data_15156 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solid-State Protein Structure Determination with Proton-Detected Triple Resonance 3D Magic-Angle Spinning NMR Spectroscopy: Beta-1 Immunoglobulin Binding Domain of Protein G (GB1) ; _BMRB_accession_number 15156 _BMRB_flat_file_name bmr15156.str _Entry_type original _Submission_date 2007-03-01 _Accession_date 2007-03-01 _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 Zhou Donghua H. . 2 Shea John J. . 3 Nieuwkoop Andrew J. . 4 Franks 'W. Trent' . . 5 Wylie Benjamin J. . 6 Mullen Charles . . 7 Sandoz Dennis . . 8 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 66 "13C chemical shifts" 333 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-27 update BMRB 'update related entry loop' 2007-08-22 update author 'add new chemical shift set' 2007-06-27 update author 'update the chemical shifts' 2007-03-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16873 'NMR determination of protein pKa values in the solid state' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solid-State Protein Structure Determination with Proton-Detected Triple Resonance 3D Magic-Angle Spinning NMR Spectroscopy ; _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Donghua H. . 2 Shea John J. . 3 Nieuwkoop Andrew J. . 4 Franks 'W. Trent' . . 5 Wylie Benjamin J. . 6 Mullen Charles . . 7 Sandoz Dennis . . 8 Rienstra Chad M. . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ####################################### # Cited references within the entry # ####################################### save_entry_citation_2 _Saveframe_category citation _Citation_full . _Citation_title ; Magic Angle Spinning Solid-State NMR of the Beta-1 Immunoglobulin Binding Domain of Protein G (GB1): 15N and 13C Chemical Shift Assignments and Conformational Analysi ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16131207 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Franks 'W Trent' . . 2 Zhou Donghua H. . 3 Wylie Benjamin J. . 4 Money Brian G. . 5 Graesser Daniel T. . 6 Frericks Heather L. . 7 Sahota Gurmukh . . 8 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full . _Journal_volume 127 _Journal_issue 35 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 12291 _Page_last 12305 _Year 2005 _Details . loop_ _Keyword Assignments dynamics GB1 Solid SSNMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name GB1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monomer $GB1 stop_ _System_molecular_weight 6222 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Precipitated beta-1 immunoglobulin binding domain of protein G (GB1)' save_ ######################## # Monomeric polymers # ######################## save_GB1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GB1 _Molecular_mass 6228.870 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 TYR 4 LYS 5 LEU 6 ILE 7 LEU 8 ASN 9 GLY 10 LYS 11 THR 12 LEU 13 LYS 14 GLY 15 GLU 16 THR 17 THR 18 THR 19 GLU 20 ALA 21 VAL 22 ASP 23 ALA 24 ALA 25 THR 26 ALA 27 GLU 28 LYS 29 VAL 30 PHE 31 LYS 32 GLN 33 TYR 34 ALA 35 ASN 36 ASP 37 ASN 38 GLY 39 VAL 40 ASP 41 GLY 42 GLU 43 TRP 44 THR 45 TYR 46 ASP 47 ASP 48 ALA 49 THR 50 LYS 51 THR 52 PHE 53 THR 54 VAL 55 THR 56 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 15380 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 16444 SC35 100.00 158 100.00 100.00 2.49e-30 BMRB 16627 Protein_GB1_(2Q6I) 100.00 56 100.00 100.00 3.39e-30 BMRB 16755 N40 67.86 40 100.00 100.00 2.26e-16 BMRB 