data_5535 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of R3H domain ; _BMRB_accession_number 5535 _BMRB_flat_file_name bmr5535.str _Entry_type original _Submission_date 2002-09-20 _Accession_date 2002-09-20 _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 Liepinsh Edvards . . 2 Otting Gottfried . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 437 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-21 original author . stop_ _Original_release_date 2003-02-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of the R3H Domain from Human Subp-2' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12547203 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liepinsh Edvards . . 2 Leonchiks Ainars . . 3 Sharipo Anatoly . . 4 Guignard Laurent . . 5 Otting Gottfried . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 326 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 217 _Page_last 223 _Year 2003 _Details . loop_ _Keyword R3H 'NMR structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Edvards Liepinsh, Ainars Leonchiks, Anatoly Sharipo, Laurent Guignard and Gottfried Otting. Solution structure of the R3H domain from human Subp-2 J. Biol. Chem., submitted. ; _Citation_title 'Solution structure of the R3H domain from human Smubp-2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12547203 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liepinsh Edvards . . 2 Leonchiks Ainars . . 3 Sharipo Anatoly . . 4 Guignard Laurent . . 5 Otting Gottfried . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 326 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 217 _Page_last 223 _Year 2003 _Details ; The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general. ; save_ ################################## # Molecular system description # ################################## save_system_R3H _Saveframe_category molecular_system _Mol_system_name 'R3H domain' _Abbreviation_common R3H _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'R3H domain' $R3H 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_R3H _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'single chain biopolymer' _Abbreviation_common R3H _Molecular_mass 9674 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; MGSLNGGSPEGVESQDGVDH FRAMIVEFMASKKMQLEFPP SLNSHDRLRVHQIAEEHGLR HDSSGEGKRRFITVSKRAGS HHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 709 MET 2 710 GLY 3 711 SER 4 712 LEU 5 713 ASN 