data_5174 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators ; _BMRB_accession_number 5174 _BMRB_flat_file_name bmr5174.str _Entry_type original _Submission_date 2001-10-11 _Accession_date 2001-10-11 _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 Hosoda Kazuo . . 2 Imamura A. . . 3 Katoh Etsuko . . 4 Hatta T. . . 5 Tachiki M. . . 6 Yamada H. . . 7 Mizuno Takeshi . . 8 Yamazaki Toshimasa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 374 "13C chemical shifts" 302 "15N chemical shifts" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-12 original author . stop_ _Original_release_date 2002-09-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22204429 _PubMed_ID 12215502 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hosoda Kazuo . . 2 Imamura A. . . 3 Katoh Etsuko . . 4 Hatta T. . . 5 Tachiki M. . . 6 Yamada H. . . 7 Mizuno Takeshi . . 8 Yamazaki Toshimasa . . stop_ _Journal_abbreviation 'Plant Cell' _Journal_volume 14 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2015 _Page_last 2029 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_ARR10 _Saveframe_category molecular_system _Mol_system_name ARR10 _Abbreviation_common ARR10 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ARR10 monomer' $ARR10 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ARR10 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ARR10 _Abbreviation_common B-motif _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; TAQKKPRVLWTHELHNKFLA AVDHLGVERAVPKKILDLMN VDKLTRENVASHLQKFRVAL KKVS ; loop_ _Residue_seq_code _Residue_label 1 THR 2 ALA 3 GLN 4 LYS 5 LYS 6 PRO 7 ARG 8 VAL 9 LEU 10 TRP 11 THR 12 HIS 13 GLU 14 LEU 15 HIS 16 ASN 17 LYS 18 PHE 19 LEU 20 ALA 21 ALA 22 VAL 23 ASP 24 HIS 25 LEU 26 GLY 27 VAL 28 GLU 29 ARG 30 ALA 31 VAL 32 PRO 33 LYS 34 LYS 35 ILE 36 LEU 37 ASP 38 LEU 39 MET 40 ASN 41 VAL 42 ASP 43 LYS 44 LEU 45 THR 46 ARG 47 GLU 48 ASN 49 VAL 50 ALA 51 SER 52 HIS 53 LEU 54 GLN 55 LYS 56 PHE 57 ARG 58 VAL 59 ALA 60 LEU 61 LYS 62 LYS 63 VAL 64 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1IRZ "Solution Structure Of Arr10-B Belonging To The Garp Family Of Plant Myb-Related Dna Binding Motifs Of The Arabidopsis Response " 100.00 64 100.00 100.00 8.74e-37 DBJ BAF00105 "predicted protein [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 EMBL CAA06432 "receiver-like protein 4 [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 EMBL CAA16597 "predicted protein [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 EMBL CAB79910 "predicted protein [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 GB AAO24590 "At4g31920 [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 GB AEE85979 "two-component response regulator ARR10 [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 REF NP_194920 "two-component response regulator ARR10 [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 REF XP_010432800 "PREDICTED: LOW QUALITY PROTEIN: two-component response regulator ARR10-like [Camelina sativa]" 100.00 576 98.44 100.00 5.50e-33 REF XP_010447471 "PREDICTED: LOW QUALITY PROTEIN: two-component response regulator ARR10 [Camelina sativa]" 100.00 548 98.44 100.00 1.69e-33 SP O49397 "RecName: Full=Two-component response regulator ARR10; AltName: Full=Receiver-like protein 4 [Arabidopsis thaliana]" 100.00 552 100.00 100.00 1.02e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $ARR10 Arabidopsis 3701 Eukaryota Viridiplantae Arabidopsis . 