data_17700 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C, 15N Chemical shifts of E. coli thioredoxin using solid-state nmr spectroscopy ; _BMRB_accession_number 17700 _BMRB_flat_file_name bmr17700.str _Entry_type original _Submission_date 2011-06-13 _Accession_date 2011-06-13 _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 Paramasivam Sivakumar . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 487 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-07-15 original author . stop_ _Original_release_date 2011-07-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16853329 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Marulanda Dabeiba . . 2 Tasayco 'Maria Luisa' . . 3 Cataldi Marcela . . 4 Arriaran Vilma . . 5 Polenova Tatyana . . stop_ _Journal_abbreviation 'J. Phys. Chem. B' _Journal_volume 109 _Journal_issue 38 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18135 _Page_last 18145 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TRX Intact' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TRX Intact' $TRX_intact 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_TRX_intact _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRX_intact _Molecular_mass . _Mol_thiol_state 'not available' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGALSKGQLK EFLDANLA ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ASP 3 LYS 4 ILE 5 ILE 6 HIS 7 LEU 8 THR 9 ASP 10 ASP 11 SER 12 PHE 13 ASP 14 THR 15 ASP 16 VAL 17 LEU 18 LYS 19 ALA 20 ASP 21 GLY 22 ALA 23 ILE 24 LEU 25 VAL 26 ASP 27 PHE 28 TRP 29 ALA 30 GLU 31 TRP 32 CYS 33 GLY 34 PRO 35 CYS 36 LYS 37 MET 38 ILE 39 ALA 40 PRO 41 ILE 42 LEU 43 ASP 44 GLU 45 ILE 46 ALA 47 ASP 48 GLU 49 TYR 50 GLN 51 GLY 52 LYS 53 LEU 54 THR 55 VAL 56 ALA 57 LYS 58 LEU 59 ASN 60 ILE 61 ASP 62 GLN 63 ASN 64 PRO 65 GLY 66 THR 67 ALA 68 PRO 69 LYS 70 TYR 71 GLY 72 ILE 73 ARG 74 GLY 75 ILE 76 PRO 77 THR 78 LEU 79 LEU 80 LEU 81 PHE 82 LYS 83 ASN 84 GLY 85 GLU 86 VAL 87 ALA 88 ALA 89 THR 90 LYS 91 VAL 92 GLY 93 ALA 94 LEU 95 SER 96 LYS 97 GLY 98 GLN 99 LEU 100 LYS 101 GLU 102 PHE 103 LEU 104 ASP 105 ALA 106 ASN 107 LEU 108 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 1812 thioredoxin 100.00 108 100.00 100.00 8.24e-71 BMRB 1813 thioredoxin 100.00 108 100.00 100.00 8.24e-71 PDB 1F6M "Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And The Nadp+ Analog, Aadp+" 100.00 108 99.07 99.07 9.29e-70 PDB 1KEB "Crystal Structure Of Double Mutant M37l,P40s E.Coli Thioredoxin" 100.00 108 98.15 99.07 3.63e-69 PDB 1SKR "T7 Dna Polymerase Complexed To Dna Primer/template And Ddatp" 100.00 108 100.00 100.00 8.24e-71 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 8.24e-71 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 8.24e-71 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 8.24e-71 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 8.24e-71 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 8.24e-71 PDB 1T7P "T7 Dna Polymerase Complexed To Dna PrimerTEMPLATE,A Nucleoside Triphosphate, And Its Processivity Factor Thioredoxin" 100.00 108 100.00 100.00 8.24e-71 PDB 1T8E "T7 Dna Polymerase Ternary Complex With Dctp At The Insertion Site." 100.00 108 100.00 100.00 8.24e-71 PDB 1THO "Crystal Structure Of A Mutant Escherichia Coli Thioredoxin With An Arginine Insertion In The Active Site" 100.93 109 99.08 99.08 4.71e-69 PDB 1TK0 "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Ddctp At The Insertion Site" 100.00 108 100.00 100.00 8.24e-71 PDB 1TK5 "T7 Dna Polymerase Binary Complex With 8 Oxo Guanosine In The