data_4414 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of Plastocyanin from the Photosynthetic Prokaryote, Prochlorothrix hollandica (minimized average structure) ; _BMRB_accession_number 4414 _BMRB_flat_file_name bmr4414.str _Entry_type original _Submission_date 1999-09-20 _Accession_date 1999-09-21 _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 Babu Charles R. . 2 Volkman Brian F. . 3 Bullerjahn George S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 546 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-02-21 original author . stop_ _Original_release_date 2000-02-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Babu, C. R., Volkman, B. F., and Bullerjahn, G. S., "NMR Solution Structure of Plastocyanin from the Photosynthetic Prokaryote, Prochlorothrix hollandica," Biochemistry 38, 4988-4995 (1999). ; _Citation_title ; NMR Solution Structure of Plastocyanin from the Photosynthetic Prokaryote, Prochlorothrix hollandica ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99230189 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Babu Charles R. . 2 Volkman Brian F. . 3 Bullerjahn George S. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 38 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4988 _Page_last 4995 _Year 1999 _Details . loop_ _Keyword 'electron transport' photosynthesis 'type I copper protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_PC _Saveframe_category molecular_system _Mol_system_name plastocyanin _Abbreviation_common PC _Enzyme_commission_number 1.10.99.1 loop_ _Mol_system_component_name _Mol_label PC $PC Cu $Cu1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all bound other' loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common plastocyanin _Name_variant T2S _Abbreviation_common PC _Molecular_mass . _Mol_thiol_state 'all bound other' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; ASVQIKMGTDKYAPLYEPKA LSISAGDTVEFVMNKVGPHN VIFDKVPAGESAPALSNTKL AIAPGSFYSVTLGTPGTYSF YCTPHRGAGMVGTITVE ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 VAL 4 GLN 5 ILE 6 LYS 7 MET 8 GLY 9 THR 10 ASP 11 LYS 12 TYR 13 ALA 14 PRO 15 LEU 16 TYR 17 GLU 18 PRO 19 LYS 20 ALA 21 LEU 22 SER 23 ILE 24 SER 25 ALA 26 GLY 27 ASP 28 THR 29 VAL 30 GLU 31 PHE 32 VAL 33 MET 34 ASN 35 LYS 36 VAL 37 GLY 38 PRO 39 HIS 40 ASN 41 VAL 42 ILE 43 PHE 44 ASP 45 LYS 46 VAL 47 PRO 48 ALA 49 GLY 50 GLU 51 SER 52 ALA 53 PRO 54 ALA 55 LEU 56 SER 57 ASN 58 THR 59 LYS 60 LEU 61 ALA 62 ILE 63 ALA 64 PRO 65 GLY 66 SER 