.62 0.02 1 9 . 4 ILE HA H 4.40 0.02 1 10 . 4 ILE HB H 1.85 0.02 1 11 . 4 ILE HG12 H 1.17 0.02 2 12 . 4 ILE HG13 H 1.39 0.02 2 13 . 4 ILE HG2 H 0.87 0.02 1 14 . 4 ILE HD1 H 0.73 0.02 1 15 . 5 PRO HA H 4.27 0.02 1 16 . 5 PRO HB2 H 1.69 0.02 2 17 . 5 PRO HB3 H 2.11 0.02 2 18 . 5 PRO HG2 H 1.77 0.02 2 19 . 5 PRO HG3 H 1.69 0.02 2 20 . 5 PRO HD2 H 3.49 0.02 2 21 . 5 PRO HD3 H 3.68 0.02 2 22 . 6 SER H H 8.35 0.02 1 23 . 6 SER HA H 4.40 0.02 1 24 . 6 SER HB2 H 4.11 0.02 2 25 . 6 SER HB3 H 4.26 0.02 2 26 . 7 TRP H H 8.68 0.02 1 27 . 7 TRP HA H 4.24 0.02 1 28 . 7 TRP HB2 H 3.22 0.02 2 29 . 7 TRP HB3 H 3.32 0.02 2 30 . 7 TRP HE3 H 7.16 0.02 1 31 . 7 TRP HZ2 H 6.81 0.02 1 32 . 7 TRP HZ3 H 6.41 0.02 1 33 . 7 TRP HH2 H 6.70 0.02 1 34 . 8 THR H H 7.98 0.02 1 35 . 8 THR HA H 3.66 0.02 1 36 . 8 THR HB H 4.09 0.02 1 37 . 8 THR HG2 H 1.09 0.02 1 38 . 9 THR H H 7.68 0.02 1 39 . 9 THR HA H 4.05 0.02 1 40 . 9 THR HB H 4.43 0.02 1 41 . 9 THR HG2 H 1.17 0.02 1 42 . 10 VAL H H 7.68 0.02 1 43 . 10 VAL HA H 3.39 0.02 1 44 . 10 VAL HB H 2.53 0.02 1 45 . 10 VAL HG1 H 1.01 0.02 2 46 . 11 ILE H H 7.76 0.02 1 47 . 11 ILE HA H 3.79 0.02 1 48 . 11 ILE HB H 2.03 0.02 1 49 . 11 ILE HG12 H 1.51 0.02 2 50 . 11 ILE HG13 H 1.87 0.02 2 51 . 11 ILE HG2 H 1.16 0.02 1 52 . 11 ILE HD1 H 0.72 0.02 1 53 . 12 LEU H H 8.48 0.02 1 54 . 12 LEU HA H 4.13 0.02 1 55 . 12 LEU HB2 H 1.89 0.02 2 56 . 12 LEU HB3 H 2.35 0.02 2 57 . 12 LEU HG H 1.69 0.02 1 58 . 12 LEU HD1 H 1.05 0.02 2 59 . 12 LEU HD2 H 0.93 0.02 2 60 . 13 VAL H H 8.26 0.02 1 61 . 13 VAL HA H 3.91 0.02 1 62 . 13 VAL HB H 2.06 0.02 1 63 . 13 VAL HG1 H 0.45 0.02 2 64 . 13 VAL HG2 H 0.99 0.02 2 65 . 14 LYS H H 8.16 0.02 1 66 . 14 LYS HA H 3.90 0.02 1 67 . 14 LYS HB2 H 1.85 0.02 2 68 . 14 LYS HB3 H 2.42 0.02 2 69 . 14 LYS HG2 H 1.64 0.02 1 70 . 14 LYS HG3 H 1.64 0.02 1 71 . 15 SER H H 8.38 0.02 1 72 . 15 SER HA H 4.23 0.02 1 73 . 15 SER HB2 H 3.81 0.02 2 74 . 15 SER HB3 H 4.10 0.02 2 75 . 16 MET H H 8.46 0.02 1 76 . 16 MET HA H 4.29 0.02 1 77 . 16 MET HB2 H 2.25 0.02 2 78 . 16 MET HB3 H 2.37 0.02 2 79 . 16 MET HG2 H 2.77 0.02 2 80 . 16 MET HG3 H 2.88 0.02 2 81 . 16 MET HE H 2.26 0.02 1 82 . 17 LEU H H 7.77 0.02 1 83 . 17 LEU HA H 3.79 0.02 1 84 . 17 LEU HB3 H 2.23 0.02 5 85 . 17 LEU HG H 1.95 0.02 5 86 . 17 LEU HD1 H 0.85 0.02 2 87 . 17 LEU HD2 H 1.09 0.02 2 88 . 18 ARG H H 8.35 0.02 1 89 . 18 ARG HA H 3.82 0.02 1 90 . 18 ARG HB2 H 1.70 0.02 1 91 . 18 ARG HB3 H 1.70 0.02 1 92 . 18 ARG HG2 H 1.99 0.02 1 93 . 18 ARG HG3 H 1.99 0.02 1 94 . 18 ARG HD2 H 3.35 0.02 2 95 . 18 ARG HD3 H 3.19 0.02 2 96 . 19 LYS H H 7.57 0.02 1 97 . 19 LYS HA H 4.11 0.02 1 98 . 19 LYS HB2 H 1.86 0.02 1 99 . 19 LYS HB3 H 1.86 0.02 1 100 . 19 LYS HG2 H 1.47 0.02 1 101 . 19 LYS HG3 H 1.47 0.02 1 102 . 19 LYS HD2 H 1.55 0.02 1 103 . 19 LYS HD3 H 1.55 0.02 1 104 . 20 ARG H H 8.00 0.02 1 105 . 20 ARG HA H 3.92 0.02 1 106 . 20 ARG HB2 H 1.99 0.02 2 107 . 20 ARG HB3 H 2.10 0.02 2 108 . 21 SER H H 7.67 0.02 1 109 . 21 SER HA H 3.96 0.02 1 110 . 21 SER HB2 H 3.79 0.02 2 111 . 21 SER HB3 H 3.94 0.02 2 112 . 22 PHE H H 9.69 0.02 1 113 . 22 PHE HA H 4.58 0.02 1 114 . 22 PHE HB2 H 2.49 0.02 2 115 . 22 PHE HB3 H 3.16 0.02 2 116 . 22 PHE HD1 H 7.24 0.02 3 117 . 22 PHE HE1 H 6.22 0.02 3 118 . 22 PHE HZ H 6.63 0.02 1 119 . 23 GLY H H 7.80 0.02 1 120 . 23 GLY HA2 H 3.51 0.02 2 121 . 23 GLY HA3 H 3.80 0.02 2 122 . 24 ASN H H 8.22 0.02 1 123 . 24 ASN HA H 4.43 0.02 1 124 . 24 ASN HB2 H 2.92 0.02 2 125 . 24 ASN HB3 H 3.02 0.02 2 126 . 24 ASN HD21 H 6.82 0.02 9 127 . 24 ASN HD22 H 7.55 0.02 9 128 . 26 PHE H H 7.56 0.02 1 129 . 26 PHE HA H 4.79 0.02 1 130 . 26 PHE HB2 H 3.01 0.02 2 131 . 26 PHE HB3 H 3.43 0.02 2 132 . 26 PHE HD1 H 7.31 0.02 3 133 . 26 PHE HE1 H 7.28 0.02 3 134 . 26 PHE HZ H 7.08 0.02 1 stop_ save_