data_11393 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the 8th C2H2 type zinc finger domain of Zinc finger protein 347 ; _BMRB_accession_number 11393 _BMRB_flat_file_name bmr11393.str _Entry_type original _Submission_date 2010-09-09 _Accession_date 2010-09-09 _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 Masuda K. . . 2 Suzuki S. . . 3 Muto Y. . . 4 Inoue M. . . 5 Kigawa T. . . 6 Terada T. . . 7 Shirouzu M. . . 8 Yokoyama S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 205 "15N chemical shifts" 30 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-09-08 original author . stop_ _Original_release_date 2011-09-08 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the 8th C2H2 type zinc finger domain of Zinc finger protein 347 ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Masuda K. . . 2 Suzuki S. . . 3 Muto Y. . . 4 Inoue M. . . 5 Kigawa T. . . 6 Terada T. . . 7 Shirouzu M. . . 8 Yokoyama S. . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Zinc finger protein 347' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'zinc finger domain' $entity_1 'ZINC ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'zinc finger domain' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; GSSGSSGTGEKPYKCHECGK VFRRNSHLARHQLIHTGEKP SGPSSG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 GLY 5 SER 6 SER 7 GLY 8 THR 9 GLY 10 GLU 11 LYS 12 PRO 13 TYR 14 LYS 15 CYS 16 HIS 17 GLU 18 CYS 19 GLY 20 LYS 21 VAL 22 PHE 23 ARG 24 ARG 25 ASN 26 SER 27 HIS 28 LEU 29 ALA 30 ARG 31 HIS 32 GLN 33 LEU 34 ILE 35 HIS 36 THR 37 GLY 38 GLU 39 LYS 40 PRO 41 SER 42 GLY 43 PRO 44 SER 45 SER 46 GLY 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 2EQ0 "Solution Structure Of The 8th C2h2 Type Zinc Finger Domain Of Zinc Finger Protein 347" 100.00 46 100.00 100.00 2.43e-23 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 Tue Jun 9 16:52:42 2009 ; 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 $entity_1 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_type _Vector_name $entity_1 'cell free synthesis' 'E. coli' Escherichia coli . plasmid P070115-13 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 1.14mM 13C-15N {PROTEIN;} 20mM d-Tris-HCl {(pH7.0);} 100mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 10% D2O {;0.050mM} ZnCl2, 1mM {IDA;} 90% H2O, 10% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1.14 mM '[U-13C; U-15N]' d-Tris-HCl 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' d-DTT 1 mM 'natural abundance' NaN3 0.02 % 'natural abundance' ZnCl2 0.050 mM 'natural abundance' IDA 1 mM 'natural abundance' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 20060702 loop_ _Vendor _Address _Electronic_address 'Delaglio F.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Vendor _Address _Electronic_address 'Johnson B.A.