data_4739 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of the calcium-bound C-terminal domain (W81-S161) of Calcium Vector Protein from Amphioxus ; _BMRB_accession_number 4739 _BMRB_flat_file_name bmr4739.str _Entry_type original _Submission_date 2000-05-19 _Accession_date 2000-05-19 _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 Theret Isabelle . . 2 Baladi Sybil . . 3 Cox Jos A. . 4 Sakamoto Hiroshi . . 5 Craescu Constantin T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 478 "15N chemical shifts" 80 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Theret, I., Baladi, S., Cox, J.A., Sakamoto, H., and Craescu, C.T., "Sequential Calcium Binding to the Regulatory Domain of Calcium Vector Protein Reveals Functional Asymmetry and a Novel Mode of Structural Rearrangement," Biochemistry 39, 7920-7926 (2000). ; _Citation_title ; Sequential Calcium Binding to the Regulatory Domain of Calcium Vector Protein Reveals Functional Asymmetry and a Novel Mode of Structural Rearrangement ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20351256 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Theret Isabelle . . 2 Baladi Sybil . . 3 Cox Jos A. . 4 Sakamoto Hiroshi . . 5 Craescu Constantin T. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 39 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7920 _Page_last 7926 _Year 2000 _Details . loop_ _Keyword EF-Hand 'Calcium binding protein' NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_C-CaVP _Saveframe_category molecular_system _Mol_system_name 'Calcium Vector Protein' _Abbreviation_common CaVP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CaVP $C-CaVP 'Ca 2+' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details ; The segment studied is the calcium-bound C-terminal domain of CaVP (Trp81-Ser161 or C-CaVP) ; save_ ######################## # Monomeric polymers # ######################## save_C-CaVP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Calcium Vector Protein' _Name_variant 'C-terminal domain of CaVP [81-161]' _Abbreviation_common CaVP _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; WVRQDDEEEILRAFKVFDAN GDGVIDFDEFKFIMQKVGEE PLTDAEVEEAMKEADEDGNG VIDIPEFMDLIKKSKNALKE S ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 81 TRP 2 82 VAL 3 83 ARG 4 84 GLN 5 85 ASP 6 86 ASP 7 87 GLU 8 88 GLU 9 89 GLU 10 90 ILE 11 91 LEU 12 92 ARG 13 93 ALA 14 94 PHE 15 95 LYS 16 96 VAL 17 97 PHE 18 98 ASP 19 99 ALA 20 100 ASN 21 101 GLY 22 102 ASP 23 103 GLY 24 104 VAL 25 105 ILE 26 106 ASP 27 107 PHE 28 108 ASP 29 109 GLU 30 110 PHE 31 111 LYS 32 112 PHE 33 113 ILE 34 114 MET 35 115 GLN 36 116 LYS 37 117 VAL 38 118 GLY 39 119 GLU 40 120 GLU 41 121 PRO 42 122 LEU 43 123 THR 44 124 ASP 45 125 ALA 46 126 GLU 47 127 VAL 48 128 GLU 49 129 GLU 50 130 ALA 51 131 MET 52 132 LYS 53 133 