data_16141 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of the HACS1 SH3 domain ; _BMRB_accession_number 16141 _BMRB_flat_file_name bmr16141.str _Entry_type original _Submission_date 2009-01-27 _Accession_date 2009-01-27 _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 Donaldson Logan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 320 "13C chemical shifts" 249 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-07 original author . stop_ _Original_release_date 2012-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR structure of the HACS1 SH3 domain' _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 Donaldson Logan . . stop_ _Journal_abbreviation 'Not known' _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 'HACS1 SH3 domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HACS1 SH3 domain' $entity 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'HACS1 SH3 domain' _Molecular_mass 7092.297 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 63 _Mol_residue_sequence ; GPFCGRARVHTDFTPSPYDT DSLKIKKGDIIDIICKTPMG MWTGMLNNKVGNFKFIYVDV ISE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 25 GLY 2 26 PRO 3 27 PHE 4 28 CYS 5 29 GLY 6 30 ARG 7 31 ALA 8 32 ARG 9 33 VAL 10 34 HIS 11 35 THR 12 36 ASP 13 37 PHE 14 38 THR 15 39 PRO 16 40 SER 17 41 PRO 18 42 TYR 19 43 ASP 20 44 THR 21 45 ASP 22 46 SER 23 47 LEU 24 48 LYS 25 49 ILE 26 50 LYS 27 51 LYS 28 52 GLY 29 53 ASP 30 54 ILE 31 55 ILE 32 56 ASP 33 57 ILE 34 58 ILE 35 59 CYS 36 60 LYS 37 61 THR 38 62 PRO 39 63 MET 40 64 GLY 41 65 MET 42 66 TRP 43 67 THR 44 68 GLY 45 69 MET 46 70 LEU 47 71 ASN 48 72 ASN 49 73 LYS 50 74 VAL 51 75 GLY 52 76 ASN 53 77 PHE 54 78 LYS 55 79 PHE 56 80 ILE 57 81 TYR 58 82 VAL 59 83 ASP 60 84 VAL 61 85 ILE 62 86 SER 63 87 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 2KEA "Nmr Solution Structure Of The Hacs1 Sh3 Domain" 100.00 63 100.00 100.00 5.64e-38 DBJ BAB84358 "NASH [Rattus norvegicus]" 100.00 364 100.00 100.00 5.26e-39 DBJ BAG54155 "unnamed protein product [Homo sapiens]" 100.00 373 100.00 100.00 2.77e-38 EMBL CAB90391 "protein with homology to KIAA0790 [Homo sapiens]" 100.00 373 100.00 100.00 2.50e-38 EMBL CDG37814 "SAM domain, SH3 domain and nuclear localization signals 1 [Homo sapiens]" 100.00 304 100.00 100.00 4.81e-39 GB AAG23355 "SAMSN1 [Homo sapiens]" 100.00 373 100.00 100.00 2.50e-38 GB AAG23356 "SAMSN1 [Mus musculus]" 100.00 364 98.41 100.00 1.21e-38 GB AAH29112 "SAM domain, SH3 domain and nuclear localization signals 1 [Homo sapiens]" 100.00 373 100.00 100.00 2.50e-38 GB AAI03063 "SAM domain, SH3 domain and nuclear localization signals 1 [Bos taurus]" 100.00 366 100.00 100.00 1.42e-38 GB AAK07746 "SH3-SAM adaptor protein [Homo sapiens]" 100.00 441 100.00 100.00 3.92e-38 REF NP_001030481 "SAM domain-containing protein SAMSN-1 [Bos taurus]" 100.00 366 100.00 100.00 1.42e-38 REF NP_001243299 "SAM domain-containing protein SAMSN-1 isoform 2 [Homo sapiens]" 100.00 441 100.00 100.00 3.20e-38 REF NP_001273452 "SAM domain-containing protein SAMSN-1 isoform 3 [Homo sapiens]" 100.00 304 100.00 100.00 4.81e-39 REF NP_071419 "SAM domain-containing protein SAMSN-1 isoform 1 [Homo sapiens]" 100.00 373 100.00 100.00 2.50e-38 REF NP_570834 "SAM domain-containing protein SAMSN-1 [Rattus norvegicus]" 100.00 364 100.00 100.00 5.26e-39 SP Q9NSI8 "RecName: Full=SAM domain-containing protein SAMSN-1; AltName: Full=Hematopoietic adaptor containing SH3 and SAM domains 1; AltN" 100.00 373 100.00 100.00 2.50e-38 TPG DAA33638 "TPA: SAM domain, SH3 domain and nuclear localization signals 1 [Bos taurus]" 100.00 366 100.00 100.00 1.42e-38 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 _Variant _Vector_name _Details $entity 'recombinant technology' . Escherichia coli K12 BL21(DE3) pDEST586 'His6-MBP-TEV fusion expression vector' 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 $entity 0.6 mM '[U-98% 13C; U-98% 15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' 'sodium azide' 0.05 % 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.1 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'peak picking' stop_ _Details 'custom OS X version' save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.21 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model NMRS _Field_strength 600 _Details 'equipped with Gen3 salt tolerant cold probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 7.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'Chemical shifts were analysed with PREDITOR (Wishart laboratory). The following corrections were made: CA = -0.44, CB = 0.41, CO = -0.31, HA = 0.05, N = 1.12, HN = 0.04' 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 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_assignments_hacs1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D CBCA(CO)NH' '3D C(CO)NH' '3D H(CCO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HACS1 SH3 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 26 2 PRO HA H 4.50 . . 2 26 2 PRO HB2 H 2.20 . . 3 26 2 PRO HG2 H 1.85 . . 4 26 2 PRO C C 177.48 . . 5 26 2 PRO CA C 61.91 . . 6 26 2 PRO CB C 45.16 . . 7 26 2 PRO CD C 44.37 . . 8 26 2 PRO CG C 26.37 . . 9 27 3 PHE H H 8.79 . . 10 27 3 PHE HA H 5.40 . . 11 27 3 PHE HB2 H 3.66 . . 12 27 3 PHE HB3 H 2.90 . . 13 27 3 PHE HD1 H 7.16 . . 14 27 3 PHE C C 175.34 . . 15 27 3 PHE CA C 56.43 . . 16 27 3 PHE CB C 42.19 . . 17 27 3 PHE N N 121.64 . . 18 28 4 CYS H H 9.17 . . 19 28 4 CYS HA H 5.14 . . 20 28 4 CYS HB2 H 3.06 . . 21 28 4 CYS HB3 H 2.75 . . 22 28 4 CYS C C 173.20 . . 23 28 4 CYS CA C 55.61 . . 24 28 4 CYS CB C 28.49 . . 25 28 4 CYS N N 117.15 . . 26 29 5 GLY H H 7.67 . . 27 29 5 GLY HA2 H 4.52 . . 28 29 5 GLY HA3 H 3.99 . . 29 29 5 GLY C C 171.69 . . 30 29 5 GLY CA C 44.29 . . 