data_26640 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C chemical shift assignment of the alpha-crystallin domain and the C-terminal domain in human alpha-B crystallin oligomers. ; _BMRB_accession_number 26640 _BMRB_flat_file_name bmr26640.str _Entry_type original _Submission_date 2015-08-26 _Accession_date 2015-08-26 _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 Mainz Andi . . 2 Reif Bernd . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 101 "13C chemical shifts" 240 "15N chemical shifts" 100 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-11-09 update author 'update entry citation' 2015-09-28 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16391 'PEG-precipitated human alpha B crystallin assigned by conventional 13C-detected solid-state MAS NMR' 25527 'Solution-state NMR assignment of the excised alpha crystallin domain of human alpha B crystallin.' stop_ _Original_release_date 2015-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The chaperone AlphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26458046 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mainz Andi . . 2 Peschek Jirka . . 3 Stavropoulou Maria . . 4 Back Katrin C. . 5 Asami Sam . . 6 Bardiaux Benjamin . . 7 Prade Elke . . 8 Peters Carsten . . 9 Weinkauf Sevil . . 10 Buchner Johannes . . 11 Reif Bernd . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_volume 22 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 898 _Page_last 905 _Year 2015 _Details . loop_ _Keyword amyloid chaperone 'magic angle spinning' 'protein aggregation' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'alpha B crystallin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alpha B crystallin, 1' $aB 'alpha B crystallin, 2' $aB 'alpha B crystallin, 3' $aB 'alpha B crystallin, 4' $aB 'alpha B crystallin, 5' $aB 'alpha B crystallin, 6' $aB 'alpha B crystallin, 7' $aB 'alpha B crystallin, 8' $aB 'alpha B crystallin, 9' $aB 'alpha B crystallin, 10' $aB 'alpha B crystallin, 11' $aB 'alpha B crystallin, 12' $aB 'alpha B crystallin, 13' $aB 'alpha B crystallin, 14' $aB 'alpha B crystallin, 15' $aB 'alpha B crystallin, 16' $aB 'alpha B crystallin, 17' $aB 'alpha B crystallin, 18' $aB 'alpha B crystallin, 19' $aB 'alpha B crystallin, 20' $aB 'alpha B crystallin, 21' $aB 'alpha B crystallin, 22' $aB 'alpha B crystallin, 23' $aB 'alpha B crystallin, 24' $aB 'alpha B crystallin, 25' $aB 'alpha B crystallin, 26' $aB 'alpha B crystallin, 27' $aB 'alpha B crystallin, 28' $aB stop_ _System_molecular_weight 560000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'molecular chaperone' 'small heat shock protein' stop_ _Database_query_date . _Details 'Heterogeneous Homooligomer consisting of 10-40 protomers (major species 24/28-mer)' save_ ######################## # Monomeric polymers # ######################## save_aB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common aB _Molecular_mass 20159 _Mol_thiol_state 'not present' loop_ _Biological_function 'molecular chaperone' 'small heat shock protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 175 _Mol_residue_sequence ; MDIAIHHPWIRRPFFPFHSP SRLFDQFFGEHLLESDLFPT STSLSPFYLRPPSFLRAPSW FDTGLSEMRLEKDRFSVNLD VKHFSPEELKVKVLGDVIEV HGKHEERQDEHGFISREFHR KYRIPADVDPLTITSSLSSD GVLTVNGPRKQVSGPERTIP ITREEKPAVTAAPKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ILE 4 ALA 5 ILE 6 HIS 7 HIS 8 PRO 9 TRP 10 ILE 11 ARG 12 ARG 13 PRO 14 PHE 15 PHE 16 PRO 17 PHE 18 HIS 19 SER 20 PRO 21 SER 22 ARG 23 LEU 24 PHE 25 ASP 26 GLN 27 PHE 28 PHE 29 GLY 30 GLU 31 HIS 32 LEU 33 LEU 34 GLU 35 SER 36 ASP 37 LEU 38 PHE 39 PRO 40 THR 41 SER 42 THR 