67 PHE 68 TYR 69 SER 70 VAL 71 THR 72 LEU 73 GLY 74 THR 75 PRO 76 GLY 77 THR 78 TYR 79 SER 80 PHE 81 TYR 82 CYS 83 THR 84 PRO 85 HIS 86 ARG 87 GLY 88 ALA 89 GLY 90 MET 91 VAL 92 GLY 93 THR 94 ILE 95 THR 96 VAL 97 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 1B3I "Nmr Solution Structure Of Plastocyanin From The Photosynthetic Prokaryote, Prochlorothrix Hollandica (Minimized Average Structu" 98.97 97 100.00 100.00 4.52e-62 PDB 2B3I "Nmr Solution Structure Of Plastocyanin From The Photosynthetic Prokaryote, Prochlorothrix Hollandica (19 Structures)" 98.97 97 100.00 100.00 4.52e-62 PDB 2JXM "Ensemble Of Twenty Structures Of The Prochlorothrix Hollandica Plastocyanin- Cytochrome F Complex" 100.00 97 100.00 100.00 8.24e-63 GB AAD09144 "plastocyanin precursor [Prochlorothrix hollandica]" 100.00 131 97.94 98.97 4.68e-62 GB KKJ00324 "plastocyanin [Prochlorothrix hollandica PCC 9006]" 100.00 131 98.97 100.00 5.29e-63 PRF 2107183A plastocyanin 100.00 131 97.94 98.97 4.68e-62 REF WP_016924140 "plastocyanin [Prochlorothrix hollandica]" 100.00 131 98.97 100.00 5.29e-63 SP P50057 "RecName: Full=Plastocyanin; Flags: Precursor" 100.00 131 98.97 100.00 9.23e-63 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 11:29:23 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 1 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Plasmid _Gene_mnemonic _Details $PC 'Prochlorothrix hollandica' 1223 Eubacteria . Prochlorothrix hollandica 'thylakoid lumen' pVAPC10 petE ; A truncated petE gene lacking the coding region for the transit peptide was cloned into an E. coli expression vector. Expressed protein accumulated as inclusion bodies that were subsequently refolded in-vitro in the presence of Cu(I) ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $PC 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3)pLysS plasmid pSCREEN 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 $PC 3 mM . 'Potassium Phosphate' 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _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 'ionic strength' 20 . mM pH 7.0 0.2 n/a pressure 1 . atm temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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_citation_label _Correction_value_citation_label H2O H 1 proton ppm 4.80 internal direct cylindrical internal parallel_to_Bo $entry_citation $entry_citation 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_chem_shift_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 $chem_shift_ref _Mol_system_component_name PC _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 ALA HA H 4.13 . 