31 29 5 GLY N N 110.21 . . 32 30 6 ARG H H 8.79 . . 33 30 6 ARG HA H 5.51 . . 34 30 6 ARG HB2 H 1.59 . . 35 30 6 ARG HB3 H 1.66 . . 36 30 6 ARG HD2 H 3.06 . . 37 30 6 ARG HD3 H 3.06 . . 38 30 6 ARG HG2 H 0.72 . . 39 30 6 ARG HG3 H 0.92 . . 40 30 6 ARG C C 173.93 . . 41 30 6 ARG CA C 54.80 . . 42 30 6 ARG CB C 35.56 . . 43 30 6 ARG CD C 44.37 . . 44 30 6 ARG CG C 27.37 . . 45 30 6 ARG N N 120.79 . . 46 31 7 ALA H H 9.25 . . 47 31 7 ALA HA H 5.40 . . 48 31 7 ALA HB H 1.22 . . 49 31 7 ALA C C 173.82 . . 50 31 7 ALA CA C 49.36 . . 51 31 7 ALA CB C 22.84 . . 52 31 7 ALA N N 124.67 . . 53 32 8 ARG H H 9.23 . . 54 32 8 ARG HA H 5.31 . . 55 32 8 ARG HB2 H 1.41 . . 56 32 8 ARG HB3 H 1.51 . . 57 32 8 ARG HD2 H 3.23 . . 58 32 8 ARG HD3 H 3.23 . . 59 32 8 ARG HG2 H 0.78 . . 60 32 8 ARG HG3 H 1.39 . . 61 32 8 ARG C C 176.22 . . 62 32 8 ARG CA C 53.38 . . 63 32 8 ARG CB C 33.37 . . 64 32 8 ARG CD C 43.37 . . 65 32 8 ARG CG C 27.37 . . 66 32 8 ARG N N 123.08 . . 67 33 9 VAL H H 9.46 . . 68 33 9 VAL HA H 3.93 . . 69 33 9 VAL HB H 2.19 . . 70 33 9 VAL HG1 H 0.79 . . 71 33 9 VAL HG2 H 0.68 . . 72 33 9 VAL C C 176.36 . . 73 33 9 VAL CA C 62.94 . . 74 33 9 VAL CB C 32.86 . . 75 33 9 VAL CG1 C 23.52 . . 76 33 9 VAL CG2 C 23.17 . . 77 33 9 VAL N N 132.60 . . 78 34 10 HIS H H 8.94 . . 79 34 10 HIS HA H 5.14 . . 80 34 10 HIS HB2 H 3.29 . . 81 34 10 HIS HB3 H 3.00 . . 82 34 10 HIS HD2 H 6.86 . . 83 34 10 HIS HE1 H 7.86 . . 84 34 10 HIS C C 174.80 . . 85 34 10 HIS CA C 54.46 . . 86 34 10 HIS CB C 32.75 . . 87 34 10 HIS CD2 C 118.57 . . 88 34 10 HIS CE1 C 140.15 . . 89 34 10 HIS N N 126.98 . . 90 35 11 THR H H 7.12 . . 91 35 11 THR HA H 4.52 . . 92 35 11 THR HB H 3.84 . . 93 35 11 THR HG2 H 1.27 . . 94 35 11 THR C C 169.68 . . 95 35 11 THR CA C 62.21 . . 96 35 11 THR CB C 74.60 . . 97 35 11 THR CG2 C 20.27 . . 98 35 11 THR N N 122.97 . . 99 36 12 ASP H H 8.12 . . 100 36 12 ASP HA H 4.27 . . 101 36 12 ASP HB2 H 2.66 . . 102 36 12 ASP HB3 H 2.50 . . 103 36 12 ASP C C 175.33 . . 104 36 12 ASP CA C 54.32 . . 105 36 12 ASP CB C 41.80 . . 106 36 12 ASP N N 123.37 . . 107 37 13 PHE H H 8.28 . . 108 37 13 PHE HA H 4.42 . . 109 37 13 PHE HB2 H 2.26 . . 110 37 13 PHE HB3 H 2.38 . . 111 37 13 PHE HD1 H 7.14 . . 112 37 13 PHE HE1 H 6.93 . . 113 37 13 PHE C C 172.58 . . 114 37 13 PHE CA C 58.78 . . 115 37 13 PHE CB C 41.50 . . 116 37 13 PHE CD1 C 132.18 . . 117 37 13 PHE CE1 C 132.51 . . 118 37 13 PHE N N 120.31 . . 119 38 14 THR H H 7.83 . . 120 38 14 THR HA H 4.51 . . 121 38 14 THR HB H 3.66 . . 122 38 14 THR HG2 H 1.05 . . 123 38 14 THR CA C 58.29 . . 124 38 14 THR CB C 70.43 . . 125 38 14 THR CG2 C 21.66 . . 126 38 14 THR N N 126.97 . . 127 39 15 PRO HA H 4.29 . . 128 39 15 PRO HB2 H 2.16 . . 129 39 15 PRO HB3 H 2.42 . . 130 39 15 PRO HD2 H 3.14 . . 131 39 15 PRO HD3 H 3.14 . . 132 39 15 PRO HG2 H 1.82 . . 133 39 15 PRO HG3 H 1.78 . . 