data_17938 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Chemical Shifts Assignments of 1H, 13C, and 15N for CAP-Gly ; _BMRB_accession_number 17938 _BMRB_flat_file_name bmr17938.str _Entry_type original _Submission_date 2011-09-14 _Accession_date 2011-09-14 _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 Yan Si . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 286 "13C chemical shifts" 247 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-10-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17937 'Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules' stop_ _Original_release_date 2011-10-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19580321 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Shangjin . . 2 Siglin Amanda . . 3 Williams John C. . 4 Polenova Tatyana . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 131 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10113 _Page_last 10126 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CAP-Gly _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CAP-Gly $CAP-Gly 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_CAP-Gly _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CAP-Gly _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 88 _Mol_residue_sequence ; TEASARPLRVGSRVEVIGKG HRGTVAYVGATLFATGKWVG VILDEAKGKNDGTVQGRKYF TCDEGHGIFVRQSQIQVFED GADTTSPE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 20 THR 2 21 GLU 3 22 ALA 4 23 SER 5 24 ALA 6 25 ARG 7 26 PRO 8 27 LEU 9 28 ARG 10 29 VAL 11 30 GLY 12 31 SER 13 32 ARG 14 33 VAL 15 34 GLU 16 35 VAL 17 36 ILE 18 37 GLY 19 38 LYS 20 39 GLY 21 40 HIS 22 41 ARG 23 42 GLY 24 43 THR 25 44 VAL 26 45 ALA 27 46 TYR 28 47 VAL 29 48 GLY 30 49 ALA 31 50 THR 32 51 LEU 33 52 PHE 34 53 ALA 35 54 THR 36 55 GLY 37 56 LYS 38 57 TRP 39 58 VAL 40 59 GLY 41 60 VAL 42 61 ILE 43 62 LEU 44 63 ASP 45 64 GLU 46 65 ALA 47 66 LYS 48 67 GLY 49 68 LYS 50 69 ASN 51 70 ASP 52 71 GLY 53 72 THR 54 73 VAL 55 74 GLN 56 75 GLY 57 76 ARG 58 77 LYS 59 78 TYR 60 79 PHE 61 80 THR 62 81 CYS 63 82 ASP 64 83 GLU 65 84 GLY 66 85 HIS 67 86 GLY 68 87 ILE 69 88 PHE 70 89 VAL 71 90 ARG 72 91 GLN 73 92 SER 74 93 GLN 75 94 ILE 76 95 GLN 77 96 VAL 78 97 PHE 79 98 GLU 80 99 ASP 81 100 GLY 82 101 ALA 83 102 ASP 84 103 THR 85 104 THR 86 105 SER 87 106 PRO 88 107 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 17937 CAP-Gly 100.00 88 100.00 100.00 1.10e-55 BMRB 19025 CAP-Gly 100.00 89 100.00 100.00 9.65e-56 BMRB 19031 CAP-Gly 100.00 89 100.00 100.00 9.65e-56 BMRB 25005 CAP-Gly 100.00 89 100.00 100.00 9.65e-56 PDB 1TXQ "Crystal Structure Of The Eb1 C-Terminal Domain Complexed With The Cap-Gly Domain Of P150glued" 98.86 93 100.00 100.00 3.19e-55 PDB 2HKN "Crystal Structure Of The Cap-Gly Domain Of Human Dynactin-1 (P150- Glued)" 98.86 97 100.00 100.00 4.19e-55 PDB 2HKQ "Crystal Structure Of The C-Terminal Domain Of Human Eb1 In Complex With The Cap-Gly Domain Of Human Dynactin-1 (P150-Glued)" 98.86 97 100.00 100.00 4.19e-55 PDB 2HL3 "Crystal Structure Of The A49m Mutant Cap-gly