6 714 GLY 7 715 GLY 8 716 SER 9 717 PRO 10 718 GLU 11 719 GLY 12 720 VAL 13 721 GLU 14 722 SER 15 723 GLN 16 724 ASP 17 725 GLY 18 726 VAL 19 727 ASP 20 728 HIS 21 729 PHE 22 730 ARG 23 731 ALA 24 732 MET 25 733 ILE 26 734 VAL 27 735 GLU 28 736 PHE 29 737 MET 30 738 ALA 31 739 SER 32 740 LYS 33 741 LYS 34 742 MET 35 743 GLN 36 744 LEU 37 745 GLU 38 746 PHE 39 747 PRO 40 748 PRO 41 749 SER 42 750 LEU 43 751 ASN 44 752 SER 45 753 HIS 46 754 ASP 47 755 ARG 48 756 LEU 49 757 ARG 50 758 VAL 51 759 HIS 52 760 GLN 53 761 ILE 54 762 ALA 55 763 GLU 56 764 GLU 57 765 HIS 58 766 GLY 59 767 LEU 60 768 ARG 61 769 HIS 62 770 ASP 63 771 SER 64 772 SER 65 773 GLY 66 774 GLU 67 775 GLY 68 776 LYS 69 777 ARG 70 778 ARG 71 779 PHE 72 780 ILE 73 781 THR 74 782 VAL 75 783 SER 76 784 LYS 77 785 ARG 78 786 ALA 79 787 GLY 80 788 SER 81 789 HIS 82 790 HIS 83 791 HIS 84 792 HIS 85 793 HIS 86 794 HIS 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 BMRB 18391 Smubp2_R3H 100.00 86 100.00 100.00 1.33e-53 PDB 1MSZ "Solution Structure Of The R3h Domain From Human Smubp-2" 100.00 86 100.00 100.00 1.33e-53 PDB 2LRR "Solution Structure Of The R3h Domain From Human Smubp-2 In Complex With 2'-Deoxyguanosine-5'-Monophosphate" 100.00 86 100.00 100.00 1.33e-53 DBJ BAD92039 "immunoglobulin mu binding protein 2 variant [Homo sapiens]" 88.37 629 100.00 100.00 2.50e-43 DBJ BAG35460 "unnamed protein product [Homo sapiens]" 88.37 993 100.00 100.00 6.31e-43 GB AAA53082 "DNA-binding protein [Homo sapiens]" 88.37 993 100.00 100.00 6.44e-43 GB AAA58611 "glial factor-1, partial [Homo sapiens]" 88.37 376 100.00 100.00 2.80e-44 GB AAA70430 "DNA helicase [Homo sapiens]" 88.37 993 100.00 100.00 6.31e-43 GB AAH00290 "IGHMBP2 protein, partial [Homo sapiens]" 88.37 868 100.00 100.00 4.64e-43 GB AAH25299 "IGHMBP2 protein, partial [Homo sapiens]" 88.37 868 100.00 100.00 4.64e-43 REF NP_002171 "DNA-binding protein SMUBP-2 [Homo sapiens]" 88.37 993 100.00 100.00 6.31e-43 REF XP_002821469 "PREDICTED: DNA-binding protein SMUBP-2, partial [Pongo abelii]" 88.37 780 98.68 98.68 5.29e-42 REF XP_003274011 "PREDICTED: DNA-binding protein SMUBP-2 [Nomascus leucogenys]" 88.37 1002 100.00 100.00 7.55e-43 REF XP_003828806 "PREDICTED: DNA-binding protein SMUBP-2 [Pan paniscus]" 88.37 1001 100.00 100.00 7.31e-43 REF XP_004051731 "PREDICTED: DNA-binding protein SMUBP-2 [Gorilla gorilla gorilla]" 88.37 997 98.68 100.00 2.47e-42 SP P38935 "RecName: Full=DNA-binding