data_5342 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for Superman Zinc Finger Domain ; _BMRB_accession_number 5342 _BMRB_flat_file_name bmr5342.str _Entry_type original _Submission_date 2002-04-09 _Accession_date 2002-04-10 _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 ISERNIA CARLA . . 2 BUCCI ENRICO . . 3 LEONE MARILISA . . 4 ZACCARO LAURA . . 5 'DI LELLO' PAOLA . . 6 'DI GILIO' GIUSEPPE . . 7 ESPOSITO SABRINA . . 8 SAVIANO MICHELE . . 9 'DI BLASIO' BENEDETTO . . 10 PEDONE CARLO . . 11 PEDONE PAOLO VINCENZO . 12 FATTORUSSO ROBERTO . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 228 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-04-10 original BMRB . stop_ _Original_release_date 2002-04-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22502270 _PubMed_ID 12616630 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 ISERNIA CARLA . . 2 BUCCI ENRICO . . 3 LEONE MARILISA . . 4 ZACCARO LAURA . . 5 'DI LELLO' PAOLA . . 6 'DI GILIO' GIUSEPPE . . 7 ESPOSITO SABRINA . . 8 SAVIANO MICHELE . . 9 'DI BLASIO' BENEDETTO . . 10 PEDONE CARLO . . 11 PEDONE PAOLO VINCENZO . 12 FATTORUSSO ROBERTO . . stop_ _Journal_abbreviation Chembiochem _Journal_volume 4 _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 180 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_Superman_Zinc_finger _Saveframe_category molecular_system _Mol_system_name 'Zinc finger domain of Superman protein' _Abbreviation_common 'Superman Zinc finger' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SUPERMAN 37' $SUP37 'Zinc ion' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SUP37 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SUPERMAN 37' _Abbreviation_common SUP37 _Molecular_mass 4502.8 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; WPPRSYTCSFCKREFRSAQA LGGHMNVHRRDRARLRL ; loop_ _Residue_seq_code _Residue_label 1 TRP 2 PRO 3 PRO 4 ARG 5 SER 6 TYR 7 THR 8 CYS 9 SER 10 PHE 11 CYS 12 LYS 13 ARG 14 GLU 15 PHE 16 ARG 17 SER 18 ALA 19 GLN 20 ALA 21 LEU 22 GLY 23 GLY 24 HIS 25 MET 26 ASN 27 VAL 28 HIS 29 ARG 30 ARG 31 ASP 32 ARG 33 ALA 34 ARG 35 LEU 36 ARG 37 LEU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1NJQ 'Nmr Structure Of The Single Qalggh Zinc Finger Domain From Arabidopsis Thaliana Superman Protein' 97.30 37 100.00 100.00 9.62e-13 DBJ BAA95724 'SUPERMAN-like protein [Arabidopsis thaliana]' 100.00 204 100.00 100.00 1.34e-14 DBJ BAD11142 'hypothetical protein [Petunia x hybrida]' 100.00 224 100.00 100.00 8.14e-15 EMBL CAO71330 'unnamed protein product [Vitis vinifera]' 97.30 182 100.00 100.00 5.54e-14 EMBL CAO71331 'unnamed protein product [Vitis vinifera]' 97.30 221 100.00 100.00 5.02e-14 GenBank AAC49116 SUPERMAN 100.00 204 100.00 100.00 1.34e-14 GenBank AAY78753 'superman protein [Arabidopsis thaliana]' 100.00 204 100.00 100.00 1.34e-14 PRF 2124420A 'SUPERMAN gene' 100.00 204 100.00 100.00 1.34e-14 REF NP_188954 'SUP (SUPERMAN); DNA binding / nucleic acid binding / transcription factor/ zinc ion binding [Arabidopsis