data_447 #Corrected using PDB structure: 1QOGA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 80 V HA 4.70 2.62 # 94 E HA 3.08 4.03 # 95 E HA 3.75 4.48 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 80 V CA 53.54 60.10 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 1 A N 39.52 122.43 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 1.54 1.62 N/A -1.28 -0.04 # #bmr447.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr447.str file): #HA CA CB CO N HN #N/A +1.58 +1.58 N/A -1.28 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.20 +/-0.20 N/A +/-0.36 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.730 0.959 0.997 N/A 0.431 0.766 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.153 0.892 0.901 N/A 1.581 0.332 # ####################### # 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 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oh Byung-Ha . . 2 Markley John L. . stop_ _BMRB_accession_number 447 _BMRB_flat_file_name bmr447.str _Entry_type revision _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _NMR_STAR_version 2.1 _Experimental_method NMR 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 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 _MEDLINE_UI_code ? 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 _Page_first 3993 _Page_last 4004 _Year 1990 save_ ################################## # Molecular system description # ################################## save_system_2Fe-2S_ferredoxin _Saveframe_category molecular_system _Mol_system_name '2Fe-2S ferredoxin' _Abbreviation_common ? loop_ _Mol_system_component_name _Mol_label '2Fe-2S ferredoxin' $2Fe-2S_ferredoxin stop_ _System_physical_state ? _System_oligomer_state ? _System_paramagnetic ? loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1CZP "A Chain A, Anabaena Pcc7119 [2fe-2s] Ferredoxin In The Reduced And Oxixized State At 1.17 A" . PDB 1QT9 "A Chain A, Oxidized [2fe-2s] Ferredoxin From Anabaena Pcc7119" . PDB 1FXA "A Chain A, [2Fe-2S] Ferredoxin" . PDB 1QOG "A Chain A, Ferredoxin Mutation S47a" . PDB 1QOF "A Chain A, Ferredoxin Mutation Q70k" . PDB 1QOB "A Chain A, Ferredoxin Mutation D62k" . PDB 1QOA "A Chain A, Ferredoxin Mutation C49s" . stop_ save_ ######################## # Monomeric polymers # ######################## save_2Fe-2S_ferredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '2Fe-2S ferredoxin' _Abbreviation_common ? ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1CZP "A Chain A, Anabaena Pcc7119 [2fe-2s]Ferredoxin In The Reduced And Oxixized State At 1.17 A" 100.00 98 100 100 1e-51 PDB 1EWY "C Chain C, Anabaena Pcc7119Ferredoxin:ferredoxin-Nadp+-Reductase Complex" 100.00 98 100 100 1e-51 PDB 1FXA "A Chain A, [2Fe-2S] Ferredoxin" 100.00 98 100 100 1e-51 PDB 1QT9 "A Chain A, Oxidized [2fe-2s] Ferredoxin FromAnabaena Pcc7119" 100.00 98 100 100 1e-51 PDB 1J7A "A Chain A, Structure Of The AnabaenaFerredoxin D68k Mutant" 100.00 98 99 99 8e-51 PDB 1J7B "A Chain A, Structure Of The AnabaenaFerredoxin Mutant E94k" 100.00 98 99 100 4e-51 PDB 1J7C "A Chain A, Structure Of The AnabaenaFerredoxin Mutant E95k" 100.00 98 99 100 4e-51 PDB 1QOA "A Chain A, Ferredoxin Mutation C49s" 100.00 98 99 99 2e-50 PDB 1QOB "A Chain A, Ferredoxin Mutation D62k" 100.00 98 99 99 8e-51 PDB 1QOF "A Chain A, Ferredoxin Mutation Q70k" 100.00 98 99 100 4e-51 PDB 1QOG "A Chain A, Ferredoxin Mutation S47a" 100.00 98 99 100 3e-51 DBJ BAB75847.1 "ferredoxin I [Nostoc sp. PCC 7120]" 98.99 99 100 100 1e-51 GenBank AAA22021.1 "ferredoxin I" 98.99 99 100 100 1e-51 PIR FENM "ferredoxin [2Fe-2S] - Nostoc muscorum" 100.00 98 99 100 3e-51 PIR AE2324 "ferredoxin I [imported] - Nostoc sp.