'Response regulator' 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 $ARR10 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid . 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 $ARR10 1.0 mM '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_B-motif-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.1 n/a temperature 288 1 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 TSP H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel TSP C 13 'methyl protons' ppm 0.00 external indirect spherical internal parallel 'liquid ammonia' N 15 nitrogen ppm 0.00 external indirect spherical internal parallel 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $B-motif-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ARR10 monomer' _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 THR HA H 3.85 . 1 2 . 1 THR HB H 4.22 . 1 3 . 1 THR HG2 H 1.4 . 1 4 . 1 THR C C 172.68 . 1 5 . 1 THR CA C 61.7 . 1 6 . 1 THR CB C 69.93 . 1 7 . 1 THR CG2 C 21.63 . 1 8 . 2 ALA HA H 4.48 . 1 9 . 2 ALA HB H 1.5 . 1 10 . 2 ALA C C 177.64 . 1 11 . 2 ALA CA C 52.79 . 1 12 . 2 ALA CB C 19.49 . 1 13 . 3 GLN H H 8.55 . 1 14 . 3 GLN HA H 4.4 . 1 15 . 3 GLN HB2 H 2.17 . 2 16 . 3 GLN HB3 H 2.07 . 2 17 . 3 GLN HG2 H 2.48 . 1 18 . 3 GLN HG3 H 2.48 . 1 19 . 3 GLN HE21 H 7.64 . 2 20 . 3 GLN HE22 H 6.98 . 2 21 . 3 GLN C C 176.12 . 1 22 . 3 GLN CA C 55.96 . 1 23 . 3 GLN CB C 29.83 . 1 24 . 3 GLN CG C 34.1 . 1 25 . 3 GLN CD C 180.74 . 1 26 . 3 GLN N N 120.3 . 1 27 . 3 GLN NE2 N 112.64 . 1 28 . 4 LYS H H 8.51 . 1 29 . 4 LYS HA H 4.41 . 1 30 . 4 LYS C C 176.51 . 1 31 . 4 LYS CA C 56.42 . 1 32 . 4 LYS CB C 33.35 . 1 33 . 4 LYS CG C 25.05 . 1 34 . 4 LYS CD C 29.33 . 1 35 . 4 LYS CE C 42.43 . 1 36 . 4 LYS N N 123.38 . 1 37 . 5 LYS H H 8.49 . 1 38 . 5 LYS HA H 4.69 . 1 39 . 5 LYS HB2 H 1.92 . 2 40 . 5 LYS HB3 H 1.81 . 2 41 . 5 LYS HG2 H 1.6 . 2 42 . 5 LYS HG3 H 1.55 . 2 43 . 5 LYS HD2 H 1.8 . 1 44 . 5 LYS HD3 H 1.8 . 1 45 . 5 LYS HE2 H 3.11 . 1 46 . 5 LYS HE3 H 3.11 . 1 47 . 5 LYS C C 174.69 . 1 48 . 5 LYS CA C 54.41 . 1 49 . 5 LYS CB C 32.66 . 1 50 . 5 LYS CG C 24.9 . 1 51 . 5 LYS CD C 29.36 . 1 52 . 5 LYS CE C 42.17 . 1 53 . 5 LYS N N 124.09 . 1 54 . 6 PRO HA H 4.52 . 1 55 . 6 PRO HB2 H 1.97 . 1 56 . 6 PRO HB3 H 2.39 . 1 57 . 6 PRO HG2 H 2.11 . 1 58 . 6 PRO HG3 H 2.11 . 1 59 . 6 PRO HD2 H 3.92 . 2 60 . 6 PRO HD3 H 3.74 . 2 61 . 6 PRO C C 176.85 . 1 62 . 6 PRO CA C 63.2 . 1 63 . 6 PRO CB C 32.45 . 1 64 . 6 PRO CG C 27.65 . 1 65 . 6 PRO CD C 50.9 . 1 66 . 7 ARG H H 8.51 . 1 67 . 7 ARG HA H 4.43 . 1 68 . 7 ARG HB2 H 1.9 . 2 69 . 7 ARG HB3 H 1.87 . 2 70 . 7 ARG HG2 H 1.78 . 2 71 . 7 ARG HG3 H 1.7 . 2 72 . 7 ARG HD2 H 3.3 . 1 73 . 7 ARG HD3 H 3.3 . 1 74 . 7 ARG C C 176.42 . 1 75 . 7 ARG CA C 56.22 . 