data_15316 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Electrostatic contributions to the stability of the GCN4 leucine zipper structure. ; _BMRB_accession_number 15316 _BMRB_flat_file_name bmr15316.str _Entry_type original _Submission_date 2007-06-19 _Accession_date 2007-06-19 _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 Matousek William M. . 2 Alexandrescu Andrei T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 182 "13C chemical shifts" 142 "15N chemical shifts" 31 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 7391 'denatured protein' stop_ _Original_release_date 2009-08-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Electrostatic contributions to the stability of the GCN4 leucine zipper structure.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17920624 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Matousek William M. . 2 Ciani Barbara . . 3 Fitch Carolyn A. . 4 Garcia-Moreno Bertrand E. . 5 Kammerer Richard A. . 6 Alexandrescu Andrei T. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 374 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 206 _Page_last 219 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name GCN4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GCN4 $GCN4p-wt stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GCN4p-wt _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GCN4p-wt _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; GSMKQLEDKVEELLSKNYHL ENEVARLKKLVGE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 MET 4 LYS 5 GLN 6 LEU 7 GLU 8 ASP 9 LYS 10 VAL 11 GLU 12 GLU 13 LEU 14 LEU 15 SER 16 LYS 17 ASN 18 TYR 19 HIS 20 LEU 21 GLU 22 ASN 23 GLU 24 VAL 25 ALA 26 ARG 27 LEU 28 LYS 29 LYS 30 LEU 31 VAL 32 GLY 33 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 1396 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1397 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1398 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1399 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1451 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1452 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1453 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 1454 "transcriptional regulator GCN4" 93.94 61 100.00 100.00 2.21e-11 BMRB 17511 LZ-GCN4 93.94 36 100.00 100.00 1.05e-10 BMRB 2062 "transcriptional regulator GCN4-p2N" 100.00 37 96.97 96.97 1.22e-11 BMRB 371 "transcriptional regulator GCN4" 93.94 33 100.00 100.00 1.02e-10 PDB 1DGC "The X-Ray Structure Of The Gcn4-Bzip Bound To AtfCREB SITE Dna Shows The Complex Depends On Dna Flexibility" 93.94 62 100.00 100.00 2.30e-11 PDB 1LD4 "Placement Of The Structural Proteins In Sindbis Virus" 93.94 57 100.00 100.00 2.25e-11 PDB 1LLM "Crystal Structure Of A Zif23-Gcn4 Chimera Bound To Dna" 84.85 88 100.00 100.00 9.56e-09 PDB 1NKN "Visualizing An Unstable Coiled Coil: The Crystal Structure Of An N-Terminal Segment