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Kujira _Saveframe_category software _Name Kujira _Version 0.9820 loop_ _Vendor _Address _Electronic_address 'Kobayashi N.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert P.' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 120 0.1 mM pH 7.0 0.05 pH pressure 1 0.001 atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference of 1H was based on the proton of water (4.784ppm at 298K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $XWINNMR $NMRPipe $NMRView $Kujira $CYANA stop_ loop_ _Experiment_label '3D 15N-separated NOESY' '3D 13C-separated NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'zinc finger domain' _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 6 6 SER HA H 4.529 0.030 1 2 6 6 SER HB2 H 3.897 0.030 2 3 6 6 SER HB3 H 3.973 0.030 2 4 7 7 GLY H H 8.094 0.030 1 5 7 7 GLY HA2 H 4.056 0.030 2 6 7 7 GLY HA3 H 4.018 0.030 2 7 7 7 GLY N N 116.883 0.300 1 8 8 8 THR H H 8.201 0.030 1 9 8 8 THR HA H 4.417 0.030 1 10 8 8 THR HB H 4.371 0.030 1 11 8 8 THR HG2 H 1.247 0.030 1 12 8 8 THR N N 113.012 0.300 1 13 10 10 GLU HA H 4.310 0.030 1 14 10 10 GLU HB2 H 2.066 0.030 2 15 10 10 GLU HB3 H 1.961 0.030 2 16 10 10 GLU HG2 H 2.318 0.030 2 17 10 10 GLU HG3 H 2.263 0.030 2 18 11 11 LYS H H 8.419 0.030 1 19 11 11 LYS HA H 4.659 0.030 1 20 11 11 LYS HB2 H 1.768 0.030 2 21 11 11 LYS HB3 H 1.857 0.030 2 22 11 11 LYS HD2 H 1.733 0.030 1 23 11 11 LYS HD3 H 1.733 0.030 1 24 11 11 LYS HE2 H 3.037 0.030 1 25 11 11 LYS HE3 H 3.037 0.030 1 26 11 11 LYS HG2 H 1.509 0.030 1 27 11 11 LYS HG3 H 1.509 0.030 1 28 11 11 LYS N N 123.465 0.300 1 29 12 12 PRO HA H 4.425 0.030 1 30 12 12 PRO HB2 H 2.100 0.030 2 31 12 12 PRO HB3 H 1.582 0.030 2 32 12 12 PRO HD2 H 3.691 0.030 2 33 12 12 PRO HD3 H 3.864 0.030 2 34 12 12 PRO HG2 H 1.568 0.030 1 35 12 12 PRO HG3 H 1.568 0.030 1 36 13 13 TYR H H 8.248 0.030 1 37 13 13 TYR HA H 4.608 0.030 1 38 13 13 TYR HB2 H 2.989 0.030 2 39 13 13 TYR HB3 H 2.874 0.030 2 40 13 13 TYR HD1 H 7.031 0.030 1 41 13 13 TYR HD2 H 7.031 0.030 1 42 13 13 TYR HE1 H 6.900 0.030 1 43 13 13 TYR HE2 H 6.900 0.030 1 44 13 13 TYR N N 120.174 0.300 1 45 14 14 LYS H H 8.469 0.030 1 46 14 14 LYS HA H 5.032 0.030 1 47 14 14 LYS HB2 H 1.511 0.030 2 48 14 14 LYS HB3 H 1.693 0.030 2 49 14 14 LYS HD2 H 1.559 0.030 1 50 14 14 LYS HD3 H 1.559 0.030 1 51 14 14 LYS HE2 H 2.892 0.030 1 52 14 14 LYS HE3 H 2.892 0.030 1 53 14 14 LYS HG2 H 1.106 0.030 2 54 14 14 LYS HG3 H 0.946 0.030 2 55 14 14 LYS N N 125.119 0.300 1 56 15 15 CYS H H 9.369 0.030 1 57 15 15 CYS HA H 4.618 0.030 1 58 15 15 CYS HB2 H 2.886 0.030 2 59 15 15 CYS HB3 H 3.429 0.030 2 60 15 15 CYS N N 127.752 0.300 1 61 16 16 HIS HA H 4.440 0.030 1 62 16 16 HIS HB2 H 3.274 0.030 1 63 16 16 HIS HB3 H 3.274 0.030 1 64 16 16 HIS HD2 H 7.193 0.030 1 65 16 16 HIS HE1 H 7.972 0.030 1 66 17 17 GLU H H 8.529 