(strain PCC 7120)" 98.99 99 100 100 1e-51 PIR S25233 "ferredoxin [2Fe-2S] I [validated] - Anabaenasp. (strain PCC 7120)" 98.99 99 100 100 1e-51 PRF 1001142A "ferredoxin II" 100.00 98 98 99 10e-51 REF NP_488188.1 "ferredoxin I [Nostoc sp. PCC 7120]" 98.99 99 100 100 1e-51 SWISS-PROT P00253 "FER_NOSMU Ferredoxin" 100.00 98 99 100 3e-51 SWISS-PROT P06543 "FER1_ANASP Ferredoxin I" 98.99 99 100 100 1e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Genus _Species _Strain $2Fe-2S_ferredoxin . ? Anabaena variabilis 7120 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method $2Fe-2S_ferredoxin 'not available' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling ? ? ? ? stop_ save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions 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 loop_ _Mol_common_name _Atom_type _Chem_shift_value TSP H 0 TMS C 0 'liquid ammonia' N 0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts 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' loop_ _Atom_shift_assign_ID _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 51.58 . 1 2 1 ALA HA H 3.92 . 1 3 1 ALA C C 171.30 . 1 4 1 ALA CB C 19.68 . 1 5 1 ALA HB H 1.13 . 1 6 1 ALA N N 39.52 . 1 7 2 THR H H 8.06 . 1 8 2 THR CA C 60.78 . 1 9 2 THR HA H 4.49 . 1 10 2 THR C C 170.80 . 1 11 2 THR CB C 70.68 . 1 12 2 THR CG2 C 23.88 . 1 13 2 THR HB H 3.74 . 1 14 2 THR HG2 H 0.99 . 1 15 2 THR N N 113.22 . 1 16 3 PHE H H 8.58 . 1 17 3 PHE CA C 56.88 . 1 18 3 PHE HA H 4.98 . 1 19 3 PHE CB C 42.78 . 1 20 3 PHE CG C 137.88 . 1 21 3 PHE HB2 H 3.30 . 2 22 3 PHE HB3 H 2.34 . 2 23 3 PHE CD1 C 131.58 . 1 24 3 PHE CD2 C 131.58 . 1 25 3 PHE CE1 C 130.78 . 1 26 3 PHE HD1 H 7.13 . 1 27 3 PHE CE2 C 130.78 . 1 28 3 PHE HD2 H 7.13 . 1 29 3 PHE CZ C 129.58 . 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 123.42 . 1 34 4 LYS H H 9.17 . 1 35 4 LYS CA C 55.88 . 1 36 4 LYS HA H 4.70 . 1 37 4 LYS C C 174.70 . 1 38 4 LYS CB C 32.78 . 1 39 4 LYS CG C 24.68 . 1 40 4 LYS HB2 H 1.28 . 2 41 4 LYS HB3 H 1.73 . 2 42 4 LYS CD C 28.88 . 1 43 4 LYS HG2 H 1.41 . 2 44 4 LYS HG3 H 1.48 . 2 45 4 LYS CE C 41.68 . 1 46 4 LYS HD2 H 1.69 . 2 47 4 LYS HD3 H 1.76 . 2 48 4 LYS NZ N 33.10 . 1 49 4 LYS HE2 H 2.92 . 2 50 4 LYS HE3 H 3.08 . 2 51 4 LYS N N 122.82 . 1 52 5 VAL H H 9.33 . 1 53 5 VAL CA C 60.68 . 1 54 5 VAL HA H 5.09 . 1 55 5 VAL CB C 33.88 . 1 56 5 VAL CG1 C 20.78 . 2 57 5 VAL CG2 C 21.58 . 2 58 5 VAL HB H 2.03 . 1 59 5 VAL HG1 H 0.78 . 2 60 5 VAL HG2 H 0.96 . 2 61 5 VAL N N 127.82 . 1 62 6 THR H H 9.27 . 1 63 6 THR CA C 61.98 . 1 64 6 THR HA H 5.01 . 1 65 6 THR C C 171.50 . 1 66 6 THR CB C 69.18 . 1 67 6 THR CG2 C 21.18 . 1 68 6 THR HB H 4.21 . 1 69 6 THR HG2 H 1.12 . 1 70 6 THR N N 125.42 . 1 71 7 LEU H H 9.35 . 1 72 7 LEU CA C 53.08 . 1 73 7 LEU HA H 4.96 . 1 74 7 LEU CB C 42.58 . 1 75 7 LEU CG C 26.18 . 1 76 7 LEU HB2 H 1.48 . 2 77 7 LEU HB3 H 1.91 . 2 78 7 LEU CD1 C 22.98 . 2 79 7 LEU CD2 C 26.08 . 2 80 7 LEU HG H 1.65 . 1 81 7 LEU HD1 H 0.62 . 2 82 7 LEU HD2 H 0.73 . 2 83 7 LEU N N 127.12 . 1 84 8 ILE H H 9.37 . 1 85 8 ILE CA C 60.28 . 1 86 8 ILE HA H 4.70 . 1 87 8 ILE CB C 41.08 . 1 88 8 ILE CG1 C 27.58 . 1 89 8 ILE CG2 C 16.68 . 1 90 8 ILE HB H 1.74 . 1 91 8 ILE CD C 13.58 . 1 92 8 ILE HG12 H 0.91 . 