data_30 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Nuclear magnetic resonance study of the globular domain of chicken histone H5: Resonance assignment and secondary structure ; _BMRB_accession_number 30 _BMRB_flat_file_name bmr30.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 Zarbock Jutta . . 2 Clore G. Marius . 3 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 382 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-09 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 ; Zarbock, Jutta, Clore, G. Marius, Gronenborn, Angela M., "Nuclear magnetic resonance study of the globular domain of chicken histone H5: Resonance assignment and secondary structure," Proc. Natl. Acad. Sci. U.S.A. 83, 7628-7632 (1986). ; _Citation_title ; Nuclear magnetic resonance study of the globular domain of chicken histone H5: Resonance assignment and secondary structure ; _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 Zarbock Jutta . . 2 Clore G. Marius . 3 Gronenborn Angela M. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 83 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7628 _Page_last 7632 _Year 1986 _Details . save_ ################################## # Molecular system description # ################################## save_system_histone_H5 _Saveframe_category molecular_system _Mol_system_name 'histone H5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'histone H5' $histone_H5 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_histone_H5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'histone H5' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; SASHPTYSEMIAAAIRAEKS RGGSSRQSIQKYIKSHYKVG HNADLQIKLSIRRLLAAGVL KQTKGVGASGSFRLAKSDK ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ALA 3 SER 4 HIS 5 PRO 6 THR 7 TYR 8 SER 9 GLU 10 MET 11 ILE 12 ALA 13 ALA 14 ALA 15 ILE 16 ARG 17 ALA 18 GLU 19 LYS 20 SER 21 ARG 22 GLY 23 GLY 24 SER 25 SER 26 ARG 27 GLN 28 SER 29 ILE 30 GLN 31 LYS 32 TYR 33 ILE 34 LYS 35 SER 36 HIS 37 TYR 38 LYS 39 VAL 40 GLY 41 HIS 42 ASN 43 ALA 44 ASP 45 LEU 46 GLN 47 ILE 48 LYS 49 LEU 50 SER 51 ILE 52 ARG 53 ARG 54 LEU 55 LEU 56 ALA 57 ALA 58 GLY 59 VAL 60 LEU 61 LYS 62 GLN 63 THR 64 LYS 65 GLY 66 VAL 67 GLY 68 ALA 69 SER 70 GLY 71 SER 72 PHE 73 ARG 74 LEU 75 ALA 76 LYS 77 SER 78 ASP 79 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-04 