134 39 15 PRO C C 175.94 . . 135 39 15 PRO CA C 61.41 . . 136 39 15 PRO CB C 33.27 . . 137 39 15 PRO CD C 51.45 . . 138 39 15 PRO CG C 26.87 . . 139 40 16 SER H H 9.10 . . 140 40 16 SER HA H 4.16 . . 141 40 16 SER HB2 H 3.88 . . 142 40 16 SER HB3 H 3.88 . . 143 40 16 SER CA C 56.67 . . 144 40 16 SER CB C 63.30 . . 145 40 16 SER N N 120.07 . . 146 41 17 PRO HA H 4.25 . . 147 41 17 PRO HB2 H 1.40 . . 148 41 17 PRO HB3 H 2.17 . . 149 41 17 PRO HD2 H 3.65 . . 150 41 17 PRO HD3 H 3.80 . . 151 41 17 PRO HG2 H 1.77 . . 152 41 17 PRO HG3 H 1.89 . . 153 41 17 PRO C C 176.40 . . 154 41 17 PRO CA C 64.30 . . 155 41 17 PRO CB C 32.19 . . 156 41 17 PRO CD C 50.81 . . 157 41 17 PRO CG C 27.37 . . 158 42 18 TYR H H 7.40 . . 159 42 18 TYR HA H 4.56 . . 160 42 18 TYR HB2 H 3.28 . . 161 42 18 TYR HB3 H 2.82 . . 162 42 18 TYR HD1 H 7.10 . . 163 42 18 TYR HE1 H 6.86 . . 164 42 18 TYR C C 175.24 . . 165 42 18 TYR CA C 56.83 . . 166 42 18 TYR CB C 38.09 . . 167 42 18 TYR CD1 C 133.21 . . 168 42 18 TYR CE1 C 118.52 . . 169 42 18 TYR N N 114.41 . . 170 43 19 ASP H H 7.65 . . 171 43 19 ASP HA H 5.01 . . 172 43 19 ASP HB2 H 3.13 . . 173 43 19 ASP HB3 H 2.64 . . 174 43 19 ASP C C 176.47 . . 175 43 19 ASP CA C 52.47 . . 176 43 19 ASP CB C 40.82 . . 177 43 19 ASP N N 124.07 . . 178 44 20 THR H H 8.11 . . 179 44 20 THR HA H 4.52 . . 180 44 20 THR HB H 4.23 . . 181 44 20 THR HG2 H 1.23 . . 182 44 20 THR CA C 62.77 . . 183 44 20 THR CB C 69.76 . . 184 44 20 THR CG2 C 21.72 . . 185 44 20 THR N N 114.75 . . 186 45 21 ASP H H 8.60 . . 187 45 21 ASP HA H 4.93 . . 188 45 21 ASP HB2 H 2.75 . . 189 45 21 ASP HB3 H 2.75 . . 190 45 21 ASP C C 176.50 . . 191 45 21 ASP CA C 54.67 . . 192 45 21 ASP CB C 42.37 . . 193 45 21 ASP N N 121.51 . . 194 46 22 SER H H 8.06 . . 195 46 22 SER HA H 4.86 . . 196 46 22 SER HB2 H 4.06 . . 197 46 22 SER HB3 H 3.80 . . 198 46 22 SER C C 173.87 . . 199 46 22 SER CA C 58.76 . . 200 46 22 SER CB C 64.28 . . 201 46 22 SER N N 118.18 . . 202 47 23 LEU H H 8.67 . . 203 47 23 LEU HA H 4.31 . . 204 47 23 LEU HB2 H 1.49 . . 205 47 23 LEU HB3 H 1.13 . . 206 47 23 LEU HD1 H 0.80 . . 207 47 23 LEU HD2 H 0.63 . . 208 47 23 LEU C C 176.18 . . 209 47 23 LEU CA C 54.28 . . 210 47 23 LEU CB C 44.58 . . 211 47 23 LEU CD1 C 21.72 . . 212 47 23 LEU CD2 C 25.52 . . 213 47 23 LEU N N 123.43 . . 214 48 24 LYS H H 8.33 . . 215 48 24 LYS HA H 4.64 . . 216 48 24 LYS HB2 H 1.69 . . 217 48 24 LYS HB3 H 1.84 . . 218 48 24 LYS HD2 H 1.21 . . 219 48 24 LYS HD3 H 1.21 . . 220 48 24 LYS HE2 H 2.93 . . 221 48 24 LYS HE3 H 2.93 . . 222 48 24 LYS HG2 H 1.52 . . 223 48 24 LYS HG3 H 1.52 . . 224 48 24 LYS C C 175.61 . . 225 48 24 LYS CA C 56.05 . . 226 48 24 LYS CB C 32.94 . . 227 48 24 LYS CD C 25.52 . . 228 48 24 LYS CE C 42.37 . . 229 48 24 LYS CG C 29.41 . . 230 48 24 LYS N N 124.32 . . 231 49 25 ILE H H 8.55 . . 232 49 25 ILE HA H 4.90 . . 233 49 25 ILE HB H 1.93 . . 