data_15965 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Transitions of the N Terminus of a Short Non-Muscle Tropomyosin upon Binding to the C Terminus in Solution ; _BMRB_accession_number 15965 _BMRB_flat_file_name bmr15965.str _Entry_type new _Submission_date 2008-09-25 _Accession_date 2008-09-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The conformational changes in the N-terminal domain of tropomyosin upon binding to the C-terminal domain to form an "overlap" complex.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Kotylanskaya Lucy . . 3 Hitchcock-DeGregori Sarah E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 231 "13C chemical shifts" 123 "15N chemical shifts" 41 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-18 update BMRB 'complete entry citation' 2009-04-02 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4995 'Solution NMR Structure and Folding Dynamics of TM1bZip' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the N Terminus of a Nonmuscle alpha-Tropomyosin in Complex with the C Terminus: Implications for Actin Binding' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19170537 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Kotlyanskaya Lucy . . 3 Hitchcock-DeGregori Sarah E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 48 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1272 _Page_last 1283 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TM1b(1-19)Zip/TM9d252-284 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_2 $TM9d(252-284) entity_1 $TM1b(1-19)Zip stop_ _System_molecular_weight 17020 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'intermolecular junction between low molecular weight non-muscle tropomyosin molecules' stop_ _Database_query_date . _Details ; The structure is of a model peptide (TM1b(1-19)Zip) of the N terminus of non-muscle,low molecular weight rat alpha tropomyosin in complex with a model peptide of the C terminus of non-muscle/smooth muscle tropomyosins, Tm9d(252-284). TM1b(1-19)Zip is residues 1-19 encoded by exon 1b of the TPM1 gene followed by the last 18 residues of the yeast transcription factor, GCN4. Gly replaces the native N-terminal acetyl group. The C-terminal model contains residues 252-284 encoded by exon 8 and exon 9d with Gly-Cys-Gly-Gly at the N terminus to allow oxidatitive cross-linking. The TM1b(1-19)Zip is labeled with either 15N or 15N and 13C. TM9d(252-284) is unlabeled. ; save_ ######################## # Monomeric polymers # ######################## save_TM1b(1-19)Zip _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TM1b(1-19)Zip _Molecular_mass 4331.956 _Mol_thiol_state 'not present' loop_ _Biological_function 'binds tropomodulin' 'forms intermolecular junction with the C terminus of neighboring tropomyosin molecule' 'regulates actin filament dynamics' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 38 _Mol_residue_sequence ; GAGSSSLEAVRRKIRSLQEQ NYHLENEVARLKKLVGER ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 GLY 4 SER 5 SER 6 SER 7 LEU 8 GLU 9 ALA 10 VAL 11 ARG 12 ARG 13 LYS 14 ILE 15 ARG 16 SER 17 LEU 18 GLN 19 GLU 20 GLN 21 ASN 22 TYR 23 HIS 24 LEU 25 GLU 26 ASN 27 GLU 28 VAL 29 ALA 30 ARG 31 LEU 32 LYS 33 LYS 34 LEU 35 VAL 36 GLY 37 GLU 38 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-05 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 1IHQ "Glytm1bzip: A Chimeric Peptide Model Of The N-Terminus Of A Rat Short Alpha Tropomyosin With The N-Terminus Encoded By Exon 1b" 97.37 38 100.00 100.00 2.37e-15 PDB 2K8X "Glytm1b(1-19)zip: A Chimeric Peptide Model Of The N-Terminus Of A Rat Short Alpha-Tropomyosin With The N-Terminus Encoded By Ex" 100.00 38 100.00 100.00 3.10e-16 PDB 3AZD "Crystal Structure Of Tropomyosin N-Terminal Fragment At 0.98a Resolution" 97.37 37 100.00 100.00 2.34e-15 DBJ BAD92278 "TPM1 protein variant [Homo sapiens]" 50.00 303 100.00 100.00 2.31e-01 DBJ BAG11063 "tropomyosin alpha-1 chain [synthetic construct]" 50.00 245 100.00 100.00 1.26e-01 DBJ BAH12832 "unnamed protein product [Homo sapiens]" 50.00 275 100.00 100.00 1.93e-01 DBJ BAH13458 "unnamed protein product [Homo sapiens]" 50.00 248 100.00 100.00 1.18e-01 GB AAA18098 "alpha-tropomyosin 5a [Rattus norvegicus]" 50.00 248 100.00 100.00 1.13e-01 GB AAA18099 "alpha-tropomyosin 5b [Rattus norvegicus]" 50.00 248 100.00 100.00 1.07e-01 GB AAA42253 "brain alpha-tropomyosin (TMBr-2) [Rattus norvegicus]" 50.00 251 100.00 100.00 1.48e-01 GB AAH50473 "TPM1 protein, partial [Homo sapiens]" 50.00 287 100.00 100.00 2.23e-01 GB AAH53545 "Tropomyosin 1 (alpha) [Homo sapiens]" 50.00 245 100.00 100.00 1.21e-01 REF NP_001018008 "tropomyosin alpha-1 chain isoform Tpm1.12br [Homo sapiens]" 50.00 245 100.00 100.00 1.21e-01 REF NP_001029245 "tropomyosin alpha-1 chain isoform Tpm1.8cy [Rattus norvegicus]" 50.00 248 100.00 100.00 1.13e-01 REF NP_001029246 "tropomyosin alpha-1 chain isoform Tpm1.9cy [Rattus norvegicus]" 50.00 248 100.00 100.00 1.07e-01 REF NP_001029247 "tropomyosin alpha-1 chain isoform Tpm1.13 [Rattus norvegicus]" 50.00 248 100.00 100.00 1.15e-01 REF NP_001157724 "tropomyosin alpha-1 chain isoform Tpm1.8cy [Mus musculus]" 50.00 248 100.00 100.00 1.13e-01 stop_ save_ save_TM9d(252-284) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TM9d(252-284) _Molecular_mass 4115.06 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'actin binding site, part of intramolecule junction between tropomyosin molecules' stop_ _Details 'There is no NMR structural information on this molecule. It is unlabeled and is not in the PDB file.' _Residue_count 37 _Mol_residue_sequence ; GCGGSIDDLEEKVAHAKEEN LSMHQMLDQTLLELNNM ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 CYS 3 GLY 4 GLY 5 SER 6 ILE 7 ASP 8 ASP 9 LEU 10 GLU 11 GLU 12 LYS 13 VAL 14 ALA 15 HIS 16 ALA 17 LYS 18 GLU 19 GLU 20 ASN 21 LEU 22 SER 23 MET 24 HIS 25 GLN 26 MET 27 LEU 28 ASP 29 GLN 30 THR 31 LEU 32 LEU 33 GLU 34 LEU 