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 1HST "Crystal Structure Of Globular Domain Of Histone H5 And Its Implications For Nucleosome Binding" 100.00 90 100.00 100.00 8.09e-47 PDB 4QLC "Crystal Structure Of Chromatosome At 3.5 Angstrom Resolution" 97.47 77 100.00 100.00 3.22e-45 EMBL CAA24994 "histone H5 [Gallus gallus]" 100.00 190 100.00 100.00 1.70e-48 GB AAA48798 "histone H5 [Gallus gallus]" 100.00 190 100.00 100.00 1.70e-48 REF NP_001038138 "histone H5 [Gallus gallus]" 100.00 190 100.00 100.00 1.70e-48 REF XP_003202290 "PREDICTED: histone H5 [Meleagris gallopavo]" 100.00 232 97.47 98.73 4.84e-46 REF XP_003640430 "PREDICTED: histone H5-like [Gallus gallus]" 100.00 190 100.00 100.00 1.70e-48 SP P02259 "RecName: Full=Histone H5" 100.00 190 100.00 100.00 1.70e-48 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 _Tissue _Fraction $histone_H5 chicken 9031 Eukaryota Metazoa Gallus gallus generic erythrocytes histone 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 $histone_H5 '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 3.7 . 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 DSS H . . ppm 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 'histone H5' _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 . 2 ALA H H 8.17 . 1 2 . 2 ALA HA H 4.26 . 1 3 . 2 ALA HB H 1.38 . 1 4 . 3 SER H H 8.37 . 1 5 . 3 SER HA H 4.37 . 1 6 . 3 SER HB2 H 3.81 . 1 7 . 3 SER HB3 H 3.81 . 1 8 . 4 HIS H H 7.84 . 1 9 . 4 HIS HA H 5.08 . 1 10 . 4 HIS HB2 H 3.14 . 2 11 . 4 HIS HB3 H 3.24 . 2 12 . 4 HIS HD2 H 8.62 . 1 13 . 4 HIS HE1 H 7.44 . 1 14 . 5 PRO HA H 4.75 . 1 15 . 5 PRO HB2 H 1.63 . 2 16 . 5 PRO HB3 H 2.4 . 2 17 . 5 PRO HG2 H 1.84 . 2 18 . 5 PRO HG3 H 2.01 . 2 19 . 5 PRO HD2 H 3.38 . 2 20 . 5 PRO HD3 H 3.84 . 2 21 . 6 THR H H 7.79 . 1 22 . 6 THR HA H 4.39 . 1 23 . 6 THR HB H 1.55 . 1 24 . 6 THR HG2 H 1.55 . 1 25 . 7 TYR H H 9.01 . 1 26 . 7 TYR HA H 3.9 . 1 27 . 7 TYR HB2 H 2.74 . 2 28 . 7 TYR HB3 H 3.02 . 2 29 . 7 TYR HD1 H 7.06 . 1 30 . 7 TYR HD2 H 7.06 . 1 31 . 7 TYR HE1 H 6.67 . 1 32 . 7 TYR HE2 H 6.67 . 1 33 . 8 SER H H 8.55 . 1 34 . 8 SER HA H 4.01 . 1 35 . 8 SER HB2 H 3.86 . 1 36 . 8 SER HB3 H 3.86 . 1 37 . 9 GLU H H 7.45 . 1 38 . 9 GLU HA H 4.04 . 1 39 . 9 GLU HB2 H 2.24 . 2 40 . 9 GLU HB3 H 2.41 . 2 41 . 9 GLU HG2 H 1.97 . 