data_4872 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Interhelical Ion Pairing in Coiled Coils: Solution Structure of a Heterodimeric Leucine Zipper and Determination of pKa Values of Glu Side Chains ; _BMRB_accession_number 4872 _BMRB_flat_file_name bmr4872.str _Entry_type original _Submission_date 2000-10-23 _Accession_date 2000-10-23 _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 Marti D. N. . 2 Jelesarov I. . . 3 Bosshard H. R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 386 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Interhelical Ion Pairing in Coiled Coils: Solution Structure of a Heterodimeric Leucine Zipper and Determination of pKa Values of Glu Side Chains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 11041845 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Marti D. N. . 2 Jelesarov I. . . 3 Bosshard H. R. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12804 _Page_last 12818 _Year 2000 _Details . loop_ _Keyword 'coiled coil' 'interhelical ion pairing' 'leucine zipper' stop_ save_ ################################## # Molecular system description # ################################## save_AB_LEUCINE_ZIPPER _Saveframe_category molecular_system _Mol_system_name 'DESIGNED HETERODIMERIC LEUCINE ZIPPER' _Abbreviation_common 'AB LEUCINE ZIPPER' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ACIDIC CHAIN' $CHAIN_A 'BASIC CHAIN' $CHAIN_B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CHAIN_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LEUCINE ZIPPER CHAIN A' _Abbreviation_common 'CHAIN A' _Molecular_mass 3557 _Mol_thiol_state 'all disulfide bound' _Details 'N- AND C-TERMINI ARE ACETYLATED AND AMIDATED, RESPECTIVELY' ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; XEVAQLEKEVAQAEAENYQLE QEVAQLEHECGX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ACE 2 2 GLU 3 3 VAL 4 4 ALA 5 5 GLN 6 6 LEU 7 7 GLU 8 8 LYS 9 9 GLU 10 10 VAL 11 11 ALA 12 12 GLN 13 13 ALA 14 14 GLU 15 15 ALA 16 16 GLU 17 17 ASN 18 18 TYR 19 19 GLN 20 20 LEU 21 21 GLU 22 22 GLN 23 23 GLU 24 24 VAL 25 25 ALA 26 26 GLN 27 27 LEU 28 28 GLU 29 29 HIS 30 30 GLU 31 31 CYS 32 32 GLY 33 33 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_CHAIN_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LEUCINE