Templating Strand" 100.00 108 100.00 100.00 8.24e-71 PDB 1TK8 "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Damp At The Elongation Site" 100.00 108 100.00 100.00 8.24e-71 PDB 1TKD "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Dcmp At The Elongation Site" 100.00 108 100.00 100.00 8.24e-71 PDB 1TXX "Active-Site Variant Of E.Coli Thioredoxin" 100.00 108 98.15 98.15 6.33e-68 PDB 1X9M "T7 Dna Polymerase In Complex With An N-2- Acetylaminofluorene-adducted Dna" 100.00 108 100.00 100.00 8.24e-71 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 8.24e-71 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 8.24e-71 PDB 1XOA "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" 99.07 108 100.00 100.00 4.28e-70 PDB 1XOB "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" 99.07 108 100.00 100.00 4.28e-70 PDB 1ZCP "Crystal Structure Of A Catalytic Site Mutant E. Coli Trxa (Caca)" 100.00 108 97.22 97.22 2.61e-67 PDB 1ZYQ "T7 Dna Polymerase In Complex With 8og And Incoming Ddatp" 100.00 108 100.00 100.00 8.24e-71 PDB 1ZZY "Crystal Structure Of Thioredoxin Mutant L7v" 100.00 108 99.07 100.00 1.95e-70 PDB 2AJQ "Structure Of Replicative Dna Polymerase Provides Insigts Into The Mechanisms For Processivity, Frameshifting And Editing" 100.00 108 100.00 100.00 8.24e-71 PDB 2BTO "Structure Of Btuba From Prosthecobacter Dejongeii" 100.00 108 100.00 100.00 8.24e-71 PDB 2EIO "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" 100.00 108 99.07 99.07 2.06e-69 PDB 2EIQ "Design Of Disulfide-linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" 100.00 108 99.07 99.07 6.34e-70 PDB 2EIR "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" 100.00 108 98.15 98.15 9.08e-69 PDB 2FCH "Crystal Structure Of Thioredoxin Mutant G74s" 100.00 108 99.07 99.07 4.19e-70 PDB 2FD3 "Crystal Structure Of Thioredoxin Mutant P34h" 100.00 108 99.07 99.07 1.09e-69 PDB 2H6X "Crystal Structure Of Thioredoxin Wild Type In Hexagonal (P61) Space Group" 100.00 108 100.00 100.00 8.24e-71 PDB 2H6Y "Crystal Structure Of Thioredoxin Mutant E48d In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 3.48e-70 PDB 2H6Z "Crystal Structure Of Thioredoxin Mutant E44d In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 3.48e-70 PDB 2H70 "Crystal Structure Of Thioredoxin Mutant D9e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2H71 "Crystal Structure Of Thioredoxin Mutant D47e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2H72 "Crystal Structure Of Thioredoxin Mutant E85d In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 3.48e-70 PDB 2H73 "Crystal Structure Of Thioredoxin Mutant D43e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2H74 "Crystal Structure Of Thioredoxin Mutant D2e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2H75 "Crystal Structure Of Thioredoxin Mutant D13e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2H76 "Crystal Structure Of Thioredoxin Mutant D10e In Hexagonal (P61) Space Group" 100.00 108 99.07 100.00 2.62e-70 PDB 2O8V "Paps Reductase In A Covalent Complex With Thioredoxin C35a" 100.00 128 99.07 99.07 2.45e-70 PDB 2TIR "Crystal Structure Analysis Of A Mutant Escherichia Coli Thioredoxin In Which Lysine 36 Is Replaced By Glutamic Acid" 100.00 108 99.07 100.00 2.51e-70 PDB 2TRX "Crystal Structure Of Thioredoxin From Escherichia Coli At 1.68 Angstroms Resolution" 100.00 108 100.00 100.00 8.24e-71 PDB 3DXB "Structure Of The Uhm Domain Of Puf60 Fused To Thioredoxin" 100.00 222 100.00 100.00 9.51e-71 PDB 3DYR "Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form" 