Of The Scallop Myosin Rod" 100.00 89 100.00 100.00 2.79e-12 PDB 1YSA "The Gcn4 Basic Region Leucine Zipper Binds Dna As A Dimer Of Uninterrupted Alpha Helices: Crystal Structure Of The Protein-Dna " 93.94 58 100.00 100.00 2.75e-11 PDB 1ZTA "The Solution Structure Of A Leucine-Zipper Motif Peptide" 93.94 35 100.00 100.00 9.03e-11 PDB 2DGC "Gcn4 Basic Domain, Leucine Zipper Complexed With AtfCREB Site Dna" 93.94 63 100.00 100.00 2.27e-11 PDB 2EFR "Crystal Structure Of The C-Terminal Tropomyosin Fragment With N- And C-Terminal Extensions Of The Leucine Zipper At 1.8 Angstro" 84.85 155 100.00 100.00 2.35e-08 PDB 2EFS "Crystal Structure Of The C-Terminal Tropomyosin Fragment With N- And C-Terminal Extensions Of The Leucine Zipper At 2.0 Angstro" 84.85 155 100.00 100.00 2.35e-08 PDB 2OVN "Nmr Structure Of The Gcn4 Trigger Peptide" 51.52 17 100.00 100.00 1.51e-01 PDB 2ZTA "X-Ray Structure Of The Gcn4 Leucine Zipper, A Two-Stranded, Parallel Coiled Coil" 93.94 34 100.00 100.00 9.83e-11 PDB 3BAS "Crystal Structure Of The N-Terminal Region Of The Scallop Myosin Rod, Monoclinic (C2) Form" 100.00 89 100.00 100.00 2.79e-12 PDB 3BAT "Crystal Structure Of The N-Terminal Region Of The Scallop Myosin Rod, Monoclinic (P21) Form" 100.00 89 100.00 100.00 2.79e-12 PDB 3I5C "Crystal Structure Of A Fusion Protein Containing The Leucine Zipper Of Gcn4 And The Ggdef Domain Of Wspr From Pseudomonas Aerug" 87.88 206 100.00 100.00 3.84e-09 PDB 4DMD "Gcn4 Leucine Zipper Domain In A Dimeric Oligomerization State" 93.94 34 100.00 100.00 9.83e-11 PDB 4DME "Gcn4 Leucine Zipper Domain In A Trimeric Oligomerization State" 93.94 35 100.00 100.00 9.95e-11 PDB 4LPZ "Arnt Transcription Factor/coactivator Complex" 51.52 44 100.00 100.00 6.57e-02 DBJ GAA22815 "K7_Gcn4p [Saccharomyces cerevisiae Kyokai no. 7]" 93.94 281 100.00 100.00 6.78e-11 EMBL CAE52206 "Gcn4p [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.85e-11 EMBL CAE52207 "Gcn4p [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.85e-11 EMBL CAE52208 "Gcn4p [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.85e-11 EMBL CAE52209 "Gcn4p [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.85e-11 EMBL CAE52210 "Gcn4p [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.78e-11 GB AAA34640 "GCN4 protein [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.93e-11 GB AAB64486 "Transcriptional activator of amino acid biosynthetic genes [Saccharomyces cerevisiae]" 93.94 281 100.00 100.00 6.93e-11 GB AAC33186 "hinge-region and leucine-zipper with N-terminal PelB-leader and C-terminal hexahistidine tag [synthetic construct]" 93.94 84 100.00 100.00 4.47e-11 GB AAD37724 "PelB-IgG kappa light chain fusion protein [Cloning vector pCLZip]" 93.94 192 100.00 100.00 8.81e-11 GB AAK07887 "cI-GCN4 repressor fusion protein [Cloning vector pJH370]" 93.94 166 100.00 100.00 1.52e-10 REF NP_010907 "amino acid starvation-responsive transcription