data_15470 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignment of the Calmodulin-Munc13-1 peptide complex ; _BMRB_accession_number 15470 _BMRB_flat_file_name bmr15470.str _Entry_type new _Submission_date 2007-09-14 _Accession_date 2007-09-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Sequential 1H, 13C and 15N backbone and side-chain resonance assignment for calmoduliln - Munc13-1 (458-492)peptide complex' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rodriguez-Castaneda Fernando A. . 2 Carlomagno Teresa . . 3 Brose Nils . . 4 Griesinger Christian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 921 "13C chemical shifts" 666 "15N chemical shifts" 191 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-18 update BMRB 'complete entry citation' 2009-12-21 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title '(1)H, (13)C and (15)N resonance assignments of the Calmodulin-Munc13-1 peptide complex.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20013162 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rodriguez-Castaneda Fernando . . 2 Coudevylle Nicolas . . 3 Becker Stefan . . 4 Brose Nils . . 5 Carlomagno Teresa . . 6 Griesinger Christian . . stop_ _Journal_abbreviation 'Biomol. NMR assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 45 _Page_last 48 _Year 2009 _Details . loop_ _Keyword calmodulin Munc13 'neurotransmitter release' 'vesicle priming' synaptosome stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Calmodulin-Munc13-1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label calmodulin $calmodulin Munc13-1 $Munc13-1_(458-492) 'Calcium I' $CA 'Calcium II' $CA 'Calcium III' $CA 'Calcium IV' $CA stop_ _System_molecular_weight 21900 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 calmodulin 2 Munc13-1 stop_ loop_ _Biological_function 'potentiation of neurotransmitter release' 'presynaptic synaptic plasticity' stop_ _Database_query_date . _Details '[4Ca2+]bound calmodulin complexed with a fragment consisting of residues 458-492 of the diacylglycerol-binding protein Munc13-1' save_ ######################## # Monomeric polymers # ######################## save_calmodulin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common calmodulin _Molecular_mass 16700 _Mol_thiol_state 'not present' loop_ _Biological_function 'Calcium signalling' 'Protein kinase activator' stop_ _Details 'Molecular entity ID _ 1' ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREANIDGDGQVNYEE 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 ASN 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 2015-10-07 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 99.32 100.00 1.91e-99 BMRB 15185 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15186 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15187 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15188 calmodulin 100.00 148 98.65 100.00 4.63e-99 BMRB 15191 Calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15624 Calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15650 calmodulin 100.00 148 98.65 100.00 1.16e-98 BMRB 15852 calmodulin 100.00 148 98.65 100.00 1.16e-98 BMRB 1634 calmodulin 100.00 148 97.97 99.32 3.06e-98 BMRB 16418 apoCaM 100.00 148 99.32 100.00 1.91e-99 BMRB 16465 entity_1 100.00 148 99.32 100.00 1.91e-99 BMRB 1648 calmodulin 100.00 148 97.97 99.32 3.06e-98 BMRB 16764 CALMODULIN 100.00 150 99.32 100.00 2.04e-99 BMRB 17264 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 17360 entity_1 100.00 148 99.32 100.00 1.91e-99 BMRB 17771 Calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 17807 Calmodulin 99.32 147 99.32 100.00 8.43e-99 BMRB 18027 CaM 100.00 148 99.32 100.00 1.91e-99 BMRB 18028 CaM 100.00 148 99.32 100.00 1.91e-99 BMRB 18556 Calmodulin 100.00 148 97.97 99.32 8.84e-98 BMRB 19036 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 19238 Calmodulin_prototypical_calcium_sensor 100.00 148 99.32 100.00 1.91e-99 BMRB 19586 entity_1 100.00 148 99.32 100.00 1.91e-99 BMRB 19604 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 25253 CaM 100.00 148 97.97 99.32 4.45e-97 BMRB 25257 CaM 100.00 148 97.97 99.32 4.45e-97 BMRB 26503 Calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 26626 CaM 100.00 148 99.32 100.00 1.91e-99 BMRB 26627 CaM 100.00 148 99.32 100.00 1.91e-99 BMRB 4056 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 4270 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 4284 Calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 4310 calmodulin 100.00 148 99.32 100.00 1.91e-99 PDB 1A29 "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" 100.00 148 99.32 100.00 1.91e-99 PDB 1CFC "Calcium-Free Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 1CFD "Calcium-Free Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 1CFF "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" 100.00 148 99.32 100.00 1.91e-99 PDB 1CKK "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" 100.00 148 99.32 100.00 1.91e-99 PDB 1CLL "Calmodulin Structure Refined At 1.7 Angstroms Resolution" 100.00 148 99.32 100.00 1.91e-99 PDB 1CM1 "Motions Of Calmodulin-Single-Conformer Refinement" 100.00 148 99.32 100.00 1.91e-99 PDB 1CM4 "Motions Of Calmodulin-four-conformer Refinement" 100.00 148 99.32 100.00 1.91e-99 PDB 1CTR "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 1DMO "Calmodulin, Nmr, 30 Structures" 100.00 148 100.00 100.00 2.48e-100 PDB 1G4Y "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 1IQ5 "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" 100.00 149 99.32 100.00 2.09e-99 PDB 1IWQ "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" 100.00 148 99.32 100.00 1.91e-99 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 99.32 100.00 1.91e-99 PDB 1K93 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 97.30 144 99.31 100.00 1.56e-96 PDB 1L7Z "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" 100.00 148 99.32 100.00 1.91e-99 PDB 1LIN "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" 100.00 148 99.32 100.00 1.91e-99 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 99.32 100.00 2.09e-99 PDB 1MUX "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" 100.00 148 99.32 100.00 1.91e-99 PDB 1MXE "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" 100.00 148 97.30 99.32 2.44e-97 PDB 1NWD "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" 100.00 148 99.32 100.00 1.91e-99 PDB 1OOJ "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" 100.00 149 97.30 98.65 4.81e-97 PDB 1PRW "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" 100.00 149 98.65 99.32 1.41e-98 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 99.32 100.00 1.91e-99 PDB 1QIW "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" 100.00 148 99.32 100.00 1.91e-99 PDB 1QX5 "Crystal Structure Of Apocalmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 1S26 "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" 100.00 148 99.32 100.00 1.91e-99 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 99.32 100.00 1.91e-99 PDB 1SY9 "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" 100.00 148 99.32 100.00 1.91e-99 PDB 1UP5 "Chicken Calmodulin" 100.00 148 98.65 99.32 1.36e-98 PDB 1WRZ "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" 100.00 149 99.32 100.00 2.09e-99 PDB 1X02 "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 1XA5 "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" 100.00 148 99.32 100.00 1.91e-99 PDB 1XFU "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" 100.00 149 98.65 100.00 5.05e-99 PDB 1XFV "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 149 98.65 100.00 5.05e-99 PDB 1XFW "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" 100.00 149 98.65 100.00 5.05e-99 PDB 1XFY "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 100.00 149 98.65 100.00 5.05e-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 98.65 100.00 5.05e-99 PDB 1Y0V "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" 97.30 146 99.31 100.00 1.60e-96 PDB 1YR5 "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" 100.00 148 99.32 100.00 1.91e-99 PDB 2BBM "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.30 99.32 2.44e-97 PDB 2BBN "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.30 99.32 2.44e-97 PDB 2BCX "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" 100.00 148 99.32 100.00 1.91e-99 PDB 2BKH "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" 100.00 149 97.30 99.32 1.90e-97 PDB 2BKI "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" 100.00 149 99.32 100.00 2.09e-99 PDB 2DFS "3-D Structure Of Myosin-V Inhibited State" 100.00 148 99.32 100.00 1.91e-99 PDB 2F2O "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 99.32 100.00 3.36e-99 PDB 2F2P "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 99.32 100.00 3.36e-99 PDB 2F3Y "CalmodulinIQ DOMAIN COMPLEX" 100.00 148 99.32 100.00 1.91e-99 PDB 2F3Z "CalmodulinIQ-Aa Domain Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 2FOT "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" 100.00 148 99.32 100.00 1.91e-99 PDB 2HQW "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" 100.00 148 99.32 100.00 1.91e-99 PDB 2JZI "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" 100.00 148 99.32 100.00 1.91e-99 PDB 2K0E "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" 100.00 148 99.32 100.00 1.91e-99 PDB 2K0F "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" 100.00 148 99.32 100.00 1.91e-99 PDB 2K0J "Solution Structure Of Cam Complexed To Drp1p" 100.00 148 98.65 100.00 1.16e-98 PDB 2K61 "Solution Structure Of Cam Complexed To Dapk Peptide" 100.00 148 98.65 100.00 1.16e-98 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 99.32 100.00 1.91e-99 PDB 2KNE "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" 100.00 148 99.32 100.00 1.91e-99 PDB 2L53 "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" 100.00 148 99.32 100.00 1.91e-99 PDB 2L7L "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" 100.00 148 99.32 100.00 1.91e-99 PDB 2LGF "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" 98.65 146 99.32 100.00 5.06e-98 PDB 2LL6 "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" 100.00 148 99.32 100.00 1.91e-99 PDB 2LL7 "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" 100.00 148 99.32 100.00 1.91e-99 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 97.97 99.32 8.84e-98 PDB 2M0J "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 2M0K "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" 100.00 148 99.32 100.00 1.91e-99 PDB 2M55 "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 2MG5 "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" 100.00 148 99.32 100.00 1.91e-99 PDB 2MGU "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" 100.00 148 99.32 100.00 1.91e-99 PDB 2O5G "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 2O60 "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" 100.00 148 99.32 100.00 1.91e-99 PDB 2R28 "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" 100.00 149 99.32 100.00 2.09e-99 PDB 2V01 "Recombinant Vertebrate Calmodulin Complexed With Pb" 100.00 149 99.32 100.00 2.09e-99 PDB 2V02 "Recombinant Vertebrate Calmodulin Complexed With Ba" 100.00 149 99.32 100.00 2.09e-99 PDB 2VAS "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" 100.00 149 97.30 99.32 1.90e-97 PDB 2VAY "Calmodulin Complexed With Cav1.1 Iq Peptide" 98.65 146 99.32 100.00 5.06e-98 PDB 2W73 "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" 100.00 149 99.32 100.00 2.09e-99 PDB 2WEL "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" 