data_6262 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of WW domains (WW3-4) from Suppressor of Deltex ; _BMRB_accession_number 6262 _BMRB_flat_file_name bmr6262.str _Entry_type original _Submission_date 2004-07-16 _Accession_date 2004-07-16 _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 Fedoroff O. Y. . 2 Avis J. M. . 3 Golovanov A. P. . 4 Baron M. . . 5 Townson S. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 351 "15N chemical shifts" 82 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-09-20 original author . stop_ _Original_release_date 2004-09-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure and dynamics of tandem WW domains in a negative regulator of notch signaling, suppressor of deltex ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15173166 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fedoroff O. Y. . 2 Townson S. A. . 3 Golovanov A. P. . 4 Baron M. . . 5 Avis J. M. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 279 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 34991 _Page_last 35000 _Year 2004 _Details . loop_ _Keyword 'WW domain' Notch stop_ save_ ################################## # Molecular system description # ################################## save_system_CG4244-PB _Saveframe_category molecular_system _Mol_system_name CG4244-PB _Abbreviation_common CG4244-PB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CG4244-PB $CG4244-PB 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_CG4244-PB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CG4244-PB _Abbreviation_common CG4244-PB _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 88 _Mol_residue_sequence ; GSPEFHMDALGPLPDGWEKK IQSDNRVYFVNHKNRTTQWE DPRTQGQEVSLINEGPLPPG WEIRYTAAGERFFVDHNTRR TTFEDPRP ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 PRO 4 GLU 5 PHE 6 HIS 7 MET 8 ASP 9 ALA 10 LEU 11 GLY 12 PRO 13 LEU 14 PRO 15 ASP 16 GLY 17 TRP 18 GLU 19 LYS 20 LYS 21 ILE 22 GLN 23 SER 24 ASP 25 ASN 26 ARG 27 VAL 28 TYR 29 PHE 30 VAL 31 ASN 32 HIS 33 LYS 34 ASN 35 ARG 36 THR 37 THR 38 GLN 39 TRP 40 GLU 41 ASP 42 PRO 43 ARG 44 THR 45 GLN 46 GLY 47 GLN 48 GLU 49 VAL 50 SER 51 LEU 52 ILE 53 ASN 54 GLU 55 GLY 56 PRO 57 LEU 58 PRO 59 PRO 60 GLY 61 TRP 62 GLU 63 ILE 64 ARG 65 TYR 66 THR 67 ALA 68 ALA 69 GLY 70 GLU 71 ARG 72 PHE 73 PHE 74 VAL 75 ASP 76 HIS 77 ASN 78 THR 79 ARG 80 ARG 81 THR 82 THR 83 PHE 84 GLU 85 ASP 86 PRO 87 ARG 88 PRO 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 1TK7 "Nmr Structure Of Ww Domains (Ww3-4) From Suppressor Of Deltex" 100.00 88 100.00 100.00 7.23e-58 GB AAL39551 "LD10565p [Drosophila melanogaster]" 92.05 518 100.00 100.00 2.93e-49 