100.00 111 99.07 99.07 2.76e-70 PDB 4KCA "Crystal Structure Of Endo-1,5-alpha-l-arabinanase From A Bovine Ruminal Metagenomic Library" 100.00 692 100.00 100.00 7.64e-66 PDB 4KCB "Crystal Structure Of Exo-1,5-alpha-l-arabinanase From Bovine Ruminal Metagenomic Library" 100.00 447 100.00 100.00 3.39e-69 DBJ BAA00903 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 109 100.00 100.00 6.13e-71 DBJ BAB38137 "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" 100.00 127 100.00 100.00 3.41e-71 DBJ BAE77517 "thioredoxin 1 [Escherichia coli str. K12 substr. W3110]" 100.00 109 100.00 100.00 6.13e-71 DBJ BAG79587 "thioredoxin [Escherichia coli SE11]" 100.00 109 100.00 100.00 6.13e-71 DBJ BAH61053 "thioredoxin [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 113 97.22 98.15 5.70e-69 EMBL CAA79851 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 109 100.00 100.00 6.13e-71 EMBL CAD09400 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 109 100.00 100.00 6.13e-71 EMBL CAP78228 "Thioredoxin 1 [Escherichia coli LF82]" 100.00 144 100.00 100.00 3.36e-71 EMBL CAQ34125 "thioredoxin 1 [Escherichia coli BL21(DE3)]" 100.00 109 100.00 100.00 6.13e-71 EMBL CAQ91183 "thioredoxin 1 [Escherichia fergusonii ATCC 35469]" 100.00 109 100.00 100.00 6.13e-71 GB AAA24533 "thioredoxin (trxA) [Escherichia coli]" 100.00 109 100.00 100.00 6.13e-71 GB AAA24534 "thioredoxin [Escherichia coli]" 100.00 127 100.00 100.00 3.41e-71 GB AAA24693 "thioredoxin [Escherichia coli]" 100.00 109 100.00 100.00 6.13e-71 GB AAA24694 "thioredoxin (trxA) [Escherichia coli]" 100.00 109 100.00 100.00 6.13e-71 GB AAA24696 "thioredoxin [Escherichia coli]" 100.93 110 99.08 99.08 3.08e-69 PIR AF0922 "thioredoxin [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 109 100.00 100.00 6.13e-71 PIR B91218 "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" 100.00 127 100.00 100.00 3.41e-71 PIR C86064 "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 127 100.00 100.00 3.41e-71 REF NP_312741 "thioredoxin [Escherichia coli O157:H7 str. Sakai]" 100.00 127 100.00 100.00 3.41e-71 REF NP_418228 "thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]" 100.00 109 100.00 100.00 6.13e-71 REF NP_457831 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 109 100.00 100.00 6.13e-71 REF NP_462806 "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 109 100.00 100.00 6.13e-71 REF NP_709584 "thioredoxin [Shigella flexneri 2a str. 301]" 100.00 127 100.00 100.00 3.41e-71 SP P0AA25 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 6.13e-71 SP P0AA26 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 6.13e-71 SP P0AA27 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 6.13e-71 SP P0AA28 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 6.13e-71 SP P0AA29 "RecName: Full=Thioredoxin-1; Short=Trx-1" 100.00 109 100.00 100.00 6.13e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $TRX_intact 'E. coli' 562 Bacteria . Escherichia coli JF521 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 $TRX_intact 'recombinant technology' . Escherichia coli JF521 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 $TRX_intact . mM '[U-100% 13C; U-100% 15N]' H2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe_and_SPARKY _Saveframe_category software _Name NMRPipe_and_SPARKY _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong 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_C-C_DARR_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D C-C DARR' _Sample_label $sample_1 save_ save_2D_N-CA_SPECIFIC_CP_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N-CA SPECIFIC CP' _Sample_label $sample_1 save_ save_2D_N-CO_SPECIFIC_CP_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N-CO SPECIFIC CP' _Sample_label $sample_1 save_ save_2D_N-CA-CX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N-CA-CX' _Sample_label $sample_1 save_ save_2D_N-CO-CX_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N-CO-CX' _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' . . M pH 7 . 