Domain Of Human Dynactin- 1 (p150-glued) In Complex With Human Eb1 C-terminal Hexa" 98.86 97 98.85 98.85 1.84e-54 PDB 2HL5 "Crystal Structure Of The C-Terminal Domain Of Human Eb1 In Complex With The A49m Mutant Cap-Gly Domain Of Human Dynactin-1 (P15" 98.86 97 98.85 98.85 1.84e-54 PDB 2HQH "Crystal Structure Of P150glued And Clip-170" 98.86 93 100.00 100.00 3.19e-55 PDB 2M02 "3d Structure Of Cap-gly Domain Of Mammalian Dynactin Determined By Magic Angle Spinning Nmr Spectroscopy" 100.00 89 100.00 100.00 9.65e-56 PDB 2MPX "Three-dimensional Structure Of Cap-gly Domain Assembled On Microtubules Determined By Mas Nmr Spectroscopy" 79.55 70 100.00 100.00 7.68e-42 PDB 3E2U "Crystal Structure Of The Zink-Knuckle 2 Domain Of Human Clip-170 In Complex With Cap-Gly Domain Of Human Dynactin-1 (P150-Glued" 98.86 97 100.00 100.00 4.19e-55 PDB 3TQ7 "Eb1cEB3C HETERODIMER IN COMPLEX WITH THE CAP-Gly Domain Of P150glued" 80.68 71 98.59 98.59 1.65e-41 DBJ BAE34241 "unnamed protein product [Mus musculus]" 100.00 1243 100.00 100.00 1.82e-51 DBJ BAE37079 "unnamed protein product [Mus musculus]" 100.00 395 100.00 100.00 1.35e-50 DBJ BAE42418 "unnamed protein product [Mus musculus]" 100.00 1239 100.00 100.00 3.25e-51 DBJ BAE42912 "unnamed protein product [Mus musculus]" 100.00 1239 100.00 100.00 2.52e-51 DBJ BAE87998 "unnamed protein product [Macaca fascicularis]" 98.86 409 100.00 100.00 2.29e-55 EMBL CAA44091 "150K dynein-associated polypeptide [Rattus norvegicus]" 100.00 1280 100.00 100.00 3.13e-51 EMBL CAA67333 "dynactin [Homo sapiens]" 98.86 1263 100.00 100.00 1.58e-50 EMBL CAE45882 "hypothetical protein [Homo sapiens]" 98.86 1278 100.00 100.00 1.97e-50 EMBL CAH10572 "hypothetical protein [Homo sapiens]" 98.86 890 100.00 100.00 5.76e-51 EMBL CAH10575 "hypothetical protein [Homo sapiens]" 98.86 890 100.00 100.00 7.42e-51 GB AAB57773 "dynactin1 [Mus musculus]" 100.00 1281 100.00 100.00 4.54e-51 GB AAD03694 "dynactin 1 [Homo sapiens]" 98.86 1261 100.00 100.00 1.58e-50 GB AAD55811 "dynactin 1 p150 isoform [Homo sapiens]" 98.86 1278 100.00 100.00 1.62e-50 GB AAH66061 "Dctn1 protein [Mus musculus]" 100.00 1264 98.86 98.86 1.03e-49 GB AAI42510 "DCTN1 protein [Bos taurus]" 98.86 1239 100.00 100.00 8.47e-51 REF NP_001092404 "dynactin subunit 1 [Bos taurus]" 98.86 1239 100.00 100.00 8.47e-51 REF NP_001127253 "dynactin subunit 1 [Pongo abelii]" 67.05 233 100.00 100.00 5.90e-35 REF NP_001128512 "dynactin subunit 1 isoform 3 [Homo sapiens]" 98.86 1253 100.00 100.00 1.16e-50 REF NP_001177765 "dynactin subunit 1 isoform 5 [Homo sapiens]" 98.86 1236 100.00 100.00 8.18e-51 REF NP_001177766 "dynactin subunit 1 isoform 6 [Homo sapiens]" 98.86 1271 100.00 100.00 1.60e-50 SP O08788 "RecName: Full=Dynactin subunit 1; AltName: Full=150 kDa dynein-associated polypeptide; AltName: Full=DAP-150; Short=DP-150; Alt" 100.00 1281 100.00 100.00 4.08e-51 SP P28023 "RecName: Full=Dynactin subunit 1; AltName: Full=150 kDa dynein-associated polypeptide; AltName: Full=DAP-150; Short=DP-150; Alt" 100.00 1280 100.00 100.00 3.13e-51 