ZIPPER CHAIN B' _Abbreviation_common 'CHAIN B' _Molecular_mass 3576 _Mol_thiol_state 'all disulfide bound' _Details 'N- AND C-TERMINI ARE ACETYLATED AND AMIDATED, RESPECTIVELY' _Residue_count 33 _Mol_residue_sequence ; XEVQALKKRVQALKARNYAA KQKVQALRHKCGX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 32 ACE 2 33 GLU 3 34 VAL 4 35 GLN 5 36 ALA 6 37 LEU 7 38 LYS 8 39 LYS 9 40 ARG 10 41 VAL 11 42 GLN 12 43 ALA 13 44 LEU 14 45 LYS 15 46 ALA 16 47 ARG 17 48 ASN 18 49 TYR 19 50 ALA 20 51 ALA 21 52 LYS 22 53 GLN 23 54 LYS 24 55 VAL 25 56 GLN 26 57 ALA 27 58 LEU 28 59 ARG 29 60 HIS 30 61 LYS 31 62 CYS 32 63 GLY 33 64 NH2 stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2007-11-12 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 1FMH 'B Chain B, Nmr Solution Structure Of ADesigned Heterodimeric Leucine Zipper' 100.00 31 100 100 5e-08 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:09:34 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'ACETYL GROUP' _BMRB_code . _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:15:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CHAIN_A . . . . . . $CHAIN_B . . . . . . stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CHAIN_A 'chemical synthesis' . . . . . $CHAIN_B 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CHAIN_A 2.1 mM . $CHAIN_B 2.1 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task 'data collection' stop_ _Details BRUKER save_ save_FELIX _Saveframe_category software _Name FELIX _Version 98 loop_ _Task 'data processing' stop_ _Details 'Molecular Simulations, Inc.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure calculation' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 10 . mM pH 5.65 0.05 n/a temperature 310 0.5 K 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_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . $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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ACIDIC CHAIN' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU H H 8.4 0.01 1 2 . 2 GLU HA H 4.17 0.01 1 3 . 2 GLU HB2 H 2.13 0.01 2 4 . 2 GLU HB3 H 2.05 0.01 2 5 . 2 GLU HG2 H 2.35 0.01 2 6 . 2 GLU HG3 H 2.27 0.01 2 7 . 3 VAL H H 8.31 0.01 1 8 . 3 VAL HA H 3.55 0.01 1 9 . 