protein SMUBP-2; AltName: Full=ATP-dependent helicase IGHMBP2; AltName: Full=Glial factor 1; Short=GF" 88.37 993 100.00 100.00 6.31e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $R3H 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 $R3H 'recombinant technology' 'E. coli' Escherichia coli M15 plasmid pQE60 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 $R3H 0.4 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version . loop_ _Task 'spectral processing' stop_ _Details . save_ save_PROSA _Saveframe_category software _Name PROSA _Version . loop_ _Task 'spectral processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_HOHAHA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H HOHAHA' _Sample_label . save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H HOHAHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.2 n/a temperature 298 1 K 'ionic strength' 0.1 . M 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 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'R3H 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 . 1 MET HA H 4.05 0.02 1 2 . 1 MET HB2 H 2.03 0.02 1 3 . 1 MET HB3 H 2.03 0.02 1 4 . 1 MET HG2 H 2.31 0.02 2 5 . 1 MET HG3 H 2.41 0.02 2 6 . 4 LEU H H 8.39 0.02 1 7 . 4 LEU HA H 4.34 0.02 1 8 . 4 LEU HB2 H 1.56 0.02 1 9 . 4 LEU HB3 H 1.56 0.02 1 10 . 4 LEU HD1 H 0.81 0.02 2 11 . 4 LEU HD2 H 0.86 0.02 2 12 . 4 LEU HG H 1.66 0.02 1 13 . 5 ASN H H 7.89 0.02 1 14 . 5 ASN HA H 4.4 0.02 1 15 . 5 ASN HB2 H 2.65 0.02 2 16 . 5 ASN HB3 H 2.76 0.02 2 17 . 9 PRO HA H 4.39 0.02 1 18 . 9 PRO HB2 H 1.89 0.02 2 19 . 9 PRO HB3 H 2.23 0.02 2 20 . 9 PRO HG2 H 1.96 0.02 1 21 . 9 PRO HG3 H 1.96 0.02 1 22 . 9 PRO HD2 H 3.67 0.02 2 23 . 9 PRO HD3 H 3.76 0.02 2 24 . 10 GLU H H 8.44 0.02 1 25 . 10 GLU HA H 4.21 0.02 1 26 . 10 GLU HB2 H 1.89 0.02 2 27 . 10 GLU HB3 H 1.99 0.02 2 28 . 10 GLU HG2 H 2.23 0.02 1 29 . 10 GLU HG3 H 2.23 0.02 1 30 . 11 GLY H H 8.327 0.02 1 31 . 11 GLY HA2 H 3.916 0.02 1 32 . 11 GLY HA3 H 3.916 0.02 1 33 . 12 VAL H H 7.865 0.02 1 34 . 12 VAL HA H 4.076 0.02 1 35 . 12 VAL HB H 2.033 0.02 1 36 . 12 VAL HG1 H 0.845 0.02 2 37 . 12 VAL HG2 H 0.867 0.02 2 38 . 13 GLU H H 8.54 0.02 1 39 . 13 GLU HA H 4.259 0.02 1 40 . 13 GLU HB2 H 1.891 0.02 2 41 . 13 GLU HB3 H 2.002 0.02 2 42 . 13 GLU HG2 H 2.222 0.02 1 43 . 13 GLU HG3 H 2.222 0.02 1 44 . 14 SER H H 8.312 0.02 1 45 . 14 SER HA H 4.381 0.02 1 46 . 14 SER HB2 H 3.787 0.02 2 47 . 14 SER HB3 H 3.844 0.02 2 48 . 