43 SER 44 LEU 45 SER 46 PRO 47 PHE 48 TYR 49 LEU 50 ARG 51 PRO 52 PRO 53 SER 54 PHE 55 LEU 56 ARG 57 ALA 58 PRO 59 SER 60 TRP 61 PHE 62 ASP 63 THR 64 GLY 65 LEU 66 SER 67 GLU 68 MET 69 ARG 70 LEU 71 GLU 72 LYS 73 ASP 74 ARG 75 PHE 76 SER 77 VAL 78 ASN 79 LEU 80 ASP 81 VAL 82 LYS 83 HIS 84 PHE 85 SER 86 PRO 87 GLU 88 GLU 89 LEU 90 LYS 91 VAL 92 LYS 93 VAL 94 LEU 95 GLY 96 ASP 97 VAL 98 ILE 99 GLU 100 VAL 101 HIS 102 GLY 103 LYS 104 HIS 105 GLU 106 GLU 107 ARG 108 GLN 109 ASP 110 GLU 111 HIS 112 GLY 113 PHE 114 ILE 115 SER 116 ARG 117 GLU 118 PHE 119 HIS 120 ARG 121 LYS 122 TYR 123 ARG 124 ILE 125 PRO 126 ALA 127 ASP 128 VAL 129 ASP 130 PRO 131 LEU 132 THR 133 ILE 134 THR 135 SER 136 SER 137 LEU 138 SER 139 SER 140 ASP 141 GLY 142 VAL 143 LEU 144 THR 145 VAL 146 ASN 147 GLY 148 PRO 149 ARG 150 LYS 151 GLN 152 VAL 153 SER 154 GLY 155 PRO 156 GLU 157 ARG 158 THR 159 ILE 160 PRO 161 ILE 162 THR 163 ARG 164 GLU 165 GLU 166 LYS 167 PRO 168 ALA 169 VAL 170 THR 171 ALA 172 ALA 173 PRO 174 LYS 175 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 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 16391 alphaB-crystallin 100.00 175 100.00 100.00 3.82e-121 BMRB 25527 HSPB5-ACD 50.86 89 98.88 100.00 9.52e-54 PDB 2KLR "Solid-State Nmr Structure Of The Alpha-Crystallin Domain In Alphab- Crystallin Oligomers" 100.00 175 100.00 100.00 3.82e-121 PDB 2N0K "Chemical Shift Assignments And Structure Of The Alpha-crystallin Domain From Human, Hspb5" 50.86 89 98.88 100.00 9.52e-54 PDB 2WJ7 "Human Alphab Crystallin" 53.71 94 97.87 97.87 7.97e-57 PDB 2YGD "Molecular Architectures Of The 24meric Eye Lens Chaperone Alphab-crystallin Elucidated By A Triple Hybrid Approach" 100.00 175 100.00 100.00 3.82e-121 PDB 3L1G "Human Alphab Crystallin" 54.29 96 100.00 100.00 4.30e-59 DBJ BAD51947 "crystallin, alpha B [Macaca fascicularis]" 100.00 175 99.43 100.00 6.59e-121 DBJ BAE27257 "unnamed protein product [Mus musculus]" 100.00 175 97.71 98.29 1.70e-118 DBJ BAE40798 "unnamed protein product [Mus musculus]" 100.00 175 97.71 98.29 1.70e-118 DBJ BAE87237 "unnamed protein product [Macaca fascicularis]" 100.00 175 99.43 100.00 6.59e-121 DBJ BAG36739 "unnamed protein product [Homo sapiens]" 100.00 175 100.00 100.00 3.82e-121 EMBL CAA42910 "alpha B-crystallin [Rattus rattus]" 100.00 175 97.14 98.29 2.12e-118 EMBL CAA42911 "alpha B-crystallin [Rattus rattus]" 99.43 174 97.13 98.28 2.26e-117 EMBL CAA64669 "alpha-B-crystallin [Oryctolagus cuniculus]" 100.00 175 98.29 98.29 7.91e-119 EMBL CAC33095 "alphaB-crystallin [Nannospalax ehrenbergi]" 97.14 170 97.06 97.65 3.40e-114 EMBL CAF02108 "alphaB-crystallin [Elephas maximus]" 96.00 168 97.02 98.21 3.00e-112 GB AAA03655 "alpha B-crystallin [Rattus norvegicus]" 100.00 175 97.14 98.29 2.12e-118 GB AAA37472 "alpha-B crystallin [Mus musculus]" 100.00 175 97.71 98.29 1.70e-118 GB AAA40977 "alpha-crystallin B chain [Rattus norvegicus]" 100.00 175 97.14 98.29 2.12e-118 GB AAA52104 "alpha-B2-crystallin [Homo sapiens]" 100.00 175 100.00 100.00 3.82e-121 GB AAA67045 "alpha(B)-2-crystallin [Mus musculus domesticus]" 100.00 175 97.71 98.29 1.70e-118 PIR I53319 "alpha B-crystallin - rat" 100.00 175 97.14 98.29 2.12e-118 PRF 2015215A "alpha-B crystallin" 100.00 175 97.14 98.29 2.12e-118 REF NP_001012475 "alpha-crystallin B chain [Ovis aries]" 100.00 175 97.14 98.29 6.04e-118 REF NP_001075876 "alpha-crystallin B chain [Oryctolagus cuniculus]" 100.00 175 98.29 98.29 7.91e-119 REF NP_001125917 "alpha-crystallin B chain [Pongo abelii]" 100.00 175 100.00 100.00 3.82e-121 REF NP_001247830 "alpha-crystallin B chain [Macaca mulatta]" 100.00 175 99.43 100.00 6.59e-121 