3 VAL HB H 2.04 0.01 1 10 . 3 VAL HG1 H 0.88 0.01 1 11 . 3 VAL HG2 H 1.01 0.01 1 12 . 4 ALA H H 8.05 0.01 1 13 . 4 ALA HA H 4.22 0.01 1 14 . 4 ALA HB H 1.46 0.01 1 15 . 5 GLN H H 7.77 0.01 1 16 . 5 GLN HA H 4.13 0.01 1 17 . 5 GLN HB2 H 2.24 0.01 2 18 . 5 GLN HB3 H 2.21 0.01 2 19 . 5 GLN HG2 H 2.47 0.01 1 20 . 5 GLN HG3 H 2.47 0.01 1 21 . 5 GLN HE21 H 7.76 0.01 1 22 . 5 GLN HE22 H 6.83 0.01 1 23 . 6 LEU H H 8.2 0.01 1 24 . 6 LEU HA H 4.16 0.01 1 25 . 6 LEU HB2 H 2.08 0.01 1 26 . 6 LEU HB3 H 1.39 0.01 1 27 . 6 LEU HG H 1.88 0.01 1 28 . 6 LEU HD1 H 0.98 0.01 2 29 . 6 LEU HD2 H 0.92 0.01 2 30 . 7 GLU H H 8.9 0.01 1 31 . 7 GLU HA H 3.93 0.01 1 32 . 7 GLU HB2 H 2.21 0.01 2 33 . 7 GLU HB3 H 1.99 0.01 2 34 . 7 GLU HG2 H 2.6 0.01 2 35 . 7 GLU HG3 H 2.22 0.01 2 36 . 8 LYS H H 7.6 0.01 1 37 . 8 LYS HA H 4.19 0.01 1 38 . 8 LYS HB2 H 2.04 0.01 1 39 . 8 LYS HB3 H 2.04 0.01 1 40 . 8 LYS HG2 H 1.67 0.01 2 41 . 8 LYS HG3 H 1.48 0.01 2 42 . 8 LYS HD2 H 1.74 0.01 1 43 . 8 LYS HD3 H 1.74 0.01 1 44 . 8 LYS HE2 H 3.01 0.01 1 45 . 8 LYS HE3 H 3.01 0.01 1 46 . 9 GLU H H 8.11 0.01 1 47 . 9 GLU HA H 4.1 0.01 1 48 . 9 GLU HB2 H 2.3 0.01 2 49 . 9 GLU HB3 H 2.18 0.01 2 50 . 9 GLU HG2 H 2.58 0.01 2 51 . 9 GLU HG3 H 2.32 0.01 2 52 . 10 VAL H H 8.77 0.01 1 53 . 10 VAL HA H 3.51 0.01 1 54 . 10 VAL HB H 2.2 0.01 1 55 . 10 VAL HG1 H 0.92 0.01 1 56 . 10 VAL HG2 H 1.07 0.01 1 57 . 11 ALA H H 7.8 0.01 1 58 . 11 ALA HA H 4.24 0.01 1 59 . 11 ALA HB H 1.58 0.01 1 60 . 12 GLN H H 8.32 0.01 1 61 . 12 GLN HA H 4.17 0.01 1 62 . 12 GLN HB2 H 2.25 0.01 2 63 . 12 GLN HB3 H 2.18 0.01 2 64 . 12 GLN HG2 H 2.59 0.01 2 65 . 12 GLN HG3 H 2.47 0.01 2 66 . 12 GLN HE21 H 7.52 0.01 1 67 . 12 GLN HE22 H 6.84 0.01 1 68 . 13 ALA H H 8.27 0.01 1 69 . 13 ALA HA H 4.3 0.01 1 70 . 13 ALA HB H 1.56 0.01 1 71 . 14 GLU H H 9.05 0.01 1 72 . 14 GLU HA H 4.09 0.01 1 73 . 14 GLU HB2 H 2.26 0.01 2 74 . 14 GLU HB3 H 2.04 0.01 2 75 . 14 GLU HG2 H 2.56 0.01 2 76 . 14 GLU HG3 H 2.27 0.01 2 77 . 15 ALA H H 7.95 0.01 1 78 . 15 ALA HA H 4.32 0.01 1 79 . 15 ALA HB H 1.61 0.01 1 80 . 16 GLU H H 8.2 0.01 1 81 . 16 GLU HA H 4.13 0.01 1 82 . 16 GLU HB2 H 2.18 0.01 2 83 . 16 GLU HB3 H 2.09 0.01 2 84 . 16 GLU HG2 H 2.44 0.01 2 85 . 16 GLU HG3 H 2.22 0.01 2 86 . 17 ASN H H 8.34 0.01 1 87 . 17 ASN HA H 4.41 0.01 1 88 . 