data_17944 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C, 15N Chemical shifts of the C-terminal fragment of E. coli thioredoxin reassembly using solid-state NMR spectroscopy ; _BMRB_accession_number 17944 _BMRB_flat_file_name bmr17944.str _Entry_type original _Submission_date 2011-09-15 _Accession_date 2011-09-15 _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 Marulanda Dabeiba . . 2 Tasayco Maria . . 3 McDermott Ann . . 4 Cataldi Marcela . . 5 Arriaran Vilma . . 6 Polenova Tatyana . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 152 "15N chemical shifts" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-10-28 original author . stop_ _Original_release_date 2011-10-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15600367 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Marulanda Dabeiba . . 2 Tasayco Maria L. . 3 McDermott Ann . . 4 Cataldi M. . . 5 Arriaran V. . . 6 Polenova Tatyana . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 126 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16608 _Page_last 16620 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C-terminal Trx reassembly' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal fragment' $C-terminal_of_Trx_reassembly 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_C-terminal_of_Trx_reassembly _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C-terminal_of_Trx_reassembly _Molecular_mass . _Mol_thiol_state 'not available' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; GIPTLLLFKNGEVAATKVGA LSKGQLKEFLDANLA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 74 GLY 2 75 ILE 3 76 PRO 4 77 THR 5 78 LEU 6 79 LEU 7 80 LEU 8 81 PHE 9 82 LYS 10 83 ASN 11 84 GLY 12 85 GLU 13 86 VAL 14 87 ALA 15 88 ALA 16 89 THR 17 90 LYS 18 91 VAL 19 92 GLY 20 93 ALA 21 94 LEU 22 95 SER 23 96 LYS 24 97 GLY 25 98 GLN 26 99 LEU 27 100 LYS 28 101 GLU 29 102 PHE 30 103 LEU 31 104 ASP 32 105 ALA 33 106 ASN 34 107 LEU 35 108 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 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 17700 TRX_intact 100.00 108 100.00 100.00 1.61e-13 BMRB 1812 thioredoxin 100.00 108 100.00 100.00 1.61e-13 BMRB 1813 thioredoxin 100.00 108 100.00 100.00 1.61e-13 PDB 1F6M "Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And The Nadp+ Analog, Aadp+" 100.00 108 100.00 100.00 1.61e-13 PDB 1KEB "Crystal Structure Of Double Mutant M37l,P40s E.Coli Thioredoxin" 100.00 108 100.00 100.00 1.62e-13 PDB 1M7T "Solution Structure And Dynamics Of The Human-Escherichia Coli Thioredoxin Chimera: Insights Into Thermodynamic Stability" 97.14 107 100.00 100.00 3.71e-13 PDB 1OAZ "Ige Fv Spe7 Complexed With A Recombinant Thioredoxin" 100.00 123 100.00 100.00 1.66e-13 PDB 1SKR "T7 Dna Polymerase Complexed To Dna Primer/template And Ddatp" 100.00 108 100.00 100.00 1.61e-13 PDB 1SKS "Binary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A CIS-Syn Thymine Dimer On The Template" 100.00 108 100.00 100.00 1.61e-13 PDB 1SKW "Binary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A DISORDERED CIS-Syn Thymine