15 GLN H H 8.476 0.02 1 49 . 15 GLN HA H 4.299 0.02 1 50 . 15 GLN HB2 H 1.916 0.02 2 51 . 15 GLN HB3 H 2.096 0.02 2 52 . 15 GLN HG2 H 2.3 0.02 1 53 . 15 GLN HG3 H 2.3 0.02 1 54 . 15 GLN HE21 H 7.482 0.02 1 55 . 15 GLN HE22 H 6.772 0.02 1 56 . 16 ASP H H 8.284 0.02 1 57 . 16 ASP HA H 4.503 0.02 1 58 . 16 ASP HB2 H 2.603 0.02 1 59 . 16 ASP HB3 H 2.603 0.02 1 60 . 17 GLY H H 8.263 0.02 1 61 . 17 GLY HA2 H 3.867 0.02 1 62 . 17 GLY HA3 H 3.867 0.02 1 63 . 18 VAL H H 7.917 0.02 1 64 . 18 VAL HA H 3.881 0.02 1 65 . 18 VAL HB H 1.992 0.02 1 66 . 18 VAL HG1 H 0.811 0.02 2 67 . 18 VAL HG2 H 0.878 0.02 2 68 . 19 ASP H H 8.353 0.02 1 69 . 19 ASP HA H 4.514 0.02 1 70 . 19 ASP HB2 H 2.557 0.02 2 71 . 19 ASP HB3 H 2.724 0.02 2 72 . 20 HIS H H 7.98 0.02 1 73 . 20 HIS HA H 4.351 0.02 1 74 . 20 HIS HB2 H 2.908 0.02 2 75 . 20 HIS HB3 H 2.99 0.02 2 76 . 20 HIS HD2 H 6.585 0.02 1 77 . 20 HIS HE1 H 7.827 0.02 1 78 . 21 PHE H H 7.853 0.02 1 79 . 21 PHE HA H 4.523 0.02 1 80 . 21 PHE HB2 H 2.9 0.02 1 81 . 21 PHE HB3 H 2.9 0.02 1 82 . 21 PHE HD1 H 7.135 0.02 1 83 . 21 PHE HD2 H 7.135 0.02 1 84 . 21 PHE HE1 H 7.349 0.02 1 85 . 21 PHE HE2 H 7.349 0.02 1 86 . 21 PHE HZ H 7.217 0.02 1 87 . 22 ARG H H 8.238 0.02 1 88 . 22 ARG HA H 3.813 0.02 1 89 . 22 ARG HB2 H 1.87 0.02 1 90 . 22 ARG HB3 H 1.87 0.02 1 91 . 22 ARG HG2 H 1.59 0.02 1 92 . 22 ARG HG3 H 1.59 0.02 1 93 . 22 ARG HD2 H 3.192 0.02 2 94 . 22 ARG HD3 H 3.345 0.02 2 95 . 23 ALA H H 7.985 0.02 1 96 . 23 ALA HA H 4.014 0.02 1 97 . 23 ALA HB H 1.428 0.02 1 98 . 24 MET H H 7.956 0.02 1 99 . 24 MET HA H 4.038 0.02 1 100 . 24 MET HB2 H 2.001 0.02 1 101 . 24 MET HB3 H 2.311 0.02 1 102 . 24 MET HG2 H 2.418 0.02 1 103 . 24 MET HG3 H 2.578 0.02 1 104 . 24 MET HE H 1.775 0.02 1 105 . 25 ILE H H 7.942 0.02 1 106 . 25 ILE HA H 3.712 0.02 1 107 . 25 ILE HB H 1.945 0.02 1 108 . 25 ILE HG2 H 0.512 0.02 1 109 . 25 ILE HG12 H 1.174 0.02 1 110 . 25 ILE HG13 H 1.758 0.02 1 111 . 25 ILE HD1 H 0.763 0.02 1 112 . 26 VAL H H 8.704 0.02 1 113 . 26 VAL HA H 3.472 0.02 1 114 . 26 VAL HB H 2.054 0.02 1 115 . 26 VAL HG1 H 0.887 0.02 1 116 . 26 VAL HG2 H 0.967 0.02 1 117 . 27 GLU H H 8.032 0.02 1 118 . 27 GLU HA H 4.02 0.02 1 119 . 27 GLU HB2 H 2.05 0.02 1 120 . 27 GLU HB3 H 2.05 0.02 1 121 . 27 GLU HG2 H 2.187 0.02 2 122 . 27 GLU HG3 H 2.342 0.02 2 123 . 28 PHE H H 7.903 0.02 1 124 . 28 PHE HA H 4.445 0.02 1 125 . 28 PHE HB2 H 3.31 0.02 1 126 . 28 PHE HB3 H 3.31 0.02 1 127 . 28 PHE HD1 H 6.98 0.02 1 128 . 