factor GCN4 [Saccharomyces cerevisiae S288c]" 93.94 281 100.00 100.00 6.93e-11 SP P03069 "RecName: Full=General control protein GCN4; AltName: Full=Amino acid biosynthesis regulatory protein" 93.94 281 100.00 100.00 6.93e-11 TPG DAA07643 "TPA: amino acid starvation-responsive transcription factor GCN4 [Saccharomyces cerevisiae S288c]" 93.94 281 100.00 100.00 6.93e-11 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GCN4p-wt 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $GCN4p-wt 'recombinant technology' . Escherichia coli BL21 NA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Native_GCN4p-wt_1 _Saveframe_category sample _Sample_type solution _Details '2.1mM 13C/15N GCN4p-wt, 150 mM NaCl, 10 mM phosphate buffer, pH 6.2, 25C' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GCN4p-wt 2.1 mM '[U-13C; U-15N]' 'sodium chloride' 150 mM 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 2000.1 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details Cryoprobe save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Native_GCN4p-wt_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Native_GCN4p-wt_1 save_ save_3D_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $Native_GCN4p-wt_1 save_ save_3D_1H-13C_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $Native_GCN4p-wt_1 save_ ####################### # Sample conditions # ####################### save_Native_GCN4p-wt_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . pH temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_native_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $Felix stop_ loop_ _Experiment_label '3D HNCACB' '3D HNCO' '3D HCCH-TOCSY' '3D 1H-13C NOESY' stop_ loop_ _Sample_label $Native_GCN4p-wt_1 stop_ _Sample_conditions_label $Native_GCN4p-wt_cond _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name GCN4 _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 0 1 GLY HA2 H 3.87 . . 2 0 1 GLY HA3 H 3.83 . . 3 0 1 GLY C C 175.0 . . 4 0 1 GLY CA C 43.4 . . 5 1 2 SER HA H 4.11 . . 6 1 2 SER C C 175.0 . . 7 1 2 SER CB C 64.5 . . 8 2 3 MET H H 8.94 . . 9 2 3 MET HA H 4.18 . . 10 2 3 MET HB2 H 2.49 . . 11 2 3 MET HB3 H 2.17 . . 12 2 3 MET HG2 H 2.57 . . 13 2 3 MET HG3 H 2.57 . . 14 2 3 MET C C 176.7 . . 15 2 3 MET CA C 58.2 . . 16 2 3 MET CB C 31.6 . . 17 2 3 MET CG C 31.9 . . 18 2 3 MET N N 122.6 . . 19 3 4 LYS H H 8.22 . . 20 3 4 LYS HA H 4.11 . . 21 3 4 LYS HB2 H 1.76 . . 22 3 4 LYS HB3 H 1.44 . . 23 3 4 LYS HE2 H 3.03 . . 24 3 4 LYS HE3 H 3.03 . . 25 3 4 LYS HG2 H 1.60 . . 26 3 4 LYS HG3 H 1.60 . . 27 3 4 LYS C C 177.3 . . 28 3 4 LYS CA C 58.2 . . 29 3 4 LYS CB C 31.6 . . 30 3 4 LYS CD C 27.9 . . 31 3 4 LYS CE C 41.7 . . 32 3 4 LYS CG C 23.9 . . 33 3 4 LYS N N 119.8 . . 34 4 5 GLN H H 7.76 . . 35 4 5 GLN HA H 4.13 . . 36 4 5 GLN HG2 H 2.44 . . 37 4 5 GLN HG3 H 2.44 . . 38 4 5 GLN C C 180.1 . . 39 4 5 GLN CA C 58.6 . . 40 4 5 GLN CB C 27.9 . . 41 4 5 GLN CG C 34.0 . . 