Dimer On The Template" 100.00 108 100.00 100.00 1.61e-13 PDB 1SL0 "Ternary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A DISORDERED CIS-Syn Thymine Dimer On The Template" 100.00 108 100.00 100.00 1.61e-13 PDB 1SL1 "Binary 5' Complex Of T7 Dna Polymerase With A Dna Primer/template Containing A Cis-syn Thymine Dimer On The Template" 100.00 108 100.00 100.00 1.61e-13 PDB 1SL2 "Ternary 5' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A CIS-Syn Thymine Dimer On The Template And An Inc" 100.00 108 100.00 100.00 1.61e-13 PDB 1SRX "Three-Dimensional Structure Of Escherichia Coli Thioredoxin-S2 To 2.8 Angstroms Resolution" 100.00 108 100.00 100.00 1.43e-13 PDB 1T7P "T7 Dna Polymerase Complexed To Dna PrimerTEMPLATE,A Nucleoside Triphosphate, And Its Processivity Factor Thioredoxin" 100.00 108 100.00 100.00 1.61e-13 PDB 1T8E "T7 Dna Polymerase Ternary Complex With Dctp At The Insertion Site." 100.00 108 100.00 100.00 1.61e-13 PDB 1THO "Crystal Structure Of A Mutant Escherichia Coli Thioredoxin With An Arginine Insertion In The Active Site" 100.00 109 100.00 100.00 1.65e-13 PDB 1TK0 "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Ddctp At The Insertion Site" 100.00 108 100.00 100.00 1.61e-13 PDB 1TK5 "T7 Dna Polymerase Binary Complex With 8 Oxo Guanosine In The Templating Strand" 100.00 108 100.00 100.00 1.61e-13 PDB 1TK8 "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Damp At The Elongation Site" 100.00 108 100.00 100.00 1.61e-13 PDB 1TKD "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Dcmp At The Elongation Site" 100.00 108 100.00 100.00 1.61e-13 PDB 1TXX "Active-Site Variant Of E.Coli Thioredoxin" 100.00 108 100.00 100.00 1.26e-13 PDB 1X9M "T7 Dna Polymerase In Complex With An N-2- Acetylaminofluorene-adducted Dna" 100.00 108 100.00 100.00 1.61e-13 PDB 1X9S "T7 Dna Polymerase In Complex With A PrimerTEMPLATE DNA Containing A Disordered N-2 Aminofluorene On The Template, Crystallized " 100.00 108 100.00 100.00 1.61e-13 PDB 1X9W "T7 Dna Polymerase In Complex With A Primer/template Dna Containing A Disordered N-2 Aminofluorene On The Template, Crystallized" 100.00 108 100.00 100.00 1.61e-13 PDB 1XOA "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" 100.00 108 100.00 100.00 1.82e-13 PDB 1XOB "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" 100.00 108 100.00 100.00 1.82e-13 PDB 1ZCP "Crystal Structure Of A Catalytic Site Mutant E. Coli Trxa (Caca)" 100.00 108 100.00 100.00 1.31e-13 PDB 1ZYQ "T7 Dna Polymerase In Complex With 8og And Incoming Ddatp" 100.00 108 100.00 100.00 1.61e-13 PDB 1ZZY "Crystal Structure Of Thioredoxin Mutant L7v" 100.00 108 100.00 100.00 1.57e-13 PDB 2AJQ "Structure Of Replicative Dna Polymerase Provides Insigts Into The Mechanisms For Processivity, Frameshifting And Editing" 100.00 108 100.00 100.00 1.61e-13 PDB 2BTO "Structure Of Btuba From Prosthecobacter Dejongeii" 100.00 108 100.00 100.00 1.61e-13 PDB 2EIO "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" 100.00 108 97.14 97.14 2.49e-12 PDB 2EIQ "Design Of