1 2 . 1 ALA HB H 1.51 . 1 3 . 2 SER H H 8.53 . 1 4 . 2 SER HA H 5.60 . 1 5 . 2 SER HB2 H 3.59 . 2 6 . 2 SER HB3 H 3.68 . 2 7 . 3 VAL H H 8.62 . 1 8 . 3 VAL HA H 4.52 . 1 9 . 3 VAL HB H 2.01 . 1 10 . 3 VAL HG1 H 0.91 . 1 11 . 3 VAL HG2 H 0.84 . 1 12 . 4 GLN H H 8.15 . 1 13 . 4 GLN HA H 5.47 . 1 14 . 4 GLN HB2 H 1.67 . 2 15 . 4 GLN HB3 H 1.99 . 2 16 . 4 GLN HG2 H 2.21 . 2 17 . 4 GLN HG3 H 2.37 . 2 18 . 4 GLN HE21 H 6.68 . 1 19 . 4 GLN HE22 H 7.61 . 1 20 . 5 ILE H H 8.59 . 1 21 . 5 ILE HA H 4.34 . 1 22 . 5 ILE HB H 1.11 . 1 23 . 5 ILE HG2 H 1.00 . 1 24 . 5 ILE HG12 H 1.37 . 2 25 . 5 ILE HG13 H 0.78 . 2 26 . 5 ILE HD1 H 0.42 . 1 27 . 6 LYS H H 8.97 . 1 28 . 6 LYS HA H 4.81 . 1 29 . 6 LYS HB2 H 2.12 . 2 30 . 6 LYS HB3 H 1.86 . 2 31 . 6 LYS HG2 H 1.30 . 1 32 . 6 LYS HG3 H 1.30 . 1 33 . 6 LYS HD2 H 1.66 . 1 34 . 6 LYS HD3 H 1.66 . 1 35 . 6 LYS HE2 H 2.97 . 1 36 . 6 LYS HE3 H 2.97 . 1 37 . 7 MET H H 8.94 . 1 38 . 7 MET HA H 4.15 . 1 39 . 7 MET HB2 H 2.50 . 1 40 . 7 MET HB3 H 1.42 . 1 41 . 7 MET HG2 H 2.30 . 2 42 . 7 MET HG3 H 2.82 . 2 43 . 7 MET HE H 1.65 . 1 44 . 8 GLY H H 7.71 . 1 45 . 8 GLY HA2 H 3.91 . 1 46 . 8 GLY HA3 H 5.10 . 1 47 . 9 THR H H 8.74 . 1 48 . 9 THR HA H 4.65 . 1 49 . 9 THR HB H 4.71 . 1 50 . 9 THR HG2 H 1.24 . 1 51 . 9 THR HG1 H 6.08 . 1 52 . 10 ASP H H 9.30 . 1 53 . 10 ASP HA H 4.28 . 1 54 . 10 ASP HB2 H 2.84 . 2 55 . 10 ASP HB3 H 2.63 . 2 56 . 11 LYS H H 7.42 . 1 57 . 11 LYS HA H 4.51 . 1 58 . 11 LYS HB2 H 2.17 . 2 59 . 11 LYS HB3 H 1.59 . 2 60 . 11 LYS HG2 H 1.52 . 2 61 . 11 LYS HG3 H 1.40 . 2 62 . 11 LYS HD2 H 1.70 . 2 63 . 11 LYS HD3 H 1.73 . 2 64 . 11 LYS HE2 H 3.04 . 1 65 . 11 LYS HE3 H 3.04 . 1 66 . 12 TYR H H 8.00 . 1 67 . 12 TYR HA H 3.41 . 1 68 . 12 TYR HB2 H 3.16 . 2 69 . 12 TYR HB3 H 3.35 . 2 70 . 12 TYR HD1 H 6.98 . 1 71 . 12 TYR HD2 H 6.98 . 1 72 . 12 TYR HE1 H 6.89 . 1 73 . 12 TYR HE2 H 6.89 . 1 74 . 13 ALA H H 7.49 . 1 75 . 13 ALA HA H 5.12 . 1 76 . 13 ALA HB H 1.31 . 1 77 . 14 PRO HA H 4.18 . 1 78 . 14 PRO HB2 H 1.74 . 1 79 . 14 PRO HB3 H 0.96 . 1 80 . 14 PRO HG2 H 2.19 . 2 81 . 14 PRO HG3 H 1.91 . 2 82 . 14 PRO HD2 H 3.75 . 2 83 . 14 PRO HD3 H 3.65 . 2 84 . 15 LEU H H 7.50 . 1 85 . 15 LEU HA H 4.38 . 1 86 . 15 LEU HB2 H 1.62 . 2 87 . 15 LEU HB3 H 1.20 . 2 88 . 15 LEU HG H 1.32 . 1 89 . 15 LEU HD1 H 1.02 . 2 90 . 15 LEU HD2 H 0.90 . 2 91 . 16 TYR H H 8.60 . 1 92 . 16 TYR HA H 5.16 . 1 93 . 16 TYR HB2 H 2.55 . 