GLU 54 134 ALA 55 135 ASP 56 136 GLU 57 137 ASP 58 138 GLY 59 139 ASN 60 140 GLY 61 141 VAL 62 142 ILE 63 143 ASP 64 144 ILE 65 145 PRO 66 146 GLU 67 147 PHE 68 148 MET 69 149 ASP 70 150 LEU 71 151 ILE 72 152 LYS 73 153 LYS 74 154 SER 75 155 LYS 76 156 ASN 77 157 ALA 78 158 LEU 79 159 LYS 80 160 GLU 81 161 SER 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 PDB 1C7V "Nmr Solution Structure Of The Calcium-Bound C-Terminal Domain (W81-S161) Of Calcium Vector Protein From Amphioxus" 100.00 81 100.00 100.00 1.41e-47 PDB 1C7W "Nmr Solution Structure Of The Calcium-Bound C-Terminal Domain (W81-S161) Of Calcium Vector Protein From Amphioxus" 100.00 81 100.00 100.00 1.41e-47 DBJ BAA19428 "calcium vector protein [Branchiostoma lanceolatum]" 100.00 162 100.00 100.00 3.45e-47 DBJ BAA19429 "calcium vector protein [Branchiostoma floridae]" 100.00 162 98.77 100.00 1.19e-46 DBJ BAA74696 "calcium vector protein [Branchiostoma floridae]" 70.37 57 98.25 100.00 7.99e-29 DBJ BAA74697 "calcium vector protein [Branchiostoma floridae]" 80.25 81 100.00 100.00 6.33e-36 DBJ BAA96551 "calcium vector protein [Branchiostoma belcheri]" 98.77 167 98.75 100.00 4.11e-46 GB AEJ84494 "calcium vector protein [Branchiostoma belcheri]" 100.00 162 100.00 100.00 3.64e-47 GB EEN54468 "hypothetical protein BRAFLDRAFT_123412 [Branchiostoma floridae]" 100.00 181 98.77 100.00 3.17e-47 REF XP_002598456 "hypothetical protein BRAFLDRAFT_123412 [Branchiostoma floridae]" 100.00 181 98.77 100.00 3.17e-47 SP O01305 "RecName: Full=Calcium vector protein; Short=CAVP" 100.00 162 98.77 100.00 1.19e-46 SP P04573 "RecName: Full=Calcium vector protein; Short=CAVP" 100.00 162 100.00 100.00 3.45e-47 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 Jun 13 15:08:34 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $C-CaVP 'amphioxus, lancelet' 7740 Eukaryota Metazoa Branchiostoma lanceolatum muscle 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 $C-CaVP 'recombinant technology' 'E. Coli' Escherichia coli . plasmid pET24a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $C-CaVP . mM 0.8 1.2 . 'Tris buffer' 20 mM . . [U-2H] KCl 100 mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C-CaVP 1 mM [U-15N] 'Tris buffer' 20 mM [U-2H] KCl 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 loop_ _Task 'Spectra processing' peak-picking 'restraint analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label . save_ save_2D_1H-1H_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _Sample_label . save_ save_2D_1H-1H_DQ-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQ-COSY' _Sample_label . save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_1H-1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQ-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 308 0.5 K 'ionic strength' 0.100 0.02 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CaVP _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 TRP HA H 4.74 0.01 1 2 . 