Disulfide-linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" 100.00 108 97.14 97.14 7.82e-13 PDB 2FCH "Crystal Structure Of Thioredoxin Mutant G74s" 97.14 108 100.00 100.00 9.07e-13 PDB 2FD3 "Crystal Structure Of Thioredoxin Mutant P34h" 100.00 108 100.00 100.00 1.44e-13 PDB 2H6X "Crystal Structure Of Thioredoxin Wild Type In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.61e-13 PDB 2H6Y "Crystal Structure Of Thioredoxin Mutant E48d In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.56e-13 PDB 2H6Z "Crystal Structure Of Thioredoxin Mutant E44d In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.56e-13 PDB 2H70 "Crystal Structure Of Thioredoxin Mutant D9e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2H71 "Crystal Structure Of Thioredoxin Mutant D47e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2H72 "Crystal Structure Of Thioredoxin Mutant E85d In Hexagonal (P61) Space Group" 100.00 108 97.14 100.00 4.52e-13 PDB 2H73 "Crystal Structure Of Thioredoxin Mutant D43e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2H74 "Crystal Structure Of Thioredoxin Mutant D2e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2H75 "Crystal Structure Of Thioredoxin Mutant D13e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2H76 "Crystal Structure Of Thioredoxin Mutant D10e In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 1.68e-13 PDB 2O8V "Paps Reductase In A Covalent Complex With Thioredoxin C35a" 100.00 128 100.00 100.00 1.14e-13 PDB 2TIR "Crystal Structure Analysis Of A Mutant Escherichia Coli Thioredoxin In Which Lysine 36 Is Replaced By Glutamic Acid" 100.00 108 100.00 100.00 1.64e-13 PDB 2TRX "Crystal Structure Of Thioredoxin From Escherichia Coli At 1.68 Angstroms Resolution" 100.00 108 100.00 100.00 1.61e-13 PDB 3DXB "Structure Of The Uhm Domain Of Puf60 Fused To Thioredoxin" 100.00 222 100.00 100.00 8.32e-14 PDB 3DYR "Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form" 100.00 111 97.14 97.14 1.04e-12 PDB 4HU7 "E. Coli Thioredoxin Variant With Pro76 As Single Proline Residue" 100.00 108 100.00 100.00 8.51e-14 PDB 4HU9 "E. Coli Thioredoxin Variant With (4s)-fluoropro76 As Single Proline Residue" 100.00 108 97.14 97.14 1.72e-12 PDB 4HUA "E. Coli Thioredoxin Variant With (4r)-fluoropro76 As Single Proline Residue" 100.00 108 97.14 97.14 1.72e-12 PDB 4KCA "Crystal Structure Of Endo-1,5-alpha-l-arabinanase From A Bovine Ruminal Metagenomic Library" 100.00 692 100.00 100.00 5.06e-13 PDB 4KCB "Crystal Structure Of Exo-1,5-alpha-l-arabinanase From Bovine Ruminal Metagenomic Library" 100.00 447 100.00 100.00 2.03e-13 PDB 4X43 "Structure Of Proline-free E. Coli Thioredoxin" 100.00 108 97.14 97.14 1.35e-12 DBJ BAA00903 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 109 100.00 100.00 1.57e-13 DBJ BAB38137 "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" 100.00 127 100.00 100.00 1.63e-13 DBJ BAE77517 "thioredoxin 1 [Escherichia coli str. K12 substr. W3110]" 100.00 109 100.00 100.00 1.57e-13 DBJ BAG79587 "thioredoxin [Escherichia coli SE11]" 100.00 109 100.00 100.00 1.57e-13 DBJ BAH61053 "thioredoxin [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 113 100.00 100.00 1.80e-13 EMBL CAA79851 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 109 100.00 100.00 1.57e-13 EMBL CAD09400 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 109 100.00 100.00 1.57e-13 EMBL CAG77109 "thioredoxin [Pectobacterium atrosepticum SCRI1043]" 97.14 108 97.06 97.06 8.89e-12 EMBL CAO95241 "Thioredoxin 1 [Erwinia tasmaniensis Et1/99]" 97.14 109 97.06 100.00 4.25e-12 EMBL CAP78228 "Thioredoxin 1 [Escherichia coli LF82]" 100.00 144 100.00 100.00 1.68e-13 GB AAA24533 "thioredoxin (trxA) [Escherichia coli]" 100.00 109 100.00 100.00 1.57e-13 GB AAA24534 "thioredoxin [Escherichia coli]" 100.00 127 100.00 100.00 1.63e-13 GB AAA24693 "thioredoxin [Escherichia coli]" 100.00 109 100.00 100.00 1.57e-13 GB AAA24694 "thioredoxin (trxA) [Escherichia coli]" 100.00 109 100.00 100.00 1.57e-13 GB AAA24696 "thioredoxin [Escherichia coli]" 102.86 110 97.22 97.22 8.28e-12 PIR AF0922 "thioredoxin [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 109 100.00 100.00 1.57e-13 PIR B91218 "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" 100.00 127 100.00 100.00 1.63e-13 PIR C86064 "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 127 100.00 100.00 1.63e-13 REF NP_312741 "thioredoxin [Escherichia coli O157:H7 str. Sakai]" 100.00 127 100.00 100.00 1.63e-13 REF NP_418228 "thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]" 100.00 109 100.00 100.00 1.57e-13 REF NP_457831 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 109 100.00 100.00 1.57e-13 REF NP_462806 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 109 100.00 100.00 1.57e-13 REF NP_709584 "thioredoxin [Shigella flexneri 2a str. 301]" 100.00 127 100.00 100.00 1.63e-13 SP P0AA25 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 1.57e-13 SP P0AA26 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 1.57e-13 SP P0AA27 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 1.57e-13 SP P0AA28 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 1.57e-13 SP P0AA29 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 1.57e-13 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 $C-terminal_of_Trx_reassembly 'E. coli' 562 Bacteria . Escherichia coli Trx 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 $C-terminal_of_Trx_reassembly 'recombinant technology' . Escherichia coli . pTK100 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C-terminal_of_Trx_reassembly 'PEG precipitate' mg '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . Goddard . . stop_ loop_ _Task 'chemical shift assignment' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_13C-13C_DARR_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C DARR' _Sample_label $sample_1 save_ save_2D_15N-13C_NCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13C NCA' _Sample_label $sample_1 save_ save_2D_15N-13C_NCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13C NCO' _Sample_label $sample_1 save_ save_2D_15N-13C_NCACX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13C