data_4473 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The molecular basis for Protein Kinase A anchoring revealed by solution NMR ; _BMRB_accession_number 4473 _BMRB_flat_file_name bmr4473.str _Entry_type original _Submission_date 1998-12-08 _Accession_date 1999-12-06 _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 Newlon M. G. . 2 Roy M. . . 3 Morikis D. . . 4 Hausken Z. E. . 5 Coghlan V. . . 6 Scott J. D. . 7 Jennings P. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 247 "13C chemical shifts" 156 "15N chemical shifts" 41 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-25 original author . stop_ _Original_release_date 2000-05-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Molecular Basis for Protein Kinase A Anchoring Revealed by Solution NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99173235 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 NEWLON M. G. . 2 ROY M. . . 3 MORIKIS D. . . 4 HAUSKEN Z. E. . 5 COGHLAN V. . . 6 SCOTT J. D. . 7 JENNINGS P. A. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 222 _Page_last 227 _Year 1999 _Details . loop_ _Keyword 'regulatory subunit' anchoring 'four-helix bundle' stop_ save_ ################################## # Molecular system description # ################################## save_Camp_dependent_protein_kinase_type_ii_regulatory_chain _Saveframe_category molecular_system _Mol_system_name 'Camp dependent protein kinase type ii regulatory chain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'chain A' $chain_A 'chain B' $chain_A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'chain A' 1 'chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_chain_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Camp dependent protein kinase type ii regulatory chain' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; HMGHIQIPPGLTELLQGYTV EVLRQQPPDLVDFAVEYFTR LREARR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 HIS 2 0 MET 3 1 GLY 4 2 HIS 5 3 ILE 6 4 GLN 7 5 ILE 8 6 PRO 9 7 PRO 10 8 GLY 11 9 LEU 12 10 THR 13 11 GLU 14 12 LEU 15 13 LEU 16 14 GLN 17 15 GLY 18 16 TYR 19 17 THR 20 18 VAL 21 19 GLU 22 20 VAL 23 21 LEU 24 22 ARG 25 23 GLN 26 24 GLN 27 25 PRO 28 26 PRO 29 27 ASP 30 28 LEU 31 29 VAL 32 30 ASP 33 31 PHE 34 32 ALA 35 33 VAL 36 34 GLU 37 35 TYR 38 36 PHE 39 37 THR 40 38 ARG 41 39 LEU 42 40 ARG 43 41 GLU 44 42 ALA 45 43 ARG 46 44 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 PDB 1L6E "Solution Structure Of The Docking And Dimerization Domain Of Protein Kinase A Ii-Alpha (Riialpha DD). ALTERNATIVELY Called The " 100.00 46 100.00 100.00 7.33e-24 PDB 1R2A "The Molecular Basis For Protein