data_4284 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+-Pump ; _BMRB_accession_number 4284 _BMRB_flat_file_name bmr4284.str _Entry_type original _Submission_date 1998-12-16 _Accession_date 1998-12-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Elshorst Bettina . . 2 Hennig Mirko . . 3 Foersterling Holger . . 4 Diener Alexander . . 5 Maurer Marcus . . 6 Schulte Petra . . 7 Schwalbe Harald . . 8 Griesinger Christian . . 9 Krebs Joachim . . 10 Schmid Holger . . 11 Vorherr Thomas . . 12 Carafoli Ernesto . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 843 "13C chemical shifts" 556 "15N chemical shifts" 143 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-01 original author . stop_ _Original_release_date 1999-10-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Elshorst, B., Hennig, M., Foersterling, H., Diener, A., Maurer, M., Schulte P., Schwalbe, H., Griesinger, C., Krebs, J., Schmid, H., Vorherr, T., and Carafoli, E., "NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+-Pump," Biochemistry 38, 12320-12332 (1999). ; _Citation_title ; NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+-Pump ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99425120 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Elshorst Bettina . . 2 Hennig Mirko . . 3 Foersterling Holger . . 4 Diener Alexander . . 5 Maurer Marcus . . 6 Schulte Petra . . 7 Schwalbe Harald . . 8 Griesinger Christian . . 9 Krebs Joachim . . 10 Schmid Holger . . 11 Vorherr Thomas . . 12 Carafoli Ernesto . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12320 _Page_last 12332 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_CaM-C20W-complex _Saveframe_category molecular_system _Mol_system_name 'Calmodulin-Ca2+-Pump-Peptide Complex' _Abbreviation_common CaM-C20W-complex _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cam $CaM C20W $C20W Ca $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CaM _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Calmodulin _Abbreviation_common CaM _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 GLN 4 LEU 5 THR 6 GLU 7 GLU 8 GLN 9 ILE 10 ALA 11 GLU 12 PHE 13 LYS 14 GLU 15 ALA 16 PHE 17 SER 18 LEU 19 PHE 20 ASP 21 LYS 22 ASP 23 GLY 24 ASP 25 GLY 26 THR 27 ILE 28 THR 29 THR 30 LYS 31 GLU 32 LEU 33 GLY 34 THR 35 VAL 36 MET 37 ARG 38 SER 39 LEU 40 GLY 41 GLN 42 ASN 43 PRO 44 THR 45 GLU 46 ALA 47 GLU 48 LEU 49 GLN 50 ASP 51 MET 52 ILE 53 ASN 54 GLU 55 VAL 56 ASP 57 ALA 58 ASP 59 GLY 60 ASN 61 GLY 62 THR 63 ILE 64 ASP 65 PHE 66 PRO 67 GLU 68 PHE 69 LEU 70 THR 71 MET 72 MET 73 ALA 74 ARG 75 LYS 76 MET 77 LYS 78 ASP 79 THR 80 ASP 81 SER 82 GLU 83 GLU 84 GLU 85 ILE 86 ARG 87 GLU 88 ALA 89 PHE 90 ARG 91 VAL 92 PHE 93 ASP 94 LYS 95 ASP 96 GLY 97 ASN 98 GLY 99 TYR 100 ILE 101 SER 102 ALA 103 ALA 104 GLU 105 LEU 106 ARG 107 HIS 108 VAL 109 MET 110 THR 111 ASN 112 LEU 113 GLY 114 GLU 115 LYS 116 LEU 117 THR 118 ASP 119 GLU 120 GLU 121 VAL 122 ASP 123 GLU 124 MET 125 ILE 126 ARG 127 GLU 128 ALA 129 ASP 130 ILE 131 ASP 132 GLY 133 ASP 134 GLY 135 GLN 136 VAL 137 ASN 138 TYR 139 GLU 140 GLU 141 PHE 142 VAL 143 GLN 144 MET 145 MET 146 THR 147 ALA 148 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15184 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15185 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15186 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15187 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15188 calmodulin 100.00 148 99.32 100.00 9.29e-100 BMRB 15191 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15470 calmodulin 100.00 148 99.32 100.00 1.91e-99 BMRB 15624 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 15650 calmodulin 100.00 148 99.32 100.00 3.16e-99 BMRB 15852 calmodulin 100.00 148 99.32 100.00 3.16e-99 BMRB 1634 calmodulin 100.00 148 97.30 99.32 2.41e-97 BMRB 16418 apoCaM 100.00 148 100.00 100.00 4.67e-100 BMRB 16465 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 1648 calmodulin 100.00 148 97.30 99.32 2.41e-97 BMRB 16764 CALMODULIN 100.00 150 100.00 100.00 4.99e-100 BMRB 17264 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 17360 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 17771 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 17807 Calmodulin 99.32 147 100.00 100.00 2.43e-99 BMRB 18027 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 18028 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 18556 Calmodulin 100.00 148 98.65 99.32 2.52e-98 BMRB 19036 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 19238 Calmodulin_prototypical_calcium_sensor 100.00 148 100.00 100.00 4.67e-100 BMRB 19586 entity_1 100.00 148 100.00 100.00 4.67e-100 BMRB 19604 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 25253 CaM 100.00 148 98.65 99.32 1.16e-97 BMRB 25257 CaM 100.00 148 98.65 99.32 1.16e-97 BMRB 26503 Calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 26626 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 26627 CaM 100.00 148 100.00 100.00 4.67e-100 BMRB 4056 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 4270 calmodulin 100.00 148 100.00 100.00 4.67e-100 BMRB 4310 calmodulin 100.00 148 100.00 100.00 4.67e-100 PDB 1A29 "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" 100.00 148 100.00 100.00 4.67e-100 PDB 1CFC "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1CFD "Calcium-Free Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1CFF "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" 100.00 148 100.00 100.00 4.67e-100 PDB 1CKK "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" 100.00 148 100.00 100.00 4.67e-100 PDB 1CLL "Calmodulin Structure Refined At 1.7 Angstroms Resolution" 100.00 148 100.00 100.00 4.67e-100 PDB 1CM1 "Motions Of Calmodulin-Single-Conformer Refinement" 100.00 148 100.00 100.00 4.67e-100 PDB 1CM4 "Motions Of Calmodulin-four-conformer Refinement" 100.00 148 100.00 100.00 4.67e-100 PDB 1CTR "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 1DMO "Calmodulin, Nmr, 30 Structures" 100.00 148 99.32 100.00 1.91e-99 PDB 1G4Y "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1IQ5 "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" 100.00 149 100.00 100.00 4.88e-100 PDB 1IWQ "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" 100.00 148 100.00 100.00 4.67e-100 PDB 1K90 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 148 100.00 100.00 4.67e-100 PDB 1K93 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 97.30 144 100.00 100.00 4.20e-97 PDB 1L7Z "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 1LIN "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" 100.00 148 100.00 100.00 4.67e-100 PDB 1LVC "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 2' Deoxy, 3' Anthr" 100.00 149 100.00 100.00 4.88e-100 PDB 1MUX "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" 100.00 148 100.00 100.00 4.67e-100 PDB 1MXE "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" 100.00 148 97.97 99.32 6.44e-98 PDB 1NWD "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" 100.00 148 100.00 100.00 4.67e-100 PDB 1OOJ "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" 100.00 149 97.97 98.65 1.21e-97 PDB 1PRW "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" 100.00 149 99.32 99.32 4.06e-99 PDB 1QIV "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 1QIW "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" 100.00 148 100.00 100.00 4.67e-100 PDB 1QX5 "Crystal Structure Of Apocalmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1S26 "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" 100.00 148 100.00 100.00 4.67e-100 PDB 1SK6 "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" 100.00 148 100.00 100.00 4.67e-100 PDB 1SY9 "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" 100.00 148 100.00 100.00 4.67e-100 PDB 1UP5 "Chicken Calmodulin" 100.00 148 99.32 99.32 3.93e-99 PDB 1WRZ "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" 100.00 149 100.00 100.00 4.88e-100 PDB 1X02 "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 1XA5 "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" 100.00 148 100.00 100.00 4.67e-100 PDB 1XFU "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" 100.00 149 99.32 100.00 1.16e-99 PDB 1XFV "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" 100.00 149 99.32 100.00 1.16e-99 PDB 1XFW "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" 100.00 149 99.32 100.00 1.16e-99 PDB 1XFY "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" 100.00 149 99.32 100.00 1.16e-99 PDB 1XFZ "Crystal Structure Of Anthrax Edema Factor (ef) In Complex With Calmodulin In The Presence Of 1 Millimolar Exogenously Added Cal" 100.00 149 99.32 100.00 1.16e-99 PDB 1Y0V "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" 97.30 146 100.00 100.00 3.61e-97 PDB 1YR5 "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" 100.00 148 100.00 100.00 4.67e-100 PDB 2BBM "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 6.44e-98 PDB 2BBN "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" 100.00 148 97.97 99.32 6.44e-98 PDB 2BCX "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2BKH "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 2BKI "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" 100.00 149 100.00 100.00 4.88e-100 PDB 2DFS "3-D Structure Of Myosin-V Inhibited State" 100.00 148 100.00 100.00 4.67e-100 PDB 2F2O "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 100.00 100.00 7.52e-100 PDB 2F2P "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" 100.00 179 100.00 100.00 7.52e-100 PDB 2F3Y "CalmodulinIQ DOMAIN COMPLEX" 100.00 148 100.00 100.00 4.67e-100 PDB 2F3Z "CalmodulinIQ-Aa Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2FOT "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" 100.00 148 100.00 100.00 4.67e-100 PDB 2HQW "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2JZI "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0E "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0F "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" 100.00 148 100.00 100.00 4.67e-100 PDB 2K0J "Solution Structure Of Cam Complexed To Drp1p" 100.00 148 99.32 100.00 3.16e-99 PDB 2K61 "Solution Structure Of Cam Complexed To Dapk Peptide" 100.00 148 99.32 100.00 3.16e-99 PDB 2KDU "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" 100.00 148 100.00 100.00 4.67e-100 PDB 2KNE "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" 100.00 148 100.00 100.00 4.67e-100 PDB 2L53 "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" 100.00 148 100.00 100.00 4.67e-100 PDB 2L7L "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" 100.00 148 100.00 100.00 4.67e-100 PDB 2LGF "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" 98.65 146 100.00 100.00 1.01e-98 PDB 2LL6 "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2LL7 "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" 100.00 148 100.00 100.00 4.67e-100 PDB 2LV6 "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" 100.00 148 98.65 99.32 2.52e-98 PDB 2M0J "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2M0K "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" 100.00 148 100.00 100.00 4.67e-100 PDB 2M55 "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 2MG5 "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" 100.00 148 100.00 100.00 4.67e-100 PDB 2MGU "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" 100.00 148 100.00 100.00 4.67e-100 PDB 2O5G "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2O60 "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" 100.00 148 100.00 100.00 4.67e-100 PDB 2R28 "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" 100.00 149 100.00 100.00 4.88e-100 PDB 2V01 "Recombinant Vertebrate Calmodulin Complexed With Pb" 100.00 149 100.00 100.00 4.88e-100 PDB 2V02 "Recombinant Vertebrate Calmodulin Complexed With Ba" 100.00 149 100.00 100.00 4.88e-100 PDB 2VAS "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" 100.00 149 97.97 99.32 4.90e-98 PDB 2VAY "Calmodulin Complexed With Cav1.1 Iq Peptide" 98.65 146 100.00 100.00 1.01e-98 PDB 2VB6 "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" 100.00 149 97.30 99.32 1.19e-97 PDB 2W73 "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" 100.00 149 100.00 100.00 4.88e-100 PDB 2WEL "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" 100.00 150 100.00 100.00 4.52e-100 PDB 2X0G "X-ray Structure Of A Dap-kinase Calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 2X51 "M6 Delta Insert1" 100.00 149 97.97 99.32 4.90e-98 PDB 2Y4V "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" 100.00 149 100.00 100.00 4.88e-100 PDB 2YGG "Complex Of Cambr And Cam" 100.00 150 100.00 100.00 5.33e-100 PDB 3BXK "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3BXL "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3BYA "Structure Of A Calmodulin Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3CLN "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" 100.00 148 99.32 100.00 1.91e-99 PDB 3DVE "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3DVJ "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3DVK "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3DVM "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" 100.00 148 100.00 100.00 4.67e-100 PDB 3EK4 "Calcium-saturated Gcamp2 Monomer" 99.32 449 100.00 100.00 8.93e-96 PDB 3EK7 "Calcium-Saturated Gcamp2 Dimer" 99.32 449 100.00 100.00 8.93e-96 PDB 3EK8 "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" 99.32 449 100.00 100.00 1.26e-95 PDB 3EKH "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" 99.32 449 99.32 99.32 8.65e-95 PDB 3EVU "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" 99.32 449 100.00 100.00 8.93e-96 PDB 3EVV "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" 99.32 449 100.00 100.00 8.93e-96 PDB 3EWT "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.96e-100 PDB 3EWV "Crystal Structure Of Calmodulin Complexed With A Peptide" 100.00 154 100.00 100.00 1.96e-100 PDB 3G43 "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" 100.00 148 100.00 100.00 4.67e-100 PDB 3GN4 "Myosin Lever Arm" 100.00 149 97.97 99.32 4.90e-98 PDB 3GOF "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" 100.00 148 100.00 100.00 4.67e-100 PDB 3HR4 "Human Inos Reductase And Calmodulin Complex" 100.00 149 100.00 100.00 4.88e-100 PDB 3IF7 "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" 100.00 148 100.00 100.00 4.67e-100 PDB 3J41 "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" 100.00 149 100.00 100.00 4.88e-100 PDB 3L9I "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 3O77 "The Structure Of Ca2+ Sensor (Case-16)" 99.32 415 100.00 100.00 4.01e-96 PDB 3O78 "The Structure Of Ca2+ Sensor (Case-12)" 99.32 415 100.00 100.00 4.42e-96 PDB 3OXQ "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" 100.00 149 100.00 100.00 4.88e-100 PDB 3SG2 "Crystal Structure Of Gcamp2-t116v,d381y" 99.32 449 99.32 99.32 1.28e-94 PDB 3SG3 "Crystal Structure Of Gcamp3-d380y" 99.32 449 98.64 99.32 1.62e-93 PDB 3SG4 "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" 100.00 448 97.97 98.65 1.11e-93 PDB 3SG5 "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" 100.00 448 97.97 98.65 9.15e-94 PDB 3SG6 "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" 99.32 450 100.00 100.00 1.14e-95 PDB 3SG7 "Crystal Structure Of Gcamp3-kf(linker 1)" 99.32 448 99.32 100.00 7.62e-95 PDB 3SJQ "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 3SUI "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" 100.00 149 100.00 100.00 4.88e-100 PDB 3U0K "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" 99.32 440 98.64 99.32 2.73e-94 PDB 3WFN "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" 100.00 182 100.00 100.00 5.62e-100 PDB 4ANJ "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" 100.00 149 97.97 99.32 4.90e-98 PDB 4BW7 "Calmodulin In Complex With Strontium" 100.00 149 100.00 100.00 4.88e-100 PDB 4BW8 "Calmodulin With Small Bend In Central Helix" 100.00 149 100.00 100.00 4.88e-100 PDB 4BYF "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" 100.00 149 100.00 100.00 4.88e-100 PDB 4CLN "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" 100.00 148 97.97 99.32 6.44e-98 PDB 4DBP "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" 100.00 149 97.97 99.32 4.90e-98 PDB 4DBQ "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" 100.00 149 97.97 99.32 4.90e-98 PDB 4DCK "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" 100.00 149 100.00 100.00 4.88e-100 PDB 4DJC "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" 100.00 152 100.00 100.00 3.41e-100 PDB 4E50 "Calmodulin And Ng Peptide Complex" 100.00 185 100.00 100.00 2.54e-100 PDB 4EHQ "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" 100.00 148 100.00 100.00 4.67e-100 PDB 4G27 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" 100.00 149 100.00 100.00 4.88e-100 PDB 4G28 "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" 100.00 149 100.00 100.00 4.88e-100 PDB 4HEX "A Novel Conformation Of Calmodulin" 100.00 156 100.00 100.00 2.09e-100 PDB 4IK1 "High Resolution Structure Of Gcampj At Ph 8.5" 99.32 448 98.64 99.32 1.39e-93 PDB 4IK3 "High Resolution Structure Of Gcamp3 At Ph 8.5" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK4 "High Resolution Structure Of Gcamp3 At Ph 5.0" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK5 "High Resolution Structure Of Delta-rest-gcamp3" 99.32 414 99.32 100.00 3.55e-95 PDB 4IK8 "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" 99.32 448 99.32 100.00 9.06e-95 PDB 4IK9 "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" 99.32 448 99.32 100.00 9.06e-95 PDB 4J9Y "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" 100.00 149 100.00 100.00 4.88e-100 PDB 4J9Z "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" 100.00 149 100.00 100.00 4.88e-100 PDB 4JPZ "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4JQ0 "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4L79 "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4LZX "Complex Of Iqcg And Ca2+-free Cam" 100.00 148 100.00 100.00 4.67e-100 PDB 4M1L "Complex Of Iqcg And Ca2+-bound Cam" 100.00 148 100.00 100.00 4.67e-100 PDB 4PJJ "Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4" 100.00 149 97.30 99.32 1.19e-97 PDB 4Q5U "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" 