data_18397 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; nanocrystalline GB1 1H, 13C, 15N assignments ; _BMRB_accession_number 18397 _BMRB_flat_file_name bmr18397.str _Entry_type original _Submission_date 2012-04-13 _Accession_date 2012-04-13 _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 Zhou Donghua . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 66 "13C chemical shifts" 186 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-09-24 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22986689 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Donghua H. . 2 Nieuwkoop Andrew J. . 3 Berthold Deborah A. . 4 Comellas Gemma . . 5 Sperling Lindsay J. . 6 Tang Ming . . 7 Shah Gautam J. . 8 Brea Elliott J. . 9 Lemkau Luisel R. . 10 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 54 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 305 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name GB1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GB1 $GB1 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_GB1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GB1 _Molecular_mass . _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 17810 entity 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 $GB1 'Streptococcal bacteria' 1301 Bacteria . Streptococcal bacteria 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 $GB1 'recombinant technology' . Escherichia coli . NA 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 $GB1 5 mg '[U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name NH _Sample_label $sample_1 save_ save_CANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _Sample_label $sample_1 save_ save_CA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CA(CO)NH _Sample_label $sample_1 save_ save_CANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _Sample_label $sample_1 save_ save_CONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CONH _Sample_label $sample_1 save_ save_CO(CA)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CO(CA)NH _Sample_label $sample_1 save_ save_CBCANH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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 NH CANH CA(CO)NH CONH CO(CA)NH CBCANH CBCA(CO)NH 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 GB1 _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 171.092 0.016 1 2 1 1 MET CA C 54.539 0.022 1 3 1 1 MET CB C 32.307 0.084 1 4 1 1 MET CG C 29.999 0.000 1 5 2 2 GLN H H 8.614 0.033 1 6 2 2 GLN HE21 H 7.936 0.000 . 7 2 2 GLN HE22 H 7.085 0.000 . 8 2 2 GLN C C 174.871 0.013 1 9 2 2 GLN CA C 56.087 0.012 1 10 2 2 GLN CB C 30.327 0.129 1 11 2 2 GLN CG C 35.600 0.000 1 12 2 2 GLN CD C 180.276 0.008 1 13 2 2 GLN N N 125.492 0.115 1 14 2 2 GLN NE2 N 113.194 0.447 1 15 3 3 TYR H H 9.227 0.079 1 16 3 3 TYR C C 174.879 0.002 1 17 3 3 TYR CA C 57.198 0.026 1 18 3 3 TYR CB C 43.525 0.000 1 19 3 3 TYR N N 123.694 0.160 1 20 4 4 LYS H H 9.393 0.019 1 21 4 4 LYS C C 173.307 0.008 1 22 4 4 LYS CA C 55.200 0.056 1 23 4 4 LYS CB C 36.295 0.075 1 24 4 4 LYS CG C 25.665 0.000 1 25 4 4 LYS CD C 29.060 0.000 1 26 4 4 LYS N N 122.412 0.123 1 27 5 5 LEU H H 9.300 0.054 1 28 5 5 LEU C C 