Kinase A Anchoring Revealed By Solution Nmr" 100.00 46 100.00 100.00 7.33e-24 PDB 2DRN "Docking And Dimerization Domain (DD) OF THE TYPE II-Alpha Regulatory Subunity Of Protein Kinase A (Pka) In Complex With A Pepti" 100.00 46 100.00 100.00 7.33e-24 PDB 2H9R "Docking And Dimerization Domain (DD) OF THE REGULATORY Subunit Of The Type Ii-Alpha Camp-Dependent Protein Kinase A Associated " 100.00 46 100.00 100.00 7.33e-24 PDB 2HWN "Crystal Structure Of Rii Alpha DimerizationDOCKING DOMAIN OF PKA Bound To The D-Akap2 Peptide" 97.83 45 97.78 97.78 3.54e-22 PDB 2IZX "Molecular Basis Of Akap Specificity For Pka Regulatory Subunits" 89.13 41 97.56 100.00 1.34e-18 PDB 2IZY "Molecular Basis Of Akap Specificity For Pka Regulatory Subunits" 97.83 54 100.00 100.00 7.52e-23 PDB 3TMH "Crystal Structure Of Dual-Specific A-Kinase Anchoring Protein 2 In Complex With Camp-Dependent Protein Kinase A Type Ii Alpha A" 100.00 48 100.00 100.00 6.55e-24 GB AAM97689 "cAMP-dependent protein kinase type II-alpha regulatory chain [Rattus norvegicus]" 97.83 401 97.78 97.78 3.20e-21 GB ABK42343 "PKA RIIalpha [synthetic construct]" 97.83 402 97.78 97.78 2.04e-21 GB EDL77146 "protein kinase, cAMP-dependent, regulatory, type 2, alpha, isoform CRA_a [Rattus norvegicus]" 97.83 401 97.78 97.78 2.36e-21 GB EDL77147 "protein kinase, cAMP-dependent, regulatory, type 2, alpha, isoform CRA_b [Rattus norvegicus]" 97.83 389 97.78 97.78 1.69e-21 GB EDL77148 "protein kinase, cAMP-dependent, regulatory, type 2, alpha, isoform CRA_a [Rattus norvegicus]" 97.83 401 97.78 97.78 2.36e-21 REF NP_062137 "cAMP-dependent protein kinase type II-alpha regulatory subunit [Rattus norvegicus]" 97.83 401 97.78 97.78 3.20e-21 REF XP_005075011 "PREDICTED: cAMP-dependent protein kinase type II-alpha regulatory subunit [Mesocricetus auratus]" 95.65 402 97.73 97.73 1.93e-20 REF XP_005347993 "PREDICTED: cAMP-dependent protein kinase type II-alpha regulatory subunit [Microtus ochrogaster]" 95.65 402 97.73 97.73 8.48e-21 REF XP_006243774 "PREDICTED: cAMP-dependent protein kinase type II-alpha regulatory subunit isoform X1 [Rattus norvegicus]" 97.83 417 97.78 97.78 2.66e-21 REF XP_006978360 "PREDICTED: cAMP-dependent protein kinase type II-alpha regulatory subunit isoform X1 [Peromyscus maniculatus bairdii]" 95.65 402 97.73 97.73 2.12e-20 SP P12368 "RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit" 97.83 401 97.78 97.78 3.20e-21 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Plasmid _Gene_mnemonic $chain_A mouse 10090 Eukaryota Metazoa Mus musculus pET-16b RIIa(1-44) 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 $chain_A 'recombinant technology' 'Escherichia coli' Escherichia coli . . 