1 TRP HB3 H 3.27 0.01 1 3 . 1 TRP HB2 H 3.27 0.01 1 4 . 1 TRP HD1 H 7.24 0.01 1 5 . 1 TRP HE1 H 10.13 0.01 1 6 . 1 TRP HE3 H 7.58 0.01 1 7 . 1 TRP HZ2 H 7.40 0.01 1 8 . 1 TRP HZ3 H 7.06 0.01 1 9 . 1 TRP HH2 H 7.11 0.01 1 10 . 2 VAL H H 7.74 0.01 1 11 . 2 VAL HA H 4.13 0.01 1 12 . 2 VAL HB H 1.78 0.01 1 13 . 2 VAL HG1 H 0.85 0.01 1 14 . 2 VAL HG2 H 0.85 0.01 1 15 . 3 ARG N N 123.17 0.1 1 16 . 3 ARG H H 8.34 0.01 1 17 . 3 ARG HA H 4.15 0.01 1 18 . 3 ARG HB2 H 1.85 0.01 2 19 . 3 ARG HB3 H 1.73 0.01 2 20 . 3 ARG HG2 H 1.64 0.01 1 21 . 3 ARG HG3 H 1.64 0.01 1 22 . 3 ARG HD2 H 3.22 0.01 1 23 . 3 ARG HD3 H 3.22 0.01 1 24 . 4 GLN N N 118.72 0.1 1 25 . 4 GLN H H 8.22 0.01 1 26 . 4 GLN HA H 4.2 0.01 1 27 . 4 GLN HB2 H 1.98 0.01 2 28 . 4 GLN HB3 H 2.1 0.01 2 29 . 4 GLN HG2 H 2.32 0.01 1 30 . 4 GLN HG3 H 2.32 0.01 1 31 . 4 GLN HE21 H 6.74 0.01 2 32 . 4 GLN HE22 H 7.55 0.01 2 33 . 4 GLN NE2 N 110.1 0.1 2 34 . 5 ASP N N 116.52 0.1 1 35 . 5 ASP H H 8.33 0.01 1 36 . 5 ASP HA H 4.53 0.01 1 37 . 5 ASP HB2 H 2.62 0.01 2 38 . 5 ASP HB3 H 2.69 0.01 2 39 . 6 ASP N N 117.85 0.1 1 40 . 6 ASP H H 7.73 0.01 1 41 . 6 ASP HA H 4.7 0.01 9 42 . 6 ASP HB2 H 2.6 0.01 2 43 . 6 ASP HB3 H 2.82 0.01 2 44 . 7 GLU N N 121.78 0.1 1 45 . 7 GLU H H 8.63 0.01 1 46 . 7 GLU HA H 3.89 0.01 1 47 . 7 GLU HB2 H 2.1 0.01 1 48 . 7 GLU HB3 H 2.1 0.01 1 49 . 7 GLU HG2 H 2.32 0.01 2 50 . 7 GLU HG3 H 2.27 0.01 2 51 . 8 GLU N N 116.52 0.1 1 52 . 8 GLU H H 8.33 0.01 1 53 . 8 GLU HA H 4.04 0.01 1 54 . 8 GLU HB2 H 2.15 0.01 1 55 . 8 GLU HB3 H 2.15 0.01 1 56 . 8 GLU HG2 H 2.3 0.01 2 57 . 8 GLU HG3 H 2.33 0.01 2 58 . 9 GLU N N 118.3 0.1 1 59 . 9 GLU H H 7.91 0.01 1 60 . 9 GLU HA H 4.14 0.01 1 61 . 9 GLU HB2 H 2.18 0.01 1 62 . 9 GLU HB3 H 2.18 0.01 1 63 . 9 GLU HG2 H 2.4 0.01 1 64 . 9 GLU HG3 H 2.4 0.01 1 65 . 10 ILE N N 119.53 0.1 1 66 . 10 ILE H H 8.05 0.01 1 67 . 10 ILE HA H 3.83 0.01 1 68 . 10 ILE HB H 2.02 0.01 1 69 . 10 ILE HG12 H 0.85 0.01 2 70 . 10 ILE HG13 H 0.98 0.01 2 71 . 10 ILE HG2 H 1.12 0.01 1 72 . 10 ILE HD1 H 0.7 0.01 1 73 . 11 LEU N N 118.37 0.1 1 74 . 11 LEU H H 8.19 0.01 1 75 . 11 LEU HA H 4.13 0.01 1 76 . 11 LEU HB2 H 1.87 0.01 2 77 . 11 LEU HB3 H 1.62 0.01 2 78 . 11 LEU HG H 1.79 0.01 1 79 . 11 LEU HD1 H 0.89 0.01 2 80 . 11 LEU HD2 H 0.83 0.01 2 81 . 12 ARG N N 117.79 0.1 1 82 . 12 ARG H H 7.98 0.01 1 83 . 12 ARG HA H 3.97 0.01 1 84 . 12 ARG HB2 H 2.06 0.01 1 85 . 12 ARG HB3 H 2.06 0.01 1 86 . 12 ARG HG2 H 1.83 0.01 1 87 . 12 ARG HG3 H 1.83 0.01 1 88 . 12 ARG HD2 H 3.22 0.01 1 89 . 12 ARG HD3 H 3.22 0.01 1 90 . 13 ALA N N 120.05 0.1 1 91 . 13 ALA H H 7.94 0.01 1 92 . 13 ALA HA H 4.12 0.01 1 93 . 13 ALA HB H 1.32 0.01 1 94 . 14 PHE N N 117.79 0.1 1 95 . 14 PHE H H 8.45 0.01 1 96 . 