100.00 150 99.32 100.00 1.22e-99 PDB 2X0G "X-ray Structure Of A Dap-kinase Calmodulin Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 2X51 "M6 Delta Insert1" 100.00 149 97.30 99.32 1.90e-97 PDB 2Y4V "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" 100.00 149 99.32 100.00 2.09e-99 PDB 2YGG "Complex Of Cambr And Cam" 100.00 150 99.32 100.00 1.31e-99 PDB 3BXK "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3BXL "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3BYA "Structure Of A Calmodulin Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3CLN "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" 100.00 148 100.00 100.00 2.48e-100 PDB 3DVE "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3DVJ "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3DVK "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3DVM "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" 100.00 148 99.32 100.00 1.91e-99 PDB 3EK4 "Calcium-saturated Gcamp2 Monomer" 99.32 449 99.32 100.00 3.93e-95 PDB 3EK7 "Calcium-Saturated Gcamp2 Dimer" 99.32 449 99.32 100.00 3.93e-95 PDB 3EK8 "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" 99.32 449 99.32 100.00 4.01e-95 PDB 3EKH "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" 99.32 449 98.64 99.32 3.45e-94 PDB 3EVU "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" 99.32 449 99.32 100.00 3.93e-95 PDB 3EVV "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" 99.32 449 99.32 100.00 3.93e-95 PDB 3EWT "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 99.32 100.00 8.19e-100 PDB 3EWV "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 99.32 100.00 8.19e-100 PDB 3G43 "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" 100.00 148 99.32 100.00 1.91e-99 PDB 3GN4 "Myosin Lever Arm" 100.00 149 97.30 99.32 1.90e-97 PDB 3GOF "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" 100.00 148 99.32 100.00 1.91e-99 PDB 3HR4 "Human Inos Reductase And Calmodulin Complex" 100.00 149 99.32 100.00 2.09e-99 PDB 3IF7 "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" 100.00 148 99.32 100.00 1.91e-99 PDB 3J41 "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" 100.00 149 99.32 100.00 2.09e-99 PDB 3L9I "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" 100.00 149 97.30 99.32 1.90e-97 PDB 3O77 "The Structure Of Ca2+ Sensor (Case-16)" 99.32 415 99.32 100.00 1.85e-95 PDB 3O78 "The Structure Of Ca2+ Sensor (Case-12)" 99.32 415 99.32 100.00 1.85e-95 PDB 3OXQ "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" 100.00 149 99.32 100.00 2.09e-99 PDB 3SG2 "Crystal Structure Of Gcamp2-t116v,d381y" 99.32 449 98.64 99.32 5.67e-94 PDB 3SG3 "Crystal Structure Of Gcamp3-d380y" 99.32 449 97.96 99.32 4.46e-93 PDB 3SG4 "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" 100.00 448 97.30 98.65 3.73e-93 PDB 3SG5 "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" 100.00 448 97.30 98.65 3.81e-93 PDB 3SG6 "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" 99.32 450 99.32 100.00 4.50e-95 PDB 3SG7 "Crystal Structure Of Gcamp3-kf(linker 1)" 99.32 448 98.64 100.00 3.39e-94 PDB 3SJQ "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" 100.00 149 99.32 100.00 2.09e-99 PDB 3SUI "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" 100.00 149 99.32 100.00 2.09e-99 PDB 3U0K "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" 99.32 440 97.96 99.32 9.15e-94 PDB 3WFN "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" 100.00 182 99.32 100.00 1.99e-99 PDB 4ANJ "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" 100.00 149 97.30 99.32 1.90e-97 PDB 4BW7 "Calmodulin In Complex With Strontium" 100.00 149 99.32 100.00 2.09e-99 PDB 4BW8 "Calmodulin With Small Bend In Central Helix" 100.00 149 99.32 100.00 2.09e-99 PDB 4BYF "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" 100.00 149 99.32 100.00 2.09e-99 PDB 4CLN "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" 100.00 148 97.30 99.32 2.44e-97 PDB 4DBP "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" 100.00 149 97.30 99.32 1.90e-97 PDB 4DBQ "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" 100.00 149 97.30 99.32 1.90e-97 PDB 4DCK "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" 100.00 149 99.32 100.00 2.09e-99 PDB 4DJC "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" 100.00 152 99.32 100.00 1.28e-99 PDB 4E50 "Calmodulin And Ng Peptide Complex" 100.00 185 99.32 100.00 9.83e-100 PDB 4EHQ "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" 100.00 148 99.32 100.00 1.91e-99 PDB 4G27 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" 100.00 149 99.32 100.00 2.09e-99 PDB 4G28 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" 100.00 149 99.32 100.00 2.09e-99 PDB 4HEX "A Novel Conformation Of Calmodulin" 100.00 156 99.32 100.00 7.68e-100 PDB 4IK1 "High Resolution Structure Of Gcampj At Ph 8.5" 99.32 448 97.96 99.32 4.24e-93 PDB 4IK3 "High Resolution Structure Of Gcamp3 At Ph 8.5" 99.32 448 98.64 100.00 3.14e-94 PDB 4IK4 "High Resolution Structure Of Gcamp3 At Ph 5.0" 99.32 448 98.64 100.00 3.14e-94 PDB 4IK5 "High Resolution Structure Of Delta-rest-gcamp3" 99.32 414 98.64 100.00 1.27e-94 PDB 4IK8 "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" 99.32 448 98.64 100.00 3.14e-94 PDB 4IK9 "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" 99.32 448 98.64 100.00 3.14e-94 PDB 4J9Y "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" 100.00 149 99.32 100.00 2.09e-99 PDB 4J9Z "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" 100.00 149 99.32 100.00 2.09e-99 PDB 4JPZ "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" 100.00 149 99.32 100.00 2.09e-99 PDB 4JQ0 "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" 100.00 149 99.32 100.00 2.09e-99 PDB 4L79 "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" 100.00 149 99.32 100.00 2.09e-99 PDB 4LZX "Complex Of Iqcg And Ca2+-free Cam" 100.00 148 99.32 100.00 1.91e-99 PDB 4M1L "Complex Of Iqcg And Ca2+-bound Cam" 100.00 148 99.32 100.00 1.91e-99 PDB 4Q5U "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" 100.00 149 99.32 100.00 2.09e-99 PDB 4QNH "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" 100.00 149 98.65 99.32 2.41e-98 PDB 4R8G "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 4UMO "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 99.32 100.00 2.09e-99 PDB 4UPU "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" 100.00 148 99.32 100.00 1.91e-99 PDB 4V0C "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 99.32 100.00 2.09e-99 DBJ BAA08302 "calmodulin [Homo sapiens]" 100.00 149 99.32 100.00 2.09e-99 DBJ BAA11896 "calmodulin [Anas platyrhynchos]" 100.00 149 99.32 100.00 2.09e-99 DBJ BAA19786 "calmodulin [Branchiostoma lanceolatum]" 100.00 149 97.30 99.32 1.90e-97 DBJ BAA19787 "calmodulin [Branchiostoma floridae]" 100.00 149 97.30 99.32 1.90e-97 DBJ BAA19788 "calmodulin [Halocynthia roretzi]" 100.00 149 97.30 99.32 1.90e-97 EMBL CAA10601 "calmodulin [Caenorhabditis elegans]" 100.00 149 97.30 98.65 4.81e-97 EMBL CAA32050 "calmodulin [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 EMBL CAA32062 "calmodulin II [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 EMBL CAA32119 "calmodulin [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 EMBL CAA32120 "calmodulin [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 GB AAA35635 "calmodulin [Homo sapiens]" 100.00 149 99.32 100.00 2.09e-99 GB AAA35641 "calmodulin [Homo sapiens]" 100.00 149 99.32 100.00 2.09e-99 GB AAA37365 "calmodulin synthesis [Mus musculus]" 100.00 149 99.32 100.00 2.09e-99 GB AAA40862 "calmodulin [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 GB AAA40863 "calmodulin [Rattus norvegicus]" 100.00 149 99.32 100.00 2.09e-99 PIR JC1305 "calmodulin - Japanese medaka" 100.00 149 99.32 100.00 2.09e-99 PIR MCON "calmodulin - salmon" 100.00 148 99.32 100.00 1.91e-99 PRF 0409298A "troponin C-like protein" 100.00 148 97.97 100.00 3.64e-99 PRF 0608335A calmodulin 100.00 148 97.30 99.32 8.66e-97 REF NP_001008160 "calmodulin [Xenopus (Silurana) tropicalis]" 100.00 149 99.32 100.00 2.09e-99 REF NP_001009759 "calmodulin [Ovis aries]" 100.00 149 99.32 100.00 2.09e-99 REF NP_001039714 "calmodulin [Bos taurus]" 100.00 149 99.32 100.00 2.09e-99 REF NP_001040234 "calmodulin [Bombyx mori]" 100.00 149 97.30 99.32 1.90e-97 REF NP_001080864 "calmodulin [Xenopus laevis]" 100.00 149 99.32 100.00 2.09e-99 SP O16305 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 97.30 98.65 4.81e-97 SP P02594 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 98.65 100.00 6.57e-99 SP P21251 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 97.97 99.32 3.94e-98 SP P62144 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 99.32 100.00 2.09e-99 SP P62145 "RecName: Full=Calmodulin; Short=CaM [Aplysia californica]" 100.00 149 97.30 99.32 1.90e-97 TPG DAA13808 "TPA: calmodulin 2-like [Bos taurus]" 100.00 216 97.97 98.65 1.07e-97 TPG DAA18029 "TPA: calmodulin [Bos taurus]" 100.00 149 97.97 99.32 3.13e-98 TPG DAA19590 "TPA: calmodulin 3 [Bos taurus]" 100.00 149 99.32 100.00 2.09e-99 TPG DAA24777 "TPA: calmodulin 2-like [Bos taurus]" 100.00 149 99.32 100.00 2.09e-99 TPG DAA24988 "TPA: calmodulin 2-like isoform 1 [Bos taurus]" 100.00 149 99.32 100.00 2.09e-99 stop_ save_ save_Munc13-1_(458-492) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Munc13-1_(458-492) _Molecular_mass 4170 _Mol_thiol_state 'not present' loop_ _Biological_function 'Vesicle priming' 'Neurotransmitter release' stop_ _Details 'Molecular entity ID _ 2' _Residue_count 36 _Mol_residue_sequence ; GSRAKANWLRAFNKVRMQLQ EARGEGEMSKSLWFKG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 458 SER 3 459 ARG 4 460 ALA 5 461 LYS 6 462 ALA 7 463 ASN 8 464 TRP 9 465 LEU 10 466 ARG 11 467 ALA 12 468 PHE 13 469 ASN 14 470 LYS 15 471 VAL 16 472 ARG 17 473 MET 18 474 GLN 19 475 LEU 20 476 GLN 21 477 GLU 22 478 ALA 23 479 ARG 24 480 GLY 25 481 GLU 26 482 GLY 27 483 GLU 28 484 MET 29 485 SER 30 486 LYS 31 487 SER 32 488 LEU 33 489 TRP 34 490 PHE 35 491 LYS 36 492 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-31 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2KDU "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" 100.00 36 100.00 100.00 1.20e-15 DBJ BAA82984 "KIAA1032 protein [Homo sapiens]" 97.22 1702 100.00 100.00 1.38e-14 DBJ BAE27895 "unnamed protein product [Mus musculus]" 97.22 1586 97.14 100.00 5.05e-14 DBJ BAJ17676 "unc-13 homolog A [synthetic construct]" 97.22 1703 100.00 100.00 1.38e-14 GB AAC52266 "Munc13-1 [Rattus norvegicus]" 97.22 1735 100.00 100.00 1.94e-14 GB AAI72223 "unc-13 homolog A (C. elegans), partial [synthetic construct]" 97.22 1791 100.00 100.00 1.39e-14 GB AAX09281 "munc 13-1 [Mus musculus]" 97.22 1712 100.00 100.00 2.21e-14 GB EDL28951 "unc-13 homolog A (C. elegans) [Mus musculus]" 97.22 1638 97.14 100.00 5.99e-14 GB ELK19163 "Protein unc-13 like protein A [Pteropus alecto]" 97.22 1693 97.14 100.00 4.89e-14 REF NP_001025044 "protein unc-13 homolog A [Mus musculus]" 97.22 1712 97.14 100.00 6.60e-14 REF NP_001073890 "protein unc-13 homolog A [Homo sapiens]" 97.22 1703 100.00 100.00 1.46e-14 REF NP_074052 "protein unc-13 homolog A [Rattus norvegicus]" 97.22 1735 100.00 100.00 1.94e-14 REF XP_002688619 "PREDICTED: protein unc-13 homolog A isoform X9 [Bos taurus]" 97.22 1707 97.14 100.00 4.67e-14 REF XP_002801170 "PREDICTED: protein unc-13 homolog A-like, partial [Macaca mulatta]" 97.22 1029 100.00 100.00 1.62e-14 SP Q4KUS2 "RecName: Full=Protein unc-13 homolog A; AltName: Full=Munc13-1 [Mus musculus]" 97.22 1712 97.14 100.00 6.60e-14 SP Q62768 "RecName: Full=Protein unc-13 homolog A; AltName: Full=Munc13-1 [Rattus norvegicus]" 97.22 1735 100.00 100.00 1.94e-14 SP Q9UPW8 "RecName: Full=Protein unc-13 homolog A; AltName: Full=Munc13-1 [Homo sapiens]" 97.22 1703 100.00 100.00 1.46e-14 TPG DAA28231 "TPA: protein unc-13 homolog A-like [Bos taurus]" 97.22 1818 97.14 100.00 8.11e-14 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 Mon Aug 20 19:28:44 2007 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA N 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $calmodulin 'African clawed frog' 8355 Eukaryota Metazoa Xenopus laevis $Munc13-1_(458-492) 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 _Variant _Vector_name _Details $calmodulin 'recombinant technology' . . . BL21 (DE3) 'pET28a and pGEX-2T' 'The his tag is off-frame, N-terminal GST fusion tag with thrombin cleavage recognition site' $Munc13-1_(458-492) 'chemical synthesis' . . . . . . 