2 93 8 ILE HG13 H 1.46 . 2 94 8 ILE HG2 H 0.91 . 1 95 8 ILE HD1 H 0.77 . 1 96 8 ILE N N 126.42 . 1 97 9 ASN H H 7.84 . 1 98 9 ASN CA C 51.08 . 1 99 9 ASN HA H 5.08 . 1 100 9 ASN C C 174.90 . 1 101 9 ASN CB C 37.88 . 1 102 9 ASN CG C 176.58 . 1 103 9 ASN HB2 H 2.48 . 2 104 9 ASN HB3 H 3.22 . 2 105 9 ASN ND2 N 111.80 . 1 106 9 ASN HD21 H 6.42 . 2 107 9 ASN HD22 H 6.80 . 2 108 9 ASN N N 125.42 . 1 109 10 GLU H H 9.45 . 1 110 10 GLU CA C 59.28 . 1 111 10 GLU HA H 4.00 . 1 112 10 GLU CB C 30.78 . 1 113 10 GLU CG C 37.18 . 1 114 10 GLU HB2 H 1.99 . 2 115 10 GLU HB3 H 2.11 . 2 116 10 GLU CD C 183.58 . 1 117 10 GLU HG2 H 2.20 . 2 118 10 GLU HG3 H 2.31 . 2 119 10 GLU N N 125.02 . 1 120 11 ALA H H 8.35 . 1 121 11 ALA CA C 54.88 . 1 122 11 ALA HA H 4.13 . 1 123 11 ALA C C 178.20 . 1 124 11 ALA CB C 18.28 . 1 125 11 ALA HB H 1.50 . 1 126 11 ALA N N 121.52 . 1 127 12 GLU H H 7.23 . 1 128 12 GLU CA C 55.78 . 1 129 12 GLU HA H 4.29 . 1 130 12 GLU C C 175.50 . 1 131 12 GLU CB C 31.18 . 1 132 12 GLU CG C 36.78 . 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 113.72 . 1 138 13 GLY H H 8.09 . 1 139 13 GLY CA C 46.38 . 1 140 13 GLY HA2 H 3.89 . 2 141 13 GLY C C 173.60 . 1 142 13 GLY HA3 H 4.01 . 2 143 13 GLY N N 109.12 . 1 144 14 THR H H 7.58 . 1 145 14 THR CA C 59.48 . 1 146 14 THR HA H 4.50 . 1 147 14 THR CB C 71.78 . 1 148 14 THR CG2 C 21.48 . 1 149 14 THR HB H 3.83 . 1 150 14 THR HG2 H 1.13 . 1 151 14 THR N N 107.62 . 1 152 15 LYS H H 8.20 . 1 153 15 LYS CA C 55.58 . 1 154 15 LYS HA H 4.91 . 1 155 15 LYS CB C 34.68 . 1 156 15 LYS CG C 24.88 . 1 157 15 LYS HB2 H 1.57 . 1 158 15 LYS HB3 H 1.57 . 1 159 15 LYS CD C 29.28 . 1 160 15 LYS HG2 H 1.10 . 2 161 15 LYS HG3 H 1.17 . 2 162 15 LYS CE C 41.48 . 1 163 15 LYS HD2 H 1.58 . 1 164 15 LYS HD3 H 1.58 . 1 165 15 LYS NZ N 33.70 . 1 166 15 LYS HE2 H 2.84 . 1 167 15 LYS HE3 H 2.84 . 1 168 15 LYS N N 122.42 . 1 169 16 HIS H H 8.75 . 1 170 16 HIS CA C 54.08 . 1 171 16 HIS HA H 5.12 . 1 172 16 HIS CB C 33.48 . 1 173 16 HIS CG C 134.18 . 1 174 16 HIS HB2 H 2.55 . 2 175 16 HIS HB3 H 2.57 . 2 176 16 HIS ND1 N 213.80 . 1 177 16 HIS CD2 C 120.78 . 1 178 16 HIS CE1 C 137.68 . 1 179 16 HIS NE2 N 183.80 . 1 180 16 HIS HD2 H 6.89 . 1 181 16 HIS HE1 H 7.99 . 1 182 16 HIS N N 124.02 . 1 183 17 GLU H H 8.91 . 1 184 17 GLU CA C 55.38 . 1 185 17 GLU HA H 5.21 . 1 186 17 GLU CB C 31.88 . 1 187 17 GLU CG C 36.78 . 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 124.02 . 1 193 18 ILE H H 9.25 . 1 194 18 ILE CA C 59.38 . 1 195 18 ILE HA H 4.88 . 1 196 18 ILE CB C 42.28 . 1 197 18 ILE CG1 C 25.68 . 1 198 18 ILE CG2 C 19.08 . 1 199 18 ILE HB H 1.95 . 1 200 18 ILE CD C 14.28 . 1 201 18 ILE HG12 H 1.11 . 2 202 18 ILE HG13 H 1.40 . 2 203 18 ILE HG2 H 1.98 . 1 204 18 ILE HD1 H 0.67 . 1 205 18 ILE N N 119.82 . 1 206 19 GLU H H 8.68 . 1 207 19 GLU CA C 55.28 . 1 208 19 GLU HA H 5.04 . 1 209 19 GLU CB C 31.18 . 1 210 19 GLU CG C 36.78 . 1 211 19 GLU HB2 H 1.82 . 2 212 19 GLU HB3 H 1.90 . 2 213 19 GLU HG2 H 2.02 . 2 214 19 GLU HG3 H 2.23 . 2 215 19 GLU N N 122.32 . 1 216 20 VAL H H 9.60 . 1 217 20 VAL CA C 59.38 . 1 218 20 VAL HA H 4.71 . 1 219 20 VAL C C 171.70 . 1 220 20 VAL CB C 35.58 . 1 221 20 VAL CG1 C 21.88 . 2 222 20 VAL CG2 C 23.28 . 2 223 20 VAL HB H 2.12 . 1 224 20 VAL HG1 H 0.92 . 2 225 20 VAL HG2 H 1.19 . 2 226 20 VAL N N 126.12 . 1 227 21 PRO CA C 62.78 . 1 228 21 PRO HA H 4.79 . 1 229 21 PRO C C 174.30 . 1 230 21 PRO CB C 33.48 . 1 231 21 PRO CG C 28.08 . 