16873 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 16882 "Ubiquitin-Binding Motif" 100.00 108 100.00 100.00 2.56e-30 BMRB 16958 ZCCHC9 100.00 164 100.00 100.00 1.75e-30 BMRB 17810 entity 100.00 56 100.00 100.00 3.39e-30 BMRB 18397 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 19394 GB1-UBM1 100.00 106 100.00 100.00 1.24e-30 BMRB 26630 Protein_G_Domain_Beta-1_Wild_Type 100.00 64 98.21 98.21 1.21e-29 PDB 1GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 1IBX "Nmr Structure Of Dff40 And Dff45 N-Terminal Domain Complex" 100.00 145 100.00 100.00 4.44e-30 PDB 1PGA "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptococcal Protein G And Comparison With Nmr" 100.00 56 98.21 98.21 4.07e-29 PDB 1PGB "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptoccocal Protein G And Comparison With Nmr" 100.00 56 98.21 98.21 4.07e-29 PDB 1PN5 "Nmr Structure Of The Nalp1 Pyrin Domain (Pyd)" 100.00 159 100.00 100.00 2.94e-30 PDB 2CWB "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" 98.21 108 98.18 98.18 1.46e-28 PDB 2DEN "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" 98.21 108 98.18 98.18 1.46e-28 PDB 2GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 2GI9 "Backbone Conformational Constraints In A Microcrystalline U- 15n-Labeled Protein By 3d Dipolar-Shift Solid-State Nmr Spectrosco" 100.00 56 100.00 100.00 3.39e-30 PDB 2I2Y "Solution Structure Of The Rrm Of Srp20 Bound To The Rna Cauc" 100.00 150 100.00 100.00 5.69e-30 PDB 2I38 "Solution Structure Of The Rrm Of Srp20" 100.00 150 100.00 100.00 6.01e-30 PDB 2JSV "Dipole Tensor-Based Refinement For Atomic-Resolution Structure Determination Of A Nanocrystalline Protein By Solid-State Nmr Sp" 100.00 56 100.00 100.00 3.39e-30 PDB 2JU6 "Solid-State Protein Structure Determination With Proton- Detected Triple Resonance 3d Magic-Angle Spinning Nmr Spectroscopy" 100.00 56 100.00 100.00 3.39e-30 PDB 2K0P "Determination Of A Protein Structure In The Solid State From Nmr Chemical Shifts" 100.00 56 100.00 100.00 3.39e-30 PDB 2KBT "Attachment Of An Nmr-Invisible Solubility Enhancement Tag (Inset) Using A Sortase-Mediated Protein Ligation Method" 100.00 142 98.21 98.21 1.28e-28 PDB 2KHU "Solution Structure Of The Ubiquitin-Binding Motif Of Human Polymerase Iota" 100.00 108 100.00 100.00 2.56e-30 PDB 2KHW "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" 100.00 108 100.00 100.00 2.56e-30 PDB 2KLK "Solution Structure Of Gb1 A34f Mutant With Rdc And Saxs" 100.00 56 98.21 98.21 3.94e-29 PDB 2KN4 "The Structure Of The Rrm Domain Of Sc35" 100.00 158 100.00 100.00 2.49e-30 PDB 2KQ4 "Atomic Resolution Protein Structure Determination By Three- Dimensional Transferred Echo Double Resonance Solid-State Nuclear M" 100.00 56 100.00 100.00 3.39e-30 PDB 2KWD "Supramolecular Protein Structure Determination By Site-Speci Range Intermolecular Solid State Nmr Spectroscopy" 100.00 56 100.00 100.00 3.39e-30 PDB 2LGI "Atomic Resolution Protein Structures Using Nmr Chemical Shift Tensors" 100.00 56 100.00 100.00 3.39e-30 PDB 2MBB "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" 100.00 106 100.00 100.00 1.24e-30 PDB 2PLP "Ultra High Resolution Backbone Conformation Of Protein Gb1 From Residual Dipolar Couplings Alone" 94.64 54 100.00 100.00 1.50e-27 PDB 2QMT "Crystal Polymorphism Of Protein Gb1 Examined By Solid-State Nmr And X-Ray Diffraction" 100.00 56 100.00 100.00 3.39e-30 PDB 2RMM "Solution Structure Of Gb1 A34f Mutant" 100.00 56 98.21 98.21 3.94e-29 PDB 3GB1 "Structures Of B1 Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 3MP9 "Structure Of Streptococcal Protein G B1 Domain At Ph 3.0" 96.43 64 100.00 100.00 7.03e-29 PDB 3UI3 "Structural And Biochemical Characterization Of Hp0315 From Helicobacter Pylori As A Vapd Protein With An Endoribonuclease Activ" 98.21 160 100.00 100.00 1.11e-28 PDB 4Q0C "3.1 A Resolution Crystal Structure Of The B. Pertussis Bvgs Periplasmic Domain" 100.00 584 98.21 98.21 1.54e-27 EMBL CAA37410 "Protein G' [Streptococcus sp. 