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 $chain_A . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _Sample_label . save_ save_3D_TOCSY-HMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY-HMQC' _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCA,HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA,HN(CO)CA _Sample_label . save_ save_13C-filtered_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-filtered NOESY' _Sample_label . save_ save_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY-HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA,HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-filtered NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 . n/a temperature 298 . K 'ionic strength' 0.012 . M pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . 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_chemical_shifts_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'chain A' _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 HIS CA C 55.09 . 1 2 . 1 HIS HA H 4.25 . 1 3 . 1 HIS CB C 29.51 . 1 4 . 1 HIS HB2 H 3.3 . 2 5 . 2 MET N N 123.70 . 1 6 . 2 MET H H 8.85 . 1 7 . 2 MET CA C 55.61 . 1 8 . 2 MET HA H 4.45 . 1 9 . 2 MET CB C 33.42 . 1 10 . 2 MET HB2 H 2.02 . 1 11 . 2 MET HB3 H 1.96 . 1 12 . 3 GLY N N 110.79 . 1 13 . 3 GLY H H 8.57 . 1 14 . 3 GLY CA C 45.17 . 1 15 . 3 GLY HA2 H 3.88 . 1 16 . 3 GLY HA3 H 3.94 . 1 17 . 4 HIS N N 118.00 . 1 18 . 4 HIS H H 8.42 . 1 19 . 4 HIS CA C 55.35 . 1 20 . 4 HIS HA H 4.72 . 1 21 . 4 HIS CB C 29.51 . 1 22 . 4 HIS HB2 H 3.19 . 1 23 . 4 HIS HB3 H 3.14 . 1 24 . 5 ILE N N 122.84 . 1 25 . 5 ILE H H 8.24 . 1 26 . 5 ILE CA C 61.36 . 1 27 . 5 ILE HA H 4.11 . 1 28 . 5 ILE CB C 38.91 . 1 29 . 5 ILE HB H 1.74 . 1 30 . 5 ILE HG12 H 1.39 . 2 31 . 5 ILE HG13 H 1.08 . 2 32 . 5 ILE HG2 H 0.81 . 1 33 . 5 ILE HD1 H 0.78 . 1 34 . 5 ILE CG1 C 26.97 . 1 35 . 5 ILE CG2 C 17.43 . 1 36 . 5 ILE CD1 C 13.06 . 1 37 . 6 GLN N N 125.31 . 1 38 . 6 GLN H H 8.39 . 1 39 . 6 GLN CA C 55.09 . 1 40 . 6 GLN HA H 4.31 . 1 41 . 6 GLN CB C 28.34 . 1 42 . 6 GLN HB2 H 1.90 . 1 43 . 6 GLN HB3 H 1.96 . 1 44 . 6 GLN HG2 H 2.22 . 2 45 . 6 GLN HE21 H 7.48 . 2 46 . 6 GLN HE22 H 6.86 . 2 47 . 6 GLN CG C 33.38 . 1 48 . 7 ILE N N 124.13 . 1 49 . 7 ILE H H 8.31 . 1 50 . 7 ILE CA C 58.22 . 1 51 . 7 ILE HA H 4.27 . 1 52 . 7 ILE CB C 38.38 . 1 53 . 7 ILE HB H 1.89 . 1 54 . 7 ILE HG12 H 1.54 . 2 55 . 7 ILE HG13 H 1.16 . 2 56 . 7 ILE HG2 H 0.95 . 1 57 . 7 ILE HD1 H 0.81 . 1 58 . 7 ILE CG1 C 27.42 . 1 59 . 7 ILE CG2 C 17.77 . 1 60 . 7 ILE CD1 C 12.28 . 1 61 . 8 PRO CA C 61.10 . 1 62 . 8 PRO HA H 4.71 . 1 63 . 