data_5074 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; LEM domain of human inner nuclear membrane protein emerin ; _BMRB_accession_number 5074 _BMRB_flat_file_name bmr5074.str _Entry_type original _Submission_date 2001-07-09 _Accession_date 2001-07-09 _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 Wolff N. . . 2 Gilquin B. . . 3 Courchay K. . . 4 Callebaut I. . . 5 Worman H. J. . 6 Zinn-Justin S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 293 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-07 original author . stop_ _Original_release_date 2003-01-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Analysis of Emerin, an inner Nuclear Membrane Protein Mutated in X-linked Emery-Dreifuss Muscular Dystrophy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21363388 _PubMed_ID 11470279 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wolff N. . . 2 Gilquin B. . . 3 Courchay K. . . 4 Callebaut I. . . 5 Worman H. J. . 6 Zinn-Justin S. . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 501 _Journal_issue 2-3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 171 _Page_last 176 _Year 2001 _Details . loop_ _Keyword emerin 'nucleus membrane domain' dystrophy stop_ save_ ################################## # Molecular system description # ################################## save_system_EMERIN _Saveframe_category molecular_system _Mol_system_name EMERIN _Abbreviation_common EMERIN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EMERIN $EMERIN 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_EMERIN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common EMERIN _Abbreviation_common EMERIN _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; DNYADLSDTELTTLLRRYNI PHGPVVGSTRRLYEKKIFEY ETQRRRLSPPSSS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ASP 2 3 ASN 3 4 TYR 4 5 ALA 5 6 ASP 6 7 LEU 7 8 SER 8 9 ASP 9 10 THR 10 11 GLU 11 12 LEU 12 13 THR 13 14 THR 14 15 LEU 15 16 LEU 16 17 ARG 17 18 ARG 18 19 TYR 19 20 ASN 20 21 ILE 21 22 PRO 22 23 HIS 23 24 GLY 24 25 PRO 25 26 VAL 26 27 VAL 27 28 GLY 28 29 SER 29 30 THR 30 31 ARG 31 32 ARG 32 33 LEU 33 34 TYR 34 35 GLU 35 36 LYS 36 37 LYS 37 38 ILE 38 39 PHE 39 40 GLU 40 41 TYR 41 42 GLU 42 43 THR 43 44 GLN 44 45 ARG 45 46 ARG 46 47 ARG 47 48 LEU 48 49 SER 49 50 PRO 50 51 PRO 51 52 SER 52 53 SER 53 54 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 1JEI "Lem Domain Of Human Inner Nuclear Membrane Protein Emerin" 100.00 53 100.00 100.00 5.87e-29 PDB 2ODC "Lem-Domain Of The Nuclear Envelope Protein Emerin" 