100.00 149 100.00 100.00 4.88e-100 PDB 4QNH "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" 100.00 149 99.32 99.32 5.95e-99 PDB 4R8G "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 4UMO "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 4.88e-100 PDB 4UPU "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" 100.00 148 100.00 100.00 4.67e-100 PDB 4V0C "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA08302 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA11896 "calmodulin [Anas platyrhynchos]" 100.00 149 100.00 100.00 4.88e-100 DBJ BAA19786 "calmodulin [Branchiostoma lanceolatum]" 100.00 149 97.97 99.32 4.90e-98 DBJ BAA19787 "calmodulin [Branchiostoma floridae]" 100.00 149 97.97 99.32 4.90e-98 DBJ BAA19788 "calmodulin [Halocynthia roretzi]" 100.00 149 97.97 99.32 4.90e-98 EMBL CAA10601 "calmodulin [Caenorhabditis elegans]" 100.00 149 97.97 98.65 1.21e-97 EMBL CAA32050 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32062 "calmodulin II [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32119 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 EMBL CAA32120 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA35635 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 GB AAA35641 "calmodulin [Homo sapiens]" 100.00 149 100.00 100.00 4.88e-100 GB AAA37365 "calmodulin synthesis [Mus musculus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA40862 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 GB AAA40863 "calmodulin [Rattus norvegicus]" 100.00 149 100.00 100.00 4.88e-100 PIR JC1305 "calmodulin - Japanese medaka" 100.00 149 100.00 100.00 4.88e-100 PIR MCON "calmodulin - salmon" 100.00 148 100.00 100.00 4.67e-100 PRF 0409298A "troponin C-like protein" 100.00 148 97.30 100.00 2.41e-98 PRF 0608335A calmodulin 100.00 148 97.97 99.32 3.31e-97 REF NP_001008160 "calmodulin [Xenopus (Silurana) tropicalis]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001009759 "calmodulin [Ovis aries]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001027633 "calmodulin [Ciona intestinalis]" 100.00 149 97.30 98.65 3.17e-97 REF NP_001039714 "calmodulin [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 REF NP_001040234 "calmodulin [Bombyx mori]" 100.00 149 97.97 99.32 4.90e-98 SP O02367 "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM" 100.00 149 97.30 98.65 3.17e-97 SP O16305 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 97.97 98.65 1.21e-97 SP O96081 "RecName: Full=Calmodulin-B; Short=CaM B" 100.00 149 97.30 98.65 3.58e-97 SP P02594 "RecName: Full=Calmodulin; Short=CaM" 100.00 149 99.32 100.00 1.57e-99 SP P05932 "RecName: Full=Calmodulin-beta; Short=Cam B" 93.24 138 97.10 99.28 5.00e-90 TPG DAA13808 "TPA: calmodulin 2-like [Bos taurus]" 100.00 216 98.65 98.65 2.37e-98 TPG DAA18029 "TPA: calmodulin [Bos taurus]" 100.00 149 98.65 99.32 7.17e-99 TPG DAA19590 "TPA: calmodulin 3 [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 TPG DAA24777 "TPA: calmodulin 2-like [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 TPG DAA24988 "TPA: calmodulin 2-like isoform 1 [Bos taurus]" 100.00 149 100.00 100.00 4.88e-100 stop_ save_ save_C20W _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C20W peptide' _Abbreviation_common C20W _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 20 _Mol_residue_sequence ; LRRGQILWFRGLNRIQTQIK ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 ARG 3 ARG 4 GLY 5 GLN 6 ILE 7 LEU 8 TRP 9 PHE 10 ARG 11 GLY 12 LEU 13 ASN 14 ARG 15 ILE 16 GLN 17 THR 18 GLN 19 ILE 20 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CaM 'African clawed frog' 8355 Eukaryota Metazoa Xenopus laevis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $CaM 'recombinant technology' E.coli Escherichia coli . plasmid pTSNco12 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CaM 1.7 mM . $C20W 1.7 mM . KCl 100 mM . CaCl2 5 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 970 loop_ _Vendor _Address _Electronic_address 'Molecular Simulations Inc.' '9685 Scranton Road, San Diego, CA 92121-2777' 'USA http://www.msi.com/' stop_ loop_ _Task 'resonance assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $sample_one save_ save_13C-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _Sample_label $sample_one save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_one save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_one save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_one save_ save_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_one save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_one save_ save_(H)CC(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH _Sample_label $sample_one save_ save_H(CCCO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _Sample_label $sample_one save_ save_NOESY-13C-HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-13C-HSQC _Sample_label $sample_one save_ save_NOESY-15N-HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-15N-HSQC _Sample_label $sample_one save_ save_(HB)CB(CCarom)H_13 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CCarom)H _Sample_label $sample_one save_ save_HMBC-HSQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name HMBC-HSQC _Sample_label $sample_one save_ save_LRCC_15 _Saveframe_category NMR_applied_experiment _Experiment_name LRCC _Sample_label $sample_one save_ save_12C,14N-NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name 12C,14N-NOESY _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-13C-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CCarom)H _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name HMBC-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name LRCC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name 12C,14N-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 303 0.05 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name cam _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 ALA CA C 52.141 0.1 1 2 . 1 ALA C C 175.940 0.1 1 3 . 1 ALA CB C 19.123 0.1 1 4 . 1 ALA HB H 1.146 0.05 1 5 . 1 ALA HA H 4.102 0.05 1 6 . 2 ASP CA C 58.836 0.1 1 7 . 2 ASP CB C 40.064 0.1 1 8 . 2 ASP N N 123.043 0.05 1 9 . 2 ASP HB3 H 1.780 0.05 2 10 . 2 ASP HB2 H 2.340 0.05 2 11 . 2 ASP HA H 3.780 0.05 1 12 . 2 ASP H H 7.488 0.05 1 13 . 4 LEU CA C 54.480 0.1 1 14 . 4 LEU C C 177.590 0.1 1 15 . 4 LEU CB C 43.301 0.1 1 16 . 4 LEU CG C 26.663 0.1 1 17 . 4 LEU CD1 C 23.543 0.1 1 18 . 4 LEU CD2 C 23.543 0.1 1 19 . 4 LEU N N 122.412 0.05 1 20 . 4 LEU HG H 1.661 0.05 1 21 . 4 LEU HB3 H 1.417 0.05 2 22 . 4 LEU HB2 H 1.661 0.05 2 23 . 4 LEU HA H 4.661 0.05 1 24 . 4 LEU H H 8.171 0.05 1 25 . 5 THR CA C 60.353 0.1 1 26 . 5 THR C C 175.320 0.1 1 27 . 5 THR CB C 71.065 0.1 1 28 . 5 THR N N 112.360 0.05 1 29 . 5 THR HG2 H 1.240 0.05 1 30 . 5 THR HB H 4.590 0.05 1 31 . 5 THR HA H 4.370 0.05 1 32 . 5 THR H H 8.617 0.05 1 33 . 6 GLU CA C 60.042 0.1 1 34 . 6 GLU C C 179.410 0.1 1 35 . 6 GLU CB C 28.834 0.1 1 36 . 6 GLU CG C 36.282 0.1 1 37 . 6 GLU N N 119.829 0.05 1 38 . 6 GLU HG3 H 2.280 0.05 1 39 . 6 GLU HG2 H 2.280 0.05 1 40 . 6 GLU HB3 H 1.950 0.05 1 41 . 6 GLU HB2 H 1.950 0.05 1 42 . 6 GLU HA H 3.880 0.05 1 43 . 6 GLU H H 8.914 0.05 1 44 . 7 GLU CA C 59.914 0.1 1 45 . 7 GLU C C 179.120 0.1 1 46 . 7 GLU CB C 28.702 0.1 1 47 . 7 GLU CG C 36.802 0.1 1 48 . 7 GLU N N 118.842 0.05 1 49 . 7 GLU HG3 H 2.230 0.05 1 50 . 7 GLU HG2 H 2.230 0.05 1 51 . 7 GLU HB3 H 1.930 0.05 1 52 . 7 GLU HB2 H 1.930 0.05 1 53 . 7 GLU HA H 3.950 0.05 1 54 . 7 GLU H H 8.622 0.05 1 55 . 8 GLN CA C 58.536 0.1 1 56 . 8 GLN C C 178.160 0.1 1 57 . 8 GLN CB C 28.746 0.1 1 58 . 8 GLN CG C 34.462 0.1 1 59 . 8 GLN N N 119.692 0.05 1 60 . 8 GLN HG3 H 2.240 0.05 1 61 . 8 GLN HG2 H 2.240 0.05 1 62 . 8 GLN HB3 H 1.890 0.05 1 63 . 8 GLN HB2 H 1.890 0.05 1 64 . 8 GLN HA H 3.770 0.05 1 65 . 8 GLN H H 7.629 0.05 1 66 . 9 ILE CA C 66.090 0.1 1 67 . 9 ILE CB C 37.556 0.1 1 68 . 9 ILE CG1 C 29.523 0.1 1 69 . 9 ILE CG2 C 17.044 0.1 1 70 . 9 ILE N N 118.892 0.05 1 71 . 9 ILE HD1 H 0.780 0.05 1 72 . 9 ILE HG2 H 1.000 0.05 1 73 . 9 ILE HG13 H 1.720 0.05 1 74 . 9 ILE HG12 H 1.720 0.05 1 75 . 9 ILE HB H 1.830 0.05 1 76 . 9 ILE HA H 3.610 0.05 1 77 . 9 ILE H H 8.274 0.05 1 78 . 10 ALA CA C 55.331 0.1 1 79 . 10 ALA C C 179.160 0.1 1 80 . 10 ALA CB C 17.510 0.1 1 81 . 10 ALA N N 120.481 0.05 1 82 . 10 ALA HB H 1.430 0.05 1 83 . 10 ALA HA H 4.030 0.05 1 84 . 10 ALA H H 7.896 0.05 1 85 . 11 GLU CA C 58.857 0.1 1 86 . 11 GLU C C 180.430 0.1 1 87 . 11 GLU CB C 29.431 0.1 1 88 . 11 GLU CG C 35.762 0.1 1 89 . 11 GLU N N 118.406 0.05 1 90 . 11 GLU HG3 H 2.250 0.05 1 91 . 11 GLU HG2 H 2.250 0.05 1 92 . 11 GLU HB3 H 1.950 0.05 1 93 . 11 GLU HB2 H 1.950 0.05 1 94 . 11 GLU HA H 4.080 0.05 1 95 . 11 GLU H H 7.576 0.05 1 96 . 12 PHE CA C 59.077 0.1 1 97 . 12 PHE C C 178.640 0.1 1 98 . 12 PHE CB C 37.452 0.1 1 99 . 12 PHE CD1 C 130.673 0.1 1 100 . 12 PHE CD2 C 130.673 0.1 1 101 . 12 PHE N N 119.489 0.05 1 102 . 12 PHE HD2 H 7.031 0.05 1 103 . 12 PHE HE2 H 7.105 0.05 1 104 . 12 PHE HZ H 7.113 0.05 1 105 . 12 PHE HE1 H 7.105 0.05 1 106 . 12 PHE HD1 H 7.031 0.05 1 107 . 12 PHE HB3 H 3.380 0.05 1 108 . 12 PHE HB2 H 3.380 0.05 1 109 . 12 PHE HA H 4.940 0.05 1 110 . 