SP Q14203 "RecName: Full=Dynactin subunit 1; AltName: Full=150 kDa dynein-associated polypeptide; AltName: Full=DAP-150; Short=DP-150; Alt" 98.86 1278 100.00 100.00 1.62e-50 TPG DAA24857 "TPA: dynactin 1 [Bos taurus]" 98.86 1239 100.00 100.00 8.47e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CAP-Gly 'E. coli' 562 Bacteria . Escherichia coli 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 $CAP-Gly 'recombinant technology' . Escherichia coli BL21(DE3) pET28b-His6-SMT3 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 $CAP-Gly 0.96 mM '[U-100% 13C; U-100% 15N]' 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 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . 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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(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 'ionic strength' 90 . mM pH 6.0 . pH pressure 1 . atm temperature 298 . 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_ ################################### # 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 '3D HNCA' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' '3D HBHA(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 CAP-Gly _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 20 1 THR H H 8.3 . 1 2 20 1 THR HA H 4.3 . 1 3 20 1 THR HB H 4.2 . 1 4 20 1 THR C C 174.7 . 1 5 20 1 THR CA C 62.1 . 1 6 20 1 THR CB C 69.6 . 1 7 20 1 THR N N 115.9 . 1 8 21 2 GLU H H 8.4 . 1 9 21 2 GLU HA H 4.2 . 1 10 21 2 GLU HB2 H 2.0 . . 11 21 2 GLU HB3 H 1.9 . . 12 21 2 GLU C C 176.5 . 1 13 21 2 GLU CA C 56.8 . 1 14 21 2 GLU CB C 30.2 . 1 15 21 2 GLU N N 123.4 . 1 16 22 3 ALA H H 8.4 . 1 17 22 3 ALA HA H 4.2 . 1 18 22 3 ALA HB H 1.3 . 1 19 22 3 ALA C C 178.0 . 1 20 22 3 ALA CA C 53.0 . 1 21 22 3 ALA CB C 19.1 . 1 22 22 3 ALA N N 125.2 . 1 23 23 4 SER H H 8.2 . 1 24 23 4 SER HA H 4.3 . 1 25 23 4 SER HB2 H 3.8 . . 26 23 4 SER C C 174.1 . 1 27 23 4 SER CA C 58.4 . 1 28 23 4 SER CB C 63.8 . 1 29 23 4 SER N N 114.4 . 1 30 24 5 ALA H H 8.1 . 1 31 24 5 ALA HA H 4.3 . 1 32 24 5 ALA HB H 1.3 . 1 33 24 5 ALA C C 177.4 . 1 34 24 5 ALA CA C 52.3 . 1 35 24 5 ALA CB C 19.3 . 1 36 24 5 ALA N N 125.7 . 1 37 25 6 ARG H H 8.2 . 1 38 25 6 ARG C C 173.9 . 1 39 25 6 ARG CA C 54.0 . 1 40 25 6 ARG N N 121.6 . 1 41 26 7 PRO HA H 4.3 . 1 42 26 7 PRO HB2 H 2.2 . . 43 26 7 PRO HB3 H 1.7 . . 44 26 7 PRO C C 175.9 . 1 45 26 7 PRO CA C 62.8 . 1 46 26 7 PRO CB C 32.2 . 1 47 27 8 LEU H H 8.2 . 1 48 27 8 LEU HA H 4.2 . 1 49 27 8 LEU HB2 H 1.4 . . 50 27 8 LEU C C 175.4 . 1 51 27 8 LEU CA C 54.9 . 1 52 27 8 LEU CB C 42.8 . 1 53 27 8 LEU N N 122.8 . 1 54 28 9 ARG H H 8.4 . 1 55 28 9 ARG HA H 4.5 . 1 56 28 9 ARG HB2 H 1.8 . . 57 28 9 ARG HB3 H 1.7 . . 58 28 9 ARG C C 176.0 . 1 59 28 9 ARG CA C 53.9 . 1 60 28 9 ARG CB C 33.1 . 1 61 28 9 ARG N N 122.9 . 1 62 29 10 VAL H H 8.6 . 1 63 29 10 VAL HA H 3.3 . 1 64 29 10 VAL HB H 1.9 . 1 65 29 10 VAL C C 177.0 . 1 66 29 10 VAL CA C 66.0 . 1 67 29 10 VAL CB C 30.8 . 1 68 29 10 VAL N N 122.6 . 1 69 30 11 GLY H H 8.9 . 1 70 30 11 GLY HA2 H 4.6 . . 