data_17810 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Atomic Resolution Protein Structures using NMR Chemical Shift Tensors ; _BMRB_accession_number 17810 _BMRB_flat_file_name bmr17810.str _Entry_type original _Submission_date 2011-07-26 _Accession_date 2011-07-26 _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 Wylie Benjamin J. . 2 Sperling Lindsay J. . 3 Nieuwkoop Andrew J. . 4 Franks William T. . 5 Oldfield Eric . . 6 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 274 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-12-02 original author . stop_ _Original_release_date 2011-12-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ultrahigh resolution protein structures using NMR chemical shift tensors' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21969532 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wylie Benjamin J. . 2 Sperling Lindsay J. . 3 Nieuwkoop Andrew J. . 4 Franks W. Trent . 5 Oldfield Eric . . 6 Rienstra Chad M. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 108 _Journal_issue 41 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16974 _Page_last 16979 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ultra-high resolution protein structures using NMR chemical shift tensors' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _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 2015-11-04 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 15156 GB1 100.00 56 100.00 100.00 3.48e-30 BMRB 15380 GB1 100.00 56 100.00 100.00 3.48e-30 BMRB 16444 SC35 100.00 158 100.00 100.00 2.55e-30 BMRB 16627 Protein_GB1_(2Q6I) 100.00 56 100.00 100.00 3.48e-30 BMRB 16755 N40 67.86 40 100.00 100.00 2.31e-16 BMRB 16873 GB1 100.00 56 100.00 100.00 3.48e-30 BMRB 16882 "Ubiquitin-Binding Motif" 100.00 108 100.00 100.00 2.62e-30 BMRB 16958 ZCCHC9 100.00 164 100.00 100.00 1.79e-30 BMRB 18397 GB1 100.00 56 100.00 100.00 3.48e-30 BMRB 19394 GB1-UBM1 100.00 106 100.00 100.00 1.27e-30 BMRB 26630 Protein_G_Domain_Beta-1_Wild_Type 100.00 64 98.21 98.21 1.24e-29 PDB 1GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.17e-29 PDB 1IBX "Nmr Structure Of Dff40 And Dff45 N-Terminal Domain Complex" 100.00 145 100.00 100.00 4.55e-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 4.17e-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 4.17e-29 PDB 1PN5 "Nmr Structure Of The Nalp1 Pyrin Domain (Pyd)" 100.00 159 100.00 100.00 3.01e-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 1.49e-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 1.49e-28 PDB 2GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.17e-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 3.48e-30 PDB 2I2Y "Solution Structure Of The Rrm Of Srp20 Bound To The Rna Cauc" 100.00 150 100.00 100.00 5.83e-30 PDB 2I38 "Solution Structure Of The Rrm Of Srp20" 100.00 150 100.00 100.00 6.15e-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 3.48e-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 3.48e-30 PDB 2K0P "Determination Of A Protein Structure In The Solid State From Nmr Chemical Shifts" 100.00 56 100.00 100.00 3.48e-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 1.31e-28 PDB 2KHU "Solution Structure Of The Ubiquitin-Binding Motif Of Human Polymerase Iota" 100.00 108 100.00 100.00 2.62e-30 PDB 2KHW "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" 100.00 108 100.00 100.00 2.62e-30 PDB 2KLK "Solution Structure Of Gb1 A34f Mutant With Rdc And Saxs" 100.00 56 98.21 98.21 4.04e-29 PDB 2KN4 "The Structure Of The Rrm Domain Of Sc35" 100.00 158 100.00 100.00 2.55e-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 3.48e-30 PDB 2KWD "Supramolecular Protein Structure Determination By Site-Speci Range Intermolecular Solid State Nmr Spectroscopy" 100.00 56 100.00 100.00 3.48e-30 PDB 2LGI "Atomic Resolution Protein Structures Using Nmr Chemical Shift Tensors" 100.00 56 100.00 100.00 3.48e-30 PDB 2MBB "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" 100.00 106 100.00 100.00 1.27e-30 PDB 2PLP "Ultra High Resolution Backbone Conformation Of Protein Gb1 From Residual Dipolar Couplings Alone" 94.64 54 100.00 100.00 1.54e-27 PDB 2QMT "Crystal Polymorphism Of Protein Gb1 Examined By Solid-State Nmr And X-Ray Diffraction" 100.00 56 100.00 100.00 3.48e-30 PDB 2RMM "Solution Structure Of Gb1 A34f Mutant" 100.00 56 98.21 98.21 4.04e-29 PDB 3GB1 "Structures Of B1 Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.17e-29 PDB 3MP9 "Structure Of Streptococcal Protein G B1 Domain At Ph 3.0" 96.43 64 100.00 100.00 7.20e-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 1.14e-28 PDB 4Q0C "3.1 A Resolution Crystal Structure Of The B. Pertussis Bvgs Periplasmic Domain" 100.00 584 98.21 98.21 1.57e-27 EMBL CAA37410 "Protein G' [Streptococcus sp. 