data_447 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Multinuclear Magnetic Resonance Studies of the 2Fe-2S, Ferredoxin from Anabaena Species Strain PCC 7120. 1. Sequence-Specific Hydrogen-1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form ; _BMRB_accession_number 447 _BMRB_flat_file_name bmr447.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Oh Byung-Ha . . 2 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 452 "13C chemical shifts" 358 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Oh, Byung-Ha, Markley, John L., "Multinuclear Magnetic Resonance Studies of the 2Fe-2S, Ferredoxin from Anabaena Species Strain PCC 7120. 1. Sequence-Specific Hydrogen-1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form," Biochemistry 29, 3993-4004 (1990). ; _Citation_title ; Multinuclear Magnetic Resonance Studies of the 2Fe-2S, Ferredoxin from Anabaena Species Strain PCC 7120. 1. Sequence-Specific Hydrogen-1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oh Byung-Ha . . 2 Markley John L. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3993 _Page_last 4004 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_2Fe-2S_ferredoxin _Saveframe_category molecular_system _Mol_system_name '2Fe-2S ferredoxin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '2Fe-2S ferredoxin' $2Fe-2S_ferredoxin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_2Fe-2S_ferredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '2Fe-2S ferredoxin' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 98 _Mol_residue_sequence ; ATFKVTLINEAEGTKHEIEV PDDEYILDAAEEQGYDLPFS CRAGACSTCAGKLVSGTVDQ SDQSFLDDDQIEAGYVLTCV AYPTSDVVIQTHKEEDLY ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 PHE 4 LYS 5 VAL 6 THR 7 LEU 8 ILE 9 ASN 10 GLU 11 ALA 12 GLU 13 GLY 14 THR 15 LYS 16 HIS 17 GLU 18 ILE 19 GLU 20 VAL 21 PRO 22 ASP 23 ASP 24 GLU 25 TYR 26 ILE 27 LEU 28 ASP 29 ALA 30 ALA 31 GLU 32 GLU 33 GLN 34 GLY 35 TYR 36 ASP 37 LEU 38 PRO 39 PHE 40 SER 41 CYS 42 ARG 43 ALA 44 GLY 45 ALA 46 CYS 47 SER 48 THR 49 CYS 50 ALA 51 GLY 52 LYS 53 LEU 54 VAL 55 SER 56 GLY 57 THR 58 VAL 59 ASP 60 GLN 61 SER 62 ASP 63 GLN 64 SER 65 PHE 66 LEU 67 ASP 68 ASP 69 ASP 70 GLN 71 ILE 72 GLU 73 ALA 74 GLY 75 TYR 76 VAL 77 LEU 78 THR 79 CYS 80 VAL 81 ALA 82 TYR 83 PRO 84 THR 85 SER 86 ASP 87 VAL 88 VAL 89 ILE 90 GLN 91 THR 92 HIS 93 LYS 94 GLU 95 GLU 96 ASP 97 LEU 98 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 BMRB 1439 "2Fe-2S ferredoxin" 100.00 98 100.00 100.00 2.07e-63 BMRB 1440 "2Fe-2S ferredoxin" 100.00 98 100.00 100.00 2.07e-63 BMRB 1441 "2Fe-2S ferredoxin" 100.00 98 100.00 100.00 2.07e-63 BMRB 2463 "2Fe-2S ferredoxin" 100.00 98 100.00 100.00 2.07e-63 BMRB 4441 "Anabaena 7120 vegetative Ferredoxin" 100.00 98 100.00 100.00 2.07e-63 BMRB 4442 "Anabaena 7120 vegetative Ferredoxin" 100.00 98 100.00 100.00 2.07e-63 PDB 1CZP "Anabaena Pcc7119 [2fe-2s] Ferredoxin In The Reduced And Oxixized State At 1.17 A" 100.00 98 100.00 100.00 2.07e-63 PDB 1EWY "Anabaena Pcc7119 Ferredoxin:ferredoxin-Nadp+-Reductase Complex" 100.00 98 100.00 100.00 2.07e-63 PDB 1FXA "Crystallization And Structure Determination To 2.5-Angstroms Resolution Of The Oxidized [2fe-2s] Ferredoxin Isolated From Anaba" 100.00 98 100.00 100.00 2.07e-63 PDB 1J7A "Structure Of The Anabaena Ferredoxin D68k Mutant" 100.00 98 98.98 98.98 1.24e-62 PDB 1J7B "Structure Of The Anabaena Ferredoxin Mutant E94k" 100.00 98 98.98 100.00 7.24e-63 PDB 1J7C "Structure Of The Anabaena Ferredoxin Mutant E95k" 100.00 98 98.98 100.00 7.24e-63 PDB 1QOA "Ferredoxin Mutation C49s" 100.00 98 98.98 98.98 2.77e-62 PDB 1QOB "Ferredoxin Mutation D62k" 100.00 98 98.98 98.98 1.24e-62 PDB 1QOF "Ferredoxin Mutation Q70k" 