12 PHE H H 8.486 0.05 1 111 . 13 LYS CA C 60.001 0.1 1 112 . 13 LYS CB C 31.510 0.1 1 113 . 13 LYS CG C 25.103 0.1 1 114 . 13 LYS CD C 28.743 0.1 1 115 . 13 LYS CE C 39.402 0.1 1 116 . 13 LYS N N 122.906 0.05 1 117 . 13 LYS HG3 H 0.939 0.05 1 118 . 13 LYS HG2 H 0.939 0.05 1 119 . 13 LYS HB3 H 1.830 0.05 1 120 . 13 LYS HB2 H 1.830 0.05 1 121 . 13 LYS HA H 3.980 0.05 1 122 . 13 LYS H H 9.101 0.05 1 123 . 14 GLU CA C 59.308 0.1 1 124 . 14 GLU C C 179.430 0.1 1 125 . 14 GLU CB C 28.781 0.1 1 126 . 14 GLU CG C 35.762 0.1 1 127 . 14 GLU N N 119.738 0.05 1 128 . 14 GLU HG3 H 2.320 0.05 1 129 . 14 GLU HG2 H 2.320 0.05 1 130 . 14 GLU HB3 H 2.140 0.05 1 131 . 14 GLU HB2 H 2.140 0.05 1 132 . 14 GLU HA H 4.050 0.05 1 133 . 14 GLU H H 7.694 0.05 1 134 . 15 ALA CA C 55.242 0.1 1 135 . 15 ALA C C 178.900 0.1 1 136 . 15 ALA CB C 17.620 0.1 1 137 . 15 ALA N N 121.966 0.05 1 138 . 15 ALA HB H 1.870 0.05 1 139 . 15 ALA HA H 4.180 0.05 1 140 . 15 ALA H H 7.902 0.05 1 141 . 16 PHE CA C 61.874 0.1 1 142 . 16 PHE C C 177.210 0.1 1 143 . 16 PHE CB C 39.313 0.1 1 144 . 16 PHE N N 118.557 0.05 1 145 . 16 PHE HD2 H 6.524 0.05 1 146 . 16 PHE HE2 H 7.075 0.05 1 147 . 16 PHE HZ H 7.196 0.05 1 148 . 16 PHE HE1 H 7.075 0.05 1 149 . 16 PHE HD1 H 6.524 0.05 1 150 . 16 PHE HB3 H 3.127 0.05 2 151 . 16 PHE HB2 H 2.830 0.05 2 152 . 16 PHE HA H 3.120 0.05 1 153 . 16 PHE H H 8.706 0.05 1 154 . 17 SER CA C 61.468 0.1 1 155 . 17 SER C C 174.750 0.1 1 156 . 17 SER CB C 63.224 0.1 1 157 . 17 SER N N 112.018 0.05 1 158 . 17 SER HB3 H 3.970 0.05 1 159 . 17 SER HB2 H 3.970 0.05 1 160 . 17 SER HA H 3.970 0.05 1 161 . 17 SER H H 7.837 0.05 1 162 . 18 LEU CA C 57.076 0.1 1 163 . 18 LEU C C 177.840 0.1 1 164 . 18 LEU CB C 41.222 0.1 1 165 . 18 LEU N N 120.220 0.05 1 166 . 18 LEU HD2 H 0.625 0.05 2 167 . 18 LEU HD1 H 0.731 0.05 2 168 . 18 LEU HG H 1.370 0.05 1 169 . 18 LEU HB3 H 1.580 0.05 1 170 . 18 LEU HB2 H 1.580 0.05 1 171 . 18 LEU HA H 3.930 0.05 1 172 . 18 LEU H H 7.312 0.05 1 173 . 19 PHE CA C 59.250 0.1 1 174 . 19 PHE C C 176.510 0.1 1 175 . 19 PHE CB C 40.788 0.1 1 176 . 19 PHE N N 114.164 0.05 1 177 . 19 PHE HD2 H 7.180 0.05 1 178 . 19 PHE HE2 H 7.248 0.05 1 179 . 19 PHE HE1 H 7.248 0.05 1 180 . 19 PHE HD1 H 7.180 0.05 1 181 . 19 PHE HB3 H 2.570 0.05 1 182 . 19 PHE HB2 H 2.570 0.05 1 183 . 19 PHE HA H 4.100 0.05 1 184 . 19 PHE H H 7.147 0.05 1 185 . 20 ASP CA C 52.251 0.1 1 186 . 20 ASP C C 177.050 0.1 1 187 . 20 ASP CB C 38.760 0.1 1 188 . 20 ASP N N 116.801 0.05 1 189 . 20 ASP HB3 H 1.430 0.05 2 190 . 20 ASP HB2 H 2.290 0.05 2 191 . 20 ASP HA H 4.470 0.05 1 192 . 20 ASP H H 7.698 0.05 1 193 . 21 LYS CA C 58.477 0.1 1 194 . 21 LYS CB C 32.244 0.1 1 195 . 21 LYS CG C 24.323 0.1 1 196 . 21 LYS CD C 27.963 0.1 1 197 . 21 LYS CE C 42.002 0.1 1 198 . 21 LYS N N 123.973 0.05 1 199 . 21 LYS HE3 H 2.920 0.05 1 200 . 21 LYS HE2 H 2.920 0.05 1 201 . 21 LYS HD3 H 1.790 0.05 1 202 . 21 LYS HD2 H 1.790 0.05 1 203 . 21 LYS HG3 H 1.420 0.05 1 204 . 21 LYS HG2 H 1.420 0.05 1 205 . 21 LYS HB3 H 1.790 0.05 1 206 . 21 LYS HB2 H 1.790 0.05 1 207 . 21 LYS HA H 3.880 0.05 1 208 . 21 LYS H H 7.591 0.05 1 209 . 22 ASP CA C 52.699 0.1 1 210 . 22 ASP C C 177.630 0.1 1 211 . 22 ASP CB C 39.343 0.1 1 212 . 22 ASP N N 113.315 0.05 1 213 . 22 ASP HB3 H 2.540 0.05 2 214 . 22 ASP HB2 H 2.950 0.05 2 215 . 22 ASP HA H 4.490 0.05 1 216 . 22 ASP H H 8.000 0.05 1 217 . 23 GLY CA C 47.144 0.1 1 218 . 23 GLY C C 175.000 0.1 1 219 . 23 GLY N N 108.678 0.05 1 220 . 23 GLY HA3 H 3.780 0.05 1 221 . 23 GLY HA2 H 3.780 0.05 1 222 . 23 GLY H H 7.587 0.05 1 223 . 24 ASP CA C 53.591 0.1 1 224 . 24 ASP C C 177.360 0.1 1 225 . 24 ASP CB C 40.157 0.1 1 226 . 24 ASP N N 120.112 0.05 1 227 . 24 ASP HB3 H 2.360 0.05 2 228 . 24 ASP HB2 H 2.950 0.05 2 229 . 24 ASP HA H 4.420 0.05 1 230 . 24 ASP H H 8.304 0.05 1 231 . 25 GLY CA C 45.285 0.1 1 232 . 25 GLY C C 173.520 0.1 1 233 . 25 GLY N N 112.549 0.05 1 234 . 25 GLY HA3 H 3.610 0.05 2 235 . 25 GLY HA2 H 4.280 0.05 2 236 . 25 GLY H H 10.530 0.05 1 237 . 26 THR CA C 59.779 0.1 1 238 . 26 THR C C 172.710 0.1 1 239 . 26 THR CB C 72.452 0.1 1 240 . 26 THR N N 112.239 0.05 1 241 . 26 THR HG2 H 0.954 0.05 1 242 . 26 THR HB H 3.736 0.05 1 243 . 26 THR HA H 5.230 0.05 1 244 . 26 THR H H 8.046 0.05 1 245 . 27 ILE CA C 60.345 0.1 1 246 . 27 ILE C C 175.950 0.1 1 247 . 27 ILE CB C 39.402 0.1 1 248 . 27 ILE CG1 C 26.403 0.1 1 249 . 27 ILE CG2 C 15.250 0.1 1 250 . 27 ILE N N 126.303 0.05 1 251 . 27 ILE HD1 H 0.748 0.05 1 252 . 27 ILE HG2 H 0.156 0.05 1 253 . 27 ILE HG13 H 1.010 0.05 1 254 . 27 ILE HG12 H 1.010 0.05 1 255 . 27 ILE HB H 1.670 0.05 1 256 . 27 ILE HA H 4.840 0.05 1 257 . 27 ILE H H 9.696 0.05 1 258 . 28 THR CA C 59.666 0.1 1 259 . 28 THR C C 176.360 0.1 1 260 . 28 THR CB C 72.222 0.1 1 261 . 28 THR N N 115.868 0.05 1 262 . 28 THR HG2 H 1.200 0.05 1 263 . 28 THR HB H 4.660 0.05 1 264 . 28 THR HA H 4.660 0.05 1 265 . 28 THR H H 8.368 0.05 1 266 . 29 THR CA C 66.254 0.1 1 267 . 29 THR C C 177.000 0.1 1 268 . 29 THR CB C 67.680 0.1 1 269 . 29 THR N N 112.198 0.05 1 270 . 29 THR HG2 H 1.170 0.05 1 271 . 29 THR HB H 4.110 0.05 1 272 . 29 THR HA H 3.710 0.05 1 273 . 29 THR H H 8.978 0.05 1 274 . 30 LYS CA C 59.150 0.1 1 275 . 30 LYS C C 179.790 0.1 1 276 . 30 LYS CB C 32.116 0.1 1 277 . 30 LYS CG C 24.583 0.1 1 278 . 30 LYS CD C 28.743 0.1 1 279 . 30 LYS CE C 41.742 0.1 1 280 . 30 LYS N N 120.174 0.05 1 281 . 30 LYS HE3 H 2.860 0.05 1 282 . 30 LYS HE2 H 2.860 0.05 1 283 . 30 LYS HG3 H 1.400 0.05 1 284 . 30 LYS HG2 H 1.400 0.05 1 285 . 30 LYS HB3 H 1.750 0.05 1 286 . 30 LYS HB2 H 1.750 0.05 1 287 . 30 LYS HA H 4.050 0.05 1 288 . 30 LYS H H 7.571 0.05 1 289 . 31 GLU CA C 59.128 0.1 1 290 . 31 GLU C C 178.080 0.1 1 291 . 31 GLU CB C 29.372 0.1 1 292 . 31 GLU CG C 37.842 0.1 1 293 . 31 GLU N N 120.882 0.05 1 294 . 31 GLU HB3 H 2.420 0.05 1 295 . 31 GLU HB2 H 2.420 0.05 1 296 . 31 GLU HA H 3.980 0.05 1 297 . 31 GLU H H 7.574 0.05 1 298 . 32 LEU CA C 58.814 0.1 1 299 . 32 LEU C C 178.850 0.1 1 300 . 32 LEU CB C 42.242 0.1 1 301 . 32 LEU CG C 25.623 0.1 1 302 . 32 LEU CD1 C 23.283 0.1 1 303 . 32 LEU CD2 C 23.283 0.1 1 304 . 32 LEU N N 119.063 0.05 1 305 . 32 LEU HB3 H 1.330 0.05 2 306 . 32 LEU HB2 H 1.650 0.05 2 307 . 32 LEU HA H 3.940 0.05 1 308 . 32 LEU H H 8.437 0.05 1 309 . 33 GLY CA C 48.218 0.1 1 310 . 33 GLY C C 175.030 0.1 1 311 . 33 GLY N N 104.936 0.05 1 312 . 33 GLY HA3 H 3.470 0.05 2 313 . 33 GLY HA2 H 3.890 0.05 2 314 . 33 GLY H H 8.558 0.05 1 315 . 34 THR CA C 66.785 0.1 1 316 . 34 THR C C 177.050 0.1 1 317 . 34 THR CB C 68.582 0.1 1 318 . 34 THR N N 117.460 0.05 1 319 . 34 THR HG2 H 1.180 0.05 1 320 . 34 THR HB H 4.240 0.05 1 321 . 34 THR HA H 3.800 0.05 1 322 . 34 THR H H 7.838 0.05 1 323 . 35 VAL CA C 66.257 0.1 1 324 . 35 VAL C C 179.110 0.1 1 325 . 35 VAL CB C 31.024 0.1 1 326 . 35 VAL CG1 C 22.503 0.1 1 327 . 35 VAL CG2 C 20.164 0.1 1 328 . 35 VAL N N 121.522 0.05 1 329 . 35 VAL HG2 H 0.317 0.05 2 330 . 35 VAL HG1 H 0.612 0.05 2 331 . 35 VAL HB H 1.890 0.05 1 332 . 35 VAL HA H 3.430 0.05 1 333 . 35 VAL H H 7.563 0.05 1 334 . 36 MET CA C 59.181 0.1 1 335 . 36 MET C C 179.120 0.1 1 336 . 36 MET CB C 31.140 0.1 1 337 . 36 MET CG C 31.648 0.1 1 338 . 36 MET CE C 16.503 0.1 1 339 . 36 MET N N 117.849 0.05 1 340 . 36 MET HE H 2.022 0.05 1 341 . 36 MET HG3 H 2.232 0.05 1 342 . 36 MET HG2 H 2.232 0.05 1 343 . 36 MET HB3 H 1.890 0.05 1 344 . 36 MET HB2 H 1.890 0.05 1 345 . 36 MET HA H 4.000 0.05 1 346 . 36 MET H H 8.382 0.05 1 347 . 37 ARG CA C 59.809 0.1 1 348 . 37 ARG C C 181.230 0.1 1 349 . 37 ARG CB C 37.842 0.1 1 350 . 37 ARG CG C 29.003 0.1 1 351 . 37 ARG CD C 43.301 0.1 1 352 . 37 ARG N N 118.139 0.05 1 353 . 37 ARG H H 7.959 0.05 1 354 . 38 SER CA C 61.364 0.1 1 355 . 38 SER C C 174.730 0.1 1 356 . 38 SER CB C 62.716 0.1 1 357 . 38 SER N N 118.299 0.05 1 358 . 38 SER HB3 H 4.000 0.05 1 359 . 38 SER HB2 H 4.000 0.05 1 360 . 38 SER HA H 4.310 0.05 1 361 . 38 SER H H 7.827 0.05 1 362 . 39 LEU CA C 54.394 0.1 1 363 . 39 LEU C C 177.320 0.1 1 364 . 39 LEU CB C 41.351 0.1 1 365 . 39 LEU CG C 25.363 0.1 1 366 . 39 LEU CD1 C 21.984 0.1 1 367 . 39 LEU CD2 C 21.984 0.1 1 368 . 39 LEU N N 120.055 0.05 1 369 . 39 LEU HG H 1.740 0.05 1 370 . 39 LEU HB3 H 1.740 0.05 1 371 . 39 LEU HB2 H 1.740 0.05 1 372 . 39 LEU HA H 4.380 0.05 1 373 . 39 LEU H H 7.281 0.05 1 374 . 40 GLY CA C 45.416 0.1 1 375 . 40 GLY N N 106.061 0.05 1 376 . 40 GLY HA3 H 4.180 0.05 2 377 . 40 GLY HA2 H 3.700 0.05 2 378 . 40 GLY H H 7.753 0.05 1 379 . 41 GLN CA C 54.406 0.1 1 380 . 41 GLN C C 173.970 0.1 1 381 . 41 GLN CB C 30.194 0.1 1 382 . 41 GLN CG C 33.682 0.1 1 383 . 41 GLN N N 117.769 0.05 1 384 . 41 GLN HE22 H 7.429 0.05 1 385 . 41 GLN HE21 H 6.724 0.05 1 386 . 41 GLN HG3 H 2.100 0.05 1 387 . 41 GLN HG2 H 2.100 0.05 1 388 . 41 GLN HB3 H 1.550 0.05 1 389 . 41 GLN HB2 H 1.550 0.05 1 390 . 41 GLN HA H 4.390 0.05 1 391 . 41 GLN H H 7.700 0.05 1 392 . 42 ASN CA C 51.158 0.1 1 393 . 42 ASN CB C 38.913 0.1 1 394 . 42 ASN ND2 N 111.493 0.05 1 395 . 42 ASN N N 115.763 0.05 1 396 . 42 ASN HD22 H 7.419 0.05 1 397 . 42 ASN HD21 H 6.605 0.05 1 398 . 42 ASN HA H 4.610 0.05 1 399 . 42 ASN H H 8.602 0.05 1 400 . 43 PRO CA C 62.020 0.1 1 401 . 43 PRO C C 177.590 0.1 1 402 . 