'group G']" 80.36 185 97.78 100.00 8.21e-20 GB AAY41168 "protein G/SspDnaE fusion protein [Expression vector pJJDuet30]" 100.00 201 98.21 100.00 2.69e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Variant $GB1 'Micrococcus pyogenes' 1280 Bacteria . Staphylococcus aureus T2Q 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 _Details $GB1 'recombinant technology' . Escherichia coli . n/a 'Synthetic GB1 T2Q (Smith, Withka, Regan, Biochemistry 1994, 33, 5510-5517 )' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details 'Microcrystalline GB1' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GB1 10 mg '[U-100% 13C; U-100% 15N]' 'Methyl Pentane diol' 0.5 v/v 'natural abundance' Isopropanol 0.25 v/v 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type 'polycrystalline powder' _Details 'Back exchanged with H20' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GB1 5 mg '[U-13C; U-15N; U-2H]' 'isopropyl alcohol' 50 % 'natural abundance' (4R)-2-Methylpentane-2,4-diol 25 % 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' 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' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_Spinsight _Saveframe_category software _Name Spinsight _Version . loop_ _Vendor _Address _Electronic_address Spinsight(Varian) . . stop_ loop_ _Task collection 'data analysis' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.16.0 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'geometry optimization' refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Infinity Plus' _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_CC_DARR_mixing_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR mixing' _Sample_label $sample_1 save_ save_2D_N(CA)CX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N(CA)CX' _Sample_label $sample_1 save_ save_2D_N(CO)CX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N(CO)CX' _Sample_label $sample_1 save_ save_3D_NCACX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_3D_CAN(COCX)_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CAN(COCX)' _Sample_label $sample_1 save_ save_2D_CC_SPC5_DQ_mixing_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC SPC5 DQ mixing' _Sample_label $sample_1 save_ save_2D_NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NH' _Sample_label $sample_2 save_ save_3D_CON(H)H_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CON(H)H' _Sample_label $sample_2 save_ save_3D_HN(H)H_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(H)H' _Sample_label $sample_2 save_ save_2D_N(H)H_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D N(H)H' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pressure 1 . atm temperature 278 . K 'temperature controller setting' 273 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . pH pressure 1 . atm temperature 281 2 K 'temperature controller setting' 263 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; All shifts are referenced to the CH peak of solid adamantane