data_6084 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups ; _BMRB_accession_number 6084 _BMRB_flat_file_name bmr6084.str _Entry_type original _Submission_date 2004-01-25 _Accession_date 2004-01-26 _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 Iwai Hideo . . 2 Wider Gerhard . . 3 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 404 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-06 original author . stop_ _Original_release_date 2004-07-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15213439 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Iwai Hideo . . 2 Wider Gerhard . . 3 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 395 _Page_last 398 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_dh434 _Saveframe_category molecular_system _Mol_system_name dh434(0-63) _Abbreviation_common dh434 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label dh434 $dh434 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_dh434 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '434 repressor' _Name_variant dh434(0-13) _Abbreviation_common dh434 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; MLMGERIRARRIQLGLNQAE LAQKVGVDQQAIEQLENGKA KRPRFLPELARALGVAVDWL LNGA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 LEU 3 2 MET 4 3 GLY 5 4 GLU 6 5 ARG 7 6 ILE 8 7 ARG 9 8 ALA 10 9 ARG 11 10 ARG 12 11 ILE 13 12 GLN 14 13 LEU 15 14 GLY 16 15 LEU 17 16 ASN 18 17 GLN 19 18 ALA 20 19 GLU 21 20 LEU 22 21 ALA 23 22 GLN 24 23 LYS 25 24 VAL 26 25 GLY 27 26 VAL 28 27 ASP 29 28 GLN 30 29 GLN 31 30 ALA 32 31 ILE 33 32 GLU 34 33 GLN 35 34 LEU 36 35 GLU 37 36 ASN 38 37 GLY 39 38 LYS 40 39 ALA 41 40 LYS 42 41 ARG 43 42 PRO 44 43 ARG 45 44 PHE 46 45 LEU 47 46 PRO 48 47 GLU 49 48 LEU 50 49 ALA 51 50 ARG 52 51 ALA 53 52 LEU 54 53 GLY 55 54 VAL 56 55 ALA 57 56 VAL 58 57 ASP 59 58 TRP 60 59 LEU 61 60 LEU 62 61 ASN 63 62 GLY 64 63 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 1SQ8 "A Variant 434 Repressor Dna Binding Domain Devoid Of Hydroxyl Groups, Nmr, 20 Structures" 100.00 64 100.00 100.00 3.24e-35 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dh434 'Bacteriophage 434' 10712 Viruses . . . 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 $dh434 'recombinant technology' . . . . . 