42 4 5 GLN N N 117.0 . . 43 5 6 LEU H H 7.85 . . 44 5 6 LEU HA H 4.13 . . 45 5 6 LEU HB2 H 1.44 . . 46 5 6 LEU HB3 H 1.44 . . 47 5 6 LEU HD1 H 0.87 . . 48 5 6 LEU HD2 H 0.87 . . 49 5 6 LEU C C 180.4 . . 50 5 6 LEU CA C 57.2 . . 51 5 6 LEU CB C 42.3 . . 52 5 6 LEU CD1 C 23.1 . . 53 5 6 LEU CD2 C 22.0 . . 54 5 6 LEU CG C 25.7 . . 55 5 6 LEU N N 121.4 . . 56 6 7 GLU H H 8.70 . . 57 6 7 GLU HA H 3.75 . . 58 6 7 GLU HB2 H 2.25 . . 59 6 7 GLU HB3 H 2.25 . . 60 6 7 GLU HG2 H 2.50 . . 61 6 7 GLU HG3 H 2.18 . . 62 6 7 GLU C C 180.4 . . 63 6 7 GLU CA C 59.6 . . 64 6 7 GLU CB C 29.3 . . 65 6 7 GLU CG C 35.3 . . 66 6 7 GLU N N 115.7 . . 67 7 8 ASP H H 8.68 . . 68 7 8 ASP HA H 4.35 . . 69 7 8 ASP HB2 H 2.86 . . 70 7 8 ASP HB3 H 2.71 . . 71 7 8 ASP C C 178.9 . . 72 7 8 ASP CA C 56.8 . . 73 7 8 ASP CB C 39.1 . . 74 7 8 ASP N N 120.2 . . 75 8 9 LYS H H 7.91 . . 76 8 9 LYS HA H 4.19 . . 77 8 9 LYS HB2 H 1.60 . . 78 8 9 LYS HB3 H 1.76 . . 79 8 9 LYS HE2 H 3.06 . . 80 8 9 LYS HE3 H 3.06 . . 81 8 9 LYS C C 179.5 . . 82 8 9 LYS CA C 57.7 . . 83 8 9 LYS CB C 30.7 . . 84 8 9 LYS CD C 27.3 . . 85 8 9 LYS CE C 41.9 . . 86 8 9 LYS CG C 23.9 . . 87 8 9 LYS N N 123.7 . . 88 9 10 VAL H H 8.46 . . 89 9 10 VAL HA H 3.38 . . 90 9 10 VAL HB H 2.25 . . 91 9 10 VAL HG1 H 1.04 . . 92 9 10 VAL HG2 H 0.88 . . 93 9 10 VAL C C 177.3 . . 94 9 10 VAL CA C 67.5 . . 95 9 10 VAL CB C 31.1 . . 96 9 10 VAL CG1 C 24.4 . . 97 9 10 VAL CG2 C 20.7 . . 98 9 10 VAL N N 120.3 . . 99 10 11 GLU H H 7.76 . . 100 10 11 GLU HA H 3.94 . . 101 10 11 GLU HB2 H 2.08 . . 102 10 11 GLU HB3 H 2.08 . . 103 10 11 GLU HG2 H 2.19 . . 104 10 11 GLU HG3 H 2.19 . . 105 10 11 GLU C C 179.5 . . 106 10 11 GLU CA C 59.1 . . 107 10 11 GLU CB C 28.8 . . 108 10 11 GLU CG C 35.4 . . 109 10 11 GLU N N 117.6 . . 110 11 12 GLU H H 8.15 . . 111 11 12 GLU HA H 4.43 . . 112 11 12 GLU HB2 H 2.09 . . 113 11 12 GLU HB3 H 2.09 . . 114 11 12 GLU HG2 H 2.41 . . 115 11 12 GLU HG3 H 2.33 . . 116 11 12 GLU C C 179.7 . . 117 11 12 GLU CA C 58.1 . . 118 11 12 GLU CB C 29.3 . . 119 11 12 GLU CG C 35.5 . . 120 11 12 GLU N N 121.2 . . 121 12 13 LEU H H 8.68 . . 122 12 13 LEU HA H 4.03 . . 123 12 13 LEU HB2 H 1.28 . . 124 12 13 LEU HB3 H 1.28 . . 125 12 13 LEU HD1 H 0.87 . . 126 12 13 LEU HD2 H 0.87 . . 127 12 13 LEU C C 179.6 . . 128 12 13 LEU CA C 57.7 . . 129 12 13 LEU CB C 42.8 . . 130 12 13 LEU CD1 C 22.3 . . 131 12 13 LEU CD2 C 22.3 . . 132 12 13 LEU CG C 27.3 . . 133 12 13 LEU N N 120.8 . . 134 13 14 LEU H H 9.07 . . 135 13 14 LEU HA H 4.10 . . 136 13 14 LEU HB2 H 1.92 . . 137 13 14 LEU HB3 H 1.92 . . 138 13 14 LEU HD1 H 0.87 . . 139 13 14 LEU HD2 H 0.87 . . 140 13 14 LEU C C 180.0 . . 141 13 14 LEU CA C 57.7 . . 142 13 14 LEU CB C 41.4 . . 143 13 14 LEU CD1 C 23.4 . . 144 13 14 LEU CD2 C 23.4 . . 145 13 14 LEU CG C 25.5 . . 146 13 14 LEU N N 122.3 . . 147 14 15 SER H H 7.80 . . 148 14 15 SER HA H 4.10 . . 149 14 15 SER HB2 H 4.10 . . 