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 . indirect . . . 0.251449530 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D C-C DARR' '2D N-CA SPECIFIC CP' '2D N-CO SPECIFIC CP' '2D N-CA-CX' '2D N-CO-CX' 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 'TRX Intact' _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 SER C C 175.2 . 1 2 1 1 SER CA C 55.80 . 1 3 1 1 SER CB C 64.90 . 1 4 1 1 SER N N 105.0 . 1 5 2 2 ASP C C 177.4 . 1 6 2 2 ASP CA C 50.80 . 1 7 2 2 ASP CB C 40.00 . 1 8 2 2 ASP CG C 178.6 . 1 9 3 3 LYS C C 174.6 . 1 10 3 3 LYS CA C 54.00 . 1 11 3 3 LYS CB C 31.10 . 1 12 3 3 LYS CG C 22.50 . 1 13 3 3 LYS CD C 26.70 . 1 14 3 3 LYS CE C 40.10 . 1 15 3 3 LYS N N 118.1 . 1 16 4 4 ILE C C 177.0 . 1 17 4 4 ILE CA C 59.60 . 1 18 4 4 ILE CB C 37.10 . 1 19 4 4 ILE CG1 C 27.70 . 1 20 4 4 ILE CG2 C 16.30 . 1 21 4 4 ILE CD1 C 13.20 . 1 22 4 4 ILE N N 119.2 . 1 23 5 5 ILE C C 176.0 . 1 24 5 5 ILE CA C 60.20 . 1 25 5 5 ILE CB C 38.00 . 1 26 5 5 ILE CG1 C 26.00 . 1 27 5 5 ILE CG2 C 16.40 . 1 28 5 5 ILE CD1 C 13.30 . 1 29 5 5 ILE N N 127.1 . 1 30 6 6 HIS C C 174.5 . 1 31 6 6 HIS CA C 53.40 . 1 32 6 6 HIS CB C 26.00 . 1 33 6 6 HIS CG C 132.2 . 1 34 6 6 HIS CD2 C 121.6 . 1 35 6 6 HIS N N 127.3 . 1 36 7 7 LEU C C 174.6 . 1 37 7 7 LEU CA C 53.50 . 1 38 7 7 LEU CB C 43.80 . 1 39 7 7 LEU CG C 26.00 . 1 40 7 7 LEU CD1 C 27.00 . . 41 7 7 LEU CD2 C 23.20 . . 42 7 7 LEU N N 124.7 . 1 43 8 8 THR C C 178.5 . 1 44 8 8 THR CA C 57.90 . 1 45 8 8 THR CB C 71.60 . 1 46 8 8 THR CG2 C 21.90 . 1 47 8 8 THR N N 107.5 . 1 48 9 9 ASP C C 178.6 . 1 49 9 9 ASP CA C 57.10 . 1 50 9 9 ASP CB C 39.60 . 1 51 9 9 ASP CG C 186.5 . 1 52 9 9 ASP N N 118.5 . 1 53 10 10 ASP C C 177.8 . 1 54 10 10 ASP CA C 55.50 . 1 55 10 10 ASP CB C 39.40 . 1 56 10 10 ASP N N 116.3 . 1 57 11 11 SER C C 174.1 . 1 58 11 11 SER CA C 58.20 . 1 59 11 11 SER CB C 63.80 . 1 60 11 11 SER N N 117.5 . 1 61 12 12 PHE C C 176.0 . 1 62 12 12 PHE CA C 62.40 . 1 63 12 12 PHE CB C 40.10 . 1 64 12 12 PHE CG C 139.1 . 1 65 12 12 PHE N N 124.4 . 1 66 13 13 ASP C C 177.8 . 1 67 13 13 ASP CA C 57.10 . 1 68 13 13 ASP CB C 38.10 . 1 69 13 13 ASP CG C 179.3 . 1 70 13 13 ASP N N 117.5 . 1 71 14 14 THR C C 174.3 . 1 72 14 14 THR CA C 65.40 . 1 73 14 14 THR CB C 68.30 . 1 74 14 14 THR CG2 C 21.50 . 1 75 14 14 THR N N 112.0 . 1 76 15 15 ASP C C 176.3 . 1 77 15 15 ASP CA C 55.20 . 1 78 15 15 ASP CB C 39.70 . 1 79 15 15 ASP CG C 177.9 . 1 80 15 15 ASP N N 118.5 . 1 81 16 16 VAL C C 176.5 . 1 82 16 16 VAL CA C 62.20 . 1 83 16 16 VAL CB C 31.60 . 1 84 16 16 VAL CG1 C 19.10 . . 85 16 16 VAL CG2 C 21.60 . . 86 16 16 VAL N N 113.0 . 1 87 17 17 LEU C C 177.7 . 1 88 17 17 LEU CA C 56.90 . 1 89 17 17 LEU CB C 37.20 . 1 90 17 17 LEU CG C 24.50 . 1 91 17 17 LEU CD1 C 23.40 . . 92 17 17 LEU CD2 C 20.10 . . 93 17 17 LEU N N 116.5 . 1 94 18 18 LYS C C 176.5 . 1 95 18 18 LYS CA C 55.20 . 1 96 18 18 LYS CB C 29.20 . 1 97 18 18 LYS CG C 25.10 . 1 98 18 18 LYS CD C 27.70 . 1 99 18 18 LYS CE C 41.30 . 1 100 18 18 LYS N N 114.9 . 1 101 19 19 ALA C C 177.0 . 1 102 19 19 ALA CA C 51.10 . 1 103 19 19 ALA CB C 19.60 . 