1 76 . 7 ARG CB C 31.29 . 1 77 . 7 ARG CG C 27.38 . 1 78 . 7 ARG CD C 43.68 . 1 79 . 7 ARG N N 121.74 . 1 80 . 8 VAL H H 8.21 . 1 81 . 8 VAL HA H 4.07 . 1 82 . 8 VAL HB H 1.99 . 1 83 . 8 VAL HG1 H 0.74 . 1 84 . 8 VAL HG2 H 0.91 . 1 85 . 8 VAL C C 175.1 . 1 86 . 8 VAL CA C 62.3 . 1 87 . 8 VAL CB C 33.15 . 1 88 . 8 VAL CG1 C 21.01 . 1 89 . 8 VAL CG2 C 21.13 . 1 90 . 8 VAL N N 122.43 . 1 91 . 9 LEU H H 8.25 . 1 92 . 9 LEU HA H 4.36 . 1 93 . 9 LEU HB2 H 1.6 . 1 94 . 9 LEU HB3 H 1.53 . 1 95 . 9 LEU HG H 1.07 . 1 96 . 9 LEU HD1 H 0.81 . 1 97 . 9 LEU HD2 H 0.79 . 1 98 . 9 LEU C C 176.52 . 1 99 . 9 LEU CA C 55.56 . 1 100 . 9 LEU CB C 43.07 . 1 101 . 9 LEU CG C 26.99 . 1 102 . 9 LEU CD1 C 23.87 . 1 103 . 9 LEU CD2 C 24.75 . 1 104 . 9 LEU N N 127.13 . 1 105 . 10 TRP H H 8.49 . 1 106 . 10 TRP HA H 4.36 . 1 107 . 10 TRP HB2 H 3 . 1 108 . 10 TRP HB3 H 3.15 . 1 109 . 10 TRP HE1 H 10.37 . 1 110 . 10 TRP HZ2 H 6.81 . 1 111 . 10 TRP HH2 H 6.7 . 1 112 . 10 TRP C C 176.52 . 1 113 . 10 TRP CA C 57.12 . 1 114 . 10 TRP CB C 26.93 . 1 115 . 10 TRP CZ2 C 112.85 . 1 116 . 10 TRP CH2 C 122.43 . 1 117 . 10 TRP N N 121.64 . 1 118 . 10 TRP NE1 N 128.68 . 1 119 . 11 THR H H 7.23 . 1 120 . 11 THR HA H 4.47 . 1 121 . 11 THR HB H 4.9 . 1 122 . 11 THR HG2 H 1.38 . 1 123 . 11 THR C C 174.74 . 1 124 . 11 THR CA C 60.53 . 1 125 . 11 THR CB C 71.47 . 1 126 . 11 THR CG2 C 22.58 . 1 127 . 11 THR N N 115.11 . 1 128 . 12 HIS H H 9.11 . 1 129 . 12 HIS HA H 4.57 . 1 130 . 12 HIS HB2 H 3.37 . 2 131 . 12 HIS HB3 H 3.31 . 2 132 . 12 HIS C C 178.02 . 1 133 . 12 HIS CA C 60.33 . 1 134 . 12 HIS CB C 30.06 . 1 135 . 12 HIS N N 120.67 . 1 136 . 13 GLU H H 8.81 . 1 137 . 13 GLU HA H 4.19 . 1 138 . 13 GLU HB2 H 2.23 . 1 139 . 13 GLU HB3 H 2.03 . 1 140 . 13 GLU HG2 H 2.42 . 2 141 . 13 GLU HG3 H 2.38 . 2 142 . 13 GLU C C 179.53 . 1 143 . 13 GLU CA C 60.1 . 1 144 . 13 GLU CB C 29.76 . 1 145 . 13 GLU CG C 36.88 . 1 146 . 13 GLU CD C 184.1 . 1 147 . 13 GLU N N 117.39 . 1 148 . 14 LEU H H 7.86 . 1 149 . 14 LEU HA H 4.12 . 1 150 . 14 LEU HB2 H 1.59 . 1 151 . 14 LEU HB3 H 1.73 . 1 152 . 14 LEU HG H 1.63 . 1 153 . 14 LEU HD1 H 0.47 . 1 154 . 14 LEU HD2 H 0.84 . 1 155 . 14 LEU C C 180.02 . 1 156 . 14 LEU CA C 58.4 . 1 157 . 14 LEU CB C 42.39 . 1 158 . 14 LEU CG C 27.55 . 1 159 . 14 LEU CD1 C 24.8 . 1 160 . 14 LEU CD2 C 25.19 . 1 161 . 14 LEU N N 121.09 . 1 162 . 15 HIS H H 9.3 . 1 163 . 15 HIS HA H 4.72 . 1 164 . 15 HIS HB2 H 3.24 . 1 165 . 15 HIS HB3 H 3.44 . 1 166 . 15 HIS HD2 H 7.22 . 1 167 . 15 HIS C C 177.65 . 1 168 . 15 HIS CA C 60.85 . 1 169 . 15 HIS CB C 31.34 . 1 170 . 15 HIS CD2 C 118.72 . 1 171 . 15 HIS N N 119.32 . 1 172 . 16 ASN H H 8.6 . 1 173 . 16 ASN HA H 4.56 . 1 174 . 16 ASN HB2 H 3.05 . 1 175 . 16 ASN HB3 H 2.84 . 1 176 . 16 ASN HD21 H 7.61 . 2 177 . 16 ASN HD22 H 6.67 . 2 178 . 16 ASN C C 179.25 . 1 179 . 16 ASN CA C 56.62 . 1 180 . 16 ASN CB C 37.75 . 1 181 . 16 ASN CG C 176.04 . 1 182 . 16 ASN N N 117.28 . 1 183 . 16 ASN ND2 N 110.44 . 1 184 . 17 LYS H H 7.98 . 1 185 . 17 LYS HA H 4.26 . 1 186 . 17 LYS HB2 H 2.21 . 1 187 . 17 LYS HB3 H 1.92 . 1 188 . 