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 $dh434 . mM 4.5 5.0 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.8 0.1 n/a temperature 286.0 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 _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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 dh434 _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 MET HA H 4.13 . 1 2 . 1 MET HB2 H 2.07 . 2 3 . 1 MET HB3 H 2.16 . 2 4 . 1 MET HG2 H 2.60 . 1 5 . 1 MET HG3 H 2.60 . 1 6 . 2 LEU H H 9.12 . 1 7 . 2 LEU HA H 4.62 . 1 8 . 2 LEU HB2 H 1.73 . 2 9 . 2 LEU HB3 H 1.84 . 2 10 . 2 LEU HG H 1.75 . 1 11 . 2 LEU HD1 H 0.95 . 2 12 . 2 LEU HD2 H 0.97 . 2 13 . 3 MET H H 9.10 . 1 14 . 3 MET HA H 3.74 . 1 15 . 3 MET HB2 H 2.17 . 2 16 . 3 MET HB3 H 2.08 . 2 17 . 3 MET HG2 H 2.53 . 1 18 . 3 MET HG3 H 2.53 . 1 19 . 3 MET HE H 2.00 . 1 20 . 4 GLY H H 9.23 . 1 21 . 4 GLY HA2 H 4.20 . 2 22 . 4 GLY HA3 H 3.60 . 2 23 . 5 GLU H H 6.87 . 1 24 . 5 GLU HA H 4.14 . 1 25 . 5 GLU HB2 H 2.36 . 2 26 . 5 GLU HB3 H 2.09 . 2 27 . 5 GLU HG2 H 2.47 . 2 28 . 5 GLU HG3 H 2.36 . 2 29 . 6 ARG H H 7.82 . 1 30 . 6 ARG HA H 4.09 . 1 31 . 6 ARG HB2 H 1.89 . 2 32 . 6 ARG HB3 H 1.82 . 2 33 . 6 ARG HG2 H 1.15 . 2 34 . 6 ARG HG3 H 1.42 . 2 35 . 6 ARG HD2 H 2.23 . 2 36 . 6 ARG HD3 H 1.49 . 2 37 . 6 ARG HE H 6.54 . 1 38 . 6 ARG HH21 H 6.32 . 1 39 . 6 ARG HH22 H 6.32 . 1 40 . 7 ILE H H 8.31 . 1 41 . 7 ILE HA H 3.47 . 1 42 . 7 ILE HB H 1.99 . 1 43 . 7 ILE HG2 H 1.08 . 1 44 . 7 ILE HG12 H 0.81 . 1 45 . 7 ILE HG13 H 0.81 . 1 46 . 7 ILE HD1 H 0.88 . 1 47 . 8 ARG H H 7.87 . 1 48 . 8 ARG HA H 4.02 . 1 49 . 8 ARG HB2 H 1.73 . 2 50 . 8 ARG HB3 H 1.88 . 2 51 . 8 ARG HG2 H 1.63 . 1 52 . 8 ARG HG3 H 1.63 . 1 53 . 8 ARG HD2 H 3.25 . 1 54 . 8 ARG HD3 H 3.25 . 1 55 . 8 ARG HE H 7.35 . 1 56 . 9 ALA H H 8.26 . 1 57 . 9 ALA HA H 4.09 . 1 58 . 9 ALA HB H 1.59 . 1 59 . 10 ARG H H 8.45 . 1 60 . 10 ARG HA H 4.33 . 1 61 . 10 ARG HB2 H 2.32 . 2 62 . 10 ARG HB3 H 2.30 . 2 63 . 10 ARG HG2 H 1.75 . 2 64 . 10 ARG HG3 H 1.82 . 2 65 . 10 ARG HD2 H 2.90 . 2 66 . 10 ARG HD3 H 3.58 . 2 67 . 10 ARG HE H 6.96 . 1 68 . 10 ARG HH21 H 6.41 . 1 69 . 10 ARG HH22 H 6.41 . 1 70 . 11 ARG H H 9.05 . 1 71 . 11 ARG HA H 3.77 . 1 72 . 11 ARG HB2 H 1.72 . 2 73 . 11 ARG HB3 H 2.31 . 2 74 . 11 ARG HG2 H 1.93 . 2 75 . 