28 PHE HD2 H 6.98 0.02 1 129 . 28 PHE HE1 H 6.808 0.02 1 130 . 28 PHE HE2 H 6.808 0.02 1 131 . 28 PHE HZ H 6.903 0.02 1 132 . 29 MET H H 8.699 0.02 1 133 . 29 MET HA H 3.518 0.02 1 134 . 29 MET HB2 H 2.098 0.02 1 135 . 29 MET HB3 H 2.169 0.02 1 136 . 29 MET HG2 H 2.425 0.02 1 137 . 29 MET HG3 H 2.712 0.02 1 138 . 29 MET HE H 2.054 0.02 1 139 . 30 ALA H H 7.088 0.02 1 140 . 30 ALA HA H 4.251 0.02 1 141 . 30 ALA HB H 1.418 0.02 1 142 . 31 SER H H 7.411 0.02 1 143 . 31 SER HA H 4.545 0.02 1 144 . 31 SER HB2 H 4.133 0.02 2 145 . 31 SER HB3 H 4.179 0.02 2 146 . 32 LYS H H 8.443 0.02 1 147 . 32 LYS HA H 4.333 0.02 1 148 . 32 LYS HB2 H 1.777 0.02 1 149 . 32 LYS HB3 H 1.953 0.02 1 150 . 32 LYS HG2 H 1.479 0.02 1 151 . 32 LYS HG3 H 1.479 0.02 1 152 . 32 LYS HD2 H 1.667 0.02 1 153 . 32 LYS HD3 H 1.667 0.02 1 154 . 32 LYS HE2 H 2.976 0.02 1 155 . 32 LYS HE3 H 2.976 0.02 1 156 . 33 LYS H H 7.961 0.02 1 157 . 33 LYS HA H 4.192 0.02 1 158 . 33 LYS HB2 H 1.911 0.02 1 159 . 33 LYS HB3 H 2.046 0.02 1 160 . 33 LYS HG2 H 1.58 0.02 2 161 . 33 LYS HG3 H 1.624 0.02 2 162 . 33 LYS HD2 H 1.816 0.02 1 163 . 33 LYS HD3 H 1.816 0.02 1 164 . 33 LYS HE2 H 3.073 0.02 1 165 . 33 LYS HE3 H 3.073 0.02 1 166 . 34 MET H H 8.69 0.02 1 167 . 34 MET HA H 4.749 0.02 1 168 . 34 MET HB2 H 2.028 0.02 1 169 . 34 MET HB3 H 2.184 0.02 1 170 . 34 MET HG2 H 2.466 0.02 2 171 . 34 MET HG3 H 2.736 0.02 2 172 . 34 MET HE H 1.947 0.02 1 173 . 35 GLN H H 7.798 0.02 1 174 . 35 GLN HA H 5.231 0.02 1 175 . 35 GLN HB2 H 1.876 0.02 1 176 . 35 GLN HB3 H 1.934 0.02 1 177 . 35 GLN HG2 H 2.172 0.02 2 178 . 35 GLN HG3 H 2.264 0.02 2 179 . 35 GLN HE21 H 7.582 0.02 1 180 . 35 GLN HE22 H 6.808 0.02 1 181 . 36 LEU H H 8.84 0.02 1 182 . 36 LEU HA H 4.182 0.02 1 183 . 36 LEU HB2 H -0.061 0.02 1 184 . 36 LEU HB3 H 0.662 0.02 1 185 . 36 LEU HD1 H 0.196 0.02 1 186 . 36 LEU HD2 H 0.436 0.02 1 187 . 36 LEU HG H 0.603 0.02 1 188 . 37 GLU H H 8.459 0.02 1 189 . 37 GLU HA H 4.826 0.02 1 190 . 37 GLU HB2 H 1.759 0.02 1 191 . 37 GLU HB3 H 1.833 0.02 1 192 . 37 GLU HG2 H 2.176 0.02 2 193 . 37 GLU HG3 H 2.282 0.02 2 194 . 38 PHE H H 8.849 0.02 1 195 . 38 PHE HA H 4.424 0.02 1 196 . 38 PHE HB2 H 2.894 0.02 1 197 . 38 PHE HB3 H 3.233 0.02 1 198 . 38 PHE HD1 H 7.107 0.02 1 199 . 38 PHE HD2 H 7.107 0.02 1 200 . 38 PHE HE1 H 7.067 0.02 1 201 . 38 PHE HE2 H 7.067 0.02 1 202 . 38 PHE HZ H 6.859 0.02 1 203 . 39 PRO HA H 4.68 0.02 1 204 . 39 PRO HB2 H 2.033 0.02 1 205 . 