NCACX' _Sample_label $sample_1 save_ save_2D_15N-13C_NCOCX_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13C NCOCX' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 10 . mM pH 3.5 . pH pressure 1 . atm temperature 273 . K 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 13C-13C DARR' '2D 15N-13C NCA' '2D 15N-13C NCO' '2D 15N-13C NCACX' '2D 15N-13C NCOCX' 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 'C-terminal fragment' _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 74 1 GLY C C 169.8 0.2 1 2 74 1 GLY CA C 43.30 0.2 1 3 74 1 GLY N N 104.7 0.2 1 4 75 2 ILE C C 173.7 0.2 1 5 75 2 ILE CA C 59.40 0.2 1 6 75 2 ILE CB C 38.60 0.2 1 7 75 2 ILE CG1 C 24.50 0.2 1 8 75 2 ILE CG2 C 20.40 0.2 1 9 75 2 ILE CD1 C 16.60 0.2 1 10 75 2 ILE N N 114.4 0.2 1 11 76 3 PRO C C 177.9 0.2 1 12 76 3 PRO CA C 62.80 0.2 1 13 76 3 PRO CB C 34.80 0.2 1 14 76 3 PRO CG C 24.70 0.2 1 15 76 3 PRO CD C 51.60 0.2 1 16 76 3 PRO N N 136.4 0.2 1 17 77 4 THR C C 171.3 0.2 1 18 77 4 THR CA C 64.00 0.2 1 19 77 4 THR CB C 75.40 0.2 1 20 77 4 THR CG2 C 20.90 0.2 1 21 77 4 THR N N 120.2 0.2 1 22 78 5 LEU C C 175.3 0.2 1 23 78 5 LEU CA C 52.60 0.2 1 24 78 5 LEU CB C 44.10 0.2 1 25 78 5 LEU CG C 26.90 0.2 1 26 78 5 LEU N N 126.1 0.2 1 27 79 6 LEU C C 175.6 0.2 1 28 79 6 LEU CA C 52.90 0.2 1 29 79 6 LEU CB C 45.50 0.2 1 30 79 6 LEU CG C 27.10 0.2 1 31 79 6 LEU N N 125.7 0.2 1 32 80 7 LEU C C 174.4 0.2 1 33 80 7 LEU CA C 52.00 0.2 1 34 80 7 LEU CB C 44.50 0.2 1 35 80 7 LEU CG C 27.20 0.2 1 36 80 7 LEU CD1 C 26.80 0.2 . 37 80 7 LEU CD2 C 23.60 0.2 . 38 80 7 LEU N N 120.0 0.2 1 39 81 8 PHE C C 176.9 0.2 1 40 81 8 PHE CA C 56.80 0.2 1 41 81 8 PHE CB C 41.70 0.2 1 42 81 8 PHE CG C 140.8 0.2 1 43 81 8 PHE CD1 C 136.4 0.2 . 44 81 8 PHE CD2 C 131.8 0.2 . 45 81 8 PHE CE1 C 133.7 0.2 . 46 81 8 PHE CE2 C 133.7 0.2 . 47 81 8 PHE N N 128.1 0.2 1 48 82 9 LYS C C 178.7 0.2 1 49 82 9 LYS CA C 55.80 0.2 1 50 82 9 LYS CB C 35.40 0.2 1 51 82 9 LYS CG C 25.20 0.2 1 52 82 9 LYS CD C 30.10 0.2 1 53 82 9 LYS CE C 41.90 0.2 1 54 82 9 LYS N N 116.7 0.2 1 55 83 10 ASN C C 176.1 0.2 1 56 83 10 ASN CA C 54.30 0.2 1 57 83 10 ASN CB C 37.50 0.2 1 58 83 10 ASN N N 123.9 0.2 1 59 84 11 GLY C C 173.9 0.2 1 60 84 11 GLY CA C 46.30 0.2 1 61 84 11 GLY N N 104.2 0.2 1 62 85 12 GLU C C 177.2 0.2 1 63 85 12 GLU CA C 55.30 0.2 1 64 85 12 GLU CB C 35.50 0.2 1 65 85 12 GLU CG C 38.10 0.2 1 66 85 12 GLU CD C 183.9 0.2 1 67 85 12 GLU N N 117.3 0.2 1 68 86 13 VAL C C 175.5 0.2 1 69 86 13 VAL CA C 64.40 0.2 1 70 86 13 VAL CB C 29.10 0.2 1 71 86 13 VAL CG1 C 22.20 0.2 . 72 86 13 VAL CG2 C 22.20 0.2 . 73 86 13 VAL N N 124.3 0.2 1 74 87 14 ALA C C 176.6 0.2 1 75 87 14 ALA CA C 51.90 0.2 1 76 87 14 ALA CB C 20.80 0.2 1 77 87 14 ALA N N 135.8 0.2 1 78 88 15 ALA C C 175.1 0.2 1 79 88 15 ALA CA C 52.70 0.2 1 80 88 15 ALA CB C 22.50 0.2 1 81 88 15 ALA N N 114.5 0.2 1 82 89 16 THR C C 173.6 0.2 1 83 89 16 THR CA C 62.40 0.2 1 84 89 16 THR CB C 71.40 0.2 1 85 89 16 THR CG2 C 21.40 0.2 1 86 89 16 THR N N 117.3 0.2 1 87 90 17 LYS C C 173.8 0.2 1 88 90 17 LYS CA C 53.80 0.2 1 89 90 17 LYS CB C 33.00 0.2 1 90 90 17 LYS CG C 26.20 0.2 1 91 90 17 LYS CD C 27.00 0.2 1 92 90 17 LYS CE C 41.90 0.2 1 93 90 17 LYS N N 127.5 0.2 1 94 91 18 VAL C C 177.3 0.2 1 95 91 18 VAL CA C 62.20 0.2 1 96 91 18 VAL CB C 33.50 0.2 1 97 91 18 VAL CG1 C 21.20 0.2 . 