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CG4244-PB 'friut fly' 7227 Eukaryota Metazoa Drosophila melanogaster 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 $CG4244-PB 'recombinant technology' 'E. coli' Escherichia coli BL21 PGEX 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 $CG4244-PB 0.5 mM [U-15N] Arg/Glu 50 mM . H2O 90 % . D2O 10 % . Na/KCl 150 mM . stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Task refinement stop_ _Details Nilges save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_E-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name E-COSY _Sample_label . save_ save_2D_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_HSQC_in_liquid_crystal_media_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQC in liquid crystal media' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name E-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQC in liquid crystal media' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.1 . n/a temperature 288 . K 'ionic strength' 150 . mM pressure 1 . atm 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 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 CG4244-PB _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 . 3 PRO HA H 4.378 . 1 2 . 4 GLU N N 120.880 . 1 3 . 4 GLU H H 8.494 . 1 4 . 4 GLU HA H 4.147 . 1 5 . 4 GLU HB3 H 2.144 . 2 6 . 4 GLU HB2 H 1.836 . 2 7 . 4 GLU HG2 H 1.990 . 2 8 . 5 PHE N N 120.980 . 1 9 . 5 PHE H H 8.198 . 1 10 . 5 PHE HA H 4.596 . 1 11 . 5 PHE HB3 H 3.017 . 2 12 . 6 HIS N N 121.656 . 1 13 . 6 HIS H H 8.249 . 1 14 . 6 HIS HA H 4.544 . 1 15 . 6 HIS HB3 H 3.043 . 2 16 . 7 MET N N 122.280 . 1 17 . 7 MET H H 8.288 . 1 18 . 7 MET HA H 4.367 . 1 19 . 7 MET HB3 H 1.979 . 2 20 . 7 MET HB2 H 2.497 . 2 21 . 8 ASP N N 122.084 . 1 22 . 8 ASP H H 8.419 . 1 23 . 8 ASP HA H 4.581 . 1 24 . 8 ASP HB3 H 2.712 . 1 25 . 8 ASP HB2 H 2.712 . 1 26 . 9 ALA N N 125.045 . 1 27 . 9 ALA H H 8.452 . 1 28 . 9 ALA HA H 4.242 . 1 29 . 9 ALA HB H 1.387 . 1 30 . 10 LEU N N 118.543 . 1 31 . 10 LEU H H 8.211 . 1 32 . 10 LEU HA H 4.278 . 1 33 . 10 LEU HB3 H 1.630 . 2 34 . 10 LEU HB2 H 1.624 . 2 35 . 10 LEU HG H 0.765 . 1 36 . 10 LEU HD1 H 1.409 . 2 37 . 11 GLY N N 108.122 . 1 38 . 11 GLY H H 7.967 . 1 39 . 11 GLY HA3 H 4.186 . 2 40 . 11 GLY HA2 H 3.910 . 2 41 . 12 PRO HA H 3.353 . 1 42 . 13 LEU N N 122.910 . 1 43 . 13 LEU H H 8.761 . 1 44 . 13 LEU HA H 4.121 . 1 45 . 13 LEU HB3 H 1.776 . 2 46 . 13 LEU HB2 H 1.469 . 2 47 . 13 LEU HG H 2.265 . 1 48 . 13 LEU HD1 H 1.079 . 2 49 . 13 LEU HD2 H 0.827 . 2 50 . 14 PRO HB3 H 1.990 . 2 51 . 14 PRO HG3 H 1.797 . 2 52 . 14 PRO HG2 H 1.449 . 2 53 . 15 ASP N N 120.667 . 1 54 . 15 ASP H H 8.547 . 1 55 . 15 ASP HA H 4.486 . 1 56 . 