17 LYS HG2 H 1.64 . 1 189 . 17 LYS HG3 H 1.89 . 1 190 . 17 LYS HD2 H 1.8 . 2 191 . 17 LYS HD3 H 1.69 . 2 192 . 17 LYS HE2 H 3.08 . 1 193 . 17 LYS HE3 H 3.08 . 1 194 . 17 LYS C C 179.39 . 1 195 . 17 LYS CA C 60.23 . 1 196 . 17 LYS CB C 33.82 . 1 197 . 17 LYS CG C 26.13 . 1 198 . 17 LYS CD C 30.09 . 1 199 . 17 LYS CE C 42.38 . 1 200 . 17 LYS N N 121.72 . 1 201 . 18 PHE H H 8.41 . 1 202 . 18 PHE HA H 4.45 . 1 203 . 18 PHE HB2 H 3.49 . 1 204 . 18 PHE HB3 H 3.83 . 1 205 . 18 PHE HD1 H 7.13 . 3 206 . 18 PHE HE1 H 6.75 . 3 207 . 18 PHE C C 175.96 . 1 208 . 18 PHE CA C 61.55 . 1 209 . 18 PHE CB C 38.98 . 1 210 . 18 PHE CD1 C 132.84 . 3 211 . 18 PHE CE1 C 130.47 . 3 212 . 18 PHE N N 124.11 . 1 213 . 19 LEU H H 8.92 . 1 214 . 19 LEU HA H 3.49 . 1 215 . 19 LEU HB2 H 1.39 . 1 216 . 19 LEU HB3 H 1.89 . 1 217 . 19 LEU HG H 1.37 . 1 218 . 19 LEU HD1 H 0.98 . 1 219 . 19 LEU HD2 H 0.76 . 1 220 . 19 LEU C C 179.62 . 1 221 . 19 LEU CA C 57.57 . 1 222 . 19 LEU CB C 41.81 . 1 223 . 19 LEU CG C 26.17 . 1 224 . 19 LEU CD1 C 25.93 . 1 225 . 19 LEU CD2 C 23.19 . 1 226 . 19 LEU N N 120.85 . 1 227 . 20 ALA H H 7.83 . 1 228 . 20 ALA HA H 4.2 . 1 229 . 20 ALA HB H 1.56 . 1 230 . 20 ALA C C 180.64 . 1 231 . 20 ALA CA C 54.9 . 1 232 . 20 ALA CB C 18.09 . 1 233 . 20 ALA N N 120.19 . 1 234 . 21 ALA H H 7.65 . 1 235 . 21 ALA HA H 4.21 . 1 236 . 21 ALA HB H 1.55 . 1 237 . 21 ALA C C 179.19 . 1 238 . 21 ALA CA C 55.11 . 1 239 . 21 ALA CB C 20.03 . 1 240 . 21 ALA N N 121.65 . 1 241 . 22 VAL H H 8.19 . 1 242 . 22 VAL HA H 3.17 . 1 243 . 22 VAL HB H 1.66 . 1 244 . 22 VAL HG1 H 0.66 . 1 245 . 22 VAL HG2 H 0.14 . 1 246 . 22 VAL C C 177.88 . 1 247 . 22 VAL CA C 67.3 . 1 248 . 22 VAL CB C 31.1 . 1 249 . 22 VAL CG1 C 22.35 . 1 250 . 22 VAL CG2 C 22.95 . 1 251 . 22 VAL N N 117.01 . 1 252 . 23 ASP H H 8.27 . 1 253 . 23 ASP HA H 4.43 . 1 254 . 23 ASP HB2 H 2.82 . 2 255 . 23 ASP HB3 H 2.67 . 2 256 . 23 ASP C C 178.47 . 1 257 . 23 ASP CA C 57.24 . 1 258 . 23 ASP CB C 41.46 . 1 259 . 23 ASP CG C 179.6 . 1 260 . 23 ASP N N 118.84 . 1 261 . 24 HIS H H 7.73 . 1 262 . 24 HIS HA H 4.33 . 1 263 . 24 HIS HB2 H 3.31 . 1 264 . 24 HIS HB3 H 3.31 . 1 265 . 24 HIS HD2 H 6.89 . 1 266 . 24 HIS C C 177.47 . 1 267 . 24 HIS CA C 59.37 . 1 268 . 24 HIS CB C 30.48 . 1 269 . 24 HIS CD2 C 120.54 . 1 270 . 24 HIS N N 116.82 . 1 271 . 25 LEU H H 7.86 . 1 272 . 25 LEU HA H 4.13 . 1 273 . 25 LEU HB2 H 1.72 . 1 274 . 25 LEU HB3 H 1.41 . 1 275 . 25 LEU HG H 1.92 . 1 276 . 25 LEU HD1 H 0.84 . 1 277 . 25 LEU HD2 H 1.03 . 1 278 . 25 LEU C C 178.34 . 1 279 . 25 LEU CA C 56.63 . 1 280 . 25 LEU CB C 43.66 . 1 281 . 25 LEU CG C 27.16 . 1 282 . 25 LEU CD1 C 27.25 . 1 283 . 25 LEU CD2 C 22.74 . 1 284 . 25 LEU N N 116.67 . 1 285 . 26 GLY H H 8.35 . 1 286 . 26 GLY HA2 H 3.81 . 1 287 . 26 GLY HA3 H 4.49 . 1 288 . 26 GLY C C 175.15 . 1 289 . 26 GLY CA C 44.68 . 1 290 . 26 GLY N N 108.75 . 1 291 . 27 VAL H H 8.75 . 1 292 . 27 VAL HA H 3.69 . 1 293 . 27 VAL HB H 2.19 . 1 294 . 27 VAL HG1 H 1.08 . 1 295 . 27 VAL HG2 H 1.16 . 1 296 . 27 VAL C C 177.14 . 1 297 . 27 VAL CA C 66.46 . 1 298 . 27 VAL CB C 31.83 . 1 299 . 