35 ASN 36 ASN 37 MET 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 3MUD "Structure Of The Tropomyosin Overlap Complex From Chicken Smooth Muscle" 89.19 175 96.97 100.00 9.42e-12 DBJ BAB22620 "unnamed protein product [Mus musculus]" 91.89 284 97.06 97.06 6.97e-13 DBJ BAD18535 "unnamed protein product [Homo sapiens]" 91.89 326 97.06 97.06 1.12e-12 DBJ BAE88136 "unnamed protein product [Macaca fascicularis]" 91.89 284 97.06 97.06 7.88e-13 DBJ BAH13458 "unnamed protein product [Homo sapiens]" 89.19 248 100.00 100.00 5.07e-13 EMBL CAA03930 "alpha-tropomyosin [Homo sapiens]" 89.19 48 100.00 100.00 4.63e-13 EMBL CAA04505 "alpha-tropomyosin [Homo sapiens]" 89.19 48 100.00 100.00 4.63e-13 EMBL CAA26258 "unnamed protein product [Rattus norvegicus]" 89.19 280 96.97 96.97 2.10e-11 EMBL CAA30930 "tropomyosin (227 AA) [Homo sapiens]" 91.89 227 97.06 97.06 6.53e-13 EMBL CAB43309 "hypothetical protein [Homo sapiens]" 91.89 284 97.06 97.06 7.72e-13 GB AAA18097 "alpha-tropomyosin 3 [Rattus norvegicus]" 91.89 284 97.06 97.06 5.61e-13 GB AAA18098 "alpha-tropomyosin 5a [Rattus norvegicus]" 89.19 248 100.00 100.00 4.68e-13 GB AAA18099 "alpha-tropomyosin 5b [Rattus norvegicus]" 89.19 248 100.00 100.00 3.99e-13 GB AAA36771 "tropomyosin [Homo sapiens]" 91.89 284 97.06 97.06 5.61e-13 GB AAA40483 "tropomyosin isoform 2 [Mus musculus]" 91.89 284 97.06 97.06 6.97e-13 PIR A22165 "tropomyosin alpha chain, smooth muscle - rat" 89.19 280 96.97 96.97 2.10e-11 PRF 1105305A "tropomyosin alpha" 89.19 280 96.97 96.97 2.10e-11 REF NP_001018004 "tropomyosin alpha-1 chain isoform Tpm1.6cy [Homo sapiens]" 91.89 284 97.06 97.06 6.75e-13 REF NP_001018006 "tropomyosin alpha-1 chain isoform Tpm1.7cy [Homo sapiens]" 91.89 284 97.06 97.06 5.61e-13 REF NP_001018007 "tropomyosin alpha-1 chain isoform Tpm1.4sm [Homo sapiens]" 91.89 284 97.06 97.06 7.72e-13 REF NP_001018020 "tropomyosin alpha-1 chain isoform Tpm1.3sm [Homo sapiens]" 91.89 284 97.06 97.06 6.09e-13 REF NP_001029241 "tropomyosin alpha-1 chain isoform Tpm1.6cy [Rattus norvegicus]" 91.89 284 97.06 97.06 6.97e-13 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name entity_2 2 CYS HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $TM1b(1-19)Zip Rat 10116 Eukaryota Metazoa Rattus norvegicus TPM1 'Residues 1-19 are the first 19 of encoded by exon 1b.' $TM9d(252-284) Rat 10116 Eukaryota Metazoa Rattus norvegicus TPM1 'Residues 252-284 are encoded by part of exon 8 and all of exon 9d' 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 $TM1b(1-19)Zip 'recombinant technology' . . . DH5alpha 'pPROEX HTa' $TM9d(252-284) 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 13C, 15N TM1b(1-19)Zip + umlabled TM9d(252-284) 100 mM NaCl, 10 mM sodium phosphate, pH 6.4 ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1b(1-19)Zip 1 mM '[U-99% 13C; U-99% 15N]' $TM9d(252-284) 1 mM 'natural abundance' NaCl 100 mM 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; 15N TM1b(1-19)Zip + umlabeled TM9d(252-284) 100 mM NaCl, 10 mM sodium phosphate, pH 6.4 ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1b(1-19)Zip 1 mM [U-15N] $TM9d(252-284) 1 mM 'natural abundance' NaCl 100 mM 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details ; heterodimer of 13C, 15N TM1b(1-19)Zip + unlabeled TM1b(1-19)Zip and unlabeled TM9d(252-284) 100 mM NaCl, 10 mM sodium phosphate, pH 6.4 ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1b(1-19)Zip 0.5 mM '[U-99% 13C; U-99% 15N]' $TM1b(1-19)Zip 0.5 mM 'natural abundance' $TM9d(252-284) 1 mM 'natural abundance' NaCl 100 mM 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AutoStructure _Saveframe_category software _Name AutoStructure _Version 1.12 loop_ _Vendor _Address _Electronic_address 'Huang, Tejero, Powers and Montelione' 'CABM, Rutgers University, Piscataway, NJ' guy@cabm.rutgers.edu stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.111 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Biospin _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 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_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_13C_15N_X-filtered_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C 15N X-filtered NOESY' _Sample_label $sample_1 save_ save_13C_15N_X-filtered_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '13C 15N X-filtered NOESY' _Sample_label $sample_3 save_ save_2D_1H-13C_HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HCCH-COSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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 temperature 293 0.1 K pH 6.4 . pH pressure 1 . atm 'ionic strength' 0.14 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct cylindrical other . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 n/a indirect cylindrical 'insert at center of experimental sample tube' . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 n/a indirect cylindrical other . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $AutoStructure $CNS $SPARKY $NMRPipe $NMRDraw stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HBHA(CO)NH' '3D HN(CO)CA' '3D HCCH-COSY' 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 entity_1 _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 1 GLY HA2 H 3.855 0.05 1 2 1 1 GLY HA3 H 3.855 0.05 1 3 1 1 GLY CA C 43.523 0.5 1 4 2 2 ALA H H 8.725 0.05 1 5 2 2 ALA HA H 4.373 0.05 1 6 2 2 ALA HB H 1.402 0.05 1 7 2 2 ALA CA C 52.891 0.5 1 8 2 2 ALA CB C 19.489 0.5 1 9 2 2 ALA N N 124.084 0.5 1 10 3 3 GLY H H 8.647 0.05 1 11 3 3 GLY HA2 H 3.996 0.05 2 12 3 3 GLY HA3 H 3.996 0.05 2 13 3 3 GLY CA C 45.438 0.5 1 14 3 3 GLY N N 108.827 0.5 1 15 4 4 SER H H 8.311 0.05 1 16 4 4 SER HA H 4.493 0.05 1 17 4 4 SER HB2 H 3.902 0.05 2 18 4 4 SER HB3 H 3.976 0.05 2 19 4 4 SER CA C 58.607 0.5 1 20 4 4 SER CB C 63.715 0.5 1 21 4 4 SER N N 115.868 0.5 1 22 5 5 SER H H 8.62 0.05 1 23 5 5 SER HA H 4.469 0.05 1 24 5 5 SER HB2 H 4.022 0.05 2 25 5 5 