thaliana]' 100.00 204 100.00 100.00 1.34e-14 SWISS-PROT Q38895 'Transcriptional regulator SUPERMAN' 100.00 204 100.00 100.00 1.34e-14 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 14:23:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SUP37 'thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana 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 $SUP37 '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 $SUP37 2 mM . $ZN 2.3 mM . stop_ save_ ############################ # Computer software used # ############################ save_Varian_Software_(VNMR) _Saveframe_category software _Name 'Varian Software (VNMR)' _Version 'VNMR 6-1B' loop_ _Task 'spectra processing' stop_ _Details . save_ save_PROSA _Saveframe_category software _Name PROSA _Version . loop_ _Task 'spectra processing' stop_ _Details 'Guntert et al., 1992' save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'spectra analysis' stop_ _Details 'Bartels et.al, 1995' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_DQFCOSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQFCOSY' _Sample_label $Sample_1 save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $Sample_1 save_ save_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $Sample_1 save_ save_1H-1H_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H ROESY' _Sample_label $Sample_1 save_ ####################### # Sample conditions # ####################### save_Experimental_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 301 0.5 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 TMS H 1 METHYL ppm 0.00 external indirect . external_to_the_sample . 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_ _Experiment_label '1H-1H DQFCOSY' '1H-1H TOCSY' '1H-1H NOESY' '1H-1H ROESY' stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $Experimental_Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SUPERMAN 37' _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 TRP H H 8.08 0.007 1 2 . 1 TRP HA H 4.49 0.007 1 3 . 1 TRP HB2 H 3.10 0.007 1 4 . 1 TRP HB3 H 3.14 0.007 1 5 . 1 TRP HD1 H 7.26 0.007 1 6 . 1 TRP HE1 H 10.04 0.007 1 7 . 1 TRP HE3 H 7.62 0.007 1 8 . 1 TRP HZ2 H 7.20 0.007 1 9 . 1 TRP HZ3 H 7.19 0.007 1 10 . 1 TRP HH2 H 7.46 0.007 1 11 . 2 PRO HA H 4.43 0.007 1 12 . 2 PRO HB2 H 1.84 0.007 1 13 . 2 PRO HB3 H 2.26 0.007 1 14 . 2 PRO HG2 H 1.96 0.007 1 15 . 2 PRO HG3 H 1.96 0.007 1 16 . 2 PRO HD2 H 3.60 0.007 1 17 . 2 PRO HD3 H 3.81 0.007 1 18 . 3 PRO HA H 4.42 0.007 1 19 . 3 PRO HB2 H 1.84 0.007 1 20 . 3 PRO HB3 H 2.27 0.007 1 21 . 3 PRO HG2 H 1.99 0.007 1 22 . 3 PRO HG3 H 1.99 0.007 1 23 . 3 PRO HD2 H 3.56 0.007 1 24 . 3 PRO HD3 H 3.84 0.007 1 25 . 4 ARG H H 8.28 0.007 1 26 . 4 ARG HA H 4.22 0.007 1 27 . 4 ARG HB2 H 1.74 0.007 1 28 . 4 ARG HB3 H 1.74 0.007 1 29 . 4 ARG HG2 H 1.52 0.007 1 30 . 4 ARG HG3 H 1.52 0.007 1 31 . 4 ARG HD2 H 3.11 0.007 1 32 . 4 ARG HD3 H 3.11 0.007 1 33 . 5 SER H H 7.87 0.007 1 34 . 5 SER HA H 4.52 0.007 1 35 . 5 SER HB2 H 3.61 0.007 1 36 . 