11 ARG HG3 H 1.26 . 2 76 . 11 ARG HD2 H 2.81 . 2 77 . 11 ARG HD3 H 2.85 . 2 78 . 11 ARG HE H 11.88 . 1 79 . 11 ARG HH11 H 9.0 . 1 80 . 11 ARG HH21 H 6.75 . 1 81 . 11 ARG HH22 H 6.75 . 1 82 . 12 ILE H H 8.46 . 1 83 . 12 ILE HA H 3.83 . 1 84 . 12 ILE HB H 1.94 . 1 85 . 12 ILE HG2 H 0.95 . 1 86 . 12 ILE HG12 H 1.15 . 2 87 . 12 ILE HG13 H 1.87 . 2 88 . 12 ILE HD1 H 0.88 . 1 89 . 13 GLN H H 8.26 . 1 90 . 13 GLN HA H 4.09 . 1 91 . 13 GLN HB2 H 2.38 . 2 92 . 13 GLN HB3 H 2.32 . 2 93 . 13 GLN HG2 H 2.58 . 1 94 . 13 GLN HG3 H 2.58 . 1 95 . 13 GLN HE21 H 7.62 . 2 96 . 13 GLN HE22 H 6.91 . 2 97 . 14 LEU H H 7.78 . 1 98 . 14 LEU HA H 4.27 . 1 99 . 14 LEU HB2 H 1.65 . 2 100 . 14 LEU HB3 H 1.91 . 2 101 . 14 LEU HG H 1.65 . 1 102 . 14 LEU HD1 H 0.85 . 2 103 . 14 LEU HD2 H 0.94 . 2 104 . 15 GLY H H 8.16 . 1 105 . 15 GLY HA2 H 3.91 . 2 106 . 15 GLY HA3 H 4.05 . 2 107 . 16 LEU H H 7.58 . 1 108 . 16 LEU HB2 H 1.72 . 2 109 . 16 LEU HB3 H 1.46 . 2 110 . 16 LEU HG H 1.59 . 1 111 . 16 LEU HD1 H 0.78 . 2 112 . 16 LEU HD2 H 0.81 . 2 113 . 17 ASN H H 9.27 . 1 114 . 17 ASN HA H 4.78 . 1 115 . 17 ASN HB2 H 2.89 . 2 116 . 17 ASN HB3 H 3.42 . 2 117 . 17 ASN HD21 H 7.50 . 2 118 . 17 ASN HD22 H 7.03 . 2 119 . 18 GLN H H 8.99 . 1 120 . 18 GLN HA H 3.67 . 1 121 . 18 GLN HB2 H 2.25 . 2 122 . 18 GLN HB3 H 1.72 . 2 123 . 18 GLN HG2 H 2.10 . 2 124 . 18 GLN HG3 H 2.62 . 2 125 . 18 GLN HE21 H 7.75 . 2 126 . 18 GLN HE22 H 7.63 . 2 127 . 19 ALA H H 8.44 . 1 128 . 19 ALA HA H 3.88 . 1 129 . 19 ALA HB H 1.49 . 1 130 . 20 GLU H H 8.94 . 1 131 . 20 GLU HA H 4.07 . 1 132 . 20 GLU HB2 H 2.25 . 2 133 . 20 GLU HB3 H 1.93 . 2 134 . 20 GLU HG2 H 2.63 . 2 135 . 20 GLU HG3 H 2.29 . 2 136 . 21 LEU H H 8.06 . 1 137 . 21 LEU HA H 4.09 . 1 138 . 21 LEU HB2 H 1.22 . 2 139 . 21 LEU HB3 H 1.93 . 2 140 . 21 LEU HG H 1.48 . 1 141 . 21 LEU HD1 H 0.94 . 2 142 . 21 LEU HD2 H 0.89 . 2 143 . 22 ALA H H 8.44 . 1 144 . 22 ALA HA H 3.50 . 1 145 . 22 ALA HB H 1.35 . 1 146 . 23 GLN H H 7.96 . 1 147 . 23 GLN HA H 4.10 . 1 148 . 23 GLN HB2 H 2.21 . 2 149 . 23 GLN HB3 H 2.45 . 2 150 . 23 GLN HG2 H 2.55 . 1 151 . 23 GLN HG3 H 2.55 . 1 152 . 23 GLN HE21 H 7.53 . 2 153 . 23 GLN HE22 H 6.88 . 2 154 . 24 LYS H H 7.63 . 1 155 . 24 LYS HA H 4.11 . 1 156 . 24 LYS HB2 H 1.99 . 2 157 . 24 LYS HB3 H 2.00 . 2 158 . 