SER HB3 H 3.939 0.05 2 26 5 5 SER CA C 59.103 0.5 1 27 5 5 SER CB C 63.474 0.5 1 28 5 5 SER N N 118.963 0.5 1 29 6 6 SER H H 8.49 0.05 1 30 6 6 SER HA H 4.388 0.05 1 31 6 6 SER HB2 H 3.905 0.05 2 32 6 6 SER HB3 H 3.936 0.05 2 33 6 6 SER CA C 59.989 0.5 1 34 6 6 SER CB C 63.455 0.5 1 35 6 6 SER N N 119.176 0.5 1 36 7 7 LEU H H 8.281 0.05 1 37 7 7 LEU HA H 4.129 0.05 1 38 7 7 LEU HB2 H 1.737 0.05 2 39 7 7 LEU HB3 H 1.62 0.05 2 40 7 7 LEU HD1 H 0.903 0.05 2 41 7 7 LEU HD2 H 0.91 0.05 2 42 7 7 LEU HG H 1.59 0.05 1 43 7 7 LEU CA C 57.627 0.5 1 44 7 7 LEU CB C 41.789 0.5 1 45 7 7 LEU CD1 C 24.455 0.5 2 46 7 7 LEU CD2 C 24.475 0.5 2 47 7 7 LEU CG C 27.404 0.5 1 48 7 7 LEU N N 123.537 0.5 1 49 8 8 GLU H H 8.192 0.05 1 50 8 8 GLU HA H 4.028 0.05 1 51 8 8 GLU HB2 H 2.036 0.05 2 52 8 8 GLU HB3 H 2.08 0.05 2 53 8 8 GLU HG2 H 2.332 0.05 2 54 8 8 GLU HG3 H 2.332 0.05 2 55 8 8 GLU CA C 59.357 0.5 1 56 8 8 GLU CB C 29.135 0.5 1 57 8 8 GLU CG C 35.981 0.5 1 58 8 8 GLU N N 118.872 0.5 1 59 9 9 ALA H H 7.973 0.05 1 60 9 9 ALA HA H 4.09 0.05 1 61 9 9 ALA HB H 1.515 0.05 1 62 9 9 ALA CA C 55.445 0.5 1 63 9 9 ALA CB C 18.235 0.5 1 64 9 9 ALA N N 121.399 0.5 1 65 10 10 VAL H H 7.889 0.05 1 66 10 10 VAL HA H 3.731 0.05 1 67 10 10 VAL HB H 2.186 0.05 1 68 10 10 VAL HG1 H 1.065 0.05 2 69 10 10 VAL HG2 H 0.932 0.05 2 70 10 10 VAL CA C 66.289 0.5 1 71 10 10 VAL CB C 31.617 0.5 1 72 10 10 VAL CG1 C 23.519 0.5 2 73 10 10 VAL CG2 C 22.681 0.5 2 74 10 10 VAL N N 119.522 0.5 1 75 11 11 ARG H H 8.299 0.05 1 76 11 11 ARG HA H 3.844 0.05 1 77 11 11 ARG HB2 H 1.925 0.05 2 78 11 11 ARG HB3 H 1.893 0.05 2 79 11 11 ARG HD2 H 3.18 0.05 2 80 11 11 ARG HD3 H 3.18 0.05 2 81 11 11 ARG HG2 H 1.837 0.05 2 82 11 11 ARG HG3 H 1.565 0.05 2 83 11 11 ARG CA C 60.565 0.5 1 84 11 11 ARG CB C 30.302 0.5 1 85 11 11 ARG CD C 43.672 0.5 1 86 11 11 ARG CG C 28.18 0.5 1 87 11 11 ARG N N 120.475 0.5 1 88 12 12 ARG H H 8.183 0.05 1 89 12 12 ARG HA H 3.998 0.05 1 90 12 12 ARG HB2 H 1.943 0.05 2 91 12 12 ARG HB3 H 1.943 0.05 2 92 12 12 ARG HD2 H 3.222 0.05 2 93 12 12 ARG HD3 H 3.222 0.05 2 94 12 12 ARG HG2 H 1.634 0.05 2 95 12 12 ARG HG3 H 1.855 0.05 2 96 12 12 ARG CA C 59.526 0.5 1 97 12 12 ARG CB C 30.264 0.5 1 98 12 12 ARG CD C 43.617 0.5 1 99 12 12 ARG CG C 27.938 0.5 1 100 12 12 ARG N N 118.44 0.5 1 101 13 13 LYS H H 7.972 0.05 1 102 13 13 LYS HA H 4.147 0.05 1 103 13 13 LYS HB2 H 2.054 0.05 2 104 13 13 LYS HB3 H 2.105 0.05 2 105 13 13 LYS HD2 H 1.709 0.05 2 106 13 13 LYS HD3 H 1.526 0.05 2 107 13 13 LYS HE2 H 3.029 0.05 2 108 13 13 LYS HE3 H 3.254 0.05 2 109 13 13 LYS HG2 H 1.599 0.05 2 110 13 13 LYS HG3 H 1.37 0.05 2 111 13 13 LYS CA C 59.104 0.5 1 112 13 13 LYS CB C 32.697 0.5 1 113 13 13 LYS CD C 29.456 0.5 1 114 13 13 LYS CE C 41.458 0.5 1 115 13 13 LYS CG C 24.821 0.5 1 116 13 13 LYS N N 122.454 0.5 1 117 14 14 ILE H H 8.291 0.05 1 118 14 14 ILE HA H 3.526 0.05 1 119 14 14 ILE HB H 1.911 0.05 1 120 14 14 ILE HD1 H 0.869 0.05 1 121 14 14 ILE HG12 H 1.821 