71 30 11 GLY HA3 H 3.4 . . 72 30 11 GLY C C 174.8 . 1 73 30 11 GLY CA C 44.7 . 1 74 30 11 GLY N N 116.8 . 1 75 31 12 SER H H 8.2 . 1 76 31 12 SER HA H 4.3 . 1 77 31 12 SER HB2 H 3.9 . . 78 31 12 SER HB3 H 3.8 . . 79 31 12 SER C C 173.0 . 1 80 31 12 SER CA C 61.1 . 1 81 31 12 SER CB C 63.8 . 1 82 31 12 SER N N 118.0 . 1 83 32 13 ARG H H 8.9 . 1 84 32 13 ARG HA H 5.0 . 1 85 32 13 ARG HB2 H 1.7 . . 86 32 13 ARG C C 176.1 . 1 87 32 13 ARG CA C 53.4 . 1 88 32 13 ARG CB C 28.7 . 1 89 32 13 ARG N N 125.2 . 1 90 33 14 VAL H H 8.7 . 1 91 33 14 VAL HA H 5.5 . 1 92 33 14 VAL HB H 1.9 . 1 93 33 14 VAL C C 174.1 . 1 94 33 14 VAL CA C 57.9 . 1 95 33 14 VAL CB C 37.3 . 1 96 33 14 VAL N N 112.5 . 1 97 34 15 GLU H H 8.8 . 1 98 34 15 GLU HA H 5.1 . 1 99 34 15 GLU HB2 H 1.8 . . 100 34 15 GLU C C 175.8 . 1 101 34 15 GLU CA C 53.8 . 1 102 34 15 GLU CB C 34.1 . 1 103 34 15 GLU N N 118.9 . 1 104 35 16 VAL H H 8.6 . 1 105 35 16 VAL HA H 4.2 . 1 106 35 16 VAL HB H 1.9 . 1 107 35 16 VAL C C 175.9 . 1 108 35 16 VAL CA C 62.8 . 1 109 35 16 VAL CB C 31.8 . 1 110 35 16 VAL N N 124.4 . 1 111 36 17 ILE H H 8.3 . 1 112 36 17 ILE HA H 3.7 . 1 113 36 17 ILE HB H 1.5 . 1 114 36 17 ILE C C 177.8 . 1 115 36 17 ILE CA C 63.9 . 1 116 36 17 ILE CB C 38.0 . 1 117 36 17 ILE N N 132.0 . 1 118 37 18 GLY H H 9.1 . 1 119 37 18 GLY HA2 H 4.3 . . 120 37 18 GLY HA3 H 3.6 . . 121 37 18 GLY C C 174.3 . 1 122 37 18 GLY CA C 45.6 . 1 123 37 18 GLY N N 117.4 . 1 124 38 19 LYS H H 7.6 . 1 125 38 19 LYS HA H 4.3 . 1 126 38 19 LYS HB2 H 1.1 . . 127 38 19 LYS C C 177.3 . 1 128 38 19 LYS CA C 55.6 . 1 129 38 19 LYS CB C 34.3 . 1 130 38 19 LYS N N 117.4 . 1 131 39 20 GLY H H 8.2 . 1 132 39 20 GLY HA2 H 4.0 . . 133 39 20 GLY HA3 H 3.7 . . 134 39 20 GLY C C 173.7 . 1 135 39 20 GLY CA C 45.4 . 1 136 39 20 GLY N N 105.7 . 1 137 40 21 HIS H H 6.2 . 1 138 40 21 HIS HA H 4.7 . 1 139 40 21 HIS HB2 H 3.3 . . 140 40 21 HIS HB3 H 2.7 . . 141 40 21 HIS C C 175.1 . 1 142 40 21 HIS CA C 54.9 . 1 143 40 21 HIS CB C 31.9 . 1 144 40 21 HIS N N 116.1 . 1 145 41 22 ARG H H 8.9 . 1 146 41 22 ARG HA H 5.5 . 1 147 41 22 ARG HB2 H 1.8 . . 148 41 22 ARG C C 177.3 . 1 149 41 22 ARG CA C 55.1 . 1 150 41 22 ARG CB C 32.5 . 1 151 41 22 ARG N N 122.6 . 1 152 42 23 GLY H H 8.9 . 1 153 42 23 GLY HA2 H 4.5 . . 154 42 23 GLY HA3 H 3.9 . . 155 42 23 GLY C C 170.9 . 1 156 42 23 GLY CA C 47.0 . 1 157 42 23 GLY N N 107.4 . 1 158 43 24 THR H H 8.5 . 1 159 43 24 THR HA H 5.1 . 1 160 43 24 THR HB H 3.7 . 1 161 43 24 THR C C 174.3 . 1 162 43 24 THR CA C 60.6 . 1 163 43 24 THR CB C 71.3 . 1 164 43 24 THR N N 116.9 . 1 165 44 25 VAL H H 9.3 . 1 166 44 25 VAL HA H 3.6 . 1 167 44 25 VAL HB H 2.3 . 1 168 44 25 VAL C C 175.5 . 1 169 44 25 VAL CA C 65.0 . 1 170 44 25 VAL CB C 31.4 . 1 171 44 25 VAL N N 127.6 . 1 172 45 26 ALA H H 9.1 . 1 173 45 26 ALA HA H 4.6 . 1 174 45 26 ALA HB H 0.7 . 1 175 45 26 ALA C C 175.8 . 1 176 45 26 ALA CA C 51.6 . 1 177 45 26 ALA CB C 21.8 . 1 178 45 26 ALA N N 131.9 . 1 179 46 27 TYR H H 7.6 . 1 180 46 27 TYR HA H 4.5 . 1 181 46 27 TYR HB2 H 3.3 . . 