1 104 19 19 ALA N N 121.8 . 1 105 20 20 ASP C C 174.8 . 1 106 20 20 ASP CA C 51.20 . 1 107 20 20 ASP CB C 39.90 . 1 108 20 20 ASP CG C 179.8 . 1 109 20 20 ASP N N 121.4 . 1 110 21 21 GLY C C 172.2 . 1 111 21 21 GLY CA C 43.40 . 1 112 21 21 GLY N N 107.2 . 1 113 22 22 ALA C C 177.2 . 1 114 22 22 ALA CA C 50.90 . 1 115 22 22 ALA CB C 19.90 . 1 116 22 22 ALA N N 122.7 . 1 117 23 23 ILE C C 172.5 . 1 118 23 23 ILE CA C 57.60 . 1 119 23 23 ILE CB C 40.30 . 1 120 23 23 ILE CG1 C 25.10 . 1 121 23 23 ILE CG2 C 12.40 . 1 122 23 23 ILE CD1 C 10.10 . 1 123 23 23 ILE N N 122.9 . 1 124 24 24 LEU C C 172.7 . 1 125 24 24 LEU CA C 52.00 . 1 126 24 24 LEU CB C 44.70 . 1 127 24 24 LEU CG C 25.90 . 1 128 24 24 LEU CD1 C 23.70 . . 129 24 24 LEU N N 129.8 . 1 130 25 25 VAL C C 176.3 . 1 131 25 25 VAL CA C 60.60 . 1 132 25 25 VAL CB C 33.00 . 1 133 25 25 VAL CG1 C 22.60 . . 134 25 25 VAL CG2 C 20.30 . . 135 25 25 VAL N N 126.2 . 1 136 26 26 ASP C C 174.2 . 1 137 26 26 ASP CA C 50.90 . 1 138 26 26 ASP CB C 38.00 . 1 139 26 26 ASP CG C 183.5 . 1 140 26 26 ASP N N 124.1 . 1 141 27 27 PHE C C 174.1 . 1 142 27 27 PHE CA C 56.80 . 1 143 27 27 PHE CB C 38.50 . 1 144 27 27 PHE CG C 139.7 . 1 145 27 27 PHE CD1 C 131.3 . . 146 27 27 PHE CD2 C 130.2 . . 147 27 27 PHE N N 128.0 . 1 148 28 28 TRP C C 174.7 . 1 149 28 28 TRP CA C 54.40 . 1 150 28 28 TRP CB C 31.40 . 1 151 28 28 TRP CG C 109.6 . 1 152 28 28 TRP CD1 C 125.8 . 1 153 28 28 TRP CD2 C 126.9 . 1 154 28 28 TRP N N 119.6 . 1 155 30 30 GLU C C 178.2 . 1 156 30 30 GLU CA C 57.50 . 1 157 30 30 GLU CB C 28.70 . 1 158 30 30 GLU CG C 34.00 . 1 159 30 30 GLU CD C 181.9 . 1 160 30 30 GLU N N 120.8 . 1 161 31 31 TRP C C 177.8 . 1 162 31 31 TRP CA C 53.40 . 1 163 31 31 TRP CB C 27.80 . 1 164 31 31 TRP CG C 108.2 . 1 165 31 31 TRP CD1 C 127.8 . 1 166 31 31 TRP CD2 C 130.5 . 1 167 31 31 TRP CE2 C 136.6 . 1 168 31 31 TRP CZ2 C 115.6 . 1 169 31 31 TRP CH2 C 124.3 . 1 170 31 31 TRP N N 110.6 . 1 171 32 32 CYS C C 174.4 . 1 172 32 32 CYS CA C 58.10 . 1 173 32 32 CYS CB C 27.90 . 1 174 32 32 CYS N N 121.0 . 1 175 33 33 GLY C C 175.5 . 1 176 33 33 GLY CA C 48.00 . 1 177 33 33 GLY N N 120.6 . 1 178 34 34 PRO C C 179.4 . 1 179 34 34 PRO CA C 64.00 . 1 180 34 34 PRO CB C 31.70 . 1 181 34 34 PRO CG C 29.10 . 1 182 34 34 PRO CD C 51.10 . 1 183 34 34 PRO N N 136.5 . 1 184 35 35 CYS CA C 62.80 . 1 185 35 35 CYS CB C 25.80 . 1 186 35 35 CYS N N 111.3 . 1 187 36 36 LYS C C 176.4 . 1 188 36 36 LYS CA C 57.90 . 1 189 36 36 LYS CB C 31.50 . 1 190 36 36 LYS CG C 23.60 . 1 191 36 36 LYS CD C 25.60 . 1 192 36 36 LYS CE C 40.00 . 1 193 36 36 LYS N N 121.1 . 1 194 37 37 MET C C 176.9 . 1 195 37 37 MET CA C 55.80 . 1 196 37 37 MET CB C 30.50 . 1 197 37 37 MET CG C 32.60 . 1 198 37 37 MET CE C 19.60 . 1 199 37 37 MET N N 117.2 . 1 200 38 38 ILE C C 176.1 . 1 201 38 38 ILE CA C 61.00 . 1 202 38 38 ILE CB C 38.60 . 1 203 38 38 ILE CG1 C 26.50 . 1 204 38 38 ILE CG2 C 16.50 . 1 205 38 38 ILE CD1 C 13.90 . 1 206 38 38 ILE N N 109.4 . 1 207 39 39 ALA C C 176.5 . 1 208 39 39 ALA CA C 56.50 . 1 209 39 39 ALA CB C 14.20 . 1 210 39 39 ALA N N 124.8 . 1 211 40 40 PRO C C 179.1 . 1 212 40 40 PRO CA C 64.60 . 1 213 40 40 PRO CB C 30.30 . 1 214 40 40 PRO CG C 27.60 . 1 215 40 40 PRO CD C 49.40 . 1 216 40 40 PRO N N 132.3 . 1 217 41 41 ILE C C 177.9 . 1 218 41 41 ILE CA C 63.50 . 1 219 41 41 ILE CB C 37.20 . 1 220 41 41 ILE CG1 C 27.50 . 1 221 41 41 ILE CG2 C 17.40 . 1 222 41 41 ILE CD1 C 12.20 . 1 223 41 41 ILE N N 117.3 . 1 224 42 42 LEU C C 173.4 . 1 225 42 42 LEU CA C 57.00 . 1 226 42 42 LEU CB C 38.60 . 