98 91 18 VAL CG2 C 21.20 0.2 . 99 91 18 VAL N N 132.1 0.2 1 100 92 19 GLY C C 171.7 0.2 1 101 92 19 GLY CA C 44.00 0.2 1 102 92 19 GLY N N 114.9 0.2 1 103 93 20 ALA C C 175.1 0.2 1 104 93 20 ALA CA C 52.80 0.2 1 105 93 20 ALA CB C 19.30 0.2 1 106 93 20 ALA N N 125.8 0.2 1 107 94 21 LEU CA C 54.70 0.2 1 108 94 21 LEU CB C 43.60 0.2 1 109 94 21 LEU CG C 26.70 0.2 1 110 94 21 LEU CD1 C 26.90 0.2 . 111 94 21 LEU CD2 C 24.00 0.2 . 112 94 21 LEU N N 124.0 0.2 1 113 95 22 SER C C 175.4 0.2 1 114 95 22 SER CA C 56.10 0.2 1 115 95 22 SER CB C 66.40 0.2 1 116 95 22 SER N N 114.5 0.2 1 117 96 23 LYS C C 178.8 0.2 1 118 96 23 LYS CA C 61.00 0.2 1 119 96 23 LYS CB C 33.60 0.2 1 120 96 23 LYS CG C 24.50 0.2 1 121 96 23 LYS CD C 29.00 0.2 1 122 96 23 LYS CE C 42.70 0.2 1 123 96 23 LYS N N 120.9 0.2 1 124 97 24 GLY C C 177.0 0.2 1 125 97 24 GLY CA C 46.90 0.2 1 126 97 24 GLY N N 106.1 0.2 1 127 98 25 GLN C C 179.8 0.2 1 128 98 25 GLN CA C 58.20 0.2 1 129 98 25 GLN CB C 29.50 0.2 1 130 98 25 GLN CG C 34.60 0.2 1 131 98 25 GLN N N 121.8 0.2 1 132 99 26 LEU C C 177.9 0.2 1 133 99 26 LEU CA C 57.90 0.2 1 134 99 26 LEU CB C 40.80 0.2 1 135 99 26 LEU CG C 27.50 0.2 1 136 99 26 LEU CD2 C 22.70 0.2 . 137 99 26 LEU N N 124.0 0.2 1 138 100 27 LYS C C 178.5 0.2 1 139 100 27 LYS CA C 60.60 0.2 1 140 100 27 LYS CB C 30.80 0.2 1 141 100 27 LYS CG C 25.40 0.2 1 142 100 27 LYS CD C 27.30 0.2 1 143 100 27 LYS CE C 42.60 0.2 1 144 100 27 LYS N N 118.9 0.2 1 145 101 28 GLU C C 179.5 0.2 1 146 101 28 GLU CA C 59.90 0.2 1 147 101 28 GLU CB C 28.50 0.2 1 148 101 28 GLU CG C 34.50 0.2 1 149 101 28 GLU CD C 181.8 0.2 1 150 101 28 GLU N N 118.7 0.2 1 151 102 29 PHE C C 177.4 0.2 1 152 102 29 PHE CA C 60.40 0.2 1 153 102 29 PHE CB C 39.60 0.2 1 154 102 29 PHE CG C 138.2 0.2 1 155 102 29 PHE CD2 C 135.7 0.2 . 156 102 29 PHE N N 120.4 0.2 1 157 103 30 LEU C C 177.4 0.2 1 158 103 30 LEU CA C 57.8 0.2 1 159 103 30 LEU CB C 40.90 0.2 1 160 103 30 LEU CG C 26.20 0.2 1 161 103 30 LEU CD1 C 23.20 0.2 . 162 103 30 LEU CD2 C 27.50 0.2 . 163 103 30 LEU N N 119.9 0.2 1 164 104 31 ASP C C 179.2 0.2 1 165 104 31 ASP CA C 57.50 0.2 1 166 104 31 ASP CB C 39.20 0.2 1 167 104 31 ASP CG C 180.7 0.2 1 168 104 31 ASP N N 120.8 0.2 1 169 105 32 ALA C C 179.1 0.2 1 170 105 32 ALA CA C 53.80 0.2 1 171 105 32 ALA CB C 19.20 0.2 1 172 105 32 ALA N N 120.9 0.2 1 173 106 33 ASN C C 178.3 0.2 1 174 106 33 ASN CA C 54.20 0.2 1 175 106 33 ASN CB C 41.60 0.2 1 176 106 33 ASN CG C 183.1 0.2 1 177 106 33 ASN N N 112.7 0.2 1 178 107 34 LEU CA C 54.60 0.2 1 179 107 34 LEU CB C 43.20 0.2 1 180 107 34 LEU CG C 26.80 0.2 1 181 107 34 LEU CD1 C 23.50 0.2 . 182 107 34 LEU CD2 C 26.80 0.2 . 183 107 34 LEU N N 121.0 0.2 1 184 108 35 ALA C C 178.0 0.2 1 185 108 35 ALA CA C 54.40 0.2 1 186 108 35 ALA CB C 19.30 0.2 1 stop_ save_