1 94 . 16 TYR HB3 H 3.09 . 1 95 . 16 TYR HD1 H 6.74 . 1 96 . 16 TYR HD2 H 6.74 . 1 97 . 16 TYR HE1 H 6.56 . 1 98 . 16 TYR HE2 H 6.56 . 1 99 . 16 TYR HH H 7.63 . 1 100 . 17 GLU H H 8.94 . 1 101 . 17 GLU HA H 4.83 . 1 102 . 17 GLU HB2 H 1.86 . 2 103 . 17 GLU HB3 H 1.75 . 2 104 . 17 GLU HG2 H 1.98 . 2 105 . 17 GLU HG3 H 2.17 . 2 106 . 18 PRO HA H 4.96 . 1 107 . 18 PRO HB2 H 2.20 . 1 108 . 18 PRO HB3 H 2.62 . 1 109 . 18 PRO HG2 H 2.10 . 2 110 . 18 PRO HG3 H 1.90 . 2 111 . 18 PRO HD2 H 3.77 . 2 112 . 18 PRO HD3 H 3.96 . 2 113 . 19 LYS H H 8.16 . 1 114 . 19 LYS HA H 4.45 . 1 115 . 19 LYS HB2 H 2.40 . 2 116 . 19 LYS HB3 H 2.11 . 2 117 . 19 LYS HG2 H 1.72 . 2 118 . 19 LYS HG3 H 1.60 . 2 119 . 19 LYS HD2 H 1.90 . 1 120 . 19 LYS HD3 H 1.90 . 1 121 . 19 LYS HE2 H 3.13 . 2 122 . 19 LYS HE3 H 3.18 . 2 123 . 20 ALA H H 7.48 . 1 124 . 20 ALA HA H 5.53 . 1 125 . 20 ALA HB H 1.31 . 1 126 . 21 LEU H H 8.00 . 1 127 . 21 LEU HA H 4.76 . 1 128 . 21 LEU HB2 H 1.54 . 2 129 . 21 LEU HB3 H 1.74 . 2 130 . 21 LEU HG H 1.55 . 1 131 . 21 LEU HD1 H 0.85 . 2 132 . 21 LEU HD2 H 0.78 . 2 133 . 22 SER H H 8.53 . 1 134 . 22 SER HA H 5.80 . 1 135 . 22 SER HB2 H 3.71 . 2 136 . 22 SER HB3 H 3.87 . 2 137 . 23 ILE H H 8.98 . 1 138 . 23 ILE HA H 4.87 . 1 139 . 23 ILE HB H 2.65 . 1 140 . 23 ILE HG2 H 0.77 . 1 141 . 23 ILE HG12 H 1.22 . 2 142 . 23 ILE HG13 H 0.74 . 2 143 . 23 ILE HD1 H 0.60 . 1 144 . 24 SER H H 8.53 . 1 145 . 24 SER HA H 5.17 . 1 146 . 24 SER HB2 H 3.67 . 2 147 . 24 SER HB3 H 3.89 . 2 148 . 25 ALA H H 8.66 . 1 149 . 25 ALA HA H 3.79 . 1 150 . 25 ALA HB H 1.24 . 1 151 . 26 GLY H H 9.29 . 1 152 . 26 GLY HA2 H 3.34 . 2 153 . 26 GLY HA3 H 4.31 . 2 154 . 27 ASP H H 8.19 . 1 155 . 27 ASP HA H 4.87 . 1 156 . 27 ASP HB2 H 3.10 . 2 157 . 27 ASP HB3 H 2.54 . 2 158 . 28 THR H H 8.43 . 1 159 . 28 THR HA H 4.89 . 1 160 . 28 THR HB H 3.81 . 1 161 . 28 THR HG2 H 0.97 . 1 162 . 29 VAL H H 9.01 . 1 163 . 29 VAL HA H 4.31 . 1 164 . 29 VAL HB H 1.56 . 1 165 . 29 VAL HG1 H 0.03 . 1 166 . 29 VAL HG2 H 0.55 . 1 167 . 30 GLU H H 8.81 . 1 168 . 30 GLU HA H 4.65 . 1 169 . 30 GLU HB2 H 1.57 . 2 170 . 30 GLU HB3 H 1.94 . 2 171 . 30 GLU HG2 H 1.87 . 2 172 . 30 GLU HG3 H 2.06 . 2 173 . 31 PHE H H 9.00 . 1 174 . 31 PHE HA H 5.19 . 1 175 . 31 PHE HB2 H 3.51 . 2 176 . 31 PHE HB3 H 3.25 . 2 177 . 31 PHE HD1 H 6.74 . 1 178 . 31 PHE HD2 H 6.74 . 1 179 . 31 PHE HE1 H 6.52 . 1 180 . 31 PHE HE2 H 6.52 . 1 181 . 31 PHE HZ H 5.67 . 1 182 . 32 VAL H H 9.28 . 1 183 . 32 VAL HA H 4.42 . 1 184 . 32 VAL HB H 1.87 . 