'This natural abundance synthetic peptide was used in the samples where calmodulin was uniformly labeled' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_13C15NCaM/Munc13-1 _Saveframe_category sample _Sample_type solution _Details 'uniformly 13C,15N labeled calmodulin bound to the syntethic Munc13-1(459-492) peptide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $calmodulin 1.5 mM '[U-13C; U-15N]' $Munc13-1_(458-492) 1.8 mM 'natural abundance' 'Calcium chloride' 10 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' 'Potassium chloride' 150 mM 'natural abundance' stop_ save_ save_13C15NMunc13-1/CaM _Saveframe_category sample _Sample_type solution _Details 'Uniformly 13C,15N labeled Munc13-1 (458-492) peptide bound to calmodulin' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Munc13-1_(458-492) 0.5 mM '[U-13C; U-15N]' $calmodulin 0.6 mM 'natural abundance' 'Calcium chloride' 10 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' 'potassium chloride' 150 mM 'natural abundance' stop_ save_ save_13C15NCaM/Munc13-1D2O _Saveframe_category sample _Sample_type solution _Details 'Uniformly 13C,15N calmodulin bound to a Munc13-1 (459-492) synthetic peptide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $calmodulin 1.5 mM '[U-13C; U-15N]' $Munc13-1_(458-492) 1.8 mM 'natural abundance' 'Calcium chloride' 10 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' 'Potassium chloride' 150 mM 'natural abundance' stop_ save_ save_15NCaM/Munc13-1Pf1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $calmodulin 1.5 mM [U-15N] $Munc13-1_(458-492) 1.8 mM 'natural abundance' 'Calcium chloride' 10 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' 'Potassium chloride' 150 mM 'natural abundance' 'Bacteriophage Pf1' 4.2 mg 'natural abundance' stop_ save_ save_13C15NMunc13-1/CaMPf1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Munc13-1_(458-492) 0.5 mM '[U-13C; U-15N]' $calmodulin 0.6 mM 'natural abundance' 'Calcium chloride' 10 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' 'Potassium chloride' 150 mM 'natural abundance' 'Bacteriophage Pf1' 4.2 mg 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' 'Rheinstetten, Germany' www.bruker-biospin.com stop_ loop_ _Task collection processing stop_ _Details 'Software provided with Bruker NMR instruments for data acquisition, processing and analysis' save_ save_Felix _Saveframe_category software _Name Felix _Version 2004 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' 'San Diego, CA. USA' www.felixnmr.com stop_ loop_ _Task processing stop_ _Details 'Felix 2004 (UNIX)' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' 'Bethesda, MD. USA' www.spin.niddk.nih.gov/nmrpipe stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard 'San Francisco, CA. USA' www.cgl.ucsf.edu/home/sparky stop_ loop_ _Task 'chemical shift assignment' 'peak picking' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600avance _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Cryogenic cooled HCN probehead with Z-gradient coil unit' save_ save_600DRX _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'HCN probehead with Z-gradient coil unit' save_ save_700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'HCN probehead with triple-axis gradient coil unit' save_ save_800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 800 _Details 'Cryogenic cooled HCN probehead with Z-gradient coil unit' save_ save_900 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details 'Cryogenic cooled HCN probehead with Z-gradient coil unit' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $13C15NCaM/Munc13-1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $13C15NCaM/Munc13-1D2O save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $13C15NCaM/Munc13-1D2O save_ save_3D_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_C(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $13C15NCaM/Munc13-1 save_ save_3D_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $13C15NCaM/Munc13-1D2O save_ save_2D_HBCBCaro_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HBCBCaro' _Sample_label $13C15NCaM/Munc13-1D2O save_ save_3D_HMBCMet_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HMBCMet' _Sample_label $13C15NCaM/Munc13-1D2O save_ save_2D_1H-15N_HSQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $13C15NMunc13-1/CaM save_ save_2D_1H-13C_HSQC_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_CBCA(CO)NH_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_C(CO)NH_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_HNCO_18 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_HNCACB_19 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_H(CCO)NH_20 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_HCCH-TOCSY_21 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_1H-15N_NOESY_22 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_1H-13C_NOESY_23 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $13C15NMunc13-1/CaM save_ save_3D_HN(CA)CO_24 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $13C15NMunc13-1/CaM save_ save_2D_HBCBCaro_25 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HBCBCaro' _Sample_label $13C15NMunc13-1/CaM save_ save_2D_1H-15N_HSQC_26 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15NCaM/Munc13-1Pf1 save_ save_2D_1H-15N_HSQC_27 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $13C15NMunc13-1/CaMPf1 save_ ####################### # Sample conditions # ####################### save_single _Saveframe_category sample_conditions _Details 'single sample condition' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 308 0.1 K pH 6.8 0.1 pH pressure 1 . atm 'ionic strength' 0.16 0.2 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 n/a indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 n/a indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' '3D H(CCO)NH' '3D C(CO)NH' '3D HCCH-TOCSY' '2D HBCBCaro' '3D HMBCMet' stop_ loop_ _Sample_label $13C15NCaM/Munc13-1 $13C15NCaM/Munc13-1D2O $13C15NMunc13-1/CaM stop_ _Sample_conditions_label $single _Chem_shift_reference_set_label $chem_shift_reference _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 HA H 4.6268 0.050 1 2 1 1 ALA HB H 1.5108 0.050 1 3 1 1 ALA CB C 19.3538 0.400 1 4 2 2 ASP H H 8.6498 0.050 1 5 2 2 ASP HA H 4.6238 0.050 1 6 2 2 ASP HB2 H 2.6578 0.050 2 7 2 2 ASP HB3 H 2.5778 0.050 2 8 2 2 ASP C C 172.776 0.400 1 9 2 2 ASP CA C 54.7208 0.400 1 10 2 2 ASP CB C 41.4108 0.400 1 11 2 2 ASP N N 120.408 0.400 1 12 3 3 GLN H H 8.3488 0.050 1 13 3 3 GLN HA H 4.3718 0.050 1 14 3 3 GLN HB2 H 2.0998 0.050 2 15 3 3 GLN HB3 H 1.9848 0.050 2 16 3 3 GLN HG2 H 2.3438 0.050 2 17 3 3 GLN C C 172.795 0.400 1 18 3 3 GLN CA C 55.5088 0.400 1 19 3 3 GLN CB C 29.6228 0.400 1 20 3 3 GLN CG C 33.7638 0.400 1 21 3 3 GLN N N 119.406 0.400 1 22 4 4 LEU H H 8.2758 0.050 1 23 4 4 LEU HA H 4.6658 0.050 1 24 4 4 LEU HB2 H 1.7198 0.050 2 25 4 4 LEU HB3 H 1.5088 0.050 2 26 4 4 LEU HD1 H 0.9218 0.050 2 27 4 4 LEU HD2 H 0.9138 0.050 2 28 4 4 LEU C C 174.846 0.400 1 29 4 4 LEU CA C 54.4288 0.400 1 30 4 4 LEU CB C 43.4358 0.400 1 31 4 4 LEU CD1 C 26.5188 0.400 2 32 4 4 LEU CD2 C 23.6078 0.400 2 33 4 4 LEU CG C 26.7118 0.400 1 34 4 4 LEU N N 122.558 0.400 1 35 5 5 THR H H 8.6608 0.050 1 36 5 5 THR HA H 4.4578 0.050 1 37 5 5 THR HB H 4.7428 0.050 1 38 5 5 THR HG2 H 1.3348 0.050 1 39 5 5 THR C C 172.634 0.400 1 40 5 5 THR CA C 60.4938 0.400 1 41 5 5 THR CB C 71.0398 0.400 1 42 5 5 THR N N 112.406 0.400 1 43 6 6 GLU H H 9.0168 0.050 1 44 6 6 GLU HA H 3.9888 0.050 1 45 6 6 GLU HB2 H 2.0698 0.050 2 46 6 6 GLU HG2 H 2.3698 0.050 2 47 6 6 GLU C C 176.679 0.400 1 48 6 6 GLU CA C 60.1138 0.400 1 49 6 6 GLU CB C 28.8778 0.400 1 50 6 6 GLU CG C 36.4658 0.400 1 51 6 6 GLU N N 120.053 0.400 1 52 7 7 GLU H H 8.6658 0.050 1 53 7 7 GLU HA H 4.0888 0.050 1 54 7 7 GLU HB2 H 2.1128 0.050 2 55 7 7 GLU HB3 H 1.9568 0.050 2 56 7 7 GLU HG2 H 2.3488 0.050 2 57 7 7 GLU C C 176.396 0.400 1 58 7 7 GLU CA C 59.4768 0.400 1 59 7 7 GLU CB C 29.2168 0.400 1 60 7 7 GLU CG C 36.5738 0.400 1 61 7 7 GLU N N 118.929 0.400 1 62 8 8 GLN H H 7.7268 0.050 1 63 8 8 GLN HA H 4.0168 0.050 1 64 8 8 GLN HB2 H 2.0748 0.050 2 65 8 8 GLN HB3 H 1.9518 0.050 2 66 8 8 GLN HG2 H 2.3468 0.050 2 67 8 8 GLN C C 175.426 0.400 1 68 8 8 GLN CA C 59.2018 0.400 1 69 8 8 GLN CB C 29.2978 0.400 1 70 8 8 GLN CG C 34.9948 0.400 1 71 8 8 GLN N N 119.631 0.400 1 72 9 9 ILE H H 8.3558 0.050 1 73 9 9 ILE HA H 3.6678 0.050 1 74 9 9 ILE HB H 1.9468 0.050 1 75 9 9 ILE HD1 H 0.8698 0.050 1 76 9 9 ILE HG12 H 1.7898 0.050 2 77 9 9 ILE HG13 H 1.1008 0.050 2 78 9 9 ILE HG2 H 1.1088 0.050 1 79 9 9 ILE C C 174.972 0.400 1 80 9 9 ILE CA C 66.2438 0.400 1 81 9 9 ILE CB C 37.6528 0.400 1 82 9 9 ILE CG1 C 30.0558 0.400 1 83 9 9 ILE CG2 C 17.3308 0.400 1 84 9 9 ILE N N 119.286 0.400 1 85 10 10 ALA H H 8.0378 0.050 1 86 10 10 ALA HA H 4.1148 0.050 1 87 10 10 ALA HB H 1.5208 0.050 1 88 10 10 ALA C C 178.227 0.400 1 89 10 10 ALA CA C 55.3388 0.400 1 90 10 10 ALA CB C 17.7468 0.400 1 91 10 10 ALA N N 120.740 0.400 1 92 11 11 GLU H H 7.8478 0.050 1 93 11 11 GLU HA H 4.1628 0.050 1 94 11 11 GLU HB2 H 2.0978 0.050 2 95 11 11 GLU HB3 H 2.0178 0.050 2 96 11 11 GLU HG2 H 2.0148 0.050 2 97 11 11 GLU C C 177.704 0.400 1 98 11 11 GLU CA C 59.4538 0.400 1 99 11 11 GLU CG C 35.5888 0.400 1 100 11 11 GLU N N 118.942 0.400 1 101 12 12 PHE H H 8.6068 0.050 1 102 12 12 PHE HA H 5.0048 0.050 1 103 12 12 PHE HB2 H 3.5338 0.050 2 104 12 12 PHE HB3 H 3.4618 0.050 2 105 12 12 PHE HD1 H 7.1668 0.050 3 106 12 12 PHE HD2 H 7.1668 0.050 3 107 12 12 PHE HE1 H 7.2128 0.050 3 108 12 12 PHE HE2 H 7.2128 0.050 3 109 12 12 PHE HZ H 6.7078 0.050 1 110 12 12 PHE C C 175.906 0.400 1 111 12 12 PHE CA C 58.9768 0.400 1 112 12 12 PHE CB C 37.4318 0.400 1 113 12 12 PHE CD1 C 128.343 0.400 3 114 12 12 PHE CD2 C 128.343 0.400 3 115 12 12 PHE N N 119.640 0.400 1 116 13 13 LYS H H 9.2148 0.050 1 117 13 13 LYS HA H 4.0098 0.050 1 118 13 13 LYS HB2 H 1.9098 0.050 2 119 13 13 LYS HD2 H 1.2578 0.050 2 120 13 13 LYS HD3 H 1.1078 0.050 2 121 13 13 LYS HE2 H 2.5478 0.050 2 122 13 13 LYS HG2 H 0.6978 0.050 2 123 13 13 LYS C C 176.515 0.400 1 124 13 13 LYS N N 122.920 0.400 1 125 14 14 GLU H H 7.7328 0.050 1 126 14 14 GLU HA H 3.8078 0.050 1 127 14 14 GLU HB2 H 1.8978 0.050 2 128 14 14 GLU HG2 H 2.0778 0.050 2 129 14 14 GLU C C 176.562 0.400 1 130 14 14 GLU N N 119.254 0.400 1 131 15 15 ALA H H 8.0278 0.050 1 132 15 15 ALA HA H 4.2028 0.050 1 133 15 15 ALA HB H 1.9258 0.050 1 134 15 15 ALA C C 176.200 0.400 1 135 15 15 ALA CA C 55.2968 0.400 1 136 15 15 ALA CB C 18.4428 0.400 1 137 15 15 ALA N N 121.803 0.400 1 138 16 16 PHE H H 8.7548 0.050 1 139 16 16 PHE