'group G']" 80.36 185 97.78 100.00 8.41e-20 GB AAY41168 "protein G/SspDnaE fusion protein [Expression vector pJJDuet30]" 100.00 201 98.21 100.00 2.75e-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 _Gene_mnemonic $entity firmicutes 1320 Bacteria . Streptococcus "Streptococcus sp. 'group G'" spg 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 $entity 'recombinant technology' . Escherichia coli BL21 Pet. stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details '20 mg [U-2-13C-glycerol; U-100% 15N] GB1, (4R)-2-Metylpentane-2,4-Diol (50% v/v), Isopropyl alcohol (25% v/v), 25 mg/mL GB1 in 50 mM sodium phosphate buffered H2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 20 mg '[U-2-13C-glycerol; U-100% 15N]' (4R)-2-Metylpentane-2,4-Diol 50 % 'natural abundance' 'Isopropyl alcohol' 25 % 'natural abundance' $entity 25 mg/mL 'natural abundance' 'sodium phosphate buffered H2O' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.18.(2-4) loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details 'Build of X-PLOR NIH with CST forcefield' save_ save_Procheck _Saveframe_category software _Name Procheck _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Spinevolution _Saveframe_category software _Name Spinevolution _Version . loop_ _Vendor _Address _Electronic_address 'M.Veshtort, R.G.Griffin' . . stop_ loop_ _Task 'data analysis' stop_ _Details 'NMR simulaitons' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' processing stop_ _Details . save_ save_Minuit _Saveframe_category software _Name Minuit _Version . loop_ _Vendor _Address _Electronic_address 'James, F; Roos, M' . . stop_ loop_ _Task 'data analysis' 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_ ############################# # NMR applied experiments # ############################# save_3D-NCA-{13C_CST}_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-{13C CST}' _Sample_label $sample_1 save_ save_3D-NCA-{1H-13C}_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NCA-{1H-13C} _Sample_label $sample_1 save_ save_3D-NCA-{13C_CST}:{15N-13C}_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-{13C CST}:{15N-13C}' _Sample_label $sample_1 save_ save_3D-NCA-1:1{13C_CST}:{1H-13C}_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-1:1{13C CST}:{1H-13C}' _Sample_label $sample_1 save_ save_3D-NCA-2:1{13C_CST}:{1H-13C}_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-2:1{13C CST}:{1H-13C}' _Sample_label $sample_1 save_ save_3D-NCA-3:1{13C_CST}:{1H-13C}_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-3:1{13C CST}:{1H-13C}' _Sample_label $sample_1 save_ save_3D-NCA-{15N_CST}_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-{15N CST}' _Sample_label $sample_1 save_ save_3D-NCA-{1H-15N}_8 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NCA-{1H-15N} _Sample_label $sample_1 save_ save_3D-NCA-1:1{15N_CST}:{1H-15N}_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-1:1{15N CST}:{1H-15N}' _Sample_label $sample_1 save_ save_3D-NCA-2:1{15N_CST}:{1H-15N}_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-2:1{15N CST}:{1H-15N}' _Sample_label $sample_1 save_ save_3D-NCA-1:2{15N_CST}:{1H-15N}_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-NCA-1:2{15N CST}:{1H-15N}' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '(4R)-2-Metylpentane-2,4-Diol (50% v/v), Isopropyl alcohol (25% v/v), 25 mg/mL GB1 in 50 mM sodium phosphate buffered H2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 5.5 . 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 'All chemical shifts referenced indirectly to DSS via adamantane spectra acquired immediately before data acquisition.' 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 . . . . DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 nitrogen ppm 0.00 na indirect . . . 1.0 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 ; For details of chemical shift assignment, please see: W. Trent Franks, Donghua H. Zhou, Benjamin J. Wylie, Brian G. Money, Daniel T. Graesser, Heather L. Frericks, Gurmukh Sahota, and Chad M. Rienstra; J. Am. Chem. Soc. 2005, 127, 12291-12305. ; loop_ _Experiment_label '3D-NCA-{13C CST}' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _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 131.97 0.11 3 19 3 3 TYR CD2 C 134.72 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 1 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_