39 PRO HB3 H 2.392 0.02 1 206 . 39 PRO HG2 H 1.908 0.02 1 207 . 39 PRO HG3 H 2.1 0.02 1 208 . 39 PRO HD2 H 3.761 0.02 1 209 . 39 PRO HD3 H 3.761 0.02 1 210 . 40 PRO HA H 3.759 0.02 1 211 . 40 PRO HB2 H 2.104 0.02 1 212 . 40 PRO HB3 H 2.392 0.02 1 213 . 40 PRO HG2 H 1.917 0.02 1 214 . 40 PRO HG3 H 2.032 0.02 1 215 . 40 PRO HD2 H 3.54 0.02 1 216 . 40 PRO HD3 H 3.736 0.02 1 217 . 41 SER H H 7.04 0.02 1 218 . 41 SER HA H 4.189 0.02 1 219 . 41 SER HB2 H 3.799 0.02 2 220 . 41 SER HB3 H 4.054 0.02 2 221 . 42 LEU H H 7.019 0.02 1 222 . 42 LEU HA H 4.42 0.02 1 223 . 42 LEU HB2 H 1.612 0.02 1 224 . 42 LEU HB3 H 1.68 0.02 1 225 . 42 LEU HD1 H 0.499 0.02 1 226 . 42 LEU HD2 H 1.03 0.02 1 227 . 42 LEU HG H 1.887 0.02 1 228 . 43 ASN H H 9.247 0.02 1 229 . 43 ASN HA H 4.756 0.02 1 230 . 43 ASN HB2 H 2.961 0.02 2 231 . 43 ASN HB3 H 3.355 0.02 2 232 . 43 ASN HD21 H 7.528 0.02 1 233 . 43 ASN HD22 H 7.027 0.02 1 234 . 44 SER H H 8.227 0.02 1 235 . 44 SER HA H 4.741 0.02 1 236 . 44 SER HB2 H 3.78 0.02 2 237 . 44 SER HB3 H 3.818 0.02 2 238 . 45 HIS H H 7.886 0.02 1 239 . 45 HIS HA H 4.25 0.02 1 240 . 45 HIS HB2 H 3.167 0.02 1 241 . 45 HIS HB3 H 3.167 0.02 1 242 . 45 HIS HD2 H 7.068 0.02 1 243 . 45 HIS HE1 H 7.882 0.02 1 244 . 46 ASP H H 8.547 0.02 1 245 . 46 ASP HA H 4.269 0.02 1 246 . 46 ASP HB2 H 2.435 0.02 1 247 . 46 ASP HB3 H 2.818 0.02 1 248 . 47 ARG H H 8.379 0.02 1 249 . 47 ARG HA H 3.323 0.02 1 250 . 47 ARG HB2 H 1.484 0.02 1 251 . 47 ARG HB3 H 1.833 0.02 1 252 . 47 ARG HG2 H 0.926 0.02 1 253 . 47 ARG HG3 H 1.37 0.02 1 254 . 47 ARG HD2 H 2.993 0.02 2 255 . 47 ARG HD3 H 3.253 0.02 2 256 . 48 LEU H H 7.564 0.02 1 257 . 48 LEU HA H 4.005 0.02 1 258 . 48 LEU HB2 H 1.62 0.02 1 259 . 48 LEU HB3 H 1.739 0.02 1 260 . 48 LEU HD1 H 0.811 0.02 2 261 . 48 LEU HD2 H 0.854 0.02 2 262 . 48 LEU HG H 1.612 0.02 1 263 . 49 ARG H H 7.52 0.02 1 264 . 49 ARG HA H 3.987 0.02 1 265 . 49 ARG HB2 H 1.826 0.02 1 266 . 49 ARG HB3 H 2.001 0.02 1 267 . 49 ARG HG2 H 1.655 0.02 2 268 . 49 ARG HG3 H 1.746 0.02 2 269 . 49 ARG HD2 H 3.206 0.02 2 270 . 49 ARG HD3 H 3.24 0.02 2 271 . 50 VAL H H 7.677 0.02 1 272 . 50 VAL HA H 2.93 0.02 1 273 . 50 VAL HB H 1.382 0.02 1 274 . 50 VAL HG1 H -0.302 0.02 1 275 . 50 VAL HG2 H -0.116 0.02 1 276 . 51 HIS H H 8.398 0.02 1 277 . 51 HIS HA H 3.486 0.02 1 278 . 51 HIS HB2 H 2.887 0.02 1 279 . 51 HIS HB3 H 3.223 0.02 1 280 . 51 HIS HD2 H 6.621 0.02 1 281 . 51 HIS HE1 H 7.689 0.02 1 282 . 52 GLN H H 7.792 0.02 1 283 . 