15 ASP HB3 H 2.727 . 2 57 . 15 ASP HB2 H 2.622 . 2 58 . 16 GLY N N 112.629 . 1 59 . 16 GLY H H 8.903 . 1 60 . 16 GLY HA3 H 4.234 . 2 61 . 16 GLY HA2 H 3.847 . 2 62 . 17 TRP N N 117.530 . 1 63 . 17 TRP H H 7.847 . 1 64 . 17 TRP HA H 6.053 . 1 65 . 17 TRP HB3 H 3.355 . 2 66 . 17 TRP HB2 H 3.071 . 2 67 . 17 TRP HD1 H 7.077 . 1 68 . 17 TRP NE1 N 130.330 . 1 69 . 17 TRP HE1 H 10.409 . 3 70 . 17 TRP HZ2 H 7.448 . 3 71 . 18 GLU N N 120.998 . 1 72 . 18 GLU H H 9.495 . 1 73 . 18 GLU HA H 4.741 . 1 74 . 18 GLU HB3 H 2.027 . 2 75 . 19 LYS N N 127.417 . 1 76 . 19 LYS H H 8.949 . 1 77 . 19 LYS HA H 4.430 . 1 78 . 19 LYS HB3 H 1.765 . 2 79 . 19 LYS HG3 H 0.820 . 2 80 . 19 LYS HG2 H 1.082 . 2 81 . 20 LYS N N 127.450 . 1 82 . 20 LYS H H 8.529 . 1 83 . 20 LYS HA H 4.430 . 1 84 . 20 LYS HB3 H 1.525 . 2 85 . 20 LYS HB2 H 0.860 . 2 86 . 20 LYS HG3 H 1.733 . 1 87 . 20 LYS HG2 H 1.733 . 1 88 . 21 ILE N N 116.605 . 1 89 . 21 ILE H H 8.026 . 1 90 . 21 ILE HA H 4.789 . 1 91 . 21 ILE HB H 1.630 . 1 92 . 21 ILE HG13 H 0.899 . 1 93 . 21 ILE HD1 H 0.899 . 1 94 . 21 ILE HG2 H 0.051 . 1 95 . 22 GLN N N 125.496 . 1 96 . 22 GLN H H 9.008 . 1 97 . 22 GLN HA H 4.872 . 1 98 . 22 GLN HB3 H 2.725 . 2 99 . 22 GLN HB2 H 2.491 . 2 100 . 22 GLN HG3 H 1.874 . 2 101 . 22 GLN HG2 H 1.361 . 2 102 . 23 SER N N 109.393 . 1 103 . 23 SER H H 8.044 . 1 104 . 23 SER HA H 4.031 . 1 105 . 24 ASP N N 119.400 . 1 106 . 24 ASP H H 7.897 . 1 107 . 24 ASP HA H 4.589 . 1 108 . 24 ASP HB3 H 2.990 . 2 109 . 24 ASP HB2 H 2.556 . 2 110 . 25 ASN N N 112.118 . 1 111 . 25 ASN H H 8.321 . 1 112 . 25 ASN HA H 4.310 . 1 113 . 25 ASN HB3 H 3.130 . 2 114 . 25 ASN HB2 H 3.052 . 2 115 . 26 ARG N N 120.002 . 1 116 . 26 ARG H H 7.851 . 1 117 . 26 ARG HA H 4.455 . 1 118 . 26 ARG HB3 H 1.904 . 2 119 . 26 ARG HB2 H 1.613 . 2 120 . 26 ARG HD2 H 4.291 . 2 121 . 27 VAL N N 124.842 . 1 122 . 27 VAL H H 8.433 . 1 123 . 27 VAL HA H 4.820 . 1 124 . 27 VAL HB H 1.945 . 1 125 . 27 VAL HG2 H 1.002 . 2 126 . 27 VAL HG1 H 0.736 . 1 127 . 28 TYR N N 120.429 . 1 128 . 28 TYR H H 8.720 . 1 129 . 28 TYR HA H 5.074 . 1 130 . 29 PHE N N 115.728 . 1 131 . 29 PHE H H 9.088 . 1 132 . 29 PHE HA H 5.264 . 1 133 . 29 PHE HB3 H 3.057 . 2 134 . 29 PHE HB2 H 2.470 . 2 135 . 29 PHE HD1 H 6.715 . 1 136 . 29 PHE HE1 H 7.036 . 1 137 . 29 PHE HZ H 7.263 . 1 138 . 29 PHE HE2 H 7.036 . 1 139 . 29 PHE HD2 H 6.715 . 1 140 . 30 VAL N N 121.990 . 1 141 . 30 VAL H H 9.422 . 1 142 . 30 VAL HA H 4.401 . 1 143 . 30 VAL HB H 1.777 . 1 144 . 31 ASN N N 124.000 . 1 145 . 31 ASN H H 8.548 . 1 146 . 31 ASN HA H 3.874 . 1 147 . 31 ASN HB3 H 2.535 . 2 148 . 32 HIS N N 121.741 . 1 149 . 32 HIS H H 8.886 . 1 150 . 32 HIS HA H 4.392 . 1 151 . 32 HIS HB3 H 3.116 . 