REF NP_001271991 "alpha-crystallin B chain [Macaca fascicularis]" 100.00 175 99.43 100.00 6.59e-121 SP P02510 "RecName: Full=Alpha-crystallin B chain; AltName: Full=Alpha(B)-crystallin" 100.00 175 97.71 97.71 1.63e-118 SP P02511 "RecName: Full=Alpha-crystallin B chain; AltName: Full=Alpha(B)-crystallin; AltName: Full=Heat shock protein beta-5; Short=HspB5" 100.00 175 100.00 100.00 3.82e-121 SP P23927 "RecName: Full=Alpha-crystallin B chain; AltName: Full=Alpha(B)-crystallin; AltName: Full=P23" 100.00 175 97.71 98.29 1.70e-118 SP P23928 "RecName: Full=Alpha-crystallin B chain; AltName: Full=Alpha(B)-crystallin" 100.00 175 97.14 98.29 2.12e-118 SP P41316 "RecName: Full=Alpha-crystallin B chain; AltName: Full=Alpha(B)-crystallin" 100.00 175 98.29 98.29 7.91e-119 TPG DAA22360 "TPA: alpha-crystallin B chain [Bos taurus]" 100.00 175 97.71 97.71 1.63e-118 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $aB Human 9606 Eukaryota Metazoa Homo sapiens 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 $aB 'recombinant technology' . Escherichia coli 'BL21 DE3' pET30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $aB 2 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solid _Details ; A concentrated protein solution (10-15 mM) was directly filled into a thin-walled 3.2mm MAS rotor. During MAS, the protein is sedimented due to its high molecular weight at the inner wall of the rotor and thus behaves like a solid. The concentration given below refers to the predicted concentration in the protein sediment. Cu(II)-EDTA was used as a doping agent to reduce the recycle delay allowing for faster data acquisition. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $aB 25 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' Cu(II)-EDTA 60 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solid _Details ; A concentrated protein solution (10-15 mM) was directly filled into a thin-walled 1.9mm MAS rotor. During MAS, the protein is sedimented due to its high molecular weight at the inner wall of the rotor and thus behaves like a solid. The concentration given below refers to the predicted concentration in the protein sediment. Cu(II)-EDTA was used as a doping agent to reduce the recycle delay allowing for faster data acquisition. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $aB 25 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' Cu(II)-EDTA 60 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details solution save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'widebore, solid-state' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details 'narrowbore, solid-state' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_2D_1H-15N_CP_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N CP' _Sample_label $sample_2 save_ save_3D_hCAhNH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCAhNH' _Sample_label $sample_2 save_ save_3D_hCOhNH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCOhNH' _Sample_label $sample_2 save_ save_2D_1H-15N_CP_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N CP' _Sample_label $sample_3 save_ save_3D_RFDR-HSQC_HHN_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D RFDR-HSQC HHN' _Sample_label $sample_3 save_ save_2D_1H-15N_CP _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N CP' _BMRB_pulse_sequence_accession_number . _Details '1H-detected 2D 1H-15N correlation experiment using cross polarization (0.5 ms) for magnetization transfer.' save_ save_3D_hCAhNH _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCAhNH' _BMRB_pulse_sequence_accession_number . _Details ; 1H-detected 3D correlation