at 40.48ppm accd. to the recomendations of Morcombe and Zilm (JMR 165, 165-174). ; 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 _Reference_correction_type _Correction_value adamantane C 13 'alkane (CH) carbon' ppm 40.48 external direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' 'Magic Angle' 1.0 n/a 0.0 adamantane N 15 'alkane (CH) carbon' ppm 40.48 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' 'Magic Angle' . n/a 0.0 stop_ save_ save_chemical_shift_reference_2 _Saveframe_category chemical_shift_reference _Details ; Reference to DSS indirectly, using adamantane low field 13C peak (40.48 ppm) as a secondary reference, according to C. R. Morcomebe and K. W. Zilm, 2003, J. Magn. Reson., 162, 479-486. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR mixing' '2D N(CA)CX' '2D N(CO)CX' '3D NCACX' '3D NCOCX' '3D CAN(COCX)' '2D CC SPC5 DQ mixing' 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 monomer _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 MET C C 171.36 0.09 1 2 1 1 MET CA C 54.33 0.08 1 3 1 1 MET CB C 32.50 0.03 1 4 1 1 MET CG C 30.25 0.07 1 5 1 1 MET CE C 15.87 0.02 1 6 1 1 MET N N 39.95 0.03 1 7 2 2 GLN C C 175.08 0.10 1 8 2 2 GLN CA C 55.88 0.05 1 9 2 2 GLN CB C 30.45 0.05 1 10 2 2 GLN CG C 35.34 0.06 1 11 2 2 GLN CD C 180.44 0.07 1 12 2 2 GLN N N 125.24 0.07 1 13 2 2 GLN NE2 N 113.22 0.03 1 14 3 3 TYR C C 174.98 0.08 1 15 3 3 TYR CA C 57.01 0.04 1 16 3 3 TYR CB C 43.67 0.10 1 17 3 3 TYR CG C 128.52 0.16 1 18 3 3 TYR CD1 C 134.72 0.11 3 19 3 3 TYR CD2 C 131.97 0.11 3 20 3 3 TYR CE1 C 118.34 0.07 3 21 3 3 TYR CE2 C 118.34 0.07 3 22 3 3 TYR CZ C 158.33 0.19 3 23 3 3 TYR N N 123.34 0.08 1 24 4 4 LYS C C 173.31 0.09 1 25 4 4 LYS CA C 54.88 0.08 1 26 4 4 LYS CB C 36.25 0.09 1 27 4 4 LYS CG C 25.65 0.08 1 28 4 4 LYS CD C 29.08 0.06 1 29 4 4 LYS CE C 42.37 0.04 1 30 4 4 LYS N N 122.67 0.06 1 31 4 4 LYS NZ N 33.14 0.10 1 32 5 5 LEU C C 174.80 0.07 1 33 5 5 LEU CA C 52.97 0.05 1 34 5 5 LEU CB C 42.54 0.08 1 35 5 5 LEU CG C 27.44 0.05 1 36 5 5 LEU CD1 C 25.95 0.08 2 37 5 5 LEU CD2 C 25.05 0.05 2 38 5 5 LEU N N 126.98 0.05 1 39 6 6 ILE C C 175.31 0.08 1 40 6 6 ILE CA C 59.97 0.07 1 41 6 6 ILE CB C 37.85 0.07 1 42 6 6 ILE CG1 C 27.47 0.07 1 43 6 6 ILE CG2 C 17.59 0.05 1 44 6 6 ILE CD1 C 12.77 0.04 1 45 6 6 ILE N N 126.26 0.07 1 46 7 7 LEU C C 175.12 0.04 1 47 7 7 LEU CA C 54.66 0.10 1 48 7 7 LEU CB C 42.90 0.07 1 49 7 7 LEU CG C 27.18 0.09 1 50 7 7 LEU CD1 C 26.94 0.09 2 51 7 7 LEU CD2 C 25.11 0.03 2 52 7 7 LEU N N 127.08 0.05 1 53 8 8 ASN C C 176.43 0.05 1 54 8 8 ASN CA C 50.72 0.07 1 55 8 8 ASN CB C 38.37 0.10 1 56 8 8 ASN CG C 176.55 0.04 1 57 8 8 ASN N N 125.11 0.07 1 58 8 8 ASN ND2 N 110.85 0.08 1 59 9 9 GLY C C 173.22 0.08 1 60 9 9 GLY CA C 44.58 0.05 1 61 9 9 GLY N N 109.62 0.03 1 62 10 10 LYS C C 179.17 0.07 1 63 10 10 LYS CA C 59.27 0.05 1 64 10 10 LYS CB C 32.85 0.07 1 65 10 10 LYS CG C 25.83 0.06 1 66 10 10 LYS CD C 29.15 0.09 1 67 10 10 LYS CE C 42.07 0.07 1 68 10 10 LYS N N 121.07 0.08 1 69 10 10 LYS NZ N 33.13 0.06 1 70 11 11 THR C C 173.42 0.09 1 71 11 11 THR CA C 61.91 0.05 1 72 11 11 THR CB C 69.49 0.05 1 73 11 11 THR CG2 C 22.63 0.07 1 74 11 11 THR N N 106.40 0.05 1 75 12 12 LEU C C 173.85 0.07 1 76 12 12 LEU CA C 54.43 0.07 1 77 12 12 LEU CB C 43.07 0.07 1 78 12 12 LEU CG C 27.93 0.08 1 79 12 12 LEU CD1 C 26.09 0.07 2 80 12 12 LEU CD2 C 23.01 0.05 2 81 12 12 LEU N N 127.76 0.06 1 82 13 13 LYS C C 175.83 0.06 1 83 13 13 LYS CA C 53.34 0.06 1 84 13 13 LYS CB C 38.83 