2 152 . 32 HIS HB2 H 3.115 . 2 153 . 32 HIS HD2 H 6.035 . 3 154 . 32 HIS HD1 H 6.841 . 3 155 . 33 LYS N N 118.353 . 1 156 . 33 LYS H H 8.138 . 1 157 . 33 LYS HA H 4.101 . 1 158 . 34 ASN N N 113.072 . 1 159 . 34 ASN H H 6.632 . 1 160 . 34 ASN HA H 2.611 . 1 161 . 35 ARG N N 115.606 . 1 162 . 35 ARG H H 7.345 . 1 163 . 35 ARG HA H 4.569 . 1 164 . 35 ARG HB3 H 2.611 . 2 165 . 36 THR N N 108.066 . 1 166 . 36 THR H H 7.562 . 1 167 . 36 THR HA H 4.886 . 1 168 . 36 THR HB H 2.548 . 1 169 . 36 THR HG2 H 0.944 . 1 170 . 37 THR N N 108.952 . 1 171 . 37 THR H H 8.078 . 1 172 . 37 THR HA H 5.567 . 1 173 . 37 THR HB H 4.215 . 1 174 . 38 GLN N N 111.973 . 1 175 . 38 GLN H H 9.175 . 1 176 . 38 GLN HA H 4.809 . 1 177 . 39 TRP N N 121.009 . 1 178 . 39 TRP H H 9.042 . 1 179 . 39 TRP HA H 5.175 . 1 180 . 39 TRP HB3 H 3.115 . 2 181 . 39 TRP HB2 H 3.560 . 2 182 . 39 TRP HD1 H 7.439 . 1 183 . 39 TRP HE3 H 8.343 . 3 184 . 40 GLU N N 116.461 . 1 185 . 40 GLU H H 8.499 . 1 186 . 40 GLU HA H 4.127 . 1 187 . 40 GLU HB3 H 1.992 . 2 188 . 41 ASP N N 124.741 . 1 189 . 41 ASP H H 8.343 . 1 190 . 41 ASP HA H 4.379 . 1 191 . 41 ASP HB3 H 2.674 . 2 192 . 42 PRO HA H 4.246 . 1 193 . 42 PRO HD3 H 2.421 . 2 194 . 42 PRO HD2 H 2.005 . 2 195 . 42 PRO HB2 H 1.423 . 2 196 . 42 PRO HG3 H 0.828 . 2 197 . 42 PRO HG2 H 0.548 . 2 198 . 43 ARG N N 118.842 . 1 199 . 43 ARG H H 8.594 . 1 200 . 43 ARG HA H 3.940 . 1 201 . 43 ARG HB3 H 1.790 . 2 202 . 43 ARG HB2 H 1.626 . 2 203 . 43 ARG HG3 H 1.148 . 2 204 . 43 ARG HG2 H 1.108 . 2 205 . 43 ARG NE N 109.900 . 1 206 . 43 ARG HE H 8.758 . 1 207 . 44 THR N N 108.463 . 1 208 . 44 THR H H 7.325 . 1 209 . 44 THR HA H 4.278 . 1 210 . 45 GLN N N 121.619 . 1 211 . 45 GLN H H 7.528 . 1 212 . 45 GLN HA H 4.278 . 1 213 . 45 GLN HB3 H 1.916 . 2 214 . 45 GLN HB2 H 2.005 . 2 215 . 45 GLN HG2 H 2.232 . 2 216 . 46 GLY N N 110.234 . 1 217 . 46 GLY H H 8.465 . 1 218 . 46 GLY HA3 H 3.933 . 2 219 . 46 GLY HA2 H 3.912 . 2 220 . 47 GLN N N 119.574 . 1 221 . 47 GLN H H 8.207 . 1 222 . 47 GLN HA H 4.304 . 1 223 . 47 GLN HB3 H 2.283 . 2 224 . 47 GLN HB2 H 2.055 . 2 225 . 47 GLN HG2 H 1.929 . 2 226 . 48 GLU N N 122.413 . 1 227 . 48 GLU H H 8.607 . 1 228 . 48 GLU HA H 4.278 . 1 229 . 48 GLU HB3 H 1.992 . 2 230 . 48 GLU HB2 H 2.258 . 2 231 . 49 VAL N N 121.619 . 1 232 . 49 VAL H H 8.227 . 1 233 . 49 VAL HA H 4.089 . 1 234 . 49 VAL HB H 2.093 . 1 235 . 49 VAL HG2 H 0.918 . 1 236 . 49 VAL HG1 H 0.918 . 1 237 . 50 SER N N 119.574 . 1 238 . 50 SER H H 8.431 . 1 239 . 50 SER HA H 4.451 . 1 240 . 50 SER HB3 H 3.848 . 2 241 . 50 SER HG H 3.848 . 1 242 . 51 LEU N N 124.842 . 1 243 . 51 LEU H H 8.379 . 1 244 . 51 LEU HA H 4.369 . 1 245 . 51 LEU HG H 1.621 . 1 246 . 