1 232 21 PRO HB2 H 2.91 . 1 233 21 PRO HB3 H 2.91 . 1 234 21 PRO CD C 51.88 . 1 235 21 PRO HG2 H 1.95 . 2 236 21 PRO HG3 H 2.20 . 2 237 21 PRO HD2 H 3.77 . 2 238 21 PRO HD3 H 3.97 . 2 239 21 PRO N N 138.02 . 1 240 22 ASP H H 8.67 . 1 241 22 ASP CA C 58.68 . 1 242 22 ASP HA H 4.40 . 1 243 22 ASP CB C 39.48 . 1 244 22 ASP HB2 H 2.66 . 2 245 22 ASP HB3 H 3.31 . 2 246 22 ASP N N 116.42 . 1 247 23 ASP H H 7.96 . 1 248 23 ASP CA C 52.08 . 1 249 23 ASP HA H 4.25 . 1 250 23 ASP CB C 39.48 . 1 251 23 ASP HB2 H 2.90 . 2 252 23 ASP HB3 H 2.31 . 2 253 23 ASP N N 116.92 . 1 254 24 GLU H H 8.04 . 1 255 24 GLU CA C 54.58 . 1 256 24 GLU HA H 4.67 . 1 257 24 GLU CB C 32.98 . 1 258 24 GLU CG C 35.28 . 1 259 24 GLU HB2 H 1.81 . 2 260 24 GLU HB3 H 2.17 . 2 261 24 GLU CD C 182.58 . 1 262 24 GLU HG2 H 2.51 . 1 263 24 GLU HG3 H 2.51 . 1 264 24 GLU N N 121.52 . 1 265 25 TYR H H 8.42 . 1 266 25 TYR CA C 54.58 . 1 267 25 TYR HA H 4.70 . 1 268 25 TYR C C 177.70 . 1 269 25 TYR CB C 38.58 . 1 270 25 TYR CG C 129.58 . 1 271 25 TYR HB2 H 2.78 . 1 272 25 TYR HB3 H 2.78 . 1 273 25 TYR CD1 C 131.98 . 1 274 25 TYR CD2 C 131.98 . 1 275 25 TYR CE1 C 117.58 . 1 276 25 TYR HD1 H 6.39 . 1 277 25 TYR CE2 C 117.58 . 1 278 25 TYR HD2 H 6.39 . 1 279 25 TYR CZ C 156.38 . 1 280 25 TYR N N 120.02 . 1 281 26 ILE H H 8.95 . 1 282 26 ILE CA C 66.88 . 1 283 26 ILE HA H 3.61 . 1 284 26 ILE C C 175.30 . 1 285 26 ILE CB C 38.88 . 1 286 26 ILE CG1 C 30.88 . 1 287 26 ILE CG2 C 16.18 . 1 288 26 ILE HB H 1.86 . 1 289 26 ILE CD C 13.58 . 1 290 26 ILE HG12 H 1.04 . 2 291 26 ILE HG13 H 2.28 . 2 292 26 ILE HG2 H 0.78 . 1 293 26 ILE HD1 H 0.76 . 1 294 26 ILE N N 119.32 . 1 295 27 LEU H H 7.33 . 1 296 27 LEU CA C 59.48 . 1 297 27 LEU HA H 3.94 . 1 298 27 LEU CB C 42.78 . 1 299 27 LEU N N 115.42 . 1 300 28 ASP H H 6.75 . 1 301 28 ASP CA C 57.48 . 1 302 28 ASP HA H 4.23 . 1 303 28 ASP CB C 40.38 . 1 304 28 ASP HB2 H 2.87 . 1 305 28 ASP HB3 H 2.87 . 1 306 28 ASP N N 116.62 . 1 307 29 ALA H H 8.12 . 1 308 29 ALA CA C 54.98 . 1 309 29 ALA HA H 4.33 . 1 310 29 ALA C C 178.20 . 1 311 29 ALA CB C 20.68 . 1 312 29 ALA HB H 1.62 . 1 313 29 ALA N N 122.12 . 1 314 30 ALA H H 8.61 . 1 315 30 ALA CA C 55.98 . 1 316 30 ALA HA H 3.99 . 1 317 30 ALA CB C 18.08 . 1 318 30 ALA HB H 1.57 . 1 319 30 ALA N N 120.62 . 1 320 31 GLU H H 8.48 . 1 321 31 GLU CA C 59.38 . 1 322 31 GLU HA H 4.20 . 1 323 31 GLU CB C 30.28 . 1 324 31 GLU CG C 36.68 . 1 325 31 GLU HB2 H 2.10 . 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 118.72 . 1 330 32 GLU H H 8.35 . 1 331 32 GLU CA C 59.18 . 1 332 32 GLU HA H 4.12 . 1 333 32 GLU C C 176.90 . 1 334 32 GLU CB C 29.48 . 1 335 32 GLU CG C 36.48 . 1 336 32 GLU HB2 H 2.30 . 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 121.12 . 1 341 33 GLN H H 7.62 . 1 342 33 GLN CA C 55.98 . 1 343 33 GLN HA H 4.35 . 1 344 33 GLN C C 173.40 . 1 345 33 GLN CB C 29.38 . 1 346 33 GLN CG C 33.78 . 1 347 33 GLN HB2 H 2.05 . 2 348 33 GLN HB3 H 2.73 . 2 349 33 GLN CD C 180.48 . 1 350 33 GLN HG2 H 2.58 . 2 351 33 GLN HG3 H 2.69 . 2 352 33 GLN NE2 N 114.80 . 1 353 33 GLN HE21 H 7.48 . 2 354 33 GLN HE22 H 7.73 . 2 355 33 GLN N N 115.62 . 1 356 34 GLY H H 7.73 . 1 357 34 GLY CA C 45.38 . 1 358 34 GLY HA2 H 3.68 . 2 359 34 GLY C C 172.40 . 1 360 34 GLY HA3 H 3.96 . 2 361 34 GLY N N 106.12 . 1 362 35 TYR H H 8.27 . 1 363 35 TYR CA C 57.58 . 1 364 35 TYR HA H 4.50 . 1 365 35 TYR CB C 38.48 . 1 366 35 TYR CG C 130.88 . 1 367 35 TYR HB2 H 2.49 . 2 368 35 TYR HB3 H 2.81 . 