17 ASN HB2 H 3.5 0.01 1 89 . 17 ASN HB3 H 2.74 0.01 1 90 . 17 ASN HD21 H 7.78 0.01 1 91 . 17 ASN HD22 H 7.31 0.01 1 92 . 18 TYR H H 8.2 0.01 1 93 . 18 TYR HA H 4.27 0.01 1 94 . 18 TYR HB2 H 3.27 0.01 2 95 . 18 TYR HB3 H 3.19 0.01 2 96 . 18 TYR HD1 H 7.2 0.01 1 97 . 18 TYR HD2 H 7.2 0.01 1 98 . 18 TYR HE1 H 6.83 0.01 1 99 . 18 TYR HE2 H 6.83 0.01 1 100 . 19 GLN H H 7.71 0.01 1 101 . 19 GLN HA H 3.98 0.01 1 102 . 19 GLN HB2 H 2.3 0.01 1 103 . 19 GLN HB3 H 2.3 0.01 1 104 . 19 GLN HG2 H 2.61 0.01 2 105 . 19 GLN HG3 H 2.53 0.01 2 106 . 20 LEU H H 8.55 0.01 1 107 . 20 LEU HA H 4.16 0.01 1 108 . 20 LEU HB2 H 2.01 0.01 1 109 . 20 LEU HB3 H 1.25 0.01 1 110 . 20 LEU HG H 1.9 0.01 1 111 . 20 LEU HD1 H 0.91 0.01 2 112 . 20 LEU HD2 H 1 0.01 2 113 . 21 GLU H H 8.69 0.01 1 114 . 21 GLU HA H 4.01 0.01 1 115 . 21 GLU HB2 H 2.03 0.01 1 116 . 21 GLU HB3 H 2.03 0.01 1 117 . 21 GLU HG2 H 2.49 0.01 2 118 . 21 GLU HG3 H 2.27 0.01 2 119 . 22 GLN H H 7.8 0.01 1 120 . 22 GLN HA H 4.05 0.01 1 121 . 22 GLN HB2 H 2.1 0.01 1 122 . 22 GLN HB3 H 2.1 0.01 1 123 . 22 GLN HG2 H 2.17 0.01 1 124 . 22 GLN HG3 H 2.17 0.01 1 125 . 22 GLN HE21 H 6.95 0.01 1 126 . 22 GLN HE22 H 6.71 0.01 1 127 . 23 GLU H H 7.93 0.01 1 128 . 23 GLU HA H 4.08 0.01 1 129 . 23 GLU HB2 H 2.19 0.01 1 130 . 23 GLU HB3 H 2.19 0.01 1 131 . 23 GLU HG2 H 2.43 0.01 2 132 . 23 GLU HG3 H 2.23 0.01 2 133 . 24 VAL H H 8.55 0.01 1 134 . 24 VAL HA H 3.37 0.01 1 135 . 24 VAL HB H 2.15 0.01 1 136 . 24 VAL HG1 H 0.87 0.01 1 137 . 24 VAL HG2 H 1.06 0.01 1 138 . 25 ALA H H 7.62 0.01 1 139 . 25 ALA HA H 4.15 0.01 1 140 . 25 ALA HB H 1.49 0.01 1 141 . 26 GLN H H 8.01 0.01 1 142 . 26 GLN HA H 4.12 0.01 1 143 . 26 GLN HB2 H 2.26 0.01 2 144 . 26 GLN HB3 H 2.23 0.01 2 145 . 26 GLN HG2 H 2.53 0.01 2 146 . 26 GLN HG3 H 2.41 0.01 2 147 . 26 GLN HE21 H 7.58 0.01 1 148 . 26 GLN HE22 H 6.76 0.01 1 149 . 27 LEU H H 8.38 0.01 1 150 . 27 LEU HA H 4.15 0.01 1 151 . 27 LEU HB2 H 2.01 0.01 1 152 . 27 LEU HB3 H 1.39 0.01 1 153 . 27 LEU HG H 1.91 0.01 1 154 . 27 LEU HD1 H 0.89 0.01 2 155 . 27 LEU HD2 H 0.98 0.01 2 156 . 28 GLU H H 8.91 0.01 1 157 . 28 GLU HA H 3.95 0.01 1 158 . 28 GLU HB2 H 2.16 0.01 2 159 . 28 GLU HB3 H 1.94 0.01 2 160 . 28 GLU HG2 H 2.5 0.01 2 161 . 28 GLU HG3 H 2.17 0.01 2 162 . 29 HIS H H 7.73 0.01 1 163 . 