100.00 98 98.98 100.00 7.57e-63 PDB 1QOG "Ferredoxin Mutation S47a" 100.00 98 98.98 100.00 5.82e-63 PDB 1QT9 "Oxidized [2fe-2s] Ferredoxin From Anabaena Pcc7119" 100.00 98 100.00 100.00 2.07e-63 DBJ BAB75847 "ferredoxin I [Nostoc sp. PCC 7120]" 100.00 99 100.00 100.00 1.71e-63 GB AAA22021 "ferredoxin I [Anabaena sp.]" 100.00 99 100.00 100.00 1.71e-63 PRF 1001142A "ferredoxin II" 100.00 98 97.96 98.98 8.42e-62 REF WP_010998287 "Ferredoxin-1 [Nostoc sp. PCC 7120]" 100.00 99 100.00 100.00 1.71e-63 SP P00253 "RecName: Full=Ferredoxin" 100.00 99 98.98 100.00 7.31e-63 SP P0A3C7 "RecName: Full=Ferredoxin-1; AltName: Full=Ferredoxin I" 100.00 99 100.00 100.00 1.71e-63 SP P0A3C8 "RecName: Full=Ferredoxin-1; AltName: Full=Ferredoxin I" 100.00 99 100.00 100.00 1.71e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $2Fe-2S_ferredoxin . 1172 Virus . Anabaena variabilis 7120 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 $2Fe-2S_ferredoxin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 TMS C . . . 0 . . . . . $entry_citation $entry_citation TSP H . . . 0 . . . . . $entry_citation $entry_citation 'liquid ammonia' N . . . 0 . . . . . $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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name '2Fe-2S ferredoxin' _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 CA C 50 . 1 2 . 1 ALA HA H 3.92 . 1 3 . 1 ALA C C 171.3 . 1 4 . 1 ALA CB C 18.1 . 1 5 . 1 ALA HB H 1.13 . 1 6 . 1 ALA N N 40.8 . 1 7 . 2 THR H H 8.06 . 1 8 . 2 THR CA C 59.2 . 1 9 . 2 THR HA H 4.49 . 1 10 . 2 THR C C 170.8 . 1 11 . 2 THR CB C 69.1 . 1 12 . 2 THR CG2 C 22.3 . 1 13 . 2 THR HB H 3.74 . 1 14 . 2 THR HG2 H .99 . 1 15 . 2 THR N N 114.5 . 1 16 . 3 PHE H H 8.58 . 1 17 . 3 PHE CA C 55.3 . 1 18 . 3 PHE HA H 4.98 . 1 19 . 3 PHE CB C 41.2 . 1 20 . 3 PHE CG C 136.3 . 1 21 . 3 PHE HB2 H 3.3 . 2 22 . 3 PHE HB3 H 2.34 . 2 23 . 3 PHE CD1 C 130 . 1 24 . 3 PHE CD2 C 130 . 1 25 . 3 PHE CE1 C 129.2 . 1 26 . 3 PHE HD1 H 7.13 . 1 27 . 3 PHE CE2 C 129.2 . 1 28 . 3 PHE HD2 H 7.13 . 1 29 . 3 PHE CZ C 128 . 1 30 . 3 PHE HE1 H 7.21 . 1 31 . 3 PHE HE2 H 7.21 . 1 32 . 3 PHE HZ H 7.11 . 1 33 . 3 PHE N N 124.7 . 1 34 . 4 LYS H H 9.17 . 1 35 . 4 LYS CA C 54.3 . 1 36 . 4 LYS HA H 4.7 . 1 37 . 4 LYS C C 174.7 . 1 38 . 4 LYS CB C 31.2 . 1 39 . 4 LYS CG C 23.1 . 1 40 . 4 LYS HB2 H 1.28 . 2 41 . 4 LYS HB3 H 1.73 . 2 42 . 4 LYS CD C 27.3 . 1 43 . 4 LYS HG2 H 1.41 . 2 44 . 4 LYS HG3 H 1.48 . 2 45 . 4 LYS CE C 40.1 . 1 46 . 4 LYS HD2 H 1.69 . 2 47 . 4 LYS HD3 H 1.76 . 2 48 . 4 LYS NZ N 33.1 . 1 49 . 4 LYS HE2 H 2.92 . 2 50 . 4 LYS HE3 H 3.08 . 2 51 . 4 LYS N N 124.1 . 1 52 . 5 VAL H H 9.33 . 1 53 . 5 VAL CA C 59.1 . 1 54 . 5 VAL HA H 5.09 . 1 55 . 5 VAL CB C 32.3 . 1 56 . 5 VAL CG1 C 19.2 . 2 57 . 5 VAL CG2 C 20 . 2 58 . 5 VAL HB H 2.03 . 1 59 . 5 VAL HG1 H .78 . 2 60 . 5 VAL HG2 H .96 . 2 61 . 5 VAL N N 129.1 . 1 62 . 6 THR H H 9.27 . 1 63 . 6 THR CA C 60.4 . 1 64 . 6 THR HA H 5.01 . 1 65 . 6 THR C C 171.5 . 1 66 . 6 THR CB C 67.6 . 1 67 . 6 THR CG2 C 19.6 . 1 68 . 6 THR HB H 4.21 . 1 69 . 6 THR HG2 H 1.12 . 1 70 . 6 THR N N 126.7 . 1 71 . 7 LEU H H 9.35 . 1 72 . 7 LEU CA C 51.5 . 1 73 . 7 LEU HA H 4.96 . 1 74 . 7 LEU CB C 41 . 1 75 . 7 LEU CG C 24.6 . 1 76 . 7 LEU HB2 H 1.48 . 2 77 . 7 LEU HB3 H 1.91 . 2 78 . 7 LEU CD1 C 21.4 . 2 79 . 7 LEU CD2 C 24.5 . 2 80 . 7 LEU HG H 1.65 . 1 81 . 7 LEU HD1 H .62 . 2 82 . 7 LEU HD2 H .73 . 2 83 . 7 LEU N N 128.4 . 1 84 . 8 ILE H H 9.37 . 1 85 . 8 ILE CA C 58.7 . 1 86 . 8 ILE HA H 4.7 . 1 87 . 8 ILE CB C 39.5 . 1 88 . 8 ILE CG1 C 26 . 1 89 . 8 ILE CG2 C 15.1 . 1 90 . 8 ILE HB H 1.74 . 1 91 . 8 ILE CD1 C 12 . 1 92 . 8 ILE HG12 H .91 . 2 93 . 8 ILE HG13 H 1.46 . 2 94 . 8 ILE HG2 H .91 . 1 95 . 