24 LYS HG2 H 1.76 . 1 159 . 24 LYS HG3 H 1.76 . 1 160 . 24 LYS HD2 H 1.64 . 2 161 . 24 LYS HD3 H 1.69 . 2 162 . 24 LYS HE2 H 3.10 . 2 163 . 24 LYS HE3 H 2.97 . 2 164 . 25 VAL H H 7.66 . 1 165 . 25 VAL HA H 3.92 . 1 166 . 25 VAL HB H 2.01 . 1 167 . 25 VAL HG1 H 0.80 . 2 168 . 25 VAL HG2 H 0.89 . 2 169 . 26 GLY H H 8.00 . 1 170 . 26 GLY HA2 H 3.86 . 2 171 . 26 GLY HA3 H 4.11 . 2 172 . 27 VAL H H 7.57 . 1 173 . 27 VAL HA H 4.64 . 1 174 . 27 VAL HB H 2.02 . 1 175 . 27 VAL HG1 H 0.05 . 2 176 . 27 VAL HG2 H 0.37 . 2 177 . 28 ASP H H 7.91 . 1 178 . 28 ASP HA H 4.73 . 1 179 . 28 ASP HB2 H 2.94 . 2 180 . 28 ASP HB3 H 2.73 . 2 181 . 29 GLN H H 8.97 . 1 182 . 29 GLN HA H 3.58 . 1 183 . 29 GLN HB2 H 2.06 . 2 184 . 29 GLN HB3 H 2.20 . 2 185 . 29 GLN HG2 H 2.31 . 1 186 . 29 GLN HG3 H 2.31 . 1 187 . 29 GLN HE21 H 7.62 . 2 188 . 29 GLN HE22 H 6.97 . 2 189 . 30 GLN H H 8.74 . 1 190 . 30 GLN HA H 4.01 . 1 191 . 30 GLN HB2 H 2.12 . 2 192 . 30 GLN HB3 H 2.04 . 2 193 . 30 GLN HG2 H 2.42 . 1 194 . 30 GLN HG3 H 2.42 . 1 195 . 30 GLN HE21 H 7.70 . 2 196 . 30 GLN HE22 H 6.88 . 2 197 . 31 ALA H H 7.80 . 1 198 . 31 ALA HA H 4.20 . 1 199 . 31 ALA HB H 1.59 . 1 200 . 32 ILE H H 7.15 . 1 201 . 32 ILE HA H 3.93 . 1 202 . 32 ILE HB H 2.33 . 1 203 . 32 ILE HG2 H 0.92 . 1 204 . 32 ILE HG12 H 1.25 . 2 205 . 32 ILE HG13 H 1.72 . 2 206 . 32 ILE HD1 H 0.57 . 1 207 . 33 GLU H H 8.35 . 1 208 . 33 GLU HA H 4.02 . 1 209 . 33 GLU HB2 H 2.05 . 2 210 . 33 GLU HB3 H 2.21 . 2 211 . 33 GLU HG2 H 2.28 . 2 212 . 33 GLU HG3 H 2.36 . 2 213 . 34 GLN H H 8.39 . 1 214 . 34 GLN HA H 4.28 . 1 215 . 34 GLN HB2 H 2.04 . 2 216 . 34 GLN HB3 H 2.09 . 2 217 . 34 GLN HG2 H 2.44 . 2 218 . 34 GLN HG3 H 2.68 . 2 219 . 34 GLN HE21 H 7.57 . 2 220 . 34 GLN HE22 H 6.95 . 2 221 . 35 LEU H H 7.53 . 1 222 . 35 LEU HA H 4.26 . 1 223 . 35 LEU HB2 H 2.07 . 2 224 . 35 LEU HB3 H 1.64 . 2 225 . 35 LEU HG H 1.81 . 1 226 . 35 LEU HD1 H 0.94 . 2 227 . 35 LEU HD2 H 0.82 . 2 228 . 36 GLU H H 8.54 . 1 229 . 36 GLU HA H 4.04 . 1 230 . 36 GLU HB2 H 1.95 . 2 231 . 36 GLU HB3 H 1.89 . 2 232 . 36 GLU HG2 H 2.21 . 2 233 . 36 GLU HG3 H 2.70 . 2 234 . 37 ASN H H 8.25 . 1 235 . 37 ASN HA H 4.74 . 1 236 . 37 ASN HB2 H 2.85 . 2 237 . 37 ASN HB3 H 3.00 . 2 238 . 37 ASN HD21 H 7.58 . 2 239 . 37 ASN HD22 H 6.72 . 2 240 . 