8 PRO CB C 31.36 . 1 64 . 8 PRO HB2 H 2.40 . 1 65 . 8 PRO HB3 H 1.85 . 1 66 . 8 PRO HG2 H 1.91 . 2 67 . 8 PRO HG3 H 2.03 . 2 68 . 8 PRO HD2 H 3.96 . 2 69 . 8 PRO HD3 H 3.45 . 2 70 . 8 PRO CG C 27.81 . 1 71 . 8 PRO CD C 50.64 . 1 72 . 9 PRO CA C 64.27 . 1 73 . 9 PRO HA H 4.39 . 1 74 . 9 PRO CB C 30.88 . 1 75 . 9 PRO HB2 H 2.33 . 1 76 . 9 PRO HB3 H 1.99 . 1 77 . 9 PRO HG2 H 2.06 . 2 78 . 9 PRO HD2 H 3.91 . 2 79 . 9 PRO HD3 H 3.73 . 2 80 . 9 PRO CG C 27.06 . 1 81 . 9 PRO CD C 51.10 . 1 82 . 10 GLY N N 108.68 . 1 83 . 10 GLY H H 8.72 . 1 84 . 10 GLY CA C 45.43 . 1 85 . 10 GLY HA2 H 3.98 . 1 86 . 10 GLY HA3 H 4.09 . 1 87 . 11 LEU N N 122.05 . 1 88 . 11 LEU H H 7.61 . 1 89 . 11 LEU CA C 59.17 . 1 90 . 11 LEU HA H 4.13 . 1 91 . 11 LEU CB C 42.30 . 1 92 . 11 LEU HB2 H 2.02 . 1 93 . 11 LEU HB3 H 1.48 . 1 94 . 11 LEU HG H 1.76 . 1 95 . 11 LEU HD1 H 1.15 . 2 96 . 11 LEU HD2 H 0.98 . 2 97 . 11 LEU CG C 21.42 . 1 98 . 11 LEU CD1 C 25.20 . 2 99 . 12 THR N N 114.52 . 1 100 . 12 THR H H 8.40 . 1 101 . 12 THR CA C 67.36 . 1 102 . 12 THR HA H 3.84 . 1 103 . 12 THR CB C 68.40 . 1 104 . 12 THR HB H 4.15 . 1 105 . 12 THR HG2 H 1.25 . 1 106 . 12 THR CG2 C 21.70 . 1 107 . 13 GLU N N 121.33 . 1 108 . 13 GLU H H 8.67 . 1 109 . 13 GLU CA C 60.31 . 1 110 . 13 GLU HA H 4.12 . 1 111 . 13 GLU CB C 27.60 . 1 112 . 13 GLU HB2 H 2.11 . 1 113 . 13 GLU HB3 H 1.98 . 1 114 . 14 LEU N N 121.62 . 1 115 . 14 LEU H H 7.93 . 1 116 . 14 LEU CA C 58.27 . 1 117 . 14 LEU HA H 4.33 . 1 118 . 14 LEU CB C 42.82 . 1 119 . 14 LEU HB2 H 2.06 . 2 120 . 14 LEU HG H 1.89 . 1 121 . 14 LEU HD1 H 1.13 . 2 122 . 14 LEU HD2 H 1.0 . 2 123 . 14 LEU CG C 26.64 . 1 124 . 14 LEU CD1 C 25.77 . 2 125 . 14 LEU CD2 C 26.33 . 2 126 . 15 LEU N N 116.97 . 1 127 . 15 LEU H H 8.36 . 1 128 . 15 LEU CA C 58.13 . 1 129 . 15 LEU HA H 4.27 . 1 130 . 15 LEU CB C 40.99 . 1 131 . 15 LEU HB2 H 2.19 . 1 132 . 15 LEU HB3 H 1.66 . 1 133 . 15 LEU HG H 2.20 . 1 134 . 15 LEU HD1 H 1.08 . 2 135 . 15 LEU HD2 H 1.01 . 2 136 . 15 LEU CG C 26.38 . 1 137 . 15 LEU CD1 C 25.77 . 2 138 . 15 LEU CD2 C 21.89 . 2 139 . 16 GLN N N 122.27 . 1 140 . 16 GLN H H 8.71 . 1 141 . 16 GLN CA C 59.51 . 1 142 . 16 GLN HA H 4.14 . 1 143 . 16 GLN CB C 27.14 . 1 144 . 16 GLN HB2 H 2.25 . 1 145 . 16 GLN HB3 H 2.13 . 1 146 . 16 GLN HG2 H 2.45 . 2 147 . 16 GLN HE21 H 7.38 . 2 148 . 16 GLN HE22 H 6.76 . 1 149 . 16 GLN CG C 33.54 . 1 150 . 17 GLY N N 105.84 . 1 151 . 17 GLY H H 8.02 . 1 152 . 17 GLY CA C 47.52 . 1 153 . 17 GLY HA2 H 3.84 . 1 154 . 17 GLY HA3 H 4.11 . 1 155 . 18 TYR N N 120.11 . 1 156 . 18 TYR H H 7.14 . 1 157 . 18 TYR CA C 60.57 . 1 158 . 18 TYR HA H 3.02 . 1 159 . 18 TYR CB C 38.38 . 1 160 . 