174.665 0.012 1 29 5 5 LEU CA C 53.053 0.031 1 30 5 5 LEU N N 126.229 0.203 1 31 6 6 ILE H H 9.170 0.062 1 32 6 6 ILE C C 175.075 0.013 1 33 6 6 ILE CA C 60.035 0.022 1 34 6 6 ILE CB C 37.888 0.000 1 35 6 6 ILE N N 126.087 0.060 1 36 7 7 LEU H H 9.381 0.054 1 37 7 7 LEU C C 174.878 0.016 1 38 7 7 LEU CA C 54.844 0.061 1 39 7 7 LEU CB C 42.990 0.000 1 40 7 7 LEU CD1 C 26.065 0.000 1 41 7 7 LEU CD2 C 25.090 0.000 1 42 7 7 LEU N N 126.765 0.469 1 43 8 8 ASN H H 9.184 0.054 1 44 8 8 ASN HD21 H 7.786 0.000 1 45 8 8 ASN HD22 H 6.878 0.113 1 46 8 8 ASN C C 176.222 0.012 1 47 8 8 ASN CA C 50.786 0.023 1 48 8 8 ASN CB C 38.353 0.056 1 49 8 8 ASN CG C 176.302 0.022 1 50 8 8 ASN N N 124.871 0.028 1 51 8 8 ASN ND2 N 110.606 0.212 1 52 9 9 GLY H H 8.320 0.047 1 53 9 9 GLY C C 173.028 0.019 1 54 9 9 GLY CA C 44.719 0.043 1 55 9 9 GLY N N 109.488 0.176 1 56 10 10 LYS H H 10.024 0.034 1 57 10 10 LYS C C 178.983 0.008 1 58 10 10 LYS CA C 59.396 0.032 1 59 10 10 LYS CB C 32.854 0.060 1 60 10 10 LYS CG C 25.641 0.000 1 61 10 10 LYS CD C 29.293 0.000 1 62 10 10 LYS N N 120.801 0.064 1 63 11 11 THR H H 9.030 0.044 1 64 11 11 THR C C 173.192 0.011 1 65 11 11 THR CA C 62.244 0.047 1 66 11 11 THR CB C 69.802 0.000 1 67 11 11 THR CG2 C 22.702 0.076 1 68 11 11 THR N N 106.632 0.090 1 69 12 12 LEU H H 7.528 0.078 1 70 12 12 LEU C C 173.605 0.008 1 71 12 12 LEU CA C 54.604 0.085 1 72 12 12 LEU CB C 43.300 0.003 1 73 12 12 LEU CD1 C 26.127 0.000 2 74 12 12 LEU N N 127.355 0.072 1 75 13 13 LYS H H 8.880 0.051 1 76 13 13 LYS C C 175.588 0.006 1 77 13 13 LYS CA C 53.559 0.057 1 78 13 13 LYS N N 123.029 0.076 1 79 14 14 GLY H H 8.732 0.030 1 80 14 14 GLY C C 171.138 0.011 1 81 14 14 GLY CA C 45.095 0.056 1 82 14 14 GLY N N 105.536 0.044 1 83 15 15 GLU H H 8.814 0.043 1 84 15 15 GLU C C 173.758 0.039 1 85 15 15 GLU CA C 53.930 0.019 1 86 15 15 GLU CB C 33.480 0.048 1 87 15 15 GLU N N 121.276 0.151 1 88 16 16 THR H H 8.985 0.018 1 89 16 16 THR C C 171.771 0.002 1 90 16 16 THR CA C 60.277 0.078 1 91 16 16 THR CB C 70.630 0.071 1 92 16 16 THR CG2 C 20.033 0.030 1 93 16 16 THR N N 115.485 0.373 1 94 17 17 THR H H 8.384 0.214 1 95 17 17 THR C C 173.808 0.036 1 96 17 17 THR CA C 60.371 0.060 1 97 17 17 THR CB C 73.011 0.068 1 98 17 17 THR CG2 C 21.462 0.183 1 99 17 17 THR N N 115.452 0.332 1 100 18 18 THR H H 9.332 0.070 1 101 18 18 THR C C 171.025 0.012 1 102 18 18 THR CA C 61.681 0.041 1 103 18 18 THR CB C 70.986 0.045 1 104 18 18 THR CG2 C 18.719 0.051 1 105 18 18 THR N N 115.981 0.053 1 106 19 19 GLU H H 7.958 0.012 1 107 19 19 GLU C C 175.629 0.005 1 108 19 19 GLU CA C 54.326 0.037 1 109 19 19 GLU N N 125.042 0.064 1 110 20 20 ALA H H 9.585 0.026 1 111 20 20 ALA C C 177.610 0.004 1 112 20 20 ALA CA C 50.812 0.021 1 113 20 20 ALA CB C 23.712 0.044 1 114 20 20 ALA N N 125.338 0.130 1 115 21 21 VAL H H 8.839 0.035 1 116 21 21 VAL C C 174.702 0.005 1 117 21 21 VAL CA C 63.727 0.044 1 118 21 21 VAL CB C 31.962 0.000 1 119 21 21 VAL CG1 C 20.989 0.000 2 120 21 21 VAL N N 116.466 0.184 1 121 22 22 ASP H H 7.381 0.029 1 122 22 22 ASP C C 174.903 0.010 1 123 22 22 ASP CA C 52.472 0.023 1 124 22 22 ASP CB C 42.674 0.456 1 125 22 22 ASP N N 115.526 0.160 1 126 23 23 