1 42 . 9 GLU HG3 H 1.97 . 1 43 . 10 MET H H 8.29 . 1 44 . 10 MET HA H 3.78 . 1 45 . 10 MET HB2 H 1.55 . 2 46 . 10 MET HB3 H 1.96 . 2 47 . 10 MET HG2 H 1.36 . 2 48 . 10 MET HG3 H 2.11 . 2 49 . 11 ILE H H 8.44 . 1 50 . 11 ILE HA H 3.46 . 1 51 . 11 ILE HB H 1.77 . 1 52 . 11 ILE HG2 H .72 . 1 53 . 12 ALA H H 7.62 . 1 54 . 12 ALA HA H 3.84 . 1 55 . 12 ALA HB H 1.42 . 1 56 . 13 ALA H H 7.89 . 1 57 . 13 ALA HA H 3.89 . 1 58 . 13 ALA HB H 1.61 . 1 59 . 14 ALA H H 8.72 . 1 60 . 14 ALA HA H 4.37 . 1 61 . 14 ALA HB H 1.39 . 1 62 . 15 ILE H H 7.84 . 1 63 . 15 ILE HA H 3.57 . 1 64 . 15 ILE HB H 1.71 . 1 65 . 15 ILE HG12 H .64 . 1 66 . 15 ILE HG13 H .64 . 1 67 . 15 ILE HG2 H 1.01 . 1 68 . 15 ILE HD1 H .89 . 1 69 . 16 ARG H H 8.28 . 1 70 . 16 ARG HA H 3.97 . 1 71 . 16 ARG HB2 H 1.8 . 1 72 . 16 ARG HB3 H 1.8 . 1 73 . 16 ARG HG2 H 1.57 . 1 74 . 16 ARG HG3 H 1.57 . 1 75 . 17 ALA H H 7.64 . 1 76 . 17 ALA HA H 4.08 . 1 77 . 17 ALA HB H 1.24 . 1 78 . 18 GLU H H 7.33 . 1 79 . 18 GLU HA H 4.19 . 1 80 . 18 GLU HB2 H 1.92 . 2 81 . 18 GLU HB3 H 2.48 . 2 82 . 18 GLU HG2 H 2.14 . 1 83 . 18 GLU HG3 H 2.14 . 1 84 . 19 LYS H H 7.77 . 1 85 . 19 LYS HA H 4.09 . 1 86 . 19 LYS HB2 H 1.93 . 1 87 . 19 LYS HB3 H 1.93 . 1 88 . 20 SER H H 8.29 . 1 89 . 20 SER HA H 4.45 . 1 90 . 20 SER HB2 H 3.84 . 1 91 . 20 SER HB3 H 3.84 . 1 92 . 21 ARG H H 8.61 . 1 93 . 21 ARG HA H 4.25 . 1 94 . 21 ARG HB2 H 1.85 . 2 95 . 21 ARG HB3 H 1.95 . 2 96 . 21 ARG HG2 H 1.73 . 1 97 . 21 ARG HG3 H 1.73 . 1 98 . 21 ARG HD2 H 3.24 . 1 99 . 21 ARG HD3 H 3.24 . 1 100 . 22 GLY H H 8.39 . 1 101 . 22 GLY HA2 H 3.93 . 1 102 . 22 GLY HA3 H 3.93 . 1 103 . 23 GLY H H 7.65 . 1 104 . 23 GLY HA2 H 3.88 . 2 105 . 23 GLY HA3 H 4.03 . 2 106 . 24 SER H H 8.53 . 1 107 . 24 SER HA H 4.36 . 1 108 . 24 SER HB2 H 3.98 . 1 109 . 24 SER HB3 H 3.98 . 1 110 . 25 SER H H 8.91 . 1 111 . 25 SER HA H 4.94 . 1 112 . 25 SER HB2 H 3.63 . 2 113 . 25 SER HB3 H 3.86 . 2 114 . 26 ARG H H 9.41 . 1 115 . 26 ARG HA H 3.87 . 1 116 . 26 ARG HB2 H 2.04 . 1 117 . 26 ARG HB3 H 2.04 . 1 118 . 26 ARG HG2 H 1.58 . 1 119 . 26 ARG HG3 H 1.58 . 1 120 . 26 ARG HD2 H 3.28 . 1 121 . 26 ARG HD3 H 3.28 . 1 122 . 26 ARG HE H 7.53 . 1 123 . 27 GLN H H 8.69 . 1 124 . 27 GLN HA H 4.02 . 1 125 . 27 GLN HB2 H 2.08 . 2 126 . 27 GLN HB3 H 2.17 . 2 127 . 27 GLN HG2 H 2.48 . 2 128 . 27 GLN HG3 H 2.56 . 