experiment using HN-CACB cross polarization (2 ms) for long-range magnetization transfer. The experiment was performed on a 3.2 mm sample rotor spinning at 20 kHZ. ; save_ save_3D_RFDR-HSQC_HHN _Saveframe_category NMR_applied_experiment _Experiment_name '3D RFDR-HSQC HHN' _BMRB_pulse_sequence_accession_number . _Details ; 1H-detected 3D correlation experiment using cross polarization for magnetization transfer and 3 ms homonuclear 1H-1H RFDR mixing. The experiment was performed on a 1.9 mm sample rotor spinning at 40 kHz. ; save_ save_3D_hCOhNH _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCOhNH' _BMRB_pulse_sequence_accession_number . _Details ; 1H-detected 3D correlation experiment using HN-CO cross polarization (2 ms) for long-range magnetization transfer. The experiment was performed on a 3.2 mm sample rotor spinning at 20 kHZ. ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'solution-state NMR experiments' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH temperature 295 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details 'MAS NMR experiments in 3.2mm rotor.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH temperature 277 . K stop_ save_ save_sample_conditions_3 _Saveframe_category sample_conditions _Details 'MAS NMR experiments in 1.9mm rotor.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH temperature 289 . 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 stop_ save_ save_chemical_shift_reference_2 _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 adamantane C 13 'methylen carbons' ppm 38.48 external direct . . . adamantane H 1 'methylen carbon' ppm 38.48 external indirect . . . adamantane N 15 'methylen carbons' ppm 38.48 external indirect . . . 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_aB_ACD _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N CP' '3D hCAhNH' '3D hCOhNH' '3D RFDR-HSQC HHN' stop_ loop_ _Sample_label $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chemical_shift_reference_2 _Mol_system_component_name 'alpha B crystallin, 1' _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 75 75 PHE C C 172.832 0.000 . 2 76 76 SER H H 8.118 0.000 . 3 76 76 SER CA C 56.290 0.000 . 4 76 76 SER N N 117.898 0.000 . 5 84 84 PHE C C 174.415 0.000 . 6 84 84 PHE CA C 57.331 0.000 . 7 85 85 SER H H 9.362 0.000 . 8 85 85 SER CA C 56.643 0.000 . 9 85 85 SER CB C 62.261 0.000 . 10 85 85 SER N N 120.771 0.000 . 11 86 86 PRO C C 178.532 0.000 . 12 86 86 PRO CA C 66.241 0.000 . 13 87 87 GLU H H 8.398 0.000 . 14 87 87 GLU C C 177.649 0.068 . 15 87 87 GLU CA C 57.647 0.181 . 16 87 87 GLU CB C 27.793 0.000 . 17 87 87 GLU N N 112.661 0.000 . 18 88 88 GLU H H 7.919 0.000 . 19 88 88 GLU C C 174.732 0.000 . 20 88 88 GLU CA C 55.883 0.045 . 21 88 88 GLU CB C 29.512 0.000 . 22 88 88 GLU N N 121.288 0.000 . 23 89 89 LEU H H 6.973 0.000 . 24 89 89 LEU C C 175.365 0.000 . 25 89 89 LEU CA C 53.214 0.000 . 26 89 89 LEU N N 120.587 0.000 . 27 90 90 LYS H H 8.388 0.000 . 28 90 90 LYS CA C 55.204 0.000 . 29 90 90 LYS CB C 36.026 0.000 . 30 90 90 LYS N N 119.397 0.000 . 31 91 91 VAL C C 174.777 0.000 . 32 91 91 VAL CA C 61.121 0.000 . 33 92 92 LYS H H 9.062 0.000 . 34 92 92 LYS C C 174.823 0.000 . 35 92 92 LYS CA C 54.571 0.000 . 36 92 92 LYS CB C 36.243 0.000 . 37 92 92 LYS N N 125.358 0.000 . 38 93 93 VAL H H 9.056 0.000 . 39 93 93 VAL C C 175.501 0.000 . 40 93 93 VAL CA C 61.085 0.000 . 41 93 93 VAL CB C 32.588 0.000 . 42 93 93 VAL N N 125.454 0.000 . 43 94 94 LEU H H 8.778 0.000 . 44 94 94 LEU C C 176.948 0.000 . 45 94 94 LEU CA C 53.666 0.000 . 46 94 94 LEU N N 131.050 0.000 . 47 95 95 GLY H H 8.575 0.000 . 