0.05 2 122 14 14 ILE HG13 H 1.87 0.05 2 123 14 14 ILE HG2 H 0.842 0.05 1 124 14 14 ILE CA C 66.269 0.5 1 125 14 14 ILE CB C 37.845 0.5 1 126 14 14 ILE CD1 C 14.607 0.5 1 127 14 14 ILE CG1 C 30.606 0.5 1 128 14 14 ILE CG2 C 16.977 0.5 1 129 14 14 ILE N N 119.298 0.5 1 130 15 15 ARG H H 8.047 0.05 1 131 15 15 ARG HA H 4.25 0.05 1 132 15 15 ARG HB2 H 1.929 0.05 2 133 15 15 ARG HB3 H 1.907 0.05 2 134 15 15 ARG HD2 H 3.248 0.05 2 135 15 15 ARG HD3 H 3.248 0.05 2 136 15 15 ARG HG2 H 1.764 0.05 2 137 15 15 ARG HG3 H 1.674 0.05 2 138 15 15 ARG CA C 59.244 0.5 1 139 15 15 ARG CB C 29.793 0.5 1 140 15 15 ARG CD C 43.429 0.5 1 141 15 15 ARG CG C 27.441 0.5 1 142 15 15 ARG N N 120.923 0.5 1 143 16 16 SER H H 8.374 0.05 1 144 16 16 SER HA H 4.344 0.05 1 145 16 16 SER HB2 H 4.056 0.05 2 146 16 16 SER HB3 H 4.044 0.05 2 147 16 16 SER CA C 61.861 0.5 1 148 16 16 SER CB C 62.882 0.5 1 149 16 16 SER N N 114.52 0.5 1 150 17 17 LEU H H 8.135 0.05 1 151 17 17 LEU HA H 4.096 0.05 1 152 17 17 LEU HB2 H 1.33 0.05 2 153 17 17 LEU HB3 H 2.142 0.05 2 154 17 17 LEU HD1 H 0.93 0.05 2 155 17 17 LEU HD2 H 0.891 0.05 2 156 17 17 LEU HG H 1.891 0.05 1 157 17 17 LEU CA C 58.197 0.5 1 158 17 17 LEU CB C 43.647 0.5 1 159 17 17 LEU CD1 C 27.092 0.5 2 160 17 17 LEU CD2 C 23.750 0.5 2 161 17 17 LEU CG C 27.492 0.5 1 162 17 17 LEU N N 122.938 0.5 1 163 18 18 GLN H H 8.649 0.05 1 164 18 18 GLN HA H 3.965 0.05 1 165 18 18 GLN HB2 H 2.008 0.05 2 166 18 18 GLN HB3 H 2.407 0.05 2 167 18 18 GLN HE21 H 6.877 0.05 2 168 18 18 GLN HE22 H 7.142 0.05 2 169 18 18 GLN HG2 H 2.335 0.05 2 170 18 18 GLN HG3 H 2.612 0.05 2 171 18 18 GLN CA C 59.45 0.5 1 172 18 18 GLN CB C 28.71 0.5 1 173 18 18 GLN CG C 35.129 0.5 1 174 18 18 GLN N N 119.456 0.5 1 175 18 18 GLN NE2 N 110.982 0.5 1 176 19 19 GLU H H 8.5 0.05 1 177 19 19 GLU HA H 4.12 0.05 1 178 19 19 GLU HB2 H 2.173 0.05 2 179 19 19 GLU HB3 H 2.231 0.05 2 180 19 19 GLU HG2 H 2.514 0.05 2 181 19 19 GLU HG3 H 2.31 0.05 2 182 19 19 GLU CA C 59.647 0.5 1 183 19 19 GLU CB C 29.625 0.5 1 184 19 19 GLU CG C 36.67 0.5 1 185 19 19 GLU N N 120.612 0.5 1 186 20 20 GLN H H 8.424 0.05 1 187 20 20 GLN HA H 4.285 0.05 1 188 20 20 GLN HB2 H 2.095 0.05 2 189 20 20 GLN HB3 H 2.217 0.05 2 190 20 20 GLN HE21 H 6.864 0.05 2 191 20 20 GLN HE22 H 7.394 0.05 2 192 20 20 GLN HG2 H 2.458 0.05 2 193 20 20 GLN HG3 H 2.605 0.05 2 194 20 20 GLN CA C 58.982 0.5 1 195 20 20 GLN CB C 28.787 0.5 1 196 20 20 GLN CG C 33.921 0.5 1 197 20 20 GLN N N 120.205 0.5 1 198 20 20 GLN NE2 N 111.019 0.5 1 199 21 21 ASN H H 8.563 0.05 1 200 21 21 ASN HA H 4.383 0.05 1 201 21 21 ASN HB2 H 3.205 0.05 1 202 21 21 ASN HB3 H 2.751 0.05 1 203 21 21 ASN HD21 H 6.807 0.05 1 204 21 21 ASN HD22 H 7.552 0.05 1 205 21 21 ASN CA C 57.475 0.5 1 206 21 21 ASN CB C 38.667 0.5 1 207 21 21 ASN N N 120.117 0.5 1 208 21 21 ASN ND2 N 106.392 0.5 1 209 22 22 TYR H H 8.115 0.05 1 210 22 22 TYR HA H 4.394 0.05 1 211 22 22 TYR HB2 H 3.2 0.05 2 212 22 22 TYR HB3 H 3.229 0.05 2 213 