43 PRO CB C 31.603 0.1 1 403 . 43 PRO CG C 26.923 0.1 1 404 . 43 PRO CD C 43.301 0.1 1 405 . 43 PRO HB3 H 2.062 0.05 2 406 . 43 PRO HB2 H 1.774 0.05 2 407 . 43 PRO HA H 4.625 0.05 1 408 . 44 THR CA C 60.363 0.1 1 409 . 44 THR C C 175.010 0.1 1 410 . 44 THR CB C 71.073 0.1 1 411 . 44 THR N N 112.354 0.05 1 412 . 44 THR HG2 H 1.250 0.05 1 413 . 44 THR HB H 4.640 0.05 1 414 . 44 THR HA H 4.360 0.05 1 415 . 44 THR H H 8.643 0.05 1 416 . 45 GLU CA C 60.060 0.1 1 417 . 45 GLU C C 178.860 0.1 1 418 . 45 GLU CB C 28.624 0.1 1 419 . 45 GLU CG C 36.022 0.1 1 420 . 45 GLU N N 120.106 0.05 1 421 . 45 GLU HG3 H 2.240 0.05 1 422 . 45 GLU HG2 H 2.240 0.05 1 423 . 45 GLU HB3 H 1.950 0.05 1 424 . 45 GLU HB2 H 1.950 0.05 1 425 . 45 GLU HA H 3.880 0.05 1 426 . 45 GLU H H 8.707 0.05 1 427 . 46 ALA CA C 54.838 0.1 1 428 . 46 ALA C C 180.150 0.1 1 429 . 46 ALA CB C 17.691 0.1 1 430 . 46 ALA N N 120.104 0.05 1 431 . 46 ALA HB H 1.300 0.05 1 432 . 46 ALA HA H 4.000 0.05 1 433 . 46 ALA H H 8.153 0.05 1 434 . 47 GLU CA C 58.860 0.1 1 435 . 47 GLU C C 180.100 0.1 1 436 . 47 GLU CB C 29.432 0.1 1 437 . 47 GLU CG C 37.062 0.1 1 438 . 47 GLU N N 118.055 0.05 1 439 . 47 GLU HG3 H 1.960 0.05 1 440 . 47 GLU HG2 H 1.960 0.05 1 441 . 47 GLU HB3 H 1.790 0.05 2 442 . 47 GLU HB2 H 2.230 0.05 2 443 . 47 GLU HA H 3.940 0.05 1 444 . 47 GLU H H 7.581 0.05 1 445 . 48 LEU CA C 58.147 0.1 1 446 . 48 LEU C C 178.460 0.1 1 447 . 48 LEU CB C 42.092 0.1 1 448 . 48 LEU CG C 26.403 0.1 1 449 . 48 LEU CD1 C 25.363 0.1 1 450 . 48 LEU CD2 C 23.283 0.1 1 451 . 48 LEU N N 119.713 0.05 1 452 . 48 LEU HG H 1.650 0.05 1 453 . 48 LEU HB3 H 1.160 0.05 2 454 . 48 LEU HB2 H 1.960 0.05 2 455 . 48 LEU HA H 3.950 0.05 1 456 . 48 LEU H H 8.067 0.05 1 457 . 49 GLN CA C 58.543 0.1 1 458 . 49 GLN C C 178.520 0.1 1 459 . 49 GLN CB C 27.790 0.1 1 460 . 49 GLN CG C 33.682 0.1 1 461 . 49 GLN N N 117.569 0.05 1 462 . 49 GLN HG3 H 2.330 0.05 1 463 . 49 GLN HG2 H 2.330 0.05 1 464 . 49 GLN HB3 H 2.060 0.05 1 465 . 49 GLN HB2 H 2.060 0.05 1 466 . 49 GLN HA H 3.740 0.05 1 467 . 49 GLN H H 8.090 0.05 1 468 . 50 ASP CA C 57.573 0.1 1 469 . 50 ASP C C 178.630 0.1 1 470 . 50 ASP CB C 40.065 0.1 1 471 . 50 ASP N N 119.382 0.05 1 472 . 50 ASP HB3 H 2.570 0.05 2 473 . 50 ASP HB2 H 2.690 0.05 2 474 . 50 ASP HA H 4.320 0.05 1 475 . 50 ASP H H 7.986 0.05 1 476 . 51 MET CA C 59.339 0.1 1 477 . 51 MET C C 178.830 0.1 1 478 . 51 MET CB C 32.553 0.1 1 479 . 51 MET CG C 32.750 0.1 1 480 . 51 MET CE C 16.779 0.1 1 481 . 51 MET N N 118.744 0.05 1 482 . 51 MET HE H 1.939 0.05 1 483 . 51 MET HG3 H 2.645 0.05 2 484 . 51 MET HG2 H 2.439 0.05 2 485 . 51 MET HB3 H 1.870 0.05 2 486 . 51 MET HB2 H 2.180 0.05 2 487 . 51 MET HA H 3.960 0.05 1 488 . 51 MET H H 7.764 0.05 1 489 . 52 ILE CA C 64.613 0.1 1 490 . 52 ILE C C 177.720 0.1 1 491 . 52 ILE CB C 36.611 0.1 1 492 . 52 ILE CG1 C 28.743 0.1 1 493 . 52 ILE CG2 C 21.464 0.1 1 494 . 52 ILE N N 117.677 0.05 1 495 . 52 ILE HD1 H 0.618 0.05 1 496 . 52 ILE HG2 H 0.968 0.05 1 497 . 52 ILE HG13 H 1.550 0.05 1 498 . 52 ILE HG12 H 1.550 0.05 1 499 . 52 ILE HB H 1.860 0.05 1 500 . 52 ILE HA H 3.440 0.05 1 501 . 52 ILE H H 7.649 0.05 1 502 . 53 ASN CA C 55.787 0.1 1 503 . 53 ASN C C 177.260 0.1 1 504 . 53 ASN CB C 37.718 0.1 1 505 . 53 ASN ND2 N 111.141 0.05 1 506 . 53 ASN N N 117.095 0.05 1 507 . 53 ASN HD22 H 7.732 0.05 1 508 . 53 ASN HD21 H 6.825 0.05 1 509 . 53 ASN HB3 H 2.890 0.05 2 510 . 53 ASN HB2 H 2.820 0.05 2 511 . 53 ASN HA H 4.310 0.05 1 512 . 53 ASN H H 8.485 0.05 1 513 . 54 GLU CA C 58.615 0.1 1 514 . 54 GLU C C 177.450 0.1 1 515 . 54 GLU CB C 29.956 0.1 1 516 . 54 GLU CG C 36.022 0.1 1 517 . 54 GLU N N 115.765 0.05 1 518 . 54 GLU HG3 H 2.300 0.05 1 519 . 54 GLU HG2 H 2.300 0.05 1 520 . 54 GLU HB3 H 2.050 0.05 2 521 . 54 GLU HB2 H 1.950 0.05 2 522 . 54 GLU HA H 3.930 0.05 1 523 . 54 GLU H H 7.469 0.05 1 524 . 55 VAL CA C 60.670 0.1 1 525 . 55 VAL C C 175.660 0.1 1 526 . 55 VAL CB C 32.123 0.1 1 527 . 55 VAL CG1 C 21.724 0.1 1 528 . 55 VAL CG2 C 19.384 0.1 1 529 . 55 VAL N N 108.472 0.05 1 530 . 55 VAL HG2 H 0.785 0.05 1 531 . 55 VAL HG1 H 0.785 0.05 1 532 . 55 VAL HB H 2.240 0.05 1 533 . 55 VAL HA H 4.320 0.05 1 534 . 55 VAL H H 7.099 0.05 1 535 . 56 ASP CA C 53.726 0.1 1 536 . 56 ASP C C 176.040 0.1 1 537 . 56 ASP CB C 39.829 0.1 1 538 . 56 ASP N N 120.993 0.05 1 539 . 56 ASP HB3 H 2.450 0.05 2 540 . 56 ASP HB2 H 2.650 0.05 2 541 . 56 ASP HA H 4.530 0.05 1 542 . 56 ASP H H 7.597 0.05 1 543 . 57 ALA CA C 54.055 0.1 1 544 . 57 ALA C C 178.570 0.1 1 545 . 57 ALA CB C 19.103 0.1 1 546 . 57 ALA N N 131.083 0.05 1 547 . 57 ALA HB H 1.430 0.05 1 548 . 57 ALA HA H 4.120 0.05 1 549 . 57 ALA H H 8.311 0.05 1 550 . 58 ASP CA C 52.597 0.1 1 551 . 58 ASP C C 177.800 0.1 1 552 . 58 ASP CB C 39.435 0.1 1 553 . 58 ASP N N 113.132 0.05 1 554 . 58 ASP HB3 H 2.560 0.05 2 555 . 58 ASP HB2 H 2.940 0.05 2 556 . 58 ASP HA H 4.550 0.05 1 557 . 58 ASP H H 8.074 0.05 1 558 . 59 GLY CA C 47.022 0.1 1 559 . 59 GLY C C 174.800 0.1 1 560 . 59 GLY N N 107.749 0.05 1 561 . 59 GLY HA3 H 3.780 0.05 2 562 . 59 GLY HA2 H 3.720 0.05 2 563 . 59 GLY H H 7.476 0.05 1 564 . 60 ASN CA C 52.509 0.1 1 565 . 60 ASN C C 176.710 0.1 1 566 . 60 ASN CB C 37.447 0.1 1 567 . 60 ASN N N 117.898 0.05 1 568 . 60 ASN HB3 H 2.550 0.05 2 569 . 60 ASN HB2 H 3.210 0.05 2 570 . 60 ASN HA H 4.570 0.05 1 571 . 60 ASN H H 8.003 0.05 1 572 . 61 GLY CA C 45.500 0.1 1 573 . 61 GLY C C 173.070 0.1 1 574 . 61 GLY N N 112.682 0.05 1 575 . 61 GLY HA3 H 3.390 0.05 2 576 . 61 GLY HA2 H 4.120 0.05 2 577 . 61 GLY H H 10.471 0.05 1 578 . 62 THR CA C 59.429 0.1 1 579 . 62 THR C C 173.030 0.1 1 580 . 62 THR CB C 71.823 0.1 1 581 . 62 THR N N 108.256 0.05 1 582 . 62 THR HG2 H 1.010 0.05 1 583 . 62 THR HB H 3.910 0.05 1 584 . 62 THR HA H 4.660 0.05 1 585 . 62 THR H H 7.577 0.05 1 586 . 63 ILE CA C 59.624 0.1 1 587 . 63 ILE C C 175.360 0.1 1 588 . 63 ILE CB C 39.309 0.1 1 589 . 63 ILE CG1 C 26.923 0.1 1 590 . 63 ILE CG2 C 18.084 0.1 1 591 . 63 ILE N N 123.137 0.05 1 592 . 63 ILE HD1 H 0.685 0.05 1 593 . 63 ILE HG2 H 1.160 0.05 1 594 . 63 ILE HG13 H 1.460 0.05 1 595 . 63 ILE HG12 H 1.460 0.05 1 596 . 63 ILE HB H 1.970 0.05 1 597 . 63 ILE HA H 5.080 0.05 1 598 . 63 ILE H H 8.795 0.05 1 599 . 64 ASP CA C 51.977 0.1 1 600 . 64 ASP C C 176.180 0.1 1 601 . 64 ASP CB C 42.029 0.1 1 602 . 64 ASP N N 127.595 0.05 1 603 . 64 ASP HB3 H 2.709 0.05 2 604 . 64 ASP HB2 H 2.959 0.05 2 605 . 64 ASP HA H 5.300 0.05 1 606 . 64 ASP H H 8.742 0.05 1 607 . 65 PHE CA C 63.389 0.1 1 608 . 65 PHE CB C 35.620 0.1 1 609 . 65 PHE CD1 C 132.700 0.1 1 610 . 65 PHE CE1 C 131.190 0.1 1 611 . 65 PHE CE2 C 131.190 0.1 1 612 . 65 PHE CD2 C 132.700 0.1 1 613 . 65 PHE N N 118.217 0.05 1 614 . 65 PHE HD2 H 6.610 0.05 1 615 . 65 PHE HE2 H 7.063 0.05 1 616 . 65 PHE HZ H 7.095 0.05 1 617 . 65 PHE HE1 H 7.063 0.05 1 618 . 65 PHE HD1 H 6.610 0.05 1 619 . 65 PHE HB3 H 2.730 0.05 2 620 . 65 PHE HB2 H 2.030 0.05 2 621 . 65 PHE HA H 3.900 0.05 1 622 . 65 PHE H H 8.852 0.05 1 623 . 66 PRO CA C 66.179 0.1 1 624 . 66 PRO C C 179.980 0.1 1 625 . 66 PRO CB C 30.303 0.1 1 626 . 66 PRO CG C 27.963 0.1 1 627 . 66 PRO CD C 40.442 0.1 1 628 . 66 PRO HB3 H 2.507 0.05 1 629 . 66 PRO HB2 H 2.507 0.05 1 630 . 66 PRO HA H 3.762 0.05 1 631 . 67 GLU CA C 58.609 0.1 1 632 . 67 GLU C C 178.800 0.1 1 633 . 67 GLU CB C 29.195 0.1 1 634 . 67 GLU CG C 36.542 0.1 1 635 . 67 GLU N N 116.955 0.05 1 636 . 67 GLU HG3 H 2.528 0.05 2 637 . 67 GLU HG2 H 2.850 0.05 2 638 . 67 GLU HB3 H 2.010 0.05 1 639 . 67 GLU HB2 H 2.010 0.05 1 640 . 67 GLU HA H 4.030 0.05 1 641 . 67 GLU H H 7.855 0.05 1 642 . 68 PHE CA C 61.133 0.1 1 643 . 68 PHE C C 176.840 0.1 1 644 . 68 PHE CB C 39.878 0.1 1 645 . 68 PHE CD1 C 132.460 0.1 1 646 . 68 PHE CE1 C 131.870 0.1 1 647 . 68 PHE CE2 C 131.870 0.1 1 648 . 68 PHE CD2 C 132.460 0.1 1 649 . 68 PHE N N 122.998 0.05 1 650 . 68 PHE HD2 H 6.490 0.05 1 651 . 68 PHE HE2 H 6.920 0.05 1 652 . 68 PHE HZ H 7.080 0.05 1 653 . 68 PHE HE1 H 6.920 0.05 1 654 . 68 PHE HD1 H 6.490 0.05 1 655 . 68 PHE HB3 H 3.370 0.05 2 656 . 68 PHE HB2 H 3.070 0.05 2 657 . 68 PHE HA H 3.870 0.05 1 658 . 68 PHE H H 8.696 0.05 1 659 . 69 LEU CA C 58.137 0.1 1 660 . 69 LEU C C 179.040 0.1 1 661 . 69 LEU CB C 40.612 0.1 1 662 . 69 LEU CG C 25.103 0.1 1 663 . 69 LEU CD1 C 23.803 0.1 1 664 . 69 LEU CD2 C 20.424 0.1 1 665 . 69 LEU N N 118.504 0.05 1 666 . 69 LEU HG H 0.924 0.05 1 667 . 69 LEU HB3 H 1.050 0.05 2 668 . 69 LEU HB2 H 1.410 0.05 2 669 . 69 LEU HA H 3.230 0.05 1 670 . 69 LEU H H 8.348 0.05 1 671 . 70 THR CA C 66.350 0.1 1 672 . 70 THR CB C 68.318 0.1 1 673 . 70 THR N N 114.811 0.05 1 674 . 70 THR HG2 H 1.080 0.05 1 675 . 70 THR HB H 4.200 0.05 1 676 . 70 THR HA H 3.690 0.05 1 677 . 70 THR H H 7.447 0.05 1 678 . 71 MET CA C 58.637 0.1 1 679 . 71 MET C C 178.020 0.1 1 680 . 71 MET CB C 30.929 0.1 1 681 . 71 MET CG C 31.648 0.1 1 682 . 71 MET CE C 16.847 0.1 1 683 . 71 MET HE H 1.638 0.05 1 684 . 71 MET HG3 H 2.335 0.05 1 685 . 71 MET HG2 H 2.335 0.05 1 686 . 71 MET HB3 H 2.010 0.05 1 687 . 71 MET HB2 H 2.010 0.05 1 688 . 71 MET HA H 3.657 0.05 1 689 . 72 MET CA C 55.654 0.1 1 690 . 72 MET C C 178.420 0.1 1 691 . 72 MET CB C 30.440 0.1 1 692 . 72 MET CG C 31.648 0.1 1 693 . 72 MET CE C 17.054 0.1 1 694 . 