48 95 95 GLY C C 173.013 0.000 . 49 95 95 GLY CA C 47.922 0.045 . 50 95 95 GLY N N 115.870 0.000 . 51 96 96 ASP H H 8.105 0.000 . 52 96 96 ASP C C 174.461 0.000 . 53 96 96 ASP CA C 52.942 0.091 . 54 96 96 ASP N N 125.301 0.000 . 55 97 97 VAL H H 7.558 0.000 . 56 97 97 VAL C C 175.546 0.000 . 57 97 97 VAL CA C 60.949 0.045 . 58 97 97 VAL N N 118.272 0.000 . 59 98 98 ILE H H 8.966 0.000 . 60 98 98 ILE C C 175.230 0.000 . 61 98 98 ILE CA C 59.245 0.085 . 62 98 98 ILE N N 123.553 0.000 . 63 99 99 GLU H H 9.460 0.000 . 64 99 99 GLU C C 174.777 0.000 . 65 99 99 GLU CA C 54.073 0.046 . 66 99 99 GLU N N 126.850 0.000 . 67 100 100 VAL H H 9.539 0.000 . 68 100 100 VAL C C 173.895 0.158 . 69 100 100 VAL CA C 61.130 0.045 . 70 100 100 VAL N N 124.201 0.000 . 71 101 101 HIS H H 9.014 0.000 . 72 101 101 HIS C C 173.873 0.000 . 73 101 101 HIS CA C 52.626 0.045 . 74 101 101 HIS CB C 33.176 0.000 . 75 101 101 HIS N N 128.495 0.000 . 76 102 102 GLY H H 6.728 0.000 . 77 102 102 GLY C C 171.023 0.000 . 78 102 102 GLY CA C 43.489 0.407 . 79 102 102 GLY N N 113.031 0.000 . 80 103 103 LYS H H 8.104 0.000 . 81 103 103 LYS C C 174.868 0.000 . 82 103 103 LYS CA C 56.019 0.000 . 83 103 103 LYS CB C 35.483 0.000 . 84 103 103 LYS N N 124.334 0.000 . 85 104 104 HIS H H 9.356 0.000 . 86 104 104 HIS C C 175.546 0.000 . 87 104 104 HIS CA C 53.757 0.090 . 88 104 104 HIS N N 124.548 0.000 . 89 105 105 GLU H H 8.961 0.000 . 90 105 105 GLU C C 176.270 0.000 . 91 105 105 GLU CA C 54.888 0.045 . 92 105 105 GLU CB C 29.331 0.000 . 93 105 105 GLU N N 122.966 0.000 . 94 106 106 GLU H H 8.626 0.000 . 95 106 106 GLU C C 175.999 0.000 . 96 106 106 GLU CA C 58.281 0.090 . 97 106 106 GLU CB C 29.512 0.000 . 98 106 106 GLU N N 121.316 0.000 . 99 107 107 ARG H H 8.756 0.000 . 100 107 107 ARG C C 174.687 0.000 . 101 107 107 ARG CA C 54.384 0.172 . 102 107 107 ARG N N 124.722 0.000 . 103 108 108 GLN H H 8.574 0.000 . 104 108 108 GLN HE21 H 7.228 0.000 2 105 108 108 GLN HE22 H 6.549 0.000 2 106 108 108 GLN CA C 55.566 0.000 . 107 108 108 GLN CB C 29.060 0.000 . 108 108 108 GLN CD C 180.726 0.022 . 109 108 108 GLN N N 122.471 0.000 . 110 108 108 GLN NE2 N 111.413 0.011 . 111 109 109 ASP H H 8.711 0.000 . 112 109 109 ASP CA C 52.129 0.000 . 113 109 109 ASP CB C 41.001 0.000 . 114 109 109 ASP N N 128.314 0.000 . 115 111 111 HIS C C 175.320 0.000 . 116 111 111 HIS CA C 54.933 0.000 . 117 112 112 GLY H H 7.324 0.000 . 118 112 112 GLY CA C 45.796 0.000 . 119 112 112 GLY N N 108.838 0.000 . 120 113 113 PHE C C 175.094 0.000 . 121 114 114 ILE H H 9.292 0.000 . 122 114 114 ILE C C 173.149 0.000 . 123 114 114 ILE CA C 56.873 0.186 . 124 114 114 ILE N N 120.794 0.000 . 125 115 115 SER H H 8.957 0.000 . 126 115 115 SER C C 172.877 0.000 . 127 115 115 SER CA C 57.014 0.091 . 128 115 115 SER N N 122.119 0.000 . 129 116 116 ARG H H 6.023 0.000 . 130 116 116 ARG C C 174.732 0.181 . 131 116 116 ARG CA C 55.295 0.000 . 132 116 116 ARG N N 115.698 0.000 . 133 117 117 GLU H H 9.074 0.000 . 134 117 117 GLU C C 174.415 0.000 . 135 117 117 GLU CA C 55.385 0.000 . 136 117 117 GLU N N 121.167 0.000 . 137 118 118 PHE H H 9.219 0.000 . 138 118 118 PHE C C 172.335 0.000 . 139 118 118 PHE CA C 56.335 0.136 . 140 118 118 PHE N N 121.749 0.000 . 141 119 119 HIS H H 8.300 0.000 . 142 119 119 HIS C C 173.737 0.000 . 143 119 119 HIS CA C 55.453 0.068 . 144 119 119 HIS N N 118.388 0.000 . 145 120 120 ARG H H 9.525 0.000 . 146 120 120 ARG CA C 52.774 0.000 . 147 120 120 ARG N N 128.902 0.000 . 148 121 121 LYS C C 175.546 0.000 . 149 121 121 LYS CA C 54.662 0.000 . 150 122 122 TYR H H 9.236 0.000 . 151 122 122 TYR CA C 56.652 0.000 . 