14 PHE HA H 3.03 0.01 1 97 . 14 PHE HB2 H 3.2 0.01 2 98 . 14 PHE HB3 H 2.71 0.01 2 99 . 14 PHE HD1 H 6.5 0.01 1 100 . 14 PHE HD2 H 6.5 0.01 1 101 . 14 PHE HE1 H 6.88 0.01 1 102 . 14 PHE HE2 H 6.88 0.01 1 103 . 14 PHE HZ H 7.1 0.01 1 104 . 15 LYS N N 113.16 0.1 1 105 . 15 LYS H H 7.64 0.01 1 106 . 15 LYS HA H 3.99 0.01 1 107 . 15 LYS HB2 H 1.62 0.01 1 108 . 15 LYS HB3 H 1.62 0.01 1 109 . 15 LYS HG2 H 1.62 0.01 4 110 . 15 LYS HG3 H 1.62 0.01 4 111 . 15 LYS HD2 H 1.74 0.01 4 112 . 15 LYS HD3 H 1.74 0.01 4 113 . 15 LYS HE2 H 3.00 0.01 1 114 . 15 LYS HE3 H 3.00 0.01 1 115 . 16 VAL N N 116.58 0.1 1 116 . 16 VAL H H 7.29 0.01 1 117 . 16 VAL HA H 3.54 0.01 1 118 . 16 VAL HB H 1.98 0.01 1 119 . 16 VAL HG1 H 0.96 0.01 2 120 . 16 VAL HG2 H 0.6 0.01 2 121 . 17 PHE N N 115.07 0.1 1 122 . 17 PHE H H 7.42 0.01 1 123 . 17 PHE HA H 4.4 0.01 1 124 . 17 PHE HB2 H 2.83 0.01 2 125 . 17 PHE HB3 H 2.58 0.01 2 126 . 17 PHE HD1 H 7.24 0.01 1 127 . 17 PHE HD2 H 7.24 0.01 1 128 . 18 ASP N N 117.1 0.1 1 129 . 18 ASP H H 7.88 0.01 1 130 . 18 ASP HA H 4.46 0.01 1 131 . 18 ASP HB2 H 2.49 0.01 2 132 . 18 ASP HB3 H 1.6 0.01 2 133 . 19 ALA N N 127.1 0.1 1 134 . 19 ALA H H 7.55 0.01 1 135 . 19 ALA HA H 4.00 0.01 1 136 . 19 ALA HB H 1.44 0.01 1 137 . 20 ASN N N 109.81 0.1 1 138 . 20 ASN H H 8.02 0.01 1 139 . 20 ASN HA H 4.76 0.01 1 140 . 20 ASN HB2 H 3.28 0.01 2 141 . 20 ASN HB3 H 2.92 0.01 2 142 . 20 ASN HD21 H 6.75 0.01 2 143 . 20 ASN HD22 H 7.81 0.01 2 144 . 20 ASN ND2 N 110.91 0.1 1 145 . 21 GLY N N 107.74 0.1 1 146 . 21 GLY H H 7.72 0.01 1 147 . 21 GLY HA2 H 3.83 0.01 2 148 . 21 GLY HA3 H 3.86 0.01 2 149 . 22 ASP N N 118.02 0.1 1 150 . 22 ASP H H 8.14 0.01 1 151 . 22 ASP HA H 4.52 0.01 1 152 . 22 ASP HB2 H 3.12 0.01 2 153 . 22 ASP HB3 H 2.43 0.01 2 154 . 23 GLY N N 111.2 0.1 1 155 . 23 GLY H H 10.48 0.01 1 156 . 23 GLY HA2 H 4.34 0.01 2 157 . 23 GLY HA3 H 3.62 0.01 2 158 . 24 VAL N N 108.42 0.1 1 159 . 24 VAL H H 7.77 0.01 1 160 . 24 VAL HA H 5.14 0.01 1 161 . 24 VAL HB H 1.78 0.01 1 162 . 24 VAL HG1 H 0.9 0.01 2 163 . 24 VAL HG2 H 0.69 0.01 2 164 . 25 ILE N N 124.38 0.1 1 165 . 25 ILE H H 9.61 0.01 1 166 . 25 ILE HA H 5.03 0.01 1 167 . 25 ILE HB H 1.99 0.01 1 168 . 25 ILE HG12 H 0.46 0.01 2 169 . 25 ILE HG13 H 0.93 0.01 2 170 . 25 ILE HG2 H 1.08 0.01 1 171 . 25 ILE HD1 H 0.13 0.01 1 172 . 26 ASP N N 126.29 0.1 1 173 . 26 ASP H H 8.85 0.01 1 174 . 26 ASP HA H 4.9 0.01 1 175 . 26 ASP HB2 H 3.41 0.01 2 176 . 26 ASP HB3 H 2.56 0.01 2 177 . 27 PHE N N 116.06 0.1 1 178 . 27 PHE H H 8.79 0.01 1 179 . 27 PHE HA H 4.47 0.01 1 180 . 27 PHE HB2 H 3.37 0.01 2 181 . 27 PHE HB3 H 3.03 0.01 2 182 . 27 PHE HD1 H 7.37 0.01 1 183 . 27 PHE HD2 H 7.37 0.01 1 184 . 27 PHE HE1 H 7.27 0.01 1 185 . 27 PHE HE2 H 7.27 0.01 1 186 . 28 ASP N N 116.11 0.1 1 187 . 28 ASP H H 7.95 0.01 1 188 . 28 ASP HA H 4.22 0.01 1 189 . 