22 22 TYR HD1 H 7.04 0.05 3 214 22 22 TYR HD2 H 7.04 0.05 3 215 22 22 TYR HE1 H 6.795 0.05 3 216 22 22 TYR HE2 H 6.795 0.05 3 217 22 22 TYR CA C 60.646 0.5 1 218 22 22 TYR CB C 37.993 0.5 1 219 22 22 TYR N N 120.082 0.5 1 220 23 23 HIS H H 8.025 0.05 1 221 23 23 HIS HA H 4.402 0.05 1 222 23 23 HIS HB2 H 3.356 0.05 2 223 23 23 HIS HB3 H 3.356 0.05 2 224 23 23 HIS HD2 H 7.168 0.05 1 225 23 23 HIS CA C 59.328 0.5 1 226 23 23 HIS CB C 29.518 0.5 1 227 23 23 HIS N N 118.108 0.5 1 228 24 24 LEU H H 8.751 0.05 1 229 24 24 LEU HA H 3.928 0.05 1 230 24 24 LEU HB2 H 2.119 0.05 2 231 24 24 LEU HB3 H 1.318 0.05 2 232 24 24 LEU HD1 H 1.014 0.05 2 233 24 24 LEU HD2 H 0.88 0.05 2 234 24 24 LEU HG H 1.963 0.05 1 235 24 24 LEU CA C 58.226 0.5 1 236 24 24 LEU CB C 43.778 0.5 1 237 24 24 LEU CD1 C 26.836 0.5 2 238 24 24 LEU CD2 C 23.343 0.5 2 239 24 24 LEU CG C 27.349 0.5 1 240 24 24 LEU N N 120.548 0.5 1 241 25 25 GLU H H 8.83 0.05 1 242 25 25 GLU HA H 3.926 0.05 1 243 25 25 GLU HB2 H 1.989 0.05 2 244 25 25 GLU HB3 H 2.179 0.05 2 245 25 25 GLU HG2 H 2.471 0.05 2 246 25 25 GLU HG3 H 2.259 0.05 2 247 25 25 GLU CA C 60.114 0.5 1 248 25 25 GLU CB C 29.339 0.5 1 249 25 25 GLU CG C 36.82 0.5 1 250 25 25 GLU N N 119.875 0.5 1 251 26 26 ASN H H 7.774 0.05 1 252 26 26 ASN HA H 4.435 0.05 1 253 26 26 ASN HB2 H 2.746 0.05 2 254 26 26 ASN HB3 H 2.906 0.05 2 255 26 26 ASN HD21 H 5.863 0.05 2 256 26 26 ASN HD22 H 7.429 0.05 2 257 26 26 ASN CA C 56.238 0.5 1 258 26 26 ASN CB C 37.945 0.5 1 259 26 26 ASN N N 119.022 0.5 1 260 26 26 ASN ND2 N 111.714 0.5 1 261 27 27 GLU H H 8.179 0.05 1 262 27 27 GLU HA H 4.436 0.05 1 263 27 27 GLU HB2 H 1.965 0.05 2 264 27 27 GLU HB3 H 2.155 0.05 2 265 27 27 GLU HG2 H 2.332 0.05 2 266 27 27 GLU HG3 H 2.081 0.05 2 267 27 27 GLU CA C 58.674 0.5 1 268 27 27 GLU CB C 30.279 0.5 1 269 27 27 GLU CG C 35.939 0.5 1 270 27 27 GLU N N 124.075 0.5 1 271 28 28 VAL H H 8.731 0.05 1 272 28 28 VAL HA H 3.385 0.05 1 273 28 28 VAL HB H 2.125 0.05 1 274 28 28 VAL HG1 H 0.881 0.05 2 275 28 28 VAL HG2 H 1.027 0.05 2 276 28 28 VAL CA C 67.756 0.5 1 277 28 28 VAL CB C 31.732 0.5 1 278 28 28 VAL CG1 C 21.776 0.5 2 279 28 28 VAL CG2 C 25.705 0.5 2 280 28 28 VAL N N 120.425 0.5 1 281 29 29 ALA H H 7.767 0.05 1 282 29 29 ALA HA H 4.01 0.05 1 283 29 29 ALA HB H 1.497 0.05 1 284 29 29 ALA CA C 55.524 0.5 1 285 29 29 ALA CB C 18.122 0.5 1 286 29 29 ALA N N 120.034 0.5 1 287 30 30 ARG H H 7.994 0.05 1 288 30 30 ARG HA H 3.965 0.05 1 289 30 30 ARG HB2 H 1.879 0.05 2 290 30 30 ARG HB3 H 2.147 0.05 2 291 30 30 ARG HD2 H 3.442 0.05 2 292 30 30 ARG HD3 H 2.987 0.05 2 293 30 30 ARG HG2 H 1.636 0.05 2 294 30 30 ARG HG3 H 1.322 0.05 2 295 30 30 ARG CA C 59.663 0.5 1 296 30 30 ARG CB C 30.86 0.5 1 297 30 30 ARG CD C 42.916 0.5 1 298 30 30 ARG CG C 27.467 0.5 1 299 30 30 ARG N N 119.884 0.5 1 300 31 31 LEU H H 8.516 0.05 1 301 31 31 LEU HA H 3.964 0.05 1 302 31 31 LEU HB2 H 1.329 0.05 2 303 31 31 LEU HB3 H 1.965 0.05 2 304 31 31 LEU HD1 H 0.828 