18 TYR HB2 H 2.82 . 1 161 . 18 TYR HB3 H 2.68 . 1 162 . 18 TYR HD1 H 6.41 . 3 163 . 18 TYR CD1 C 132.50 . 3 164 . 18 TYR CE1 C 118.0 . 3 165 . 18 TYR HE1 H 6.30 . 3 166 . 19 THR N N 115.67 . 1 167 . 19 THR H H 8.07 . 1 168 . 19 THR CA C 68.41 . 1 169 . 19 THR HA H 3.30 . 1 170 . 19 THR CB C 68.67 . 1 171 . 19 THR HB H 4.36 . 1 172 . 19 THR HG2 H 1.12 . 1 173 . 19 THR CG2 C 20.89 . 1 174 . 20 VAL N N 118.97 . 1 175 . 20 VAL H H 8.35 . 1 176 . 20 VAL CA C 66.58 . 1 177 . 20 VAL HA H 3.48 . 1 178 . 20 VAL CB C 31.86 . 1 179 . 20 VAL HB H 2.15 . 1 180 . 20 VAL HG1 H 1.08 . 2 181 . 20 VAL HG2 H 0.92 . 2 182 . 20 VAL CG1 C 22.98 . 2 183 . 20 VAL CG2 C 21.15 . 2 184 . 21 GLU N N 118.50 . 1 185 . 21 GLU H H 7.23 . 1 186 . 21 GLU CA C 59.08 . 1 187 . 21 GLU HA H 4.22 . 1 188 . 21 GLU CB C 27.26 . 1 189 . 21 GLU HB2 H 1.92 . 1 190 . 21 GLU HB3 H 2.12 . 1 191 . 21 GLU HG2 H 2.53 . 2 192 . 21 GLU CG C 35.92 . 1 193 . 22 VAL N N 121.16 . 1 194 . 22 VAL H H 8.29 . 1 195 . 22 VAL CA C 66.84 . 1 196 . 22 VAL HA H 2.73 . 1 197 . 22 VAL CB C 31.07 . 1 198 . 22 VAL HB H 1.87 . 1 199 . 22 VAL HG1 H 0.59 . 2 200 . 22 VAL HG2 H 0.25 . 2 201 . 22 VAL CG1 C 23.50 . 2 202 . 22 VAL CG2 C 22.98 . 2 203 . 23 LEU N N 119.33 . 1 204 . 23 LEU H H 8.05 . 1 205 . 23 LEU CA C 57.70 . 1 206 . 23 LEU HA H 3.85 . 1 207 . 23 LEU CB C 40.99 . 1 208 . 23 LEU HB2 H 1.81 . 1 209 . 23 LEU HB3 H 1.40 . 1 210 . 23 LEU HG H 1.36 . 1 211 . 23 LEU HD1 H 0.79 . 2 212 . 23 LEU HD2 H 0.77 . 2 213 . 23 LEU CG C 27.16 . 1 214 . 23 LEU CD1 C 24.03 . 1 215 . 23 LEU CD2 C 24.03 . 1 216 . 24 ARG N N 116.85 . 1 217 . 24 ARG H H 7.73 . 1 218 . 24 ARG CA C 59.11 . 1 219 . 24 ARG HA H 4.11 . 1 220 . 24 ARG CB C 31.40 . 1 221 . 24 ARG HB2 H 1.85 . 2 222 . 24 ARG HG2 H 1.50 . 2 223 . 24 ARG HD2 H 3.17 . 2 224 . 24 ARG CG C 26.70 . 1 225 . 24 ARG CD C 43.30 . 1 226 . 25 GLN N N 114.70 . 1 227 . 25 GLN H H 8.43 . 1 228 . 25 GLN CA C 57.44 . 1 229 . 25 GLN HA H 4.14 . 1 230 . 25 GLN CB C 29.20 . 1 231 . 25 GLN HB2 H 1.93 . 1 232 . 25 GLN HB3 H 1.47 . 1 233 . 25 GLN HG2 H 2.27 . 2 234 . 25 GLN HG3 H 2.48 . 2 235 . 25 GLN HE21 H 7.99 . 1 236 . 25 GLN HE22 H 6.93 . 1 237 . 25 GLN CG C 34.04 . 1 238 . 26 GLN N N 113.59 . 1 239 . 26 GLN H H 8.20 . 1 240 . 26 GLN CA C 55.61 . 1 241 . 26 GLN HA H 3.78 . 1 242 . 26 GLN CB C 26.90 . 1 243 . 26 GLN HB2 H 1.98 . 2 244 . 26 GLN HG2 H 2.13 . 2 245 . 26 GLN HE21 H 7.60 . 2 246 . 26 GLN HE22 H 6.87 . 2 247 . 26 GLN CG C 33.42 . 1 248 . 27 PRO CA C 60.72 . 1 249 . 27 PRO HA H 4.58 . 1 250 . 27 PRO CB C 31.49 . 1 251 . 27 PRO HB2 H 1.73 . 2 252 . 27 PRO HG2 H 1.49 . 2 253 . 27 PRO HD2 H 3.41 . 2 254 . 27 PRO HD3 H 2.82 . 2 255 . 