1 227 42 42 LEU CG C 25.70 . 1 228 42 42 LEU CD1 C 23.70 . . 229 42 42 LEU CD2 C 21.70 . . 230 42 42 LEU N N 119.6 . 1 231 43 43 ASP CA C 56.30 . 1 232 43 43 ASP CB C 38.00 . 1 233 43 43 ASP CG C 183.8 . 1 234 43 43 ASP N N 118.1 . 1 235 44 44 GLU C C 179.1 . 1 236 44 44 GLU CA C 57.90 . 1 237 44 44 GLU CB C 28.40 . 1 238 44 44 GLU CG C 33.80 . 1 239 44 44 GLU CD C 181.4 . 1 240 44 44 GLU N N 118.3 . 1 241 45 45 ILE C C 176.2 . 1 242 45 45 ILE CA C 61.40 . 1 243 45 45 ILE CB C 35.30 . 1 244 45 45 ILE CG1 C 29.20 . 1 245 45 45 ILE CG2 C 17.70 . 1 246 45 45 ILE CD1 C 10.10 . 1 247 45 45 ILE N N 122.7 . 1 248 46 46 ALA C C 179.2 . 1 249 46 46 ALA CA C 54.30 . 1 250 46 46 ALA CB C 17.70 . 1 251 46 46 ALA N N 121.6 . 1 252 47 47 ASP C C 177.6 . 1 253 47 47 ASP CA C 56.10 . 1 254 47 47 ASP CB C 40.50 . 1 255 47 47 ASP CG C 179.2 . 1 256 47 47 ASP N N 114.0 . 1 257 48 48 GLU C C 177.3 . 1 258 48 48 GLU CA C 58.30 . 1 259 48 48 GLU CB C 29.20 . 1 260 48 48 GLU CG C 35.10 . 1 261 48 48 GLU CD C 181.0 . 1 262 48 48 GLU N N 119.5 . 1 263 49 49 TYR C C 176.5 . 1 264 49 49 TYR CA C 55.60 . 1 265 49 49 TYR CB C 35.30 . 1 266 49 49 TYR CE1 C 117.9 . . 267 49 49 TYR N N 114.9 . 1 268 50 50 GLN C C 177.5 . 1 269 50 50 GLN CA C 57.50 . 1 270 50 50 GLN CB C 26.50 . 1 271 50 50 GLN CG C 30.80 . 1 272 50 50 GLN CD C 183.1 . 1 273 50 50 GLN N N 121.3 . 1 274 51 51 GLY C C 175.6 . 1 275 51 51 GLY CA C 41.40 . 1 276 51 51 GLY N N 116.6 . 1 277 52 52 LYS C C 176.5 . 1 278 52 52 LYS CA C 55.40 . 1 279 52 52 LYS CB C 34.80 . 1 280 52 52 LYS CG C 24.00 . 1 281 52 52 LYS CD C 28.80 . 1 282 52 52 LYS CE C 40.90 . 1 283 52 52 LYS N N 116.4 . 1 284 53 53 LEU C C 176.0 . 1 285 53 53 LEU CA C 53.70 . 1 286 53 53 LEU CB C 45.70 . 1 287 53 53 LEU CG C 23.30 . 1 288 53 53 LEU CD1 C 25.50 . . 289 53 53 LEU CD2 C 23.20 . . 290 53 53 LEU N N 118.6 . 1 291 54 54 THR C C 171.2 . 1 292 54 54 THR CA C 61.00 . 1 293 54 54 THR CB C 69.40 . 1 294 54 54 THR CG2 C 21.10 . 1 295 54 54 THR N N 123.3 . 1 296 55 55 VAL C C 171.7 . 1 297 55 55 VAL CA C 60.60 . 1 298 55 55 VAL CB C 32.00 . 1 299 55 55 VAL CG1 C 21.90 . . 300 55 55 VAL CG2 C 21.30 . . 301 55 55 VAL N N 129.4 . 1 302 56 56 ALA C C 174.7 . 1 303 56 56 ALA CA C 48.90 . 1 304 56 56 ALA CB C 23.50 . 1 305 56 56 ALA N N 128.3 . 1 306 57 57 LYS C C 174.8 . 1 307 57 57 LYS CA C 54.10 . 1 308 57 57 LYS CB C 44.30 . 1 309 57 57 LYS CG C 24.30 . 1 310 57 57 LYS CD C 26.40 . 1 311 57 57 LYS CE C 42.10 . 1 312 57 57 LYS N N 117.6 . 1 313 58 58 LEU C C 172.5 . 1 314 58 58 LEU CA C 52.60 . 1 315 58 58 LEU CB C 43.70 . 1 316 58 58 LEU CG C 27.70 . 1 317 58 58 LEU CD1 C 22.90 . . 318 58 58 LEU N N 123.5 . 1 319 59 59 ASN C C 175.2 . 1 320 59 59 ASN CA C 50.90 . 1 321 59 59 ASN CB C 37.70 . 1 322 59 59 ASN CG C 176.9 . 1 323 59 59 ASN N N 126.4 . 1 324 60 60 ILE C C 176.9 . 1 325 60 60 ILE CA C 62.70 . 1 326 60 60 ILE CB C 37.00 . 1 327 60 60 ILE CG1 C 24.30 . 1 328 60 60 ILE CG2 C 18.80 . 1 329 60 60 ILE CD1 C 14.50 . 1 330 60 60 ILE N N 120.8 . 1 331 61 61 ASP C C 176.3 . 1 332 61 61 ASP CA C 55.70 . 1 333 61 61 ASP CB C 39.90 . 1 334 61 61 ASP CG C 179.5 . 1 335 61 61 ASP N N 122.1 . 1 336 62 62 GLN C C 177.3 . 1 337 62 62 GLN CA C 57.40 . 1 338 62 62 GLN CB C 28.40 . 1 339 62 62 GLN CG C 31.30 . 1 340 62 62 GLN CD C 181.1 . 1 341 62 62 GLN N N 116.3 . 1 342 63 63 ASN C C 175.7 . 1 343 63 63 ASN CA C 50.80 . 1 344 63 63 ASN CB C 40.00 . 1 345 63 63 ASN CG C 178.1 . 1 346 63 63 ASN N N 116.3 . 1 347 64 64 PRO C C 177.7 . 1 348 64 64 PRO CA C 62.90 . 1 349 64 64 PRO CB C 32.10 . 1 350 64 64 PRO CG C 25.10 . 