8 ILE HD1 H .77 . 1 96 . 8 ILE N N 127.7 . 1 97 . 9 ASN H H 7.84 . 1 98 . 9 ASN CA C 49.5 . 1 99 . 9 ASN HA H 5.08 . 1 100 . 9 ASN C C 174.9 . 1 101 . 9 ASN CB C 36.3 . 1 102 . 9 ASN CG C 175 . 1 103 . 9 ASN HB2 H 2.48 . 2 104 . 9 ASN HB3 H 3.22 . 2 105 . 9 ASN ND2 N 111.8 . 1 106 . 9 ASN HD21 H 6.42 . 2 107 . 9 ASN HD22 H 6.8 . 2 108 . 9 ASN N N 126.7 . 1 109 . 10 GLU H H 9.45 . 1 110 . 10 GLU CA C 57.7 . 1 111 . 10 GLU HA H 4 . 1 112 . 10 GLU CB C 29.2 . 1 113 . 10 GLU CG C 35.6 . 1 114 . 10 GLU HB2 H 1.99 . 2 115 . 10 GLU HB3 H 2.11 . 2 116 . 10 GLU CD C 182 . 1 117 . 10 GLU HG2 H 2.2 . 2 118 . 10 GLU HG3 H 2.31 . 2 119 . 10 GLU N N 126.3 . 1 120 . 11 ALA H H 8.35 . 1 121 . 11 ALA CA C 53.3 . 1 122 . 11 ALA HA H 4.13 . 1 123 . 11 ALA C C 178.2 . 1 124 . 11 ALA CB C 16.7 . 1 125 . 11 ALA HB H 1.5 . 1 126 . 11 ALA N N 122.8 . 1 127 . 12 GLU H H 7.23 . 1 128 . 12 GLU CA C 54.2 . 1 129 . 12 GLU HA H 4.29 . 1 130 . 12 GLU C C 175.5 . 1 131 . 12 GLU CB C 29.6 . 1 132 . 12 GLU CG C 35.2 . 1 133 . 12 GLU HB2 H 1.51 . 2 134 . 12 GLU HB3 H 2.18 . 2 135 . 12 GLU HG2 H 2.23 . 1 136 . 12 GLU HG3 H 2.23 . 1 137 . 12 GLU N N 115 . 1 138 . 13 GLY H H 8.09 . 1 139 . 13 GLY CA C 44.8 . 1 140 . 13 GLY HA2 H 3.89 . 2 141 . 13 GLY C C 173.6 . 1 142 . 13 GLY HA3 H 4.01 . 2 143 . 13 GLY N N 110.4 . 1 144 . 14 THR H H 7.58 . 1 145 . 14 THR CA C 57.9 . 1 146 . 14 THR HA H 4.5 . 1 147 . 14 THR CB C 70.2 . 1 148 . 14 THR CG2 C 19.9 . 1 149 . 14 THR HB H 3.83 . 1 150 . 14 THR HG2 H 1.13 . 1 151 . 14 THR N N 108.9 . 1 152 . 15 LYS H H 8.2 . 1 153 . 15 LYS CA C 54 . 1 154 . 15 LYS HA H 4.91 . 1 155 . 15 LYS CB C 33.1 . 1 156 . 15 LYS CG C 23.3 . 1 157 . 15 LYS HB2 H 1.57 . 1 158 . 15 LYS HB3 H 1.57 . 1 159 . 15 LYS CD C 27.7 . 1 160 . 15 LYS HG2 H 1.1 . 2 161 . 15 LYS HG3 H 1.17 . 2 162 . 15 LYS CE C 39.9 . 1 163 . 15 LYS HD2 H 1.58 . 1 164 . 15 LYS HD3 H 1.58 . 1 165 . 15 LYS NZ N 33.7 . 1 166 . 15 LYS HE2 H 2.84 . 1 167 . 15 LYS HE3 H 2.84 . 1 168 . 15 LYS N N 123.7 . 1 169 . 16 HIS H H 8.75 . 1 170 . 16 HIS CA C 52.5 . 1 171 . 16 HIS HA H 5.12 . 1 172 . 16 HIS CB C 31.9 . 1 173 . 16 HIS CG C 132.6 . 1 174 . 16 HIS HB2 H 2.55 . 2 175 . 16 HIS HB3 H 2.57 . 2 176 . 16 HIS ND1 N 213.8 . 1 177 . 16 HIS CD2 C 119.2 . 1 178 . 16 HIS CE1 C 136.1 . 1 179 . 16 HIS NE2 N 183.8 . 1 180 . 16 HIS HD2 H 6.89 . 1 181 . 16 HIS HE1 H 7.99 . 1 182 . 16 HIS N N 125.3 . 1 183 . 17 GLU H H 8.91 . 1 184 . 17 GLU CA C 53.8 . 1 185 . 17 GLU HA H 5.21 . 1 186 . 17 GLU CB C 30.3 . 1 187 . 17 GLU CG C 35.2 . 1 188 . 17 GLU HB2 H 1.94 . 1 189 . 17 GLU HB3 H 1.94 . 1 190 . 17 GLU HG2 H 2.16 . 1 191 . 17 GLU HG3 H 2.16 . 1 192 . 17 GLU N N 125.3 . 1 193 . 18 ILE H H 9.25 . 1 194 . 18 ILE CA C 57.8 . 1 195 . 18 ILE HA H 4.88 . 1 196 . 18 ILE CB C 40.7 . 1 197 . 18 ILE CG1 C 24.1 . 1 198 . 18 ILE CG2 C 17.5 . 1 199 . 18 ILE HB H 1.95 . 1 200 . 18 ILE CD1 C 12.7 . 1 201 . 18 ILE HG12 H 1.11 . 2 202 . 18 ILE HG13 H 1.4 . 2 203 . 18 ILE HG2 H 1.98 . 1 204 . 18 ILE HD1 H .67 . 1 205 . 18 ILE N N 121.1 . 1 206 . 19 GLU H H 8.68 . 1 207 . 19 GLU CA C 53.7 . 1 208 . 19 GLU HA H 5.04 . 1 209 . 19 GLU CB C 29.6 . 1 210 . 19 GLU CG C 35.2 . 1 211 . 19 GLU HB2 H 1.82 . 2 212 . 19 GLU HB3 H 1.9 . 2 213 . 19 GLU HG2 H 2.02 . 2 214 . 19 GLU HG3 H 2.23 . 2 215 . 19 GLU N N 123.6 . 1 216 . 20 VAL H H 9.6 . 1 217 . 20 VAL CA C 57.8 . 1 218 . 20 VAL HA H 4.71 . 1 219 . 20 VAL C C 171.7 . 1 220 . 20 VAL CB C 34 . 1 221 . 20 VAL CG1 C 20.3 . 2 222 . 20 VAL CG2 C 21.7 . 2 223 . 20 VAL HB H 2.12 . 1 224 . 20 VAL HG1 H .92 . 2 225 . 20 VAL HG2 H 1.19 . 2 226 . 20 VAL N N 127.4 . 1 227 . 21 PRO CA C 61.2 . 1 228 . 21 PRO HA H 4.79 . 1 229 . 21 PRO C C 174.3 . 1 230 . 21 PRO CB C 31.9 . 1 231 . 