28 ASP HB2 H 2.83 0.01 2 190 . 28 ASP HB3 H 2.65 0.01 2 191 . 29 GLU N N 119.7 0.1 1 192 . 29 GLU H H 8.65 0.01 1 193 . 29 GLU HA H 4.14 0.01 1 194 . 29 GLU HB2 H 2.51 0.01 1 195 . 29 GLU HB3 H 2.51 0.01 1 196 . 29 GLU HG2 H 2.32 0.01 2 197 . 29 GLU HG3 H 2.85 0.01 2 198 . 30 PHE N N 120.8 0.1 1 199 . 30 PHE H H 9.16 0.01 1 200 . 30 PHE HA H 3.95 0.01 1 201 . 30 PHE HB2 H 3.18 0.01 2 202 . 30 PHE HB3 H 3.08 0.01 2 203 . 30 PHE HD1 H 6.88 0.01 1 204 . 30 PHE HD2 H 6.88 0.01 1 205 . 30 PHE HE1 H 7.2 0.01 1 206 . 30 PHE HE2 H 7.2 0.01 1 207 . 30 PHE HZ H 7.00 0.01 1 208 . 31 LYS N N 116.7 0.1 1 209 . 31 LYS H H 8.45 0.01 1 210 . 31 LYS HA H 3.03 0.01 1 211 . 31 LYS HB2 H 1.74 0.01 1 212 . 31 LYS HB3 H 1.74 0.01 1 213 . 31 LYS HG2 H 1.45 0.01 1 214 . 31 LYS HG3 H 1.45 0.01 1 215 . 31 LYS HD2 H 1.73 0.01 1 216 . 31 LYS HD3 H 1.73 0.01 1 217 . 31 LYS HE2 H 3.00 0.01 1 218 . 31 LYS HE3 H 3.00 0.01 1 219 . 32 PHE N N 115.07 0.1 1 220 . 32 PHE H H 7.43 0.01 1 221 . 32 PHE HA H 4.19 0.01 1 222 . 32 PHE HB2 H 3.22 0.01 1 223 . 32 PHE HB3 H 3.22 0.01 1 224 . 32 PHE HD1 H 7.33 0.01 1 225 . 32 PHE HD2 H 7.33 0.01 1 226 . 32 PHE HE1 H 7.27 0.01 1 227 . 32 PHE HE2 H 7.27 0.01 1 228 . 33 ILE N N 115.82 0.1 1 229 . 33 ILE H H 7.24 0.01 1 230 . 33 ILE HA H 3.15 0.01 1 231 . 33 ILE HB H 1.42 0.01 1 232 . 33 ILE HG12 H 1.04 0.01 2 233 . 33 ILE HG13 H 0.19 0.01 2 234 . 33 ILE HG2 H 0.53 0.01 1 235 . 33 ILE HD1 H 0.18 0.01 1 236 . 34 MET N N 112.7 0.1 1 237 . 34 MET H H 7.52 0.01 1 238 . 34 MET HA H 4.18 0.01 1 239 . 34 MET HB2 H 1.8 0.01 2 240 . 34 MET HB3 H 1.71 0.01 2 241 . 34 MET HG2 H 1.92 0.01 1 242 . 34 MET HG3 H 1.92 0.01 1 243 . 35 GLN N N 115.01 0.1 1 244 . 35 GLN H H 7.72 0.01 1 245 . 35 GLN HA H 4.24 0.01 1 246 . 35 GLN HB2 H 2.04 0.01 1 247 . 35 GLN HB3 H 2.04 0.01 1 248 . 35 GLN HG2 H 2.4 0.01 1 249 . 35 GLN HG3 H 2.4 0.01 1 250 . 35 GLN HE21 H 7.18 0.01 2 251 . 35 GLN HE22 H 7.07 0.01 2 252 . 35 GLN NE2 N 109.17 0.1 1 253 . 36 LYS N N 117.39 0.1 1 254 . 36 LYS H H 7.78 0.01 1 255 . 36 LYS HA H 4.32 0.01 1 256 . 36 LYS HB2 H 1.68 0.01 1 257 . 36 LYS HB3 H 1.68 0.01 1 258 . 36 LYS HG2 H 1.27 0.01 1 259 . 36 LYS HG3 H 1.27 0.01 1 260 . 36 LYS HD2 H 1.53 0.01 1 261 . 36 LYS HD3 H 1.53 0.01 1 262 . 36 LYS HE2 H 2.87 0.01 1 263 . 36 LYS HE3 H 2.87 0.01 1 264 . 37 VAL N N 115.94 0.1 1 265 . 37 VAL H H 7.73 0.01 1 266 . 37 VAL HA H 4.7 0.01 1 267 . 37 VAL HB H 2.1 0.01 1 268 . 37 VAL HG1 H 1.17 0.01 2 269 . 37 VAL HG2 H 0.82 0.01 2 270 . 38 GLY N N 108.65 0.1 1 271 . 38 GLY H H 8.01 0.01 1 272 . 38 GLY HA2 H 4.00 0.01 2 273 . 38 GLY HA3 H 3.92 0.01 2 274 . 39 GLU N N 117.39 0.1 1 275 . 39 GLU H H 8.13 0.01 1 276 . 39 GLU HA H 4.27 0.01 1 277 . 39 GLU HB2 H 1.92 0.01 1 278 . 39 GLU HB3 H 1.92 0.01 1 279 . 39 GLU HG2 H 2.12 0.01 2 280 . 39 GLU HG3 H 2.24 0.01 2 281 . 