27 PRO CG C 26.00 . 1 256 . 27 PRO CD C 50.67 . 1 257 . 28 PRO CA C 64.14 . 1 258 . 28 PRO HA H 4.37 . 1 259 . 28 PRO CB C 31.77 . 1 260 . 28 PRO HB2 H 2.33 . 1 261 . 28 PRO HB3 H 1.99 . 1 262 . 28 PRO HG2 H 2.06 . 2 263 . 28 PRO HD2 H 3.83 . 2 264 . 28 PRO HD3 H 3.75 . 2 265 . 28 PRO CG C 26.86 . 1 266 . 28 PRO CD C 50.62 . 1 267 . 29 ASP N N 115.70 . 1 268 . 29 ASP H H 7.59 . 1 269 . 29 ASP CA C 52.74 . 1 270 . 29 ASP HA H 4.97 . 1 271 . 29 ASP CB C 43.28 . 1 272 . 29 ASP HB2 H 2.92 . 1 273 . 29 ASP HB3 H 2.53 . 1 274 . 30 LEU N N 126.21 . 1 275 . 30 LEU H H 9.04 . 1 276 . 30 LEU CA C 58.72 . 1 277 . 30 LEU HA H 3.89 . 1 278 . 30 LEU CB C 41.40 . 1 279 . 30 LEU HB2 H 1.86 . 1 280 . 30 LEU HB3 H 1.61 . 1 281 . 30 LEU HG H 1.84 . 1 282 . 30 LEU HD1 H 0.79 . 2 283 . 30 LEU HD2 H 0.84 . 2 284 . 30 LEU CG C 25.40 . 1 285 . 30 LEU CD1 C 23.40 . 2 286 . 30 LEU CD2 C 25.91 . 2 287 . 31 VAL N N 121.48 . 1 288 . 31 VAL H H 8.22 . 1 289 . 31 VAL CA C 67.10 . 1 290 . 31 VAL HA H 3.61 . 1 291 . 31 VAL CB C 31.60 . 1 292 . 31 VAL HB H 2.31 . 1 293 . 31 VAL HG1 H 1.16 . 2 294 . 31 VAL HG2 H 1.04 . 2 295 . 31 VAL CG1 C 24.55 . 2 296 . 31 VAL CG2 C 22.46 . 2 297 . 32 ASP N N 120.44 . 1 298 . 32 ASP H H 8.59 . 1 299 . 32 ASP CA C 57.44 . 1 300 . 32 ASP HA H 4.28 . 1 301 . 32 ASP CB C 40.47 . 1 302 . 32 ASP HB2 H 2.70 . 2 303 . 33 PHE N N 116.96 . 1 304 . 33 PHE H H 8.02 . 1 305 . 33 PHE CA C 61.62 . 1 306 . 33 PHE HA H 4.38 . 1 307 . 33 PHE CB C 39.95 . 1 308 . 33 PHE HB2 H 3.27 . 1 309 . 33 PHE HB3 H 2.82 . 1 310 . 33 PHE HD1 H 7.15 . 3 311 . 33 PHE HD2 H 6.95 . 3 312 . 33 PHE HE1 H 6.95 . 3 313 . 33 PHE CD1 C 132.20 . 3 314 . 33 PHE CE1 C 130.5 . 3 315 . 34 ALA N N 121.08 . 1 316 . 34 ALA H H 8.05 . 1 317 . 34 ALA CA C 56.14 . 1 318 . 34 ALA HA H 3.73 . 1 319 . 34 ALA CB C 16.46 . 1 320 . 34 ALA HB H 0.62 . 1 321 . 35 VAL N N 116.92 . 1 322 . 35 VAL H H 8.11 . 1 323 . 35 VAL CA C 68.67 . 1 324 . 35 VAL HA H 3.38 . 1 325 . 35 VAL CB C 31.86 . 1 326 . 35 VAL HB H 2.27 . 1 327 . 35 VAL HG1 H 1.02 . 2 328 . 35 VAL HG2 H 0.89 . 2 329 . 35 VAL CG1 C 23.24 . 2 330 . 35 VAL CG2 C 21.68 . 2 331 . 36 GLU N N 120.73 . 1 332 . 36 GLU H H 7.77 . 1 333 . 36 GLU CA C 59.79 . 1 334 . 36 GLU HA H 3.93 . 1 335 . 36 GLU CB C 27.80 . 1 336 . 36 GLU HB2 H 1.93 . 1 337 . 36 GLU HB3 H 2.03 . 1 338 . 36 GLU HG2 H 2.25 . 2 339 . 36 GLU HG3 H 2.38 . 2 340 . 36 GLU CG C 35.12 . 1 341 . 37 TYR N N 120.69 . 1 342 . 37 TYR H H 9.01 . 1 343 . 37 TYR CA C 61.36 . 1 344 . 37 TYR HA H 3.59 . 1 345 . 37 TYR CB C 38.65 . 1 346 . 37 TYR HB2 H 2.24 . 1 347 . 37 TYR HB3 H 2.17 . 1 348 . 37 TYR HD1 H 5.83 . 3 349 . 37 TYR HE1 H 6.41 . 3 350 . 