5 SER HB3 H 3.61 0.007 1 37 . 6 TYR H H 8.70 0.007 1 38 . 6 TYR HA H 4.56 0.007 1 39 . 6 TYR HB2 H 2.69 0.007 1 40 . 6 TYR HB3 H 2.82 0.007 1 41 . 6 TYR HD1 H 6.90 0.007 1 42 . 6 TYR HD2 H 6.90 0.007 1 43 . 6 TYR HE1 H 6.68 0.007 1 44 . 6 TYR HE2 H 6.68 0.007 1 45 . 7 THR H H 8.47 0.007 1 46 . 7 THR HA H 4.91 0.007 1 47 . 7 THR HB H 3.73 0.007 1 48 . 7 THR HG2 H 0.94 0.007 1 49 . 8 CYS H H 9.10 0.007 1 50 . 8 CYS HA H 4.53 0.007 1 51 . 8 CYS HB2 H 2.92 0.007 1 52 . 8 CYS HB3 H 3.38 0.007 1 53 . 9 SER H H 8.92 0.007 1 54 . 9 SER HA H 4.10 0.007 1 55 . 9 SER HB2 H 3.66 0.007 1 56 . 9 SER HB3 H 3.72 0.007 1 57 . 10 PHE H H 8.95 0.007 1 58 . 10 PHE HA H 4.35 0.007 1 59 . 10 PHE HB2 H 2.00 0.007 1 60 . 10 PHE HB3 H 2.46 0.007 1 61 . 10 PHE HD1 H 6.98 0.007 1 62 . 10 PHE HD2 H 6.98 0.007 1 63 . 10 PHE HE1 H 7.23 0.007 1 64 . 10 PHE HE2 H 7.23 0.007 1 65 . 10 PHE HZ H 7.25 0.007 1 66 . 11 CYS H H 8.37 0.007 1 67 . 11 CYS HA H 5.08 0.007 1 68 . 11 CYS HB2 H 2.96 0.007 1 69 . 11 CYS HB3 H 3.44 0.007 1 70 . 12 LYS H H 8.01 0.007 1 71 . 12 LYS HA H 4.06 0.007 1 72 . 12 LYS HB2 H 1.95 0.007 1 73 . 12 LYS HB3 H 2.14 0.007 1 74 . 12 LYS HG2 H 1.20 0.007 1 75 . 12 LYS HG3 H 1.33 0.007 1 76 . 12 LYS HD2 H 1.54 0.007 1 77 . 12 LYS HD3 H 1.65 0.007 1 78 . 12 LYS HE2 H 2.98 0.007 1 79 . 12 LYS HE3 H 2.98 0.007 1 80 . 13 ARG H H 7.85 0.007 1 81 . 13 ARG HA H 4.06 0.007 1 82 . 13 ARG HB2 H 1.32 0.007 1 83 . 13 ARG HB3 H 1.82 0.007 1 84 . 13 ARG HG2 H 1.47 0.007 1 85 . 13 ARG HG3 H 1.53 0.007 1 86 . 13 ARG HD2 H 3.12 0.007 1 87 . 13 ARG HD3 H 3.12 0.007 1 88 . 14 GLU H H 7.99 0.007 1 89 . 14 GLU HA H 4.80 0.007 1 90 . 14 GLU HB2 H 1.67 0.007 1 91 . 14 GLU HB3 H 1.75 0.007 1 92 . 14 GLU HG2 H 2.14 0.007 1 93 . 14 GLU HG3 H 2.14 0.007 1 94 . 15 PHE H H 8.89 0.007 1 95 . 15 PHE HA H 4.62 0.007 1 96 . 15 PHE HB2 H 2.81 0.007 1 97 . 15 PHE HB3 H 3.21 0.007 1 98 . 15 PHE HD1 H 7.18 0.007 1 99 . 15 PHE HD2 H 7.18 0.007 1 100 . 15 PHE HE1 H 6.74 0.007 1 101 . 15 PHE HE2 H 6.74 0.007 1 102 . 15 PHE HZ H 5.95 0.007 1 103 . 16 ARG H H 7.43 0.007 1 104 . 16 ARG HA H 4.55 0.007 1 105 . 16 ARG HB2 H 1.84 0.007 1 106 . 16 ARG HB3 H 1.84 0.007 1 107 . 16 ARG HG2 H 1.64 0.007 1 108 . 16 ARG HG3 H 1.64 0.007 1 109 . 16 ARG HD2 H 3.14 0.007 1 110 . 16 ARG HD3 H 3.14 0.007 1 111 . 17 SER H H 7.32 0.007 1 112 . 17 SER HA H 4.39 0.007 1 113 . 17 SER HB2 H 3.81 0.007 1 114 . 17 SER HB3 H 4.06 0.007 1 115 . 18 ALA H H 8.32 0.007 1 116 . 18 ALA HA H 3.35 0.007 1 117 . 18 ALA HB H 1.12 0.007 1 118 . 19 GLN H H 7.88 0.007 1 119 . 19 GLN HA H 3.94 0.007 1 120 . 19 GLN HB2 H 1.90 0.007 1 121 . 19 GLN HB3 H 1.99 0.007 1 122 . 19 GLN HG2 H 2.34 0.007 1 123 . 19 GLN HG3 H 2.34 0.007 1 124 . 20 ALA H H 7.88 0.007 1 125 . 20 ALA HA H 4.05 0.007 1 126 . 20 ALA HB H 1.53 0.007 1 127 . 21 LEU H H 7.35 0.007 1 128 . 21 LEU HA H 3.12 0.007 1 129 . 21 LEU HB2 H 1.27 0.007 1 130 . 21 LEU HB3 H 1.76 0.007 1 131 . 21 LEU HG H 1.53 0.007 1 132 . 21 LEU HD1 H 0.92 0.007 1 133 . 21 LEU HD2 H 0.98 0.007 1 134 . 