27 VAL CG1 C 20.65 . 1 300 . 27 VAL CG2 C 22.44 . 1 301 . 27 VAL N N 124.4 . 1 302 . 28 GLU H H 8.97 . 1 303 . 28 GLU HA H 4.31 . 1 304 . 28 GLU HB2 H 2.18 . 2 305 . 28 GLU HB3 H 2.1 . 2 306 . 28 GLU HG2 H 2.44 . 2 307 . 28 GLU HG3 H 2.38 . 2 308 . 28 GLU C C 177.64 . 1 309 . 28 GLU CA C 58.7 . 1 310 . 28 GLU CB C 29.45 . 1 311 . 28 GLU CG C 36.85 . 1 312 . 28 GLU CD C 184.1 . 1 313 . 28 GLU N N 118.14 . 1 314 . 29 ARG H H 7.49 . 1 315 . 29 ARG HA H 4.53 . 1 316 . 29 ARG HB2 H 1.89 . 1 317 . 29 ARG HB3 H 2.01 . 1 318 . 29 ARG HG2 H 1.7 . 1 319 . 29 ARG HG3 H 1.7 . 1 320 . 29 ARG HD2 H 3.35 . 1 321 . 29 ARG HD3 H 3.35 . 1 322 . 29 ARG C C 176.71 . 1 323 . 29 ARG CA C 55.51 . 1 324 . 29 ARG CB C 31.7 . 1 325 . 29 ARG CG C 27.76 . 1 326 . 29 ARG CD C 43.55 . 1 327 . 29 ARG N N 115.48 . 1 328 . 30 ALA H H 7.66 . 1 329 . 30 ALA HA H 4.15 . 1 330 . 30 ALA HB H 1.37 . 1 331 . 30 ALA C C 175.58 . 1 332 . 30 ALA CA C 53.48 . 1 333 . 30 ALA CB C 18.89 . 1 334 . 30 ALA N N 122.61 . 1 335 . 31 VAL H H 6.99 . 1 336 . 31 VAL HA H 4.96 . 1 337 . 31 VAL HB H 2.54 . 1 338 . 31 VAL HG1 H 1.18 . 1 339 . 31 VAL HG2 H 1.13 . 1 340 . 31 VAL C C 175.66 . 1 341 . 31 VAL CA C 58.17 . 1 342 . 31 VAL CB C 32.95 . 1 343 . 31 VAL CG1 C 21.79 . 1 344 . 31 VAL CG2 C 19.71 . 1 345 . 31 VAL N N 114.54 . 1 346 . 32 PRO HA H 4.16 . 1 347 . 32 PRO HB2 H 2.38 . 1 348 . 32 PRO HB3 H 2.38 . 1 349 . 32 PRO HG2 H 2.61 . 2 350 . 32 PRO HG3 H 1.94 . 2 351 . 32 PRO HD2 H 4.21 . 1 352 . 32 PRO HD3 H 4.04 . 1 353 . 32 PRO C C 177.26 . 1 354 . 32 PRO CA C 67.53 . 1 355 . 32 PRO CB C 32.93 . 1 356 . 32 PRO CG C 28.56 . 1 357 . 32 PRO CD C 51.21 . 1 358 . 33 LYS H H 9.33 . 1 359 . 33 LYS HA H 4.03 . 1 360 . 33 LYS HB2 H 2.09 . 2 361 . 33 LYS HB3 H 1.92 . 2 362 . 33 LYS HG2 H 1.59 . 1 363 . 33 LYS HG3 H 1.59 . 1 364 . 33 LYS HD2 H 1.92 . 2 365 . 33 LYS HD3 H 1.73 . 2 366 . 33 LYS HE2 H 3.13 . 1 367 . 33 LYS HE3 H 3.13 . 1 368 . 33 LYS C C 177.66 . 1 369 . 33 LYS CA C 60.35 . 1 370 . 33 LYS CB C 33.09 . 1 371 . 33 LYS CG C 25.28 . 1 372 . 33 LYS CD C 29.33 . 1 373 . 33 LYS CE C 42.18 . 1 374 . 33 LYS N N 116.84 . 1 375 . 34 LYS H H 6.8 . 1 376 . 34 LYS HA H 4.37 . 1 377 . 34 LYS HB2 H 2.07 . 2 378 . 34 LYS HB3 H 1.95 . 2 379 . 34 LYS HG2 H 1.65 . 1 380 . 34 LYS HG3 H 1.65 . 1 381 . 34 LYS HD2 H 1.89 . 1 382 . 34 LYS HD3 H 1.89 . 1 383 . 34 LYS HE2 H 3.1 . 1 384 . 34 LYS HE3 H 3.1 . 1 385 . 34 LYS C C 179.47 . 1 386 . 34 LYS CA C 58.47 . 1 387 . 34 LYS CB C 33.29 . 1 388 . 34 LYS CG C 26.09 . 1 389 . 34 LYS CD C 29.02 . 1 390 . 34 LYS CE C 42.13 . 1 391 . 34 LYS N N 114.99 . 1 392 . 35 ILE H H 7.87 . 1 393 . 35 ILE HA H 3.53 . 1 394 . 35 ILE HB H 2.02 . 1 395 . 35 ILE HG12 H 0.64 . 1 396 . 35 ILE HG13 H 1.65 . 1 397 . 35 ILE HG2 H 1.01 . 1 398 . 35 ILE HD1 H 0.68 . 1 399 . 35 ILE C C 177.59 . 1 400 . 35 ILE CA C 65.48 . 1 401 . 35 ILE CB C 38.54 . 1 402 . 35 ILE CG1 C 28.89 . 1 403 . 35 ILE CG2 C 18.92 . 1 404 . 35 ILE CD1 C 15.96 . 1 405 . 35 ILE N N 118.62 . 1 406 . 36 LEU H H 8.54 . 1 407 . 36 LEU HA H 4.14 . 1 408 . 36 LEU HB2 H 1.67 . 1 409 . 36 LEU HB3 H 2.13 . 