0.09 1 85 13 13 LYS CG C 26.12 0.08 1 86 13 13 LYS CD C 29.76 0.02 1 87 13 13 LYS CE C 43.00 0.10 1 88 13 13 LYS N N 123.25 0.06 1 89 13 13 LYS NZ N 31.33 0.10 1 90 14 14 GLY C C 171.37 0.10 1 91 14 14 GLY CA C 44.89 0.08 1 92 14 14 GLY N N 105.61 0.07 1 93 15 15 GLU C C 174.11 0.09 1 94 15 15 GLU CA C 53.89 0.06 1 95 15 15 GLU CB C 34.16 0.08 1 96 15 15 GLU CG C 35.14 0.10 1 97 15 15 GLU CD C 181.88 0.10 1 98 15 15 GLU N N 121.07 0.05 1 99 16 16 THR C C 172.04 0.09 1 100 16 16 THR CA C 60.12 0.06 1 101 16 16 THR CB C 70.51 0.06 1 102 16 16 THR CG2 C 20.07 0.08 1 103 16 16 THR N N 115.18 0.08 1 104 17 17 THR C C 174.25 0.07 1 105 17 17 THR CA C 60.32 0.10 1 106 17 17 THR CB C 72.64 0.07 1 107 17 17 THR CG2 C 21.79 0.10 1 108 17 17 THR N N 116.05 0.07 1 109 18 18 THR C C 171.27 0.06 1 110 18 18 THR CA C 61.31 0.08 1 111 18 18 THR CB C 70.84 0.04 1 112 18 18 THR CG2 C 18.91 0.08 1 113 18 18 THR N N 116.26 0.08 1 114 19 19 GLU C C 175.90 0.08 1 115 19 19 GLU CA C 54.33 0.08 1 116 19 19 GLU CB C 30.56 0.10 1 117 19 19 GLU CG C 35.75 0.06 1 118 19 19 GLU CD C 182.18 0.08 1 119 19 19 GLU N N 125.35 0.10 1 120 20 20 ALA C C 177.79 0.09 1 121 20 20 ALA CA C 50.69 0.04 1 122 20 20 ALA CB C 23.67 0.04 1 123 20 20 ALA N N 125.88 0.04 1 124 21 21 VAL C C 175.10 0.10 1 125 21 21 VAL CA C 63.47 0.10 1 126 21 21 VAL CB C 31.96 0.10 1 127 21 21 VAL CG1 C 20.20 0.10 2 128 21 21 VAL CG2 C 21.22 0.10 2 129 21 21 VAL N N 116.28 0.09 1 130 22 22 ASP C C 175.08 0.09 1 131 22 22 ASP CA C 52.53 0.07 1 132 22 22 ASP CB C 42.30 0.09 1 133 22 22 ASP CG C 179.88 0.04 1 134 22 22 ASP N N 115.52 0.07 1 135 23 23 ALA C C 179.73 0.04 1 136 23 23 ALA CA C 54.55 0.07 1 137 23 23 ALA CB C 18.20 0.04 1 138 23 23 ALA N N 122.82 0.05 1 139 24 24 ALA C C 181.53 0.09 1 140 24 24 ALA CA C 54.54 0.07 1 141 24 24 ALA CB C 18.20 0.07 1 142 24 24 ALA N N 120.75 0.04 1 143 25 25 THR C C 175.92 0.06 1 144 25 25 THR CA C 67.23 0.12 1 145 25 25 THR CB C 67.82 0.11 1 146 25 25 THR CG2 C 21.38 0.08 1 147 25 25 THR N N 117.37 0.07 1 148 26 26 ALA C C 177.28 0.07 1 149 26 26 ALA CA C 55.02 0.09 1 150 26 26 ALA CB C 17.55 0.09 1 151 26 26 ALA N N 123.99 0.08 1 152 27 27 GLU C C 177.82 0.07 1 153 27 27 GLU CA C 59.09 0.05 1 154 27 27 GLU CB C 29.06 0.08 1 155 27 27 GLU CG C 35.54 0.07 1 156 27 27 GLU CD C 181.73 0.08 1 157 27 27 GLU N N 116.35 0.04 1 158 28 28 LYS C C 179.24 0.04 1 159 28 28 LYS CA C 60.19 0.05 1 160 28 28 LYS CB C 32.79 0.05 1 161 28 28 LYS CG C 26.47 0.08 1 162 28 28 LYS CD C 30.07 0.07 1 163 28 28 LYS CE C 42.282 0.03 1 164 28 28 LYS N N 117.38 0.06 1 165 28 28 LYS NZ N 32.57 0.10 1 166 29 29 VAL C C 178.98 0.09 1 167 29 29 VAL CA C 66.31 0.08 1 168 29 29 VAL CB C 31.92 0.07 1 169 29 29 VAL CG1 C 22.19 0.06 2 170 29 29 VAL CG2 C 20.99 0.04 2 171 29 29 VAL N N 119.34 0.05 1 172 30 30 PHE C C 179.09 0.20 1 173 30 30 PHE CA C 57.54 0.06 1 174 30 30 PHE CB C 37.49 0.07 1 175 30 30 PHE CG C 138.38 0.20 1 176 30 30 PHE CD1 C 132.33 0.23 3 177 30 30 PHE CD2 C 132.33 0.23 3 178 30 30 PHE CE1 C 130.90 0.35 3 179 30 30 PHE CE2 C 130.90 0.35 3 180 30 30 PHE CZ C 130.90 0.35 1 181 30 30 PHE N N 118.68 0.07 1 182 31 31 LYS C C 179.57 0.09 1 183 31 31 LYS CA C 60.11 0.07 1 184 31 31 LYS CB C 31.61 0.08 1 185 31 31 LYS CG C 27.25 0.08 1 186 31 31 LYS CD C 29.30 0.06 1 187 31 31 LYS CE C 41.24 0.10 1 188 31 31 LYS N N 120.76 0.05 1 189 31 31 LYS NZ N 32.20 0.08 1 190 32 32 GLN C C 177.58 0.08 1 191 32 32 GLN CA C 58.92 0.06 1 192 32 32 GLN CB C 28.97 0.06 1 193 32 32 