2 129 . 28 SER H H 8.32 . 1 130 . 28 SER HA H 4.24 . 1 131 . 28 SER HB2 H 4.05 . 2 132 . 28 SER HB3 H 4.16 . 2 133 . 29 ILE H H 8.4 . 1 134 . 29 ILE HA H 3.64 . 1 135 . 29 ILE HB H 1.99 . 1 136 . 29 ILE HG2 H .93 . 1 137 . 30 GLN H H 8.58 . 1 138 . 30 GLN HA H 3.95 . 1 139 . 30 GLN HB2 H 2.16 . 1 140 . 30 GLN HB3 H 2.16 . 1 141 . 30 GLN HG2 H 2.33 . 2 142 . 30 GLN HG3 H 2.42 . 2 143 . 31 LYS H H 8.12 . 1 144 . 31 LYS HA H 4.04 . 1 145 . 31 LYS HB2 H 2.01 . 1 146 . 31 LYS HB3 H 2.01 . 1 147 . 31 LYS HG2 H 1.51 . 1 148 . 31 LYS HG3 H 1.51 . 1 149 . 31 LYS HD2 H 1.75 . 1 150 . 31 LYS HD3 H 1.75 . 1 151 . 31 LYS HE2 H 3.2 . 1 152 . 31 LYS HE3 H 3.2 . 1 153 . 32 TYR H H 8.39 . 1 154 . 32 TYR HA H 4.1 . 1 155 . 32 TYR HB2 H 3.24 . 1 156 . 32 TYR HB3 H 3.24 . 1 157 . 32 TYR HD1 H 6.93 . 1 158 . 32 TYR HD2 H 6.93 . 1 159 . 32 TYR HE1 H 6.42 . 1 160 . 32 TYR HE2 H 6.42 . 1 161 . 33 ILE H H 8.96 . 1 162 . 33 ILE HA H 3.94 . 1 163 . 33 ILE HB H 2.33 . 1 164 . 33 ILE HG12 H 1.13 . 1 165 . 33 ILE HG13 H 1.13 . 1 166 . 33 ILE HG2 H .83 . 1 167 . 34 LYS H H 8.24 . 1 168 . 34 LYS HA H 4.07 . 1 169 . 34 LYS HB2 H 1.65 . 1 170 . 34 LYS HB3 H 1.65 . 1 171 . 35 SER H H 7.56 . 1 172 . 35 SER HA H 4.44 . 1 173 . 35 SER HB2 H 3.78 . 2 174 . 35 SER HB3 H 3.84 . 2 175 . 36 HIS H H 7.65 . 1 176 . 36 HIS HA H 4.27 . 1 177 . 36 HIS HB2 H 2.12 . 2 178 . 36 HIS HB3 H 2.42 . 2 179 . 36 HIS HD2 H 8.23 . 1 180 . 36 HIS HE1 H 6.85 . 1 181 . 37 TYR H H 8.22 . 1 182 . 37 TYR HA H 4.88 . 1 183 . 37 TYR HB2 H 2.74 . 2 184 . 37 TYR HB3 H 2.96 . 2 185 . 37 TYR HD1 H 7.4 . 1 186 . 37 TYR HD2 H 7.4 . 1 187 . 37 TYR HE1 H 6.81 . 1 188 . 37 TYR HE2 H 6.81 . 1 189 . 38 LYS H H 7.97 . 1 190 . 38 LYS HA H 4.5 . 1 191 . 38 LYS HB2 H .88 . 1 192 . 38 LYS HB3 H .88 . 1 193 . 39 VAL H H 8.28 . 1 194 . 39 VAL HA H 3.94 . 1 195 . 39 VAL HB H 2.09 . 1 196 . 39 VAL HG1 H .95 . 2 197 . 39 VAL HG2 H 1.09 . 2 198 . 41 HIS H H 7.91 . 1 199 . 41 HIS HA H 5.11 . 1 200 . 41 HIS HB2 H 3.2 . 2 201 . 41 HIS HB3 H 3.34 . 2 202 . 41 HIS HD2 H 8.62 . 1 203 . 41 HIS HE1 H 7.44 . 1 204 . 42 ASN H H 8.62 . 1 205 . 42 ASN HA H 4.93 . 1 206 . 42 ASN HB2 H 2.97 . 1 207 . 42 ASN HB3 H 2.97 . 1 208 . 43 ALA H H 7.5 . 1 209 . 43 ALA HA H 4.09 . 1 210 . 43 ALA HB H 1.52 . 1 211 . 44 ASP H H 8.58 . 1 212 . 44 ASP HA H 4.15 . 1 213 . 44 ASP HB2 H 2.84 . 