182 46 27 TYR HB3 H 2.3 . . 183 46 27 TYR C C 172.9 . 1 184 46 27 TYR CA C 58.5 . 1 185 46 27 TYR CB C 43.1 . 1 186 46 27 TYR N N 119.6 . 1 187 47 28 VAL H H 8.1 . 1 188 47 28 VAL HA H 4.8 . 1 189 47 28 VAL HB H 1.8 . 1 190 47 28 VAL C C 174.5 . 1 191 47 28 VAL CA C 61.5 . 1 192 47 28 VAL CB C 35.1 . 1 193 47 28 VAL N N 128.0 . 1 194 48 29 GLY H H 8.9 . 1 195 48 29 GLY HA2 H 4.4 . . 196 48 29 GLY HA3 H 3.9 . . 197 48 29 GLY C C 171.9 . 1 198 48 29 GLY CA C 45.0 . 1 199 48 29 GLY N N 112.9 . 1 200 49 30 ALA H H 8.7 . 1 201 49 30 ALA HA H 4.9 . 1 202 49 30 ALA HB H 1.5 . 1 203 49 30 ALA C C 178.5 . 1 204 49 30 ALA CA C 51.6 . 1 205 49 30 ALA CB C 20.1 . 1 206 49 30 ALA N N 123.6 . 1 207 50 31 THR H H 10.1 . 1 208 50 31 THR HA H 4.8 . 1 209 50 31 THR HB H 3.1 . 1 210 50 31 THR C C 173.2 . 1 211 50 31 THR CA C 59.3 . 1 212 50 31 THR CB C 72.2 . 1 213 50 31 THR N N 112.1 . 1 214 51 32 LEU H H 7.7 . 1 215 51 32 LEU HA H 4.4 . 1 216 51 32 LEU HB2 H 1.7 . . 217 51 32 LEU C C 177.7 . 1 218 51 32 LEU CA C 54.7 . 1 219 51 32 LEU CB C 41.9 . 1 220 51 32 LEU N N 113.4 . 1 221 52 33 PHE H H 6.4 . 1 222 52 33 PHE HA H 4.6 . 1 223 52 33 PHE HB2 H 3.1 . . 224 52 33 PHE HB3 H 2.5 . . 225 52 33 PHE C C 174.2 . 1 226 52 33 PHE CA C 56.2 . 1 227 52 33 PHE CB C 38.6 . 1 228 52 33 PHE N N 111.5 . 1 229 53 34 ALA H H 6.8 . 1 230 53 34 ALA HA H 4.6 . 1 231 53 34 ALA HB H 1.6 . 1 232 53 34 ALA C C 176.0 . 1 233 53 34 ALA CA C 51.9 . 1 234 53 34 ALA CB C 22.2 . 1 235 53 34 ALA N N 123.2 . 1 236 54 35 THR H H 8.4 . 1 237 54 35 THR HA H 4.5 . 1 238 54 35 THR C C 176.1 . 1 239 54 35 THR CA C 61.9 . 1 240 54 35 THR CB C 70.7 . 1 241 54 35 THR N N 110.5 . 1 242 55 36 GLY H H 8.8 . 1 243 55 36 GLY HA2 H 4.0 . . 244 55 36 GLY HA3 H 3.9 . . 245 55 36 GLY C C 172.4 . 1 246 55 36 GLY CA C 44.9 . 1 247 55 36 GLY N N 109.2 . 1 248 56 37 LYS H H 8.5 . 1 249 56 37 LYS HA H 4.2 . 1 250 56 37 LYS HB2 H 1.6 . . 251 56 37 LYS C C 176.4 . 1 252 56 37 LYS CA C 56.6 . 1 253 56 37 LYS CB C 33.5 . 1 254 56 37 LYS N N 120.9 . 1 255 57 38 TRP H H 9.1 . 1 256 57 38 TRP HA H 4.8 . 1 257 57 38 TRP HB2 H 3.3 . . 258 57 38 TRP HB3 H 3.0 . . 259 57 38 TRP C C 173.7 . 1 260 57 38 TRP CA C 56.6 . 1 261 57 38 TRP CB C 34.1 . 1 262 57 38 TRP N N 128.7 . 1 263 58 39 VAL H H 9.5 . 1 264 58 39 VAL HA H 5.0 . 1 265 58 39 VAL HB H 2.0 . 1 266 58 39 VAL C C 176.3 . 1 267 58 39 VAL CA C 60.8 . 1 268 58 39 VAL CB C 33.1 . 1 269 58 39 VAL N N 119.7 . 1 270 59 40 GLY H H 10.0 . 1 271 59 40 GLY HA2 H 4.5 . . 272 59 40 GLY HA3 H 2.7 . . 273 59 40 GLY C C 172.1 . 1 274 59 40 GLY CA C 45.7 . 1 275 59 40 GLY N N 115.5 . 1 276 60 41 VAL H H 9.1 . 1 277 60 41 VAL HA H 4.1 . 1 278 60 41 VAL HB H 1.7 . 1 279 60 41 VAL C C 173.1 . 1 280 60 41 VAL CA C 60.6 . 1 281 60 41 VAL CB C 34.9 . 1 282 60 41 VAL N N 128.4 . 1 283 61 42 ILE H H 8.6 . 1 284 61 42 ILE HA H 4.3 . 1 285 61 42 ILE HB H 1.7 . 1 286 61 42 ILE C C 177.4 . 1 287 61 42 ILE CA C 60.4 . 1 288 61 42 ILE CB C 38.7 . 1 289 61 42 ILE N N 124.6 . 1 290 62 43 LEU H H 10.1 . 1 291 62 43 LEU HA H 4.6 . 