234 49 25 ILE HD1 H 0.77 . . 235 49 25 ILE HG12 H 1.63 . . 236 49 25 ILE HG13 H 1.38 . . 237 49 25 ILE HG2 H 0.62 . . 238 49 25 ILE C C 173.87 . . 239 49 25 ILE CA C 59.16 . . 240 49 25 ILE CB C 41.68 . . 241 49 25 ILE CD1 C 12.17 . . 242 49 25 ILE CG1 C 25.37 . . 243 49 25 ILE CG2 C 18.08 . . 244 49 25 ILE N N 121.14 . . 245 50 26 LYS H H 9.22 . . 246 50 26 LYS HA H 4.90 . . 247 50 26 LYS HB2 H 1.21 . . 248 50 26 LYS HD2 H 1.59 . . 249 50 26 LYS HE2 H 2.95 . . 250 50 26 LYS HG2 H 1.32 . . 251 50 26 LYS C C 174.68 . . 252 50 26 LYS CA C 52.91 . . 253 50 26 LYS CB C 36.30 . . 254 50 26 LYS CD C 23.37 . . 255 50 26 LYS CE C 42.37 . . 256 50 26 LYS CG C 28.37 . . 257 50 26 LYS N N 126.70 . . 258 51 27 LYS H H 8.66 . . 259 51 27 LYS HA H 3.45 . . 260 51 27 LYS HB2 H 1.66 . . 261 51 27 LYS HB3 H 1.57 . . 262 51 27 LYS HD2 H 1.22 . . 263 51 27 LYS HD3 H 1.22 . . 264 51 27 LYS HE2 H 2.95 . . 265 51 27 LYS HE3 H 2.95 . . 266 51 27 LYS HG2 H 1.58 . . 267 51 27 LYS HG3 H 1.58 . . 268 51 27 LYS C C 177.01 . . 269 51 27 LYS CA C 58.27 . . 270 51 27 LYS CB C 32.79 . . 271 51 27 LYS CD C 24.37 . . 272 51 27 LYS CE C 42.37 . . 273 51 27 LYS CG C 29.37 . . 274 51 27 LYS N N 122.24 . . 275 52 28 GLY H H 9.00 . . 276 52 28 GLY HA2 H 4.57 . . 277 52 28 GLY HA3 H 3.47 . . 278 52 28 GLY C C 174.30 . . 279 52 28 GLY CA C 44.36 . . 280 52 28 GLY N N 115.89 . . 281 53 29 ASP H H 8.54 . . 282 53 29 ASP HA H 4.46 . . 283 53 29 ASP HB2 H 2.68 . . 284 53 29 ASP HB3 H 2.36 . . 285 53 29 ASP C C 174.67 . . 286 53 29 ASP CA C 55.41 . . 287 53 29 ASP CB C 42.55 . . 288 53 29 ASP N N 123.96 . . 289 54 30 ILE H H 8.32 . . 290 54 30 ILE HA H 4.98 . . 291 54 30 ILE HB H 1.78 . . 292 54 30 ILE HD1 H 0.78 . . 293 54 30 ILE HG12 H 1.14 . . 294 54 30 ILE HG13 H 1.14 . . 295 54 30 ILE HG2 H 0.69 . . 296 54 30 ILE C C 174.53 . . 297 54 30 ILE CA C 58.42 . . 298 54 30 ILE CB C 38.64 . . 299 54 30 ILE CD1 C 11.63 . . 300 54 30 ILE CG1 C 27.37 . . 301 54 30 ILE CG2 C 17.46 . . 302 54 30 ILE N N 121.73 . . 303 55 31 ILE H H 9.07 . . 304 55 31 ILE HA H 4.20 . . 305 55 31 ILE HB H 1.07 . . 306 55 31 ILE HD1 H -0.31 . . 307 55 31 ILE HG2 H 0.34 . . 308 55 31 ILE C C 175.72 . . 309 55 31 ILE CA C 58.93 . . 310 55 31 ILE CB C 42.61 . . 311 55 31 ILE CD1 C 12.95 . . 312 55 31 ILE CG2 C 17.54 . . 313 55 31 ILE N N 127.47 . . 314 56 32 ASP H H 8.19 . . 315 56 32 ASP HA H 4.90 . . 316 56 32 ASP HB2 H 1.75 . . 317 56 32 ASP HB3 H 0.97 . . 318 56 32 ASP C C 174.50 . . 319 56 32 ASP CA C 54.35 . . 320 56 32 ASP CB C 42.61 . . 321 56 32 ASP N N 128.25 . . 322 57 33 ILE H H 8.94 . . 323 57 33 ILE HD1 H 0.94 . . 324 57 33 ILE HG2 H 0.74 . . 325 57 33 ILE CA C 63.63 . . 326 57 33 ILE CB C 38.78 . . 327 57 33 ILE CD1 C 14.75 . . 328 57 33 ILE CG2 C 19.26 . . 329 57 33 ILE N N 124.46 . . 330 58 34 ILE HA H 4.32 . . 331 58 34 ILE HB H 1.86 . . 332 58 34 ILE HD1 H 0.78 . . 