2 214 . 44 ASP HB3 H 2.93 . 2 215 . 45 LEU H H 7.69 . 1 216 . 45 LEU HA H 4.07 . 1 217 . 45 LEU HB2 H 1.74 . 1 218 . 45 LEU HB3 H 1.74 . 1 219 . 46 GLN H H 7.7 . 1 220 . 46 GLN HA H 3.72 . 1 221 . 46 GLN HB2 H .99 . 2 222 . 46 GLN HB3 H 1.38 . 2 223 . 46 GLN HG2 H 2.09 . 1 224 . 46 GLN HG3 H 2.09 . 1 225 . 47 ILE H H 8.74 . 1 226 . 47 ILE HA H 3.42 . 1 227 . 47 ILE HB H 1.99 . 1 228 . 47 ILE HG12 H 1.02 . 1 229 . 47 ILE HG13 H 1.02 . 1 230 . 47 ILE HG2 H .85 . 1 231 . 48 LYS H H 7.62 . 1 232 . 48 LYS HA H 3.7 . 1 233 . 48 LYS HB2 H 1.92 . 2 234 . 48 LYS HB3 H 2.03 . 2 235 . 48 LYS HG2 H 1.26 . 1 236 . 48 LYS HG3 H 1.26 . 1 237 . 48 LYS HD2 H 1.55 . 1 238 . 48 LYS HD3 H 1.55 . 1 239 . 49 LEU H H 8.24 . 1 240 . 49 LEU HA H 3.94 . 1 241 . 49 LEU HB2 H 1.46 . 2 242 . 49 LEU HB3 H 1.72 . 2 243 . 49 LEU HG H 1.64 . 1 244 . 50 SER H H 8.12 . 1 245 . 50 SER HA H 4.15 . 1 246 . 50 SER HB2 H 3.59 . 2 247 . 50 SER HB3 H 3.86 . 2 248 . 51 ILE H H 8.47 . 1 249 . 51 ILE HA H 3.24 . 1 250 . 51 ILE HB H 1.71 . 1 251 . 51 ILE HG12 H .48 . 1 252 . 51 ILE HG13 H .48 . 1 253 . 51 ILE HG2 H .23 . 1 254 . 52 ARG H H 7.38 . 1 255 . 52 ARG HA H 3.9 . 1 256 . 52 ARG HB2 H 1.99 . 1 257 . 52 ARG HB3 H 1.99 . 1 258 . 52 ARG HG2 H 1.68 . 2 259 . 52 ARG HG3 H 1.85 . 2 260 . 52 ARG HD2 H 3.21 . 1 261 . 52 ARG HD3 H 3.21 . 1 262 . 52 ARG HE H 7.24 . 1 263 . 53 ARG H H 7.85 . 1 264 . 53 ARG HA H 4.09 . 1 265 . 53 ARG HB2 H 1.95 . 2 266 . 53 ARG HB3 H 2.01 . 2 267 . 53 ARG HG2 H 1.67 . 2 268 . 53 ARG HG3 H 1.82 . 2 269 . 53 ARG HD2 H 3.23 . 1 270 . 53 ARG HD3 H 3.23 . 1 271 . 53 ARG HE H 7.31 . 1 272 . 54 LEU H H 8.82 . 1 273 . 54 LEU HA H 4.08 . 1 274 . 54 LEU HB2 H 1.91 . 1 275 . 54 LEU HB3 H 1.91 . 1 276 . 54 LEU HG H 1.28 . 1 277 . 54 LEU HD1 H .75 . 1 278 . 54 LEU HD2 H .75 . 1 279 . 55 LEU H H 8.79 . 1 280 . 55 LEU HA H 4.29 . 1 281 . 55 LEU HB2 H 1.65 . 2 282 . 55 LEU HB3 H 1.88 . 2 283 . 56 ALA H H 7.78 . 1 284 . 56 ALA HA H 4.14 . 1 285 . 56 ALA HB H 1.55 . 1 286 . 57 ALA H H 8.53 . 1 287 . 57 ALA HA H 4.78 . 1 288 . 57 ALA HB H 1.34 . 1 289 . 58 GLY H H 7.78 . 1 290 . 58 GLY HA2 H 3.86 . 2 291 . 58 GLY HA3 H 4.12 . 2 292 . 59 VAL H H 7.93 . 1 293 . 59 VAL HA H 3.83 . 1 294 . 59 VAL HB H 1.91 . 1 295 . 59 VAL HG1 H .95 . 2 296 . 59 VAL HG2 H .99 . 2 297 . 60 LEU H H 6.81 . 1 298 . 