HA H 3.2708 0.050 1 140 16 16 PHE HB2 H 2.9218 0.050 2 141 16 16 PHE HD1 H 6.5058 0.050 3 142 16 16 PHE HD2 H 6.5058 0.050 3 143 16 16 PHE HE1 H 6.9738 0.050 3 144 16 16 PHE HE2 H 6.9738 0.050 3 145 16 16 PHE C C 174.515 0.400 1 146 16 16 PHE CA C 61.9028 0.400 1 147 16 16 PHE CB C 39.7248 0.400 1 148 16 16 PHE CE1 C 129.482 0.400 3 149 16 16 PHE CE2 C 129.482 0.400 3 150 16 16 PHE N N 118.544 0.400 1 151 17 17 SER H H 8.0948 0.050 1 152 17 17 SER HA H 4.1188 0.050 1 153 17 17 SER HB2 H 4.1028 0.050 2 154 17 17 SER C C 172.086 0.400 1 155 17 17 SER CA C 61.6608 0.400 1 156 17 17 SER CB C 63.2668 0.400 1 157 17 17 SER N N 112.660 0.400 1 158 18 18 LEU H H 7.4048 0.050 1 159 18 18 LEU HA H 3.9878 0.050 1 160 18 18 LEU HB2 H 1.6978 0.050 2 161 18 18 LEU HB3 H 1.4898 0.050 2 162 18 18 LEU HD1 H 0.6838 0.050 2 163 18 18 LEU HD2 H 0.8008 0.050 2 164 18 18 LEU HG H 1.3278 0.050 1 165 18 18 LEU C C 174.982 0.400 1 166 18 18 LEU CB C 41.4138 0.400 1 167 18 18 LEU N N 120.184 0.400 1 168 19 19 PHE H H 7.0848 0.050 1 169 19 19 PHE HA H 3.8578 0.050 1 170 19 19 PHE HB2 H 2.631 0.050 2 171 19 19 PHE HD1 H 7.3118 0.050 3 172 19 19 PHE HD2 H 7.3118 0.050 3 173 19 19 PHE HE1 H 7.2768 0.050 3 174 19 19 PHE HE2 H 7.2768 0.050 3 175 19 19 PHE C C 173.816 0.400 1 176 19 19 PHE CB C 41.4328 0.400 1 177 19 19 PHE CD1 C 128.595 0.400 3 178 19 19 PHE CD2 C 128.595 0.400 3 179 19 19 PHE N N 114.926 0.400 1 180 20 20 ASP H H 7.7588 0.050 1 181 20 20 ASP HA H 4.5518 0.050 1 182 20 20 ASP HB2 H 2.4478 0.050 2 183 20 20 ASP C C 174.355 0.400 1 184 20 20 ASP CB C 39.0518 0.400 1 185 20 20 ASP N N 116.333 0.400 1 186 21 21 LYS H H 7.6578 0.050 1 187 21 21 LYS HA H 3.9788 0.050 1 188 21 21 LYS HB2 H 1.8628 0.050 2 189 21 21 LYS HD2 H 1.8878 0.050 2 190 21 21 LYS HE2 H 2.9678 0.050 2 191 21 21 LYS HG2 H 1.5388 0.050 2 192 21 21 LYS C C 175.352 0.400 1 193 21 21 LYS CA C 58.4158 0.400 1 194 21 21 LYS CB C 32.6218 0.400 1 195 21 21 LYS CD C 28.1138 0.400 1 196 21 21 LYS CE C 41.9438 0.400 1 197 21 21 LYS CG C 24.1018 0.400 1 198 21 21 LYS N N 123.905 0.400 1 199 22 22 ASP H H 8.1708 0.050 1 200 22 22 ASP HA H 4.5878 0.050 1 201 22 22 ASP HB2 H 2.7078 0.050 2 202 22 22 ASP HB3 H 2.2978 0.050 2 203 22 22 ASP C C 174.872 0.400 1 204 22 22 ASP CA C 52.9928 0.400 1 205 22 22 ASP CB C 39.6798 0.400 1 206 22 22 ASP N N 113.617 0.400 1 207 23 23 GLY H H 7.7238 0.050 1 208 23 23 GLY HA2 H 3.8868 0.050 2 209 23 23 GLY HA3 H 3.8808 0.050 2 210 23 23 GLY C C 172.439 0.400 1 211 23 23 GLY CA C 47.3378 0.400 1 212 23 23 GLY N N 108.896 0.400 1 213 24 24 ASP H H 8.4838 0.050 1 214 24 24 ASP HA H 4.4938 0.050 1 215 24 24 ASP HB2 H 3.0608 0.050 2 216 24 24 ASP HB3 H 2.4508 0.050 2 217 24 24 ASP C C 174.627 0.400 1 218 24 24 ASP CA C 53.8208 0.400 1 219 24 24 ASP CB C 40.4658 0.400 1 220 24 24 ASP N N 120.446 0.400 1 221 25 25 GLY H H 10.6268 0.050 1 222 25 25 GLY HA2 H 4.3938 0.050 2 223 25 25 GLY HA3 H 3.7288 0.050 2 224 25 25 GLY C C 170.854 0.400 1 225 25 25 GLY CA C 45.2538 0.400 1 226 25 25 GLY N N 112.712 0.400 1 227 26 26 THR H H 8.2408 0.050 1 228 26 26 THR HA H 5.4288 0.050 1 229 26 26 THR HB H 3.8598 0.050 1 230 26 26 THR HG2 H 1.0698 0.050 1 231 26 26 THR C C 170.112 0.400 1 232 26 26 THR CB C 72.5468 0.400 1 233 26 26 THR CG2 C 21.7198 0.400 1 234 26 26 THR N N 111.977 0.400 1 235 27 27 ILE H H 9.9298 0.050 1 236 27 27 ILE HA H 4.8338 0.050 1 237 27 27 ILE HB H 1.8038 0.050 1 238 27 27 ILE HG12 H 1.2588 0.050 2 239 27 27 ILE HG13 H 0.9878 0.050 2 240 27 27 ILE HG2 H 0.3518 0.050 1 241 27 27 ILE C C 173.259 0.400 1 242 27 27 ILE N N 126.544 0.400 1 243 28 28 THR H H 8.3888 0.050 1 244 28 28 THR HA H 4.8678 0.050 1 245 28 28 THR HB H 4.8228 0.050 1 246 28 28 THR HG2 H 1.2978 0.050 1 247 28 28 THR C C 173.729 0.400 1 248 28 28 THR CA C 59.1738 0.400 1 249 28 28 THR CB C 72.1978 0.400 1 250 28 28 THR N N 115.935 0.400 1 251 29 29 THR H H 9.1708 0.050 1 252 29 29 THR HA H 3.7388 0.050 1 253 29 29 THR HB H 4.1838 0.050 1 254 29 29 THR HG2 H 1.1998 0.050 1 255 29 29 THR C C 174.376 0.400 1 256 29 29 THR CA C 66.4158 0.400 1 257 29 29 THR CB C 68.1808 0.400 1 258 29 29 THR CG2 C 23.4908 0.400 1 259 29 29 THR N N 112.731 0.400 1 260 30 30 LYS H H 7.6038 0.050 1 261 30 30 LYS HA H 4.1078 0.050 1 262 30 30 LYS HB2 H 1.8228 0.050 2 263 30 30 LYS HD2 H 1.6858 0.050 2 264 30 30 LYS HE2 H 2.9798 0.050 2 265 30 30 LYS HG2 H 1.4218 0.050 2 266 30 30 LYS C C 177.096 0.400 1 267 30 30 LYS CA C 59.2648 0.400 1 268 30 30 LYS CB C 32.4218 0.400 1 269 30 30 LYS CD C 28.9608 0.400 1 270 30 30 LYS CE C 41.8798 0.400 1 271 30 30 LYS CG C 24.6968 0.400 1 272 30 30 LYS N N 120.172 0.400 1 273 31 31 GLU H H 7.7168 0.050 1 274 31 31 GLU HA H 4.1198 0.050 1 275 31 31 GLU HB2 H 2.7148 0.050 2 276 31 31 GLU HG2 H 2.4038 0.050 2 277 31 31 GLU C C 176.336 0.400 1 278 31 31 GLU CA C 59.5238 0.400 1 279 31 31 GLU CG C 38.8128 0.400 1 280 31 31 GLU N N 121.065 0.400 1 281 32 32 LEU H H 8.6388 0.050 1 282 32 32 LEU HA H 4.0978 0.050 1 283 32 32 LEU HB2 H 1.8158 0.050 2 284 32 32 LEU HB3 H 1.3948 0.050 2 285 32 32 LEU HD1 H 0.6208 0.050 2 286 32 32 LEU HD2 H 0.6018 0.050 2 287 32 32 LEU HG H 0.5868 0.050 1 288 32 32 LEU C C 176.129 0.400 1 289 32 32 LEU CA C 57.7408 0.400 1 290 32 32 LEU CB C 42.2968 0.400 1 291 32 32 LEU CD1 C 25.8618 0.400 2 292 32 32 LEU CD2 C 23.5738 0.400 2 293 32 32 LEU CG C 25.9618 0.400 1 294 32 32 LEU N N 119.776 0.400 1 295 33 33 GLY H H 8.7038 0.050 1 296 33 33 GLY HA2 H 3.9738 0.050 2 297 33 33 GLY HA3 H 3.5418 0.050 2 298 33 33 GLY C C 172.329 0.400 1 299 33 33 GLY CA C 48.2338 0.400 1 300 33 33 GLY N N 105.213 0.400 1 301 34 34 THR H H 7.9948 0.050 1 302 34 34 THR HA H 3.9408 0.050 1 303 34 34 THR HB H 4.3668 0.050 1 304 34 34 THR HG2 H 1.2878 0.050 1 305 34 34 THR CA C 66.7648 0.400 1 306 34 34 THR CB C 68.6728 0.400 1 307 34 34 THR N N 117.782 0.400 1 308 35 35 VAL H H 7.8458 0.050 1 309 35 35 VAL HA H 3.6148 0.050 1 310 35 35 VAL HB H 2.0888 0.050 1 311 35 35 VAL HG1 H 0.8688 0.050 2 312 35 35 VAL HG2 H 0.5318 0.050 2 313 35 35 VAL C C 176.416 0.400 1 314 35 35 VAL CA C 66.5858 0.400 1 315 35 35 VAL CB C 31.4628 0.400 1 316 35 35 VAL CG2 C 20.5538 0.400 2 317 35 35 VAL N N 121.773 0.400 1 318 36 36 MET H H 8.6078 0.050 1 319 36 36 MET HA H 4.1078 0.050 1 320 36 36 MET HB2 H 1.6478 0.050 2 321 36 36 MET HE H 1.8768 0.050 1 322 36 36 MET HG2 H 2.4908 0.050 2 323 36 36 MET C C 176.427 0.400 1 324 36 36 MET CA C 59.0398 0.400 1 325 36 36 MET CE C 17.4538 0.400 1 326 36 36 MET CG C 32.9598 0.400 1 327 36 36 MET N N 117.819 0.400 1 328 37 37 ARG H H 8.5168 0.050 1 329 37 37 ARG HA H 4.7788 0.050 1 330 37 37 ARG HB2 H 1.9028 0.050 2 331 37 37 ARG HD2 H 3.2908 0.050 2 332 37 37 ARG HD3 H 3.1358 0.050 2 333 37 37 ARG HG2 H 1.8178 0.050 2 334 37 37 ARG C C 178.461 0.400 1 335 37 37 ARG CA C 59.2508 0.400 1 336 37 37 ARG CB C 29.5288 0.400 1 337 37 37 ARG CD C 43.3388 0.400 1 338 37 37 ARG CG C 29.3938 0.400 1 339 37 37 ARG N N 118.513 0.400 1 340 38 38 SER H H 7.9658 0.050 1 341 38 38 SER HA H 4.4128 0.050 1 342 38 38 SER HB2 H 4.0548 0.050 2 343 38 38 SER C C 172.053 0.400 1 344 38 38 SER CA C 61.2398 0.400 1 345 38 38 SER CB C 63.1948 0.400 1 346 38 38 SER N N 118.269 0.400 1 347 39 39 LEU H H 7.4338 0.050 1 348 39 39 LEU HA H 4.4918 0.050 1 349 39 39 LEU HB2 H 1.8358 0.050 2 350 39 39 LEU HD1 H 0.8268 0.050 2 351 39 39 LEU HD2 H 0.8108 0.050 2 352 39 39 LEU HG H 0.8018 0.050 1 353 39 39 LEU C C 174.161 0.400 1 354 39 39 LEU CA C 54.5358 0.400 1 355 39 39 LEU CB C 42.0178 0.400 1 356 39 39 LEU CD1 C 25.6788 0.400 2 357 39 39 LEU CD2 C 22.4138 0.400 2 358 39 39 LEU CG C 25.9148 0.400 1 359 39 39 LEU N N 120.296 0.400 1 360 40 40 GLY H H 7.8938 0.050 1 361 40 40 GLY HA2 H 4.2518 0.050 2 362 40 40 GLY HA3 H 3.7918 0.050 2 363 40 40 GLY C C 171.564 0.400 1 364 40 40 GLY CA C 45.4398 0.400 1 365 40 40 GLY N N 106.425 0.400 1 366 41 41 GLN H H 7.7978 0.050 1 367 41 41 GLN HA H 4.4858 0.050 1 368 41 41 GLN HB2 H 1.6168 0.050 2 369 41 41 GLN HE21 H 7.4098 0.050 2 370 41 41 GLN HE22 H 6.7788 0.050 2 371 41 41 GLN HG2 H 2.1668 0.050 2 372 41 41 GLN HG3 H 2.1138 0.050 2 373 41 41 GLN C C 171.332 0.400 1 374 41 41 GLN CA C 54.4658 0.400 1 375 41 41 GLN CB C 30.6968 0.400 1 376 41 41 GLN CG C 33.5098 0.400 1 377 41 41 GLN N N 117.557 0.400 1 378 41 41 GLN NE2 N 110.556 0.400 1 379 42 42 ASN H H 8.7018 0.050 1 380 42 42 ASN HA H 4.3298 0.050 1 381 42 42 ASN HB2 H 2.6418 0.050 2 382 42 42 ASN HD21 H 7.7668 0.050 2 383 42 42 ASN HD22 H 6.9678 0.050 2 384 42 42 ASN N N 116.151 0.400 1 385 42 42 ASN ND2 N 114.422 0.400 1 386 43 43 PRO HA H 4.7228 0.050 1 387 43 43 PRO HB2 H 1.9038 0.050 2 388 43 43 PRO HD2 H 3.5758 0.050 2 389 43 43 PRO HD3 H 3.2618 0.050 2 390 43 43 PRO HG2 H 1.9418 0.050 2 391 43 43 PRO C C 174.906 0.400 1 392 43 43 PRO CA C 61.9858 0.400 1 393 43 43 PRO CB C 31.9148 0.400 1 394 44 44 THR H H 8.6648 0.050 1 395 44 44 THR HA H 4.4338 0.050 1 396 44 44 THR HB H 4.7188 0.050 1 397 44 44 THR HG2 H 1.4328 0.050 1 398 44 44 THR C C 172.336 0.400 1 399 44 44 THR CA C 60.5658 0.400 1 400 44 44 THR CB C 70.7718 0.400 1 401 44 44 THR N N 112.272 0.400 1 402 45 45 GLU H H 8.8228 0.050 1 403 45 45 GLU HA H 3.9828 0.050 1 404 45 45 GLU HB2 H 1.4588 0.050 2 405 45 45 GLU HG2 H 2.3548 0.050 2 406 45 45 GLU C C 176.176 0.400 1 407 45 45 GLU CA C 59.9988 0.400 1 408 45 45 GLU CB C 29.4078 0.400 1 409 45 45 GLU CG C 36.3798 0.400 1 410 45 45 GLU N N 120.212 0.400 1 411 46 46 ALA H H 8.2698 0.050 1 412 46 46 ALA HA H 4.0878 0.050 1 413 46 46 ALA HB H 1.3958 0.050 1 414 46 46 ALA C C 177.394 0.400 1 415 46 46 ALA CA C 55.0398 0.400 1 416 46 46 ALA CB C 18.1898 0.400 1 417 46 46 ALA N N 120.147 0.400 1 418 47 47 GLU H H 7.6948 0.050 1 419 47 47 GLU HA H 3.9848 0.050 1 420 47 47 GLU HB2 H 1.8868 0.050 2 421 47 47 GLU HG2 H 2.4058 0.050 2 422 47 47 GLU C C 177.405 0.400 1 423 47 47 GLU CA C 58.9238 0.400 1 424 47 47 GLU CB C 28.2468 0.400 1 425 47 47 GLU CG C 33.9888 0.400 1 426 47 47 GLU N N 118.332 0.400 1 427 48 48 LEU H H 8.1268 0.050 1 428 48 48 LEU HA H 4.0138 0.050 1 429 48 48 LEU HB2 H 2.0508 0.050 2 430 48 48 LEU HD1 H 0.7938 0.050 2 431 48 48 LEU HD2 H 0.6978 0.050 2 432 48 48 LEU HG H 1.0458 0.050 1 433 48 48 LEU C C 175.752 0.400 1 434 48 48 LEU CA C 57.8508 0.400 1 435 48 48 LEU CB C 42.1988 0.400 1 436 48 48 LEU CG C 25.8498 0.400 1 437 48 48 LEU N N 119.439 0.400 1 438 49 49 GLN H H 8.2468 0.050 1 439 49 49 GLN HA H 3.8418 0.050 1 440 49 49 GLN HB2 H 1.8108 0.050 2 441 49 49 GLN HE21 H 7.5158 0.050 2 442 49 49 GLN HE22 H 6.9308 0.050 2 443 49 49 GLN HG2 H 2.4358 0.050 2 444 49 49 GLN C C 175.703 0.400 1 445 49 49 GLN CA C 59.1438 0.400 1 446 49 49 GLN CG C 37.2758 0.400 1 447 49 49 GLN N N 117.775 0.400 1 448 49 49 GLN NE2 N 112.455 0.400 1 449 50 50 ASP H H 8.1208 0.050 1 450 50 50 ASP HA H 4.4378 0.050 1 451 50 50 ASP HB2 H 2.8628 0.050 2 452 50 50 ASP CA C 57.1128 0.400 1 453 50 50 ASP CB C 40.0358 0.400 1 454 50 50 ASP N N 119.405 0.400 1 455 51 51 MET H H 7.9218 0.050 1 456 51 51 MET HA H 4.0798 0.050 1 457 51 51 MET HB2 H 1.9378 0.050 2 458 51 51 MET HB3 H 1.6278 0.050 2 459 51 51 MET HE H 1.6978 0.050 1 460 51 51 MET HG2 H 2.4078 0.050 2 461 51 51 MET HG3 H 2.1978 0.050 2 462 51 51 MET N N 118.728 0.400 1 463 52 52 ILE H H 7.5878 0.050 1 464 52 52 ILE HA H 3.7538 0.050 1 465 52 52 ILE HB H 2.0858 0.050 1 466 52 52 ILE HD1 H 0.6988 0.050 1 467 52 52 ILE HG12 H 1.5958 0.050 2 468 52 52 ILE HG13 H 1.2778 0.050 2 469 52 52 ILE HG2 H 0.7698 0.050 1 470 52 52 ILE C C 174.965 0.400 1 471 52 52 ILE CA C 64.1228 0.400 1 472 52 52 ILE CB C 36.377 0.400 1 473 52 52 ILE CD1 C 11.4728 0.400 1 474 52 52 ILE CG2 