333 58 34 ILE HG12 H 1.24 . . 334 58 34 ILE HG2 H 0.66 . . 335 58 34 ILE C C 175.23 . . 336 58 34 ILE CA C 63.49 . . 337 58 34 ILE CB C 40.50 . . 338 58 34 ILE CD1 C 13.98 . . 339 58 34 ILE CG2 C 16.56 . . 340 59 35 CYS H H 7.95 . . 341 59 35 CYS HA H 4.58 . . 342 59 35 CYS HB2 H 2.81 . . 343 59 35 CYS HB3 H 2.81 . . 344 59 35 CYS C C 171.66 . . 345 59 35 CYS CA C 57.01 . . 346 59 35 CYS CB C 30.25 . . 347 59 35 CYS N N 116.97 . . 348 60 36 LYS H H 8.42 . . 349 60 36 LYS HA H 3.35 . . 350 60 36 LYS HB2 H 0.89 . . 351 60 36 LYS HB3 H 0.71 . . 352 60 36 LYS HD2 H -0.68 . . 353 60 36 LYS HD3 H 0.40 . . 354 60 36 LYS HE2 H 2.19 . . 355 60 36 LYS HE3 H 2.19 . . 356 60 36 LYS HG2 H 1.06 . . 357 60 36 LYS HG3 H 1.01 . . 358 60 36 LYS C C 175.07 . . 359 60 36 LYS CA C 53.77 . . 360 60 36 LYS CB C 33.78 . . 361 60 36 LYS CD C 23.88 . . 362 60 36 LYS CE C 42.37 . . 363 60 36 LYS CG C 29.51 . . 364 60 36 LYS N N 126.08 . . 365 61 37 THR H H 6.98 . . 366 61 37 THR HG2 H 1.21 . . 367 61 37 THR CA C 59.24 . . 368 61 37 THR CB C 70.11 . . 369 61 37 THR N N 115.85 . . 370 63 39 MET H H 8.43 . . 371 63 39 MET HE H 2.09 . . 372 63 39 MET CE C 17.02 . . 373 63 39 MET N N 124.82 . . 374 64 40 GLY C C 172.83 . . 375 64 40 GLY CA C 45.05 . . 376 65 41 MET H H 7.70 . . 377 65 41 MET HA H 4.64 . . 378 65 41 MET HB2 H 2.32 . . 379 65 41 MET HB3 H 2.40 . . 380 65 41 MET HE H 2.31 . . 381 65 41 MET HG2 H 1.86 . . 382 65 41 MET HG3 H 1.86 . . 383 65 41 MET C C 175.28 . . 384 65 41 MET CA C 54.34 . . 385 65 41 MET CB C 33.08 . . 386 65 41 MET CE C 18.04 . . 387 65 41 MET N N 119.96 . . 388 66 42 TRP H H 8.64 . . 389 66 42 TRP HA H 5.07 . . 390 66 42 TRP HB2 H 2.80 . . 391 66 42 TRP HB3 H 1.78 . . 392 66 42 TRP HD1 H 7.02 . . 393 66 42 TRP HE1 H 9.87 . . 394 66 42 TRP HE3 H 7.46 . . 395 66 42 TRP HH2 H 7.15 . . 396 66 42 TRP HZ2 H 7.15 . . 397 66 42 TRP HZ3 H 6.88 . . 398 66 42 TRP C C 174.05 . . 399 66 42 TRP CA C 54.12 . . 400 66 42 TRP CB C 31.98 . . 401 66 42 TRP CD1 C 123.40 . . 402 66 42 TRP CE3 C 120.31 . . 403 66 42 TRP CH2 C 125.26 . . 404 66 42 TRP CZ2 C 115.43 . . 405 66 42 TRP CZ3 C 121.22 . . 406 66 42 TRP N N 129.04 . . 407 66 42 TRP NE1 N 127.72 . . 408 67 43 THR H H 8.67 . . 409 67 43 THR HA H 5.42 . . 410 67 43 THR HB H 3.88 . . 411 67 43 THR HG2 H 1.15 . . 412 67 43 THR C C 175.40 . . 413 67 43 THR CA C 60.77 . . 414 67 43 THR CB C 71.51 . . 415 67 43 THR CG2 C 22.30 . . 416 67 43 THR N N 115.48 . . 417 68 44 GLY H H 9.72 . . 418 68 44 GLY HA2 H 4.82 . . 419 68 44 GLY HA3 H 3.98 . . 420 68 44 GLY C C 167.89 . . 421 68 44 GLY CA C 45.84 . . 422 68 44 GLY N N 115.06 . . 423 69 45 MET H H 9.39 . . 424 69 45 MET HA H 5.63 . . 425 69 45 MET HE H 1.94 . . 426 69 45 MET C C 173.78 . . 427 69 45 MET CA C 53.60 . . 428 69 45 MET CB C 37.85 . . 429 69 45 MET CE C 17.07 . . 430 69 45 MET CG C 32.37 . . 431 69 45 MET N N 121.04 . . 