52 GLN HA H 3.856 0.02 1 284 . 52 GLN HB2 H 2.033 0.02 1 285 . 52 GLN HB3 H 2.217 0.02 1 286 . 52 GLN HG2 H 2.285 0.02 1 287 . 52 GLN HG3 H 2.524 0.02 1 288 . 52 GLN HE21 H 7.467 0.02 1 289 . 52 GLN HE22 H 6.702 0.02 1 290 . 53 ILE H H 8.454 0.02 1 291 . 53 ILE HA H 3.802 0.02 1 292 . 53 ILE HB H 1.547 0.02 1 293 . 53 ILE HG2 H 0.953 0.02 1 294 . 53 ILE HG12 H 1.546 0.02 1 295 . 53 ILE HG13 H 1.902 0.02 1 296 . 53 ILE HD1 H 0.75 0.02 1 297 . 54 ALA H H 8.778 0.02 1 298 . 54 ALA HA H 3.925 0.02 1 299 . 54 ALA HB H 1.215 0.02 1 300 . 55 GLU H H 7.903 0.02 1 301 . 55 GLU HA H 4.151 0.02 1 302 . 55 GLU HB2 H 2.042 0.02 1 303 . 55 GLU HB3 H 2.153 0.02 1 304 . 55 GLU HG2 H 2.291 0.02 2 305 . 55 GLU HG3 H 2.45 0.02 2 306 . 56 GLU H H 8.01 0.02 1 307 . 56 GLU HA H 3.947 0.02 1 308 . 56 GLU HB2 H 2.012 0.02 1 309 . 56 GLU HB3 H 2.168 0.02 1 310 . 56 GLU HG2 H 1.928 0.02 2 311 . 56 GLU HG3 H 2.309 0.02 2 312 . 57 HIS H H 7.411 0.02 1 313 . 57 HIS HA H 4.454 0.02 1 314 . 57 HIS HB2 H 2.69 0.02 1 315 . 57 HIS HB3 H 3.664 0.02 1 316 . 57 HIS HD2 H 7.031 0.02 1 317 . 57 HIS HE1 H 7.552 0.02 1 318 . 58 GLY H H 8.009 0.02 1 319 . 58 GLY HA2 H 3.946 0.02 1 320 . 58 GLY HA3 H 3.984 0.02 1 321 . 59 LEU H H 8.028 0.02 1 322 . 59 LEU HA H 4.585 0.02 1 323 . 59 LEU HB2 H 1.611 0.02 1 324 . 59 LEU HB3 H 1.702 0.02 1 325 . 59 LEU HD1 H 0.945 0.02 1 326 . 59 LEU HD2 H 0.965 0.02 1 327 . 59 LEU HG H 1.698 0.02 1 328 . 60 ARG H H 8.672 0.02 1 329 . 60 ARG HA H 4.394 0.02 1 330 . 60 ARG HB2 H 1.665 0.02 1 331 . 60 ARG HB3 H 1.69 0.02 1 332 . 60 ARG HG2 H 1.551 0.02 2 333 . 60 ARG HG3 H 1.879 0.02 2 334 . 60 ARG HD2 H 3.012 0.02 2 335 . 60 ARG HD3 H 3.127 0.02 2 336 . 61 HIS H H 8.495 0.02 1 337 . 61 HIS HA H 5.235 0.02 1 338 . 61 HIS HB2 H 2.63 0.02 1 339 . 61 HIS HB3 H 2.777 0.02 1 340 . 61 HIS HD2 H 7.438 0.02 1 341 . 61 HIS HE1 H 8.186 0.02 1 342 . 62 ASP H H 8.205 0.02 1 343 . 62 ASP HA H 4.9 0.02 1 344 . 62 ASP HB2 H 2.359 0.02 1 345 . 62 ASP HB3 H 2.536 0.02 1 346 . 63 SER H H 8.993 0.02 1 347 . 63 SER HA H 5.171 0.02 1 348 . 63 SER HB2 H 3.411 0.02 1 349 . 63 SER HB3 H 3.714 0.02 1 350 . 64 SER H H 8.257 0.02 1 351 . 64 SER HA H 4.471 0.02 1 352 . 64 SER HB2 H 3.282 0.02 2 353 . 64 SER HB3 H 3.325 0.02 2 354 . 65 GLY H H 8.225 0.02 1 355 . 65 GLY HA2 H 3.708 0.02 2 356 . 65 GLY HA3 H 4.361 0.02 2 357 . 66 GLU H H 8.037 0.02 1 358 . 66 GLU HA H 4.643 0.02 1 359 . 66 GLU HB2 H 1.814 0.02 2 360 . 