0.05 2 305 31 31 LEU HD2 H 0.916 0.05 2 306 31 31 LEU HG H 1.678 0.05 1 307 31 31 LEU CA C 58.141 0.5 1 308 31 31 LEU CB C 44.129 0.5 1 309 31 31 LEU CD1 C 23.777 0.5 2 310 31 31 LEU CD2 C 28.076 0.5 2 311 31 31 LEU CG C 28.083 0.5 1 312 31 31 LEU N N 120.609 0.5 1 313 32 32 LYS H H 9.048 0.05 1 314 32 32 LYS HA H 3.822 0.05 1 315 32 32 LYS HB2 H 1.836 0.05 2 316 32 32 LYS HB3 H 1.861 0.05 2 317 32 32 LYS HD2 H 1.628 0.05 2 318 32 32 LYS HD3 H 1.47 0.05 2 319 32 32 LYS HE2 H 2.822 0.05 2 320 32 32 LYS HE3 H 3.08 0.05 2 321 32 32 LYS HG2 H 1.788 0.05 2 322 32 32 LYS HG3 H 1.316 0.05 2 323 32 32 LYS CA C 60.976 0.5 1 324 32 32 LYS CB C 32.591 0.5 1 325 32 32 LYS CD C 29.919 0.5 1 326 32 32 LYS CE C 42.066 0.5 1 327 32 32 LYS CG C 27.714 0.5 1 328 32 32 LYS N N 118.822 0.5 1 329 33 33 LYS H H 7.381 0.05 1 330 33 33 LYS HA H 4.141 0.05 1 331 33 33 LYS HB2 H 1.902 0.05 2 332 33 33 LYS HB3 H 1.964 0.05 2 333 33 33 LYS HD2 H 1.704 0.05 2 334 33 33 LYS HD3 H 1.715 0.05 2 335 33 33 LYS HE2 H 2.989 0.05 2 336 33 33 LYS HE3 H 2.989 0.05 2 337 33 33 LYS HG2 H 1.596 0.05 2 338 33 33 LYS HG3 H 1.454 0.05 2 339 33 33 LYS CA C 58.987 0.5 1 340 33 33 LYS CB C 32.372 0.5 1 341 33 33 LYS CD C 29.318 0.5 1 342 33 33 LYS CE C 42.272 0.5 1 343 33 33 LYS CG C 25.365 0.5 1 344 33 33 LYS N N 117.698 0.5 1 345 34 34 LEU H H 7.475 0.05 1 346 34 34 LEU HA H 4.185 0.05 1 347 34 34 LEU HB2 H 1.621 0.05 2 348 34 34 LEU HB3 H 2.07 0.05 2 349 34 34 LEU HD1 H 0.953 0.05 2 350 34 34 LEU HD2 H 0.903 0.05 2 351 34 34 LEU HG H 1.838 0.05 1 352 34 34 LEU CA C 57.475 0.5 1 353 34 34 LEU CB C 42.687 0.5 1 354 34 34 LEU CD1 C 25.614 0.5 2 355 34 34 LEU CD2 C 23.377 0.5 2 356 34 34 LEU CG C 26.875 0.5 1 357 34 34 LEU N N 118.971 0.5 1 358 35 35 VAL H H 7.794 0.05 1 359 35 35 VAL HA H 4.086 0.05 1 360 35 35 VAL HB H 2.239 0.05 1 361 35 35 VAL HG1 H 0.932 0.05 2 362 35 35 VAL HG2 H 0.988 0.05 2 363 35 35 VAL CA C 62.99 0.5 1 364 35 35 VAL CB C 32.638 0.5 1 365 35 35 VAL CG1 C 21.982 0.5 2 366 35 35 VAL CG2 C 21.982 0.5 2 367 35 35 VAL N N 113.834 0.5 1 368 36 36 GLY H H 7.873 0.05 1 369 36 36 GLY HA2 H 3.88 0.05 2 370 36 36 GLY HA3 H 4.099 0.05 2 371 36 36 GLY CA C 45.946 0.5 1 372 36 36 GLY N N 109.267 0.5 1 373 37 37 GLU H H 7.978 0.05 1 374 37 37 GLU HA H 4.357 0.05 1 375 37 37 GLU HB2 H 2.038 0.05 2 376 37 37 GLU HB3 H 1.738 0.05 2 377 37 37 GLU HG2 H 2.25 0.05 2 378 37 37 GLU HG3 H 2.25 0.05 2 379 37 37 GLU CA C 56.352 0.5 1 380 37 37 GLU CB C 31.523 0.5 1 381 37 37 GLU CG C 36.766 0.5 1 382 37 37 GLU N N 120.938 0.5 1 383 38 38 ARG H H 7.983 0.05 1 384 38 38 ARG HA H 4.13 0.05 1 385 38 38 ARG HB2 H 1.677 0.05 2 386 38 38 ARG HB3 H 1.823 0.05 2 387 38 38 ARG HD2 H 3.196 0.05 2 388 38 38 ARG HD3 H 3.196 0.05 2 389 38 38 ARG HG2 H 1.614 0.05 2 390 38 38 ARG HG3 H 1.614 0.05 2 391 38 38 ARG CA C 57.541 0.5 1 392 38 38 ARG CB C 31.666 0.5 1 393 38 38 ARG CD C 43.524 0.5 1 394 38 38 ARG CG C 27.455 0.5 1 395 38 38 ARG N N 127.3 0.5 1 stop_ save_