86.79 47 100.00 100.00 5.05e-24 PDB 2ODG "Complex Of Barrier-To-Autointegration Factor And Lem-Domain Of Emerin" 86.79 47 100.00 100.00 5.05e-24 DBJ BAA10972 "emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 DBJ BAG73116 "emerin [synthetic construct]" 100.00 254 100.00 100.00 1.93e-27 EMBL CAA57817 "emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 EMBL CAA60500 "emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 EMBL CAG38773 "EMD [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 EMBL CAL38599 "hypothetical protein [synthetic construct]" 100.00 254 100.00 100.00 1.93e-27 GB AAA92645 "emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 GB AAH00738 "Emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 GB AAP36065 "emerin (Emery-Dreifuss muscular dystrophy) [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 GB AAP36933 "Homo sapiens emerin (Emery-Dreifuss muscular dystrophy) [synthetic construct]" 100.00 255 100.00 100.00 1.88e-27 GB AAX32283 "emerin [synthetic construct]" 100.00 254 100.00 100.00 1.93e-27 REF NP_000108 "emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 REF XP_003279349 "PREDICTED: emerin [Nomascus leucogenys]" 100.00 254 100.00 100.00 2.14e-27 REF XP_003779813 "PREDICTED: LOW QUALITY PROTEIN: emerin [Pongo abelii]" 100.00 253 100.00 100.00 1.71e-27 REF XP_003804767 "PREDICTED: emerin isoform X2 [Pan paniscus]" 100.00 254 100.00 100.00 1.93e-27 REF XP_004065169 "PREDICTED: emerin [Gorilla gorilla gorilla]" 100.00 254 100.00 100.00 1.81e-27 SP P50402 "RecName: Full=Emerin [Homo sapiens]" 100.00 254 100.00 100.00 1.93e-27 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EMERIN Human 9606 Eukaryota Metazoa Homo sapiens 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 $EMERIN 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EMERIN 1 mM . NaH2PO4/Na2HPO4 20 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2.0 loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _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 6.3 . n/a temperature 298 . K 'ionic strength' 20 . mM 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 . H 1 . ppm . . . . . . 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 EMERIN _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 ASP HA H 4.90 . . 2 . 1 ASP HB2 H 2.11 . . 3 . 1 ASP HB3 H 2.36 . . 4 . 2 ASN H H 9.35 . . 5 . 2 ASN HA H 4.58 . . 6 . 2 ASN HB2 H 2.63 . . 7 . 2 ASN HB3 H 2.72 . . 8 . 2 ASN HD21 H 6.86 . . 9 . 2 ASN HD22 H 7.55 . . 10 . 3 TYR H H 8.22 . . 11 . 3 TYR HA H 4.47 . . 12 . 