29 HIS HA H 4.51 0.01 1 164 . 29 HIS HB2 H 3.48 0.01 2 165 . 29 HIS HB3 H 3.37 0.01 2 166 . 29 HIS HD2 H 7.36 0.01 1 167 . 29 HIS HE1 H 8.52 0.01 1 168 . 30 GLU H H 8.25 0.01 1 169 . 30 GLU HA H 4.19 0.01 1 170 . 30 GLU HB2 H 2.19 0.01 2 171 . 30 GLU HB3 H 2.16 0.01 2 172 . 30 GLU HG2 H 2.46 0.01 2 173 . 30 GLU HG3 H 2.37 0.01 2 174 . 31 CYS H H 8.46 0.01 1 175 . 31 CYS HA H 4.79 0.01 1 176 . 31 CYS HB2 H 3.29 0.01 2 177 . 31 CYS HB3 H 3.23 0.01 2 178 . 32 GLY H H 7.92 0.01 1 179 . 32 GLY HA2 H 3.96 0.01 2 180 . 32 GLY HA3 H 3.96 0.01 2 181 . 33 NH2 HN1 H 7.06 0.01 2 182 . 33 NH2 HN2 H 7.41 0.01 2 stop_ save_ save_chemical_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'BASIC CHAIN' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU H H 8.42 0.01 1 2 . 2 GLU HA H 4.29 0.01 1 3 . 2 GLU HB2 H 2.12 0.01 2 4 . 2 GLU HB3 H 2.03 0.01 2 5 . 2 GLU HG2 H 2.38 0.01 2 6 . 2 GLU HG3 H 2.32 0.01 2 7 . 3 VAL H H 8.38 0.01 1 8 . 3 VAL HA H 3.61 0.01 1 9 . 3 VAL HB H 2.06 0.01 1 10 . 3 VAL HG1 H 0.91 0.01 1 11 . 3 VAL HG2 H 1.03 0.01 1 12 . 4 GLN H H 8.39 0.01 1 13 . 4 GLN HA H 4 0.01 1 14 . 4 GLN HB2 H 2.19 0.01 2 15 . 4 GLN HB3 H 2.1 0.01 2 16 . 4 GLN HG2 H 2.49 0.01 1 17 . 4 GLN HG3 H 2.49 0.01 1 18 . 4 GLN HE21 H 7.52 0.01 1 19 . 4 GLN HE22 H 6.91 0.01 1 20 . 5 ALA H H 7.88 0.01 1 21 . 5 ALA HA H 4.15 0.01 1 22 . 5 ALA HB H 1.54 0.01 1 23 . 6 LEU H H 8.19 0.01 1 24 . 6 LEU HA H 4.1 0.01 1 25 . 6 LEU HB2 H 2.06 0.01 1 26 . 6 LEU HB3 H 1.39 0.01 1 27 . 6 LEU HG H 1.89 0.01 1 28 . 6 LEU HD1 H 0.93 0.01 2 29 . 6 LEU HD2 H 0.98 0.01 2 30 . 7 LYS H H 8.54 0.01 1 31 . 7 LYS HA H 3.91 0.01 1 32 . 7 LYS HB2 H 1.94 0.01 2 33 . 7 LYS HB3 H 1.88 0.01 2 34 . 7 LYS HG2 H 1.42 0.01 1 35 . 7 LYS HG3 H 1.42 0.01 1 36 . 7 LYS HD2 H 1.74 0.01 2 37 . 7 LYS HD3 H 1.66 0.01 2 38 . 7 LYS HE2 H 2.94 0.01 2 39 . 7 LYS HE3 H 2.87 0.01 2 40 . 8 LYS H H 7.84 0.01 1 41 . 8 LYS HA H 4.09 0.01 1 42 . 8 LYS HB2 H 1.96 0.01 1 43 . 8 LYS HB3 H 1.96 0.01 1 44 . 8 LYS HG2 H 1.5 0.01 1 45 . 8 LYS HG3 H 1.5 0.01 1 46 . 8 LYS HD2 H 1.72 0.01 2 47 . 8 LYS HD3 H 1.67 0.01 2 48 . 8 LYS HE2 H 3 0.01 1 49 . 8 LYS HE3 H 3 0.01 1 50 . 9 ARG H H 7.92 0.01 1 51 . 9 ARG HA H 4.2 0.01 1 52 . 9 ARG HB2 H 2.13 0.01 2 53 . 9 ARG HB3 H 2.03 0.01 2 54 . 