21 PRO CG C 26.5 . 1 232 . 21 PRO HB2 H 2.91 . 1 233 . 21 PRO HB3 H 2.91 . 1 234 . 21 PRO CD C 50.3 . 1 235 . 21 PRO HG2 H 1.95 . 2 236 . 21 PRO HG3 H 2.2 . 2 237 . 21 PRO HD2 H 3.77 . 2 238 . 21 PRO HD3 H 3.97 . 2 239 . 21 PRO N N 139.3 . 1 240 . 22 ASP H H 8.67 . 1 241 . 22 ASP CA C 57.1 . 1 242 . 22 ASP HA H 4.4 . 1 243 . 22 ASP CB C 37.9 . 1 244 . 22 ASP HB2 H 2.66 . 2 245 . 22 ASP HB3 H 3.31 . 2 246 . 22 ASP N N 117.7 . 1 247 . 23 ASP H H 7.96 . 1 248 . 23 ASP CA C 50.5 . 1 249 . 23 ASP HA H 4.25 . 1 250 . 23 ASP CB C 37.9 . 1 251 . 23 ASP HB2 H 2.9 . 2 252 . 23 ASP HB3 H 2.31 . 2 253 . 23 ASP N N 118.2 . 1 254 . 24 GLU H H 8.04 . 1 255 . 24 GLU CA C 53 . 1 256 . 24 GLU HA H 4.67 . 1 257 . 24 GLU CB C 31.4 . 1 258 . 24 GLU CG C 33.7 . 1 259 . 24 GLU HB2 H 1.81 . 2 260 . 24 GLU HB3 H 2.17 . 2 261 . 24 GLU CD C 181 . 1 262 . 24 GLU HG2 H 2.51 . 1 263 . 24 GLU HG3 H 2.51 . 1 264 . 24 GLU N N 122.8 . 1 265 . 25 TYR H H 8.42 . 1 266 . 25 TYR CA C 53 . 1 267 . 25 TYR HA H 4.7 . 1 268 . 25 TYR C C 177.7 . 1 269 . 25 TYR CB C 37 . 1 270 . 25 TYR CG C 128 . 1 271 . 25 TYR HB2 H 2.78 . 1 272 . 25 TYR HB3 H 2.78 . 1 273 . 25 TYR CD1 C 130.4 . 1 274 . 25 TYR CD2 C 130.4 . 1 275 . 25 TYR CE1 C 116 . 1 276 . 25 TYR HD1 H 6.39 . 1 277 . 25 TYR CE2 C 116 . 1 278 . 25 TYR HD2 H 6.39 . 1 279 . 25 TYR CZ C 154.8 . 1 280 . 25 TYR N N 121.3 . 1 281 . 26 ILE H H 8.95 . 1 282 . 26 ILE CA C 65.3 . 1 283 . 26 ILE HA H 3.61 . 1 284 . 26 ILE C C 175.3 . 1 285 . 26 ILE CB C 37.3 . 1 286 . 26 ILE CG1 C 29.3 . 1 287 . 26 ILE CG2 C 14.6 . 1 288 . 26 ILE HB H 1.86 . 1 289 . 26 ILE CD1 C 12 . 1 290 . 26 ILE HG12 H 1.04 . 2 291 . 26 ILE HG13 H 2.28 . 2 292 . 26 ILE HG2 H .78 . 1 293 . 26 ILE HD1 H .76 . 1 294 . 26 ILE N N 120.6 . 1 295 . 27 LEU H H 7.33 . 1 296 . 27 LEU CA C 57.9 . 1 297 . 27 LEU HA H 3.94 . 1 298 . 27 LEU CB C 41.2 . 1 299 . 27 LEU N N 116.7 . 1 300 . 28 ASP H H 6.75 . 1 301 . 28 ASP CA C 55.9 . 1 302 . 28 ASP HA H 4.23 . 1 303 . 28 ASP CB C 38.8 . 1 304 . 28 ASP HB2 H 2.87 . 1 305 . 28 ASP HB3 H 2.87 . 1 306 . 28 ASP N N 117.9 . 1 307 . 29 ALA H H 8.12 . 1 308 . 29 ALA CA C 53.4 . 1 309 . 29 ALA HA H 4.33 . 1 310 . 29 ALA C C 178.2 . 1 311 . 29 ALA CB C 19.1 . 1 312 . 29 ALA HB H 1.62 . 1 313 . 29 ALA N N 123.4 . 1 314 . 30 ALA H H 8.61 . 1 315 . 30 ALA CA C 54.4 . 1 316 . 30 ALA HA H 3.99 . 1 317 . 30 ALA CB C 16.5 . 1 318 . 30 ALA HB H 1.57 . 1 319 . 30 ALA N N 121.9 . 1 320 . 31 GLU H H 8.48 . 1 321 . 31 GLU CA C 57.8 . 1 322 . 31 GLU HA H 4.2 . 1 323 . 31 GLU CB C 28.7 . 1 324 . 31 GLU CG C 35.1 . 1 325 . 31 GLU HB2 H 2.1 . 2 326 . 31 GLU HB3 H 2.38 . 2 327 . 31 GLU HG2 H 2.57 . 1 328 . 31 GLU HG3 H 2.57 . 1 329 . 31 GLU N N 120 . 1 330 . 32 GLU H H 8.35 . 1 331 . 32 GLU CA C 57.6 . 1 332 . 32 GLU HA H 4.12 . 1 333 . 32 GLU C C 176.9 . 1 334 . 32 GLU CB C 27.9 . 1 335 . 32 GLU CG C 34.9 . 1 336 . 32 GLU HB2 H 2.3 . 2 337 . 32 GLU HB3 H 2.38 . 2 338 . 32 GLU HG2 H 2.43 . 2 339 . 32 GLU HG3 H 2.52 . 2 340 . 32 GLU N N 122.4 . 1 341 . 33 GLN H H 7.62 . 1 342 . 33 GLN CA C 54.4 . 1 343 . 33 GLN HA H 4.35 . 1 344 . 33 GLN C C 173.4 . 1 345 . 33 GLN CB C 27.8 . 1 346 . 33 GLN CG C 32.2 . 1 347 . 33 GLN HB2 H 2.05 . 2 348 . 33 GLN HB3 H 2.73 . 2 349 . 33 GLN CD C 178.9 . 1 350 . 33 GLN HG2 H 2.58 . 2 351 . 33 GLN HG3 H 2.69 . 2 352 . 33 GLN NE2 N 114.8 . 1 353 . 33 GLN HE21 H 7.48 . 2 354 . 33 GLN HE22 H 7.73 . 2 355 . 33 GLN N N 116.9 . 1 356 . 34 GLY H H 7.73 . 1 357 . 34 GLY CA C 43.8 . 1 358 . 34 GLY HA2 H 3.68 . 2 359 . 34 GLY C C 172.4 . 1 360 . 34 GLY HA3 H 3.96 . 2 361 . 34 GLY N N 107.4 . 1 362 . 35 TYR H H 8.27 . 1 363 . 35 TYR CA C 56 . 1 364 . 35 TYR HA H 4.5 . 1 365 . 35 TYR CB C 36.9 . 1 366 . 35 TYR CG C 129.3 . 1 367 . 