1 185 . 32 VAL HG1 H 0.82 . 2 186 . 32 VAL HG2 H 0.80 . 2 187 . 33 MET H H 9.30 . 1 188 . 33 MET HA H 4.55 . 1 189 . 33 MET HB2 H 1.88 . 2 190 . 33 MET HB3 H 2.11 . 2 191 . 33 MET HG2 H 2.58 . 2 192 . 33 MET HG3 H 1.64 . 2 193 . 33 MET HE H 1.77 . 1 194 . 34 ASN H H 8.70 . 1 195 . 34 ASN HA H 5.26 . 1 196 . 34 ASN HB2 H 2.25 . 1 197 . 34 ASN HB3 H 3.40 . 1 198 . 34 ASN HD21 H 7.40 . 1 199 . 34 ASN HD22 H 7.70 . 1 200 . 35 LYS H H 7.60 . 1 201 . 35 LYS HA H 4.72 . 1 202 . 35 LYS HB2 H 1.40 . 1 203 . 35 LYS HB3 H 1.40 . 1 204 . 35 LYS HG2 H 1.75 . 1 205 . 35 LYS HG3 H 1.75 . 1 206 . 35 LYS HD2 H 0.96 . 2 207 . 35 LYS HD3 H 1.08 . 2 208 . 35 LYS HE2 H 2.86 . 1 209 . 35 LYS HE3 H 2.86 . 1 210 . 36 VAL H H 9.09 . 1 211 . 36 VAL HA H 3.83 . 1 212 . 36 VAL HB H 2.35 . 1 213 . 36 VAL HG1 H 1.06 . 2 214 . 36 VAL HG2 H 0.60 . 2 215 . 37 GLY H H 7.96 . 1 216 . 37 GLY HA2 H 2.69 . 2 217 . 37 GLY HA3 H 3.09 . 2 218 . 38 PRO HA H 4.63 . 1 219 . 38 PRO HB2 H 2.15 . 1 220 . 38 PRO HB3 H 2.15 . 1 221 . 38 PRO HG2 H 1.76 . 2 222 . 38 PRO HG3 H 1.72 . 2 223 . 38 PRO HD2 H 3.51 . 2 224 . 38 PRO HD3 H 3.48 . 2 225 . 39 HIS H H 7.15 . 1 226 . 39 HIS HA H 5.49 . 1 227 . 39 HIS HB2 H 2.49 . 1 228 . 39 HIS HB3 H 3.62 . 1 229 . 39 HIS HD2 H 6.75 . 1 230 . 39 HIS HE1 H 6.95 . 1 231 . 39 HIS HE2 H 11.49 . 1 232 . 40 ASN H H 8.74 . 1 233 . 40 ASN HA H 4.81 . 1 234 . 40 ASN HB2 H 3.80 . 2 235 . 40 ASN HB3 H 2.91 . 2 236 . 40 ASN HD21 H 6.62 . 1 237 . 40 ASN HD22 H 7.01 . 1 238 . 41 VAL H H 7.37 . 1 239 . 41 VAL HA H 4.02 . 1 240 . 41 VAL HB H 1.95 . 1 241 . 41 VAL HG1 H -0.06 . 2 242 . 41 VAL HG2 H 0.35 . 2 243 . 42 ILE H H 9.38 . 1 244 . 42 ILE HA H 4.04 . 1 245 . 42 ILE HB H 0.79 . 1 246 . 42 ILE HG2 H 0.60 . 1 247 . 42 ILE HG12 H 1.07 . 2 248 . 42 ILE HG13 H 1.15 . 2 249 . 42 ILE HD1 H 0.70 . 1 250 . 43 PHE H H 8.87 . 1 251 . 43 PHE HA H 4.80 . 1 252 . 43 PHE HB2 H 3.11 . 2 253 . 43 PHE HB3 H 2.69 . 2 254 . 43 PHE HD1 H 7.15 . 1 255 . 43 PHE HD2 H 7.15 . 1 256 . 43 PHE HE1 H 6.87 . 1 257 . 43 PHE HE2 H 6.87 . 1 258 . 43 PHE HZ H 6.66 . 1 259 . 44 ASP H H 9.31 . 1 260 . 44 ASP HA H 4.92 . 1 261 . 44 ASP HB2 H 2.76 . 2 262 . 44 ASP HB3 H 2.80 . 2 263 . 45 LYS H H 7.76 . 1 264 . 45 LYS HA H 4.73 . 1 265 . 45 LYS HB2 H 1.86 . 1 266 . 45 LYS HB3 H 1.86 . 1 267 . 45 LYS HG2 H 1.46 . 2 268 . 45 LYS HG3 H 1.38 . 2 269 . 45 LYS HD2 H 1.69 . 1 270 . 45 LYS HD3 H 1.69 . 1 271 . 45 LYS HE2 H 3.01 . 1 272 . 45 LYS HE3 H 3.01 . 1 273 . 46 VAL H H 8.22 . 1 274 . 46 VAL HA H 4.85 . 