66 GLU HB3 H 1.961 0.02 2 361 . 66 GLU HG2 H 2.145 0.02 1 362 . 66 GLU HG3 H 2.145 0.02 1 363 . 67 GLY H H 8.911 0.02 1 364 . 67 GLY HA2 H 3.726 0.02 2 365 . 67 GLY HA3 H 3.9 0.02 2 366 . 68 LYS H H 7.962 0.02 1 367 . 68 LYS HA H 4.278 0.02 1 368 . 68 LYS HB2 H 1.641 0.02 1 369 . 68 LYS HB3 H 1.951 0.02 1 370 . 68 LYS HG2 H 1.377 0.02 1 371 . 68 LYS HG3 H 1.453 0.02 1 372 . 68 LYS HD2 H 1.605 0.02 1 373 . 68 LYS HD3 H 1.605 0.02 1 374 . 68 LYS HE2 H 2.932 0.02 1 375 . 68 LYS HE3 H 2.932 0.02 1 376 . 69 ARG H H 7.94 0.02 1 377 . 69 ARG HA H 4.36 0.02 1 378 . 69 ARG HB2 H 1.909 0.02 1 379 . 69 ARG HB3 H 2.08 0.02 1 380 . 69 ARG HG2 H 1.571 0.02 1 381 . 69 ARG HG3 H 1.658 0.02 1 382 . 69 ARG HD2 H 3.199 0.02 1 383 . 69 ARG HD3 H 3.199 0.02 1 384 . 70 ARG H H 7.251 0.02 1 385 . 70 ARG HA H 4.693 0.02 1 386 . 70 ARG HB2 H 1.178 0.02 2 387 . 70 ARG HB3 H 1.657 0.02 2 388 . 70 ARG HG2 H 1.04 0.02 1 389 . 70 ARG HG3 H 1.323 0.02 1 390 . 70 ARG HD2 H 2.993 0.02 2 391 . 70 ARG HD3 H 3.041 0.02 2 392 . 71 PHE H H 8.691 0.02 1 393 . 71 PHE HA H 5.104 0.02 1 394 . 71 PHE HB2 H 2.591 0.02 2 395 . 71 PHE HB3 H 3.343 0.02 2 396 . 71 PHE HD1 H 7.297 0.02 1 397 . 71 PHE HD2 H 7.297 0.02 1 398 . 71 PHE HE1 H 7.131 0.02 1 399 . 71 PHE HE2 H 7.131 0.02 1 400 . 71 PHE HZ H 7.104 0.02 1 401 . 72 ILE H H 8.566 0.02 1 402 . 72 ILE HA H 4.631 0.02 1 403 . 72 ILE HB H 1.279 0.02 1 404 . 72 ILE HG2 H 0.508 0.02 1 405 . 72 ILE HG12 H 0.558 0.02 1 406 . 72 ILE HG13 H 1.207 0.02 1 407 . 72 ILE HD1 H -0.096 0.02 1 408 . 73 THR H H 8.348 0.02 1 409 . 73 THR HA H 5.096 0.02 1 410 . 73 THR HB H 3.811 0.02 1 411 . 73 THR HG2 H 1.009 0.02 1 412 . 74 VAL H H 9.19 0.02 1 413 . 74 VAL HA H 5.276 0.02 1 414 . 74 VAL HB H 1.932 0.02 1 415 . 74 VAL HG1 H 0.75 0.02 1 416 . 74 VAL HG2 H 0.893 0.02 1 417 . 75 SER H H 8.851 0.02 1 418 . 75 SER HA H 5.5 0.02 1 419 . 75 SER HB2 H 3.818 0.02 1 420 . 75 SER HB3 H 3.888 0.02 1 421 . 76 LYS H H 8.216 0.02 1 422 . 76 LYS HA H 4.472 0.02 1 423 . 76 LYS HB2 H 1.705 0.02 1 424 . 76 LYS HB3 H 1.946 0.02 1 425 . 76 LYS HG2 H 1.219 0.02 1 426 . 76 LYS HG3 H 1.311 0.02 1 427 . 77 ARG H H 8.995 0.02 1 428 . 77 ARG HA H 4.285 0.02 1 429 . 77 ARG HB2 H 1.715 0.02 1 430 . 77 ARG HB3 H 1.816 0.02 1 431 . 77 ARG HG2 H 1.578 0.02 1 432 . 77 ARG HG3 H 1.578 0.02 1 433 . 77 ARG HD2 H 3.145 0.02 1 434 . 77 ARG HD3 H 3.145 0.02 1 435 . 78 ALA H H 8.388 0.02 1 436 . 78 ALA HA H 4.266 0.02 1 437 . 78 ALA HB H 1.349 0.02 1 stop_ save_