9 ARG HG2 H 1.86 0.01 2 55 . 9 ARG HG3 H 1.7 0.01 2 56 . 9 ARG HD2 H 3.32 0.01 2 57 . 9 ARG HD3 H 3.15 0.01 2 58 . 9 ARG HE H 7.22 0.01 1 59 . 10 VAL H H 8.54 0.01 1 60 . 10 VAL HA H 3.56 0.01 1 61 . 10 VAL HB H 2.2 0.01 1 62 . 10 VAL HG1 H 1.01 0.01 1 63 . 10 VAL HG2 H 1.08 0.01 1 64 . 11 GLN H H 7.87 0.01 1 65 . 11 GLN HA H 4 0.01 1 66 . 11 GLN HB2 H 2.21 0.01 1 67 . 11 GLN HB3 H 2.21 0.01 1 68 . 11 GLN HG2 H 2.57 0.01 2 69 . 11 GLN HG3 H 2.47 0.01 2 70 . 12 ALA H H 8.15 0.01 1 71 . 12 ALA HA H 4.25 0.01 1 72 . 12 ALA HB H 1.59 0.01 1 73 . 13 LEU H H 8.42 0.01 1 74 . 13 LEU HA H 4.01 0.01 1 75 . 13 LEU HB2 H 2.03 0.01 1 76 . 13 LEU HB3 H 1.31 0.01 1 77 . 13 LEU HG H 1.85 0.01 1 78 . 13 LEU HD1 H 0.88 0.01 2 79 . 13 LEU HD2 H 1.01 0.01 2 80 . 14 LYS H H 8.69 0.01 1 81 . 14 LYS HA H 4.05 0.01 1 82 . 14 LYS HB2 H 1.99 0.01 2 83 . 14 LYS HB3 H 1.89 0.01 2 84 . 14 LYS HG2 H 1.48 0.01 1 85 . 14 LYS HG3 H 1.48 0.01 1 86 . 14 LYS HD2 H 1.74 0.01 2 87 . 14 LYS HD3 H 1.7 0.01 2 88 . 14 LYS HE2 H 2.95 0.01 1 89 . 14 LYS HE3 H 2.95 0.01 1 90 . 15 ALA H H 7.83 0.01 1 91 . 15 ALA HA H 4.35 0.01 1 92 . 15 ALA HB H 1.6 0.01 1 93 . 16 ARG H H 8.07 0.01 1 94 . 16 ARG HA H 4.2 0.01 1 95 . 16 ARG HB2 H 2.02 0.01 1 96 . 16 ARG HB3 H 2.02 0.01 1 97 . 16 ARG HG2 H 1.92 0.01 2 98 . 16 ARG HG3 H 1.76 0.01 2 99 . 16 ARG HD2 H 3.27 0.01 2 100 . 16 ARG HD3 H 3.15 0.01 2 101 . 16 ARG HE H 7.56 0.01 1 102 . 17 ASN H H 8.97 0.01 1 103 . 17 ASN HA H 4.53 0.01 1 104 . 17 ASN HB2 H 3.06 0.01 1 105 . 17 ASN HB3 H 2.71 0.01 1 106 . 17 ASN HD21 H 7.71 0.01 1 107 . 17 ASN HD22 H 6.82 0.01 1 108 . 18 TYR H H 8.36 0.01 1 109 . 18 TYR HA H 4.21 0.01 1 110 . 18 TYR HB2 H 3.28 0.01 2 111 . 18 TYR HB3 H 3.19 0.01 2 112 . 18 TYR HD1 H 7.2 0.01 1 113 . 18 TYR HD2 H 7.2 0.01 1 114 . 18 TYR HE1 H 6.84 0.01 1 115 . 18 TYR HE2 H 6.84 0.01 1 116 . 19 ALA H H 7.81 0.01 1 117 . 19 ALA HA H 4.15 0.01 1 118 . 19 ALA HB H 1.61 0.01 1 119 . 20 ALA H H 8.42 0.01 1 120 . 20 ALA HA H 4.2 0.01 1 121 . 20 ALA HB H 1.54 0.01 1 122 . 21 LYS H H 8.47 0.01 1 123 . 21 LYS HA H 3.87 0.01 1 124 . 21 LYS HB2 H 1.94 0.01 2 125 . 21 LYS HB3 H 1.89 0.01 2 126 . 21 LYS HG2 H 1.45 0.01 1 127 . 21 LYS HG3 H 1.45 0.01 1 128 . 21 LYS HD2 H 1.69 0.01 1 129 . 21 LYS HD3 H 1.69 0.01 1 130 . 21 LYS HE2 H 2.95 0.01 1 131 . 