152 122 122 TYR CB C 41.544 0.000 . 153 122 122 TYR N N 120.138 0.000 . 154 123 123 ARG C C 176.270 0.000 . 155 123 123 ARG CA C 54.797 0.000 . 156 124 124 ILE H H 8.616 0.000 . 157 124 124 ILE CA C 59.592 0.000 . 158 124 124 ILE N N 127.895 0.000 . 159 125 125 PRO C C 176.722 0.136 . 160 125 125 PRO CA C 62.623 0.000 . 161 126 126 ALA H H 8.276 0.000 . 162 126 126 ALA C C 177.175 0.000 . 163 126 126 ALA CA C 54.571 0.000 . 164 126 126 ALA CB C 18.113 0.000 . 165 126 126 ALA N N 121.197 0.000 . 166 127 127 ASP H H 8.058 0.000 . 167 127 127 ASP C C 173.918 0.000 . 168 127 127 ASP CA C 52.671 0.000 . 169 127 127 ASP N N 113.699 0.000 . 170 128 128 VAL H H 7.326 0.000 . 171 128 128 VAL C C 174.642 0.000 . 172 128 128 VAL CA C 61.085 0.000 . 173 128 128 VAL N N 120.515 0.000 . 174 129 129 ASP H H 8.575 0.000 . 175 129 129 ASP CA C 51.314 0.000 . 176 129 129 ASP CB C 40.820 0.000 . 177 129 129 ASP N N 127.725 0.000 . 178 130 130 PRO C C 178.170 0.000 . 179 130 130 PRO CA C 64.432 0.000 . 180 131 131 LEU H H 8.234 0.000 . 181 131 131 LEU C C 178.260 0.000 . 182 131 131 LEU CA C 56.561 0.000 . 183 131 131 LEU N N 116.006 0.000 . 184 132 132 THR H H 7.911 0.000 . 185 132 132 THR C C 174.008 0.000 . 186 132 132 THR CA C 60.940 0.181 . 187 132 132 THR N N 107.608 0.000 . 188 133 133 ILE H H 6.574 0.000 . 189 133 133 ILE C C 176.270 0.000 . 190 133 133 ILE CA C 60.786 0.027 . 191 133 133 ILE CB C 36.786 0.000 . 192 133 133 ILE CG1 C 27.160 0.000 . 193 133 133 ILE N N 122.303 0.000 . 194 134 134 THR H H 8.874 0.000 . 195 134 134 THR C C 173.059 0.046 . 196 134 134 THR CA C 60.044 0.226 . 197 134 134 THR N N 118.098 0.000 . 198 135 135 SER H H 8.452 0.000 . 199 135 135 SER C C 173.104 0.000 . 200 135 135 SER CA C 57.104 0.000 . 201 135 135 SER N N 113.038 0.000 . 202 136 136 SER H H 8.780 0.000 . 203 136 136 SER C C 171.566 0.045 . 204 136 136 SER CA C 56.969 0.045 . 205 136 136 SER CB C 66.422 0.000 . 206 136 136 SER N N 118.696 0.000 . 207 137 137 LEU H H 8.421 0.000 . 208 137 137 LEU C C 176.315 0.000 . 209 137 137 LEU CA C 53.124 0.000 . 210 137 137 LEU CB C 43.263 0.000 . 211 137 137 LEU N N 123.674 0.000 . 212 138 138 SER H H 8.747 0.000 . 213 138 138 SER CA C 57.014 0.000 . 214 138 138 SER CB C 65.156 0.000 . 215 138 138 SER N N 123.539 0.000 . 216 140 140 ASP C C 176.315 0.000 . 217 140 140 ASP CA C 53.214 0.000 . 218 141 141 GLY H H 7.674 0.000 . 219 141 141 GLY C C 171.566 0.000 . 220 141 141 GLY CA C 47.243 0.000 . 221 141 141 GLY N N 108.018 0.000 . 222 142 142 VAL H H 7.416 0.000 . 223 142 142 VAL C C 176.406 0.000 . 224 142 142 VAL CA C 61.379 0.068 . 225 142 142 VAL N N 117.883 0.000 . 226 143 143 LEU H H 9.321 0.000 . 227 143 143 LEU C C 174.777 0.000 . 228 143 143 LEU CA C 54.277 0.158 . 229 143 143 LEU N N 131.025 0.000 . 230 144 144 THR H H 9.030 0.000 . 231 144 144 THR C C 174.687 0.000 . 232 144 144 THR CA C 61.175 0.045 . 233 144 144 THR N N 125.199 0.000 . 234 145 145 VAL H H 9.011 0.000 . 235 145 145 VAL CA C 61.010 0.026 . 236 145 145 VAL N N 128.257 0.000 . 237 146 146 ASN H H 8.884 0.000 . 238 146 146 ASN C C 174.054 0.000 . 239 146 146 ASN CA C 52.248 0.196 . 240 146 146 ASN N N 122.436 0.000 . 241 147 147 GLY H H 8.725 0.000 . 242 147 147 GLY CA C 45.434 0.000 . 243 147 147 GLY N N 105.969 0.000 . 244 160 160 PRO C C 176.360 0.000 . 245 160 160 PRO CA C 62.984 0.000 . 246 161 161 ILE H H 8.305 0.000 . 247 161 161 ILE C C 177.717 0.000 . 248 161 161 ILE CA C 60.904 0.000 . 