1 351 64 64 PRO CD C 49.00 . 1 352 64 64 PRO N N 128.4 . 1 353 65 65 GLY C C 173.7 . 1 354 65 65 GLY CA C 45.40 . 1 355 65 65 GLY N N 111.9 . 1 356 66 66 THR C C 175.4 . 1 357 66 66 THR CA C 68.90 . 1 358 66 66 THR CB C 67.40 . 1 359 66 66 THR CG2 C 19.40 . 1 360 66 66 THR N N 117.6 . 1 361 67 67 ALA C C 176.1 . 1 362 67 67 ALA CA C 56.30 . 1 363 67 67 ALA CB C 14.60 . 1 364 67 67 ALA N N 124.3 . 1 365 68 68 PRO C C 179.1 . 1 366 68 68 PRO CA C 64.80 . 1 367 68 68 PRO CB C 30.00 . 1 368 68 68 PRO CG C 28.10 . 1 369 68 68 PRO CD C 49.60 . 1 370 68 68 PRO N N 133.5 . 1 371 69 69 LYS C C 178.0 . 1 372 69 69 LYS CA C 57.10 . 1 373 69 69 LYS CB C 31.60 . 1 374 69 69 LYS CG C 21.50 . 1 375 69 69 LYS CD C 25.80 . 1 376 69 69 LYS CE C 39.90 . 1 377 69 69 LYS N N 117.1 . 1 378 70 70 TYR C C 177.2 . 1 379 70 70 TYR CA C 57.60 . 1 380 70 70 TYR CB C 38.90 . 1 381 70 70 TYR CG C 131.5 . 1 382 70 70 TYR CE2 C 116.8 . . 383 70 70 TYR N N 114.6 . 1 384 71 71 GLY C C 173.0 . 1 385 71 71 GLY CA C 45.90 . 1 386 71 71 GLY N N 107.1 . 1 387 72 72 ILE C C 176.1 . 1 388 72 72 ILE CA C 60.50 . 1 389 72 72 ILE CB C 35.50 . 1 390 72 72 ILE CG1 C 26.00 . 1 391 72 72 ILE CG2 C 17.50 . 1 392 72 72 ILE CD1 C 14.10 . 1 393 72 72 ILE N N 120.9 . 1 394 73 73 ARG C C 177.7 . 1 395 73 73 ARG CA C 57.70 . 1 396 73 73 ARG CB C 30.70 . 1 397 73 73 ARG CG C 24.70 . 1 398 73 73 ARG CD C 41.20 . 1 399 73 73 ARG CZ C 158.3 . 1 400 73 73 ARG N N 128.4 . 1 401 74 74 GLY C C 172.0 . 1 402 74 74 GLY CA C 43.80 . 1 403 74 74 GLY N N 108.1 . 1 404 75 75 ILE C C 175.8 . 1 405 75 75 ILE CA C 56.90 . 1 406 75 75 ILE CB C 40.20 . 1 407 75 75 ILE CG1 C 21.60 . 1 408 75 75 ILE CG2 C 19.50 . 1 409 75 75 ILE CD1 C 17.10 . 1 410 75 75 ILE N N 113.5 . 1 411 76 76 PRO C C 178.0 . 1 412 76 76 PRO CA C 62.70 . 1 413 76 76 PRO CB C 32.40 . 1 414 76 76 PRO CG C 25.60 . 1 415 76 76 PRO CD C 49.10 . 1 416 76 76 PRO N N 130.9 . 1 417 77 77 THR C C 171.6 . 1 418 77 77 THR CA C 62.80 . 1 419 77 77 THR CB C 71.80 . 1 420 77 77 THR CG2 C 21.80 . 1 421 77 77 THR N N 118.7 . 1 422 78 78 LEU C C 173.9 . 1 423 78 78 LEU CA C 52.20 . 1 424 78 78 LEU CB C 43.70 . 1 425 78 78 LEU CG C 26.50 . 1 426 78 78 LEU CD1 C 26.50 . . 427 78 78 LEU CD2 C 22.50 . . 428 78 78 LEU N N 127.5 . 1 429 79 79 LEU C C 172.7 . 1 430 79 79 LEU CA C 51.90 . 1 431 79 79 LEU CB C 44.40 . 1 432 79 79 LEU CG C 26.10 . 1 433 79 79 LEU CD1 C 24.20 . . 434 79 79 LEU CD2 C 23.70 . . 435 79 79 LEU N N 123.1 . 1 436 80 80 LEU C C 174.1 . 1 437 80 80 LEU CA C 51.90 . 1 438 80 80 LEU CB C 43.80 . 1 439 80 80 LEU CG C 25.90 . 1 440 80 80 LEU CD1 C 25.90 . . 441 80 80 LEU CD2 C 22.90 . . 442 80 80 LEU N N 125.5 . 1 443 81 81 PHE C C 176.4 . 1 444 81 81 PHE CA C 57.50 . 1 445 81 81 PHE CB C 39.60 . 1 446 81 81 PHE CG C 140.1 . 1 447 81 81 PHE CD1 C 132.6 . . 448 81 81 PHE CD2 C 131.6 . . 449 81 81 PHE N N 127.7 . 1 450 82 82 LYS C C 176.7 . 1 451 82 82 LYS CA C 55.30 . 1 452 82 82 LYS CB C 34.20 . 1 453 82 82 LYS CG C 23.70 . 1 454 82 82 LYS CD C 26.80 . 1 455 82 82 LYS CE C 41.10 . 1 456 82 82 LYS N N 117.3 . 1 457 83 83 ASN C C 175.2 . 1 458 83 83 ASN CA C 53.40 . 1 459 83 83 ASN CB C 33.50 . 1 460 83 83 ASN CG C 176.5 . 1 461 83 83 ASN N N 126.9 . 1 462 84 84 GLY C C 173.5 . 1 463 84 84 GLY CA C 45.60 . 1 464 84 84 GLY N N 104.1 . 1 465 85 85 GLU C C 177.9 . 1 466 85 85 GLU CA C 52.80 . 1 467 85 85 GLU CB C 31.90 . 1 468 85 85 GLU CG C 34.20 . 1 469 85 85 GLU CD C 181.9 . 1 470 85 85 GLU N N 118.6 . 1 471 86 86 VAL C C 175.5 . 1 472 86 86 VAL CA C 63.50 . 1 473 86 86 VAL CB C 30.90 . 