72 MET N N 116.338 0.05 1 695 . 72 MET HE H 1.581 0.05 1 696 . 72 MET HB3 H 1.000 0.05 1 697 . 72 MET HB2 H 1.000 0.05 1 698 . 72 MET HA H 3.890 0.05 1 699 . 72 MET H H 7.944 0.05 1 700 . 73 ALA CA C 54.767 0.1 1 701 . 73 ALA C C 179.720 0.1 1 702 . 73 ALA CB C 17.666 0.1 1 703 . 73 ALA N N 121.423 0.05 1 704 . 73 ALA HB H 1.310 0.05 1 705 . 73 ALA HA H 3.960 0.05 1 706 . 73 ALA H H 8.101 0.05 1 707 . 74 ARG CA C 58.397 0.1 1 708 . 74 ARG CB C 29.937 0.1 1 709 . 74 ARG CD C 40.962 0.1 1 710 . 74 ARG N N 116.220 0.05 1 711 . 74 ARG HD3 H 2.980 0.05 1 712 . 74 ARG HD2 H 2.980 0.05 1 713 . 74 ARG HG3 H 1.320 0.05 1 714 . 74 ARG HG2 H 1.320 0.05 1 715 . 74 ARG HB3 H 1.560 0.05 2 716 . 74 ARG HB2 H 1.730 0.05 2 717 . 74 ARG HA H 3.980 0.05 1 718 . 74 ARG H H 7.450 0.05 1 719 . 75 LYS CA C 57.079 0.1 1 720 . 75 LYS CB C 32.122 0.1 1 721 . 75 LYS CG C 24.583 0.1 1 722 . 75 LYS N N 118.037 0.05 1 723 . 75 LYS HG3 H 1.300 0.05 1 724 . 75 LYS HG2 H 1.300 0.05 1 725 . 75 LYS HB3 H 1.760 0.05 1 726 . 75 LYS HB2 H 1.760 0.05 1 727 . 75 LYS HA H 3.950 0.05 1 728 . 75 LYS H H 7.548 0.05 1 729 . 76 MET CA C 56.559 0.1 1 730 . 76 MET CB C 32.381 0.1 1 731 . 76 MET CG C 32.199 0.1 1 732 . 76 MET CE C 16.916 0.1 1 733 . 76 MET N N 117.832 0.05 1 734 . 76 MET HE H 1.895 0.05 1 735 . 76 MET H H 7.736 0.05 1 736 . 77 LYS CA C 56.560 0.1 1 737 . 77 LYS C C 176.350 0.1 1 738 . 77 LYS CB C 32.642 0.1 1 739 . 77 LYS CG C 24.323 0.1 1 740 . 77 LYS CD C 28.743 0.1 1 741 . 77 LYS CE C 40.962 0.1 1 742 . 77 LYS HE3 H 2.860 0.05 1 743 . 77 LYS HE2 H 2.860 0.05 1 744 . 77 LYS HD3 H 1.530 0.05 1 745 . 77 LYS HD2 H 1.530 0.05 1 746 . 77 LYS HG3 H 1.330 0.05 1 747 . 77 LYS HG2 H 1.330 0.05 1 748 . 77 LYS HB3 H 1.722 0.05 1 749 . 77 LYS HB2 H 1.722 0.05 1 750 . 77 LYS HA H 4.180 0.05 1 751 . 78 ASP CA C 54.818 0.1 1 752 . 78 ASP C C 176.460 0.1 1 753 . 78 ASP CB C 40.874 0.1 1 754 . 78 ASP N N 120.866 0.05 1 755 . 78 ASP HB3 H 2.590 0.05 2 756 . 78 ASP HB2 H 2.610 0.05 2 757 . 78 ASP HA H 4.610 0.05 1 758 . 78 ASP H H 8.134 0.05 1 759 . 79 THR CA C 62.135 0.1 1 760 . 79 THR C C 174.340 0.1 1 761 . 79 THR CB C 69.697 0.1 1 762 . 79 THR N N 113.610 0.05 1 763 . 79 THR HG2 H 1.090 0.05 1 764 . 79 THR HB H 4.200 0.05 1 765 . 79 THR HA H 4.200 0.05 1 766 . 79 THR H H 7.950 0.05 1 767 . 80 ASP CA C 54.583 0.1 1 768 . 80 ASP C C 176.660 0.1 1 769 . 80 ASP CB C 41.145 0.1 1 770 . 80 ASP N N 122.501 0.05 1 771 . 80 ASP HB3 H 2.630 0.05 1 772 . 80 ASP HB2 H 2.630 0.05 1 773 . 80 ASP HA H 4.610 0.05 1 774 . 80 ASP H H 8.306 0.05 1 775 . 81 SER CA C 59.335 0.1 1 776 . 81 SER C C 175.300 0.1 1 777 . 81 SER CB C 63.528 0.1 1 778 . 81 SER N N 116.586 0.05 1 779 . 81 SER HB3 H 3.920 0.05 1 780 . 81 SER HB2 H 3.920 0.05 1 781 . 81 SER HA H 4.340 0.05 1 782 . 81 SER H H 8.324 0.05 1 783 . 82 GLU CA C 58.746 0.1 1 784 . 82 GLU C C 177.940 0.1 1 785 . 82 GLU CB C 29.258 0.1 1 786 . 82 GLU CG C 36.282 0.1 1 787 . 82 GLU N N 122.059 0.05 1 788 . 82 GLU HG3 H 2.250 0.05 1 789 . 82 GLU HG2 H 2.250 0.05 1 790 . 82 GLU HB3 H 2.030 0.05 1 791 . 82 GLU HB2 H 2.030 0.05 1 792 . 82 GLU HA H 4.030 0.05 1 793 . 82 GLU H H 8.399 0.05 1 794 . 83 GLU CA C 59.418 0.1 1 795 . 83 GLU C C 175.540 0.1 1 796 . 83 GLU CB C 29.234 0.1 1 797 . 83 GLU N N 118.992 0.05 1 798 . 83 GLU HA H 4.380 0.05 1 799 . 83 GLU H H 8.199 0.05 1 800 . 84 GLU CA C 55.216 0.1 1 801 . 84 GLU C C 175.520 0.1 1 802 . 84 GLU CB C 29.293 0.1 1 803 . 84 GLU CG C 33.422 0.1 1 804 . 84 GLU N N 119.054 0.05 1 805 . 84 GLU HG3 H 2.258 0.05 1 806 . 84 GLU HG2 H 2.258 0.05 1 807 . 84 GLU HB3 H 1.840 0.05 1 808 . 84 GLU HB2 H 1.840 0.05 1 809 . 84 GLU HA H 4.259 0.05 1 810 . 84 GLU H H 8.231 0.05 1 811 . 86 ARG CA C 58.637 0.1 1 812 . 86 ARG CB C 28.857 0.1 1 813 . 86 ARG HB3 H 1.984 0.05 1 814 . 86 ARG HB2 H 1.984 0.05 1 815 . 86 ARG HA H 3.997 0.05 1 816 . 87 GLU CA C 58.899 0.1 1 817 . 87 GLU C C 178.970 0.1 1 818 . 87 GLU CB C 32.642 0.1 1 819 . 87 GLU CG C 39.402 0.1 1 820 . 87 GLU N N 120.531 0.05 1 821 . 87 GLU HB3 H 1.810 0.05 1 822 . 87 GLU HB2 H 1.810 0.05 1 823 . 87 GLU HA H 4.030 0.05 1 824 . 87 GLU H H 7.891 0.05 1 825 . 88 ALA CA C 55.234 0.1 1 826 . 88 ALA C C 178.910 0.1 1 827 . 88 ALA CB C 17.583 0.1 1 828 . 88 ALA N N 118.364 0.05 1 829 . 88 ALA HB H 1.800 0.05 1 830 . 88 ALA HA H 4.050 0.05 1 831 . 88 ALA H H 8.434 0.05 1 832 . 89 PHE CA C 62.357 0.1 1 833 . 89 PHE C C 176.220 0.1 1 834 . 89 PHE CB C 38.751 0.1 1 835 . 89 PHE N N 118.039 0.05 1 836 . 89 PHE HB3 H 2.900 0.05 1 837 . 89 PHE HB2 H 2.900 0.05 1 838 . 89 PHE HA H 3.130 0.05 1 839 . 89 PHE H H 8.448 0.05 1 840 . 90 ARG CA C 58.463 0.1 1 841 . 90 ARG C C 177.660 0.1 1 842 . 90 ARG CB C 29.755 0.1 1 843 . 90 ARG CG C 27.443 0.1 1 844 . 90 ARG CD C 43.301 0.1 1 845 . 90 ARG N N 114.095 0.05 1 846 . 90 ARG HD3 H 3.140 0.05 1 847 . 90 ARG HD2 H 3.140 0.05 1 848 . 90 ARG HG3 H 1.640 0.05 1 849 . 90 ARG HG2 H 1.640 0.05 1 850 . 90 ARG HB3 H 1.860 0.05 1 851 . 90 ARG HB2 H 1.860 0.05 1 852 . 90 ARG HA H 3.790 0.05 1 853 . 90 ARG H H 7.605 0.05 1 854 . 91 VAL CA C 65.631 0.1 1 855 . 91 VAL C C 176.690 0.1 1 856 . 91 VAL CB C 30.757 0.1 1 857 . 91 VAL CG1 C 22.243 0.1 1 858 . 91 VAL CG2 C 20.684 0.1 1 859 . 91 VAL N N 117.981 0.05 1 860 . 91 VAL HG2 H 0.488 0.05 2 861 . 91 VAL HG1 H 0.904 0.05 2 862 . 91 VAL HB H 1.990 0.05 1 863 . 91 VAL HA H 3.360 0.05 1 864 . 91 VAL H H 7.269 0.05 1 865 . 92 PHE CA C 61.073 0.1 1 866 . 92 PHE C C 176.010 0.1 1 867 . 92 PHE CB C 40.782 0.1 1 868 . 92 PHE N N 113.887 0.05 1 869 . 92 PHE HD2 H 7.118 0.05 1 870 . 92 PHE HD1 H 7.118 0.05 1 871 . 92 PHE HB3 H 2.440 0.05 2 872 . 92 PHE HB2 H 2.740 0.05 2 873 . 92 PHE HA H 4.140 0.05 1 874 . 92 PHE H H 6.923 0.05 1 875 . 93 ASP CA C 51.682 0.1 1 876 . 93 ASP C C 177.710 0.1 1 877 . 93 ASP CB C 37.927 0.1 1 878 . 93 ASP N N 114.002 0.05 1 879 . 93 ASP HB3 H 1.200 0.05 2 880 . 93 ASP HB2 H 2.110 0.05 2 881 . 93 ASP HA H 4.470 0.05 1 882 . 93 ASP H H 7.768 0.05 1 883 . 94 LYS CA C 59.213 0.1 1 884 . 94 LYS C C 178.210 0.1 1 885 . 94 LYS CB C 32.442 0.1 1 886 . 94 LYS CG C 23.543 0.1 1 887 . 94 LYS CD C 28.483 0.1 1 888 . 94 LYS CE C 40.182 0.1 1 889 . 94 LYS N N 124.816 0.05 1 890 . 94 LYS HG3 H 1.405 0.05 1 891 . 94 LYS HG2 H 1.405 0.05 1 892 . 94 LYS HB3 H 1.690 0.05 1 893 . 94 LYS HB2 H 1.690 0.05 1 894 . 94 LYS HA H 3.770 0.05 1 895 . 94 LYS H H 7.534 0.05 1 896 . 95 ASP CA C 52.985 0.1 1 897 . 95 ASP C C 177.810 0.1 1 898 . 95 ASP CB C 39.477 0.1 1 899 . 95 ASP N N 113.652 0.05 1 900 . 95 ASP HB3 H 2.590 0.05 2 901 . 95 ASP HB2 H 3.000 0.05 2 902 . 95 ASP HA H 4.450 0.05 1 903 . 95 ASP H H 8.363 0.05 1 904 . 96 GLY CA C 46.884 0.1 1 905 . 96 GLY C C 175.100 0.1 1 906 . 96 GLY N N 108.862 0.05 1 907 . 96 GLY HA3 H 3.760 0.05 1 908 . 96 GLY HA2 H 3.760 0.05 1 909 . 96 GLY H H 7.783 0.05 1 910 . 97 ASN CA C 53.083 0.1 1 911 . 97 ASN C C 175.980 0.1 1 912 . 97 ASN CB C 37.831 0.1 1 913 . 97 ASN N N 119.368 0.05 1 914 . 97 ASN HB3 H 2.600 0.05 2 915 . 97 ASN HB2 H 3.320 0.05 2 916 . 97 ASN HA H 4.570 0.05 1 917 . 97 ASN H H 8.301 0.05 1 918 . 98 GLY CA C 44.786 0.1 1 919 . 98 GLY C C 172.680 0.1 1 920 . 98 GLY N N 112.396 0.05 1 921 . 98 GLY HA3 H 3.390 0.05 2 922 . 98 GLY HA2 H 4.040 0.05 2 923 . 98 GLY H H 10.657 0.05 1 924 . 99 TYR CA C 56.136 0.1 1 925 . 99 TYR C C 174.560 0.1 1 926 . 99 TYR CB C 42.335 0.1 1 927 . 99 TYR CD1 C 132.462 0.1 1 928 . 99 TYR CE1 C 118.791 0.1 1 929 . 99 TYR CE2 C 118.791 0.1 1 930 . 99 TYR CD2 C 132.462 0.1 1 931 . 99 TYR N N 115.917 0.05 1 932 . 99 TYR HD2 H 6.654 0.05 1 933 . 99 TYR HE2 H 6.790 0.05 1 934 . 99 TYR HE1 H 6.790 0.05 1 935 . 99 TYR HD1 H 6.654 0.05 1 936 . 99 TYR HB3 H 2.412 0.05 2 937 . 99 TYR HB2 H 2.480 0.05 2 938 . 99 TYR HA H 4.910 0.05 1 939 . 99 TYR H H 7.616 0.05 1 940 . 100 ILE CA C 61.234 0.1 1 941 . 100 ILE C C 175.500 0.1 1 942 . 100 ILE CB C 39.141 0.1 1 943 . 100 ILE CG1 C 26.143 0.1 1 944 . 100 ILE CG2 C 17.564 0.1 1 945 . 100 ILE N N 127.027 0.05 1 946 . 100 ILE HD1 H 0.473 0.05 1 947 . 100 ILE HG2 H 0.913 0.05 1 948 . 100 ILE HG13 H 1.270 0.05 2 949 . 100 ILE HG12 H 0.090 0.05 2 950 . 100 ILE HB H 1.870 0.05 1 951 . 100 ILE HA H 4.570 0.05 1 952 . 100 ILE H H 10.033 0.05 1 953 . 101 SER CA C 55.609 0.1 1 954 . 101 SER C C 174.960 0.1 1 955 . 101 SER CB C 66.615 0.1 1 956 . 101 SER N N 123.351 0.05 1 957 . 101 SER HB3 H 3.900 0.05 2 958 . 101 SER HB2 H 4.390 0.05 2 959 . 101 SER HA H 4.880 0.05 1 960 . 101 SER H H 8.868 0.05 1 961 . 102 ALA CA C 55.746 0.1 1 962 . 102 ALA C C 179.200 0.1 1 963 . 102 ALA CB C 17.571 0.1 1 964 . 102 ALA N N 122.815 0.05 1 965 . 102 ALA HB H 1.370 0.05 1 966 . 102 ALA HA H 3.805 0.05 1 967 . 102 ALA H H 9.265 0.05 1 968 . 103 ALA CA C 55.162 0.1 1 969 . 103 ALA C C 180.980 0.1 1 970 . 103 ALA CB C 17.861 0.1 1 971 . 103 ALA N N 117.886 0.05 1 972 . 103 ALA HB H 1.350 0.05 1 973 . 103 ALA HA H 3.960 0.05 1 974 . 103 ALA H H 8.152 0.05 1 975 . 104 GLU CA C 59.238 0.1 1 976 . 104 GLU C C 179.020 0.1 1 977 . 104 GLU CB C 28.788 0.1 1 978 . 104 GLU CG C 37.842 0.1 1 979 . 104 GLU N N 119.063 0.05 1 980 . 104 GLU HG3 H 2.280 0.05 1 981 . 104 GLU HG2 H 2.280 0.05 1 982 . 104 GLU HB3 H 1.890 0.05 1 983 . 104 GLU HB2 H 1.890 0.05 1 984 . 104 GLU HA H 4.050 0.05 1 985 . 