GLN CG C 34.18 0.09 1 194 32 32 GLN CD C 180.04 0.05 1 195 32 32 GLN N N 121.29 0.03 1 196 32 32 GLN NE2 N 115.61 0.06 1 197 33 33 TYR C C 178.82 0.07 1 198 33 33 TYR CA C 61.59 0.04 1 199 33 33 TYR CB C 36.98 0.19 1 200 33 33 TYR CG C 129.82 0.13 1 201 33 33 TYR CD1 C 132.53 0.10 3 202 33 33 TYR CD2 C 132.53 0.10 3 203 33 33 TYR CE1 C 118.69 0.19 3 204 33 33 TYR CE2 C 118.69 0.19 3 205 33 33 TYR CZ C 159.36 0.09 1 206 33 33 TYR N N 120.99 0.04 1 207 34 34 ALA C C 179.62 0.08 1 208 34 34 ALA CA C 56.07 0.05 1 209 34 34 ALA CB C 18.10 0.05 1 210 34 34 ALA N N 122.68 0.04 1 211 35 35 ASN C C 179.56 0.10 1 212 35 35 ASN CA C 57.04 0.09 1 213 35 35 ASN CB C 39.25 0.09 1 214 35 35 ASN CG C 176.11 0.07 1 215 35 35 ASN N N 118.20 0.06 1 216 35 35 ASN ND2 N 113.20 0.08 1 217 36 36 ASP C C 176.18 0.04 1 218 36 36 ASP CA C 55.91 0.06 1 219 36 36 ASP CB C 38.31 0.06 1 220 36 36 ASP CG C 177.80 0.10 1 221 36 36 ASP N N 121.08 0.05 1 222 37 37 ASN C C 174.28 0.08 1 223 37 37 ASN CA C 53.51 0.05 1 224 37 37 ASN CB C 40.35 0.08 1 225 37 37 ASN CG C 176.88 0.08 1 226 37 37 ASN N N 115.04 0.07 1 227 37 37 ASN ND2 N 114.59 0.08 1 228 38 38 GLY C C 174.03 0.08 1 229 38 38 GLY CA C 46.80 0.07 1 230 38 38 GLY N N 108.35 0.05 1 231 39 39 VAL C C 175.20 0.10 1 232 39 39 VAL CA C 61.72 0.07 1 233 39 39 VAL CB C 31.94 0.07 1 234 39 39 VAL CG1 C 21.94 0.04 1 235 39 39 VAL CG2 C 18.20 0.04 1 236 39 39 VAL N N 121.79 0.05 1 237 40 40 ASP C C 174.89 0.08 1 238 40 40 ASP CA C 52.77 0.05 1 239 40 40 ASP CB C 41.71 0.06 1 240 40 40 ASP CG C 180.73 0.10 1 241 40 40 ASP N N 131.05 0.04 1 242 41 41 GLY C C 172.81 0.08 1 243 41 41 GLY CA C 45.10 0.08 1 244 41 41 GLY N N 108.10 0.03 1 245 42 42 GLU C C 177.94 0.08 1 246 42 42 GLU CA C 55.10 0.09 1 247 42 42 GLU CB C 31.48 0.09 1 248 42 42 GLU CG C 35.68 0.13 1 249 42 42 GLU CD C 181.82 0.07 1 250 42 42 GLU N N 119.02 0.05 1 251 43 43 TRP C C 177.42 0.08 1 252 43 43 TRP CA C 57.46 0.06 1 253 43 43 TRP CB C 33.81 0.08 1 254 43 43 TRP CG C 111.78 0.07 1 255 43 43 TRP CD1 C 127.17 0.08 1 256 43 43 TRP CD2 C 129.71 0.05 1 257 43 43 TRP CE2 C 138.49 0.05 1 258 43 43 TRP CE3 C 119.87 0.09 1 259 43 43 TRP CZ2 C 114.71 0.09 1 260 43 43 TRP CZ3 C 120.63 0.06 1 261 43 43 TRP CH2 C 123.17 0.06 1 262 43 43 TRP N N 124.95 0.06 1 263 43 43 TRP NE1 N 131.65 0.12 1 264 44 44 THR C C 174.03 0.06 1 265 44 44 THR CA C 60.94 0.10 1 266 44 44 THR CB C 73.09 0.06 1 267 44 44 THR CG2 C 21.12 0.10 1 268 44 44 THR N N 109.21 0.08 1 269 45 45 TYR C C 171.91 0.09 1 270 45 45 TYR CA C 57.84 0.06 1 271 45 45 TYR CB C 42.62 0.05 1 272 45 45 TYR CG C 127.79 0.06 1 273 45 45 TYR CD1 C 132.51 0.06 3 274 45 45 TYR CD2 C 132.19 0.16 3 275 45 45 TYR CE1 C 118.79 0.08 3 276 45 45 TYR CE2 C 116.22 0.06 3 277 45 45 TYR CZ C 157.53 0.10 1 278 45 45 TYR N N 118.61 0.08 1 279 46 46 ASP C C 176.30 0.06 1 280 46 46 ASP CA C 50.89 0.05 1 281 46 46 ASP CB C 42.60 0.07 1 282 46 46 ASP CG C 180.17 0.08 1 283 46 46 ASP N N 126.34 0.06 1 284 47 47 ASP C C 177.51 0.09 1 285 47 47 ASP CA C 54.64 0.07 1 286 47 47 ASP CB C 43.00 0.08 1 287 47 47 ASP CG C 179.84 0.07 1 288 47 47 ASP N N 123.39 0.03 1 289 48 48 ALA C C 179.70 0.05 1 290 48 48 ALA CA C 53.99 0.04 1 291 48 48 ALA CB C 19.00 0.04 1 292 48 48 ALA N N 118.98 0.06 1 293 49 49 THR C C 175.84 0.09 1 294 49 49 THR CA C 60.27 0.08 1 295 49 49 THR CB C 69.90 0.06 1 296 49 49 THR CG2 C 21.57 0.05 1 297 49 49 THR N N 104.23 0.03 1 298 50 50 LYS C C 175.47 0.10 1 299 50 50 LYS CA C 55.59 0.08 1 300 50 50 LYS CB