40 GLU N N 117.79 0.1 1 282 . 40 GLU H H 8.05 0.01 1 283 . 40 GLU HA H 4.62 0.01 1 284 . 40 GLU HB2 H 2.02 0.01 2 285 . 40 GLU HB3 H 1.86 0.01 2 286 . 40 GLU HG2 H 2.23 0.01 1 287 . 40 GLU HG3 H 2.23 0.01 1 288 . 41 PRO HA H 4.33 0.01 1 289 . 41 PRO HB2 H 2.1 0.01 2 290 . 41 PRO HB3 H 2.27 0.01 2 291 . 41 PRO HD2 H 3.64 0.01 1 292 . 41 PRO HD3 H 3.64 0.01 1 293 . 42 LEU N N 119.47 0.1 1 294 . 42 LEU H H 7.73 0.01 1 295 . 42 LEU HA H 4.1 0.01 1 296 . 42 LEU HB2 H 1.91 0.01 1 297 . 42 LEU HB3 H 1.91 0.01 1 298 . 42 LEU HG H 1.91 0.01 1 299 . 42 LEU HD1 H 0.78 0.01 2 300 . 42 LEU HD2 H 0.81 0.01 2 301 . 43 THR N N 112.3 0.1 1 302 . 43 THR H H 9.00 0.01 1 303 . 43 THR HA H 4.45 0.01 1 304 . 43 THR HB H 4.67 0.01 1 305 . 43 THR HG2 H 1.37 0.01 1 306 . 44 ASP N N 119.82 0.1 1 307 . 44 ASP H H 8.89 0.01 1 308 . 44 ASP HA H 4.37 0.01 1 309 . 44 ASP HB2 H 2.82 0.01 2 310 . 44 ASP HB3 H 2.7 0.01 2 311 . 45 ALA N N 119.53 0.1 1 312 . 45 ALA H H 8.37 0.01 1 313 . 45 ALA HA H 4.22 0.01 1 314 . 45 ALA HB H 1.45 0.01 1 315 . 46 GLU N N 116.98 0.1 1 316 . 46 GLU H H 7.72 0.01 1 317 . 46 GLU HA H 4.12 0.01 1 318 . 46 GLU HB2 H 2.03 0.01 1 319 . 46 GLU HB3 H 2.03 0.01 1 320 . 46 GLU HG2 H 2.45 0.01 2 321 . 46 GLU HG3 H 2.38 0.01 2 322 . 47 VAL N N 120.16 0.1 1 323 . 47 VAL H H 8.49 0.01 1 324 . 47 VAL HA H 3.73 0.01 1 325 . 47 VAL HB H 2.36 0.01 1 326 . 47 VAL HG1 H 1.04 0.01 2 327 . 47 VAL HG2 H 0.95 0.01 2 328 . 48 GLU N N 118.95 0.1 1 329 . 48 GLU H H 8.35 0.01 1 330 . 48 GLU HA H 4.04 0.01 1 331 . 48 GLU HB2 H 2.19 0.01 1 332 . 48 GLU HB3 H 2.19 0.01 1 333 . 48 GLU HG2 H 2.45 0.01 1 334 . 48 GLU HG3 H 2.45 0.01 1 335 . 49 GLU N N 117.15 0.1 1 336 . 49 GLU H H 7.85 0.01 1 337 . 49 GLU HA H 4.02 0.01 1 338 . 49 GLU HB2 H 2.13 0.01 1 339 . 49 GLU HB3 H 2.13 0.01 1 340 . 49 GLU HG2 H 2.34 0.01 2 341 . 49 GLU HG3 H 2.4 0.01 2 342 . 50 ALA N N 119.99 0.1 1 343 . 50 ALA H H 8.05 0.01 1 344 . 50 ALA HA H 4.26 0.01 1 345 . 50 ALA HB H 1.44 0.01 1 346 . 51 MET N N 118.54 0.1 1 347 . 51 MET H H 8.57 0.01 1 348 . 51 MET HA H 3.35 0.01 1 349 . 51 MET HB2 H 2.17 0.01 2 350 . 51 MET HB3 H 2.39 0.01 2 351 . 51 MET HG2 H 1.69 0.01 2 352 . 51 MET HG3 H 1.88 0.01 4 353 . 51 MET HE H 1.84 0.01 4 354 . 52 LYS N N 115.94 0.1 1 355 . 52 LYS H H 7.87 0.01 1 356 . 52 LYS HA H 4.01 0.01 1 357 . 52 LYS HB2 H 1.91 0.01 1 358 . 52 LYS HB3 H 1.91 0.01 1 359 . 52 LYS HG2 H 1.65 0.01 1 360 . 52 LYS HG3 H 1.65 0.01 1 361 . 52 LYS HD2 H 1.8 0.01 1 362 . 52 LYS HD3 H 1.8 0.01 1 363 . 52 LYS HE2 H 3.22 0.01 1 364 . 52 LYS HE3 H 3.22 0.01 1 365 . 53 GLU N N 114.67 0.1 1 366 . 53 GLU H H 7.65 0.01 1 367 . 53 GLU HA H 3.97 0.01 1 368 . 53 GLU HB2 H 2.26 0.01 2 369 . 53 GLU HB3 H 2.06 0.01 2 370 . 53 GLU HG2 H 2.43 0.01 1 371 . 53 GLU HG3 H 2.43 0.01 1 372 . 54 ALA N N 117.91 0.1 1 373 . 54 ALA H H 7.54 0.01 1 374 . 