1 275 . 46 VAL HB H 1.91 . 1 276 . 46 VAL HG1 H 0.69 . 2 277 . 46 VAL HG2 H 1.08 . 2 278 . 47 PRO HA H 4.37 . 1 279 . 47 PRO HB2 H 1.56 . 1 280 . 47 PRO HB3 H 2.38 . 1 281 . 47 PRO HG2 H 1.41 . 1 282 . 47 PRO HG3 H 1.41 . 1 283 . 47 PRO HD2 H 2.24 . 2 284 . 47 PRO HD3 H 2.18 . 2 285 . 48 ALA H H 8.28 . 1 286 . 48 ALA HA H 4.18 . 1 287 . 48 ALA HB H 1.42 . 1 288 . 49 GLY H H 8.61 . 1 289 . 49 GLY HA2 H 3.60 . 2 290 . 49 GLY HA3 H 4.50 . 2 291 . 50 GLU H H 7.84 . 1 292 . 50 GLU HA H 4.52 . 1 293 . 50 GLU HB2 H 2.05 . 2 294 . 50 GLU HB3 H 1.79 . 2 295 . 50 GLU HG2 H 2.65 . 2 296 . 50 GLU HG3 H 2.00 . 2 297 . 51 SER H H 9.08 . 1 298 . 51 SER HA H 4.84 . 1 299 . 51 SER HB2 H 3.77 . 2 300 . 51 SER HB3 H 3.81 . 2 301 . 52 ALA H H 9.23 . 1 302 . 52 ALA HA H 4.12 . 1 303 . 52 ALA HB H 1.52 . 1 304 . 53 PRO HA H 4.38 . 1 305 . 53 PRO HB2 H 2.40 . 1 306 . 53 PRO HB3 H 1.85 . 1 307 . 53 PRO HG2 H 2.11 . 2 308 . 53 PRO HG3 H 2.04 . 2 309 . 53 PRO HD2 H 3.80 . 2 310 . 53 PRO HD3 H 4.10 . 2 311 . 54 ALA H H 7.32 . 1 312 . 54 ALA HA H 4.26 . 1 313 . 54 ALA HB H 1.58 . 1 314 . 55 LEU H H 7.53 . 1 315 . 55 LEU HA H 4.32 . 1 316 . 55 LEU HB2 H 0.77 . 2 317 . 55 LEU HB3 H 1.29 . 2 318 . 55 LEU HG H 1.90 . 1 319 . 55 LEU HD1 H 0.64 . 1 320 . 55 LEU HD2 H 0.69 . 1 321 . 56 SER H H 7.24 . 1 322 . 56 SER HA H 4.57 . 1 323 . 56 SER HB2 H 4.14 . 2 324 . 56 SER HB3 H 4.26 . 2 325 . 56 SER HG H 5.73 . 1 326 . 57 ASN H H 9.30 . 1 327 . 57 ASN HA H 4.53 . 1 328 . 57 ASN HB2 H 1.64 . 2 329 . 57 ASN HB3 H 2.79 . 2 330 . 58 THR H H 8.35 . 1 331 . 58 THR HA H 3.93 . 1 332 . 58 THR HB H 4.38 . 1 333 . 58 THR HG2 H 1.27 . 1 334 . 59 LYS H H 7.71 . 1 335 . 59 LYS HA H 4.03 . 1 336 . 59 LYS HB2 H 1.89 . 1 337 . 59 LYS HB3 H 1.89 . 1 338 . 59 LYS HG2 H 1.46 . 2 339 . 59 LYS HG3 H 1.55 . 2 340 . 59 LYS HD2 H 1.79 . 1 341 . 59 LYS HD3 H 1.79 . 1 342 . 59 LYS HE2 H 3.10 . 1 343 . 59 LYS HE3 H 3.10 . 1 344 . 60 LEU H H 7.78 . 1 345 . 60 LEU HA H 4.18 . 1 346 . 60 LEU HB2 H 1.69 . 2 347 . 60 LEU HB3 H 1.08 . 2 348 . 60 LEU HG H 1.75 . 1 349 . 60 LEU HD1 H 0.60 . 2 350 . 60 LEU HD2 H 0.86 . 2 351 . 61 ALA H H 8.80 . 1 352 . 61 ALA HA H 4.21 . 1 353 . 61 ALA HB H 0.75 . 1 354 . 62 ILE H H 8.13 . 1 355 . 62 ILE HA H 4.32 . 1 356 . 62 ILE HB H 1.78 . 1 357 . 62 ILE HG2 H 0.85 . 1 358 . 62 ILE HG12 H 1.38 . 2 359 . 62 ILE HG13 H 1.12 . 2 360 . 62 ILE HD1 H 0.81 . 1 361 . 63 ALA H H 8.00 . 1 362 . 63 ALA HA H 4.73 . 1 363 . 63 ALA HB H 1.42 . 1 364 . 64 PRO HA H 4.24 . 1 365 . 64 PRO HB2 H 2.41 . 