150 14 15 SER HB3 H 4.10 . . 151 14 15 SER C C 177.8 . . 152 14 15 SER CA C 61.0 . . 153 14 15 SER CB C 62.4 . . 154 14 15 SER N N 114.8 . . 155 15 16 LYS H H 8.32 . . 156 15 16 LYS HA H 4.14 . . 157 15 16 LYS HB2 H 1.84 . . 158 15 16 LYS HB3 H 1.68 . . 159 15 16 LYS HE2 H 2.94 . . 160 15 16 LYS HE3 H 2.94 . . 161 15 16 LYS HG2 H 1.44 . . 162 15 16 LYS HG3 H 1.44 . . 163 15 16 LYS C C 178.9 . . 164 15 16 LYS CA C 59.1 . . 165 15 16 LYS CB C 32.5 . . 166 15 16 LYS CD C 25.2 . . 167 15 16 LYS CE C 41.5 . . 168 15 16 LYS CG C 28.9 . . 169 15 16 LYS N N 122.7 . . 170 16 17 ASN H H 8.84 . . 171 16 17 ASN HA H 4.34 . . 172 16 17 ASN HB2 H 3.30 . . 173 16 17 ASN HB3 H 2.73 . . 174 16 17 ASN C C 177.4 . . 175 16 17 ASN CA C 56.8 . . 176 16 17 ASN CB C 38.6 . . 177 16 17 ASN N N 119.9 . . 178 17 18 TYR H H 8.23 . . 179 17 18 TYR HA H 4.39 . . 180 17 18 TYR HB2 H 3.22 . . 181 17 18 TYR HB3 H 3.22 . . 182 17 18 TYR HD1 H 7.07 . . 183 17 18 TYR HD2 H 7.07 . . 184 17 18 TYR HE1 H 6.82 . . 185 17 18 TYR HE2 H 6.82 . . 186 17 18 TYR C C 178.2 . . 187 17 18 TYR CA C 60.5 . . 188 17 18 TYR CB C 37.7 . . 189 17 18 TYR N N 120.4 . . 190 18 19 HIS H H 7.87 . . 191 18 19 HIS HA H 4.37 . . 192 18 19 HIS HB2 H 3.38 . . 193 18 19 HIS HB3 H 3.38 . . 194 18 19 HIS HD2 H 7.23 . . 195 18 19 HIS HE1 H 8.22 . . 196 18 19 HIS C C 178.4 . . 197 18 19 HIS CA C 59.1 . . 198 18 19 HIS CB C 28.3 . . 199 18 19 HIS N N 117.0 . . 200 19 20 LEU H H 8.60 . . 201 19 20 LEU HA H 3.99 . . 202 19 20 LEU HB2 H 1.28 . . 203 19 20 LEU HB3 H 1.28 . . 204 19 20 LEU HD1 H 0.94 . . 205 19 20 LEU HD2 H 0.94 . . 206 19 20 LEU HG H 2.09 . . 207 19 20 LEU C C 178.9 . . 208 19 20 LEU CA C 57.7 . . 209 19 20 LEU CB C 43.2 . . 210 19 20 LEU CG C 26.3 . . 211 19 20 LEU N N 121.2 . . 212 20 21 GLU H H 8.87 . . 213 20 21 GLU HA H 3.86 . . 214 20 21 GLU HB2 H 2.25 . . 215 20 21 GLU HB3 H 2.25 . . 216 20 21 GLU HG2 H 2.49 . . 217 20 21 GLU HG3 H 2.25 . . 218 20 21 GLU C C 180.5 . . 219 20 21 GLU CA C 59.6 . . 220 20 21 GLU CB C 28.8 . . 221 20 21 GLU CG C 36.4 . . 222 20 21 GLU N N 119.8 . . 223 21 22 ASN H H 7.76 . . 224 21 22 ASN HA H 4.45 . . 225 21 22 ASN HB2 H 2.73 . . 226 21 22 ASN HB3 H 2.81 . . 227 21 22 ASN C C 178.1 . . 228 21 22 ASN CA C 55.4 . . 229 21 22 ASN CB C 37.2 . . 230 21 22 ASN N N 119.2 . . 231 22 23 GLU H H 8.02 . . 232 22 23 GLU HA H 4.43 . . 233 22 23 GLU HB2 H 2.09 . . 234 22 23 GLU HB3 H 2.09 . . 235 22 23 GLU HG2 H 2.25 . . 236 22 23 GLU HG3 H 2.16 . . 237 22 23 GLU C C 178.3 . . 238 22 23 GLU CA C 58.2 . . 239 22 23 GLU CB C 29.7 . . 240 22 23 GLU CG C 36.3 . . 241 22 23 GLU N N 124.0 . . 242 23 24 VAL H H 8.70 . . 243 23 24 VAL HA H 3.40 . . 244 23 24 VAL HB H 2.08 . . 245 23 24 VAL HG1 H 1.04 . . 246 23 24 VAL HG2 H 0.88 . . 247 23 24 VAL C C 177.5 . . 248 23 24 VAL CA C 67.0 . . 249 23 24 VAL CB C 31.1 . . 250 23 24 VAL CG1 C 25.0 . . 251 23 24 VAL CG2 C 21.0 . . 252 23 24 VAL N N 120.3 . . 