3 TYR HB2 H 2.87 . . 13 . 3 TYR HB3 H 3.20 . . 14 . 3 TYR HE1 H 6.99 . . 15 . 3 TYR HD1 H 7.13 . . 16 . 4 ALA H H 7.95 . . 17 . 4 ALA HA H 4.27 . . 18 . 4 ALA HB H 1.48 . . 19 . 5 ASP H H 7.96 . . 20 . 5 ASP HA H 4.61 . . 21 . 5 ASP HB2 H 2.66 . . 22 . 5 ASP HB3 H 2.84 . . 23 . 6 LEU H H 7.48 . . 24 . 6 LEU HA H 4.57 . . 25 . 6 LEU HB2 H 1.96 . . 26 . 6 LEU HG H 1.59 . . 27 . 6 LEU HD1 H 0.90 . . 28 . 6 LEU HD2 H 1.03 . . 29 . 7 SER H H 9.73 . . 30 . 7 SER HA H 4.65 . . 31 . 7 SER HB2 H 4.19 . . 32 . 7 SER HB3 H 4.53 . . 33 . 8 ASP H H 9.30 . . 34 . 8 ASP HA H 4.24 . . 35 . 8 ASP HB2 H 2.74 . . 36 . 8 ASP HB3 H 2.78 . . 37 . 9 THR H H 8.37 . . 38 . 9 THR HA H 4.02 . . 39 . 9 THR HB H 4.12 . . 40 . 9 THR HG2 H 1.29 . . 41 . 10 GLU H H 8.08 . . 42 . 10 GLU HA H 4.07 . . 43 . 10 GLU HB2 H 2.06 . . 44 . 10 GLU HG2 H 2.34 . . 45 . 10 GLU HG3 H 2.39 . . 46 . 11 LEU H H 8.89 . . 47 . 11 LEU HA H 3.96 . . 48 . 11 LEU HB2 H 1.85 . . 49 . 11 LEU HG H 1.62 . . 50 . 11 LEU HD1 H 0.97 . . 51 . 11 LEU HD2 H 0.97 . . 52 . 12 THR H H 8.07 . . 53 . 12 THR HA H 3.47 . . 54 . 12 THR HB H 4.46 . . 55 . 12 THR HG2 H 1.18 . . 56 . 13 THR H H 8.14 . . 57 . 13 THR HA H 3.78 . . 58 . 13 THR HB H 4.34 . . 59 . 13 THR HG2 H 1.19 . . 60 . 14 LEU H H 7.49 . . 61 . 14 LEU HA H 3.65 . . 62 . 14 LEU HB2 H 1.32 . . 63 . 14 LEU HB3 H 1.78 . . 64 . 14 LEU HG H 1.53 . . 65 . 14 LEU HD1 H 0.71 . . 66 . 14 LEU HD2 H 0.81 . . 67 . 15 LEU H H 7.95 . . 68 . 15 LEU HA H 3.69 . . 69 . 15 LEU HB2 H 0.07 . . 70 . 15 LEU HB3 H 1.42 . . 71 . 15 LEU HG H 1.71 . . 72 . 15 LEU HD1 H 0.75 . . 73 . 15 LEU HD2 H 0.96 . . 74 . 16 ARG H H 7.93 . . 75 . 16 ARG HA H 4.25 . . 76 . 16 ARG HB2 H 1.94 . . 77 . 16 ARG HB3 H 1.99 . . 78 . 16 ARG HG2 H 1.70 . . 79 . 16 ARG HG3 H 1.86 . . 80 . 16 ARG HD2 H 3.28 . . 81 . 16 ARG HE H 7.32 . . 82 . 17 ARG H H 8.27 . . 83 . 17 ARG HA H 3.95 . . 84 . 17 ARG HB2 H 1.69 . . 85 . 17 ARG HB3 H 1.83 . . 86 . 17 ARG HG2 H 1.57 . . 87 . 17 ARG HD2 H 2.93 . . 88 . 17 ARG HD3 H 3.13 . . 89 . 17 ARG HE H 7.13 . . 90 . 18 TYR H H 7.78 . . 91 . 18 TYR HA H 4.65 . . 92 . 18 TYR HB2 H 2.40 . . 93 . 18 TYR HB3 H 2.33 . . 94 . 18 TYR HE1 H 6.86 . . 95 . 18 TYR HD1 H 6.65 . . 96 . 19 ASN H H 8.00 . . 97 . 19 ASN HA H 4.38 . . 98 . 19 ASN HB2 H 2.82 . . 99 . 19 ASN HB3 H 3.23 . . 100 . 19 ASN HD21 H 6.91 . . 101 . 19 ASN HD22 H 7.67 . . 102 . 20 ILE H H 8.43 . . 103 . 20 ILE HA H 4.46 . . 104 . 20 ILE HB H 1.73 . . 105 . 20 ILE HG12 H 1.56 . . 106 . 20 ILE HD1 H 0.80 . . 107 . 20 ILE HG2 H 1.07 . . 108 . 21 PRO HA H 4.48 . . 109 . 