2 366 . 64 PRO HB3 H 1.98 . 2 367 . 64 PRO HG2 H 2.05 . 2 368 . 64 PRO HG3 H 2.17 . 2 369 . 64 PRO HD2 H 3.94 . 2 370 . 64 PRO HD3 H 3.69 . 2 371 . 65 GLY H H 8.39 . 1 372 . 65 GLY HA2 H 3.82 . 2 373 . 65 GLY HA3 H 4.72 . 2 374 . 66 SER HA H 4.07 . 1 375 . 66 SER HB2 H 3.89 . 2 376 . 66 SER HB3 H 3.83 . 2 377 . 67 PHE H H 9.55 . 1 378 . 67 PHE HA H 5.40 . 1 379 . 67 PHE HB2 H 3.19 . 2 380 . 67 PHE HB3 H 3.32 . 2 381 . 67 PHE HD1 H 7.40 . 1 382 . 67 PHE HD2 H 7.40 . 1 383 . 67 PHE HE1 H 7.23 . 1 384 . 67 PHE HE2 H 7.23 . 1 385 . 67 PHE HZ H 7.82 . 1 386 . 68 TYR H H 8.15 . 1 387 . 68 TYR HA H 4.86 . 1 388 . 68 TYR HB2 H 2.99 . 2 389 . 68 TYR HB3 H 2.95 . 2 390 . 68 TYR HD1 H 6.80 . 1 391 . 68 TYR HD2 H 6.80 . 1 392 . 68 TYR HE1 H 6.38 . 1 393 . 68 TYR HE2 H 6.38 . 1 394 . 68 TYR HH H 9.12 . 1 395 . 69 SER H H 8.15 . 1 396 . 69 SER HA H 5.59 . 1 397 . 69 SER HB2 H 3.47 . 2 398 . 69 SER HB3 H 3.50 . 2 399 . 70 VAL H H 8.81 . 1 400 . 70 VAL HA H 4.58 . 1 401 . 70 VAL HB H 1.86 . 1 402 . 70 VAL HG1 H 0.82 . 2 403 . 70 VAL HG2 H 0.96 . 2 404 . 71 THR H H 8.41 . 1 405 . 71 THR HA H 4.77 . 1 406 . 71 THR HB H 3.75 . 1 407 . 71 THR HG2 H 0.93 . 1 408 . 72 LEU H H 7.56 . 1 409 . 72 LEU HA H 4.55 . 1 410 . 72 LEU HB2 H 1.55 . 1 411 . 72 LEU HB3 H 0.79 . 1 412 . 72 LEU HG H 1.17 . 1 413 . 72 LEU HD1 H 0.30 . 2 414 . 72 LEU HD2 H 0.03 . 2 415 . 73 GLY H H 8.90 . 1 416 . 73 GLY HA2 H 3.95 . 2 417 . 73 GLY HA3 H 3.83 . 2 418 . 74 THR H H 7.24 . 1 419 . 74 THR HA H 4.72 . 1 420 . 74 THR HB H 3.97 . 1 421 . 74 THR HG2 H 1.44 . 1 422 . 74 THR HG1 H 6.42 . 1 423 . 75 PRO HA H 4.24 . 1 424 . 75 PRO HB2 H 1.96 . 1 425 . 75 PRO HB3 H 2.41 . 1 426 . 75 PRO HG2 H 1.88 . 2 427 . 75 PRO HG3 H 2.19 . 2 428 . 75 PRO HD2 H 3.80 . 1 429 . 75 PRO HD3 H 4.11 . 1 430 . 76 GLY H H 9.09 . 1 431 . 76 GLY HA2 H 3.91 . 2 432 . 76 GLY HA3 H 4.61 . 2 433 . 77 THR H H 8.36 . 1 434 . 77 THR HA H 5.13 . 1 435 . 77 THR HB H 3.92 . 1 436 . 77 THR HG2 H 1.22 . 1 437 . 77 THR HG1 H 6.28 . 1 438 . 78 TYR H H 9.73 . 1 439 . 78 TYR HA H 5.57 . 1 440 . 78 TYR HB2 H 3.53 . 1 441 . 78 TYR HB3 H 3.12 . 1 442 . 78 TYR HD1 H 7.15 . 1 443 . 78 TYR HD2 H 7.15 . 1 444 . 78 TYR HE1 H 6.66 . 1 445 . 78 TYR HE2 H 6.66 . 1 446 . 78 TYR HH H 10.17 . 1 447 . 79 SER H H 9.66 . 1 448 . 79 SER HA H 5.50 . 1 449 . 79 SER HB2 H 4.00 . 2 450 . 79 SER HB3 H 4.11 . 2 451 . 80 PHE H H 8.22 . 1 452 . 80 PHE HA H 5.64 . 1 453 . 80 PHE HB2 H 1.58 . 2 454 . 80 PHE HB3 H 1.93 . 2 455 . 80 PHE HD1 H 6.36 . 1 456 . 80 PHE HD2 H 6.36 . 