52 ILE N N 121.006 . 1 247 . 52 ILE H H 8.042 . 1 248 . 52 ILE HA H 4.130 . 1 249 . 52 ILE HB H 1.849 . 1 250 . 52 ILE HG13 H 0.909 . 1 251 . 52 ILE HG12 H 1.178 . 1 252 . 53 ASN N N 122.919 . 1 253 . 53 ASN H H 8.533 . 1 254 . 53 ASN HA H 4.682 . 1 255 . 53 ASN HB3 H 2.713 . 2 256 . 53 ASN HB2 H 2.803 . 2 257 . 54 GLU N N 121.770 . 1 258 . 54 GLU H H 8.393 . 1 259 . 54 GLU HA H 4.368 . 1 260 . 54 GLU HB3 H 1.923 . 2 261 . 54 GLU HB2 H 2.087 . 2 262 . 54 GLU HG3 H 2.236 . 2 263 . 54 GLU HG2 H 2.743 . 2 264 . 55 GLY N N 109.523 . 1 265 . 55 GLY H H 8.486 . 1 266 . 55 GLY HA3 H 4.204 . 2 267 . 55 GLY HA2 H 3.921 . 2 268 . 56 PRO HA H 3.604 . 1 269 . 57 LEU N N 122.910 . 1 270 . 57 LEU H H 8.695 . 1 271 . 57 LEU HA H 4.176 . 1 272 . 57 LEU HB3 H 1.776 . 2 273 . 57 LEU HB2 H 1.469 . 2 274 . 57 LEU HG H 2.237 . 1 275 . 57 LEU HD1 H 1.051 . 2 276 . 57 LEU HD2 H 0.800 . 2 277 . 59 PRO HA H 4.473 . 1 278 . 60 GLY N N 112.769 . 1 279 . 60 GLY H H 9.123 . 1 280 . 60 GLY HA3 H 4.493 . 2 281 . 60 GLY HA2 H 4.278 . 2 282 . 61 TRP N N 117.565 . 1 283 . 61 TRP H H 7.654 . 1 284 . 61 TRP HA H 6.103 . 1 285 . 61 TRP HB3 H 3.143 . 2 286 . 61 TRP HB2 H 3.254 . 2 287 . 61 TRP HD1 H 7.062 . 1 288 . 61 TRP NE1 N 130.330 . 1 289 . 61 TRP HE1 H 10.477 . 3 290 . 61 TRP HZ2 H 7.315 . 3 291 . 62 GLU N N 119.756 . 1 292 . 62 GLU H H 9.379 . 1 293 . 62 GLU HA H 4.799 . 1 294 . 62 GLU HB3 H 2.238 . 2 295 . 62 GLU HB2 H 2.023 . 2 296 . 63 ILE N N 123.722 . 1 297 . 63 ILE H H 8.655 . 1 298 . 63 ILE HA H 4.262 . 1 299 . 63 ILE HB H 1.465 . 1 300 . 63 ILE HG13 H 0.457 . 1 301 . 63 ILE HG12 H 0.630 . 1 302 . 64 ARG N N 127.393 . 1 303 . 64 ARG H H 8.022 . 1 304 . 64 ARG HA H 4.232 . 1 305 . 64 ARG HG3 H -0.090 . 2 306 . 65 TYR N N 114.309 . 1 307 . 65 TYR H H 8.050 . 1 308 . 65 TYR HA H 5.444 . 1 309 . 65 TYR HB3 H 2.645 . 2 310 . 65 TYR HB2 H 2.642 . 2 311 . 65 TYR HD1 H 6.800 . 1 312 . 65 TYR HE1 H 7.133 . 1 313 . 65 TYR HE2 H 7.133 . 1 314 . 65 TYR HD2 H 6.800 . 1 315 . 66 THR N N 113.835 . 1 316 . 66 THR H H 9.601 . 1 317 . 66 THR HA H 4.600 . 1 318 . 67 ALA N N 125.045 . 1 319 . 67 ALA H H 8.452 . 1 320 . 67 ALA HA H 4.242 . 1 321 . 67 ALA HB H 1.387 . 1 322 . 68 ALA N N 117.328 . 1 323 . 68 ALA H H 7.652 . 1 324 . 68 ALA HA H 4.426 . 1 325 . 68 ALA HB H 1.457 . 1 326 . 69 GLY N N 107.896 . 1 327 . 69 GLY H H 8.264 . 1 328 . 69 GLY HA3 H 4.286 . 2 329 . 69 GLY HA2 H 3.680 . 2 330 . 70 GLU N N 120.276 . 1 331 . 70 GLU H H 7.775 . 1 332 . 70 GLU HA H 4.534 . 1 333 . 70 GLU HB3 H 2.203 . 2 334 . 70 GLU HB2 H 1.457 . 2 335 . 71 ARG N N 127.108 . 1 336 . 71 ARG H H 8.885 . 1 337 . 71 ARG HA H 4.115 . 1 338 . 71 ARG HB3 H 2.965 . 2 339 . 71 ARG HB2 H 1.566 . 2 340 . 