C 28.03 0.08 1 301 50 50 LYS CG C 24.39 0.11 1 302 50 50 LYS CD C 28.29 0.20 1 303 50 50 LYS CE C 43.33 0.09 1 304 50 50 LYS N N 119.71 0.06 1 305 50 50 LYS NZ N 33.86 0.03 1 306 51 51 THR C C 174.44 0.07 1 307 51 51 THR CA C 62.47 0.08 1 308 51 51 THR CB C 71.71 0.08 1 309 51 51 THR CG2 C 21.29 0.08 1 310 51 51 THR N N 112.00 0.04 1 311 52 52 PHE C C 175.81 0.10 1 312 52 52 PHE CA C 56.58 0.08 1 313 52 52 PHE CB C 43.06 0.17 1 314 52 52 PHE CG C 140.02 0.17 1 315 52 52 PHE CD1 C 131.62 0.30 3 316 52 52 PHE CD2 C 131.62 0.30 3 317 52 52 PHE CE1 C 130.46 0.30 3 318 52 52 PHE CE2 C 130.46 0.30 3 319 52 52 PHE CZ C 130.46 0.30 1 320 52 52 PHE N N 130.28 0.04 1 321 53 53 THR C C 172.25 0.06 1 322 53 53 THR CA C 60.39 0.07 1 323 53 53 THR CB C 71.89 0.10 1 324 53 53 THR CG2 C 21.10 0.10 1 325 53 53 THR N N 112.21 0.06 1 326 54 54 VAL C C 172.62 0.04 1 327 54 54 VAL CA C 58.48 0.07 1 328 54 54 VAL CB C 32.72 0.08 1 329 54 54 VAL CG1 C 21.86 0.10 2 330 54 54 VAL CG2 C 19.75 0.06 2 331 54 54 VAL N N 118.43 0.09 1 332 55 55 THR C C 174.17 0.05 1 333 55 55 THR CA C 61.32 0.09 1 334 55 55 THR CB C 72.09 0.05 1 335 55 55 THR CG2 C 21.51 0.05 1 336 55 55 THR N N 124.10 0.05 1 337 56 56 GLU C C 180.50 0.08 1 338 56 56 GLU CA C 57.56 0.04 1 339 56 56 GLU CB C 33.31 0.06 1 340 56 56 GLU CG C 38.81 0.06 1 341 56 56 GLU CD C 183.20 0.09 1 342 56 56 GLU N N 131.08 0.08 1 stop_ save_ save_assigned_chem_shift_list_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D NH' '3D CON(H)H' '3D HN(H)H' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chemical_shift_reference_2 _Mol_system_component_name monomer _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 MET C C 171.265 . . 2 2 2 GLN H H 8.311 . . 3 2 2 GLN HE21 H 7.862 . . 4 2 2 GLN HE22 H 6.949 . . 5 2 2 GLN C C 174.792 . . 6 2 2 GLN CD C 180.365 . . 7 2 2 GLN N N 125.015 . . 8 2 2 GLN NE2 N 113.104 . . 9 3 3 TYR H H 9.001 . . 10 3 3 TYR C C 174.719 . . 11 3 3 TYR N N 123.389 . . 12 4 4 LYS H H 9.151 . . 13 4 4 LYS C C 173.100 . . 14 4 4 LYS N N 122.658 . . 15 5 5 LEU H H 9.136 . . 16 5 5 LEU C C 174.672 . . 17 5 5 LEU N N 126.769 . . 18 6 6 ILE H H 8.942 . . 19 6 6 ILE C C 175.031 . . 20 6 6 ILE N N 125.852 . . 21 7 7 LEU H H 9.173 . . 22 7 7 LEU C C 174.948 . . 23 7 7 LEU N N 126.518 . . 24 8 8 ASN H H 8.974 . . 25 8 8 ASN HD21 H 7.723 . . 26 8 8 ASN HD22 H 6.654 . . 27 8 8 ASN C C 176.378 . . 28 8 8 ASN N N 124.540 . . 29 8 8 ASN ND2 N 110.671 . . 30 9 9 GLY H H 8.137 . . 31 9 9 GLY C C 173.022 . . 32 9 9 GLY N N 109.154 . . 33 10 10 LYS H H 9.882 . . 34 10 10 LYS C C 178.929 . . 35 10 10 LYS N N 120.772 . . 36 11 11 THR H H 8.943 . . 37 11 11 THR C C 173.206 . . 38 11 11 THR N N 106.171 . . 39 12 12 LEU H H 7.323 . . 40 12 12 LEU C C 173.760 . . 41 12 12 LEU N N 127.577 . . 42 13 13 LYS H H 8.835 . . 43 13 13 LYS C C 175.654 . . 44 13 13 LYS N N 122.904 . . 45 14 14 GLY H H 8.498 . . 46 14 14 GLY C C 171.140 . . 47 14 14 GLY N N 105.150 . . 48 15 15 GLU H H 8.796 . . 49 15 15 GLU C C 173.997 . . 50 15 15 GLU N N 120.803 . . 51 16 16 THR H H 8.806 . . 52 16 16 THR C C 171.810 . . 53 16 16 THR N N 114.440 . . 54 17 17 THR H H 8.332 . . 55 17 17 THR C C 174.149 . . 56 17 17 THR N N 116.150 . . 57 18 18 THR H H 9.130 . . 58 18 18 THR C C 171.093 . . 59 18 18 THR N N 115.801 . . 60 19 19 GLU H H 7.775 . . 61 19 19 GLU C C 175.629 . . 62 19 19 GLU N N 125.285 . . 63 20 20 ALA H H 9.318 . . 64 20 20 ALA C C 177.504 . . 65 20 20 ALA N N 124.894 . . 66 21 21 VAL H H 8.568 . . 