C 16.2578 0.400 1 475 52 52 ILE N N 117.735 0.400 1 476 53 53 ASN H H 8.7088 0.050 1 477 53 53 ASN HA H 4.4348 0.050 1 478 53 53 ASN HB2 H 2.9978 0.050 2 479 53 53 ASN HB3 H 2.8708 0.050 2 480 53 53 ASN HD21 H 7.8368 0.050 2 481 53 53 ASN HD22 H 6.9718 0.050 2 482 53 53 ASN C C 174.533 0.400 1 483 53 53 ASN CB C 37.9058 0.400 1 484 53 53 ASN N N 117.691 0.400 1 485 53 53 ASN ND2 N 110.953 0.400 1 486 54 54 GLU H H 7.6898 0.050 1 487 54 54 GLU HA H 4.0438 0.050 1 488 54 54 GLU HB2 H 1.8668 0.050 2 489 54 54 GLU HG2 H 2.3468 0.050 2 490 54 54 GLU CA C 58.6148 0.400 1 491 54 54 GLU CG C 35.9758 0.400 1 492 54 54 GLU N N 115.838 0.400 1 493 55 55 VAL H H 7.2148 0.050 1 494 55 55 VAL HA H 4.2588 0.050 1 495 55 55 VAL HB H 2.1608 0.050 1 496 55 55 VAL HG1 H 0.8278 0.050 2 497 55 55 VAL HG2 H 0.8788 0.050 2 498 55 55 VAL C C 172.915 0.400 1 499 55 55 VAL CA C 60.9138 0.400 1 500 55 55 VAL CG1 C 22.5128 0.400 2 501 55 55 VAL CG2 C 20.8048 0.400 2 502 55 55 VAL N N 110.912 0.400 1 503 56 56 ASP H H 7.7608 0.050 1 504 56 56 ASP HA H 4.5098 0.050 1 505 56 56 ASP HB2 H 3.0068 0.050 2 506 56 56 ASP HB3 H 2.7238 0.050 2 507 56 56 ASP C C 173.361 0.400 1 508 56 56 ASP CA C 53.8648 0.400 1 509 56 56 ASP CB C 40.1588 0.400 1 510 56 56 ASP N N 120.629 0.400 1 511 57 57 ALA H H 8.2438 0.050 1 512 57 57 ALA HA H 4.2228 0.050 1 513 57 57 ALA HB H 1.5318 0.050 1 514 57 57 ALA C C 175.842 0.400 1 515 57 57 ALA CA C 54.2908 0.400 1 516 57 57 ALA CB C 19.4558 0.400 1 517 57 57 ALA N N 131.226 0.400 1 518 58 58 ASP H H 8.2578 0.050 1 519 58 58 ASP HA H 4.6198 0.050 1 520 58 58 ASP HB2 H 3.0668 0.050 2 521 58 58 ASP HB3 H 2.6918 0.050 2 522 58 58 ASP C C 175.471 0.400 1 523 58 58 ASP CA C 52.7878 0.400 1 524 58 58 ASP CB C 39.7758 0.400 1 525 58 58 ASP N N 113.496 0.400 1 526 59 59 GLY H H 7.6128 0.050 1 527 59 59 GLY HA2 H 3.8788 0.050 2 528 59 59 GLY HA3 H 3.8278 0.050 2 529 59 59 GLY C C 172.107 0.400 1 530 59 59 GLY CA C 46.9268 0.400 1 531 59 59 GLY N N 108.087 0.400 1 532 60 60 ASN H H 8.1948 0.050 1 533 60 60 ASN HA H 4.6068 0.050 1 534 60 60 ASN HB2 H 3.3368 0.050 2 535 60 60 ASN HB3 H 2.6538 0.050 2 536 60 60 ASN C C 174.007 0.400 1 537 60 60 ASN CB C 37.6628 0.400 1 538 60 60 ASN N N 118.324 0.400 1 539 61 61 GLY H H 10.5728 0.050 1 540 61 61 GLY HA2 H 4.2558 0.050 2 541 61 61 GLY HA3 H 3.4938 0.050 2 542 61 61 GLY C C 170.445 0.400 1 543 61 61 GLY CA C 45.4348 0.400 1 544 61 61 GLY N N 112.871 0.400 1 545 62 62 THR H H 7.6938 0.050 1 546 62 62 THR HA H 4.7958 0.050 1 547 62 62 THR HB H 4.0208 0.050 1 548 62 62 THR HG2 H 1.1598 0.050 1 549 62 62 THR C C 170.378 0.400 1 550 62 62 THR CB C 72.1128 0.400 1 551 62 62 THR CG2 C 22.1088 0.400 1 552 62 62 THR N N 108.099 0.400 1 553 63 63 ILE H H 8.8238 0.050 1 554 63 63 ILE HA H 5.2228 0.050 1 555 63 63 ILE HB H 2.1488 0.050 1 556 63 63 ILE HD1 H 0.3718 0.050 1 557 63 63 ILE HG13 H 0.9158 0.050 2 558 63 63 ILE HG2 H 1.1978 0.050 1 559 63 63 ILE C C 172.687 0.400 1 560 63 63 ILE CA C 58.9958 0.400 1 561 63 63 ILE CD1 C 15.3698 0.400 1 562 63 63 ILE CG1 C 27.365 0.400 1 563 63 63 ILE CG2 C 18.3588 0.400 1 564 63 63 ILE N N 123.323 0.400 1 565 64 64 ASP H H 8.8928 0.050 1 566 64 64 ASP HA H 5.4908 0.050 1 567 64 64 ASP HB2 H 3.1518 0.050 2 568 64 64 ASP HB3 H 2.8708 0.050 2 569 64 64 ASP C C 173.494 0.400 1 570 64 64 ASP CA C 51.8118 0.400 1 571 64 64 ASP CB C 42.2468 0.400 1 572 64 64 ASP N N 127.718 0.400 1 573 65 65 PHE H H 8.9878 0.050 1 574 65 65 PHE HA H 3.7838 0.050 1 575 65 65 PHE HB2 H 2.8208 0.050 2 576 65 65 PHE HB3 H 2.0848 0.050 2 577 65 65 PHE HD1 H 6.7628 0.050 3 578 65 65 PHE HD2 H 6.7628 0.050 3 579 65 65 PHE HE1 H 7.2108 0.050 3 580 65 65 PHE HE2 H 7.2108 0.050 3 581 65 65 PHE CB C 35.6308 0.400 1 582 65 65 PHE CD1 C 129.971 0.400 3 583 65 65 PHE CD2 C 129.971 0.400 3 584 65 65 PHE CE1 C 128.531 0.400 3 585 65 65 PHE CE2 C 128.531 0.400 3 586 65 65 PHE N N 118.282 0.400 1 587 66 66 PRO HA H 3.8528 0.050 1 588 66 66 PRO HB2 H 2.1578 0.050 2 589 66 66 PRO HB3 H 1.8038 0.050 2 590 66 66 PRO HD2 H 3.7078 0.050 2 591 66 66 PRO HG2 H 1.3648 0.050 2 592 67 67 GLU H H 8.1738 0.050 1 593 67 67 GLU HA H 4.4498 0.050 1 594 67 67 GLU HB2 H 1.7678 0.050 1 595 67 67 GLU HB3 H 1.7678 0.050 1 596 67 67 GLU HG2 H 2.6078 0.050 1 597 67 67 GLU HG3 H 2.2878 0.050 1 598 67 67 GLU N N 116.980 0.400 1 599 68 68 PHE H H 8.6708 0.050 1 600 68 68 PHE HA H 3.6278 0.050 1 601 68 68 PHE HB2 H 3.1278 0.050 2 602 68 68 PHE HB3 H 2.8278 0.050 2 603 68 68 PHE HD1 H 6.9108 0.050 3 604 68 68 PHE HD2 H 6.9108 0.050 3 605 68 68 PHE HE1 H 7.1818 0.050 3 606 68 68 PHE HE2 H 7.1818 0.050 3 607 68 68 PHE CD1 C 129.642 0.400 3 608 68 68 PHE CD2 C 129.642 0.400 3 609 68 68 PHE CE1 C 129.082 0.400 3 610 68 68 PHE CE2 C 129.082 0.400 3 611 68 68 PHE N N 122.872 0.400 1 612 69 69 LEU H H 8.6748 0.050 1 613 69 69 LEU HA H 3.9398 0.050 1 614 69 69 LEU HB2 H 1.3058 0.050 2 615 69 69 LEU HD1 H 0.8388 0.050 2 616 69 69 LEU HD2 H 0.0638 0.050 2 617 69 69 LEU HG H 0.6778 0.050 1 618 69 69 LEU CB C 38.6428 0.400 1 619 69 69 LEU CD1 C 25.5958 0.400 2 620 69 69 LEU N N 119.155 0.400 1 621 70 70 THR H H 7.5458 0.050 1 622 70 70 THR HA H 3.4478 0.050 1 623 70 70 THR HB H 4.1948 0.050 1 624 70 70 THR HG2 H 1.2488 0.050 1 625 70 70 THR CB C 67.8278 0.400 1 626 70 70 THR N N 114.017 0.400 1 627 71 71 MET H H 7.6178 0.050 1 628 71 71 MET HA H 3.4178 0.050 1 629 71 71 MET HB2 H 1.7678 0.050 2 630 71 71 MET HE H 1.3978 0.050 1 631 71 71 MET HG2 H 2.0978 0.050 2 632 71 71 MET N N 119.160 0.400 1 633 72 72 MET H H 8.1888 0.050 1 634 72 72 MET HA H 3.6478 0.050 1 635 72 72 MET HB2 H 1.0678 0.050 2 636 72 72 MET HB3 H 0.9978 0.050 2 637 72 72 MET HG2 H 1.4578 0.050 2 638 72 72 MET HG3 H 1.3778 0.050 2 639 72 72 MET C C 175.697 0.400 1 640 72 72 MET CA C 60.0268 0.400 1 641 72 72 MET CG C 31.9708 0.400 1 642 72 72 MET N N 115.879 0.400 1 643 73 73 ALA H H 7.8968 0.050 1 644 73 73 ALA HA H 4.0248 0.050 1 645 73 73 ALA HB H 1.3728 0.050 1 646 73 73 ALA C C 177.075 0.400 1 647 73 73 ALA CB C 18.2718 0.400 1 648 73 73 ALA N N 120.060 0.400 1 649 74 74 ARG H H 7.4768 0.050 1 650 74 74 ARG HA H 3.7378 0.050 1 651 74 74 ARG HB2 H 1.4878 0.050 2 652 74 74 ARG HB3 H 1.3178 0.050 2 653 74 74 ARG HD2 H 2.7378 0.050 2 654 74 74 ARG HG2 H 1.0778 0.050 2 655 74 74 ARG C C 175.040 0.400 1 656 74 74 ARG CD C 43.7328 0.400 1 657 74 74 ARG CG C 27.3618 0.400 1 658 74 74 ARG N N 116.115 0.400 1 659 75 75 LYS H H 7.7728 0.050 1 660 75 75 LYS HA H 3.9348 0.050 1 661 75 75 LYS HB2 H 1.8288 0.050 2 662 75 75 LYS HD2 H 1.6878 0.050 2 663 75 75 LYS HE2 H 3.5488 0.050 2 664 75 75 LYS HG2 H 1.4908 0.050 2 665 75 75 LYS C C 174.877 0.400 1 666 75 75 LYS CE C 40.7878 0.400 1 667 75 75 LYS N N 118.389 0.400 1 668 76 76 MET H H 7.9748 0.050 1 669 76 76 MET HA H 4.3438 0.050 1 670 76 76 MET HB2 H 2.1528 0.050 2 671 76 76 MET HB3 H 2.1098 0.050 2 672 76 76 MET HE H 2.0868 0.050 1 673 76 76 MET HG2 H 2.6608 0.050 2 674 76 76 MET HG3 H 2.6188 0.050 2 675 76 76 MET C C 173.683 0.400 1 676 76 76 MET CA C 56.4598 0.400 1 677 76 76 MET CE C 17.0608 0.400 1 678 76 76 MET CG C 32.1808 0.400 1 679 76 76 MET N N 117.535 0.400 1 680 77 77 LYS H H 7.7548 0.050 1 681 77 77 LYS HA H 4.2988 0.050 1 682 77 77 LYS HB2 H 1.8628 0.050 2 683 77 77 LYS HB3 H 1.8208 0.050 2 684 77 77 LYS HD2 H 1.6868 0.050 2 685 77 77 LYS HE2 H 2.9838 0.050 2 686 77 77 LYS HG2 H 1.4828 0.050 2 687 77 77 LYS C C 173.704 0.400 1 688 77 77 LYS CA C 56.8018 0.400 1 689 77 77 LYS CB C 32.7798 0.400 1 690 77 77 LYS CD C 28.8688 0.400 1 691 77 77 LYS CE C 41.9038 0.400 1 692 77 77 LYS CG C 24.5088 0.400 1 693 77 77 LYS N N 119.562 0.400 1 694 78 78 ASP H H 8.1648 0.050 1 695 78 78 ASP HA H 4.7048 0.050 1 696 78 78 ASP HB2 H 2.8028 0.050 2 697 78 78 ASP HB3 H 2.7438 0.050 2 698 78 78 ASP C C 173.716 0.400 1 699 78 78 ASP CA C 54.3988 0.400 1 700 78 78 ASP CB C 40.8618 0.400 1 701 78 78 ASP N N 120.459 0.400 1 702 79 79 THR H H 8.0398 0.050 1 703 79 79 THR HA H 4.3208 0.050 1 704 79 79 THR HB H 4.2538 0.050 1 705 79 79 THR HG2 H 1.2238 0.050 1 706 79 79 THR C C 171.541 0.400 1 707 79 79 THR CA C 62.1658 0.400 1 708 79 79 THR CB C 69.7638 0.400 1 709 79 79 THR CG2 C 21.4248 0.400 1 710 79 79 THR N N 113.759 0.400 1 711 80 80 ASP H H 8.4268 0.050 1 712 80 80 ASP HA H 4.7098 0.050 1 713 80 80 ASP HB2 H 2.7928 0.050 2 714 80 80 ASP C C 173.897 0.400 1 715 80 80 ASP CA C 54.4298 0.400 1 716 80 80 ASP CB C 40.9508 0.400 1 717 80 80 ASP N N 122.666 0.400 1 718 81 81 SER H H 8.4558 0.050 1 719 81 81 SER HA H 4.4138 0.050 1 720 81 81 SER HB2 H 3.9998 0.050 2 721 81 81 SER C C 172.788 0.400 1 722 81 81 SER CA C 59.4528 0.400 1 723 81 81 SER CB C 63.0578 0.400 1 724 81 81 SER N N 117.057 0.400 1 725 82 82 GLU H H 8.5098 0.050 1 726 82 82 GLU HA H 4.1568 0.050 1 727 82 82 GLU HB2 H 2.1328 0.050 2 728 82 82 GLU HG2 H 2.3588 0.050 2 729 82 82 GLU C C 175.133 0.400 1 730 82 82 GLU CA C 58.6118 0.400 1 731 82 82 GLU CB C 29.7828 0.400 1 732 82 82 GLU CG C 36.6058 0.400 1 733 82 82 GLU N N 122.235 0.400 1 734 83 83 GLU H H 8.2248 0.050 1 735 83 83 GLU HA H 4.1048 0.050 1 736 83 83 GLU HB2 H 2.0948 0.050 2 737 83 83 GLU HG2 H 2.3658 0.050 2 738 83 83 GLU C C 176.436 0.400 1 739 83 83 GLU CA C 59.2618 0.400 1 740 83 83 GLU CB C 29.5468 0.400 1 741 83 83 GLU CG C 35.8858 0.400 1 742 83 83 GLU N N 119.203 0.400 1 743 84 84 GLU H H 8.1158 0.050 1 744 84 84 GLU HA H 4.1448 0.050 1 745 84 84 GLU HB2 H 2.1508 0.050 2 746 84 84 GLU HG2 H 2.4798 0.050 2 747 84 84 GLU HG3 H 2.3118 0.050 2 748 84 84 GLU C C 177.343 0.400 1 749 84 84 GLU CA C 59.6828 0.400 1 750 84 84 GLU CB C 30.3448 0.400 1 751 84 84 GLU CG C 36.2148 0.400 1 752 84 84 GLU N N 117.902 0.400 1 753 85 85 ILE H H 8.0018 0.050 1 754 85 85 ILE HA H 4.0898 0.050 1 755 85 85 ILE HB H 2.2168 0.050 1 756 85 85 ILE HD1 H 0.7028 0.050 1 757 85 85 ILE HG12 H 1.9488 0.050 2 758 85 85 ILE HG13 H 0.9628 0.050 2 759 85 85 ILE HG2 H 1.1078 0.050 1 760 85 85 ILE C C 174.656 0.400 1 761 85 85 ILE CA C 65.6048 0.400 1 762 85 85 ILE CB C 37.4178 0.400 1 763 85 85 ILE CD1 C 13.3228 0.400 1 764 85 85 ILE CG1 C 29.7868 0.400 1 765 85 85 ILE CG2 C 18.5638 0.400 1 766 85 85 ILE N N 119.580 0.400 1 767 86 86 ARG H H 8.3748 0.050 1 768 86 86 ARG HA H 4.1548 0.050 1 769 86 86 ARG HB2 H 2.0668 0.050 2 770 86 86 ARG HB3 H 1.8628 0.050 2 771 86 86 ARG HD2 H 2.9658 0.050 2 772 86 86 ARG HG2 H 1.6538 0.050 2 773 86 86 ARG HG3 H 1.5228 0.050 2 774 86 86 ARG CA C 60.3318 0.400 1 775 86 86 ARG CB C 29.9378 0.400 1 776 86 86 ARG CD C 42.9598 0.400 1 777 86 86 ARG CG C 27.3348 0.400 1 778 86 86 ARG N N 121.213 0.400 1 779 87 87 GLU H H 8.3608 0.050 1 780 87 87 GLU HA H 4.0938 0.050 1 781 87 87 GLU HB2 H 2.0958 0.050 2 782 87 87 GLU HG2 H 2.3498 0.050 2 783 87 87 GLU CA C 59.2028 0.400 1 784 87 87 GLU CB C 29.6808 0.400 1 785 87 87 GLU CG C 36.2078 0.400 1 786 87 87 GLU N N 117.579 0.400 1 787 88 88 ALA H H 8.3528 0.050 1 788 88 88 ALA HA H 4.1738 0.050 1 789 88 88 ALA HB H 1.9338 0.050 1 790 88 88 ALA C C 176.595 0.400 1 791 88 88 ALA CA C 54.9348 0.400 1 792 88 88 ALA CB C 18.5808 0.400 1 793 88 88 ALA N N 120.095 0.400 1 794 89 89 PHE H H 8.8348 0.050 1 795 89 89 PHE HA H 3.3128 0.050 1 796 89 89 PHE HB2 H 3.0008 0.050 2 797 89 89 PHE HD1 H 6.5598 0.050 3 798 89 89 PHE HD2 H 6.5598 0.050 3 799 89 89 PHE HE1 H 7.0808 0.050 3 800 89 89 PHE HE2 H 7.0808 0.050 3 801 89 89 PHE HZ H 7.2848 0.050 1 802 89 89 PHE C C 173.566 0.400 1 803 89 89 PHE CA C 61.8048 0.400 1 804 89 89 PHE CB C 38.9878 0.400 1 805 89 89 PHE CE1 C 126.947 0.400 3 806 89 89 PHE CE2 C 126.947 0.400 3 807 89 89 PHE N N 118.860 0.400 1 808 90 90 ARG H H 7.6278 0.050 1 809 90 90 ARG HA