253 24 25 ALA H H 7.77 . . 254 24 25 ALA HA H 4.04 . . 255 24 25 ALA HB H 1.44 . . 256 24 25 ALA C C 180.5 . . 257 24 25 ALA CA C 54.9 . . 258 24 25 ALA CB C 17.6 . . 259 24 25 ALA N N 120.0 . . 260 25 26 ARG H H 7.92 . . 261 25 26 ARG HA H 4.00 . . 262 25 26 ARG HB2 H 1.84 . . 263 25 26 ARG HB3 H 1.84 . . 264 25 26 ARG HD2 H 3.42 . . 265 25 26 ARG HD3 H 2.99 . . 266 25 26 ARG HG2 H 2.17 . . 267 25 26 ARG HG3 H 2.17 . . 268 25 26 ARG C C 178.5 . . 269 25 26 ARG CA C 59.1 . . 270 25 26 ARG CB C 30.2 . . 271 25 26 ARG CD C 42.4 . . 272 25 26 ARG CG C 26.8 . . 273 25 26 ARG N N 119.9 . . 274 26 27 LEU H H 8.45 . . 275 26 27 LEU HA H 3.94 . . 276 26 27 LEU HB2 H 1.92 . . 277 26 27 LEU HB3 H 1.28 . . 278 26 27 LEU HD1 H 0.87 . . 279 26 27 LEU HD2 H 0.87 . . 280 26 27 LEU C C 179.2 . . 281 26 27 LEU CA C 57.7 . . 282 26 27 LEU CB C 43.7 . . 283 26 27 LEU CD1 C 23.1 . . 284 26 27 LEU CD2 C 23.1 . . 285 26 27 LEU CG C 27.3 . . 286 26 27 LEU N N 120.6 . . 287 27 28 LYS H H 9.02 . . 288 27 28 LYS HA H 3.78 . . 289 27 28 LYS HB2 H 1.76 . . 290 27 28 LYS HB3 H 1.28 . . 291 27 28 LYS HE2 H 2.89 . . 292 27 28 LYS HE3 H 2.89 . . 293 27 28 LYS HG2 H 1.60 . . 294 27 28 LYS HG3 H 1.60 . . 295 27 28 LYS C C 179.5 . . 296 27 28 LYS CA C 60.5 . . 297 27 28 LYS CB C 32.1 . . 298 27 28 LYS CD C 29.2 . . 299 27 28 LYS CE C 41.4 . . 300 27 28 LYS CG C 27.1 . . 301 27 28 LYS N N 118.8 . . 302 28 29 LYS H H 7.30 . . 303 28 29 LYS HA H 4.11 . . 304 28 29 LYS HB2 H 1.92 . . 305 28 29 LYS HB3 H 1.68 . . 306 28 29 LYS HE2 H 3.01 . . 307 28 29 LYS HE3 H 3.01 . . 308 28 29 LYS HG2 H 1.52 . . 309 28 29 LYS HG3 H 1.52 . . 310 28 29 LYS C C 179.3 . . 311 28 29 LYS CA C 58.2 . . 312 28 29 LYS CB C 32.1 . . 313 28 29 LYS CD C 28.4 . . 314 28 29 LYS CE C 41.2 . . 315 28 29 LYS CG C 24.7 . . 316 28 29 LYS N N 117.1 . . 317 29 30 LEU H H 7.42 . . 318 29 30 LEU HA H 4.18 . . 319 29 30 LEU HB2 H 1.60 . . 320 29 30 LEU HB3 H 1.60 . . 321 29 30 LEU HD1 H 0.96 . . 322 29 30 LEU HD2 H 0.96 . . 323 29 30 LEU HG H 2.09 . . 324 29 30 LEU C C 179.1 . . 325 29 30 LEU CA C 56.8 . . 326 29 30 LEU CB C 42.3 . . 327 29 30 LEU CD1 C 22.3 . . 328 29 30 LEU CD2 C 22.3 . . 329 29 30 LEU CG C 25.0 . . 330 29 30 LEU N N 118.8 . . 331 30 31 VAL H H 7.67 . . 332 30 31 VAL HA H 4.11 . . 333 30 31 VAL HB H 2.17 . . 334 30 31 VAL HG1 H 0.96 . . 335 30 31 VAL HG2 H 0.96 . . 336 30 31 VAL C C 176.5 . . 337 30 31 VAL CA C 61.9 . . 338 30 31 VAL CB C 32.1 . . 339 30 31 VAL CG1 C 21.2 . . 340 30 31 VAL CG2 C 21.2 . . 341 30 31 VAL N N 113.4 . . 342 31 32 GLY H H 7.87 . . 343 31 32 GLY HA2 H 4.11 . . 344 31 32 GLY HA3 H 3.86 . . 345 31 32 GLY C C 174.4 . . 346 31 32 GLY CA C 45.6 . . 347 31 32 GLY N N 109.8 . . 348 32 33 GLU H H 7.83 . . 349 32 33 GLU HA H 4.21 . . 350 32 33 GLU HG2 H 2.33 . . 351 32 33 GLU HG3 H 2.12 . . 352 32 33 GLU CA C 57.2 . . 353 32 33 GLU CB C 21.6 . . 354 32 33 GLU CG C 35.5 . . 355 32 33 GLU N N 125.7 . . stop_ save_