1 410 . 36 LEU HG H 1.76 . 1 411 . 36 LEU HD1 H 0.93 . 2 412 . 36 LEU HD2 H 0.97 . 2 413 . 36 LEU C C 180 . 1 414 . 36 LEU CA C 58.48 . 1 415 . 36 LEU CB C 42.58 . 1 416 . 36 LEU CG C 26.94 . 1 417 . 36 LEU CD1 C 24.61 . 1 418 . 36 LEU CD2 C 26 . 1 419 . 36 LEU N N 119.36 . 1 420 . 37 ASP H H 7.99 . 1 421 . 37 ASP HA H 4.48 . 1 422 . 37 ASP HB2 H 2.88 . 2 423 . 37 ASP HB3 H 2.81 . 2 424 . 37 ASP C C 178.66 . 1 425 . 37 ASP CA C 57.41 . 1 426 . 37 ASP CB C 40.81 . 1 427 . 37 ASP CG C 179 . 1 428 . 37 ASP N N 118.82 . 1 429 . 38 LEU H H 7.55 . 1 430 . 38 LEU HA H 4.22 . 1 431 . 38 LEU HB2 H 1.96 . 1 432 . 38 LEU HB3 H 1.6 . 1 433 . 38 LEU HG H 1.9 . 1 434 . 38 LEU HD1 H 1 . 2 435 . 38 LEU HD2 H 0.89 . 2 436 . 38 LEU C C 179.39 . 1 437 . 38 LEU CA C 57.19 . 1 438 . 38 LEU CB C 42.79 . 1 439 . 38 LEU CG C 27.56 . 1 440 . 38 LEU CD1 C 26.21 . 1 441 . 38 LEU CD2 C 23.37 . 1 442 . 38 LEU N N 118.48 . 1 443 . 39 MET H H 8.45 . 1 444 . 39 MET HA H 3.99 . 1 445 . 39 MET HB2 H 2.2 . 1 446 . 39 MET HB3 H 2.2 . 1 447 . 39 MET HG2 H 3.01 . 2 448 . 39 MET HG3 H 2.26 . 2 449 . 39 MET HE H 2.22 . 1 450 . 39 MET C C 176.69 . 1 451 . 39 MET CA C 59.71 . 1 452 . 39 MET CB C 33.93 . 1 453 . 39 MET CG C 32.55 . 1 454 . 39 MET CE C 17.39 . 1 455 . 39 MET N N 117.3 . 1 456 . 40 ASN H H 7.81 . 1 457 . 40 ASN HA H 4.51 . 1 458 . 40 ASN HB2 H 3.25 . 2 459 . 40 ASN HB3 H 2.48 . 2 460 . 40 ASN HD21 H 7.57 . 2 461 . 40 ASN HD22 H 6.79 . 2 462 . 40 ASN C C 174.24 . 1 463 . 40 ASN CA C 54.12 . 1 464 . 40 ASN CB C 37.54 . 1 465 . 40 ASN CG C 178.49 . 1 466 . 40 ASN N N 113.13 . 1 467 . 40 ASN ND2 N 110.99 . 1 468 . 41 VAL H H 8.62 . 1 469 . 41 VAL HA H 4.48 . 1 470 . 41 VAL HB H 2.04 . 1 471 . 41 VAL HG1 H 0.95 . 2 472 . 41 VAL HG2 H 0.89 . 2 473 . 41 VAL C C 175.86 . 1 474 . 41 VAL CA C 60.6 . 1 475 . 41 VAL CB C 34.3 . 1 476 . 41 VAL CG1 C 21.9 . 1 477 . 41 VAL CG2 C 20.35 . 1 478 . 41 VAL N N 116.57 . 1 479 . 42 ASP H H 8.57 . 1 480 . 42 ASP HA H 4.6 . 1 481 . 42 ASP HB2 H 2.78 . 2 482 . 42 ASP HB3 H 2.71 . 2 483 . 42 ASP C C 177.29 . 1 484 . 42 ASP CA C 55.79 . 1 485 . 42 ASP CB C 41.59 . 1 486 . 42 ASP CG C 179.95 . 1 487 . 42 ASP N N 124.82 . 1 488 . 43 LYS H H 8.13 . 1 489 . 43 LYS HA H 4.06 . 1 490 . 43 LYS HB2 H 1.99 . 2 491 . 43 LYS HB3 H 1.91 . 2 492 . 43 LYS HG2 H 1.41 . 1 493 . 43 LYS HG3 H 1.41 . 1 494 . 43 LYS HD2 H 1.7 . 1 495 . 43 LYS HD3 H 1.7 . 1 496 . 43 LYS HE2 H 3.03 . 1 497 . 43 LYS HE3 H 3.03 . 1 498 . 43 LYS C C 176.28 . 1 499 . 43 LYS CA C 58.15 . 1 500 . 43 LYS CB C 31.74 . 1 501 . 43 LYS CG C 25.26 . 1 502 . 43 LYS CD C 29.22 . 1 503 . 43 LYS CE C 42.13 . 1 504 . 43 LYS N N 114.53 . 1 505 . 44 LEU H H 7.39 . 1 506 . 44 LEU HA H 4.51 . 1 507 . 44 LEU HB2 H 1.61 . 2 508 . 44 LEU HB3 H 1.38 . 2 509 . 44 LEU HG H 1.52 . 1 510 . 44 LEU HD1 H 0.68 . 2 511 . 44 LEU HD2 H 0.6 . 2 512 . 44 LEU C C 176.44 . 1 513 . 44 LEU CA C 54.72 . 1 514 . 44 LEU CB C 44.51 . 1 515 . 44 LEU CG C 27.12 . 1 516 . 44 LEU N N 120.36 . 1 517 . 45 THR H H 8.46 . 1 518 . 45 THR HA H 4.87 . 1 519 . 45 THR HB H 4.87 . 1 520 . 45 THR HG2 H 1.38 . 1 521 . 