37 TYR CD1 C 132.70 . 3 351 . 37 TYR CE1 C 117.70 . 3 352 . 38 PHE N N 115.31 . 1 353 . 38 PHE H H 8.68 . 1 354 . 38 PHE CA C 62.66 . 1 355 . 38 PHE HA H 4.08 . 1 356 . 38 PHE CB C 38.12 . 1 357 . 38 PHE HB2 H 3.17 . 1 358 . 38 PHE HB3 H 2.76 . 1 359 . 38 PHE HD1 H 7.29 . 3 360 . 38 PHE HE1 H 6.65 . 3 361 . 38 PHE CD1 C 132.20 . 3 362 . 38 PHE CE1 C 130.20 . 3 363 . 38 PHE HZ H 6.65 . 1 364 . 39 THR N N 116.96 . 1 365 . 39 THR H H 8.01 . 1 366 . 39 THR CA C 68.14 . 1 367 . 39 THR HA H 3.76 . 1 368 . 39 THR CB C 68.67 . 1 369 . 39 THR HB H 4.25 . 1 370 . 39 THR HG2 H 1.14 . 1 371 . 39 THR CG2 C 20.89 . 1 372 . 40 ARG N N 121.66 . 1 373 . 40 ARG H H 7.79 . 1 374 . 40 ARG CA C 59.53 . 1 375 . 40 ARG HA H 3.87 . 1 376 . 40 ARG CB C 28.40 . 1 377 . 40 ARG HB2 H 1.73 . 1 378 . 40 ARG HB3 H 2.20 . 1 379 . 40 ARG HG2 H 1.60 . 2 380 . 40 ARG HG3 H 1.52 . 2 381 . 40 ARG HD2 H 3.08 . 2 382 . 40 ARG CG C 27.42 . 1 383 . 40 ARG CD C 43.52 . 1 384 . 41 LEU N N 119.39 . 1 385 . 41 LEU H H 7.46 . 1 386 . 41 LEU CA C 57.97 . 1 387 . 41 LEU HA H 3.91 . 1 388 . 41 LEU CB C 41.10 . 1 389 . 41 LEU HB2 H 1.54 . 2 390 . 41 LEU HG H 1.38 . 1 391 . 41 LEU HD1 H 0.76 . 2 392 . 41 LEU HD2 H 0.72 . 2 393 . 41 LEU CG C 27.1 . 1 394 . 41 LEU CD1 C 23.92 . 2 395 . 41 LEU CD2 C 24.30 . 2 396 . 42 ARG N N 119.36 . 1 397 . 42 ARG H H 7.94 . 1 398 . 42 ARG CA C 59.54 . 1 399 . 42 ARG HA H 3.88 . 1 400 . 42 ARG CB C 29.50 . 1 401 . 42 ARG HB2 H 1.79 . 2 402 . 42 ARG HG2 H 1.64 . 2 403 . 42 ARG HD2 H 3.30 . 2 404 . 42 ARG HD3 H 3.05 . 2 405 . 42 ARG CG C 25.96 . 1 406 . 42 ARG CD C 44.24 . 1 407 . 43 GLU N N 116.96 . 1 408 . 43 GLU H H 7.97 . 1 409 . 43 GLU CA C 57.70 . 1 410 . 43 GLU HA H 4.11 . 1 411 . 43 GLU CB C 28.20 . 1 412 . 43 GLU HB2 H 2.03 . 1 413 . 43 GLU HB3 H 2.08 . 1 414 . 43 GLU HG2 H 2.42 . 2 415 . 43 GLU HG3 H 2.48 . 2 416 . 43 GLU CG C 35.80 . 1 417 . 44 ALA N N 120.69 . 1 418 . 44 ALA H H 7.63 . 1 419 . 44 ALA CA C 53.26 . 1 420 . 44 ALA HA H 4.25 . 1 421 . 44 ALA CB C 19.07 . 1 422 . 44 ALA HB H 1.43 . 1 423 . 45 ARG N N 118.11 . 1 424 . 45 ARG H H 7.49 . 1 425 . 45 ARG CA C 56.81 . 1 426 . 45 ARG HA H 4.28 . 1 427 . 45 ARG CB C 30.81 . 1 428 . 45 ARG HB2 H 1.83 . 1 429 . 45 ARG HB3 H 1.96 . 1 430 . 45 ARG HG2 H 1.72 . 2 431 . 45 ARG HD2 H 3.20 . 2 432 . 45 ARG CG C 26.36 . 1 433 . 45 ARG CD C 43.91 . 1 434 . 46 ARG N N 126.14 . 1 435 . 46 ARG H H 7.80 . 1 436 . 46 ARG CA C 56.66 . 1 437 . 46 ARG HA H 4.16 . 1 438 . 46 ARG CB C 31.34 . 1 439 . 46 ARG HB2 H 1.72 . 1 440 . 46 ARG HB3 H 1.84 . 1 441 . 46 ARG HG2 H 1.64 . 2 442 . 46 ARG HD2 H 3.19 . 2 443 . 46 ARG CG C 27.16 . 1 444 . 46 ARG CD C 43.34 . 1 stop_ save_