104 GLU H H 7.665 0.05 1 986 . 105 LEU CA C 58.322 0.1 1 987 . 105 LEU C C 178.500 0.1 1 988 . 105 LEU CB C 42.329 0.1 1 989 . 105 LEU CG C 26.670 0.1 1 990 . 105 LEU CD1 C 25.880 0.1 1 991 . 105 LEU CD2 C 24.583 0.1 1 992 . 105 LEU N N 119.904 0.05 1 993 . 105 LEU HD2 H 0.470 0.05 2 994 . 105 LEU HD1 H 0.540 0.05 2 995 . 105 LEU HG H 1.240 0.05 1 996 . 105 LEU HB3 H 1.644 0.05 2 997 . 105 LEU HB2 H 1.434 0.05 2 998 . 105 LEU HA H 3.910 0.05 1 999 . 105 LEU H H 8.570 0.05 1 1000 . 106 ARG CA C 59.784 0.1 1 1001 . 106 ARG C C 178.840 0.1 1 1002 . 106 ARG CB C 30.167 0.1 1 1003 . 106 ARG CG C 27.443 0.1 1 1004 . 106 ARG CD C 43.561 0.1 1 1005 . 106 ARG N N 116.322 0.05 1 1006 . 106 ARG HD3 H 3.140 0.05 1 1007 . 106 ARG HD2 H 3.140 0.05 1 1008 . 106 ARG HG3 H 1.500 0.05 1 1009 . 106 ARG HG2 H 1.500 0.05 1 1010 . 106 ARG HB3 H 1.840 0.05 1 1011 . 106 ARG HB2 H 1.840 0.05 1 1012 . 106 ARG HA H 3.640 0.05 1 1013 . 106 ARG H H 8.340 0.05 1 1014 . 107 HIS CA C 59.809 0.1 1 1015 . 107 HIS C C 177.740 0.1 1 1016 . 107 HIS CB C 30.439 0.1 1 1017 . 107 HIS N N 119.391 0.05 1 1018 . 107 HIS HB3 H 3.230 0.05 2 1019 . 107 HIS HB2 H 3.130 0.05 2 1020 . 107 HIS HA H 4.170 0.05 1 1021 . 107 HIS H H 7.837 0.05 1 1022 . 108 VAL CA C 66.864 0.1 1 1023 . 108 VAL C C 178.480 0.1 1 1024 . 108 VAL CB C 31.863 0.1 1 1025 . 108 VAL CG1 C 23.543 0.1 1 1026 . 108 VAL CG2 C 20.684 0.1 1 1027 . 108 VAL N N 119.487 0.05 1 1028 . 108 VAL HG2 H 0.440 0.05 2 1029 . 108 VAL HG1 H 1.180 0.05 2 1030 . 108 VAL HB H 2.030 0.05 1 1031 . 108 VAL HA H 3.450 0.05 1 1032 . 108 VAL H H 8.906 0.05 1 1033 . 109 MET CA C 57.554 0.1 1 1034 . 109 MET C C 178.870 0.1 1 1035 . 109 MET CB C 29.820 0.1 1 1036 . 109 MET CG C 33.519 0.1 1 1037 . 109 MET CE C 15.921 0.1 1 1038 . 109 MET N N 114.866 0.05 1 1039 . 109 MET HE H 1.788 0.05 1 1040 . 109 MET HG3 H 2.599 0.05 2 1041 . 109 MET HG2 H 2.506 0.05 2 1042 . 109 MET HB3 H 1.850 0.05 2 1043 . 109 MET HB2 H 2.060 0.05 2 1044 . 109 MET HA H 4.210 0.05 1 1045 . 109 MET H H 8.453 0.05 1 1046 . 110 THR CA C 66.676 0.1 1 1047 . 110 THR C C 178.260 0.1 1 1048 . 110 THR CB C 68.385 0.1 1 1049 . 110 THR N N 114.900 0.05 1 1050 . 110 THR HG2 H 1.120 0.05 1 1051 . 110 THR HB H 4.210 0.05 1 1052 . 110 THR HA H 3.930 0.05 1 1053 . 110 THR H H 7.765 0.05 1 1054 . 111 ASN CA C 56.007 0.1 1 1055 . 111 ASN C C 176.630 0.1 1 1056 . 111 ASN CB C 37.988 0.1 1 1057 . 111 ASN ND2 N 110.936 0.05 1 1058 . 111 ASN N N 122.422 0.05 1 1059 . 111 ASN HD22 H 7.238 0.05 1 1060 . 111 ASN HD21 H 6.388 0.05 1 1061 . 111 ASN HB3 H 2.700 0.05 1 1062 . 111 ASN HB2 H 2.700 0.05 1 1063 . 111 ASN HA H 4.260 0.05 1 1064 . 111 ASN H H 7.834 0.05 1 1065 . 112 LEU CA C 55.197 0.1 1 1066 . 112 LEU C C 176.660 0.1 1 1067 . 112 LEU CB C 41.748 0.1 1 1068 . 112 LEU CG C 26.143 0.1 1 1069 . 112 LEU CD1 C 21.724 0.1 1 1070 . 112 LEU CD2 C 21.724 0.1 1 1071 . 112 LEU N N 117.907 0.05 1 1072 . 112 LEU HG H 1.830 0.05 1 1073 . 112 LEU HB3 H 1.490 0.05 2 1074 . 112 LEU HB2 H 1.830 0.05 2 1075 . 112 LEU HA H 4.230 0.05 1 1076 . 112 LEU H H 7.797 0.05 1 1077 . 113 GLY CA C 44.895 0.1 1 1078 . 113 GLY C C 173.990 0.1 1 1079 . 113 GLY N N 105.014 0.05 1 1080 . 113 GLY HA3 H 3.580 0.05 2 1081 . 113 GLY HA2 H 4.220 0.05 2 1082 . 113 GLY H H 7.609 0.05 1 1083 . 114 GLU CA C 54.414 0.1 1 1084 . 114 GLU C C 174.210 0.1 1 1085 . 114 GLU CB C 29.642 0.1 1 1086 . 114 GLU CG C 34.722 0.1 1 1087 . 114 GLU N N 120.417 0.05 1 1088 . 114 GLU HG3 H 1.820 0.05 1 1089 . 114 GLU HG2 H 1.820 0.05 1 1090 . 114 GLU HB3 H 1.520 0.05 1 1091 . 114 GLU HB2 H 1.520 0.05 1 1092 . 114 GLU HA H 4.260 0.05 1 1093 . 114 GLU H H 7.952 0.05 1 1094 . 115 LYS CA C 55.620 0.1 1 1095 . 115 LYS C C 175.470 0.1 1 1096 . 115 LYS CB C 31.377 0.1 1 1097 . 115 LYS CG C 24.323 0.1 1 1098 . 115 LYS CD C 29.003 0.1 1 1099 . 115 LYS CE C 41.742 0.1 1 1100 . 115 LYS N N 123.699 0.05 1 1101 . 115 LYS HG3 H 1.220 0.05 1 1102 . 115 LYS HG2 H 1.220 0.05 1 1103 . 115 LYS HB3 H 1.600 0.05 1 1104 . 115 LYS HB2 H 1.600 0.05 1 1105 . 115 LYS HA H 4.190 0.05 1 1106 . 115 LYS H H 8.252 0.05 1 1107 . 116 LEU CA C 53.793 0.1 1 1108 . 116 LEU C C 178.130 0.1 1 1109 . 116 LEU CB C 44.405 0.1 1 1110 . 116 LEU CG C 27.703 0.1 1 1111 . 116 LEU CD1 C 26.923 0.1 1 1112 . 116 LEU CD2 C 26.923 0.1 1 1113 . 116 LEU N N 124.420 0.05 1 1114 . 116 LEU HG H 0.618 0.05 1 1115 . 116 LEU HB3 H 1.470 0.05 1 1116 . 116 LEU HB2 H 1.470 0.05 1 1117 . 116 LEU HA H 4.670 0.05 1 1118 . 116 LEU H H 7.983 0.05 1 1119 . 117 THR CA C 60.318 0.1 1 1120 . 117 THR C C 175.440 0.1 1 1121 . 117 THR CB C 71.169 0.1 1 1122 . 117 THR N N 113.414 0.05 1 1123 . 117 THR HG2 H 1.200 0.05 1 1124 . 117 THR HB H 4.680 0.05 1 1125 . 117 THR HA H 4.400 0.05 1 1126 . 117 THR H H 9.072 0.05 1 1127 . 118 ASP CA C 57.787 0.1 1 1128 . 118 ASP C C 178.590 0.1 1 1129 . 118 ASP CB C 39.446 0.1 1 1130 . 118 ASP N N 120.273 0.05 1 1131 . 118 ASP HB3 H 2.490 0.05 2 1132 . 118 ASP HB2 H 2.630 0.05 2 1133 . 118 ASP HA H 4.140 0.05 1 1134 . 118 ASP H H 8.746 0.05 1 1135 . 119 GLU CA C 59.470 0.1 1 1136 . 119 GLU C C 179.030 0.1 1 1137 . 119 GLU CB C 28.789 0.1 1 1138 . 119 GLU CG C 36.542 0.1 1 1139 . 119 GLU N N 118.618 0.05 1 1140 . 119 GLU HG3 H 2.250 0.05 1 1141 . 119 GLU HG2 H 2.250 0.05 1 1142 . 119 GLU HB3 H 1.860 0.05 1 1143 . 119 GLU HB2 H 1.860 0.05 1 1144 . 119 GLU HA H 3.990 0.05 1 1145 . 119 GLU H H 8.403 0.05 1 1146 . 120 GLU CA C 59.429 0.1 1 1147 . 120 GLU C C 179.350 0.1 1 1148 . 120 GLU CB C 29.913 0.1 1 1149 . 120 GLU CG C 36.542 0.1 1 1150 . 120 GLU N N 120.029 0.05 1 1151 . 120 GLU HG3 H 2.260 0.05 1 1152 . 120 GLU HG2 H 2.260 0.05 1 1153 . 120 GLU HB3 H 1.910 0.05 1 1154 . 120 GLU HB2 H 1.910 0.05 1 1155 . 120 GLU HA H 3.970 0.05 1 1156 . 120 GLU H H 7.525 0.05 1 1157 . 121 VAL CA C 64.606 0.1 1 1158 . 121 VAL C C 177.920 0.1 1 1159 . 121 VAL CB C 36.979 0.1 1 1160 . 121 VAL CG1 C 18.604 0.1 1 1161 . 121 VAL CG2 C 28.743 0.1 1 1162 . 121 VAL N N 120.504 0.05 1 1163 . 121 VAL HG2 H 0.659 0.05 2 1164 . 121 VAL HG1 H 1.040 0.05 2 1165 . 121 VAL HB H 2.100 0.05 1 1166 . 121 VAL HA H 3.880 0.05 1 1167 . 121 VAL H H 7.791 0.05 1 1168 . 122 ASP CA C 60.017 0.1 1 1169 . 122 ASP C C 179.130 0.1 1 1170 . 122 ASP CB C 29.505 0.1 1 1171 . 122 ASP N N 120.998 0.05 1 1172 . 122 ASP HB3 H 1.790 0.05 2 1173 . 122 ASP HB2 H 2.020 0.05 2 1174 . 122 ASP HA H 4.050 0.05 1 1175 . 122 ASP H H 8.322 0.05 1 1176 . 123 GLU CA C 59.420 0.1 1 1177 . 123 GLU C C 178.500 0.1 1 1178 . 123 GLU CB C 29.003 0.1 1 1179 . 123 GLU CG C 35.762 0.1 1 1180 . 123 GLU N N 117.405 0.05 1 1181 . 123 GLU HG3 H 2.270 0.05 1 1182 . 123 GLU HG2 H 2.270 0.05 1 1183 . 123 GLU HB3 H 2.020 0.05 1 1184 . 123 GLU HB2 H 2.020 0.05 1 1185 . 123 GLU HA H 4.030 0.05 1 1186 . 123 GLU H H 8.125 0.05 1 1187 . 124 MET CA C 59.420 0.1 1 1188 . 124 MET C C 180.090 0.1 1 1189 . 124 MET CB C 29.102 0.1 1 1190 . 124 MET CG C 33.850 0.1 1 1191 . 124 MET CE C 14.850 0.1 1 1192 . 124 MET N N 117.961 0.05 1 1193 . 124 MET HE H 0.419 0.05 1 1194 . 124 MET HB3 H 2.040 0.05 1 1195 . 124 MET HB2 H 2.040 0.05 1 1196 . 124 MET H H 8.021 0.05 1 1197 . 125 ILE CA C 64.020 0.1 1 1198 . 125 ILE C C 177.380 0.1 1 1199 . 125 ILE CB C 35.762 0.1 1 1200 . 125 ILE CG1 C 27.443 0.1 1 1201 . 125 ILE CG2 C 16.524 0.1 1 1202 . 125 ILE N N 119.873 0.05 1 1203 . 125 ILE HD1 H 0.672 0.05 1 1204 . 125 ILE HG2 H 0.672 0.05 1 1205 . 125 ILE HG13 H 1.310 0.05 2 1206 . 125 ILE HG12 H 1.500 0.05 2 1207 . 125 ILE HB H 2.130 0.05 1 1208 . 125 ILE HA H 3.630 0.05 1 1209 . 125 ILE H H 7.991 0.05 1 1210 . 126 ARG CA C 59.457 0.1 1 1211 . 126 ARG C C 178.870 0.1 1 1212 . 126 ARG CB C 29.895 0.1 1 1213 . 126 ARG CG C 27.703 0.1 1 1214 . 126 ARG CD C 43.301 0.1 1 1215 . 126 ARG N N 117.804 0.05 1 1216 . 126 ARG HD3 H 3.220 0.05 1 1217 . 126 ARG HD2 H 3.220 0.05 1 1218 . 126 ARG HG3 H 1.570 0.05 1 1219 . 126 ARG HG2 H 1.570 0.05 1 1220 . 126 ARG HB3 H 1.800 0.05 1 1221 . 126 ARG HB2 H 1.800 0.05 1 1222 . 126 ARG HA H 3.940 0.05 1 1223 . 126 ARG H H 8.558 0.05 1 1224 . 127 GLU CA C 58.067 0.1 1 1225 . 127 GLU C C 176.280 0.1 1 1226 . 127 GLU CB C 29.646 0.1 1 1227 . 127 GLU CG C 35.242 0.1 1 1228 . 127 GLU N N 115.002 0.05 1 1229 . 127 GLU HG3 H 2.280 0.05 1 1230 . 127 GLU HG2 H 2.280 0.05 1 1231 . 127 GLU HB3 H 2.060 0.05 1 1232 . 127 GLU HB2 H 2.060 0.05 1 1233 . 127 GLU HA H 3.930 0.05 1 1234 . 127 GLU H H 7.784 0.05 1 1235 . 128 ALA CA C 51.427 0.1 1 1236 . 128 ALA C C 177.680 0.1 1 1237 . 128 ALA CB C 21.725 0.1 1 1238 . 128 ALA N N 115.779 0.05 1 1239 . 128 ALA HB H 1.140 0.05 1 1240 . 128 ALA HA H 4.370 0.05 1 1241 . 128 ALA H H 6.994 0.05 1 1242 . 129 ASP CA C 54.158 0.1 1 1243 . 129 ASP C C 175.730 0.1 1 1244 . 129 ASP CB C 39.876 0.1 1 1245 . 129 ASP N N 116.908 0.05 1 1246 . 129 ASP HB3 H 2.410 0.05 2 1247 . 129 ASP HB2 H 2.730 0.05 2 1248 . 129 ASP HA H 4.380 0.05 1 1249 . 129 ASP H H 8.222 0.05 1 1250 . 130 ILE CA C 63.097 0.1 1 1251 . 130 ILE C C 177.680 0.1 1 1252 . 130 ILE CB C 38.707 0.1 1 1253 . 130 ILE CG1 C 27.443 0.1 1 1254 . 130 ILE CG2 C 17.044 0.1 1 1255 . 130 ILE N N 127.534 0.05 1 1256 . 130 ILE HD1 H 0.795 0.05 1 1257 . 130 ILE HG2 H 1.160 0.05 1 1258 . 130 ILE HG13 H 1.590 0.05 1 1259 . 130 ILE HG12 H 1.590 0.05 1 1260 . 