54 ALA HA H 4.31 0.01 1 375 . 54 ALA HB H 1.4 0.01 1 376 . 55 ASP N N 115.82 0.1 1 377 . 55 ASP H H 7.82 0.01 1 378 . 55 ASP HA H 4.53 0.01 1 379 . 55 ASP HB2 H 2.87 0.01 2 380 . 55 ASP HB3 H 2.2 0.01 2 381 . 56 GLU N N 124.79 0.1 1 382 . 56 GLU H H 7.56 0.01 1 383 . 56 GLU HA H 4.01 0.01 1 384 . 56 GLU HB2 H 2.16 0.01 1 385 . 56 GLU HB3 H 2.16 0.01 1 386 . 56 GLU HG2 H 2.57 0.01 2 387 . 56 GLU HG3 H 2.38 0.01 2 388 . 57 ASP N N 112.76 0.1 1 389 . 57 ASP H H 8.33 0.01 1 390 . 57 ASP HA H 4.63 0.01 1 391 . 57 ASP HB2 H 3.08 0.01 2 392 . 57 ASP HB3 H 2.73 0.01 2 393 . 58 GLY N N 107.21 0.1 1 394 . 58 GLY H H 7.63 0.01 1 395 . 58 GLY HA2 H 3.92 0.01 2 396 . 58 GLY HA3 H 3.77 0.01 2 397 . 59 ASN N N 117.68 0.1 1 398 . 59 ASN H H 8.2 0.01 1 399 . 59 ASN HA H 4.6 0.01 1 400 . 59 ASN HB2 H 3.34 0.01 2 401 . 59 ASN HB3 H 2.65 0.01 2 402 . 59 ASN HD21 H 6.75 0.01 2 403 . 59 ASN HD22 H 7.81 0.01 2 404 . 59 ASN ND2 N 113.28 0.1 1 405 . 60 GLY N N 111.95 0.1 1 406 . 60 GLY H H 10.69 0.01 1 407 . 60 GLY HA2 H 4.24 0.01 2 408 . 60 GLY HA3 H 3.4 0.01 2 409 . 61 VAL N N 107.44 0.1 1 410 . 61 VAL H H 7.41 0.01 1 411 . 61 VAL HA H 4.83 0.01 1 412 . 61 VAL HB H 1.73 0.01 1 413 . 61 VAL HG1 H 0.85 0.01 2 414 . 61 VAL HG2 H 0.64 0.01 2 415 . 62 ILE N N 124.67 0.1 1 416 . 62 ILE H H 9.52 0.01 1 417 . 62 ILE HA H 5.2 0.01 1 418 . 62 ILE HB H 2.2 0.01 1 419 . 62 ILE HG12 H 1.26 0.01 2 420 . 62 ILE HG13 H 1.08 0.01 2 421 . 62 ILE HG2 H 1.25 0.01 1 422 . 62 ILE HD1 H 0.53 0.01 1 423 . 63 ASP N N 127.22 0.1 1 424 . 63 ASP H H 8.76 0.01 1 425 . 63 ASP HA H 5.12 0.01 1 426 . 63 ASP HB2 H 3.33 0.01 2 427 . 63 ASP HB3 H 2.55 0.01 2 428 . 64 ILE N N 114.84 0.1 1 429 . 64 ILE H H 8.19 0.01 1 430 . 64 ILE HA H 3.51 0.01 1 431 . 64 ILE HB H 1.71 0.01 1 432 . 64 ILE HG12 H 0.8 0.01 2 433 . 64 ILE HG13 H -0.63 0.01 2 434 . 64 ILE HG2 H 0.64 0.01 1 435 . 64 ILE HD1 H 0.45 0.01 1 436 . 65 PRO HA H 4.22 0.01 1 437 . 65 PRO HB2 H 2.27 0.01 1 438 . 65 PRO HB3 H 2.27 0.01 1 439 . 65 PRO HG2 H 2.19 0.01 2 440 . 65 PRO HG3 H 1.86 0.01 2 441 . 65 PRO HD2 H 3.74 0.01 2 442 . 65 PRO HD3 H 3.51 0.01 2 443 . 66 GLU N N 115.42 0.1 1 444 . 66 GLU H H 8.38 0.01 1 445 . 66 GLU HA H 4.24 0.01 1 446 . 66 GLU HB2 H 2.62 0.01 2 447 . 66 GLU HB3 H 2.65 0.01 2 448 . 66 GLU HG2 H 2.42 0.01 2 449 . 66 GLU HG3 H 3.07 0.01 2 450 . 67 PHE N N 123.34 0.1 1 451 . 67 PHE H H 9.29 0.01 1 452 . 67 PHE HA H 4.17 0.01 1 453 . 67 PHE HB2 H 3.53 0.01 2 454 . 67 PHE HB3 H 3.36 0.01 2 455 . 67 PHE HD1 H 7.04 0.01 1 456 . 67 PHE HD2 H 7.04 0.01 1 457 . 67 PHE HE1 H 7.29 0.01 1 458 . 67 PHE HE2 H 7.29 0.01 1 459 . 67 PHE HZ H 7.16 0.01 1 460 . 68 MET N N 115.77 0.1 1 461 . 68 MET H H 8.98 0.01 1 462 . 68 MET HA H 3.93 0.01 1 463 . 68 MET HB2 H 2.34 0.01 2 464 . 68 MET HB3 H 2.08 0.01 2 465 . 68 MET HG2 H 2.88 0.01 2 466 . 68 MET HG3 H 2.57 0.01 2 467 . 