38 GLY H H 7.51 . 1 241 . 38 GLY HA2 H 4.11 . 2 242 . 38 GLY HA3 H 4.15 . 2 243 . 39 LYS H H 8.52 . 1 244 . 39 LYS HA H 4.28 . 1 245 . 39 LYS HB2 H 1.94 . 2 246 . 39 LYS HB3 H 1.83 . 2 247 . 39 LYS HG2 H 1.33 . 2 248 . 39 LYS HG3 H 1.46 . 2 249 . 39 LYS HD2 H 1.68 . 1 250 . 39 LYS HD3 H 1.68 . 1 251 . 39 LYS HE2 H 3.00 . 1 252 . 39 LYS HE3 H 3.00 . 1 253 . 40 ALA H H 7.75 . 1 254 . 40 ALA HA H 4.47 . 1 255 . 40 ALA HB H 1.28 . 1 256 . 41 LYS H H 8.38 . 1 257 . 41 LYS HA H 4.31 . 1 258 . 41 LYS HB2 H 1.88 . 2 259 . 41 LYS HB3 H 1.69 . 2 260 . 41 LYS HG2 H 1.46 . 2 261 . 41 LYS HG3 H 1.42 . 2 262 . 41 LYS HD2 H 1.73 . 1 263 . 41 LYS HD3 H 1.73 . 1 264 . 41 LYS HE2 H 3.02 . 1 265 . 41 LYS HE3 H 3.02 . 1 266 . 42 ARG H H 8.52 . 1 267 . 42 ARG HA H 4.22 . 1 268 . 42 ARG HB2 H 1.76 . 2 269 . 42 ARG HB3 H 1.57 . 2 270 . 42 ARG HG2 H 1.50 . 1 271 . 42 ARG HG3 H 1.50 . 1 272 . 42 ARG HD2 H 3.16 . 1 273 . 42 ARG HD3 H 3.16 . 1 274 . 42 ARG HE H 7.27 . 1 275 . 43 PRO HA H 4.45 . 1 276 . 43 PRO HB2 H 0.37 . 2 277 . 43 PRO HB3 H 1.73 . 2 278 . 43 PRO HG2 H 1.44 . 2 279 . 43 PRO HG3 H 1.54 . 2 280 . 43 PRO HD2 H 3.45 . 2 281 . 43 PRO HD3 H 3.36 . 2 282 . 44 ARG H H 9.24 . 1 283 . 44 ARG HA H 4.22 . 1 284 . 44 ARG HB2 H 1.93 . 2 285 . 44 ARG HB3 H 2.00 . 2 286 . 44 ARG HG2 H 1.80 . 1 287 . 44 ARG HG3 H 1.80 . 1 288 . 44 ARG HD2 H 3.29 . 1 289 . 44 ARG HD3 H 3.29 . 1 290 . 44 ARG HE H 7.36 . 1 291 . 45 PHE H H 6.46 . 1 292 . 45 PHE HA H 5.33 . 1 293 . 45 PHE HB2 H 3.67 . 2 294 . 45 PHE HB3 H 2.86 . 2 295 . 45 PHE HD1 H 7.27 . 1 296 . 45 PHE HD2 H 7.27 . 1 297 . 45 PHE HE1 H 7.31 . 1 298 . 45 PHE HE2 H 7.31 . 1 299 . 45 PHE HZ H 7.22 . 1 300 . 46 LEU H H 7.38 . 1 301 . 46 LEU HA H 4.08 . 1 302 . 46 LEU HB2 H 1.75 . 2 303 . 46 LEU HB3 H 1.76 . 2 304 . 46 LEU HG H 1.65 . 1 305 . 46 LEU HD1 H 0.85 . 2 306 . 46 LEU HD2 H 0.92 . 2 307 . 47 PRO HA H 4.16 . 1 308 . 47 PRO HB2 H 2.40 . 1 309 . 47 PRO HB3 H 2.40 . 1 310 . 47 PRO HG2 H 1.92 . 2 311 . 47 PRO HG3 H 2.31 . 2 312 . 47 PRO HD2 H 3.82 . 2 313 . 47 PRO HD3 H 3.78 . 2 314 . 48 GLU H H 8.90 . 1 315 . 48 GLU HA H 4.10 . 1 316 . 48 GLU HB2 H 2.14 . 2 317 . 48 GLU HB3 H 2.47 . 2 318 . 48 GLU HG2 H 2.39 . 2 319 . 48 GLU HG3 H 2.74 . 2 320 . 49 LEU H H 8.66 . 1 321 . 49 LEU HA H 4.15 . 1 322 . 49 LEU HB2 H 1.68 . 