ALA H H 9.379 0.033 1 127 23 23 ALA C C 179.756 0.010 1 128 23 23 ALA CA C 54.754 0.029 1 129 23 23 ALA CB C 18.233 0.041 1 130 23 23 ALA N N 122.995 0.280 1 131 24 24 ALA H H 8.282 0.016 1 132 24 24 ALA C C 181.382 0.042 1 133 24 24 ALA CA C 54.717 0.030 1 134 24 24 ALA CB C 18.136 0.041 1 135 24 24 ALA N N 120.606 0.170 1 136 25 25 THR H H 8.537 0.040 1 137 25 25 THR C C 175.655 0.011 1 138 25 25 THR CA C 67.566 0.030 1 139 25 25 THR CB C 67.595 0.000 1 140 25 25 THR CG2 C 21.293 0.026 1 141 25 25 THR N N 117.026 0.039 1 142 26 26 ALA H H 7.441 0.032 1 143 26 26 ALA C C 177.254 0.177 1 144 26 26 ALA CA C 55.243 0.033 1 145 26 26 ALA CB C 17.563 0.068 1 146 26 26 ALA N N 123.886 0.148 1 147 27 27 GLU H H 8.848 0.034 1 148 27 27 GLU C C 177.705 0.011 1 149 27 27 GLU CA C 59.304 0.080 1 150 27 27 GLU CB C 29.137 0.006 1 151 27 27 GLU N N 116.190 0.025 1 152 28 28 LYS H H 7.047 0.053 1 153 28 28 LYS C C 178.784 0.004 1 154 28 28 LYS CA C 60.492 0.072 1 155 28 28 LYS CB C 32.794 0.031 1 156 28 28 LYS N N 117.225 0.088 1 157 29 29 VAL H H 7.651 0.029 1 158 29 29 VAL C C 178.587 0.023 1 159 29 29 VAL CA C 66.603 0.009 1 160 29 29 VAL CB C 32.004 0.011 1 161 29 29 VAL CG1 C 22.242 0.000 1 162 29 29 VAL CG2 C 21.093 0.000 1 163 29 29 VAL N N 119.031 0.148 1 164 30 30 PHE H H 8.795 0.012 1 165 30 30 PHE C C 178.919 0.003 1 166 30 30 PHE CA C 57.407 0.118 1 167 30 30 PHE N N 118.349 0.065 1 168 31 31 LYS H H 9.199 0.039 1 169 31 31 LYS C C 179.592 0.031 1 170 31 31 LYS CA C 60.311 0.033 1 171 31 31 LYS CB C 31.855 0.000 1 172 31 31 LYS CD C 29.227 0.000 1 173 31 31 LYS N N 120.627 0.104 1 174 32 32 GLN H H 7.999 0.044 1 175 32 32 GLN HE21 H 8.153 0.000 1 176 32 32 GLN HE22 H 7.044 0.000 1 177 32 32 GLN C C 177.398 0.009 1 178 32 32 GLN CA C 59.045 0.010 1 179 32 32 GLN CB C 28.971 0.030 1 180 32 32 GLN CD C 179.759 0.008 1 181 32 32 GLN N N 121.124 0.090 1 182 32 32 GLN NE2 N 115.639 0.601 1 183 33 33 TYR H H 8.765 0.055 1 184 33 33 TYR C C 178.535 0.013 1 185 33 33 TYR CA C 61.876 0.046 1 186 33 33 TYR CB C 38.895 0.000 1 187 33 33 TYR N N 120.732 0.058 1 188 34 34 ALA H H 9.351 0.023 1 189 34 34 ALA C C 179.403 0.007 1 190 34 34 ALA CA C 56.301 0.051 1 191 34 34 ALA CB C 17.980 0.031 1 192 34 34 ALA N N 122.513 0.061 1 193 35 35 ASN H H 8.490 0.019 1 194 35 35 ASN HD21 H 7.725 0.000 1 195 35 35 ASN HD22 H 7.104 0.128 1 196 35 35 ASN C C 179.449 0.100 1 197 35 35 ASN CA C 57.277 0.013 1 198 35 35 ASN CB C 39.420 0.043 1 199 35 35 ASN CG C 175.980 0.013 1 200 35 35 ASN N N 118.069 0.101 1 201 35 35 ASN ND2 N 113.083 0.461 1 202 36 36 ASP H H 9.138 0.022 1 203 36 36 ASP C C 175.893 0.001 1 204 36 36 ASP CA C 56.078 0.029 1 205 36 36 ASP CB C 38.448 0.090 1 206 36 36 ASP N N 120.981 0.032 1 207 37 37 ASN H H 7.390 0.083 1 208 37 37 ASN HD21 H 6.709 0.000 1 209 37 37 ASN HD22 H 6.013 0.086 1 210 37 37 ASN C C 174.041 0.008 1 211 37 37 ASN CA C 53.696 0.018 1 212 37 37 ASN CB C 40.478 0.116 1 213 37 37 ASN CG C 176.605 0.016 1 214 37 37 ASN N N 114.744 0.098 1 215 37 37 ASN ND2 N 113.876 0.442 1 216 38 38 GLY H H 8.015 0.022 1 217 38 38 GLY C C 173.849 0.027 1 218 38 38 GLY CA C 47.033 0.069 1 219 38 38 GLY N N 108.276 0.074 1 220 