21 LYS HE3 H 2.95 0.01 1 132 . 22 GLN H H 7.74 0.01 1 133 . 22 GLN HA H 3.98 0.01 1 134 . 22 GLN HB2 H 2.11 0.01 1 135 . 22 GLN HB3 H 2.11 0.01 1 136 . 22 GLN HG2 H 2.24 0.01 1 137 . 22 GLN HG3 H 2.24 0.01 1 138 . 22 GLN HE21 H 6.84 0.01 1 139 . 22 GLN HE22 H 6.74 0.01 1 140 . 23 LYS H H 7.84 0.01 1 141 . 23 LYS HA H 4.15 0.01 1 142 . 23 LYS HB2 H 2.03 0.01 2 143 . 23 LYS HB3 H 2 0.01 2 144 . 23 LYS HG2 H 1.44 0.01 1 145 . 23 LYS HG3 H 1.44 0.01 1 146 . 23 LYS HD2 H 1.74 0.01 1 147 . 23 LYS HD3 H 1.74 0.01 1 148 . 23 LYS HE2 H 2.94 0.01 1 149 . 23 LYS HE3 H 2.94 0.01 1 150 . 24 VAL H H 8.57 0.01 1 151 . 24 VAL HA H 3.48 0.01 1 152 . 24 VAL HB H 2.15 0.01 1 153 . 24 VAL HG1 H 0.88 0.01 1 154 . 24 VAL HG2 H 1.05 0.01 1 155 . 25 GLN H H 7.75 0.01 1 156 . 25 GLN HA H 3.92 0.01 1 157 . 25 GLN HB2 H 2.13 0.01 1 158 . 25 GLN HB3 H 2.13 0.01 1 159 . 25 GLN HG2 H 2.49 0.01 2 160 . 25 GLN HG3 H 2.4 0.01 2 161 . 26 ALA H H 7.86 0.01 1 162 . 26 ALA HA H 4.22 0.01 1 163 . 26 ALA HB H 1.57 0.01 1 164 . 27 LEU H H 8.55 0.01 1 165 . 27 LEU HA H 4.12 0.01 1 166 . 27 LEU HB2 H 2.02 0.01 1 167 . 27 LEU HB3 H 1.39 0.01 1 168 . 27 LEU HG H 1.88 0.01 1 169 . 27 LEU HD1 H 0.88 0.01 2 170 . 27 LEU HD2 H 0.96 0.01 2 171 . 28 ARG H H 8.7 0.01 1 172 . 28 ARG HA H 3.99 0.01 1 173 . 28 ARG HB2 H 1.88 0.01 2 174 . 28 ARG HB3 H 1.8 0.01 2 175 . 28 ARG HG2 H 1.64 0.01 1 176 . 28 ARG HG3 H 1.64 0.01 1 177 . 28 ARG HD2 H 3.17 0.01 2 178 . 28 ARG HD3 H 3.06 0.01 2 179 . 28 ARG HE H 7.13 0.01 1 180 . 29 HIS H H 7.74 0.01 1 181 . 29 HIS HA H 4.49 0.01 1 182 . 29 HIS HB2 H 3.36 0.01 2 183 . 29 HIS HB3 H 3.29 0.01 2 184 . 29 HIS HD2 H 7.26 0.01 1 185 . 29 HIS HE1 H 8.28 0.01 1 186 . 30 LYS H H 7.91 0.01 1 187 . 30 LYS HA H 4.22 0.01 1 188 . 30 LYS HB2 H 2.06 0.01 2 189 . 30 LYS HB3 H 2 0.01 2 190 . 30 LYS HG2 H 1.57 0.01 2 191 . 30 LYS HG3 H 1.5 0.01 2 192 . 30 LYS HD2 H 1.72 0.01 1 193 . 30 LYS HD3 H 1.72 0.01 1 194 . 30 LYS HE2 H 3.03 0.01 1 195 . 30 LYS HE3 H 3.03 0.01 1 196 . 31 CYS H H 8.3 0.01 1 197 . 31 CYS HA H 4.67 0.01 1 198 . 31 CYS HB2 H 3.36 0.01 2 199 . 31 CYS HB3 H 3.18 0.01 2 200 . 32 GLY H H 8 0.01 1 201 . 32 GLY HA2 H 3.97 0.01 2 202 . 32 GLY HA3 H 3.97 0.01 2 203 . 33 NH2 HN1 H 7.07 0.01 2 204 . 33 NH2 HN2 H 7.33 0.01 2 stop_ save_