21 PRO HB2 H 2.00 . . 110 . 21 PRO HB3 H 2.36 . . 111 . 21 PRO HG2 H 2.22 . . 112 . 21 PRO HG3 H 2.09 . . 113 . 21 PRO HD2 H 3.86 . . 114 . 21 PRO HD3 H 4.26 . . 115 . 22 HIS H H 8.28 . . 116 . 22 HIS HA H 4.99 . . 117 . 22 HIS HB2 H 2.48 . . 118 . 22 HIS HB3 H 2.76 . . 119 . 22 HIS HD2 H 7.21 . . 120 . 22 HIS HE1 H 8.21 . . 121 . 23 GLY H H 7.65 . . 122 . 23 GLY HA2 H 3.96 . . 123 . 23 GLY HA3 H 4.48 . . 124 . 24 PRO HA H 4.38 . . 125 . 24 PRO HB2 H 1.90 . . 126 . 24 PRO HB3 H 2.35 . . 127 . 24 PRO HG2 H 2.19 . . 128 . 24 PRO HG3 H 2.06 . . 129 . 24 PRO HD2 H 3.71 . . 130 . 25 VAL H H 8.90 . . 131 . 25 VAL HA H 3.91 . . 132 . 25 VAL HB H 2.04 . . 133 . 25 VAL HG1 H 0.70 . . 134 . 25 VAL HG2 H 0.88 . . 135 . 26 VAL H H 7.79 . . 136 . 26 VAL HA H 4.82 . . 137 . 26 VAL HB H 2.49 . . 138 . 26 VAL HG1 H 0.97 . . 139 . 26 VAL HG2 H 0.97 . . 140 . 27 GLY H H 9.14 . . 141 . 27 GLY HA2 H 3.90 . . 142 . 27 GLY HA3 H 4.18 . . 143 . 28 SER H H 8.46 . . 144 . 28 SER HA H 4.48 . . 145 . 28 SER HB2 H 4.12 . . 146 . 28 SER HB3 H 4.00 . . 147 . 29 THR H H 7.96 . . 148 . 29 THR HA H 4.70 . . 149 . 29 THR HB H 4.57 . . 150 . 29 THR HG2 H 1.28 . . 151 . 30 ARG H H 7.99 . . 152 . 30 ARG HA H 4.10 . . 153 . 30 ARG HB2 H 2.04 . . 154 . 30 ARG HB3 H 1.96 . . 155 . 30 ARG HG2 H 1.56 . . 156 . 30 ARG HD3 H 3.19 . . 157 . 30 ARG HD2 H 3.39 . . 158 . 30 ARG HE H 6.71 . . 159 . 31 ARG H H 8.82 . . 160 . 31 ARG HA H 4.09 . . 161 . 31 ARG HB2 H 1.89 . . 162 . 31 ARG HB3 H 1.94 . . 163 . 31 ARG HG2 H 1.81 . . 164 . 31 ARG HD2 H 3.33 . . 165 . 31 ARG HE H 7.51 . . 166 . 32 LEU H H 7.65 . . 167 . 32 LEU HA H 4.11 . . 168 . 32 LEU HB3 H 1.59 . . 169 . 32 LEU HG H 1.36 . . 170 . 32 LEU HB2 H 1.53 . . 171 . 32 LEU HD1 H 0.89 . . 172 . 32 LEU HD2 H 0.73 . . 173 . 33 TYR H H 7.48 . . 174 . 33 TYR HA H 4.50 . . 175 . 33 TYR HB2 H 2.96 . . 176 . 33 TYR HB3 H 3.25 . . 177 . 33 TYR HD1 H 7.06 . . 178 . 33 TYR HE1 H 7.06 . . 179 . 34 GLU H H 8.82 . . 180 . 34 GLU HA H 3.82 . . 181 . 34 GLU HB2 H 2.16 . . 182 . 34 GLU HB3 H 2.37 . . 183 . 34 GLU HG2 H 2.69 . . 184 . 35 LYS H H 7.81 . . 185 . 35 LYS HA H 4.31 . . 186 . 35 LYS HB2 H 2.07 . . 187 . 35 LYS HB3 H 2.18 . . 188 . 35 LYS HG2 H 1.57 . . 189 . 35 LYS HD2 H 1.70 . . 190 . 35 LYS HE2 H 3.07 . . 191 . 36 LYS H H 7.96 . . 192 . 36 LYS HA H 4.34 . . 193 . 36 LYS HB2 H 2.30 . . 194 . 36 LYS HG2 H 1.77 . . 195 . 36 LYS HG3 H 1.86 . . 196 . 36 LYS HD2 H 2.06 . . 197 . 36 LYS HE2 H 2.99 . . 198 . 36 LYS HE3 H 3.18 . . 199 . 37 ILE H H 8.35 . . 200 . 37 ILE HA H 3.71 . . 201 . 37 ILE HB H 1.83 . . 