67 21 21 VAL C C 174.897 . . 68 21 21 VAL N N 115.548 . . 69 22 22 ASP H H 7.215 . . 70 22 22 ASP C C 175.127 . . 71 22 22 ASP N N 114.784 . . 72 23 23 ALA H H 9.180 . . 73 23 23 ALA C C 179.690 . . 74 23 23 ALA N N 122.464 . . 75 24 24 ALA H H 7.992 . . 76 24 24 ALA C C 181.256 . . 77 24 24 ALA N N 120.130 . . 78 25 25 THR H H 8.512 . . 79 25 25 THR C C 175.701 . . 80 25 25 THR N N 116.945 . . 81 26 26 ALA H H 7.231 . . 82 26 26 ALA C C 177.166 . . 83 26 26 ALA N N 123.213 . . 84 27 27 GLU H H 8.618 . . 85 27 27 GLU C C 177.760 . . 86 27 27 GLU N N 115.998 . . 87 28 28 LYS H H 6.990 . . 88 28 28 LYS C C 178.695 . . 89 28 28 LYS N N 116.843 . . 90 29 29 VAL H H 7.444 . . 91 29 29 VAL C C 178.361 . . 92 29 29 VAL N N 118.194 . . 93 30 30 PHE H H 8.647 . . 94 30 30 PHE C C 178.990 . . 95 30 30 PHE N N 118.179 . . 96 31 31 LYS H H 9.029 . . 97 31 31 LYS C C 179.575 . . 98 31 31 LYS N N 120.075 . . 99 32 32 GLN H H 7.829 . . 100 32 32 GLN HE21 H 7.993 . . 101 32 32 GLN HE22 H 6.825 . . 102 32 32 GLN C C 177.431 . . 103 32 32 GLN CD C 179.660 . . 104 32 32 GLN N N 120.860 . . 105 32 32 GLN NE2 N 115.326 . . 106 33 33 TYR H H 8.597 . . 107 33 33 TYR C C 178.431 . . 108 33 33 TYR N N 120.471 . . 109 34 34 ALA H H 9.098 . . 110 34 34 ALA C C 179.404 . . 111 34 34 ALA N N 122.006 . . 112 35 35 ASN H H 8.383 . . 113 35 35 ASN HD21 H 7.595 . . 114 35 35 ASN HD22 H 7.147 . . 115 35 35 ASN C C 179.403 . . 116 35 35 ASN CG C 176.003 . . 117 35 35 ASN N N 117.814 . . 118 35 35 ASN ND2 N 113.195 . . 119 36 36 ASP H H 9.022 . . 120 36 36 ASP C C 175.908 . . 121 36 36 ASP N N 120.808 . . 122 37 37 ASN H H 7.233 . . 123 37 37 ASN HD21 H 6.455 . . 124 37 37 ASN HD22 H 5.798 . . 125 37 37 ASN C C 174.036 . . 126 37 37 ASN CG C 176.528 . . 127 37 37 ASN N N 114.480 . . 128 37 37 ASN ND2 N 112.980 . . 129 38 38 GLY H H 7.873 . . 130 38 38 GLY C C 173.869 . . 131 38 38 GLY N N 107.870 . . 132 39 39 VAL H H 8.194 . . 133 39 39 VAL C C 174.944 . . 134 39 39 VAL N N 121.459 . . 135 40 40 ASP H H 8.991 . . 136 40 40 ASP C C 175.020 . . 137 40 40 ASP N N 130.513 . . 138 41 41 GLY H H 7.817 . . 139 41 41 GLY C C 172.560 . . 140 41 41 GLY N N 107.636 . . 141 42 42 GLU H H 8.572 . . 142 42 42 GLU C C 177.750 . . 143 42 42 GLU N N 119.296 . . 144 43 43 TRP H H 9.182 . . 145 43 43 TRP C C 176.720 . . 146 43 43 TRP N N 124.658 . . 147 44 44 THR H H 8.898 . . 148 44 44 THR HG1 H 6.536 . . 149 44 44 THR C C 173.773 . . 150 44 44 THR N N 108.361 . . 151 45 45 TYR H H 9.235 . . 152 45 45 TYR C C 171.741 . . 153 45 45 TYR N N 118.367 . . 154 46 46 ASP H H 7.378 . . 155 46 46 ASP C C 176.138 . . 156 46 46 ASP N N 126.107 . . 157 47 47 ASP H H 8.646 . . 158 47 47 ASP C C 177.133 . . 159 47 47 ASP N N 123.211 . . 160 48 48 ALA H H 8.565 . . 161 48 48 ALA C C 179.132 . . 162 48 48 ALA N N 118.697 . . 163 49 49 THR H H 6.923 . . 164 49 49 THR C C 175.440 . . 165 49 49 THR N N 103.995 . . 166 50 50 LYS H H 7.940 . . 167 50 50 LYS C C 175.340 . . 168 50 50 LYS N N 118.864 . . 169 51 51 THR H H 7.367 . . 170 51 51 THR C C 174.138 . . 171 51 51 THR N N 112.128 . . 172 52 52 PHE H H 10.655 . . 173 52 52 PHE C C 175.612 . . 174 52 52 PHE N N 129.563 . . 175 53 53 THR H H 9.215 . . 176 53 53 THR C C 171.876 . . 177 53 53 THR N N 111.902 . . 178 54 54 VAL H H 8.096 . . 179 54 54 VAL C C 172.499 . . 180 54 54 VAL N N 117.814 . . 181 55 55 THR H H 8.357 . . 182 55 55 THR C C 173.852 . . 183 55 55 THR N N 123.561 . . 184 56 56 GLU H H 7.841 . . 185 56 56 GLU N N 130.365 . . stop_ save_