2 369 35 TYR CD1 C 132.28 . 1 370 35 TYR CD2 C 132.28 . 1 371 35 TYR CE1 C 117.68 . 1 372 35 TYR HD1 H 6.80 . 1 373 35 TYR CE2 C 117.68 . 1 374 35 TYR HD2 H 6.80 . 1 375 35 TYR CZ C 156.38 . 1 376 35 TYR HE1 H 6.34 . 1 377 35 TYR HE2 H 6.34 . 1 378 35 TYR N N 121.82 . 1 379 36 ASP H H 8.34 . 1 380 36 ASP CA C 53.98 . 1 381 36 ASP HA H 4.84 . 1 382 36 ASP CB C 41.58 . 1 383 36 ASP CG C 180.48 . 1 384 36 ASP HB2 H 2.58 . 2 385 36 ASP HB3 H 2.73 . 2 386 36 ASP N N 121.72 . 1 387 37 LEU H H 8.22 . 1 388 37 LEU CA C 51.98 . 1 389 37 LEU HA H 4.73 . 1 390 37 LEU C C 173.20 . 1 391 37 LEU CB C 43.18 . 1 392 37 LEU CG C 27.58 . 1 393 37 LEU HB2 H 1.53 . 2 394 37 LEU HB3 H 2.01 . 2 395 37 LEU CD1 C 23.58 . 2 396 37 LEU CD2 C 25.48 . 2 397 37 LEU HG H 1.67 . 1 398 37 LEU HD1 H 0.86 . 2 399 37 LEU HD2 H 1.07 . 2 400 37 LEU N N 125.72 . 1 401 38 PRO CA C 62.78 . 1 402 38 PRO HA H 4.40 . 1 403 38 PRO C C 175.00 . 1 404 38 PRO CB C 32.28 . 1 405 38 PRO CG C 27.88 . 1 406 38 PRO CD C 49.58 . 1 407 38 PRO HD2 H 3.15 . 2 408 38 PRO HD3 H 3.20 . 2 409 38 PRO N N 133.02 . 1 410 39 PHE CG C 137.88 . 1 411 39 PHE CD1 C 133.78 . 1 412 39 PHE CD2 C 133.78 . 1 413 39 PHE CE1 C 131.98 . 1 414 39 PHE CE2 C 131.98 . 1 415 39 PHE CZ C 131.48 . 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 84.90 . 1 420 42 ARG CZ C 158.68 . 1 421 42 ARG HE H 7.13 . 1 422 42 ARG NH1 N 71.40 . 2 423 42 ARG NH2 N 73.20 . 2 424 50 ALA CA C 53.58 . 1 425 50 ALA C C 176.90 . 1 426 50 ALA CB C 19.28 . 1 427 50 ALA HB H 1.20 . 1 428 51 GLY H H 9.82 . 1 429 51 GLY CA C 43.88 . 1 430 51 GLY HA2 H 3.41 . 2 431 51 GLY C C 169.60 . 1 432 51 GLY HA3 H 4.93 . 2 433 51 GLY N N 111.82 . 1 434 52 LYS H H 9.54 . 1 435 52 LYS CA C 55.18 . 1 436 52 LYS HA H 4.81 . 1 437 52 LYS C C 173.60 . 1 438 52 LYS CB C 37.68 . 1 439 52 LYS CG C 25.48 . 1 440 52 LYS HB2 H 1.24 . 2 441 52 LYS HB3 H 1.86 . 2 442 52 LYS CD C 29.48 . 1 443 52 LYS HG2 H 0.29 . 2 444 52 LYS HG3 H 1.07 . 2 445 52 LYS CE C 42.08 . 1 446 52 LYS HD2 H 1.43 . 1 447 52 LYS HD3 H 1.43 . 1 448 52 LYS NZ N 35.00 . 1 449 52 LYS HE2 H 1.31 . 2 450 52 LYS HE3 H 2.73 . 2 451 52 LYS N N 121.82 . 1 452 53 LEU H H 9.50 . 1 453 53 LEU CA C 56.58 . 1 454 53 LEU HA H 4.14 . 1 455 53 LEU C C 175.30 . 1 456 53 LEU CB C 42.78 . 1 457 53 LEU CG C 26.98 . 1 458 53 LEU HB2 H 1.29 . 2 459 53 LEU HB3 H 1.67 . 2 460 53 LEU CD1 C 23.18 . 2 461 53 LEU CD2 C 24.28 . 2 462 53 LEU HG H 1.50 . 1 463 53 LEU HD1 H 0.67 . 2 464 53 LEU HD2 H 0.81 . 2 465 53 LEU N N 129.02 . 1 466 54 VAL H H 9.09 . 1 467 54 VAL CA C 63.78 . 1 468 54 VAL HA H 3.97 . 1 469 54 VAL C C 174.70 . 1 470 54 VAL CB C 32.98 . 1 471 54 VAL CG1 C 20.38 . 2 472 54 VAL CG2 C 21.58 . 2 473 54 VAL HB H 1.79 . 1 474 54 VAL HG1 H 0.93 . 1 475 54 VAL HG2 H 0.93 . 1 476 54 VAL N N 125.12 . 1 477 55 SER H H 7.84 . 1 478 55 SER CA C 57.88 . 1 479 55 SER HA H 4.62 . 1 480 55 SER CB C 64.78 . 1 481 55 SER HB2 H 3.78 . 2 482 55 SER HB3 H 3.88 . 2 483 55 SER N N 111.42 . 1 484 56 GLY H H 8.44 . 1 485 56 GLY CA C 43.88 . 1 486 56 GLY HA2 H 3.79 . 2 487 56 GLY C C 170.70 . 1 488 56 GLY HA3 H 4.83 . 2 489 56 GLY N N 109.22 . 1 490 57 THR H H 7.94 . 1 491 57 THR CA C 59.48 . 1 492 57 THR HA H 4.73 . 1 493 57 THR C C 171.70 . 1 494 57 THR CB C 72.28 . 1 495 57 THR CG2 C 21.28 . 1 496 57 THR HB H 4.02 . 1 497 57 THR HG2 H 1.01 . 1 498 57 THR N N 106.12 . 1 499 58 VAL H H 8.27 . 1 500 58 VAL CA C 58.08 . 1 501 58 VAL HA H 5.12 . 1 502 58 VAL C C 173.40 . 