1 292 62 43 LEU HB2 H 2.2 . . 293 62 43 LEU HB3 H 1.9 . . 294 62 43 LEU C C 177.7 . 1 295 62 43 LEU CA C 55.4 . 1 296 62 43 LEU CB C 41.7 . 1 297 62 43 LEU N N 132.3 . 1 298 63 44 ASP H H 9.0 . 1 299 63 44 ASP HA H 4.4 . 1 300 63 44 ASP HB2 H 2.9 . . 301 63 44 ASP HB3 H 2.7 . . 302 63 44 ASP C C 177.5 . 1 303 63 44 ASP CA C 57.2 . 1 304 63 44 ASP CB C 39.9 . 1 305 63 44 ASP N N 125.0 . 1 306 64 45 GLU H H 8.7 . 1 307 64 45 GLU HA H 4.5 . 1 308 64 45 GLU HB2 H 1.9 . . 309 64 45 GLU HB3 H 1.6 . . 310 64 45 GLU C C 176.6 . 1 311 64 45 GLU CA C 54.3 . 1 312 64 45 GLU CB C 32.8 . 1 313 64 45 GLU N N 117.6 . 1 314 65 46 ALA H H 8.5 . 1 315 65 46 ALA HA H 3.3 . 1 316 65 46 ALA HB H 1.0 . 1 317 65 46 ALA C C 177.5 . 1 318 65 46 ALA CA C 50.8 . 1 319 65 46 ALA CB C 15.4 . 1 320 65 46 ALA N N 125.0 . 1 321 66 47 LYS H H 7.8 . 1 322 66 47 LYS HA H 4.5 . 1 323 66 47 LYS HB2 H 1.7 . . 324 66 47 LYS HB3 H 0.7 . . 325 66 47 LYS C C 175.9 . 1 326 66 47 LYS CA C 53.8 . 1 327 66 47 LYS CB C 33.2 . 1 328 66 47 LYS N N 122.3 . 1 329 67 48 GLY H H 8.5 . 1 330 67 48 GLY HA2 H 4.6 . . 331 67 48 GLY HA3 H 3.9 . . 332 67 48 GLY C C 172.7 . 1 333 67 48 GLY CA C 44.1 . 1 334 67 48 GLY N N 108.9 . 1 335 68 49 LYS H H 8.3 . 1 336 68 49 LYS HA H 4.6 . 1 337 68 49 LYS HB2 H 2.0 . . 338 68 49 LYS HB3 H 1.8 . . 339 68 49 LYS C C 175.7 . 1 340 68 49 LYS CA C 55.9 . 1 341 68 49 LYS CB C 38.4 . 1 342 68 49 LYS N N 116.1 . 1 343 69 50 ASN H H 8.5 . 1 344 69 50 ASN HA H 5.2 . 1 345 69 50 ASN HB2 H 2.9 . . 346 69 50 ASN HB3 H 2.8 . . 347 69 50 ASN C C 173.1 . 1 348 69 50 ASN CA C 53.3 . 1 349 69 50 ASN CB C 40.6 . 1 350 69 50 ASN N N 116.7 . 1 351 70 51 ASP H H 8.1 . 1 352 70 51 ASP HA H 4.7 . 1 353 70 51 ASP HB2 H 3.5 . . 354 70 51 ASP HB3 H 2.3 . . 355 70 51 ASP C C 177.7 . 1 356 70 51 ASP CA C 52.9 . 1 357 70 51 ASP CB C 40.6 . 1 358 70 51 ASP N N 119.2 . 1 359 71 52 GLY H H 8.8 . 1 360 71 52 GLY HA2 H 3.6 . . 361 71 52 GLY HA3 H 1.3 . . 362 71 52 GLY C C 174.1 . 1 363 71 52 GLY CA C 43.3 . 1 364 71 52 GLY N N 110.0 . 1 365 72 53 THR H H 7.8 . 1 366 72 53 THR HA H 5.3 . 1 367 72 53 THR HB H 4.1 . 1 368 72 53 THR C C 174.4 . 1 369 72 53 THR CA C 61.2 . 1 370 72 53 THR CB C 69.2 . 1 371 72 53 THR N N 117.1 . 1 372 73 54 VAL H H 8.4 . 1 373 73 54 VAL HA H 4.1 . 1 374 73 54 VAL HB H 1.8 . 1 375 73 54 VAL C C 176.5 . 1 376 73 54 VAL CA C 61.6 . 1 377 73 54 VAL CB C 36.0 . 1 378 73 54 VAL N N 122.8 . 1 379 74 55 GLN H H 9.8 . 1 380 74 55 GLN HA H 3.8 . 1 381 74 55 GLN HB2 H 2.3 . . 382 74 55 GLN HB3 H 1.9 . . 383 74 55 GLN C C 175.9 . 1 384 74 55 GLN CA C 56.6 . 1 385 74 55 GLN CB C 27.0 . 1 386 74 55 GLN N N 129.5 . 1 387 75 56 GLY H H 8.6 . 1 388 75 56 GLY HA2 H 4.0 . . 389 75 56 GLY HA3 H 3.5 . . 390 75 56 GLY C C 173.1 . 1 391 75 56 GLY CA C 45.4 . 1 392 75 56 GLY N N 103.7 . 1 393 76 57 ARG H H 7.6 . 1 394 76 57 ARG HA H 4.4 . 1 395 76 57 ARG HB2 H 1.6 . . 396 76 57 ARG HB3 H 1.5 . . 397 76 57 ARG C C 172.6 . 1 398 76 57 ARG CA C 53.7 . 1 399 76 57 ARG CB C 31.2 . 1 400 76 57 ARG N N 121.9 . 1 401 77 58 LYS H H 8.5 . 