60 LEU HA H 5.22 . 1 299 . 60 LEU HB2 H 1.26 . 1 300 . 60 LEU HB3 H 1.26 . 1 301 . 60 LEU HG H 1.53 . 1 302 . 60 LEU HD1 H .67 . 1 303 . 60 LEU HD2 H .67 . 1 304 . 61 LYS H H 8.89 . 1 305 . 61 LYS HA H 4.54 . 1 306 . 61 LYS HB2 H 1.49 . 1 307 . 61 LYS HB3 H 1.49 . 1 308 . 61 LYS HG2 H 1.25 . 1 309 . 61 LYS HG3 H 1.25 . 1 310 . 62 GLN H H 8.88 . 1 311 . 62 GLN HA H 4.9 . 1 312 . 62 GLN HB2 H 2.01 . 1 313 . 62 GLN HB3 H 2.01 . 1 314 . 62 GLN HG2 H 2.14 . 1 315 . 62 GLN HG3 H 2.14 . 1 316 . 63 THR H H 8.58 . 1 317 . 63 THR HA H 4.32 . 1 318 . 63 THR HB H 4.06 . 1 319 . 63 THR HG2 H 1.04 . 1 320 . 64 LYS H H 8.2 . 1 321 . 64 LYS HA H 4.32 . 1 322 . 64 LYS HB2 H 1.73 . 2 323 . 64 LYS HB3 H 1.84 . 2 324 . 65 GLY H H 8.33 . 1 325 . 65 GLY HA2 H 4.03 . 1 326 . 65 GLY HA3 H 4.03 . 1 327 . 66 VAL H H 8.05 . 1 328 . 66 VAL HA H 4.11 . 1 329 . 66 VAL HB H 2.04 . 1 330 . 66 VAL HG1 H .91 . 1 331 . 66 VAL HG2 H .91 . 1 332 . 67 GLY H H 8.64 . 1 333 . 67 GLY HA2 H 3.84 . 2 334 . 67 GLY HA3 H 3.99 . 2 335 . 68 ALA H H 8.43 . 1 336 . 68 ALA HA H 4.31 . 1 337 . 68 ALA HB H 1.41 . 1 338 . 69 SER H H 8.07 . 1 339 . 69 SER HA H 4.52 . 1 340 . 69 SER HB2 H 3.98 . 1 341 . 69 SER HB3 H 3.98 . 1 342 . 70 GLY H H 8.07 . 1 343 . 70 GLY HA2 H 3.75 . 2 344 . 70 GLY HA3 H 4.03 . 2 345 . 71 SER H H 7.78 . 1 346 . 71 SER HA H 4.47 . 1 347 . 71 SER HB2 H 3.41 . 1 348 . 71 SER HB3 H 3.41 . 1 349 . 72 PHE H H 8.53 . 1 350 . 72 PHE HA H 5.38 . 1 351 . 72 PHE HB2 H 2.69 . 2 352 . 72 PHE HB3 H 2.91 . 2 353 . 72 PHE HD1 H 7.04 . 1 354 . 72 PHE HD2 H 7.04 . 1 355 . 72 PHE HE1 H 7.18 . 1 356 . 72 PHE HE2 H 7.18 . 1 357 . 72 PHE HZ H 7.26 . 1 358 . 73 ARG H H 8.83 . 1 359 . 73 ARG HA H 4.54 . 1 360 . 73 ARG HB2 H 1.85 . 1 361 . 73 ARG HB3 H 1.85 . 1 362 . 73 ARG HG2 H 1.49 . 1 363 . 73 ARG HG3 H 1.49 . 1 364 . 74 LEU H H 8.64 . 1 365 . 74 LEU HA H 4.61 . 1 366 . 74 LEU HB2 H 1.59 . 2 367 . 74 LEU HB3 H 1.67 . 2 368 . 75 ALA H H 7.25 . 1 369 . 75 ALA HA H 4.13 . 1 370 . 75 ALA HB H 1.3 . 1 371 . 76 LYS H H 8.34 . 1 372 . 76 LYS HA H 4.31 . 1 373 . 76 LYS HB2 H 1.76 . 1 374 . 76 LYS HB3 H 1.76 . 1 375 . 77 SER H H 7.24 . 1 376 . 77 SER HA H 4.4 . 1 377 . 77 SER HB2 H 3.81 . 2 378 . 77 SER HB3 H 3.87 . 2 379 . 78 ASP H H 8.43 . 1 380 . 78 ASP HA H 4.67 . 1 381 . 78 ASP HB2 H 2.77 . 2 382 . 78 ASP HB3 H 2.86 . 2 stop_ save_