2 323 . 49 LEU HB3 H 2.21 . 2 324 . 49 LEU HG H 1.01 . 1 325 . 49 LEU HD1 H 0.97 . 2 326 . 49 LEU HD2 H 1.01 . 2 327 . 50 ALA H H 8.77 . 1 328 . 50 ALA HA H 3.82 . 1 329 . 50 ALA HB H 1.57 . 1 330 . 51 ARG H H 7.89 . 1 331 . 51 ARG HA H 4.16 . 1 332 . 51 ARG HB2 H 1.97 . 1 333 . 51 ARG HB3 H 1.97 . 1 334 . 51 ARG HG2 H 1.64 . 2 335 . 51 ARG HG3 H 1.83 . 2 336 . 51 ARG HD2 H 3.30 . 1 337 . 51 ARG HD3 H 3.30 . 1 338 . 51 ARG HE H 7.43 . 1 339 . 52 ALA H H 8.13 . 1 340 . 52 ALA HA H 4.13 . 1 341 . 52 ALA HB H 1.41 . 1 342 . 53 LEU H H 7.78 . 1 343 . 53 LEU HA H 4.30 . 1 344 . 53 LEU HB2 H 1.61 . 2 345 . 53 LEU HB3 H 1.96 . 2 346 . 53 LEU HG H 1.68 . 1 347 . 53 LEU HD1 H 0.94 . 2 348 . 53 LEU HD2 H 0.82 . 2 349 . 54 GLY H H 8.07 . 1 350 . 54 GLY HA2 H 3.97 . 2 351 . 54 GLY HA3 H 3.91 . 2 352 . 55 VAL H H 8.00 . 1 353 . 55 VAL HA H 4.61 . 1 354 . 55 VAL HB H 2.13 . 1 355 . 55 VAL HG1 H 0.33 . 2 356 . 55 VAL HG2 H 0.88 . 2 357 . 56 ALA H H 8.46 . 1 358 . 56 ALA HA H 4.59 . 1 359 . 56 ALA HB H 1.61 . 1 360 . 57 VAL H H 9.10 . 1 361 . 57 VAL HA H 3.47 . 1 362 . 57 VAL HB H 2.08 . 1 363 . 57 VAL HG1 H 0.96 . 2 364 . 57 VAL HG2 H 1.05 . 2 365 . 58 ASP H H 8.71 . 1 366 . 58 ASP HA H 4.38 . 1 367 . 58 ASP HB2 H 2.68 . 2 368 . 58 ASP HB3 H 2.70 . 2 369 . 59 TRP H H 7.28 . 1 370 . 59 TRP HA H 4.19 . 1 371 . 59 TRP HB2 H 3.39 . 2 372 . 59 TRP HB3 H 3.57 . 2 373 . 59 TRP HD1 H 7.22 . 1 374 . 59 TRP HE3 H 7.30 . 1 375 . 59 TRP HE1 H 10.43 . 1 376 . 59 TRP HZ3 H 6.74 . 1 377 . 59 TRP HZ2 H 7.55 . 1 378 . 59 TRP HH2 H 7.28 . 1 379 . 60 LEU H H 7.74 . 1 380 . 60 LEU HA H 3.57 . 1 381 . 60 LEU HB2 H 2.22 . 2 382 . 60 LEU HB3 H 1.69 . 2 383 . 60 LEU HG H 1.96 . 1 384 . 60 LEU HD1 H 0.89 . 2 385 . 60 LEU HD2 H 0.94 . 2 386 . 61 LEU H H 7.99 . 1 387 . 61 LEU HA H 4.08 . 1 388 . 61 LEU HB2 H 1.69 . 2 389 . 61 LEU HB3 H 1.42 . 2 390 . 61 LEU HG H 1.67 . 1 391 . 61 LEU HD1 H 0.83 . 2 392 . 61 LEU HD2 H 0.85 . 2 393 . 62 ASN H H 8.09 . 1 394 . 62 ASN HA H 4.99 . 1 395 . 62 ASN HB2 H 2.74 . 2 396 . 62 ASN HB3 H 2.79 . 2 397 . 62 ASN HD21 H 7.74 . 2 398 . 62 ASN HD22 H 6.99 . 2 399 . 63 GLY H H 8.31 . 1 400 . 63 GLY HA2 H 3.63 . 2 401 . 63 GLY HA3 H 3.00 . 2 402 . 64 ALA H H 7.71 . 1 403 . 64 ALA HA H 4.25 . 1 404 . 64 ALA HB H 1.42 . 1 stop_ save_