432 70 46 LEU H H 9.12 . . 433 70 46 LEU HA H 4.75 . . 434 70 46 LEU HB2 H 1.73 . . 435 70 46 LEU HB3 H 1.73 . . 436 70 46 LEU HD1 H 0.85 . . 437 70 46 LEU C C 175.69 . . 438 70 46 LEU CA C 53.60 . . 439 70 46 LEU CB C 47.08 . . 440 70 46 LEU CD1 C 27.37 . . 441 70 46 LEU N N 130.33 . . 442 71 47 ASN H H 9.85 . . 443 71 47 ASN HA H 4.41 . . 444 71 47 ASN HB2 H 2.97 . . 445 71 47 ASN HB3 H 2.74 . . 446 71 47 ASN HD21 H 7.66 . . 447 71 47 ASN HD22 H 7.13 . . 448 71 47 ASN C C 174.26 . . 449 71 47 ASN CA C 54.25 . . 450 71 47 ASN CB C 37.78 . . 451 71 47 ASN N N 130.25 . . 452 71 47 ASN ND2 N 114.01 . . 453 72 48 ASN H H 9.02 . . 454 72 48 ASN HA H 4.47 . . 455 72 48 ASN HB2 H 3.06 . . 456 72 48 ASN HB3 H 3.06 . . 457 72 48 ASN HD21 H 7.49 . . 458 72 48 ASN HD22 H 6.88 . . 459 72 48 ASN C C 173.16 . . 460 72 48 ASN CA C 54.81 . . 461 72 48 ASN CB C 38.22 . . 462 72 48 ASN N N 110.38 . . 463 72 48 ASN ND2 N 112.35 . . 464 73 49 LYS H H 7.88 . . 465 73 49 LYS HA H 4.75 . . 466 73 49 LYS HB2 H 1.86 . . 467 73 49 LYS HB3 H 1.76 . . 468 73 49 LYS HD2 H 1.43 . . 469 73 49 LYS HE2 H 3.07 . . 470 73 49 LYS HE3 H 3.07 . . 471 73 49 LYS C C 174.14 . . 472 73 49 LYS CA C 54.58 . . 473 73 49 LYS CB C 35.48 . . 474 73 49 LYS CD C 24.37 . . 475 73 49 LYS CE C 42.37 . . 476 73 49 LYS CG C 28.37 . . 477 73 49 LYS N N 122.04 . . 478 74 50 VAL H H 8.58 . . 479 74 50 VAL HA H 5.03 . . 480 74 50 VAL HB H 1.87 . . 481 74 50 VAL HG1 H 0.84 . . 482 74 50 VAL HG2 H 0.70 . . 483 74 50 VAL C C 176.46 . . 484 74 50 VAL CA C 60.35 . . 485 74 50 VAL CB C 33.49 . . 486 74 50 VAL CG1 C 22.09 . . 487 74 50 VAL CG2 C 21.34 . . 488 74 50 VAL N N 124.95 . . 489 75 51 GLY H H 9.03 . . 490 75 51 GLY HA2 H 4.44 . . 491 75 51 GLY HA3 H 4.03 . . 492 75 51 GLY C C 171.21 . . 493 75 51 GLY CA C 45.42 . . 494 75 51 GLY N N 114.12 . . 495 76 52 ASN H H 8.93 . . 496 76 52 ASN HA H 6.21 . . 497 76 52 ASN HB2 H 2.84 . . 498 76 52 ASN HB3 H 2.78 . . 499 76 52 ASN HD21 H 7.53 . . 500 76 52 ASN HD22 H 6.96 . . 501 76 52 ASN C C 176.39 . . 502 76 52 ASN CA C 51.58 . . 503 76 52 ASN CB C 41.36 . . 504 76 52 ASN N N 117.63 . . 505 76 52 ASN ND2 N 112.17 . . 506 77 53 PHE H H 9.17 . . 507 77 53 PHE HA H 4.82 . . 508 77 53 PHE HB2 H 3.11 . . 509 77 53 PHE HB3 H 2.73 . . 510 77 53 PHE HD1 H 6.90 . . 511 77 53 PHE HE1 H 7.29 . . 512 77 53 PHE CA C 55.96 . . 513 77 53 PHE CB C 41.24 . . 514 77 53 PHE CD1 C 132.85 . . 515 77 53 PHE CE1 C 131.43 . . 516 77 53 PHE N N 118.86 . . 517 78 54 LYS H H 8.60 . . 518 78 54 LYS HA H 4.58 . . 519 78 54 LYS HB2 H 1.28 . . 520 78 54 LYS HB3 H 1.38 . . 521 78 54 LYS HD2 H 1.09 . . 522 78 54 LYS HD3 H 1.09 . . 523 78 54 LYS HE2 H 2.76 . . 524 78 54 LYS HE3 H 2.76 . . 525 78 54 LYS HG2 H 1.33 . . 526 78 54 LYS HG3 H 1.29 . . 527 78 54 LYS C C 177.41 . . 528 78 54 LYS CA C 55.07 . . 529 78 54 LYS CB C 34.51 . . 530 78 54 LYS CD C 26.37 . . 