H 3.9408 0.050 1 810 90 90 ARG HB2 H 1.9898 0.050 2 811 90 90 ARG HB3 H 1.9528 0.050 2 812 90 90 ARG HD2 H 3.2628 0.050 2 813 90 90 ARG HG2 H 1.9688 0.050 2 814 90 90 ARG HG3 H 1.7988 0.050 2 815 90 90 ARG C C 174.665 0.400 1 816 90 90 ARG CA C 58.3618 0.400 1 817 90 90 ARG CB C 30.3938 0.400 1 818 90 90 ARG CD C 43.3538 0.400 1 819 90 90 ARG CG C 27.8308 0.400 1 820 90 90 ARG N N 114.460 0.400 1 821 91 91 VAL H H 7.4118 0.050 1 822 91 91 VAL HA H 3.5488 0.050 1 823 91 91 VAL HB H 2.2488 0.050 1 824 91 91 VAL HG1 H 1.0318 0.050 2 825 91 91 VAL HG2 H 0.7098 0.050 2 826 91 91 VAL C C 174.176 0.400 1 827 91 91 VAL CA C 65.6048 0.400 1 828 91 91 VAL CB C 31.0978 0.400 1 829 91 91 VAL CG1 C 22.5558 0.400 2 830 91 91 VAL CG2 C 20.9048 0.400 2 831 91 91 VAL N N 117.632 0.400 1 832 92 92 PHE H H 7.2058 0.050 1 833 92 92 PHE HA H 4.1938 0.050 1 834 92 92 PHE HB2 H 2.7418 0.050 2 835 92 92 PHE HD1 H 7.5308 0.050 3 836 92 92 PHE HD2 H 7.5308 0.050 3 837 92 92 PHE HE1 H 7.2868 0.050 3 838 92 92 PHE HE2 H 7.2868 0.050 3 839 92 92 PHE C C 173.432 0.400 1 840 92 92 PHE CA C 60.5698 0.400 1 841 92 92 PHE CB C 41.0488 0.400 1 842 92 92 PHE CD1 C 130.697 0.400 3 843 92 92 PHE CD2 C 130.697 0.400 3 844 92 92 PHE CE1 C 129.847 0.400 3 845 92 92 PHE CE2 C 129.847 0.400 3 846 92 92 PHE N N 114.928 0.400 1 847 93 93 ASP H H 7.8908 0.050 1 848 93 93 ASP HA H 4.5588 0.050 1 849 93 93 ASP HB2 H 2.2178 0.050 2 850 93 93 ASP C C 174.487 0.400 1 851 93 93 ASP CA C 52.4208 0.400 1 852 93 93 ASP CB C 38.8108 0.400 1 853 93 93 ASP N N 114.746 0.400 1 854 94 94 LYS H H 7.4178 0.050 1 855 94 94 LYS HA H 3.8858 0.050 1 856 94 94 LYS HB2 H 1.8608 0.050 2 857 94 94 LYS HD2 H 1.6468 0.050 2 858 94 94 LYS HD3 H 1.4968 0.050 2 859 94 94 LYS HE2 H 2.8508 0.050 2 860 94 94 LYS HG2 H 1.5198 0.050 2 861 94 94 LYS HG3 H 1.4738 0.050 2 862 94 94 LYS C C 175.567 0.400 1 863 94 94 LYS CA C 59.3298 0.400 1 864 94 94 LYS CB C 32.5108 0.400 1 865 94 94 LYS CD C 28.2778 0.400 1 866 94 94 LYS CE C 41.5298 0.400 1 867 94 94 LYS CG C 23.7708 0.400 1 868 94 94 LYS N N 124.290 0.400 1 869 95 95 ASP H H 8.4428 0.050 1 870 95 95 ASP HA H 4.5038 0.050 1 871 95 95 ASP HB2 H 2.6828 0.050 2 872 95 95 ASP HB3 H 2.1948 0.050 2 873 95 95 ASP C C 175.057 0.400 1 874 95 95 ASP CA C 53.9748 0.400 1 875 95 95 ASP CB C 39.9358 0.400 1 876 95 95 ASP N N 113.716 0.400 1 877 96 96 GLY H H 7.9008 0.050 1 878 96 96 GLY HA2 H 3.9218 0.050 2 879 96 96 GLY HA3 H 3.8578 0.050 2 880 96 96 GLY C C 172.324 0.400 1 881 96 96 GLY CA C 46.9648 0.400 1 882 96 96 GLY N N 109.038 0.400 1 883 97 97 ASN H H 8.4328 0.050 1 884 97 97 ASN HA H 4.6208 0.050 1 885 97 97 ASN HB2 H 3.3158 0.050 2 886 97 97 ASN HB3 H 2.6908 0.050 2 887 97 97 ASN HD21 H 8.0918 0.050 2 888 97 97 ASN HD22 H 7.4058 0.050 2 889 97 97 ASN C C 173.111 0.400 1 890 97 97 ASN CA C 51.9718 0.400 1 891 97 97 ASN CB C 37.3228 0.400 1 892 97 97 ASN N N 119.490 0.400 1 893 97 97 ASN ND2 N 116.123 0.400 1 894 98 98 GLY H H 10.7648 0.050 1 895 98 98 GLY HA2 H 4.0968 0.050 2 896 98 98 GLY HA3 H 3.4538 0.050 2 897 98 98 GLY C C 169.922 0.400 1 898 98 98 GLY CA C 44.6868 0.400 1 899 98 98 GLY N N 112.415 0.400 1 900 99 99 TYR H H 7.6948 0.050 1 901 99 99 TYR HA H 5.0578 0.050 1 902 99 99 TYR HB2 H 2.5608 0.050 2 903 99 99 TYR HB3 H 2.5378 0.050 2 904 99 99 TYR HD1 H 6.7708 0.050 3 905 99 99 TYR HD2 H 6.7708 0.050 3 906 99 99 TYR HE1 H 6.9438 0.050 3 907 99 99 TYR HE2 H 6.9438 0.050 3 908 99 99 TYR C C 171.883 0.400 1 909 99 99 TYR CA C 55.7868 0.400 1 910 99 99 TYR CB C 42.7778 0.400 1 911 99 99 TYR CD1 C 131.470 0.400 3 912 99 99 TYR CD2 C 131.470 0.400 3 913 99 99 TYR CE1 C 116.395 0.400 3 914 99 99 TYR CE2 C 116.395 0.400 3 915 99 99 TYR N N 115.788 0.400 1 916 100 100 ILE H H 10.2758 0.050 1 917 100 100 ILE HA H 4.7148 0.050 1 918 100 100 ILE HB H 1.9998 0.050 1 919 100 100 ILE HD1 H 0.6218 0.050 1 920 100 100 ILE HG12 H 1.5078 0.050 2 921 100 100 ILE HG13 H 0.6148 0.050 2 922 100 100 ILE HG2 H 1.1548 0.050 1 923 100 100 ILE C C 172.814 0.400 1 924 100 100 ILE CA C 61.4788 0.400 1 925 100 100 ILE CB C 39.6218 0.400 1 926 100 100 ILE CD1 C 16.1228 0.400 1 927 100 100 ILE CG1 C 26.7908 0.400 1 928 100 100 ILE CG2 C 17.5398 0.400 1 929 100 100 ILE N N 126.892 0.400 1 930 101 101 SER H H 8.9958 0.050 1 931 101 101 SER HA H 5.0128 0.050 1 932 101 101 SER HB2 H 4.0118 0.050 2 933 101 101 SER C C 172.611 0.400 1 934 101 101 SER CA C 55.3568 0.400 1 935 101 101 SER CB C 66.6608 0.400 1 936 101 101 SER N N 123.234 0.400 1 937 102 102 ALA H H 9.3348 0.050 1 938 102 102 ALA HA H 3.9268 0.050 1 939 102 102 ALA HB H 1.5048 0.050 1 940 102 102 ALA C C 176.445 0.400 1 941 102 102 ALA CA C 55.9148 0.400 1 942 102 102 ALA CB C 17.7798 0.400 1 943 102 102 ALA N N 122.755 0.400 1 944 103 103 ALA H H 8.3158 0.050 1 945 103 103 ALA HA H 4.0298 0.050 1 946 103 103 ALA HB H 1.4298 0.050 1 947 103 103 ALA C C 178.770 0.400 1 948 103 103 ALA CA C 54.8718 0.400 1 949 103 103 ALA CB C 18.3008 0.400 1 950 103 103 ALA N N 118.198 0.400 1 951 104 104 GLU H H 7.9448 0.050 1 952 104 104 GLU HA H 4.0258 0.050 1 953 104 104 GLU HB2 H 1.8718 0.050 2 954 104 104 GLU HG2 H 2.6128 0.050 2 955 104 104 GLU C C 176.136 0.400 1 956 104 104 GLU CA C 59.0858 0.400 1 957 104 104 GLU CG C 37.9988 0.400 1 958 104 104 GLU N N 119.337 0.400 1 959 105 105 LEU H H 8.6268 0.050 1 960 105 105 LEU HA H 4.1598 0.050 1 961 105 105 LEU HB2 H 1.9418 0.050 2 962 105 105 LEU HD1 H 0.7698 0.050 2 963 105 105 LEU HD2 H 0.7538 0.050 2 964 105 105 LEU HG H 1.5638 0.050 1 965 105 105 LEU C C 175.538 0.400 1 966 105 105 LEU CA C 57.9358 0.400 1 967 105 105 LEU CB C 42.1528 0.400 1 968 105 105 LEU CD1 C 23.8488 0.400 2 969 105 105 LEU CD2 C 23.777 0.400 2 970 105 105 LEU CG C 26.6848 0.400 1 971 105 105 LEU N N 120.144 0.400 1 972 106 106 ARG H H 8.7128 0.050 1 973 106 106 ARG HA H 3.8018 0.050 1 974 106 106 ARG HB2 H 1.9498 0.050 2 975 106 106 ARG HB3 H 1.7308 0.050 2 976 106 106 ARG HD2 H 3.2588 0.050 2 977 106 106 ARG HD3 H 3.1358 0.050 2 978 106 106 ARG HG2 H 1.6418 0.050 2 979 106 106 ARG C C 175.898 0.400 1 980 106 106 ARG CA C 59.8628 0.400 1 981 106 106 ARG CB C 30.0268 0.400 1 982 106 106 ARG CD C 43.4158 0.400 1 983 106 106 ARG CG C 27.4768 0.400 1 984 106 106 ARG N N 117.740 0.400 1 985 107 107 HIS H H 7.8868 0.050 1 986 107 107 HIS HA H 4.3998 0.050 1 987 107 107 HIS HB2 H 3.4228 0.050 2 988 107 107 HIS HB3 H 3.3728 0.050 2 989 107 107 HIS HD2 H 7.2578 0.050 1 990 107 107 HIS HE1 H 8.5098 0.050 1 991 107 107 HIS C C 175.029 0.400 1 992 107 107 HIS CA C 59.0188 0.400 1 993 107 107 HIS CB C 28.6158 0.400 1 994 107 107 HIS CD2 C 118.538 0.400 1 995 107 107 HIS CE1 C 134.929 0.400 1 996 107 107 HIS N N 117.720 0.400 1 997 108 108 VAL H H 8.4398 0.050 1 998 108 108 VAL HA H 3.5928 0.050 1 999 108 108 VAL HB H 2.0938 0.050 1 1000 108 108 VAL HG1 H 1.0148 0.050 2 1001 108 108 VAL HG2 H 0.4988 0.050 2 1002 108 108 VAL C C 175.248 0.400 1 1003 108 108 VAL CA C 66.5638 0.400 1 1004 108 108 VAL CB C 31.5708 0.400 1 1005 108 108 VAL CG1 C 23.7288 0.400 2 1006 108 108 VAL CG2 C 20.5588 0.400 2 1007 108 108 VAL N N 119.959 0.400 1 1008 109 109 MET H H 8.4358 0.050 1 1009 109 109 MET HA H 4.2358 0.050 1 1010 109 109 MET HB2 H 2.3128 0.050 2 1011 109 109 MET HE H 1.8318 0.050 1 1012 109 109 MET HG2 H 2.7948 0.050 2 1013 109 109 MET HG3 H 2.3318 0.050 2 1014 109 109 MET C C 176.437 0.400 1 1015 109 109 MET CA C 57.3908 0.400 1 1016 109 109 MET CB C 29.5328 0.400 1 1017 109 109 MET CE C 16.9208 0.400 1 1018 109 109 MET CG C 32.3898 0.400 1 1019 109 109 MET N N 115.295 0.400 1 1020 110 110 THR H H 8.1258 0.050 1 1021 110 110 THR HA H 4.0568 0.050 1 1022 110 110 THR HB H 4.2578 0.050 1 1023 110 110 THR HG2 H 1.2748 0.050 1 1024 110 110 THR C C 175.497 0.400 1 1025 110 110 THR CA C 66.5808 0.400 1 1026 110 110 THR CB C 68.5218 0.400 1 1027 110 110 THR CG2 C 21.3928 0.400 1 1028 110 110 THR N N 115.318 0.400 1 1029 111 111 ASN H H 7.9988 0.050 1 1030 111 111 ASN HA H 4.4508 0.050 1 1031 111 111 ASN HB2 H 2.7928 0.050 2 1032 111 111 ASN HD21 H 7.5168 0.050 2 1033 111 111 ASN HD22 H 6.7198 0.050 2 1034 111 111 ASN CA C 55.8368 0.400 1 1035 111 111 ASN CB C 37.9678 0.400 1 1036 111 111 ASN N N 122.630 0.400 1 1037 111 111 ASN ND2 N 111.625 0.400 1 1038 112 112 LEU H H 7.9058 0.050 1 1039 112 112 LEU HA H 4.3308 0.050 1 1040 112 112 LEU HB2 H 1.9378 0.050 2 1041 112 112 LEU HB3 H 1.6348 0.050 2 1042 112 112 LEU HD1 H 0.8158 0.050 2 1043 112 112 LEU HD2 H 0.7718 0.050 2 1044 112 112 LEU HG H 1.6608 0.050 1 1045 112 112 LEU C C 174.584 0.400 1 1046 112 112 LEU CA C 54.8318 0.400 1 1047 112 112 LEU CB C 42.5438 0.400 1 1048 112 112 LEU CD1 C 25.9018 0.400 2 1049 112 112 LEU CD2 C 22.0388 0.400 2 1050 112 112 LEU CG C 26.2718 0.400 1 1051 112 112 LEU N N 117.455 0.400 1 1052 113 113 GLY H H 7.9138 0.050 1 1053 113 113 GLY HA2 H 4.1398 0.050 2 1054 113 113 GLY HA3 H 3.7798 0.050 2 1055 113 113 GLY C C 171.823 0.400 1 1056 113 113 GLY CA C 45.5118 0.400 1 1057 113 113 GLY N N 107.043 0.400 1 1058 114 114 GLU H H 7.8588 0.050 1 1059 114 114 GLU HA H 4.3238 0.050 1 1060 114 114 GLU HB2 H 1.7328 0.050 2 1061 114 114 GLU HG2 H 2.1188 0.050 2 1062 114 114 GLU HG3 H 1.9848 0.050 2 1063 114 114 GLU C C 172.814 0.400 1 1064 114 114 GLU CA C 55.1648 0.400 1 1065 114 114 GLU CB C 30.5298 0.400 1 1066 114 114 GLU CG C 35.2058 0.400 1 1067 114 114 GLU N N 119.028 0.400 1 1068 115 115 LYS H H 8.6538 0.050 1 1069 115 115 LYS HA H 4.3778 0.050 1 1070 115 115 LYS HB2 H 1.7448 0.050 2 1071 115 115 LYS HB3 H 1.6408 0.050 2 1072 115 115 LYS HD2 H 1.6378 0.050 2 1073 115 115 LYS HE2 H 2.9508 0.050 2 1074 115 115 LYS HG2 H 1.2958 0.050 2 1075 115 115 LYS C C 172.455 0.400 1 1076 115 115 LYS CA C 55.2348 0.400 1 1077 115 115 LYS CB C 31.7618 0.400 1 1078 115 115 LYS CD C 28.8418 0.400 1 1079 115 115 LYS CE C 41.4828 0.400 1 1080 115 115 LYS CG C 24.3778 0.400 1 1081 115 115 LYS N N 123.982 0.400 1 1082 116 116 LEU H H 8.0528 0.050 1 1083 116 116 LEU HA H 4.6688 0.050 1 1084 116 116 LEU HB2 H 1.5498 0.050 2 1085 116 116 LEU HB3 H 1.3748 0.050 2 1086 116 116 LEU HD1 H 0.6908 0.050 2 1087 116 116 LEU HD2 H 0.6898 0.050 2 1088 116 116 LEU HG H 0.6798 0.050 1 1089 116 116 LEU C C 175.378 0.400 1 1090 116 116 LEU CA C 54.1328 0.400 1 1091 116 116 LEU CB C 44.1758 0.400 1 1092 116 116 LEU CD1 C 24.0658 0.400 2 1093 116 116 LEU CD2 C 23.7548 0.400 2 1094 116 116 LEU CG C 26.9828 0.400 1 1095 116 116 LEU N N 124.274 0.400 1 1096 117 117 THR H H 9.1258 0.050 1 1097 117 117 THR HA H 4.4238 0.050 1 1098 117 117 THR HB H 4.7248 0.050 1 1099 117 117 THR HG2 H 1.3388 0.050 1 1100 117 117 THR CA C 60.9128 0.400 1 1101 117 117 THR CB C 70.9388 0.400 1 1102 117 117 THR CG2 C 21.5258 0.400 1 1103 117 117 THR N N 113.635 0.400 1 1104 118 118 ASP H H 8.9128 0.050 1 1105 118 118 ASP HA H 4.2238 0.050 1 1106 118 118 ASP HB2 H 3.0378 0.050 2 1107 118 118 ASP HB3 H 2.6168 0.050 2 1108 118 118 ASP C C 175.917 0.400 1 1109 118 118 ASP CA C 57.6808 0.400 1 1110 118 118 ASP CB C 39.5228 0.400 1 1111 118 118 ASP N N 120.870 0.400 1 1112 119 119 GLU H H 8.6268 0.050 1 1113 119 119 GLU HA H 4.1258 0.050 1 1114 119 119 GLU HB2 H 2.3388 0.050 2 1115 119 119 GLU HB3 H 2.0548 0.050 2 1116 119 119 GLU HG2 H 2.3498 0.050 2 1117 119 119 GLU C C 176.438 0.400 1 1118 119 119 GLU CA C 59.7978 0.400 1 1119 119 119 GLU CB C 28.7848 0.400 1 1120 119 119 GLU CG C 35.8818 0.400 1 1121 119 119 GLU N N 118.815 0.400 1 1122 120 120 GLU H H 7.7748 0.050 1 1123 120 120 GLU HA H 3.9208 0.050 1 1124 120 120 GLU HB2 H 2.1208 0.050 2 1125 120 120 GLU HG2 H 2.3668 0.050 2 1126 120 120 GLU C C 176.259 0.400 1 1127 120 120 GLU CA C 59.5158 