1 474 86 86 VAL CG1 C 22.60 . . 475 86 86 VAL CG2 C 22.40 . . 476 86 86 VAL N N 123.1 . 1 477 87 87 ALA C C 177.2 . 1 478 87 87 ALA CA C 51.70 . 1 479 87 87 ALA CB C 19.60 . 1 480 87 87 ALA N N 133.3 . 1 481 88 88 ALA C C 174.5 . 1 482 88 88 ALA CA C 51.50 . 1 483 88 88 ALA CB C 21.60 . 1 484 88 88 ALA N N 118.4 . 1 485 89 89 THR C C 171.3 . 1 486 89 89 THR CA C 63.20 . 1 487 89 89 THR CB C 71.40 . 1 488 89 89 THR CG2 C 21.90 . 1 489 89 89 THR N N 116.4 . 1 490 90 90 LYS C C 173.3 . 1 491 90 90 LYS CA C 53.20 . 1 492 90 90 LYS CB C 32.10 . 1 493 90 90 LYS CG C 22.30 . 1 494 90 90 LYS CD C 26.00 . 1 495 90 90 LYS CE C 39.50 . 1 496 90 90 LYS N N 126.7 . 1 497 91 91 VAL C C 173.8 . 1 498 91 91 VAL CA C 60.80 . 1 499 91 91 VAL CB C 33.20 . 1 500 91 91 VAL CG1 C 22.20 . . 501 91 91 VAL CG2 C 22.10 . . 502 91 91 VAL N N 126.4 . 1 503 92 92 GLY C C 170.1 . 1 504 92 92 GLY CA C 40.20 . 1 505 92 92 GLY N N 113.9 . 1 506 93 93 ALA C C 176.9 . 1 507 93 93 ALA CA C 50.70 . 1 508 93 93 ALA CB C 19.70 . 1 509 93 93 ALA N N 118.8 . 1 510 94 94 LEU C C 174.6 . 1 511 94 94 LEU CA C 52.00 . 1 512 94 94 LEU CB C 42.60 . 1 513 94 94 LEU CG C 25.80 . 1 514 94 94 LEU CD1 C 25.80 . . 515 94 94 LEU CD2 C 21.50 . . 516 94 94 LEU N N 119.8 . 1 517 95 95 SER C C 174.6 . 1 518 95 95 SER CA C 55.30 . 1 519 95 95 SER CB C 65.50 . 1 520 95 95 SER N N 118.5 . 1 521 96 96 LYS C C 177.7 . 1 522 96 96 LYS CA C 60.00 . 1 523 96 96 LYS CB C 31.20 . 1 524 96 96 LYS CG C 24.60 . 1 525 96 96 LYS CD C 28.30 . 1 526 96 96 LYS CE C 40.40 . 1 527 96 96 LYS N N 120.6 . 1 528 97 97 GLY C C 176.8 . 1 529 97 97 GLY CA C 46.30 . 1 530 97 97 GLY N N 105.4 . 1 531 98 98 GLN C C 178.0 . 1 532 98 98 GLN CA C 58.10 . 1 533 98 98 GLN CB C 27.70 . 1 534 98 98 GLN CG C 31.20 . 1 535 98 98 GLN CD C 179.2 . 1 536 98 98 GLN N N 120.3 . 1 537 99 99 LEU C C 176.0 . 1 538 99 99 LEU CA C 57.20 . 1 539 99 99 LEU CB C 40.30 . 1 540 99 99 LEU CG C 26.40 . 1 541 99 99 LEU CD1 C 25.70 . . 542 99 99 LEU CD2 C 21.90 . . 543 99 99 LEU N N 123.2 . 1 544 100 100 LYS C C 177.1 . 1 545 100 100 LYS CA C 59.90 . 1 546 100 100 LYS CB C 30.70 . 1 547 100 100 LYS CD C 25.70 . 1 548 100 100 LYS CE C 41.70 . 1 549 100 100 LYS N N 119.0 . 1 550 101 101 GLU C C 179.3 . 1 551 101 101 GLU CA C 58.00 . 1 552 101 101 GLU CB C 28.60 . 1 553 101 101 GLU CG C 33.80 . 1 554 101 101 GLU CD C 182.1 . 1 555 101 101 GLU N N 117.1 . 1 556 102 102 PHE C C 176.5 . 1 557 102 102 PHE CA C 59.30 . 1 558 102 102 PHE CB C 38.20 . 1 559 102 102 PHE CG C 137.7 . 1 560 102 102 PHE CD1 C 131.7 . . 561 102 102 PHE N N 120.3 . 1 562 103 103 LEU C C 176.6 . 1 563 103 103 LEU CA C 55.80 . 1 564 103 103 LEU CB C 39.80 . 1 565 103 103 LEU CG C 22.40 . 1 566 103 103 LEU CD1 C 22.30 . . 567 103 103 LEU CD2 C 18.40 . . 568 103 103 LEU N N 121.1 . 1 569 104 104 ASP C C 176.4 . 1 570 104 104 ASP CA C 55.60 . 1 571 104 104 ASP CB C 39.40 . 1 572 104 104 ASP CG C 180.8 . 1 573 104 104 ASP N N 119.9 . 1 574 105 105 ALA C C 177.7 . 1 575 105 105 ALA CA C 53.10 . 1 576 105 105 ALA CB C 18.30 . 1 577 105 105 ALA N N 117.6 . 1 578 106 106 ASN C C 175.4 . 1 579 106 106 ASN CA C 53.80 . 1 580 106 106 ASN CB C 41.70 . 1 581 106 106 ASN CG C 176.0 . 1 582 106 106 ASN N N 112.2 . 1 583 107 107 LEU C C 173.7 . 1 584 107 107 LEU CA C 52.20 . 1 585 107 107 LEU CB C 44.60 . 1 586 107 107 LEU CG C 23.60 . 1 587 107 107 LEU CD1 C 23.60 . . 588 107 107 LEU CD2 C 26.00 . . 589 107 107 LEU N N 121.1 . 1 590 108 108 ALA C C 178.4 . 1 591 108 108 ALA CA C 53.50 . 1 592 108 108 ALA CB C 18.90 . 1 593 108 108 ALA N N 127.7 . 1 stop_ save_