0.030 1 67 17 17 GLU HA H 4.203 0.030 1 68 17 17 GLU HB2 H 1.333 0.030 1 69 17 17 GLU HB3 H 1.333 0.030 1 70 17 17 GLU HG2 H 1.842 0.030 2 71 17 17 GLU HG3 H 1.711 0.030 2 72 17 17 GLU N N 120.822 0.300 1 73 18 18 CYS H H 7.947 0.030 1 74 18 18 CYS HA H 5.210 0.030 1 75 18 18 CYS HB2 H 3.481 0.030 2 76 18 18 CYS HB3 H 2.906 0.030 2 77 18 18 CYS N N 114.346 0.300 1 78 19 19 GLY H H 8.268 0.030 1 79 19 19 GLY HA2 H 3.743 0.030 2 80 19 19 GLY HA3 H 4.293 0.030 2 81 19 19 GLY N N 113.758 0.300 1 82 20 20 LYS H H 7.911 0.030 1 83 20 20 LYS HA H 4.044 0.030 1 84 20 20 LYS HB2 H 1.406 0.030 2 85 20 20 LYS HB3 H 1.266 0.030 2 86 20 20 LYS HD2 H 1.528 0.030 1 87 20 20 LYS HD3 H 1.528 0.030 1 88 20 20 LYS HE2 H 2.973 0.030 1 89 20 20 LYS HE3 H 2.973 0.030 1 90 20 20 LYS HG2 H 1.155 0.030 2 91 20 20 LYS HG3 H 1.535 0.030 2 92 20 20 LYS N N 122.502 0.300 1 93 21 21 VAL H H 7.650 0.030 1 94 21 21 VAL HA H 4.831 0.030 1 95 21 21 VAL HB H 1.891 0.030 1 96 21 21 VAL HG1 H 0.855 0.030 1 97 21 21 VAL HG2 H 0.852 0.030 1 98 21 21 VAL N N 116.749 0.300 1 99 22 22 PHE H H 8.850 0.030 1 100 22 22 PHE HA H 4.830 0.030 1 101 22 22 PHE HB2 H 2.795 0.030 2 102 22 22 PHE HB3 H 3.513 0.030 2 103 22 22 PHE HD1 H 7.315 0.030 1 104 22 22 PHE HD2 H 7.315 0.030 1 105 22 22 PHE HE1 H 6.877 0.030 1 106 22 22 PHE HE2 H 6.877 0.030 1 107 22 22 PHE HZ H 6.231 0.030 1 108 22 22 PHE N N 121.158 0.300 1 109 23 23 ARG H H 8.432 0.030 1 110 23 23 ARG HA H 4.652 0.030 1 111 23 23 ARG HB2 H 2.135 0.030 2 112 23 23 ARG HB3 H 1.996 0.030 2 113 23 23 ARG HD2 H 3.329 0.030 1 114 23 23 ARG HD3 H 3.329 0.030 1 115 23 23 ARG HG2 H 1.807 0.030 2 116 23 23 ARG HG3 H 1.894 0.030 2 117 23 23 ARG N N 118.944 0.300 1 118 24 24 ARG H H 7.298 0.030 1 119 24 24 ARG HA H 4.659 0.030 1 120 24 24 ARG HB2 H 1.731 0.030 2 121 24 24 ARG HB3 H 0.910 0.030 2 122 24 24 ARG HD2 H 3.086 0.030 2 123 24 24 ARG HD3 H 2.994 0.030 2 124 24 24 ARG HG2 H 1.457 0.030 1 125 24 24 ARG HG3 H 1.457 0.030 1 126 24 24 ARG N N 113.312 0.300 1 127 25 25 ASN HA H 3.594 0.030 1 128 25 25 ASN HB2 H 2.463 0.030 2 129 25 25 ASN HB3 H 2.264 0.030 2 130 25 25 ASN HD21 H 7.362 0.030 2 131 25 25 ASN HD22 H 6.846 0.030 2 132 25 25 ASN ND2 N 112.284 0.300 1 133 26 26 SER HA H 4.097 0.030 1 134 26 26 SER HB2 H 3.902 0.030 1 135 26 26 SER HB3 H 3.902 0.030 1 136 27 27 HIS H H 6.815 0.030 1 137 27 27 HIS HA H 4.473 0.030 1 138 27 27 HIS HB2 H 3.418 0.030 2 139 27 27 HIS HB3 H 3.330 0.030 2 140 27 27 HIS HD2 H 7.018 0.030 1 141 27 27 HIS HE1 H 7.882 0.030 1 142 27 27 HIS N N 121.893 0.300 1 143 28 28 LEU H H 7.106 0.030 1 144 28 28 LEU HA H 3.227 0.030 1 145 28 28 LEU HB2 H 2.035 0.030 2 146 28 28 LEU HB3 H 1.268 0.030 2 147 28 28 LEU HD1 H 1.075 0.030 1 148 28 28 LEU HD2 H 1.040 0.030 1 149 28 28 LEU HG H 1.566 0.030 1 150 28 28 LEU N N 122.244 0.300 1 151 29 29 ALA H H 8.297 0.030 1 