39 39 VAL H H 8.336 0.028 1 221 39 39 VAL C C 174.959 0.007 1 222 39 39 VAL CA C 61.952 0.014 1 223 39 39 VAL CB C 31.827 0.094 1 224 39 39 VAL CG1 C 22.015 0.080 2 225 39 39 VAL N N 121.642 0.046 1 226 40 40 ASP H H 9.221 0.040 1 227 40 40 ASP C C 174.739 0.048 1 228 40 40 ASP CA C 52.637 0.074 1 229 40 40 ASP CB C 41.176 0.007 1 230 40 40 ASP N N 130.657 0.072 1 231 41 41 GLY H H 8.174 0.014 1 232 41 41 GLY C C 172.643 0.014 1 233 41 41 GLY CA C 45.256 0.025 1 234 41 41 GLY N N 108.113 0.142 1 235 42 42 GLU H H 8.678 0.018 1 236 42 42 GLU C C 177.760 0.009 1 237 42 42 GLU CA C 54.921 0.023 1 238 42 42 GLU CB C 31.053 0.000 1 239 42 42 GLU N N 118.256 0.325 1 240 43 43 TRP H H 9.310 0.061 1 241 43 43 TRP HE1 H 10.645 0.000 1 242 43 43 TRP C C 177.163 0.013 1 243 43 43 TRP CA C 57.710 0.040 1 244 43 43 TRP CB C 33.649 0.000 1 245 43 43 TRP N N 124.691 0.102 1 246 43 43 TRP NE1 N 130.989 0.000 1 247 44 44 THR H H 9.172 0.143 1 248 44 44 THR C C 173.743 0.011 1 249 44 44 THR CA C 61.162 0.064 1 250 44 44 THR CG2 C 20.900 0.000 1 251 44 44 THR N N 109.013 0.084 1 252 45 45 TYR H H 9.461 0.018 1 253 45 45 TYR C C 171.761 0.016 1 254 45 45 TYR CA C 58.067 0.015 1 255 45 45 TYR N N 118.389 0.099 1 256 46 46 ASP H H 7.597 0.057 1 257 46 46 ASP C C 175.751 0.069 1 258 46 46 ASP CA C 50.843 0.041 1 259 46 46 ASP CB C 42.096 0.109 1 260 46 46 ASP N N 126.303 0.063 1 261 47 47 ASP H H 8.920 0.028 1 262 47 47 ASP C C 177.013 0.006 1 263 47 47 ASP CA C 54.694 0.036 1 264 47 47 ASP CB C 42.930 0.142 1 265 47 47 ASP N N 123.239 0.048 1 266 48 48 ALA H H 8.485 0.042 1 267 48 48 ALA C C 179.369 0.053 1 268 48 48 ALA CA C 54.027 0.096 1 269 48 48 ALA CB C 19.069 0.032 1 270 48 48 ALA N N 118.389 0.204 1 271 49 49 THR H H 7.041 0.017 1 272 49 49 THR C C 175.691 0.005 1 273 49 49 THR CA C 60.457 0.029 1 274 49 49 THR CB C 69.903 0.013 1 275 49 49 THR CG2 C 21.600 0.017 1 276 49 49 THR N N 104.191 0.068 1 277 50 50 LYS H H 7.980 0.112 1 278 50 50 LYS C C 175.244 0.004 1 279 50 50 LYS CA C 55.502 0.028 1 280 50 50 LYS N N 119.386 0.080 1 281 51 51 THR H H 7.563 0.044 1 282 51 51 THR C C 174.145 0.005 1 283 51 51 THR CA C 62.662 0.030 1 284 51 51 THR CB C 71.835 0.128 1 285 51 51 THR CG2 C 21.019 0.101 1 286 51 51 THR N N 111.885 0.160 1 287 52 52 PHE H H 10.846 0.032 1 288 52 52 PHE C C 175.577 0.011 1 289 52 52 PHE CA C 56.675 0.100 1 290 52 52 PHE CB C 43.466 0.114 1 291 52 52 PHE N N 130.269 0.120 1 292 53 53 THR H H 9.386 0.098 1 293 53 53 THR C C 171.904 0.007 1 294 53 53 THR CA C 60.435 0.028 1 295 53 53 THR CG2 C 20.975 0.000 1 296 53 53 THR N N 111.920 0.167 1 297 54 54 VAL H H 8.353 0.098 1 298 54 54 VAL C C 172.442 0.006 1 299 54 54 VAL CA C 58.666 0.019 1 300 54 54 VAL CB C 32.588 0.049 1 301 54 54 VAL CG1 C 21.876 0.027 2 302 54 54 VAL N N 118.136 0.037 1 303 55 55 THR H H 8.548 0.028 1 304 55 55 THR C C 174.055 0.006 1 305 55 55 THR CA C 61.514 0.056 1 306 55 55 THR CB C 72.302 0.042 1 307 55 55 THR CG2 C 21.298 0.078 1 308 55 55 THR N N 123.794 0.043 1 309 56 56 GLU H H 8.046 0.025 1 310 56 56 GLU C C 180.103 0.001 1 311 56 56 GLU CA C 57.562 0.029 1 312 56 56 GLU CB C 33.192 0.019 1 313 56 56 GLU N N 131.081 0.103 1 stop_ save_