71 ARG HG3 H 0.820 . 2 341 . 71 ARG HG2 H 1.022 . 2 342 . 71 ARG HE H 6.775 . 1 343 . 71 ARG HH21 H 6.658 . 1 344 . 72 PHE N N 122.266 . 1 345 . 72 PHE H H 8.968 . 1 346 . 72 PHE HA H 4.752 . 1 347 . 72 PHE HB3 H 2.937 . 2 348 . 72 PHE HB2 H 4.125 . 2 349 . 72 PHE HD1 H 6.929 . 1 350 . 72 PHE HE1 H 6.796 . 1 351 . 72 PHE HZ H 7.129 . 1 352 . 72 PHE HE2 H 6.796 . 1 353 . 72 PHE HD2 H 6.929 . 1 354 . 73 PHE N N 115.881 . 1 355 . 73 PHE H H 9.152 . 1 356 . 73 PHE HA H 5.172 . 1 357 . 73 PHE HB3 H 3.291 . 2 358 . 73 PHE HB2 H 2.457 . 2 359 . 73 PHE HD1 H 7.023 . 3 360 . 73 PHE HE1 H 6.755 . 3 361 . 73 PHE HZ H 6.742 . 1 362 . 73 PHE HE2 H 7.076 . 3 363 . 73 PHE HD2 H 7.036 . 3 364 . 74 VAL N N 122.478 . 1 365 . 74 VAL H H 9.356 . 1 366 . 74 VAL HA H 4.177 . 1 367 . 74 VAL HB H 1.721 . 1 368 . 74 VAL HG2 H 0.618 . 2 369 . 74 VAL HG1 H 0.276 . 2 370 . 75 ASP N N 124.283 . 1 371 . 75 ASP H H 8.369 . 1 372 . 75 ASP HA H 4.441 . 1 373 . 75 ASP HB3 H 3.711 . 1 374 . 75 ASP HB2 H 1.908 . 2 375 . 76 HIS N N 122.657 . 1 376 . 76 HIS H H 8.881 . 1 377 . 76 HIS HA H 4.286 . 1 378 . 76 HIS HB3 H 3.307 . 2 379 . 76 HIS HB2 H 3.059 . 2 380 . 76 HIS HD2 H 6.118 . 3 381 . 76 HIS HE1 H 6.869 . 3 382 . 77 ASN N N 115.429 . 1 383 . 77 ASN H H 8.391 . 1 384 . 77 ASN HA H 4.339 . 1 385 . 77 ASN HB3 H 3.307 . 2 386 . 77 ASN HB2 H 2.654 . 2 387 . 77 ASN ND2 N 118.642 . 1 388 . 77 ASN HD21 H 7.867 . 2 389 . 77 ASN HD22 H 7.955 . 2 390 . 78 THR N N 103.759 . 1 391 . 78 THR H H 6.456 . 1 392 . 78 THR HA H 4.224 . 1 393 . 78 THR HB H 4.332 . 1 394 . 79 ARG N N 118.344 . 1 395 . 79 ARG H H 7.352 . 1 396 . 79 ARG HA H 4.255 . 1 397 . 79 ARG HD3 H 2.281 . 2 398 . 80 ARG N N 116.811 . 1 399 . 80 ARG H H 7.310 . 1 400 . 80 ARG HA H 4.169 . 1 401 . 80 ARG HG3 H 1.535 . 2 402 . 81 THR N N 109.902 . 1 403 . 81 THR H H 8.120 . 1 404 . 81 THR HA H 5.458 . 1 405 . 81 THR HB H 4.130 . 1 406 . 82 THR N N 114.002 . 1 407 . 82 THR H H 9.149 . 1 408 . 82 THR HA H 4.690 . 1 409 . 82 THR HB H 4.457 . 1 410 . 83 PHE N N 125.157 . 1 411 . 83 PHE H H 9.327 . 1 412 . 83 PHE HA H 5.110 . 1 413 . 83 PHE HB3 H 2.980 . 2 414 . 83 PHE HB2 H 3.602 . 2 415 . 83 PHE HD1 H 7.689 . 1 416 . 83 PHE HD2 H 7.689 . 1 417 . 84 GLU N N 123.269 . 1 418 . 84 GLU H H 8.931 . 1 419 . 84 GLU HA H 4.239 . 1 420 . 84 GLU HG2 H 1.923 . 2 421 . 85 ASP N N 128.435 . 1 422 . 85 ASP H H 8.178 . 1 423 . 85 ASP HB3 H 2.623 . 2 424 . 86 PRO HA H 3.565 . 1 425 . 87 ARG N N 124.333 . 1 426 . 87 ARG H H 8.104 . 1 427 . 87 ARG HA H 3.979 . 1 428 . 87 ARG HB3 H 2.737 . 2 429 . 87 ARG HB2 H 1.749 . 2 430 . 87 ARG HG3 H 1.162 . 1 431 . 87 ARG HG2 H 1.162 . 1 432 . 87 ARG NE N 111.975 . 1 433 . 87 ARG HE H 9.210 . 1 stop_ save_