0.400 1 1128 120 120 GLU CB C 30.8308 0.400 1 1129 120 120 GLU CG C 38.2848 0.400 1 1130 120 120 GLU N N 120.193 0.400 1 1131 121 121 VAL H H 8.0268 0.050 1 1132 121 121 VAL HA H 3.5098 0.050 1 1133 121 121 VAL HB H 2.1848 0.050 1 1134 121 121 VAL HG1 H 0.8808 0.050 2 1135 121 121 VAL HG2 H 0.9418 0.050 2 1136 121 121 VAL C C 175.276 0.400 1 1137 121 121 VAL CA C 66.8298 0.400 1 1138 121 121 VAL CB C 31.1878 0.400 1 1139 121 121 VAL CG1 C 23.3228 0.400 2 1140 121 121 VAL CG2 C 21.8348 0.400 2 1141 121 121 VAL N N 121.619 0.400 1 1142 122 122 ASP H H 8.1848 0.050 1 1143 122 122 ASP HA H 4.3648 0.050 1 1144 122 122 ASP HB2 H 2.7908 0.050 2 1145 122 122 ASP HB3 H 2.6998 0.050 2 1146 122 122 ASP C C 176.327 0.400 1 1147 122 122 ASP CA C 57.5188 0.400 1 1148 122 122 ASP CB C 40.0848 0.400 1 1149 122 122 ASP N N 119.587 0.400 1 1150 123 123 GLU H H 8.1898 0.050 1 1151 123 123 GLU HA H 3.9668 0.050 1 1152 123 123 GLU HB2 H 2.2938 0.050 2 1153 123 123 GLU HG2 H 2.4258 0.050 2 1154 123 123 GLU C C 175.641 0.400 1 1155 123 123 GLU CA C 59.3828 0.400 1 1156 123 123 GLU CB C 30.1128 0.400 1 1157 123 123 GLU CG C 36.4218 0.400 1 1158 123 123 GLU N N 119.238 0.400 1 1159 124 124 MET H H 7.7708 0.050 1 1160 124 124 MET HA H 3.9128 0.050 1 1161 124 124 MET HB2 H 1.8458 0.050 2 1162 124 124 MET HE H 0.6608 0.050 1 1163 124 124 MET HG2 H 2.7888 0.050 2 1164 124 124 MET C C 177.098 0.400 1 1165 124 124 MET CA C 60.6858 0.400 1 1166 124 124 MET CB C 33.3538 0.400 1 1167 124 124 MET CE C 14.9908 0.400 1 1168 124 124 MET N N 118.205 0.400 1 1169 125 125 ILE H H 7.8768 0.050 1 1170 125 125 ILE HA H 3.8498 0.050 1 1171 125 125 ILE HB H 2.3988 0.050 1 1172 125 125 ILE HD1 H 0.8248 0.050 1 1173 125 125 ILE HG12 H 1.7318 0.050 2 1174 125 125 ILE HG13 H 1.4938 0.050 2 1175 125 125 ILE HG2 H 0.8108 0.050 1 1176 125 125 ILE CA C 63.0148 0.400 1 1177 125 125 ILE CB C 35.5488 0.400 1 1178 125 125 ILE CD1 C 9.4738 0.400 1 1179 125 125 ILE CG1 C 26.9728 0.400 1 1180 125 125 ILE CG2 C 16.4428 0.400 1 1181 125 125 ILE N N 119.224 0.400 1 1182 126 126 ARG H H 8.5118 0.050 1 1183 126 126 ARG HA H 4.0908 0.050 1 1184 126 126 ARG HB2 H 1.8898 0.050 2 1185 126 126 ARG HD2 H 3.2478 0.050 2 1186 126 126 ARG HG2 H 1.8238 0.050 2 1187 126 126 ARG HG3 H 1.6708 0.050 2 1188 126 126 ARG C C 176.484 0.400 1 1189 126 126 ARG CA C 59.5788 0.400 1 1190 126 126 ARG CB C 30.2498 0.400 1 1191 126 126 ARG CD C 43.4668 0.400 1 1192 126 126 ARG CG C 27.9058 0.400 1 1193 126 126 ARG N N 117.057 0.400 1 1194 127 127 GLU H H 8.2808 0.050 1 1195 127 127 GLU HA H 4.0608 0.050 1 1196 127 127 GLU HB2 H 2.3078 0.050 2 1197 127 127 GLU HG2 H 2.4958 0.050 2 1198 127 127 GLU C C 174.423 0.400 1 1199 127 127 GLU CA C 58.8898 0.400 1 1200 127 127 GLU CB C 30.1128 0.400 1 1201 127 127 GLU CG C 36.6448 0.400 1 1202 127 127 GLU N N 115.021 0.400 1 1203 128 128 ALA H H 7.2248 0.050 1 1204 128 128 ALA HA H 4.3508 0.050 1 1205 128 128 ALA HB H 1.2118 0.050 1 1206 128 128 ALA C C 174.788 0.400 1 1207 128 128 ALA CA C 51.6648 0.400 1 1208 128 128 ALA CB C 20.8668 0.400 1 1209 128 128 ALA N N 116.627 0.400 1 1210 129 129 ASN H H 7.8978 0.050 1 1211 129 129 ASN HA H 4.4838 0.050 1 1212 129 129 ASN HB2 H 2.8958 0.050 2 1213 129 129 ASN HB3 H 2.5088 0.050 2 1214 129 129 ASN C C 172.792 0.400 1 1215 129 129 ASN CA C 54.3598 0.400 1 1216 129 129 ASN CB C 40.3068 0.400 1 1217 129 129 ASN N N 117.321 0.400 1 1218 130 130 ILE H H 8.2758 0.050 1 1219 130 130 ILE HA H 3.8998 0.050 1 1220 130 130 ILE HB H 1.9548 0.050 1 1221 130 130 ILE HD1 H 0.8608 0.050 1 1222 130 130 ILE HG12 H 1.6528 0.050 2 1223 130 130 ILE HG13 H 1.2608 0.050 2 1224 130 130 ILE HG2 H 0.9198 0.050 1 1225 130 130 ILE C C 175.157 0.400 1 1226 130 130 ILE CA C 63.2378 0.400 1 1227 130 130 ILE CB C 38.5768 0.400 1 1228 130 130 ILE CD1 C 12.3058 0.400 1 1229 130 130 ILE CG1 C 27.6178 0.400 1 1230 130 130 ILE CG2 C 17.2438 0.400 1 1231 130 130 ILE N N 127.388 0.400 1 1232 131 131 ASP H H 8.4118 0.050 1 1233 131 131 ASP HA H 4.5008 0.050 1 1234 131 131 ASP HB2 H 3.0488 0.050 2 1235 131 131 ASP HB3 H 2.6358 0.050 2 1236 131 131 ASP C C 175.047 0.400 1 1237 131 131 ASP CA C 54.0058 0.400 1 1238 131 131 ASP CB C 40.0758 0.400 1 1239 131 131 ASP N N 116.226 0.400 1 1240 132 132 GLY H H 7.6768 0.050 1 1241 132 132 GLY HA2 H 3.9908 0.050 2 1242 132 132 GLY HA3 H 3.8608 0.050 2 1243 132 132 GLY C C 172.439 0.400 1 1244 132 132 GLY CA C 47.2278 0.400 1 1245 132 132 GLY N N 108.352 0.400 1 1246 133 133 ASP H H 8.4278 0.050 1 1247 133 133 ASP HA H 4.4988 0.050 1 1248 133 133 ASP HB2 H 2.9688 0.050 2 1249 133 133 ASP HB3 H 2.5268 0.050 2 1250 133 133 ASP C C 174.740 0.400 1 1251 133 133 ASP CA C 53.9868 0.400 1 1252 133 133 ASP CB C 39.9928 0.400 1 1253 133 133 ASP N N 120.564 0.400 1 1254 134 134 GLY H H 10.3178 0.050 1 1255 134 134 GLY HA2 H 4.0688 0.050 2 1256 134 134 GLY HA3 H 3.4518 0.050 2 1257 134 134 GLY C C 169.860 0.400 1 1258 134 134 GLY CA C 45.5158 0.400 1 1259 134 134 GLY N N 112.342 0.400 1 1260 135 135 GLN H H 7.9788 0.050 1 1261 135 135 GLN HA H 4.9768 0.050 1 1262 135 135 GLN HB2 H 1.7268 0.050 2 1263 135 135 GLN HE21 H 6.5038 0.050 2 1264 135 135 GLN HE22 H 5.9758 0.050 2 1265 135 135 GLN HG2 H 2.0118 0.050 2 1266 135 135 GLN HG3 H 1.6658 0.050 2 1267 135 135 GLN C C 172.149 0.400 1 1268 135 135 GLN CA C 53.2138 0.400 1 1269 135 135 GLN CB C 32.3578 0.400 1 1270 135 135 GLN CG C 33.0208 0.400 1 1271 135 135 GLN N N 114.483 0.400 1 1272 135 135 GLN NE2 N 108.133 0.400 1 1273 136 136 VAL H H 9.1448 0.050 1 1274 136 136 VAL HA H 5.2068 0.050 1 1275 136 136 VAL HB H 2.3778 0.050 1 1276 136 136 VAL HG1 H 1.1408 0.050 2 1277 136 136 VAL HG2 H 1.0668 0.050 2 1278 136 136 VAL C C 172.968 0.400 1 1279 136 136 VAL CA C 61.6478 0.400 1 1280 136 136 VAL CG1 C 23.0538 0.400 2 1281 136 136 VAL CG2 C 21.0718 0.400 2 1282 136 136 VAL N N 124.979 0.400 1 1283 137 137 ASN H H 9.6288 0.050 1 1284 137 137 ASN HA H 5.3468 0.050 1 1285 137 137 ASN HB2 H 3.1808 0.050 2 1286 137 137 ASN HD21 H 7.5038 0.050 2 1287 137 137 ASN HD22 H 7.3288 0.050 2 1288 137 137 ASN C C 171.857 0.400 1 1289 137 137 ASN CA C 50.7558 0.400 1 1290 137 137 ASN CB C 38.3368 0.400 1 1291 137 137 ASN N N 128.916 0.400 1 1292 137 137 ASN ND2 N 111.858 0.400 1 1293 138 138 TYR H H 8.3428 0.050 1 1294 138 138 TYR HA H 3.2258 0.050 1 1295 138 138 TYR HB2 H 2.3428 0.050 2 1296 138 138 TYR HB3 H 2.0148 0.050 2 1297 138 138 TYR HD1 H 6.2598 0.050 3 1298 138 138 TYR HD2 H 6.2598 0.050 3 1299 138 138 TYR HE1 H 6.4808 0.050 3 1300 138 138 TYR HE2 H 6.4808 0.050 3 1301 138 138 TYR C C 173.214 0.400 1 1302 138 138 TYR CA C 62.0288 0.400 1 1303 138 138 TYR CB C 37.5368 0.400 1 1304 138 138 TYR CD1 C 130.347 0.400 3 1305 138 138 TYR CD2 C 130.347 0.400 3 1306 138 138 TYR CE1 C 116.007 0.400 3 1307 138 138 TYR CE2 C 116.007 0.400 3 1308 138 138 TYR N N 118.187 0.400 1 1309 139 139 GLU H H 8.0338 0.050 1 1310 139 139 GLU HA H 3.5918 0.050 1 1311 139 139 GLU HB2 H 2.0058 0.050 2 1312 139 139 GLU HG2 H 2.3258 0.050 2 1313 139 139 GLU HG3 H 2.2958 0.050 2 1314 139 139 GLU C C 177.373 0.400 1 1315 139 139 GLU CA C 59.7578 0.400 1 1316 139 139 GLU CG C 35.8908 0.400 1 1317 139 139 GLU N N 117.957 0.400 1 1318 140 140 GLU H H 8.7048 0.050 1 1319 140 140 GLU HA H 3.8288 0.050 1 1320 140 140 GLU HB2 H 2.1588 0.050 2 1321 140 140 GLU HB3 H 1.9918 0.050 2 1322 140 140 GLU HG2 H 2.8448 0.050 2 1323 140 140 GLU HG3 H 2.3648 0.050 2 1324 140 140 GLU C C 176.476 0.400 1 1325 140 140 GLU CA C 58.5078 0.400 1 1326 140 140 GLU CB C 28.8998 0.400 1 1327 140 140 GLU CG C 37.4508 0.400 1 1328 140 140 GLU N N 119.391 0.400 1 1329 141 141 PHE H H 8.4738 0.050 1 1330 141 141 PHE HA H 3.3988 0.050 1 1331 141 141 PHE HB2 H 3.2698 0.050 2 1332 141 141 PHE HB3 H 2.8878 0.050 2 1333 141 141 PHE HD1 H 6.6488 0.050 3 1334 141 141 PHE HD2 H 6.6488 0.050 3 1335 141 141 PHE HE1 H 7.0578 0.050 3 1336 141 141 PHE HE2 H 7.0578 0.050 3 1337 141 141 PHE HZ H 8.5208 0.050 1 1338 141 141 PHE C C 173.478 0.400 1 1339 141 141 PHE CA C 61.5828 0.400 1 1340 141 141 PHE CB C 39.8728 0.400 1 1341 141 141 PHE CD1 C 129.982 0.400 3 1342 141 141 PHE CD2 C 129.982 0.400 3 1343 141 141 PHE CE1 C 129.459 0.400 3 1344 141 141 PHE CE2 C 129.466 0.400 3 1345 141 141 PHE N N 123.444 0.400 1 1346 142 142 VAL H H 8.6118 0.050 1 1347 142 142 VAL HA H 2.9608 0.050 1 1348 142 142 VAL HB H 1.7098 0.050 1 1349 142 142 VAL HG1 H 0.6598 0.050 2 1350 142 142 VAL HG2 H 0.4038 0.050 2 1351 142 142 VAL C C 176.735 0.400 1 1352 142 142 VAL CA C 66.8108 0.400 1 1353 142 142 VAL CB C 31.3188 0.400 1 1354 142 142 VAL CG1 C 21.1198 0.400 2 1355 142 142 VAL CG2 C 22.8868 0.400 2 1356 142 142 VAL N N 118.366 0.400 1 1357 143 143 GLN H H 7.8028 0.050 1 1358 143 143 GLN HA H 3.7798 0.050 1 1359 143 143 GLN HB2 H 2.0018 0.050 2 1360 143 143 GLN HE21 H 7.3518 0.050 2 1361 143 143 GLN HE22 H 6.7088 0.050 2 1362 143 143 GLN HG2 H 2.3288 0.050 2 1363 143 143 GLN CA C 58.7918 0.400 1 1364 143 143 GLN CB C 27.9958 0.400 1 1365 143 143 GLN CG C 33.7228 0.400 1 1366 143 143 GLN N N 119.002 0.400 1 1367 143 143 GLN NE2 N 111.126 0.400 1 1368 144 144 MET H H 7.3888 0.050 1 1369 144 144 MET HA H 4.1898 0.050 1 1370 144 144 MET HB2 H 1.4298 0.050 2 1371 144 144 MET HE H 1.6808 0.050 1 1372 144 144 MET HG2 H 1.6998 0.050 2 1373 144 144 MET C C 173.938 0.400 1 1374 144 144 MET CA C 56.4348 0.400 1 1375 144 144 MET CE C 16.0918 0.400 1 1376 144 144 MET CG C 30.6068 0.400 1 1377 144 144 MET N N 116.678 0.400 1 1378 145 145 MET H H 7.3048 0.050 1 1379 145 145 MET HA H 4.0238 0.050 1 1380 145 145 MET HB2 H 1.4938 0.050 2 1381 145 145 MET HB3 H 1.1088 0.050 2 1382 145 145 MET HE H 1.1438 0.050 1 1383 145 145 MET HG2 H 1.4608 0.050 2 1384 145 145 MET HG3 H 1.3398 0.050 2 1385 145 145 MET C C 174.791 0.400 1 1386 145 145 MET CA C 55.0798 0.400 1 1387 145 145 MET CB C 32.0368 0.400 1 1388 145 145 MET CE C 18.1958 0.400 1 1389 145 145 MET CG C 32.2298 0.400 1 1390 145 145 MET N N 112.325 0.400 1 1391 146 146 THR H H 7.4728 0.050 1 1392 146 146 THR HA H 4.2518 0.050 1 1393 146 146 THR HB H 4.1468 0.050 1 1394 146 146 THR HG2 H 1.0658 0.050 1 1395 146 146 THR C C 171.522 0.400 1 1396 146 146 THR CA C 61.8998 0.400 1 1397 146 146 THR CB C 70.5428 0.400 1 1398 146 146 THR CG2 C 21.1358 0.400 1 1399 146 146 THR N N 108.155 0.400 1 1400 147 147 ALA H H 7.8608 0.050 1 1401 147 147 ALA HA H 4.3328 0.050 1 1402 147 147 ALA HB H 1.3908 0.050 1 1403 147 147 ALA C C 174.107 0.400 1 1404 147 147 ALA CA C 52.4268 0.400 1 1405 147 147 ALA CB C 19.0508 0.400 1 1406 147 147 ALA N N 126.675 0.400 1 1407 148 148 LYS H H 8.0078 0.050 1 1408 148 148 LYS HA H 4.0798 0.050 1 1409 148 148 LYS HB2 H 1.7998 0.050 2 1410 148 148 LYS HB3 H 1.7308 0.050 2 1411 148 148 LYS HD2 H 1.6478 0.050 2 1412 148 148 LYS HE2 H 2.9868 0.050 2 1413 148 148 LYS HG2 H 1.3938 0.050 2 1414 148 148 LYS CA C 57.6978 0.400 1 1415 148 148 LYS CD C 28.8568 0.400 1 1416 148 148 LYS CE C 41.6988 0.400 1 1417 148 148 LYS CG C 24.7878 0.400 1 1418 148 148 LYS N N 126.400 0.400 1 stop_ save_ save_assigned_chemical_shifts_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' '3D H(CCO)NH' '3D C(CO)NH' '3D HCCH-TOCSY' '2D HBCBCaro' '3D HMBCMet' stop_ loop_ _Sample_label $13C15NCaM/Munc13-1 $13C15NCaM/Munc13-1D2O $13C15NMunc13-1/CaM stop_ _Sample_conditions_label $single _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name Munc13-1 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 458 2 SER H H 8.193 0.05 1 2 458 2 SER HB2 H 3.879 0.05 2 3 458 2 SER C C 172.550 0.5 1 4 458 2 SER CA C 55.709 0.5 1 5 458 2 SER CB C 61.137 0.5 1 6 458 2 SER N N 120.637 0.5 1 7 459 3 ARG H H 8.654 