531 78 54 LYS CE C 42.37 . . 532 78 54 LYS CG C 29.37 . . 533 78 54 LYS N N 121.51 . . 534 79 55 PHE H H 7.63 . . 535 79 55 PHE HA H 3.59 . . 536 79 55 PHE HB2 H 1.83 . . 537 79 55 PHE HB3 H 1.13 . . 538 79 55 PHE HD1 H 6.67 . . 539 79 55 PHE HE1 H 7.22 . . 540 79 55 PHE C C 175.75 . . 541 79 55 PHE CA C 58.44 . . 542 79 55 PHE CB C 36.87 . . 543 79 55 PHE CD1 C 132.07 . . 544 79 55 PHE CE1 C 131.40 . . 545 79 55 PHE N N 122.61 . . 546 80 56 ILE H H 6.15 . . 547 80 56 ILE HA H 3.88 . . 548 80 56 ILE HB H 1.62 . . 549 80 56 ILE HD1 H 0.48 . . 550 80 56 ILE HG12 H 0.18 . . 551 80 56 ILE HG13 H 0.35 . . 552 80 56 ILE HG2 H 0.40 . . 553 80 56 ILE C C 175.43 . . 554 80 56 ILE CA C 62.18 . . 555 80 56 ILE CB C 38.14 . . 556 80 56 ILE CD1 C 13.91 . . 557 80 56 ILE CG1 C 25.92 . . 558 80 56 ILE CG2 C 17.71 . . 559 80 56 ILE N N 112.26 . . 560 81 57 TYR H H 6.89 . . 561 81 57 TYR HA H 4.46 . . 562 81 57 TYR HB2 H 3.65 . . 563 81 57 TYR HB3 H 2.47 . . 564 81 57 TYR HD1 H 6.93 . . 565 81 57 TYR HE1 H 6.43 . . 566 81 57 TYR C C 174.12 . . 567 81 57 TYR CA C 56.48 . . 568 81 57 TYR CB C 39.71 . . 569 81 57 TYR CD1 C 132.73 . . 570 81 57 TYR CE1 C 118.05 . . 571 81 57 TYR N N 118.25 . . 572 82 58 VAL H H 7.36 . . 573 82 58 VAL HA H 5.00 . . 574 82 58 VAL HB H 1.80 . . 575 82 58 VAL HG1 H 0.58 . . 576 82 58 VAL HG2 H 0.79 . . 577 82 58 VAL C C 173.17 . . 578 82 58 VAL CA C 57.50 . . 579 82 58 VAL CB C 35.45 . . 580 82 58 VAL CG1 C 21.03 . . 581 82 58 VAL CG2 C 18.70 . . 582 82 58 VAL N N 109.70 . . 583 83 59 ASP H H 8.66 . . 584 83 59 ASP HA H 5.27 . . 585 83 59 ASP HB2 H 2.53 . . 586 83 59 ASP HB3 H 2.66 . . 587 83 59 ASP C C 175.65 . . 588 83 59 ASP CA C 52.96 . . 589 83 59 ASP CB C 44.36 . . 590 83 59 ASP N N 117.99 . . 591 84 60 VAL H H 9.33 . . 592 84 60 VAL HA H 4.22 . . 593 84 60 VAL HB H 2.19 . . 594 84 60 VAL HG1 H 1.30 . . 595 84 60 VAL HG2 H 1.10 . . 596 84 60 VAL C C 176.46 . . 597 84 60 VAL CA C 64.21 . . 598 84 60 VAL CB C 32.17 . . 599 84 60 VAL CG1 C 22.37 . . 600 84 60 VAL CG2 C 21.68 . . 601 84 60 VAL N N 125.80 . . 602 85 61 ILE H H 8.74 . . 603 85 61 ILE HA H 4.51 . . 604 85 61 ILE HB H 1.92 . . 605 85 61 ILE HD1 H 0.86 . . 606 85 61 ILE HG12 H 1.41 . . 607 85 61 ILE HG13 H 1.41 . . 608 85 61 ILE HG2 H 0.92 . . 609 85 61 ILE C C 175.53 . . 610 85 61 ILE CA C 61.04 . . 611 85 61 ILE CB C 39.76 . . 612 85 61 ILE CD1 C 13.26 . . 613 85 61 ILE CG2 C 17.82 . . 614 85 61 ILE N N 126.34 . . 615 86 62 SER H H 8.33 . . 616 86 62 SER HA H 4.64 . . 617 86 62 SER HB2 H 3.86 . . 618 86 62 SER HB3 H 3.94 . . 619 86 62 SER C C 172.81 . . 620 86 62 SER CA C 57.90 . . 621 86 62 SER CB C 64.62 . . 622 86 62 SER N N 120.37 . . 623 87 63 GLU H H 8.12 . . 624 87 63 GLU HA H 4.28 . . 625 87 63 GLU HB2 H 1.88 . . 626 87 63 GLU HB3 H 2.10 . . 627 87 63 GLU CA C 57.47 . . 628 87 63 GLU CB C 31.72 . . 629 87 63 GLU N N 128.60 . . stop_ save_