1 503 58 VAL CB C 36.08 . 1 504 58 VAL CG1 C 18.58 . 2 505 58 VAL CG2 C 22.08 . 2 506 58 VAL HB H 2.01 . 1 507 58 VAL HG1 H 0.73 . 2 508 58 VAL HG2 H 0.76 . 2 509 58 VAL N N 108.92 . 1 510 59 ASP H H 9.49 . 1 511 59 ASP CA C 53.18 . 1 512 59 ASP HA H 5.05 . 1 513 59 ASP CB C 42.68 . 1 514 59 ASP CG C 180.68 . 1 515 59 ASP HB2 H 2.49 . 2 516 59 ASP HB3 H 3.10 . 2 517 59 ASP N N 120.62 . 1 518 60 GLN H H 9.26 . 1 519 60 GLN CA C 52.68 . 1 520 60 GLN HA H 5.74 . 1 521 60 GLN CB C 27.98 . 1 522 60 GLN CG C 31.68 . 1 523 60 GLN HB2 H 1.39 . 1 524 60 GLN HB3 H 1.39 . 1 525 60 GLN CD C 177.58 . 1 526 60 GLN HG2 H 2.29 . 2 527 60 GLN HG3 H 2.48 . 2 528 60 GLN NE2 N 108.60 . 1 529 60 GLN HE21 H 6.86 . 2 530 60 GLN HE22 H 7.06 . 2 531 60 GLN N N 123.82 . 1 532 61 SER H H 8.43 . 1 533 61 SER CA C 62.48 . 1 534 61 SER HA H 4.27 . 1 535 61 SER C C 173.70 . 1 536 61 SER CB C 63.28 . 1 537 61 SER HB2 H 4.08 . 2 538 61 SER HB3 H 4.15 . 2 539 61 SER N N 117.52 . 1 540 62 ASP H H 8.83 . 1 541 62 ASP CA C 55.58 . 1 542 62 ASP HA H 4.78 . 1 543 62 ASP CB C 41.28 . 1 544 62 ASP HB2 H 2.51 . 2 545 62 ASP HB3 H 2.58 . 2 546 62 ASP N N 119.02 . 1 547 63 GLN H H 8.57 . 1 548 63 GLN CA C 55.78 . 1 549 63 GLN HA H 4.41 . 1 550 63 GLN CB C 27.48 . 1 551 63 GLN CG C 32.48 . 1 552 63 GLN HB2 H 2.08 . 2 553 63 GLN HB3 H 2.51 . 2 554 63 GLN CD C 179.08 . 1 555 63 GLN NE2 N 111.90 . 1 556 63 GLN HE21 H 6.94 . 2 557 63 GLN HE22 H 7.44 . 2 558 63 GLN N N 122.42 . 1 559 64 SER CA C 57.78 . 1 560 64 SER HA H 4.77 . 1 561 64 SER CB C 65.18 . 1 562 64 SER HB2 H 3.73 . 2 563 64 SER HB3 H 4.01 . 2 564 65 PHE CA C 60.98 . 1 565 65 PHE HA H 4.44 . 1 566 65 PHE CB C 43.88 . 1 567 65 PHE CG C 138.78 . 1 568 65 PHE CD1 C 131.88 . 1 569 65 PHE CD2 C 131.88 . 1 570 65 PHE CE1 C 130.78 . 1 571 65 PHE HD1 H 7.56 . 1 572 65 PHE CE2 C 130.78 . 1 573 65 PHE HD2 H 7.56 . 1 574 65 PHE CZ C 129.88 . 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 54.48 . 1 580 66 LEU HA H 4.33 . 1 581 66 LEU CB C 42.48 . 1 582 66 LEU HB2 H 1.36 . 2 583 66 LEU HB3 H 1.72 . 2 584 66 LEU N N 121.12 . 1 585 67 ASP H H 8.74 . 1 586 67 ASP CA C 52.28 . 1 587 67 ASP HA H 4.65 . 1 588 67 ASP CB C 41.38 . 1 589 67 ASP HB2 H 2.62 . 2 590 67 ASP HB3 H 3.12 . 2 591 67 ASP N N 122.52 . 1 592 68 ASP H H 8.40 . 1 593 68 ASP CA C 57.98 . 1 594 68 ASP HA H 4.33 . 1 595 68 ASP CB C 40.38 . 1 596 68 ASP CG C 178.78 . 1 597 68 ASP HB2 H 2.59 . 2 598 68 ASP HB3 H 2.74 . 2 599 68 ASP N N 116.72 . 1 600 69 ASP H H 8.23 . 1 601 69 ASP CA C 57.48 . 1 602 69 ASP HA H 4.45 . 1 603 69 ASP CB C 40.08 . 1 604 69 ASP HB2 H 2.67 . 2 605 69 ASP HB3 H 2.86 . 2 606 69 ASP N N 120.82 . 1 607 70 GLN H H 8.70 . 1 608 70 GLN CA C 58.88 . 1 609 70 GLN HA H 4.29 . 1 610 70 GLN CB C 28.88 . 1 611 70 GLN CG C 34.28 . 1 612 70 GLN HB2 H 1.74 . 2 613 70 GLN HB3 H 2.54 . 2 614 70 GLN CD C 178.88 . 1 615 70 GLN HG2 H 2.19 . 2 616 70 GLN HG3 H 2.76 . 2 617 70 GLN NE2 N 111.80 . 1 618 70 GLN HE21 H 7.37 . 2 619 70 GLN HE22 H 6.47 . 2 620 70 GLN N N 122.92 . 1 621 71 ILE H H 8.45 . 1 622 71 ILE CA C 64.48 . 1 623 71 ILE HA H 3.99 . 1 624 71 ILE C C 180.10 . 1 625 71 ILE CB C 37.58 . 1 626 71 ILE CG1 C 29.08 . 1 627 71 ILE CG2 C 17.08 . 1 628 71 ILE HB H 2.05 . 1 629 71 ILE CD C 12.28 . 1 630 71 ILE HG12 H 1.06 . 2 631 71 ILE HG13 H 1.69 . 2 632 71 ILE HG2 H 0.99 . 1 633 71 ILE HD1 H 0.80 . 1 634 71 ILE N N 120.82 . 1 635 72 GLU H H 8.48 . 1 636 72 GLU CA C 59.28 . 1 637 72 GLU HA H 4.08 . 1 638 72 GLU C C 176.20 . 