35 TYR HB2 H 2.49 . 2 368 . 35 TYR HB3 H 2.81 . 2 369 . 35 TYR CD1 C 130.7 . 1 370 . 35 TYR CD2 C 130.7 . 1 371 . 35 TYR CE1 C 116.1 . 1 372 . 35 TYR HD1 H 6.8 . 1 373 . 35 TYR CE2 C 116.1 . 1 374 . 35 TYR HD2 H 6.8 . 1 375 . 35 TYR CZ C 154.8 . 1 376 . 35 TYR HE1 H 6.34 . 1 377 . 35 TYR HE2 H 6.34 . 1 378 . 35 TYR N N 123.1 . 1 379 . 36 ASP H H 8.34 . 1 380 . 36 ASP CA C 52.4 . 1 381 . 36 ASP HA H 4.84 . 1 382 . 36 ASP CB C 40 . 1 383 . 36 ASP CG C 178.9 . 1 384 . 36 ASP HB2 H 2.58 . 2 385 . 36 ASP HB3 H 2.73 . 2 386 . 36 ASP N N 123 . 1 387 . 37 LEU H H 8.22 . 1 388 . 37 LEU CA C 50.4 . 1 389 . 37 LEU HA H 4.73 . 1 390 . 37 LEU C C 173.2 . 1 391 . 37 LEU CB C 41.6 . 1 392 . 37 LEU CG C 26 . 1 393 . 37 LEU HB2 H 1.53 . 2 394 . 37 LEU HB3 H 2.01 . 2 395 . 37 LEU CD1 C 22 . 2 396 . 37 LEU CD2 C 23.9 . 2 397 . 37 LEU HG H 1.67 . 1 398 . 37 LEU HD1 H .86 . 2 399 . 37 LEU HD2 H 1.07 . 2 400 . 37 LEU N N 127 . 1 401 . 38 PRO CA C 61.2 . 1 402 . 38 PRO HA H 4.4 . 1 403 . 38 PRO C C 175 . 1 404 . 38 PRO CB C 30.7 . 1 405 . 38 PRO CG C 26.3 . 1 406 . 38 PRO CD C 48 . 1 407 . 38 PRO HD2 H 3.15 . 2 408 . 38 PRO HD3 H 3.2 . 2 409 . 38 PRO N N 134.3 . 1 410 . 39 PHE CG C 136.3 . 1 411 . 39 PHE CD1 C 132.2 . 1 412 . 39 PHE CD2 C 132.2 . 1 413 . 39 PHE CE1 C 130.4 . 1 414 . 39 PHE CE2 C 130.4 . 1 415 . 39 PHE CZ C 129.9 . 1 416 . 39 PHE HE1 H 7.23 . 1 417 . 39 PHE HE2 H 7.23 . 1 418 . 39 PHE HZ H 7.34 . 1 419 . 42 ARG NE N 84.9 . 1 420 . 42 ARG CZ C 157.1 . 1 421 . 42 ARG HE H 7.13 . 1 422 . 42 ARG NH1 N 71.4 . 2 423 . 42 ARG NH2 N 73.2 . 2 424 . 50 ALA CA C 52 . 1 425 . 50 ALA C C 176.9 . 1 426 . 50 ALA CB C 17.7 . 1 427 . 50 ALA HB H 1.2 . 1 428 . 51 GLY H H 9.82 . 1 429 . 51 GLY CA C 42.3 . 1 430 . 51 GLY HA2 H 3.41 . 2 431 . 51 GLY C C 169.6 . 1 432 . 51 GLY HA3 H 4.93 . 2 433 . 51 GLY N N 113.1 . 1 434 . 52 LYS H H 9.54 . 1 435 . 52 LYS CA C 53.6 . 1 436 . 52 LYS HA H 4.81 . 1 437 . 52 LYS C C 173.6 . 1 438 . 52 LYS CB C 36.1 . 1 439 . 52 LYS CG C 23.9 . 1 440 . 52 LYS HB2 H 1.24 . 2 441 . 52 LYS HB3 H 1.86 . 2 442 . 52 LYS CD C 27.9 . 1 443 . 52 LYS HG2 H .29 . 2 444 . 52 LYS HG3 H 1.07 . 2 445 . 52 LYS CE C 40.5 . 1 446 . 52 LYS HD2 H 1.43 . 1 447 . 52 LYS HD3 H 1.43 . 1 448 . 52 LYS NZ N 35 . 1 449 . 52 LYS HE2 H 1.31 . 2 450 . 52 LYS HE3 H 2.73 . 2 451 . 52 LYS N N 123.1 . 1 452 . 53 LEU H H 9.5 . 1 453 . 53 LEU CA C 55 . 1 454 . 53 LEU HA H 4.14 . 1 455 . 53 LEU C C 175.3 . 1 456 . 53 LEU CB C 41.2 . 1 457 . 53 LEU CG C 25.4 . 1 458 . 53 LEU HB2 H 1.29 . 2 459 . 53 LEU HB3 H 1.67 . 2 460 . 53 LEU CD1 C 21.6 . 2 461 . 53 LEU CD2 C 22.7 . 2 462 . 53 LEU HG H 1.5 . 1 463 . 53 LEU HD1 H .67 . 2 464 . 53 LEU HD2 H .81 . 2 465 . 53 LEU N N 130.3 . 1 466 . 54 VAL H H 9.09 . 1 467 . 54 VAL CA C 62.2 . 1 468 . 54 VAL HA H 3.97 . 1 469 . 54 VAL C C 174.7 . 1 470 . 54 VAL CB C 31.4 . 1 471 . 54 VAL CG1 C 18.8 . 2 472 . 54 VAL CG2 C 20 . 2 473 . 54 VAL HB H 1.79 . 1 474 . 54 VAL HG1 H .93 . 1 475 . 54 VAL HG2 H .93 . 1 476 . 54 VAL N N 126.4 . 1 477 . 55 SER H H 7.84 . 1 478 . 55 SER CA C 56.3 . 1 479 . 55 SER HA H 4.62 . 1 480 . 55 SER CB C 63.2 . 1 481 . 55 SER HB2 H 3.78 . 2 482 . 55 SER HB3 H 3.88 . 2 483 . 55 SER N N 112.7 . 1 484 . 56 GLY H H 8.44 . 1 485 . 56 GLY CA C 42.3 . 1 486 . 56 GLY HA2 H 3.79 . 2 487 . 56 GLY C C 170.7 . 1 488 . 56 GLY HA3 H 4.83 . 2 489 . 56 GLY N N 110.5 . 1 490 . 57 THR H H 7.94 . 1 491 . 57 THR CA C 57.9 . 1 492 . 57 THR HA H 4.73 . 1 493 . 57 THR C C 171.7 . 1 494 . 57 THR CB C 70.7 . 1 495 . 57 THR CG2 C 19.7 . 1 496 . 57 THR HB H 4.02 . 1 497 . 57 THR HG2 H 1.01 . 1 498 . 57 THR N N 107.4 . 1 499 . 58 VAL H H 8.27 . 1 500 . 58 VAL CA C 56.5 . 1 501 . 58 VAL HA H 5.12 . 1 502 . 58 VAL C C 173.4 . 1 503 . 