45 THR C C 176.25 . 1 522 . 45 THR CA C 59.63 . 1 523 . 45 THR CB C 72.74 . 1 524 . 45 THR CG2 C 21.85 . 1 525 . 45 THR N N 112.83 . 1 526 . 46 ARG H H 9.37 . 1 527 . 46 ARG HA H 3.82 . 1 528 . 46 ARG HB2 H 2.08 . 2 529 . 46 ARG HB3 H 1.98 . 2 530 . 46 ARG HG2 H 1.74 . 2 531 . 46 ARG HG3 H 1.65 . 2 532 . 46 ARG HD2 H 3.48 . 2 533 . 46 ARG HD3 H 3.36 . 2 534 . 46 ARG C C 178.24 . 1 535 . 46 ARG CA C 60.64 . 1 536 . 46 ARG CB C 30.03 . 1 537 . 46 ARG CG C 27.75 . 1 538 . 46 ARG CD C 43.78 . 1 539 . 46 ARG N N 121.8 . 1 540 . 47 GLU H H 8.94 . 1 541 . 47 GLU HA H 4.21 . 1 542 . 47 GLU HB2 H 2.23 . 2 543 . 47 GLU HB3 H 2.11 . 2 544 . 47 GLU HG2 H 2.57 . 2 545 . 47 GLU HG3 H 2.43 . 2 546 . 47 GLU C C 179.43 . 1 547 . 47 GLU CA C 60.55 . 1 548 . 47 GLU CB C 29.08 . 1 549 . 47 GLU CG C 37.26 . 1 550 . 47 GLU CD C 184.43 . 1 551 . 47 GLU N N 118.67 . 1 552 . 48 ASN H H 8.23 . 1 553 . 48 ASN HA H 4.91 . 1 554 . 48 ASN HB2 H 3.3 . 1 555 . 48 ASN HB3 H 2.98 . 1 556 . 48 ASN C C 179.21 . 1 557 . 48 ASN CA C 56.43 . 1 558 . 48 ASN CB C 40.28 . 1 559 . 48 ASN CG C 175.29 . 1 560 . 48 ASN N N 118.31 . 1 561 . 48 ASN ND2 N 110.02 . 1 562 . 49 VAL H H 8.16 . 1 563 . 49 VAL HA H 3.94 . 1 564 . 49 VAL HB H 2.47 . 1 565 . 49 VAL HG1 H 1.35 . 1 566 . 49 VAL HG2 H 1.43 . 1 567 . 49 VAL C C 177.1 . 1 568 . 49 VAL CA C 67.83 . 1 569 . 49 VAL CB C 31.82 . 1 570 . 49 VAL CG1 C 23.64 . 1 571 . 49 VAL CG2 C 25.46 . 1 572 . 49 VAL N N 119.41 . 1 573 . 50 ALA H H 9.41 . 1 574 . 50 ALA HA H 4.17 . 1 575 . 50 ALA HB H 1.74 . 1 576 . 50 ALA C C 180.77 . 1 577 . 50 ALA CA C 56.23 . 1 578 . 50 ALA CB C 18.62 . 1 579 . 50 ALA N N 123.41 . 1 580 . 51 SER H H 8.43 . 1 581 . 51 SER HA H 4.43 . 1 582 . 51 SER HB2 H 4.21 . 1 583 . 51 SER HB3 H 4.21 . 1 584 . 51 SER C C 176.95 . 1 585 . 51 SER CA C 61.61 . 1 586 . 51 SER CB C 63.05 . 1 587 . 51 SER N N 113.37 . 1 588 . 52 HIS H H 7.85 . 1 589 . 52 HIS HA H 4.1 . 1 590 . 52 HIS HB2 H 2.63 . 1 591 . 52 HIS HB3 H 2.4 . 1 592 . 52 HIS C C 177.33 . 1 593 . 52 HIS CA C 59.47 . 1 594 . 52 HIS CB C 29.74 . 1 595 . 52 HIS N N 122.25 . 1 596 . 53 LEU H H 9.11 . 1 597 . 53 LEU HA H 4.41 . 1 598 . 53 LEU HB2 H 1.67 . 1 599 . 53 LEU HB3 H 2.36 . 1 600 . 53 LEU HG H 1.83 . 1 601 . 53 LEU HD1 H 1.12 . 2 602 . 53 LEU HD2 H 1 . 2 603 . 53 LEU C C 177.64 . 1 604 . 53 LEU CA C 58.25 . 1 605 . 53 LEU CB C 43.05 . 1 606 . 53 LEU CG C 27.25 . 1 607 . 53 LEU CD1 C 23.01 . 1 608 . 53 LEU CD2 C 26.27 . 1 609 . 53 LEU N N 119.34 . 1 610 . 54 GLN H H 8.12 . 1 611 . 54 GLN HA H 4.26 . 1 612 . 54 GLN HB2 H 2.34 . 1 613 . 54 GLN HB3 H 2.34 . 1 614 . 54 GLN HG2 H 2.62 . 2 615 . 54 GLN HG3 H 2.58 . 2 616 . 54 GLN HE21 H 7.53 . 2 617 . 54 GLN HE22 H 6.96 . 2 618 . 54 GLN C C 178.56 . 1 619 . 54 GLN CA C 59.44 . 1 620 . 54 GLN CB C 28.15 . 1 621 . 54 GLN CG C 33.68 . 1 622 . 54 GLN CD C 180.25 . 1 623 . 54 GLN N N 118.85 . 1 624 . 54 GLN NE2 N 111.5 . 1 625 . 55 LYS H H 7.55 . 1 626 . 55 LYS HA H 4.03 . 1 627 . 55 LYS HB2 H 1.81 . 1 628 . 55 LYS HB3 H 1.81 . 1 629 . 55 LYS HG2 H 1.64 . 2 630 . 55 LYS HG3 H 1.41 . 2 631 . 55 LYS HD2 H 1.7 . 1 632 . 