1 639 72 GLU CB C 29.18 . 1 640 72 GLU CG C 36.28 . 1 641 72 GLU HB2 H 2.20 . 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 123.72 . 1 646 73 ALA H H 7.74 . 1 647 73 ALA CA C 52.78 . 1 648 73 ALA HA H 4.31 . 1 649 73 ALA C C 175.50 . 1 650 73 ALA CB C 19.28 . 1 651 73 ALA HB H 1.75 . 1 652 73 ALA N N 119.22 . 1 653 74 GLY H H 7.79 . 1 654 74 GLY CA C 44.88 . 1 655 74 GLY HA2 H 3.78 . 2 656 74 GLY C C 173.00 . 1 657 74 GLY HA3 H 4.33 . 2 658 74 GLY N N 103.32 . 1 659 75 TYR H H 7.96 . 1 660 75 TYR CA C 61.08 . 1 661 75 TYR HA H 5.02 . 1 662 75 TYR CB C 39.08 . 1 663 75 TYR CG C 132.28 . 1 664 75 TYR HB2 H 2.67 . 2 665 75 TYR HB3 H 2.79 . 2 666 75 TYR CD1 C 132.98 . 1 667 75 TYR CD2 C 132.98 . 1 668 75 TYR CE1 C 118.18 . 1 669 75 TYR HD1 H 7.33 . 1 670 75 TYR CE2 C 118.18 . 1 671 75 TYR HD2 H 7.33 . 1 672 75 TYR CZ C 151.78 . 1 673 75 TYR HE1 H 6.77 . 1 674 75 TYR HE2 H 6.77 . 1 675 75 TYR N N 118.82 . 1 676 76 VAL H H 8.68 . 1 677 76 VAL CA C 58.88 . 1 678 76 VAL HA H 4.83 . 1 679 76 VAL CB C 36.78 . 1 680 76 VAL CG1 C 21.68 . 2 681 76 VAL CG2 C 22.18 . 2 682 76 VAL HB H 1.57 . 1 683 76 VAL HG1 H 0.60 . 2 684 76 VAL HG2 H 0.71 . 2 685 76 VAL N N 117.82 . 1 686 78 THR CA C 61.78 . 1 687 78 THR HA H 4.43 . 1 688 78 THR CB C 69.88 . 1 689 78 THR CG2 C 21.58 . 1 690 78 THR HB H 4.17 . 1 691 78 THR HG2 H 1.18 . 1 692 80 VAL CA C 53.58 . 1 693 80 VAL HA H 4.74 . 1 694 80 VAL CB C 31.18 . 1 695 80 VAL CG1 C 23.38 . 1 696 80 VAL CG2 C 23.38 . 1 697 81 ALA H H 6.36 . 1 698 81 ALA CA C 50.18 . 1 699 81 ALA HA H 5.14 . 1 700 81 ALA C C 174.40 . 1 701 81 ALA CB C 21.88 . 1 702 81 ALA HB H 1.07 . 1 703 81 ALA N N 121.32 . 1 704 82 TYR H H 9.13 . 1 705 82 TYR CA C 54.78 . 1 706 82 TYR HA H 5.49 . 1 707 82 TYR C C 173.90 . 1 708 82 TYR CB C 39.68 . 1 709 82 TYR CG C 129.98 . 1 710 82 TYR HB2 H 2.88 . 2 711 82 TYR HB3 H 3.21 . 2 712 82 TYR CD1 C 133.68 . 1 713 82 TYR CD2 C 133.68 . 1 714 82 TYR CE1 C 117.98 . 1 715 82 TYR HD1 H 7.13 . 1 716 82 TYR CE2 C 117.98 . 1 717 82 TYR HD2 H 7.13 . 1 718 82 TYR CZ C 157.58 . 1 719 82 TYR HE1 H 6.43 . 1 720 82 TYR HE2 H 6.43 . 1 721 82 TYR N N 123.92 . 1 722 83 PRO CA C 63.58 . 1 723 83 PRO HA H 4.73 . 1 724 83 PRO C C 174.90 . 1 725 83 PRO CB C 31.08 . 1 726 83 PRO CG C 28.08 . 1 727 83 PRO HB2 H 1.99 . 2 728 83 PRO HB3 H 2.21 . 2 729 83 PRO CD C 50.48 . 1 730 83 PRO HD2 H 4.09 . 2 731 83 PRO HD3 H 4.41 . 2 732 83 PRO N N 136.52 . 1 733 84 THR H H 8.46 . 1 734 84 THR CA C 60.18 . 1 735 84 THR HA H 4.23 . 1 736 84 THR C C 170.60 . 1 737 84 THR CB C 68.38 . 1 738 84 THR CG2 C 23.18 . 1 739 84 THR HB H 4.44 . 1 740 84 THR HG2 H 1.11 . 1 741 84 THR N N 110.42 . 1 742 85 SER H H 7.73 . 1 743 85 SER CA C 57.68 . 1 744 85 SER HA H 3.57 . 1 745 85 SER C C 170.20 . 1 746 85 SER CB C 65.98 . 1 747 85 SER HB2 H 3.74 . 2 748 85 SER HB3 H 4.09 . 2 749 85 SER N N 117.52 . 1 750 86 ASP H H 8.54 . 1 751 86 ASP CA C 56.58 . 1 752 86 ASP HA H 5.33 . 1 753 86 ASP C C 178.20 . 1 754 86 ASP CB C 39.98 . 1 755 86 ASP HB2 H 2.61 . 2 756 86 ASP HB3 H 2.76 . 2 757 86 ASP N N 118.02 . 1 758 87 VAL H H 9.05 . 1 759 87 VAL CA C 60.68 . 1 760 87 VAL HA H 4.92 . 1 761 87 VAL C C 172.50 . 1 762 87 VAL CB C 37.48 . 1 763 87 VAL CG1 C 22.98 . 1 764 87 VAL CG2 C 22.98 . 1 765 87 VAL HB H 1.92 . 1 766 87 VAL HG1 H 0.89 . 2 767 87 VAL HG2 H 1.01 . 2 768 87 VAL N N 125.32 . 1 769 88 VAL H H 8.55 . 1 770 88 VAL CA C 61.88 . 1 771 88 VAL HA H 4.78 . 1 772 88 VAL C C 173.30 . 