58 VAL CB C 34.5 . 1 504 . 58 VAL CG1 C 17 . 2 505 . 58 VAL CG2 C 20.5 . 2 506 . 58 VAL HB H 2.01 . 1 507 . 58 VAL HG1 H .73 . 2 508 . 58 VAL HG2 H .76 . 2 509 . 58 VAL N N 110.2 . 1 510 . 59 ASP H H 9.49 . 1 511 . 59 ASP CA C 51.6 . 1 512 . 59 ASP HA H 5.05 . 1 513 . 59 ASP CB C 41.1 . 1 514 . 59 ASP CG C 179.1 . 1 515 . 59 ASP HB2 H 2.49 . 2 516 . 59 ASP HB3 H 3.1 . 2 517 . 59 ASP N N 121.9 . 1 518 . 60 GLN H H 9.26 . 1 519 . 60 GLN CA C 51.1 . 1 520 . 60 GLN HA H 5.74 . 1 521 . 60 GLN CB C 26.4 . 1 522 . 60 GLN CG C 30.1 . 1 523 . 60 GLN HB2 H 1.39 . 1 524 . 60 GLN HB3 H 1.39 . 1 525 . 60 GLN CD C 176 . 1 526 . 60 GLN HG2 H 2.29 . 2 527 . 60 GLN HG3 H 2.48 . 2 528 . 60 GLN NE2 N 108.6 . 1 529 . 60 GLN HE21 H 6.86 . 2 530 . 60 GLN HE22 H 7.06 . 2 531 . 60 GLN N N 125.1 . 1 532 . 61 SER H H 8.43 . 1 533 . 61 SER CA C 60.9 . 1 534 . 61 SER HA H 4.27 . 1 535 . 61 SER C C 173.7 . 1 536 . 61 SER CB C 61.7 . 1 537 . 61 SER HB2 H 4.08 . 2 538 . 61 SER HB3 H 4.15 . 2 539 . 61 SER N N 118.8 . 1 540 . 62 ASP H H 8.83 . 1 541 . 62 ASP CA C 54 . 1 542 . 62 ASP HA H 4.78 . 1 543 . 62 ASP CB C 39.7 . 1 544 . 62 ASP HB2 H 2.51 . 2 545 . 62 ASP HB3 H 2.58 . 2 546 . 62 ASP N N 120.3 . 1 547 . 63 GLN H H 8.57 . 1 548 . 63 GLN CA C 54.2 . 1 549 . 63 GLN HA H 4.41 . 1 550 . 63 GLN CB C 25.9 . 1 551 . 63 GLN CG C 30.9 . 1 552 . 63 GLN HB2 H 2.08 . 2 553 . 63 GLN HB3 H 2.51 . 2 554 . 63 GLN CD C 177.5 . 1 555 . 63 GLN NE2 N 111.9 . 1 556 . 63 GLN HE21 H 6.94 . 2 557 . 63 GLN HE22 H 7.44 . 2 558 . 63 GLN N N 123.7 . 1 559 . 64 SER CA C 56.2 . 1 560 . 64 SER HA H 4.77 . 1 561 . 64 SER CB C 63.6 . 1 562 . 64 SER HB2 H 3.73 . 2 563 . 64 SER HB3 H 4.01 . 2 564 . 65 PHE CA C 59.4 . 1 565 . 65 PHE HA H 4.44 . 1 566 . 65 PHE CB C 42.3 . 1 567 . 65 PHE CG C 137.2 . 1 568 . 65 PHE CD1 C 130.3 . 1 569 . 65 PHE CD2 C 130.3 . 1 570 . 65 PHE CE1 C 129.2 . 1 571 . 65 PHE HD1 H 7.56 . 1 572 . 65 PHE CE2 C 129.2 . 1 573 . 65 PHE HD2 H 7.56 . 1 574 . 65 PHE CZ C 128.3 . 1 575 . 65 PHE HE1 H 7.45 . 1 576 . 65 PHE HE2 H 7.45 . 1 577 . 65 PHE HZ H 7.35 . 1 578 . 66 LEU H H 10.48 . 1 579 . 66 LEU CA C 52.9 . 1 580 . 66 LEU HA H 4.33 . 1 581 . 66 LEU CB C 40.9 . 1 582 . 66 LEU HB2 H 1.36 . 2 583 . 66 LEU HB3 H 1.72 . 2 584 . 66 LEU N N 122.4 . 1 585 . 67 ASP H H 8.74 . 1 586 . 67 ASP CA C 50.7 . 1 587 . 67 ASP HA H 4.65 . 1 588 . 67 ASP CB C 39.8 . 1 589 . 67 ASP HB2 H 2.62 . 2 590 . 67 ASP HB3 H 3.12 . 2 591 . 67 ASP N N 123.8 . 1 592 . 68 ASP H H 8.4 . 1 593 . 68 ASP CA C 56.4 . 1 594 . 68 ASP HA H 4.33 . 1 595 . 68 ASP CB C 38.8 . 1 596 . 68 ASP CG C 177.2 . 1 597 . 68 ASP HB2 H 2.59 . 2 598 . 68 ASP HB3 H 2.74 . 2 599 . 68 ASP N N 118 . 1 600 . 69 ASP H H 8.23 . 1 601 . 69 ASP CA C 55.9 . 1 602 . 69 ASP HA H 4.45 . 1 603 . 69 ASP CB C 38.5 . 1 604 . 69 ASP HB2 H 2.67 . 2 605 . 69 ASP HB3 H 2.86 . 2 606 . 69 ASP N N 122.1 . 1 607 . 70 GLN H H 8.7 . 1 608 . 70 GLN CA C 57.3 . 1 609 . 70 GLN HA H 4.29 . 1 610 . 70 GLN CB C 27.3 . 1 611 . 70 GLN CG C 32.7 . 1 612 . 70 GLN HB2 H 1.74 . 2 613 . 70 GLN HB3 H 2.54 . 2 614 . 70 GLN CD C 177.3 . 1 615 . 70 GLN HG2 H 2.19 . 2 616 . 70 GLN HG3 H 2.76 . 2 617 . 70 GLN NE2 N 111.8 . 1 618 . 70 GLN HE21 H 7.37 . 2 619 . 70 GLN HE22 H 6.47 . 2 620 . 70 GLN N N 124.2 . 1 621 . 71 ILE H H 8.45 . 1 622 . 71 ILE CA C 62.9 . 1 623 . 71 ILE HA H 3.99 . 1 624 . 71 ILE C C 180.1 . 1 625 . 71 ILE CB C 36 . 1 626 . 71 ILE CG1 C 27.5 . 1 627 . 71 ILE CG2 C 15.5 . 1 628 . 71 ILE HB H 2.05 . 1 629 . 71 ILE CD1 C 10.7 . 1 630 . 71 ILE HG12 H 1.06 . 2 631 . 71 ILE HG13 H 1.69 . 2 632 . 71 ILE HG2 H .99 . 1 633 . 71 ILE HD1 H .8 . 1 634 . 71 ILE N N 122.1 . 1 635 . 72 GLU H H 8.48 . 1 636 . 72 GLU CA C 57.7 . 1 637 . 72 GLU HA H 4.08 . 1 638 . 