152 29 29 ALA HA H 4.151 0.030 1 153 29 29 ALA HB H 1.410 0.030 1 154 29 29 ALA N N 121.114 0.300 1 155 30 30 ARG H H 7.433 0.030 1 156 30 30 ARG HA H 4.091 0.030 1 157 30 30 ARG HB2 H 1.891 0.030 1 158 30 30 ARG HB3 H 1.891 0.030 1 159 30 30 ARG HD2 H 3.226 0.030 1 160 30 30 ARG HD3 H 3.226 0.030 1 161 30 30 ARG HG2 H 1.760 0.030 2 162 30 30 ARG HG3 H 1.708 0.030 2 163 30 30 ARG N N 116.361 0.300 1 164 31 31 HIS H H 7.648 0.030 1 165 31 31 HIS HA H 4.226 0.030 1 166 31 31 HIS HB2 H 3.150 0.030 2 167 31 31 HIS HB3 H 2.894 0.030 2 168 31 31 HIS HD2 H 6.960 0.030 1 169 31 31 HIS HE1 H 8.089 0.030 1 170 31 31 HIS N N 119.547 0.300 1 171 32 32 GLN H H 8.412 0.030 1 172 32 32 GLN HA H 3.738 0.030 1 173 32 32 GLN HB2 H 2.326 0.030 2 174 32 32 GLN HB3 H 2.255 0.030 2 175 32 32 GLN HE21 H 7.650 0.030 2 176 32 32 GLN HE22 H 7.118 0.030 2 177 32 32 GLN HG2 H 2.823 0.030 1 178 32 32 GLN HG3 H 2.823 0.030 1 179 32 32 GLN N N 115.112 0.300 1 180 32 32 GLN NE2 N 112.311 0.300 1 181 33 33 LEU H H 7.116 0.030 1 182 33 33 LEU HA H 4.176 0.030 1 183 33 33 LEU HB2 H 1.791 0.030 2 184 33 33 LEU HB3 H 1.541 0.030 2 185 33 33 LEU HD1 H 0.881 0.030 1 186 33 33 LEU HD2 H 0.983 0.030 1 187 33 33 LEU HG H 1.909 0.030 1 188 33 33 LEU N N 117.802 0.300 1 189 34 34 ILE H H 7.888 0.030 1 190 34 34 ILE HA H 4.006 0.030 1 191 34 34 ILE HB H 1.710 0.030 1 192 34 34 ILE HD1 H 0.739 0.030 1 193 34 34 ILE HG12 H 0.991 0.030 2 194 34 34 ILE HG13 H 0.836 0.030 2 195 34 34 ILE HG2 H 0.619 0.030 1 196 34 34 ILE N N 116.294 0.300 1 197 35 35 HIS H H 7.281 0.030 1 198 35 35 HIS HA H 4.907 0.030 1 199 35 35 HIS HB2 H 3.275 0.030 2 200 35 35 HIS HB3 H 3.389 0.030 2 201 35 35 HIS HD2 H 6.780 0.030 1 202 35 35 HIS HE1 H 8.087 0.030 1 203 35 35 HIS N N 117.742 0.300 1 204 36 36 THR H H 7.859 0.030 1 205 36 36 THR HA H 4.407 0.030 1 206 36 36 THR HB H 4.330 0.030 1 207 36 36 THR HG2 H 1.295 0.030 1 208 36 36 THR N N 111.826 0.300 1 209 37 37 GLY HA2 H 4.042 0.030 2 210 38 38 GLU H H 8.129 0.030 1 211 38 38 GLU HA H 4.310 0.030 1 212 38 38 GLU HB2 H 2.062 0.030 2 213 38 38 GLU HB3 H 1.958 0.030 2 214 38 38 GLU HG2 H 2.335 0.030 2 215 38 38 GLU HG3 H 2.267 0.030 2 216 38 38 GLU N N 120.447 0.300 1 217 39 39 LYS H H 8.313 0.030 1 218 39 39 LYS HA H 4.590 0.030 1 219 39 39 LYS HB2 H 1.656 0.030 1 220 39 39 LYS HB3 H 1.656 0.030 1 221 39 39 LYS HD2 H 1.630 0.030 1 222 39 39 LYS HD3 H 1.630 0.030 1 223 39 39 LYS HE2 H 2.972 0.030 1 224 39 39 LYS HE3 H 2.972 0.030 1 225 39 39 LYS HG2 H 1.374 0.030 2 226 39 39 LYS HG3 H 1.280 0.030 2 227 39 39 LYS N N 122.800 0.300 1 228 40 40 PRO HD2 H 3.709 0.030 2 229 40 40 PRO HD3 H 3.628 0.030 2 230 40 40 PRO HG2 H 1.923 0.030 2 231 40 40 PRO HG3 H 1.783 0.030 2 232 41 41 SER H H 8.526 0.030 1 233 41 41 SER N N 121.733 0.300 1 234 44 44 SER H H 8.543 0.030 1 235 44 44 SER N N 116.597 0.300 1 stop_ save_