55 LYS HD3 H 1.7 . 1 633 . 55 LYS HE2 H 3.02 . 1 634 . 55 LYS HE3 H 3.02 . 1 635 . 55 LYS C C 178.98 . 1 636 . 55 LYS CA C 59.46 . 1 637 . 55 LYS CB C 32.74 . 1 638 . 55 LYS CG C 25.6 . 1 639 . 55 LYS CD C 29.63 . 1 640 . 55 LYS CE C 42.11 . 1 641 . 55 LYS N N 117.39 . 1 642 . 56 PHE H H 8.11 . 1 643 . 56 PHE HA H 4.37 . 1 644 . 56 PHE HB2 H 3.15 . 1 645 . 56 PHE HB3 H 3.4 . 1 646 . 56 PHE HD1 H 7.29 . 3 647 . 56 PHE C C 176.91 . 1 648 . 56 PHE CA C 60.79 . 1 649 . 56 PHE CB C 39.95 . 1 650 . 56 PHE CD1 C 131.21 . 3 651 . 56 PHE N N 120.64 . 1 652 . 57 ARG H H 8.48 . 1 653 . 57 ARG HA H 3.88 . 1 654 . 57 ARG HB2 H 2.07 . 2 655 . 57 ARG HB3 H 1.96 . 2 656 . 57 ARG HG2 H 2.06 . 2 657 . 57 ARG HG3 H 1.7 . 2 658 . 57 ARG HD2 H 3.32 . 1 659 . 57 ARG HD3 H 3.32 . 1 660 . 57 ARG C C 179.29 . 1 661 . 57 ARG CA C 60.04 . 1 662 . 57 ARG CB C 30.45 . 1 663 . 57 ARG CG C 29.18 . 1 664 . 57 ARG CD C 43.96 . 1 665 . 57 ARG N N 117.63 . 1 666 . 58 VAL H H 7.92 . 1 667 . 58 VAL HA H 3.83 . 1 668 . 58 VAL HB H 2.2 . 1 669 . 58 VAL HG1 H 1.03 . 2 670 . 58 VAL HG2 H 1.16 . 2 671 . 58 VAL C C 178.08 . 1 672 . 58 VAL CA C 65.82 . 1 673 . 58 VAL CB C 32.01 . 1 674 . 58 VAL CG1 C 21.34 . 1 675 . 58 VAL CG2 C 22.83 . 1 676 . 58 VAL N N 118.6 . 1 677 . 59 ALA H H 7.69 . 1 678 . 59 ALA HA H 4.23 . 1 679 . 59 ALA HB H 1.5 . 1 680 . 59 ALA C C 179.55 . 1 681 . 59 ALA CA C 54.14 . 1 682 . 59 ALA CB C 18.59 . 1 683 . 59 ALA N N 122.55 . 1 684 . 60 LEU H H 7.69 . 1 685 . 60 LEU HA H 4.14 . 1 686 . 60 LEU HB2 H 1.54 . 1 687 . 60 LEU HB3 H 1.62 . 1 688 . 60 LEU HG H 1.55 . 1 689 . 60 LEU HD1 H 0.79 . 2 690 . 60 LEU HD2 H 0.8 . 2 691 . 60 LEU C C 178.37 . 1 692 . 60 LEU CA C 56.24 . 1 693 . 60 LEU CB C 42.51 . 1 694 . 60 LEU CG C 26.62 . 1 695 . 60 LEU CD1 C 25.38 . 1 696 . 60 LEU CD2 C 23.59 . 1 697 . 60 LEU N N 118.21 . 1 698 . 61 LYS H H 7.69 . 1 699 . 61 LYS HA H 4.29 . 1 700 . 61 LYS HB2 H 1.98 . 2 701 . 61 LYS HB3 H 1.92 . 2 702 . 61 LYS HG2 H 1.62 . 2 703 . 61 LYS HG3 H 1.52 . 2 704 . 61 LYS HD2 H 1.78 . 1 705 . 61 LYS HD3 H 1.78 . 1 706 . 61 LYS HE2 H 3.08 . 1 707 . 61 LYS HE3 H 3.08 . 1 708 . 61 LYS C C 176.95 . 1 709 . 61 LYS CA C 56.95 . 1 710 . 61 LYS CB C 32.84 . 1 711 . 61 LYS CG C 25.14 . 1 712 . 61 LYS CD C 30.35 . 1 713 . 61 LYS CE C 42.38 . 1 714 . 61 LYS N N 118.76 . 1 715 . 62 LYS H H 7.98 . 1 716 . 62 LYS HA H 4.41 . 1 717 . 62 LYS C C 176.83 . 1 718 . 62 LYS CA C 56.87 . 1 719 . 62 LYS CB C 33.17 . 1 720 . 62 LYS CG C 25.08 . 1 721 . 62 LYS CD C 29.3 . 1 722 . 62 LYS CE C 42.38 . 1 723 . 62 LYS N N 120.97 . 1 724 . 63 VAL H H 8.08 . 1 725 . 63 VAL HA H 4.31 . 1 726 . 63 VAL HB H 2.26 . 1 727 . 63 VAL HG1 H 1.05 . 2 728 . 63 VAL HG2 H 1.04 . 2 729 . 63 VAL C C 175.66 . 1 730 . 63 VAL CA C 62.44 . 1 731 . 63 VAL CB C 32.94 . 1 732 . 63 VAL CG1 C 21.48 . 1 733 . 63 VAL CG2 C 20.51 . 1 734 . 63 VAL N N 120.06 . 1 735 . 64 SER H H 7.99 . 1 736 . 64 SER HA H 4.37 . 1 737 . 64 SER HB2 H 3.93 . 1 738 . 64 SER HB3 H 3.93 . 1 739 . 64 SER C C 178.87 . 1 740 . 64 SER CA C 60.12 . 1 741 . 64 SER CB C 65.19 . 1 742 . 64 SER N N 124.41 . 1 stop_ save_