249 161 161 ILE N N 124.057 0.000 . stop_ save_ save_aB_ACD_b _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N CP' '3D hCAhNH' '3D hCOhNH' '3D RFDR-HSQC HHN' stop_ loop_ _Sample_label $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chemical_shift_reference_2 _Mol_system_component_name 'alpha B crystallin, 1' _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 85 85 SER H H 9.270 0.000 . 2 85 85 SER CB C 62.568 0.000 . 3 85 85 SER N N 120.352 0.000 . 4 88 88 GLU H H 7.674 0.000 . 5 88 88 GLU CA C 56.697 0.000 . 6 88 88 GLU CB C 30.553 0.000 . 7 88 88 GLU N N 121.169 0.000 . 8 93 93 VAL C C 174.913 0.000 . 9 93 93 VAL CA C 61.311 0.000 . 10 94 94 LEU H H 8.581 0.000 . 11 94 94 LEU CA C 54.119 0.000 . 12 94 94 LEU N N 129.798 0.000 . 13 95 95 GLY H H 8.617 0.000 . 14 95 95 GLY CA C 47.913 0.000 . 15 95 95 GLY N N 116.181 0.000 . 16 99 99 GLU H H 9.553 0.000 . 17 99 99 GLU CA C 53.938 0.000 . 18 99 99 GLU N N 127.311 0.000 . 19 100 100 VAL CA C 60.904 0.000 . 20 101 101 HIS H H 8.870 0.000 . 21 101 101 HIS CA C 52.762 0.000 . 22 101 101 HIS N N 127.594 0.000 . 23 102 102 GLY H H 6.985 0.000 . 24 102 102 GLY C C 170.480 0.000 . 25 102 102 GLY CA C 43.028 0.000 . 26 102 102 GLY N N 113.110 0.000 . 27 103 103 LYS H H 7.856 0.000 . 28 103 103 LYS C C 174.687 0.000 . 29 103 103 LYS CA C 56.222 0.023 . 30 103 103 LYS N N 124.060 0.000 . 31 104 104 HIS H H 9.346 0.000 . 32 104 104 HIS CA C 53.703 0.000 . 33 104 104 HIS N N 123.746 0.000 . 34 115 115 SER C C 173.036 0.000 . 35 116 116 ARG H H 6.104 0.000 . 36 116 116 ARG C C 175.478 0.000 . 37 116 116 ARG CA C 56.236 0.000 . 38 116 116 ARG N N 115.962 0.000 . 39 126 126 ALA C C 177.559 0.000 . 40 127 127 ASP H H 8.083 0.000 . 41 127 127 ASP N N 112.792 0.000 . 42 131 131 LEU C C 178.758 0.000 . 43 132 132 THR H H 7.812 0.000 . 44 132 132 THR C C 173.918 0.000 . 45 132 132 THR CA C 60.994 0.000 . 46 132 132 THR N N 106.795 0.000 . 47 133 133 ILE H H 6.744 0.000 . 48 133 133 ILE CA C 60.632 0.000 . 49 133 133 ILE N N 122.915 0.000 . stop_ save_ save_aB_CTD _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HN(CO)CA' '3D HN(CA)CO' 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 'alpha B crystallin, 1' _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 1 152 152 VAL CA C 62.265 0.000 . 2 153 153 SER H H 8.265 0.000 . 3 153 153 SER C C 175.414 0.000 . 4 153 153 SER CA C 58.427 0.003 . 5 153 153 SER N N 119.623 0.000 . 6 154 154 GLY H H 8.123 0.000 . 7 154 154 GLY C C 172.778 0.000 . 8 154 154 GLY CA C 44.963 0.000 . 9 154 154 GLY N N 110.595 0.000 . 10 155 155 PRO C C 178.131 0.011 . 11 155 155 PRO CA C 63.443 0.000 . 12 156 156 GLU H H 8.397 0.000 . 13 156 156 GLU C C 177.527 0.000 . 14 156 156 GLU CA C 56.980 0.000 . 15 156 156 GLU N N 120.739 0.000 . 16 157 157 ARG H H 8.138 0.000 . 17 157 157 ARG C C 177.235 0.015 . 18 157 157 ARG CA C 56.138 0.014 . 19 157 157 ARG N N 121.944 0.000 . 20 158 158 THR H H 8.031 0.000 . 21 158 158 THR C C 175.141 0.021 . 22 158 158 THR CA C 62.124 0.012 . 23 158 158 THR N N 116.269 0.000 . 24 159 159 ILE H H 8.032 0.000 . 25 159 159 ILE C C 175.381 0.000 . 26 159 159 ILE CA C 58.825 0.000 . 27 159 159 ILE N N 125.242 0.000 . 28 160 160 PRO C C 177.700 0.000 . 29 160 160 PRO CA C 63.252 0.000 . 30 161 161 ILE H H 8.078 0.000 . 31 161 161 ILE C C 177.555 0.008 . 32 161 161 ILE CA C 61.387 0.032 . 33 161 161 ILE N N 121.279 0.000 . 34 162 162 THR H H 8.030 0.000 . 35 162 162 THR C C 175.051 0.004 . 36 162 162 THR CA C 61.904 0.026 . 37 162 162 THR N N 118.979 0.000 . 38 163 163 ARG H H 8.222 0.000 . 39 163 163 ARG C C 176.784 0.006 . 40 163 163 ARG CA C 56.137 0.053 . 41 163 163 ARG N N 123.834 0.000 . 42 164 164 GLU H H 8.264 0.000 . 43 164 164 GLU C C 177.080 0.015 . 44 164 164 GLU CA C 56.462 0.018 . 45 164 164 GLU N N 122.629 0.000 . 