202 . 37 ILE HG12 H 1.80 . . 203 . 37 ILE HG2 H 0.76 . . 204 . 37 ILE HD1 H 0.96 . . 205 . 38 PHE H H 8.28 . . 206 . 38 PHE HA H 4.56 . . 207 . 38 PHE HB2 H 3.41 . . 208 . 38 PHE HD1 H 7.47 . . 209 . 38 PHE HE1 H 7.41 . . 210 . 39 GLU H H 8.83 . . 211 . 39 GLU HA H 3.86 . . 212 . 39 GLU HB2 H 2.16 . . 213 . 39 GLU HG2 H 2.31 . . 214 . 39 GLU HG3 H 2.73 . . 215 . 40 TYR H H 8.12 . . 216 . 40 TYR HA H 4.06 . . 217 . 40 TYR HB2 H 3.10 . . 218 . 40 TYR HB3 H 3.16 . . 219 . 40 TYR HD1 H 6.63 . . 220 . 40 TYR HE1 H 6.43 . . 221 . 41 GLU H H 8.99 . . 222 . 41 GLU HA H 3.86 . . 223 . 41 GLU HB2 H 2.09 . . 224 . 41 GLU HB3 H 2.29 . . 225 . 41 GLU HG2 H 2.97 . . 226 . 41 GLU HG3 H 2.33 . . 227 . 42 THR H H 8.19 . . 228 . 42 THR HA H 3.92 . . 229 . 42 THR HB H 4.08 . . 230 . 42 THR HG2 H 1.07 . . 231 . 43 GLN H H 7.68 . . 232 . 43 GLN HA H 4.12 . . 233 . 43 GLN HB2 H 2.08 . . 234 . 43 GLN HG2 H 2.39 . . 235 . 43 GLN HG3 H 2.46 . . 236 . 43 GLN HE21 H 6.85 . . 237 . 43 GLN HE22 H 7.43 . . 238 . 44 ARG H H 7.78 . . 239 . 44 ARG HA H 4.24 . . 240 . 44 ARG HB2 H 1.86 . . 241 . 44 ARG HB3 H 1.93 . . 242 . 44 ARG HG2 H 1.70 . . 243 . 44 ARG HG3 H 1.77 . . 244 . 44 ARG HD2 H 3.25 . . 245 . 44 ARG HE H 7.32 . . 246 . 45 ARG H H 7.78 . . 247 . 45 ARG HA H 4.08 . . 248 . 45 ARG HB2 H 1.84 . . 249 . 45 ARG HB3 H 1.61 . . 250 . 45 ARG HG2 H 1.52 . . 251 . 45 ARG HD2 H 3.01 . . 252 . 45 ARG HE H 7.23 . . 253 . 46 ARG H H 7.93 . . 254 . 46 ARG HA H 4.31 . . 255 . 46 ARG HB2 H 1.88 . . 256 . 46 ARG HB3 H 1.94 . . 257 . 46 ARG HG2 H 1.68 . . 258 . 46 ARG HG3 H 1.75 . . 259 . 46 ARG HD2 H 3.25 . . 260 . 46 ARG HE H 7.28 . . 261 . 47 LEU H H 8.06 . . 262 . 47 LEU HA H 4.43 . . 263 . 47 LEU HB2 H 1.74 . . 264 . 47 LEU HG H 1.66 . . 265 . 47 LEU HD1 H 0.92 . . 266 . 47 LEU HD2 H 0.97 . . 267 . 48 SER H H 8.19 . . 268 . 48 SER HA H 4.81 . . 269 . 48 SER HB2 H 3.83 . . 270 . 48 SER HB3 H 3.95 . . 271 . 49 PRO HA H 4.79 . . 272 . 49 PRO HB2 H 2.44 . . 273 . 49 PRO HB3 H 2.00 . . 274 . 49 PRO HG2 H 2.11 . . 275 . 49 PRO HD2 H 3.74 . . 276 . 49 PRO HD3 H 3.89 . . 277 . 50 PRO HA H 4.54 . . 278 . 50 PRO HB2 H 2.40 . . 279 . 50 PRO HB3 H 2.04 . . 280 . 50 PRO HG2 H 2.11 . . 281 . 50 PRO HD2 H 3.74 . . 282 . 50 PRO HD3 H 3.89 . . 283 . 51 SER H H 8.54 . . 284 . 51 SER HA H 4.54 . . 285 . 51 SER HB2 H 4.00 . . 286 . 51 SER HB3 H 3.96 . . 287 . 52 SER H H 8.48 . . 288 . 52 SER HA H 4.62 . . 289 . 52 SER HB2 H 4.01 . . 290 . 52 SER HB3 H 3.96 . . 291 . 53 SER H H 8.11 . . 292 . 53 SER HA H 4.36 . . 293 . 53 SER HB2 H 3.93 . . stop_ save_