1 457 . 80 PHE HE1 H 5.91 . 1 458 . 80 PHE HE2 H 5.91 . 1 459 . 80 PHE HZ H 6.76 . 1 460 . 81 TYR H H 9.34 . 1 461 . 81 TYR HA H 5.42 . 1 462 . 81 TYR HB2 H 3.16 . 2 463 . 81 TYR HB3 H 3.12 . 2 464 . 81 TYR HD1 H 6.83 . 1 465 . 81 TYR HD2 H 6.83 . 1 466 . 81 TYR HE1 H 6.67 . 1 467 . 81 TYR HE2 H 6.67 . 1 468 . 82 CYS H H 7.82 . 1 469 . 82 CYS HA H 5.17 . 1 470 . 82 CYS HB2 H 3.09 . 2 471 . 82 CYS HB3 H 3.40 . 2 472 . 83 THR H H 9.92 . 1 473 . 83 THR HA H 4.22 . 1 474 . 83 THR HB H 4.42 . 1 475 . 83 THR HG2 H 1.36 . 1 476 . 84 PRO HA H 4.12 . 1 477 . 84 PRO HB2 H 1.01 . 1 478 . 84 PRO HB3 H 1.93 . 1 479 . 84 PRO HG2 H 2.18 . 2 480 . 84 PRO HG3 H 1.58 . 2 481 . 84 PRO HD2 H 4.56 . 2 482 . 84 PRO HD3 H 3.29 . 2 483 . 85 HIS HA H 5.07 . 1 484 . 85 HIS HB2 H 3.62 . 2 485 . 85 HIS HB3 H 3.59 . 2 486 . 85 HIS HD2 H 7.04 . 1 487 . 85 HIS HE1 H 7.59 . 1 488 . 85 HIS HE2 H 11.24 . 1 489 . 86 ARG H H 8.13 . 1 490 . 86 ARG HA H 3.94 . 1 491 . 86 ARG HB2 H 1.77 . 1 492 . 86 ARG HB3 H 1.77 . 1 493 . 86 ARG HG2 H 1.21 . 2 494 . 86 ARG HG3 H 1.48 . 2 495 . 86 ARG HD2 H 2.73 . 2 496 . 86 ARG HD3 H 2.33 . 2 497 . 87 GLY H H 9.19 . 1 498 . 87 GLY HA2 H 3.83 . 2 499 . 87 GLY HA3 H 3.97 . 2 500 . 88 ALA H H 7.83 . 1 501 . 88 ALA HA H 4.69 . 1 502 . 88 ALA HB H 1.66 . 1 503 . 89 GLY H H 7.98 . 1 504 . 89 GLY HA2 H 3.84 . 2 505 . 89 GLY HA3 H 4.48 . 2 506 . 90 MET H H 8.00 . 1 507 . 90 MET HA H 4.85 . 1 508 . 90 MET HB2 H 2.33 . 1 509 . 90 MET HB3 H 1.89 . 1 510 . 90 MET HG2 H 2.08 . 2 511 . 90 MET HG3 H 2.44 . 2 512 . 90 MET HE H 0.48 . 1 513 . 91 VAL H H 8.00 . 1 514 . 91 VAL HA H 5.25 . 1 515 . 91 VAL HB H 2.36 . 1 516 . 91 VAL HG1 H 0.84 . 2 517 . 91 VAL HG2 H 1.03 . 2 518 . 92 GLY H H 8.18 . 1 519 . 92 GLY HA2 H 2.87 . 2 520 . 92 GLY HA3 H 4.70 . 2 521 . 93 THR H H 8.15 . 1 522 . 93 THR HA H 5.30 . 1 523 . 93 THR HB H 3.99 . 1 524 . 93 THR HG2 H 1.19 . 1 525 . 94 ILE H H 9.56 . 1 526 . 94 ILE HA H 5.01 . 1 527 . 94 ILE HB H 1.64 . 1 528 . 94 ILE HG2 H 0.70 . 1 529 . 94 ILE HG12 H 1.00 . 2 530 . 94 ILE HG13 H 1.86 . 2 531 . 94 ILE HD1 H 0.72 . 1 532 . 95 THR H H 9.22 . 1 533 . 95 THR HA H 5.01 . 1 534 . 95 THR HB H 4.16 . 1 535 . 95 THR HG2 H 1.19 . 1 536 . 96 VAL H H 9.39 . 1 537 . 96 VAL HA H 4.45 . 1 538 . 96 VAL HB H 2.44 . 1 539 . 96 VAL HG1 H 0.69 . 2 540 . 96 VAL HG2 H 0.61 . 2 541 . 97 GLU H H 8.76 . 1 542 . 97 GLU HA H 4.43 . 1 543 . 97 GLU HB2 H 2.06 . 2 544 . 97 GLU HB3 H 1.96 . 2 545 . 97 GLU HG2 H 2.25 . 2 546 . 97 GLU HG3 H 2.19 . 2 stop_ save_