1 402 77 58 LYS HA H 4.3 . 1 403 77 58 LYS HB2 H 1.6 . . 404 77 58 LYS HB3 H 1.4 . . 405 77 58 LYS C C 175.8 . 1 406 77 58 LYS CA C 56.2 . 1 407 77 58 LYS CB C 32.4 . 1 408 77 58 LYS N N 127.3 . 1 409 78 59 TYR H H 8.8 . 1 410 78 59 TYR HA H 4.2 . 1 411 78 59 TYR HB2 H 2.9 . . 412 78 59 TYR HB3 H 2.4 . . 413 78 59 TYR C C 174.8 . 1 414 78 59 TYR CA C 60.4 . 1 415 78 59 TYR CB C 39.6 . 1 416 78 59 TYR N N 127.5 . 1 417 79 60 PHE H H 8.0 . 1 418 79 60 PHE HA H 4.8 . 1 419 79 60 PHE HB2 H 3.4 . . 420 79 60 PHE HB3 H 3.2 . . 421 79 60 PHE C C 172.1 . 1 422 79 60 PHE CA C 55.7 . 1 423 79 60 PHE CB C 38.7 . 1 424 79 60 PHE N N 113.8 . 1 425 80 61 THR H H 8.6 . 1 426 80 61 THR HA H 4.7 . 1 427 80 61 THR HB H 3.9 . 1 428 80 61 THR C C 172.6 . 1 429 80 61 THR CA C 62.3 . 1 430 80 61 THR CB C 71.0 . 1 431 80 61 THR N N 114.6 . 1 432 81 62 CYS H H 7.9 . 1 433 81 62 CYS HA H 4.8 . 1 434 81 62 CYS HB2 H 3.3 . . 435 81 62 CYS HB3 H 2.8 . . 436 81 62 CYS C C 172.0 . 1 437 81 62 CYS CA C 55.9 . 1 438 81 62 CYS CB C 31.8 . 1 439 81 62 CYS N N 120.5 . 1 440 82 63 ASP H H 8.2 . 1 441 82 63 ASP HA H 4.5 . 1 442 82 63 ASP HB2 H 2.6 . . 443 82 63 ASP HB3 H 2.0 . . 444 82 63 ASP C C 176.5 . 1 445 82 63 ASP CA C 54.7 . 1 446 82 63 ASP CB C 41.2 . 1 447 82 63 ASP N N 118.1 . 1 448 83 64 GLU H H 8.8 . 1 449 83 64 GLU HA H 3.8 . 1 450 83 64 GLU HB2 H 2.1 . . 451 83 64 GLU HB3 H 1.9 . . 452 83 64 GLU C C 177.7 . 1 453 83 64 GLU CA C 58.2 . 1 454 83 64 GLU CB C 29.6 . 1 455 83 64 GLU N N 121.2 . 1 456 84 65 GLY H H 8.2 . 1 457 84 65 GLY HA2 H 4.1 . . 458 84 65 GLY HA3 H 3.3 . . 459 84 65 GLY C C 174.4 . 1 460 84 65 GLY CA C 45.3 . 1 461 84 65 GLY N N 111.7 . 1 462 85 66 HIS H H 8.2 . 1 463 85 66 HIS HA H 4.7 . 1 464 85 66 HIS HB2 H 3.7 . . 465 85 66 HIS HB3 H 3.4 . . 466 85 66 HIS C C 173.8 . 1 467 85 66 HIS CA C 56.3 . 1 468 85 66 HIS CB C 29.2 . 1 469 85 66 HIS N N 113.7 . 1 470 86 67 GLY H H 9.1 . 1 471 86 67 GLY HA2 H 5.0 . . 472 86 67 GLY HA3 H 3.6 . . 473 86 67 GLY C C 174.2 . 1 474 86 67 GLY CA C 45.6 . 1 475 86 67 GLY N N 112.1 . 1 476 87 68 ILE H H 8.9 . 1 477 87 68 ILE HA H 4.8 . 1 478 87 68 ILE HB H 1.8 . 1 479 87 68 ILE C C 172.5 . 1 480 87 68 ILE CA C 60.4 . 1 481 87 68 ILE CB C 43.5 . 1 482 87 68 ILE N N 119.3 . 1 483 88 69 PHE H H 8.9 . 1 484 88 69 PHE HA H 5.8 . 1 485 88 69 PHE HB2 H 3.0 . . 486 88 69 PHE HB3 H 2.6 . . 487 88 69 PHE C C 175.6 . 1 488 88 69 PHE CA C 57.6 . 1 489 88 69 PHE CB C 41.9 . 1 490 88 69 PHE N N 122.9 . 1 491 89 70 VAL H H 9.6 . 1 492 89 70 VAL HA H 5.2 . 1 493 89 70 VAL HB H 2.5 . 1 494 89 70 VAL C C 175.2 . 1 495 89 70 VAL CA C 58.9 . 1 496 89 70 VAL CB C 36.5 . 1 497 89 70 VAL N N 115.3 . 1 498 90 71 ARG H H 8.7 . 1 499 90 71 ARG HA H 4.2 . 1 500 90 71 ARG HB2 H 2.0 . . 501 90 71 ARG HB3 H 1.7 . . 502 90 71 ARG C C 178.7 . 1 503 90 71 ARG CA C 53.5 . 1 504 90 71 ARG CB C 31.5 . 1 505 90 71 ARG N N 117.9 . 1 506 91 72 GLN H H 9.4 . 1 507 91 72 GLN HA H 3.6 . 1 508 91 72 GLN HB2 H 1.9 . . 509 91 72 GLN HB3 H 1.8 . . 510 91 72 GLN C C 176.2 . 1 511 91 72 GLN CA C 59.6 . 