0.05 1 8 459 3 ARG HA H 3.838 0.05 1 9 459 3 ARG HG2 H 1.546 0.05 2 10 459 3 ARG C C 174.192 0.5 1 11 459 3 ARG CA C 55.993 0.5 1 12 459 3 ARG CB C 27.411 0.5 1 13 459 3 ARG CG C 23.675 0.5 1 14 459 3 ARG N N 125.365 0.5 1 15 460 4 ALA H H 8.193 0.05 1 16 460 4 ALA HA H 4.164 0.05 1 17 460 4 ALA HB H 1.353 0.05 1 18 460 4 ALA C C 176.557 0.5 1 19 460 4 ALA CA C 52.358 0.5 1 20 460 4 ALA CB C 15.958 0.5 1 21 460 4 ALA N N 120.862 0.5 1 22 461 5 LYS H H 7.9 0.05 1 23 461 5 LYS HA H 4.185 0.05 1 24 461 5 LYS HB2 H 1.895 0.05 2 25 461 5 LYS HB3 H 1.863 0.05 2 26 461 5 LYS C C 175.175 0.5 1 27 461 5 LYS CA C 56.959 0.5 1 28 461 5 LYS CB C 28.819 0.5 1 29 461 5 LYS CD C 26.742 0.5 1 30 461 5 LYS N N 118.064 0.5 1 31 462 6 ALA H H 7.778 0.05 1 32 462 6 ALA HA H 4.06 0.05 1 33 462 6 ALA HB H 1.444 0.05 1 34 462 6 ALA C C 178.002 0.5 1 35 462 6 ALA CA C 52.15 0.5 1 36 462 6 ALA CB C 14.865 0.5 1 37 462 6 ALA N N 120.253 0.5 1 38 463 7 ASN H H 8.372 0.05 1 39 463 7 ASN HA H 4.459 0.05 1 40 463 7 ASN HB2 H 2.858 0.05 2 41 463 7 ASN HB3 H 2.683 0.05 2 42 463 7 ASN C C 175.009 0.5 1 43 463 7 ASN CA C 53.033 0.5 1 44 463 7 ASN CB C 35.5 0.5 1 45 463 7 ASN N N 118.243 0.5 1 46 464 8 TRP H H 8.533 0.05 1 47 464 8 TRP HA H 4.203 0.05 1 48 464 8 TRP HB2 H 3.382 0.05 2 49 464 8 TRP HB3 H 2.867 0.05 2 50 464 8 TRP HD1 H 7.313 0.05 1 51 464 8 TRP HE1 H 10.381 0.05 1 52 464 8 TRP HH2 H 6.987 0.05 1 53 464 8 TRP HZ2 H 7.128 0.05 1 54 464 8 TRP C C 175.578 0.5 1 55 464 8 TRP CA C 58.19 0.5 1 56 464 8 TRP CB C 26.538 0.5 1 57 464 8 TRP CD1 C 128.771 0.5 1 58 464 8 TRP N N 121.805 0.5 1 59 464 8 TRP NE1 N 129.285 0.5 1 60 465 9 LEU H H 8.264 0.05 1 61 465 9 LEU HA H 4.172 0.05 1 62 465 9 LEU HB2 H 1.841 0.05 2 63 465 9 LEU HB3 H 1.6 0.05 2 64 465 9 LEU HD1 H 0.881 0.05 2 65 465 9 LEU HD2 H 0.886 0.05 2 66 465 9 LEU HG H 1.785 0.05 1 67 465 9 LEU C C 176.568 0.5 1 68 465 9 LEU CA C 55.499 0.5 1 69 465 9 LEU CB C 38.641 0.5 1 70 465 9 LEU CD1 C 21.682 0.5 1 71 465 9 LEU CG C 23.208 0.5 1 72 465 9 LEU N N 118.722 0.5 1 73 466 10 ARG H H 8.264 0.05 1 74 466 10 ARG HA H 4.128 0.05 1 75 466 10 ARG HB2 H 1.927 0.05 2 76 466 10 ARG HD2 H 3.251 0.05 2 77 466 10 ARG HG2 H 0.882 0.05 2 78 466 10 ARG C C 175.900 0.5 1 79 466 10 ARG CA C 56.888 0.5 1 80 466 10 ARG CB C 27.368 0.5 1 81 466 10 ARG CG C 23.738 0.5 1 82 466 10 ARG N N 120.684 0.5 1 83 467 11 ALA H H 8.067 0.05 1 84 467 11 ALA HA H 3.978 0.05 1 85 467 11 ALA HB H 1.584 0.05 1 86 467 11 ALA C C 175.888 0.5 1 87 467 11 ALA CA C 52.558 0.5 1 88 467 11 ALA CB C 16.041 0.5 1 89 467 11 ALA N N 121.482 0.5 1 90 468 12 PHE H H 9.052 0.05 1 91 468 12 PHE HA H 4.35 0.05 1 92 468 12 PHE HB2 H 3.418 0.05 2 93 468 12 PHE HB3 H 3.354 0.05 2 94 468 12 PHE HD1 H 7.082 0.05 3 95 468 12 PHE HD2 H 7.082 0.05 3 96 468 12 PHE HE1 H 7.157 0.05 3 97 468 12 PHE HE2 H 7.157 0.05 3 98 468 12 PHE C C 173.951 0.5 1 99 468 12 PHE CA C 58.326 0.5 1 100 468 12 PHE CB C 37.668 0.5 1 101 468 12 PHE CE1 C 129.841 0.5 3 102 468 12 PHE CE2 C 129.841 0.5 3 103 468 12 PHE N N 117.615 0.5 1 104 469 13 ASN H H 8.602 0.05 1 105 469 13 ASN HA H 4.166 0.05 1 106 469 13 ASN HB2 H 2.95 0.05 2 107 469 13 ASN HB3 H 2.703 0.05 2 108 469 13 ASN C C 174.785 0.5 1 109 469 13 ASN CA C 53.709 0.5 1 110 469 13 ASN CB C 35.325 0.5 1 111 469 13 ASN N N 116.425 0.5 1 112 470 14 LYS H H 8.076 0.05 1 113 470 14 LYS HA H 4.045 0.05 1 114 470 14 LYS HB2 H 2.01 0.05 2 115 470 14 LYS HB3 H 1.839 0.05 2 116 470 14 LYS HD2 H 1.681 0.05 2 117 470 14 LYS HD3 H 1.617 0.05 2 118 470 14 LYS HE2 H 2.928 0.05 2 119 470 14 LYS HG2 H 1.681 0.05 2 120 470 14 LYS HG3 H 1.4 0.05 2 121 470 14 LYS C C 176.194 0.5 1 122 470 14 LYS CA C 57.174 0.5 1 123 470 14 LYS CB C 30.526 0.5 1 124 470 14 LYS CD C 26.002 0.5 1 125 470 14 LYS CG C 22.045 0.5 1 126 470 14 LYS N N 119.958 0.5 1 127 471 15 VAL H H 8.41 0.05 1 128 471 15 VAL HA H 3.532 0.05 1 129 471 15 VAL HB H 2.218 0.05 1 130 471 15 VAL HG1 H 0.938 0.05 2 131 471 15 VAL HG2 H 0.839 0.05 2 132 471 15 VAL C C 174.970 0.5 1 133 471 15 VAL CA C 64.19 0.5 1 134 471 15 VAL CB C 28.483 0.5 1 135 471 15 VAL CG1 C 22.436 0.5 2 136 471 15 VAL CG2 C 19.422 0.5 2 137 471 15 VAL N N 121.488 0.5 1 138 472 16 ARG H H 8.639 0.05 1 139 472 16 ARG HA H 3.763 0.05 1 140 472 16 ARG HB2 H 1.565 0.05 2 141 472 16 ARG HD2 H 3.333 0.05 2 142 472 16 ARG HD3 H 2.98 0.05 2 143 472 16 ARG HG2 H 1.335 0.05 2 144 472 16 ARG HG3 H 1.207 0.05 2 145 472 16 ARG C C 175.887 0.5 1 146 472 16 ARG CA C 56.805 0.5 1 147 472 16 ARG CB C 26.506 0.5 1 148 472 16 ARG CD C 40.184 0.5 1 149 472 16 ARG CG C 22.439 0.5 1 150 472 16 ARG N N 119.209 0.5 1 151 473 17 MET H H 7.701 0.05 1 152 473 17 MET HA H 4.105 0.05 1 153 473 17 MET HB2 H 2.115 0.05 2 154 473 17 MET HB3 H 2.1 0.05 2 155 473 17 MET HE H 2.509 0.05 1 156 473 17 MET HG2 H 2.186 0.05 2 157 473 17 MET C C 175.604 0.5 1 158 473 17 MET CA C 55.673 0.5 1 159 473 17 MET CB C 29.324 0.5 1 160 473 17 MET CE C 14.99 0.5 1 161 473 17 MET N N 117.427 0.5 1 162 474 18 GLN H H 7.733 0.05 1 163 474 18 GLN HA H 4.049 0.05 1 164 474 18 GLN HB2 H 2.142 0.05 2 165 474 18 GLN HB3 H 2.084 0.05 2 166 474 18 GLN HG2 H 2.438 0.05 2 167 474 18 GLN HG3 H 2.262 0.05 2 168 474 18 GLN C C 175.931 0.5 1 169 474 18 GLN CA C 55.976 0.5 1 170 474 18 GLN CB C 24.407 0.5 1 171 474 18 GLN CG C 31.276 0.5 1 172 474 18 GLN N N 119.752 0.5 1 173 475 19 LEU H H 8.151 0.05 1 174 475 19 LEU HA H 4.013 0.05 1 175 475 19 LEU HB2 H 1.871 0.05 2 176 475 19 LEU HB3 H 1.371 0.05 2 177 475 19 LEU HD1 H 0.733 0.05 2 178 475 19 LEU HD2 H 0.718 0.05 2 179 475 19 LEU HG H 1.78 0.05 1 180 475 19 LEU C C 176.150 0.5 1 181 475 19 LEU CA C 54.386 0.5 1 182 475 19 LEU CB C 39.047 0.5 1 183 475 19 LEU CD1 C 24.762 0.5 2 184 475 19 LEU CD2 C 20.787 0.5 2 185 475 19 LEU CG C 25.563 0.5 1 186 475 19 LEU N N 120.063 0.5 1 187 476 20 GLN H H 7.911 0.05 1 188 476 20 GLN HA H 3.98 0.05 1 189 476 20 GLN HB2 H 2.33 0.05 2 190 476 20 GLN HB3 H 2.078 0.05 2 191 476 20 GLN HG2 H 2.412 0.05 2 192 476 20 GLN HG3 H 2.337 0.05 2 193 476 20 GLN C C 175.284 0.5 1 194 476 20 GLN CA C 55.365 0.5 1 195 476 20 GLN CB C 25.474 0.5 1 196 476 20 GLN CG C 31.233 0.5 1 197 476 20 GLN N N 118.054 0.5 1 198 477 21 GLU H H 7.975 0.05 1 199 477 21 GLU HA H 4.016 0.05 1 200 477 21 GLU HB2 H 2.012 0.05 2 201 477 21 GLU HG2 H 2.31 0.05 2 202 477 21 GLU HG3 H 2.184 0.05 2 203 477 21 GLU C C 174.854 0.5 1 204 477 21 GLU CA C 55.49 0.5 1 205 477 21 GLU CB C 26.666 0.5 1 206 477 21 GLU CG C 34.168 0.5 1 207 477 21 GLU N N 119.803 0.5 1 208 478 22 ALA H H 7.726 0.05 1 209 478 22 ALA HA H 4.19 0.05 1 210 478 22 ALA HB H 1.385 0.05 1 211 478 22 ALA C C 175.491 0.5 1 212 478 22 ALA CA C 50.517 0.5 1 213 478 22 ALA CB C 15.961 0.5 1 214 478 22 ALA N N 121.648 0.5 1 215 479 23 ARG H H 7.645 0.05 1 216 479 23 ARG HA H 4.211 0.05 1 217 479 23 ARG HB2 H 1.834 0.05 2 218 479 23 ARG HD2 H 3.135 0.05 2 219 479 23 ARG HG2 H 1.678 0.05 2 220 479 23 ARG HG3 H 1.617 0.05 2 221 479 23 ARG C C 174.086 0.5 1 222 479 23 ARG CA C 53.836 0.5 1 223 479 23 ARG CB C 27.401 0.5 1 224 479 23 ARG CD C 40.823 0.5 1 225 479 23 ARG CG C 24.527 0.5 1 226 479 23 ARG N N 117.484 0.5 1 227 480 24 GLY H H 7.961 0.05 1 228 480 24 GLY HA2 H 3.909 0.05 2 229 480 24 GLY HA3 H 3.909 0.05 2 230 480 24 GLY C C 171.195 0.5 1 231 480 24 GLY CA C 42.457 0.5 1 232 480 24 GLY N N 107.622 0.5 1 233 481 25 GLU H H 8.163 0.05 1 234 481 25 GLU HA H 4.269 0.05 1 235 481 25 GLU HB2 H 2.049 0.05 2 236 481 25 GLU HB3 H 1.889 0.05 2 237 481 25 GLU HG2 H 2.202 0.05 2 238 481 25 GLU C C 174.077 0.5 1 239 481 25 GLU CA C 53.78 0.5 1 240 481 25 GLU CB C 27.272 0.5 1 241 481 25 GLU CG C 33.333 0.5 1 242 481 25 GLU N N 120.497 0.5 1 243 482 26 GLY H H 8.35 0.05 1 244 482 26 GLY HA2 H 3.902 0.05 2 245 482 26 GLY HA3 H 3.902 0.05 2 246 482 26 GLY C C 171.213 0.5 1 247 482 26 GLY CA C 42.485 0.5 1 248 482 26 GLY N N 108.85 0.5 1 249 483 27 GLU H H 8.142 0.05 1 250 483 27 GLU HA H 4.132 0.05 1 251 483 27 GLU HB2 H 2.027 0.05 2 252 483 27 GLU HB3 H 1.911 0.05 2 253 483 27 GLU HG2 H 2.201 0.05 2 254 483 27 GLU C C 174.078 0.5 1 255 483 27 GLU CA C 54.039 0.5 1 256 483 27 GLU CB C 27.066 0.5 1 257 483 27 GLU CG C 33.267 0.5 1 258 483 27 GLU N N 120.369 0.5 1 259 484 28 MET H H 8.348 0.05 1 260 484 28 MET HA H 4.175 0.05 1 261 484 28 MET HB2 H 2.022 0.05 2 262 484 28 MET HB3 H 1.948 0.05 2 263 484 28 MET HE H 2.052 0.05 1 264 484 28 MET HG3 H 2.176 0.05 2 265 484 28 MET C C 173.796 0.5 1 266 484 28 MET CA C 53.324 0.5 1 267 484 28 MET CB C 29.849 0.5 1 268 484 28 MET CE C 14.43 0.5 1 269 484 28 MET CG C 33.966 0.5 1 270 484 28 MET N N 120.436 0.5 1 271 485 29 SER H H 8.125 0.05 1 272 485 29 SER HA H 4.338 0.05 1 273 485 29 SER HB2 H 4.12 0.05 2 274 485 29 SER HB3 H 3.842 0.05 2 275 485 29 SER C C 171.585 0.5 1 276 485 29 SER CA C 56.067 0.5 1 277 485 29 SER CB C 60.603 0.5 1 278 485 29 SER N N 115.589 0.5 1 279 486 30 LYS H H 7.986 0.05 1 280 486 30 LYS HA H 4.22 0.05 1 281 486 30 LYS HB2 H 1.706 0.05 2 282 486 30 LYS HB3 H 1.596 0.05 2 283 486 30 LYS HE2 H 2.837 0.05 2 284 486 30 LYS HG2 H 1.275 0.05 2 285 486 30 LYS C C 173.803 0.5 1 286 486 30 LYS CA C 53.958 0.5 1 287 486 30 LYS CB C 30.005 0.5 1 288 486 30 LYS CD C 26.823 0.5 1 289 486 30 LYS CE C 39.61 0.5 1 290 486 30 LYS CG C 22.144 0.5 1 291 486 30 LYS N N 122.255 0.5 1 292 487 31 SER H H 7.972 0.05 1 293 487 31 SER HA H 3.676 0.05 1 294 487 31 SER HB2 H 3.806 0.05 2 295 487 31 SER HB3 H 3.744 0.05 2 296 487 31 SER C C 171.460 0.5 1 297 487 31 SER CA C 55.826 0.5 1 298 487 31 SER CB C 61.064 0.5 1 299 487 31 SER N N 114.856 0.5 1 300 488 32 LEU H H 8.017 0.05 1 301 488 32 LEU HA H 4.3 0.05 1 302 488 32 LEU HB2 H 1.427 0.05 2 303 488 32 LEU HB3 H 1.272 0.05 2 304 488 32 LEU HD1 H 0.733 0.05 2 305 488 32 LEU HD2 H 0.689 0.05 2 306 488 32 LEU HG H 1.426 0.05 1 307 488 32 LEU C C 174.074 0.5 1 308 488 32 LEU CA C 53.057 0.5 1 309 488 32 LEU CB C 39.082 0.5 1 310 488 32 LEU CD1 C 20.626 0.5 2 311 488 32 LEU CD2 C 18.346 0.5 2 312 488 32 LEU N N 123.172 0.5 1 313 489 33 TRP H H 7.636 0.05 1 314 489 33 TRP HA H 4.124 0.05 1 315 489 33 TRP HB2 H 2.964 0.05 2 316 489 33 TRP HB3 H 2.925 0.05 2 317 489 33 TRP HD1 H 7.073 0.05 1 318 489 33 TRP HE1 H 9.797 0.05 1 319 489 33 TRP HH2 H 7.075 0.05 1 320 489 33 TRP HZ2 H 7.204 0.05 1 321 489 33 TRP C C 172.511 0.5 1 322 489 33 TRP CA C 53.958 0.5 1 323 489 33 TRP CB C 26.283 0.5 1 324 489 33 TRP CD1 C 129.291 0.5 1 325 489 33 TRP N N 117.409 0.5 1 326 489 33 TRP NE1 N 130.113 0.5 1 327 490 34 PHE H H 7.377 0.05 1 328 490 34 PHE HA H 4.325 0.05 1 329 490 34 PHE HB2 H 2.844 0.05 2 330 490 34 PHE HD1 H 7.05 0.05 3 331 490 34 PHE HD2 H 7.05 0.05 3 332 490 34 PHE HE1 H 6.986 0.05 3 333 490 34 PHE HE2 H 6.986 0.05 3 334 490 34 PHE HZ H 7.242 0.05 1 335 490 34 PHE C C 172.418 0.5 1 336 490 34 PHE CA C 55.014 0.5 1 337 490 34 PHE CB C 36.68 0.5 1 338 490 34 PHE CE1 C 129.98 0.5 3 339 490 34 PHE CE2 C 129.98 0.5 3 340 490 34 PHE N N 119.308 0.5 1 341 491 35 LYS H H 7.864 0.05 1 342 491 35 LYS HA H 4.195 0.05 1 343 491 35 LYS HB2 H 1.759 0.05 2 344 491 35 LYS HB3 H 1.595 0.05 2 345 491 35 LYS HD2 H 1.611 0.05 2 346 491 35 LYS HE2 H 2.902 0.05 2 347 491 35 LYS HG2 H 1.297 0.05 2 348 491 35 LYS C C 172.483 0.5 1 349 491 35 LYS CA C 53.521 0.5 1 350 491 35 LYS CB C 30.222 0.5 1 351 491 35 LYS CD C 26.208 0.5 1 352 491 35 LYS CE C 39.534 0.5 1 353 491 35 LYS CG C 20.917 0.5 1 354 491 35 LYS N N 123.484 0.5 1 355 492 36 GLY H H 7.381 0.05 1 356 492 36 GLY HA2 H 3.647 0.05 2 357 492 36 GLY HA3 H 3.647 0.05 2 358 492 36 GLY C C 175.656 0.5 1 359 492 36 GLY CA C 43.436 0.5 1 360 492 36 GLY N N 115.197 0.5 1 stop_ save_