72 GLU C C 176.2 . 1 639 . 72 GLU CB C 27.6 . 1 640 . 72 GLU CG C 34.7 . 1 641 . 72 GLU HB2 H 2.2 . 2 642 . 72 GLU HB3 H 2.25 . 2 643 . 72 GLU HG2 H 2.36 . 2 644 . 72 GLU HG3 H 2.43 . 2 645 . 72 GLU N N 125 . 1 646 . 73 ALA H H 7.74 . 1 647 . 73 ALA CA C 51.2 . 1 648 . 73 ALA HA H 4.31 . 1 649 . 73 ALA C C 175.5 . 1 650 . 73 ALA CB C 17.7 . 1 651 . 73 ALA HB H 1.75 . 1 652 . 73 ALA N N 120.5 . 1 653 . 74 GLY H H 7.79 . 1 654 . 74 GLY CA C 43.3 . 1 655 . 74 GLY HA2 H 3.78 . 2 656 . 74 GLY C C 173 . 1 657 . 74 GLY HA3 H 4.33 . 2 658 . 74 GLY N N 104.6 . 1 659 . 75 TYR H H 7.96 . 1 660 . 75 TYR CA C 59.5 . 1 661 . 75 TYR HA H 5.02 . 1 662 . 75 TYR CB C 37.5 . 1 663 . 75 TYR CG C 130.7 . 1 664 . 75 TYR HB2 H 2.67 . 2 665 . 75 TYR HB3 H 2.79 . 2 666 . 75 TYR CD1 C 131.4 . 1 667 . 75 TYR CD2 C 131.4 . 1 668 . 75 TYR CE1 C 116.6 . 1 669 . 75 TYR HD1 H 7.33 . 1 670 . 75 TYR CE2 C 116.6 . 1 671 . 75 TYR HD2 H 7.33 . 1 672 . 75 TYR CZ C 150.2 . 1 673 . 75 TYR HE1 H 6.77 . 1 674 . 75 TYR HE2 H 6.77 . 1 675 . 75 TYR N N 120.1 . 1 676 . 76 VAL H H 8.68 . 1 677 . 76 VAL CA C 57.3 . 1 678 . 76 VAL HA H 4.83 . 1 679 . 76 VAL CB C 35.2 . 1 680 . 76 VAL CG1 C 20.1 . 2 681 . 76 VAL CG2 C 20.6 . 2 682 . 76 VAL HB H 1.57 . 1 683 . 76 VAL HG1 H .6 . 2 684 . 76 VAL HG2 H .71 . 2 685 . 76 VAL N N 119.1 . 1 686 . 78 THR CA C 60.2 . 1 687 . 78 THR HA H 4.43 . 1 688 . 78 THR CB C 68.3 . 1 689 . 78 THR CG2 C 20 . 1 690 . 78 THR HB H 4.17 . 1 691 . 78 THR HG2 H 1.18 . 1 692 . 80 VAL CA C 52 . 1 693 . 80 VAL HA H 4.74 . 1 694 . 80 VAL CB C 29.6 . 1 695 . 80 VAL CG1 C 21.8 . 1 696 . 80 VAL CG2 C 21.8 . 1 697 . 81 ALA H H 6.36 . 1 698 . 81 ALA CA C 48.6 . 1 699 . 81 ALA HA H 5.14 . 1 700 . 81 ALA C C 174.4 . 1 701 . 81 ALA CB C 20.3 . 1 702 . 81 ALA HB H 1.07 . 1 703 . 81 ALA N N 122.6 . 1 704 . 82 TYR H H 9.13 . 1 705 . 82 TYR CA C 53.2 . 1 706 . 82 TYR HA H 5.49 . 1 707 . 82 TYR C C 173.9 . 1 708 . 82 TYR CB C 38.1 . 1 709 . 82 TYR CG C 128.4 . 1 710 . 82 TYR HB2 H 2.88 . 2 711 . 82 TYR HB3 H 3.21 . 2 712 . 82 TYR CD1 C 132.1 . 1 713 . 82 TYR CD2 C 132.1 . 1 714 . 82 TYR CE1 C 116.4 . 1 715 . 82 TYR HD1 H 7.13 . 1 716 . 82 TYR CE2 C 116.4 . 1 717 . 82 TYR HD2 H 7.13 . 1 718 . 82 TYR CZ C 156 . 1 719 . 82 TYR HE1 H 6.43 . 1 720 . 82 TYR HE2 H 6.43 . 1 721 . 82 TYR N N 125.2 . 1 722 . 83 PRO CA C 62 . 1 723 . 83 PRO HA H 4.73 . 1 724 . 83 PRO C C 174.9 . 1 725 . 83 PRO CB C 29.5 . 1 726 . 83 PRO CG C 26.5 . 1 727 . 83 PRO HB2 H 1.99 . 2 728 . 83 PRO HB3 H 2.21 . 2 729 . 83 PRO CD C 48.9 . 1 730 . 83 PRO HD2 H 4.09 . 2 731 . 83 PRO HD3 H 4.41 . 2 732 . 83 PRO N N 137.8 . 1 733 . 84 THR H H 8.46 . 1 734 . 84 THR CA C 58.6 . 1 735 . 84 THR HA H 4.23 . 1 736 . 84 THR C C 170.6 . 1 737 . 84 THR CB C 66.8 . 1 738 . 84 THR CG2 C 21.6 . 1 739 . 84 THR HB H 4.44 . 1 740 . 84 THR HG2 H 1.11 . 1 741 . 84 THR N N 111.7 . 1 742 . 85 SER H H 7.73 . 1 743 . 85 SER CA C 56.1 . 1 744 . 85 SER HA H 3.57 . 1 745 . 85 SER C C 170.2 . 1 746 . 85 SER CB C 64.4 . 1 747 . 85 SER HB2 H 3.74 . 2 748 . 85 SER HB3 H 4.09 . 2 749 . 85 SER N N 118.8 . 1 750 . 86 ASP H H 8.54 . 1 751 . 86 ASP CA C 55 . 1 752 . 86 ASP HA H 5.33 . 1 753 . 86 ASP C C 178.2 . 1 754 . 86 ASP CB C 38.4 . 1 755 . 86 ASP HB2 H 2.61 . 2 756 . 86 ASP HB3 H 2.76 . 2 757 . 86 ASP N N 119.3 . 1 758 . 87 VAL H H 9.05 . 1 759 . 87 VAL CA C 59.1 . 1 760 . 87 VAL HA H 4.92 . 1 761 . 87 VAL C C 172.5 . 1 762 . 87 VAL CB C 35.9 . 1 763 . 87 VAL CG1 C 21.4 . 1 764 . 87 VAL CG2 C 21.4 . 1 765 . 87 VAL HB H 1.92 . 1 766 . 87 VAL HG1 H .89 . 2 767 . 87 VAL HG2 H 1.01 . 2 768 . 87 VAL N N 126.6 . 1 769 . 88 VAL H H 8.55 . 1 770 . 88 VAL CA C 60.3 . 1 771 . 88 VAL HA H 4.78 . 1 772 . 88 VAL C C 173.3 . 1 773 . 88 VAL CB C 31.7 . 