1 512 91 72 GLN CB C 27.8 . 1 513 91 72 GLN N N 121.9 . 1 514 92 73 SER H H 7.6 . 1 515 92 73 SER HA H 4.2 . 1 516 92 73 SER HB2 H 4.0 . . 517 92 73 SER HB3 H 3.8 . . 518 92 73 SER C C 175.3 . 1 519 92 73 SER CA C 59.2 . 1 520 92 73 SER CB C 62.7 . 1 521 92 73 SER N N 108.9 . 1 522 93 74 GLN H H 7.9 . 1 523 93 74 GLN HA H 4.3 . 1 524 93 74 GLN HB2 H 2.4 . . 525 93 74 GLN C C 175.4 . 1 526 93 74 GLN CA C 56.3 . 1 527 93 74 GLN CB C 30.7 . 1 528 93 74 GLN N N 118.1 . 1 529 94 75 ILE H H 7.5 . 1 530 94 75 ILE HA H 5.4 . 1 531 94 75 ILE HB H 1.6 . 1 532 94 75 ILE C C 173.6 . 1 533 94 75 ILE CA C 58.3 . 1 534 94 75 ILE CB C 42.8 . 1 535 94 75 ILE N N 112.9 . 1 536 95 76 GLN H H 8.6 . 1 537 95 76 GLN HA H 4.8 . 1 538 95 76 GLN HB2 H 1.9 . . 539 95 76 GLN C C 175.0 . 1 540 95 76 GLN CA C 53.6 . 1 541 95 76 GLN CB C 32.5 . 1 542 95 76 GLN N N 118.8 . 1 543 96 77 VAL H H 8.8 . 1 544 96 77 VAL HA H 4.4 . 1 545 96 77 VAL HB H 1.9 . 1 546 96 77 VAL C C 175.9 . 1 547 96 77 VAL CA C 62.5 . 1 548 96 77 VAL CB C 32.7 . 1 549 96 77 VAL N N 125.5 . 1 550 97 78 PHE H H 8.4 . 1 551 97 78 PHE HA H 4.8 . 1 552 97 78 PHE HB2 H 2.9 . . 553 97 78 PHE C C 174.3 . 1 554 97 78 PHE CA C 56.8 . 1 555 97 78 PHE CB C 40.9 . 1 556 97 78 PHE N N 125.7 . 1 557 98 79 GLU H H 8.4 . 1 558 98 79 GLU HA H 4.3 . 1 559 98 79 GLU HB2 H 2.0 . . 560 98 79 GLU HB3 H 1.8 . . 561 98 79 GLU C C 175.4 . 1 562 98 79 GLU CA C 55.9 . 1 563 98 79 GLU CB C 31.1 . 1 564 98 79 GLU N N 122.1 . 1 565 99 80 ASP H H 8.5 . 1 566 99 80 ASP HA H 4.6 . 1 567 99 80 ASP HB2 H 2.7 . . 568 99 80 ASP HB3 H 2.6 . . 569 99 80 ASP C C 176.8 . 1 570 99 80 ASP CA C 54.5 . 1 571 99 80 ASP CB C 41.5 . 1 572 99 80 ASP N N 123.3 . 1 573 100 81 GLY H H 8.5 . 1 574 100 81 GLY HA2 H 3.9 . . 575 100 81 GLY C C 174.0 . 1 576 100 81 GLY CA C 45.4 . 1 577 100 81 GLY N N 110.0 . 1 578 101 82 ALA H H 8.2 . 1 579 101 82 ALA HA H 4.3 . 1 580 101 82 ALA HB H 1.3 . 1 581 101 82 ALA C C 177.5 . 1 582 101 82 ALA CA C 52.6 . 1 583 101 82 ALA CB C 19.4 . 1 584 101 82 ALA N N 123.4 . 1 585 102 83 ASP H H 8.4 . 1 586 102 83 ASP HA H 4.6 . 1 587 102 83 ASP HB2 H 2.7 . . 588 102 83 ASP HB3 H 2.6 . . 589 102 83 ASP C C 176.6 . 1 590 102 83 ASP CA C 54.2 . 1 591 102 83 ASP CB C 40.9 . 1 592 102 83 ASP N N 119.4 . 1 593 103 84 THR H H 8.1 . 1 594 103 84 THR HA H 4.4 . 1 595 103 84 THR HB H 4.3 . 1 596 103 84 THR C C 174.8 . 1 597 103 84 THR CA C 61.7 . 1 598 103 84 THR CB C 69.6 . 1 599 103 84 THR N N 114.3 . 1 600 104 85 THR H H 8.2 . 1 601 104 85 THR HA H 4.3 . 1 602 104 85 THR HB H 4.2 . 1 603 104 85 THR C C 174.4 . 1 604 104 85 THR CA C 62.0 . 1 605 104 85 THR CB C 70.1 . 1 606 104 85 THR N N 116.4 . 1 607 105 86 SER H H 8.4 . 1 608 105 86 SER C C 172.7 . 1 609 105 86 SER N N 120.0 . 1 610 106 87 PRO HA H 4.4 . 1 611 106 87 PRO HB2 H 2.2 . . 612 106 87 PRO HB3 H 2.0 . . 613 106 87 PRO C C 176.1 . 1 614 106 87 PRO CA C 63.4 . 1 615 106 87 PRO CB C 32.2 . 1 616 107 88 GLU H H 8.0 . 1 617 107 88 GLU C C 181.0 . 1 618 107 88 GLU CA C 58.1 . 1 619 107 88 GLU N N 126.0 . 1 stop_ save_