68 MET HE H 2.08 0.01 1 468 . 69 ASP N N 116.89 0.1 1 469 . 69 ASP H H 7.77 0.01 1 470 . 69 ASP HA H 4.46 0.01 1 471 . 69 ASP HB2 H 2.7 0.01 2 472 . 69 ASP HB3 H 2.91 0.01 2 473 . 70 LEU N N 120.62 0.1 1 474 . 70 LEU H H 7.98 0.01 1 475 . 70 LEU HA H 4.09 0.01 1 476 . 70 LEU HB2 H 1.74 0.01 1 477 . 70 LEU HB3 H 1.74 0.01 1 478 . 70 LEU HG H 1.51 0.01 1 479 . 70 LEU HD2 H 0.94 0.01 2 480 . 70 LEU HD1 H 0.85 0.01 2 481 . 71 ILE N N 116.81 0.1 1 482 . 71 ILE H H 7.94 0.01 1 483 . 71 ILE HA H 3.63 0.01 1 484 . 71 ILE HB H 1.8 0.01 1 485 . 71 ILE HG12 H 0.99 0.01 2 486 . 71 ILE HG13 H 0.87 0.01 2 487 . 71 ILE HG2 H 0.68 0.01 1 488 . 71 ILE HD1 H 0.4 0.01 1 489 . 72 LYS N N 117.85 0.1 1 490 . 72 LYS H H 8.00 0.01 1 491 . 72 LYS HA H 4.03 0.01 1 492 . 72 LYS HB2 H 1.93 0.01 1 493 . 72 LYS HB3 H 1.93 0.01 1 494 . 72 LYS HG2 H 1.42 0.01 1 495 . 72 LYS HG3 H 1.42 0.01 1 496 . 72 LYS HD2 H 1.65 0.01 1 497 . 72 LYS HD3 H 1.65 0.01 1 498 . 72 LYS HE2 H 2.94 0.01 1 499 . 72 LYS HE3 H 2.94 0.01 1 500 . 73 LYS N N 120.45 0.1 1 501 . 73 LYS H H 8.11 0.01 1 502 . 73 LYS HA H 4.25 0.01 1 503 . 73 LYS HB3 H 1.81 0.01 2 504 . 73 LYS HB2 H 1.87 0.01 2 505 . 73 LYS HG2 H 1.47 0.01 1 506 . 73 LYS HG3 H 1.47 0.01 1 507 . 73 LYS HD2 H 1.67 0.01 1 508 . 73 LYS HD3 H 1.67 0.01 1 509 . 73 LYS HE2 H 2.97 0.01 1 510 . 73 LYS HE3 H 2.97 0.01 1 511 . 74 SER N N 113.45 0.1 1 512 . 74 SER H H 7.77 0.01 1 513 . 74 SER HA H 4.37 0.01 1 514 . 74 SER HB2 H 3.95 0.01 1 515 . 74 SER HB3 H 3.95 0.01 1 516 . 75 LYS HA H 4.27 0.01 1 517 . 75 LYS HB3 H 1.8 0.01 2 518 . 75 LYS HB2 H 1.86 0.01 9 519 . 76 ASN N N 116.64 0.1 1 520 . 76 ASN H H 8.18 0.01 1 521 . 76 ASN HA H 4.66 0.01 1 522 . 76 ASN HB2 H 2.82 0.01 2 523 . 76 ASN HB3 H 2.72 0.01 2 524 . 76 ASN HD21 H 7.52 0.01 1 525 . 76 ASN HD22 H 6.87 0.01 1 526 . 77 ALA N N 121.67 0.1 1 527 . 77 ALA H H 8.04 0.01 1 528 . 77 ALA HA H 4.26 0.01 1 529 . 77 ALA HB H 1.37 0.01 1 530 . 78 LEU N N 118.2 0.1 1 531 . 78 LEU H H 7.99 0.01 1 532 . 78 LEU HA H 4.32 0.01 1 533 . 78 LEU HB2 H 1.65 0.01 1 534 . 78 LEU HB3 H 1.65 0.01 1 535 . 78 LEU HG H 1.62 0.01 1 536 . 78 LEU HD2 H 0.9 0.01 2 537 . 78 LEU HD1 H 0.85 0.01 2 538 . 79 LYS N N 121.38 0.1 1 539 . 79 LYS H H 8.05 0.01 1 540 . 79 LYS HA H 4.34 0.01 1 541 . 79 LYS HB2 H 1.75 0.01 2 542 . 79 LYS HB3 H 1.83 0.01 2 543 . 79 LYS HG2 H 1.41 0.01 1 544 . 79 LYS HG3 H 1.41 0.01 1 545 . 79 LYS HE2 H 3.00 0.01 1 546 . 79 LYS HE3 H 3.00 0.01 1 547 . 80 GLU N N 120.97 0.1 1 548 . 80 GLU H H 8.38 0.01 1 549 . 80 GLU HA H 4.33 0.01 1 550 . 80 GLU HB2 H 2.11 0.01 2 551 . 80 GLU HB3 H 1.92 0.01 2 552 . 80 GLU HG2 H 2.27 0.01 1 553 . 80 GLU HG3 H 2.27 0.01 1 554 . 81 SER N N 120.17 0.1 9 555 . 81 SER H H 7.89 0.01 1 556 . 81 SER HA H 4.26 0.01 1 557 . 81 SER HB2 H 3.85 0.01 1 558 . 81 SER HB3 H 3.85 0.01 1 stop_ save_