1 774 . 88 VAL CG1 C 18.9 . 2 775 . 88 VAL CG2 C 19.8 . 2 776 . 88 VAL HB H 2.03 . 1 777 . 88 VAL HG1 H .87 . 2 778 . 88 VAL HG2 H .92 . 2 779 . 88 VAL N N 128.5 . 1 780 . 89 ILE H H 9.46 . 1 781 . 89 ILE CA C 57.7 . 1 782 . 89 ILE HA H 4.91 . 1 783 . 89 ILE CB C 41.7 . 1 784 . 89 ILE CG1 C 27 . 1 785 . 89 ILE CG2 C 14.5 . 1 786 . 89 ILE HB H 1.51 . 1 787 . 89 ILE CD1 C 12.9 . 1 788 . 89 ILE HG12 H .82 . 2 789 . 89 ILE HG13 H 1.44 . 2 790 . 89 ILE HG2 H .71 . 1 791 . 89 ILE HD1 H .49 . 1 792 . 89 ILE N N 128.8 . 1 793 . 90 GLN H H 9.21 . 1 794 . 90 GLN CA C 52.3 . 1 795 . 90 GLN HA H 5.47 . 1 796 . 90 GLN C C 175.2 . 1 797 . 90 GLN CB C 27.5 . 1 798 . 90 GLN CG C 31.8 . 1 799 . 90 GLN HB2 H 2.09 . 2 800 . 90 GLN HB3 H 2.3 . 2 801 . 90 GLN CD C 177 . 1 802 . 90 GLN HG2 H 2.18 . 2 803 . 90 GLN HG3 H 2.3 . 2 804 . 90 GLN NE2 N 110.9 . 1 805 . 90 GLN HE21 H 6.52 . 2 806 . 90 GLN HE22 H 7.25 . 2 807 . 90 GLN N N 127.3 . 1 808 . 91 THR H H 9.12 . 1 809 . 91 THR CA C 59.8 . 1 810 . 91 THR HA H 4.56 . 1 811 . 91 THR C C 172.6 . 1 812 . 91 THR CB C 67.3 . 1 813 . 91 THR CG2 C 21.1 . 1 814 . 91 THR HB H 4.67 . 1 815 . 91 THR HG2 H 1.18 . 1 816 . 91 THR N N 116.7 . 1 817 . 92 HIS H H 9.14 . 1 818 . 92 HIS CA C 57.2 . 1 819 . 92 HIS HA H 4.52 . 1 820 . 92 HIS C C 176.7 . 1 821 . 92 HIS CB C 24.6 . 1 822 . 92 HIS CG C 138 . 1 823 . 92 HIS HB2 H 3.31 . 2 824 . 92 HIS HB3 H 3.39 . 2 825 . 92 HIS ND1 N 243.1 . 1 826 . 92 HIS CD2 C 116.3 . 1 827 . 92 HIS CE1 C 136.5 . 1 828 . 92 HIS NE2 N 168.6 . 1 829 . 92 HIS HD2 H 7.18 . 1 830 . 92 HIS HE1 H 7.81 . 1 831 . 92 HIS N N 113.8 . 1 832 . 93 LYS H H 7.43 . 1 833 . 93 LYS HA H 4.74 . 1 834 . 93 LYS CB C 31.1 . 1 835 . 93 LYS CG C 23.1 . 1 836 . 93 LYS HB2 H 1.21 . 1 837 . 93 LYS HB3 H 1.21 . 1 838 . 93 LYS CD C 27.5 . 1 839 . 93 LYS HG2 H 2.36 . 1 840 . 93 LYS HG3 H 2.36 . 1 841 . 93 LYS CE C 40.3 . 1 842 . 93 LYS HD2 H 1.73 . 1 843 . 93 LYS HD3 H 1.73 . 1 844 . 93 LYS NZ N 33.5 . 1 845 . 93 LYS HE2 H 3.01 . 1 846 . 93 LYS HE3 H 3.01 . 1 847 . 93 LYS N N 115.3 . 1 848 . 94 GLU H H 8.33 . 1 849 . 94 GLU CA C 59.4 . 1 850 . 94 GLU HA H 3.12 . 1 851 . 94 GLU C C 175.7 . 1 852 . 94 GLU CB C 27.7 . 1 853 . 94 GLU CG C 33.9 . 1 854 . 94 GLU HB2 H 1.94 . 1 855 . 94 GLU HB3 H 1.94 . 1 856 . 94 GLU CD C 179 . 1 857 . 94 GLU HG2 H 2.13 . 1 858 . 94 GLU HG3 H 2.13 . 1 859 . 94 GLU N N 122.9 . 1 860 . 95 GLU H H 8.65 . 1 861 . 95 GLU CA C 56.8 . 1 862 . 95 GLU HA H 3.79 . 1 863 . 95 GLU C C 176 . 1 864 . 95 GLU CB C 27.5 . 1 865 . 95 GLU HB2 H 2.05 . 2 866 . 95 GLU HB3 H 2.09 . 2 867 . 95 GLU HG2 H 2.28 . 2 868 . 95 GLU HG3 H 2.32 . 2 869 . 95 GLU N N 114.7 . 1 870 . 96 ASP H H 7.87 . 1 871 . 96 ASP CA C 53.7 . 1 872 . 96 ASP HA H 4.39 . 1 873 . 96 ASP C C 175.8 . 1 874 . 96 ASP CB C 39.7 . 1 875 . 96 ASP HB2 H 2.94 . 1 876 . 96 ASP HB3 H 2.94 . 1 877 . 96 ASP N N 120.4 . 1 878 . 97 LEU H H 7.81 . 1 879 . 97 LEU CA C 53.1 . 1 880 . 97 LEU HA H 3.99 . 1 881 . 97 LEU CB C 39.6 . 1 882 . 97 LEU CG C 25.2 . 1 883 . 97 LEU HB2 H 1.33 . 2 884 . 97 LEU HB3 H 1.66 . 2 885 . 97 LEU CD1 C 19.6 . 2 886 . 97 LEU CD2 C 24.6 . 2 887 . 97 LEU HG H 1.14 . 1 888 . 97 LEU HD1 H 0 . 2 889 . 97 LEU HD2 H .6 . 2 890 . 97 LEU N N 119.1 . 1 891 . 98 TYR H H 7.07 . 1 892 . 98 TYR CA C 57.4 . 1 893 . 98 TYR HA H 4.38 . 1 894 . 98 TYR CB C 38.3 . 1 895 . 98 TYR CG C 130.7 . 1 896 . 98 TYR HB2 H 2.81 . 2 897 . 98 TYR HB3 H 3.17 . 2 898 . 98 TYR CD1 C 116.6 . 1 899 . 98 TYR CD2 C 116.6 . 1 900 . 98 TYR CE1 C 131.6 . 1 901 . 98 TYR HD1 H 7.13 . 1 902 . 98 TYR CE2 C 131.6 . 1 903 . 98 TYR HD2 H 7.13 . 1 904 . 98 TYR CZ C 155.5 . 1 905 . 98 TYR HE1 H 6.79 . 1 906 . 98 TYR HE2 H 6.79 . 1 907 . 98 TYR N N 125.2 . 1 stop_ save_