1 773 88 VAL CB C 33.28 . 1 774 88 VAL CG1 C 20.48 . 2 775 88 VAL CG2 C 21.38 . 2 776 88 VAL HB H 2.03 . 1 777 88 VAL HG1 H 0.87 . 2 778 88 VAL HG2 H 0.92 . 2 779 88 VAL N N 127.22 . 1 780 89 ILE H H 9.46 . 1 781 89 ILE CA C 59.28 . 1 782 89 ILE HA H 4.91 . 1 783 89 ILE CB C 43.28 . 1 784 89 ILE CG1 C 28.58 . 1 785 89 ILE CG2 C 16.08 . 1 786 89 ILE HB H 1.51 . 1 787 89 ILE CD C 14.48 . 1 788 89 ILE HG12 H 0.82 . 2 789 89 ILE HG13 H 1.44 . 2 790 89 ILE HG2 H 0.71 . 1 791 89 ILE HD1 H 0.49 . 1 792 89 ILE N N 127.52 . 1 793 90 GLN H H 9.21 . 1 794 90 GLN CA C 53.88 . 1 795 90 GLN HA H 5.47 . 1 796 90 GLN C C 175.20 . 1 797 90 GLN CB C 29.08 . 1 798 90 GLN CG C 33.38 . 1 799 90 GLN HB2 H 2.09 . 2 800 90 GLN HB3 H 2.30 . 2 801 90 GLN CD C 178.58 . 1 802 90 GLN HG2 H 2.18 . 2 803 90 GLN HG3 H 2.30 . 2 804 90 GLN NE2 N 110.90 . 1 805 90 GLN HE21 H 6.52 . 2 806 90 GLN HE22 H 7.25 . 2 807 90 GLN N N 126.02 . 1 808 91 THR H H 9.12 . 1 809 91 THR CA C 61.38 . 1 810 91 THR HA H 4.56 . 1 811 91 THR C C 172.60 . 1 812 91 THR CB C 68.88 . 1 813 91 THR CG2 C 22.68 . 1 814 91 THR HB H 4.67 . 1 815 91 THR HG2 H 1.18 . 1 816 91 THR N N 115.42 . 1 817 92 HIS H H 9.14 . 1 818 92 HIS CA C 58.78 . 1 819 92 HIS HA H 4.52 . 1 820 92 HIS C C 176.70 . 1 821 92 HIS CB C 26.18 . 1 822 92 HIS CG C 139.58 . 1 823 92 HIS HB2 H 3.31 . 2 824 92 HIS HB3 H 3.39 . 2 825 92 HIS ND1 N 243.10 . 1 826 92 HIS CD2 C 117.88 . 1 827 92 HIS CE1 C 138.08 . 1 828 92 HIS NE2 N 168.60 . 1 829 92 HIS HD2 H 7.18 . 1 830 92 HIS HE1 H 7.81 . 1 831 92 HIS N N 112.52 . 1 832 93 LYS H H 7.43 . 1 833 93 LYS HA H 4.74 . 1 834 93 LYS CB C 32.68 . 1 835 93 LYS CG C 24.68 . 1 836 93 LYS HB2 H 1.21 . 1 837 93 LYS HB3 H 1.21 . 1 838 93 LYS CD C 29.08 . 1 839 93 LYS HG2 H 2.36 . 1 840 93 LYS HG3 H 2.36 . 1 841 93 LYS CE C 41.88 . 1 842 93 LYS HD2 H 1.73 . 1 843 93 LYS HD3 H 1.73 . 1 844 93 LYS NZ N 33.50 . 1 845 93 LYS HE2 H 3.01 . 1 846 93 LYS HE3 H 3.01 . 1 847 93 LYS N N 114.02 . 1 848 94 GLU H H 8.33 . 1 849 94 GLU CA C 60.98 . 1 850 94 GLU HA H 3.12 . 1 851 94 GLU C C 175.70 . 1 852 94 GLU CB C 29.28 . 1 853 94 GLU CG C 35.48 . 1 854 94 GLU HB2 H 1.94 . 1 855 94 GLU HB3 H 1.94 . 1 856 94 GLU CD C 180.58 . 1 857 94 GLU HG2 H 2.13 . 1 858 94 GLU HG3 H 2.13 . 1 859 94 GLU N N 121.62 . 1 860 95 GLU H H 8.65 . 1 861 95 GLU CA C 58.38 . 1 862 95 GLU HA H 3.79 . 1 863 95 GLU C C 176.00 . 1 864 95 GLU CB C 29.08 . 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 113.42 . 1 870 96 ASP H H 7.87 . 1 871 96 ASP CA C 55.28 . 1 872 96 ASP HA H 4.39 . 1 873 96 ASP C C 175.80 . 1 874 96 ASP CB C 41.28 . 1 875 96 ASP HB2 H 2.94 . 1 876 96 ASP HB3 H 2.94 . 1 877 96 ASP N N 119.12 . 1 878 97 LEU H H 7.81 . 1 879 97 LEU CA C 54.68 . 1 880 97 LEU HA H 3.99 . 1 881 97 LEU CB C 41.18 . 1 882 97 LEU CG C 26.78 . 1 883 97 LEU HB2 H 1.33 . 2 884 97 LEU HB3 H 1.66 . 2 885 97 LEU CD1 C 21.18 . 2 886 97 LEU CD2 C 26.18 . 2 887 97 LEU HG H 1.14 . 1 888 97 LEU HD1 H 0.00 . 2 889 97 LEU HD2 H 0.60 . 2 890 97 LEU N N 117.82 . 1 891 98 TYR H H 7.07 . 1 892 98 TYR CA C 58.98 . 1 893 98 TYR HA H 4.38 . 1 894 98 TYR CB C 39.88 . 1 895 98 TYR CG C 132.28 . 1 896 98 TYR HB2 H 2.81 . 2 897 98 TYR HB3 H 3.17 . 2 898 98 TYR CD1 C 118.18 . 1 899 98 TYR CD2 C 118.18 . 1 900 98 TYR CE1 C 133.18 . 1 901 98 TYR HD1 H 7.13 . 1 902 98 TYR CE2 C 133.18 . 1 903 98 TYR HD2 H 7.13 . 1 904 98 TYR CZ C 157.08 . 1 905 98 TYR HE1 H 6.79 . 1 906 98 TYR HE2 H 6.79 . 1 907 98 TYR N N 123.92 . 1 stop_ save_