46 165 165 GLU H H 8.296 0.000 . 47 165 165 GLU C C 177.059 0.017 . 48 165 165 GLU CA C 56.398 0.046 . 49 165 165 GLU N N 123.151 0.000 . 50 166 166 LYS H H 8.236 0.000 . 51 166 166 LYS C C 175.230 0.000 . 52 166 166 LYS CA C 54.302 0.000 . 53 166 166 LYS N N 123.834 0.000 . 54 167 167 PRO C C 177.552 0.003 . 55 167 167 PRO CA C 63.135 0.000 . 56 168 168 ALA H H 8.243 0.000 . 57 168 168 ALA C C 178.863 0.016 . 58 168 168 ALA CA C 52.566 0.002 . 59 168 168 ALA N N 124.524 0.000 . 60 169 169 VAL H H 8.005 0.000 . 61 169 169 VAL C C 177.387 0.052 . 62 169 169 VAL CA C 62.397 0.018 . 63 169 169 VAL N N 119.651 0.000 . 64 170 170 THR H H 8.022 0.000 . 65 170 170 THR C C 174.899 0.024 . 66 170 170 THR CA C 61.944 0.014 . 67 170 170 THR N N 118.566 0.000 . 68 171 171 ALA H H 8.105 0.000 . 69 171 171 ALA C C 177.831 0.009 . 70 171 171 ALA CA C 52.274 0.008 . 71 171 171 ALA N N 126.847 0.000 . 72 172 172 ALA H H 8.088 0.000 . 73 172 172 ALA C C 176.467 0.000 . 74 172 172 ALA CA C 50.621 0.000 . 75 172 172 ALA N N 125.011 0.000 . 76 173 173 PRO C C 177.733 0.005 . 77 173 173 PRO CA C 63.106 0.000 . 78 174 174 LYS H H 8.211 0.000 . 79 174 174 LYS C C 176.731 0.003 . 80 174 174 LYS CA C 56.551 0.011 . 81 174 174 LYS N N 122.246 0.000 . 82 175 175 LYS H H 7.785 0.000 . 83 175 175 LYS C C 182.297 0.000 . 84 175 175 LYS CA C 57.925 0.000 . 85 175 175 LYS N N 128.028 0.000 . stop_ save_ save_aB_CTD_b _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HN(CO)CA' '3D HN(CA)CO' 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 'alpha B crystallin, 1' _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 1 153 153 SER C C 175.296 0.000 . 2 154 154 GLY H H 8.064 0.000 . 3 154 154 GLY CA C 44.444 0.000 . 4 154 154 GLY N N 110.609 0.000 . 5 155 155 PRO C C 177.579 0.000 . 6 155 155 PRO CA C 62.640 0.000 . 7 156 156 GLU H H 8.508 0.000 . 8 156 156 GLU C C 177.334 0.004 . 9 156 156 GLU CA C 57.029 0.050 . 10 156 156 GLU N N 121.707 0.000 . 11 157 157 ARG H H 8.349 0.000 . 12 157 157 ARG C C 177.158 0.109 . 13 157 157 ARG CA C 56.043 0.067 . 14 157 157 ARG N N 122.626 0.000 . 15 158 158 THR H H 7.939 0.000 . 16 158 158 THR C C 173.939 0.000 . 17 158 158 THR CA C 62.215 0.022 . 18 158 158 THR N N 116.386 0.000 . 19 159 159 ILE H H 7.717 0.000 . 20 159 159 ILE C C 175.837 0.000 . 21 159 159 ILE CA C 58.209 0.000 . 22 159 159 ILE N N 121.440 0.000 . 23 160 160 PRO C C 177.144 0.001 . 24 160 160 PRO CA C 62.811 0.024 . 25 161 161 ILE H H 8.280 0.000 . 26 161 161 ILE C C 177.630 0.000 . 27 161 161 ILE CA C 62.080 0.000 . 28 161 161 ILE N N 120.823 0.000 . 29 165 165 GLU C C 176.132 0.010 . 30 165 165 GLU CA C 56.562 0.042 . 31 166 166 LYS H H 7.970 0.000 . 32 166 166 LYS C C 175.474 0.000 . 33 166 166 LYS CA C 53.760 0.000 . 34 166 166 LYS N N 121.997 0.000 . 35 167 167 PRO C C 176.534 0.030 . 36 167 167 PRO CA C 62.889 0.000 . 37 168 168 ALA H H 8.288 0.000 . 38 168 168 ALA C C 178.923 0.016 . 39 168 168 ALA CA C 52.672 0.018 . 40 168 168 ALA N N 123.676 0.000 . 41 169 169 VAL H H 8.134 0.000 . 42 169 169 VAL C C 177.363 0.028 . 43 169 169 VAL CA C 62.410 0.000 . 44 169 169 VAL N N 120.304 0.000 . 45 170 170 THR H H 8.048 0.000 . 46 170 170 THR C C 174.251 0.014 . 47 170 170 THR CA C 61.904 0.000 . 48 170 170 THR N N 118.640 0.000 . 49 171 171 ALA H H 8.105 0.000 . 50 171 171 ALA C C 177.103 0.008 . 51 171 171 ALA CA C 52.479 0.000 . 52 171 171 ALA N N 126.847 0.000 . 53 172 172 ALA H H 7.852 0.000 . 54 172 172 ALA C C 176.431 0.000 . 55 172 172 ALA CA C 50.429 0.000 . 56 172 172 ALA N N 123.016 0.000 . 57 175 175 LYS H H 7.819 0.000 . 58 175 175 LYS N N 128.492 0.000 . stop_ save_