22 GLY H H 8.30 0.007 1 135 . 22 GLY HA2 H 3.65 0.007 1 136 . 22 GLY HA3 H 3.79 0.007 1 137 . 23 GLY H H 7.88 0.007 1 138 . 23 GLY HA2 H 3.81 0.007 1 139 . 23 GLY HA3 H 4.05 0.007 1 140 . 24 HIS H H 7.46 0.007 1 141 . 24 HIS HA H 4.27 0.007 1 142 . 24 HIS HB2 H 2.65 0.007 1 143 . 24 HIS HB3 H 3.01 0.007 1 144 . 24 HIS HD2 H 6.99 0.007 3 145 . 24 HIS HE1 H 7.97 0.007 3 146 . 25 MET H H 7.44 0.007 1 147 . 25 MET HA H 4.04 0.007 1 148 . 25 MET HB2 H 1.65 0.007 1 149 . 25 MET HB3 H 1.83 0.007 1 150 . 25 MET HG2 H 2.15 0.007 1 151 . 25 MET HG3 H 2.15 0.007 1 152 . 25 MET HE H 2.44 0.007 1 153 . 26 ASN H H 7.35 0.007 1 154 . 26 ASN HA H 4.31 0.007 1 155 . 26 ASN HB2 H 2.70 0.007 1 156 . 26 ASN HB3 H 2.76 0.007 1 157 . 27 VAL H H 7.86 0.007 1 158 . 27 VAL HA H 3.73 0.007 1 159 . 27 VAL HB H 1.80 0.007 1 160 . 27 VAL HG1 H 0.47 0.007 1 161 . 27 VAL HG2 H 0.57 0.007 1 162 . 28 HIS H H 6.95 0.007 1 163 . 28 HIS HA H 4.57 0.007 1 164 . 28 HIS HB2 H 2.42 0.007 1 165 . 28 HIS HB3 H 2.57 0.007 1 166 . 28 HIS HD2 H 6.77 0.007 1 167 . 28 HIS HE1 H 8.04 0.007 1 168 . 29 ARG H H 7.44 0.007 1 169 . 29 ARG HA H 4.73 0.007 1 170 . 29 ARG HB2 H 1.65 0.007 1 171 . 29 ARG HB3 H 1.65 0.007 1 172 . 29 ARG HG2 H 1.55 0.007 1 173 . 29 ARG HG3 H 1.55 0.007 1 174 . 29 ARG HD2 H 3.20 0.007 1 175 . 29 ARG HD3 H 3.20 0.007 1 176 . 30 ARG H H 8.28 0.007 1 177 . 30 ARG HA H 4.13 0.007 1 178 . 30 ARG HB2 H 1.63 0.007 1 179 . 30 ARG HB3 H 1.63 0.007 1 180 . 30 ARG HG2 H 1.53 0.007 1 181 . 30 ARG HG3 H 1.53 0.007 1 182 . 30 ARG HD2 H 3.12 0.007 1 183 . 30 ARG HD3 H 3.12 0.007 1 184 . 31 ASP H H 7.80 0.007 1 185 . 31 ASP HA H 4.50 0.007 1 186 . 31 ASP HB2 H 3.56 0.007 1 187 . 31 ASP HB3 H 3.56 0.007 1 188 . 32 ARG H H 8.09 0.007 1 189 . 32 ARG HA H 4.26 0.007 1 190 . 32 ARG HB2 H 1.80 0.007 1 191 . 32 ARG HB3 H 1.80 0.007 1 192 . 32 ARG HG2 H 1.61 0.007 1 193 . 32 ARG HG3 H 1.61 0.007 1 194 . 32 ARG HD2 H 3.12 0.007 1 195 . 32 ARG HD3 H 3.12 0.007 1 196 . 33 ALA H H 8.02 0.007 1 197 . 33 ALA HA H 4.19 0.007 1 198 . 33 ALA HB H 1.39 0.007 1 199 . 34 ARG H H 7.93 0.007 1 200 . 34 ARG HA H 4.18 0.007 1 201 . 34 ARG HB2 H 1.78 0.007 1 202 . 34 ARG HB3 H 1.83 0.007 1 203 . 34 ARG HG2 H 1.56 0.007 1 204 . 34 ARG HG3 H 1.56 0.007 1 205 . 34 ARG HD2 H 3.14 0.007 1 206 . 34 ARG HD3 H 3.14 0.007 1 207 . 35 LEU H H 7.89 0.007 1 208 . 35 LEU HA H 4.23 0.007 1 209 . 35 LEU HB2 H 1.64 0.007 1 210 . 35 LEU HB3 H 1.64 0.007 1 211 . 35 LEU HG H 1.60 0.007 1 212 . 35 LEU HD1 H 0.81 0.007 1 213 . 35 LEU HD2 H 0.88 0.007 1 214 . 36 ARG H H 8.03 0.007 1 215 . 36 ARG HA H 4.25 0.007 1 216 . 36 ARG HB2 H 1.62 0.007 1 217 . 36 ARG HB3 H 1.62 0.007 1 218 . 36 ARG HG2 H 1.57 0.007 1 219 . 36 ARG HG3 H 1.57 0.007 1 220 . 36 ARG HD2 H 3.11 0.007 1 221 . 36 ARG HD3 H 3.11 0.007 1 222 . 37 LEU H H 7.89 0.007 1 223 . 37 LEU HA H 4.23 0.007 1 224 . 37 LEU HB2 H 1.64 0.007 1 225 . 37 LEU HB3 H 1.64 0.007 1 226 . 37 LEU HG H 1.57 0.007 1 227 . 37 LEU HD1 H 0.81 0.007 1 228 . 37 LEU HD2 H 0.88 0.007 1 stop_ save_