130 ILE HB H 1.870 0.05 1 1261 . 130 ILE HA H 3.870 0.05 1 1262 . 130 ILE H H 8.287 0.05 1 1263 . 131 ASP CA C 53.889 0.1 1 1264 . 131 ASP C C 178.190 0.1 1 1265 . 131 ASP CB C 39.585 0.1 1 1266 . 131 ASP N N 116.362 0.05 1 1267 . 131 ASP HB3 H 2.570 0.05 2 1268 . 131 ASP HB2 H 2.980 0.05 2 1269 . 131 ASP HA H 4.420 0.05 1 1270 . 131 ASP H H 8.226 0.05 1 1271 . 132 GLY CA C 47.318 0.1 1 1272 . 132 GLY C C 175.120 0.1 1 1273 . 132 GLY N N 107.942 0.05 1 1274 . 132 GLY HA3 H 3.730 0.05 2 1275 . 132 GLY HA2 H 3.910 0.05 2 1276 . 132 GLY H H 7.569 0.05 1 1277 . 133 ASP CA C 53.536 0.1 1 1278 . 133 ASP C C 177.480 0.1 1 1279 . 133 ASP CB C 39.908 0.1 1 1280 . 133 ASP N N 120.090 0.05 1 1281 . 133 ASP HB3 H 2.430 0.05 2 1282 . 133 ASP HB2 H 2.890 0.05 2 1283 . 133 ASP HA H 4.400 0.05 1 1284 . 133 ASP H H 8.253 0.05 1 1285 . 134 GLY CA C 45.695 0.1 1 1286 . 134 GLY C C 172.580 0.1 1 1287 . 134 GLY N N 111.850 0.05 1 1288 . 134 GLY HA3 H 3.330 0.05 2 1289 . 134 GLY HA2 H 3.960 0.05 2 1290 . 134 GLY H H 10.047 0.05 1 1291 . 135 GLN CA C 53.055 0.1 1 1292 . 135 GLN C C 175.060 0.1 1 1293 . 135 GLN CB C 32.490 0.1 1 1294 . 135 GLN CG C 32.490 0.1 1 1295 . 135 GLN N N 114.774 0.05 1 1296 . 135 GLN HE22 H 6.437 0.05 1 1297 . 135 GLN HE21 H 5.900 0.05 1 1298 . 135 GLN HG3 H 1.930 0.05 1 1299 . 135 GLN HG2 H 1.930 0.05 1 1300 . 135 GLN HB3 H 1.710 0.05 2 1301 . 135 GLN HB2 H 1.930 0.05 2 1302 . 135 GLN HA H 4.930 0.05 1 1303 . 135 GLN H H 7.952 0.05 1 1304 . 136 VAL CA C 61.523 0.1 1 1305 . 136 VAL C C 175.670 0.1 1 1306 . 136 VAL CB C 33.208 0.1 1 1307 . 136 VAL CG1 C 21.724 0.1 1 1308 . 136 VAL CG2 C 21.724 0.1 1 1309 . 136 VAL N N 124.739 0.05 1 1310 . 136 VAL HG2 H 0.991 0.05 1 1311 . 136 VAL HG1 H 0.991 0.05 1 1312 . 136 VAL HB H 2.280 0.05 1 1313 . 136 VAL HA H 5.100 0.05 1 1314 . 136 VAL H H 9.039 0.05 1 1315 . 137 ASN CA C 50.883 0.1 1 1316 . 137 ASN C C 174.690 0.1 1 1317 . 137 ASN CB C 38.214 0.1 1 1318 . 137 ASN ND2 N 110.672 0.05 1 1319 . 137 ASN N N 128.576 0.05 1 1320 . 137 ASN HD22 H 7.361 0.05 1 1321 . 137 ASN HD21 H 6.640 0.05 1 1322 . 137 ASN HB3 H 2.820 0.05 2 1323 . 137 ASN HB2 H 3.100 0.05 2 1324 . 137 ASN HA H 5.280 0.05 1 1325 . 137 ASN H H 9.446 0.05 1 1326 . 138 TYR CA C 62.226 0.1 1 1327 . 138 TYR C C 175.950 0.1 1 1328 . 138 TYR CB C 37.619 0.1 1 1329 . 138 TYR CD1 C 133.351 0.1 1 1330 . 138 TYR CE1 C 118.612 0.1 1 1331 . 138 TYR CE2 C 118.612 0.1 1 1332 . 138 TYR CD2 C 133.351 0.1 1 1333 . 138 TYR N N 118.140 0.05 1 1334 . 138 TYR HD2 H 6.140 0.05 1 1335 . 138 TYR HE2 H 6.369 0.05 1 1336 . 138 TYR HE1 H 6.369 0.05 1 1337 . 138 TYR HD1 H 6.140 0.05 1 1338 . 138 TYR HB3 H 1.942 0.05 2 1339 . 138 TYR HB2 H 2.285 0.05 2 1340 . 138 TYR HA H 3.141 0.05 1 1341 . 138 TYR H H 8.227 0.05 1 1342 . 139 GLU CA C 60.108 0.1 1 1343 . 139 GLU C C 180.250 0.1 1 1344 . 139 GLU CB C 28.546 0.1 1 1345 . 139 GLU CG C 36.542 0.1 1 1346 . 139 GLU N N 117.825 0.05 1 1347 . 139 GLU HG3 H 2.220 0.05 1 1348 . 139 GLU HG2 H 2.220 0.05 1 1349 . 139 GLU HB3 H 1.850 0.05 2 1350 . 139 GLU HB2 H 1.940 0.05 2 1351 . 139 GLU HA H 3.530 0.05 1 1352 . 139 GLU H H 7.957 0.05 1 1353 . 140 GLU CA C 58.683 0.1 1 1354 . 140 GLU C C 179.220 0.1 1 1355 . 140 GLU CB C 28.736 0.1 1 1356 . 140 GLU CG C 36.802 0.1 1 1357 . 140 GLU N N 119.137 0.05 1 1358 . 140 GLU HG3 H 2.210 0.05 1 1359 . 140 GLU HG2 H 2.210 0.05 1 1360 . 140 GLU HB3 H 1.900 0.05 1 1361 . 140 GLU HB2 H 1.900 0.05 1 1362 . 140 GLU HA H 3.780 0.05 1 1363 . 140 GLU H H 8.578 0.05 1 1364 . 141 PHE CA C 61.901 0.1 1 1365 . 141 PHE C C 176.420 0.1 1 1366 . 141 PHE CB C 39.964 0.1 1 1367 . 141 PHE N N 123.219 0.05 1 1368 . 141 PHE HD2 H 6.530 0.05 1 1369 . 141 PHE HE2 H 7.070 0.05 1 1370 . 141 PHE HE1 H 7.070 0.05 1 1371 . 141 PHE HD1 H 6.530 0.05 1 1372 . 141 PHE HB3 H 2.820 0.05 2 1373 . 141 PHE HB2 H 3.070 0.05 2 1374 . 141 PHE HA H 3.148 0.05 1 1375 . 141 PHE H H 8.442 0.05 1 1376 . 142 VAL CA C 66.714 0.1 1 1377 . 142 VAL CB C 31.019 0.1 1 1378 . 142 VAL N N 118.254 0.05 1 1379 . 142 VAL HG2 H 0.343 0.05 2 1380 . 142 VAL HG1 H 0.616 0.05 2 1381 . 142 VAL HB H 1.630 0.05 1 1382 . 142 VAL HA H 3.000 0.05 1 1383 . 142 VAL H H 8.534 0.05 1 1384 . 143 GLN CA C 58.639 0.1 1 1385 . 143 GLN C C 177.760 0.1 1 1386 . 143 GLN CB C 27.703 0.1 1 1387 . 143 GLN CG C 33.682 0.1 1 1388 . 143 GLN HG3 H 2.284 0.05 1 1389 . 143 GLN HG2 H 2.284 0.05 1 1390 . 143 GLN HB3 H 1.915 0.05 1 1391 . 143 GLN HB2 H 1.915 0.05 1 1392 . 143 GLN HA H 3.713 0.05 1 1393 . 144 MET CA C 57.204 0.1 1 1394 . 144 MET C C 177.430 0.1 1 1395 . 144 MET CB C 30.770 0.1 1 1396 . 144 MET CG C 30.546 0.1 1 1397 . 144 MET CE C 15.952 0.1 1 1398 . 144 MET N N 117.527 0.05 1 1399 . 144 MET HE H 1.037 0.05 1 1400 . 144 MET HB3 H 1.600 0.05 1 1401 . 144 MET HB2 H 1.600 0.05 1 1402 . 144 MET HA H 4.060 0.05 1 1403 . 144 MET H H 7.320 0.05 1 1404 . 145 MET CA C 57.013 0.1 1 1405 . 145 MET C C 177.440 0.1 1 1406 . 145 MET CB C 31.108 0.1 1 1407 . 145 MET CG C 31.097 0.1 1 1408 . 145 MET CE C 17.536 0.1 1 1409 . 145 MET N N 113.501 0.05 1 1410 . 145 MET HE H 1.561 0.05 1 1411 . 145 MET HB3 H 1.700 0.05 1 1412 . 145 MET HB2 H 1.700 0.05 1 1413 . 145 MET HA H 4.050 0.05 1 1414 . 145 MET H H 7.519 0.05 1 1415 . 146 THR CA C 61.952 0.1 1 1416 . 146 THR C C 174.060 0.1 1 1417 . 146 THR CB C 70.084 0.1 1 1418 . 146 THR N N 108.316 0.05 1 1419 . 146 THR HG2 H 1.060 0.05 1 1420 . 146 THR HB H 4.220 0.05 1 1421 . 146 THR HA H 4.220 0.05 1 1422 . 146 THR H H 7.480 0.05 1 1423 . 147 ALA CA C 52.711 0.1 1 1424 . 147 ALA C C 176.350 0.1 1 1425 . 147 ALA CB C 18.575 0.1 1 1426 . 147 ALA N N 125.837 0.05 1 1427 . 147 ALA HB H 1.350 0.05 1 1428 . 147 ALA HA H 4.230 0.05 1 1429 . 147 ALA H H 7.465 0.05 1 1430 . 148 LYS CA C 57.451 0.1 1 1431 . 148 LYS CB C 33.389 0.1 1 1432 . 148 LYS N N 125.094 0.05 1 1433 . 148 LYS HE3 H 2.800 0.05 1 1434 . 148 LYS HE2 H 2.800 0.05 1 1435 . 148 LYS HD3 H 1.640 0.05 1 1436 . 148 LYS HD2 H 1.640 0.05 1 1437 . 148 LYS HG3 H 1.290 0.05 1 1438 . 148 LYS HG2 H 1.290 0.05 1 1439 . 148 LYS HB3 H 1.510 0.05 1 1440 . 148 LYS HB2 H 1.510 0.05 1 1441 . 148 LYS HA H 3.950 0.05 1 1442 . 148 LYS H H 7.612 0.05 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name C20W _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 . 4 GLY H H 7.84 0.05 1 2 . 4 GLY HA2 H 4.06 0.05 2 3 . 4 GLY HA3 H 3.56 0.05 2 4 . 5 GLN H H 8.00 0.05 1 5 . 5 GLN HA H 4.03 0.05 1 6 . 5 GLN HG2 H 2.05 0.05 2 7 . 5 GLN HG3 H 1.99 0.05 2 8 . 5 GLN HE21 H 7.58 0.05 1 9 . 5 GLN HE22 H 6.72 0.05 1 10 . 6 ILE H H 7.70 0.05 1 11 . 6 ILE HA H 3.73 0.05 1 12 . 6 ILE HB H 1.84 0.05 1 13 . 6 ILE HG12 H 1.57 0.05 1 14 . 6 ILE HG13 H 1.57 0.05 1 15 . 6 ILE HG2 H 0.76 0.05 1 16 . 6 ILE HD1 H 0.57 0.05 1 17 . 7 LEU H H 7.52 0.05 1 18 . 7 LEU HA H 4.03 0.05 1 19 . 7 LEU HB2 H 1.59 0.05 2 20 . 7 LEU HB3 H 1.40 0.05 2 21 . 7 LEU HD2 H 0.59 0.05 1 22 . 8 TRP H H 8.06 0.05 1 23 . 8 TRP HA H 4.29 0.05 1 24 . 8 TRP HB2 H 3.49 0.05 2 25 . 8 TRP HB3 H 3.08 0.05 2 26 . 8 TRP HD1 H 7.10 0.05 1 27 . 8 TRP HE1 H 10.23 0.05 1 28 . 8 TRP HE3 H 7.04 0.05 1 29 . 8 TRP HZ2 H 6.76 0.05 1 30 . 8 TRP HZ3 H 5.76 0.05 1 31 . 8 TRP HH2 H 6.51 0.05 1 32 . 9 PHE H H 8.45 0.05 1 33 . 9 PHE HA H 4.02 0.05 1 34 . 9 PHE HB2 H 3.07 0.05 2 35 . 9 PHE HB3 H 2.97 0.05 2 36 . 9 PHE HD1 H 7.09 0.05 1 37 . 9 PHE HD2 H 7.09 0.05 1 38 . 9 PHE HE1 H 7.16 0.05 1 39 . 9 PHE HE2 H 7.16 0.05 1 40 . 10 ARG H H 8.17 0.05 1 41 . 10 ARG HA H 3.62 0.05 1 42 . 10 ARG HB2 H 1.86 0.05 1 43 . 10 ARG HB3 H 1.86 0.05 1 44 . 10 ARG HG2 H 1.74 0.05 1 45 . 10 ARG HG3 H 1.74 0.05 1 46 . 11 GLY H H 8.59 0.05 1 47 . 11 GLY HA2 H 4.06 0.05 2 48 . 11 GLY HA3 H 3.64 0.05 2 49 . 12 LEU H H 8.58 0.05 1 50 . 12 LEU HA H 4.39 0.05 1 51 . 12 LEU HB2 H 1.71 0.05 1 52 . 12 LEU HB3 H 1.71 0.05 1 53 . 12 LEU HG H 1.75 0.05 1 54 . 12 LEU HD1 H 0.79 0.05 1 55 . 12 LEU HD2 H 0.92 0.05 1 56 . 13 ASN H H 8.21 0.05 1 57 . 13 ASN HA H 4.39 0.05 1 58 . 13 ASN HB2 H 2.77 0.05 2 59 . 13 ASN HB3 H 2.67 0.05 2 60 . 13 ASN HD21 H 6.68 0.05 1 61 . 13 ASN HD22 H 7.47 0.05 1 62 . 14 ARG H H 7.87 0.05 1 63 . 14 ARG HA H 4.05 0.05 1 64 . 14 ARG HB2 H 2.02 0.05 2 65 . 14 ARG HB3 H 1.81 0.05 2 66 . 14 ARG HG2 H 1.70 0.05 1 67 . 14 ARG HG3 H 1.70 0.05 1 68 . 14 ARG HD2 H 3.63 0.05 2 69 . 14 ARG HD3 H 3.55 0.05 2 70 . 14 ARG HE H 7.45 0.05 1 71 . 15 ILE H H 7.64 0.05 1 72 . 15 ILE HA H 4.00 0.05 1 73 . 15 ILE HB H 1.78 0.05 1 74 . 15 ILE HG12 H 1.64 0.05 2 75 . 15 ILE HG13 H 1.55 0.05 2 76 . 15 ILE HG2 H 1.21 0.05 1 77 . 15 ILE HD1 H 0.72 0.05 1 78 . 16 GLN H H 7.74 0.05 1 79 . 16 GLN HA H 4.20 0.05 1 80 . 16 GLN HB2 H 1.97 0.05 2 81 . 16 GLN HB3 H 1.89 0.05 2 82 . 16 GLN HG2 H 2.25 0.05 2 83 . 16 GLN HG3 H 2.22 0.05 2 84 . 16 GLN HE21 H 6.61 0.05 1 85 . 16 GLN HE22 H 7.28 0.05 1 86 . 17 THR H H 7.72 0.05 1 87 . 17 THR HA H 4.19 0.05 1 88 . 17 THR HB H 4.00 0.05 1 89 . 17 THR HG2 H 0.73 0.05 1 90 . 18 GLN H H 8.01 0.05 1 91 . 18 GLN HA H 3.56 0.05 1 92 . 18 GLN HB2 H 1.89 0.05 1 93 . 18 GLN HB3 H 1.89 0.05 1 94 . 18 GLN HG2 H 2.42 0.05 2 95 . 18 GLN HG3 H 2.29 0.05 2 96 . 18 GLN HE21 H 7.37 0.05 1 97 . 18 GLN HE22 H 6.74 0.05 1 98 . 19 ILE H H 7.60 0.05 1 99 . 19 ILE HA H 4.15 0.05 1 100 . 19 ILE HB H 1.99 0.05 1 stop_ save_