data_4126 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure and Dynamics of a De Novo Designed Three-helix Bundle Protein ; _BMRB_accession_number 4126 _BMRB_flat_file_name bmr4126.str _Entry_type update _Submission_date 1998-03-19 _Accession_date 1998-03-19 _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 Walsh Scott T.R. . 2 Cheng Hong . . 3 Bryson James W. . 4 Roder Heinrich . . 5 DeGrado William F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 417 "13C chemical shifts" 312 "15N chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-06 original author original 2001-02-27 update author 'new chemical shifts added' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Walsh, S.T.R., Cheng, H., Bryson, J.W., Roder, H., and DeGrado, W.F., "Solution Structure and Dynamics of a De Novo Designed Three-helix Bundle Protein," Proc. Natl. Acad. Sci. USA 96, 5486-5491 (1999). ; _Citation_title 'Solution Structure and Dynamics of a De Novo Designed Three-helix Bundle Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99254067 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Walsh Scott T.R. . 2 Cheng Hong . . 3 Bryson James W. . 4 Roder Heinrich . . 5 DeGrado William F. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 96 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5486 _Page_last 5491 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_a3D _Saveframe_category molecular_system _Mol_system_name 'single chain three helix bundle' _Abbreviation_common a3D _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'three helix bundle' $a3D stop_ _System_molecular_weight 7977 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_a3D _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common a3D _Abbreviation_common a3D _Molecular_mass 7977 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; MGSWAEFKQRLAAIKTRLQA LGGSEAELAAFEKEIAAFES ELQAYKGKGNPEVEALRKEA AAIRDELQAYRHN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 TRP 5 ALA 6 GLU 7 PHE 8 LYS 9 GLN 10 ARG 11 LEU 12 ALA 13 ALA 14 ILE 15 LYS 16 THR 17 ARG 18 LEU 19 GLN 20 ALA 21 LEU 22 GLY 23 GLY 24 SER 25 GLU 26 ALA 27 GLU 28 LEU 29 ALA 30 ALA 31 PHE 32 GLU 33 LYS 34 GLU 35 ILE 36 ALA 37 ALA 38 PHE 39 GLU 40 SER 41 GLU 42 LEU 43 GLN 44 ALA 45 TYR 46 LYS 47 GLY 48 LYS 49 GLY 50 ASN 51 PRO 52 GLU 53 VAL 54 GLU 55 ALA 56 LEU 57 ARG 58 LYS 59 GLU 60 ALA 61 ALA 62 ALA 63 ILE 64 ARG 65 ASP 66 GLU 67 LEU 68 GLN 69 ALA 70 TYR 71 ARG 72 HIS 73 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 2A3D "Solution Structure Of A De Novo Designed Single Chain Three- Helix Bundle (A3d)" 100.00 73 100.00 100.00 2.13e-42 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $a3D . . . . . . 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 _Details $a3D 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET-16b ; a3D was cloned into pET-16b using the Nco-I and HindIII restriction sites. The protein was produced in E. coli strain BL21(DE3). ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $a3D 3 mM '[U-15N; U-13C]' 'deuterated acetate' 50 mM . 'sodium azide' 0.05 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'three helix bundle' _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 . 3 SER CA C 55.200 0.15 1 2 . 3 SER C C 172.500 0.15 1 3 . 3 SER CB C 62.200 0.15 1 4 . 3 SER HA H 4.470 0.02 1 5 . 3 SER HB2 H 3.960 0.02 2 6 . 3 SER HG H 3.820 0.02 1 7 . 4 TRP N N 122.500 0.15 1 8 . 4 TRP CA C 57.000 0.15 1 9 . 4 TRP C C 175.100 0.15 1 10 . 4 TRP CB C 26.600 0.15 1 11 . 4 TRP CD1 C 127.220 0.15 1 12 . 4 TRP NE1 N 128.100 0.15 1 13 . 4 TRP CE3 C 137.600 0.15 1 14 . 4 TRP CZ2 C 114.320 0.15 1 15 . 4 TRP CZ3 C 138.390 0.15 1 16 . 4 TRP H H 8.500 0.02 1 17 . 4 TRP HA H 4.550 0.02 1 18 . 4 TRP HB2 H 3.250 0.02 2 19 . 4 TRP HD1 H 7.230 0.02 1 20 . 4 TRP HE1 H 10.050 0.02 3 21 . 4 TRP HE3 H 7.240 0.02 3 22 . 4 TRP HZ2 H 7.250 0.02 3 23 . 4 TRP HZ3 H 6.520 0.02 3 24 . 4 TRP HH2 H 6.840 0.02 1 25 . 5 ALA N N 120.700 0.15 1 26 . 5 ALA CA C 53.000 0.15 1 27 . 5 ALA C C 178.600 0.15 1 28 . 5 ALA CB C 15.700 0.15 1 29 . 5 ALA H H 8.270 0.02 1 30 . 5 ALA HA H 3.890 0.02 1 31 . 5 ALA HB H 1.350 0.02 1 32 . 6 GLU N N 118.000 0.15 1 33 . 6 GLU CA C 57.000 0.15 1 34 . 6 GLU C C 177.300 0.15 1 35 . 6 GLU CB C 26.900 0.15 1 36 . 6 GLU CG C 34.500 0.15 1 37 . 6 GLU H H 7.850 0.02 1 38 . 6 GLU HA H 4.000 0.02 1 39 . 6 GLU HB2 H 2.080 0.02 2 40 . 6 GLU HB3 H 2.030 0.02 2 41 . 6 GLU HG2 H 2.200 0.02 2 42 . 6 GLU HG3 H 2.150 0.02 2 43 . 7 PHE N N 119.600 0.15 1 44 . 7 PHE CA C 58.600 0.15 1 45 . 7 PHE C C 175.800 0.15 1 46 . 7 PHE CB C 36.700 0.15 1 47 . 7 PHE CD1 C 130.960 0.15 1 48 . 7 PHE CD2 C 130.960 0.15 1 49 . 7 PHE CE1 C 131.040 0.15 1 50 . 7 PHE CE2 C 131.040 0.15 1 51 . 7 PHE CZ C 129.620 0.15 1 52 . 7 PHE H H 7.960 0.02 1 53 . 7 PHE HA H 4.300 0.02 1 54 . 7 PHE HB2 H 3.160 0.02 2 55 . 7 PHE HB3 H 3.060 0.02 2 56 . 7 PHE HD1 H 7.030 0.02 1 57 . 7 PHE HD2 H 7.030 0.02 1 58 . 7 PHE HE1 H 6.990 0.02 1 59 . 7 PHE HE2 H 6.990 0.02 1 60 . 7 PHE HZ H 7.110 0.02 1 61 . 8 LYS N N 118.600 0.15 1 62 . 8 LYS CA C 58.000 0.15 1 63 . 8 LYS C C 177.400 0.15 1 64 . 8 LYS CB C 29.800 0.15 1 65 . 8 LYS CG C 22.900 0.15 1 66 . 8 LYS CD C 27.000 0.15 1 67 . 8 LYS CE C 39.600 0.15 1 68 . 8 LYS H H 8.250 0.02 1 69 . 8 LYS HA H 3.790 0.02 1 70 . 8 LYS HB2 H 1.820 0.02 2 71 . 8 LYS HB3 H 1.790 0.02 2 72 . 8 LYS HG2 H 1.350 0.02 2 73 . 8 LYS HG3 H 1.290 0.02 2 74 . 8 LYS HD2 H 1.610 0.02 1 75 . 8 LYS HD3 H 1.610 0.02 1 76 . 8 LYS HE2 H 2.890 0.02 1 77 . 8 LYS HE3 H 2.890 0.02 1 78 . 9 GLN N N 119.000 0.15 1 79 . 9 GLN CA C 56.300 0.15 1 80 . 9 GLN C C 176.600 0.15 1 81 . 9 GLN CB C 26.000 0.15 1 82 . 9 GLN CG C 31.500 0.15 1 83 . 9 GLN NE2 N 110.900 0.15 1 84 . 9 GLN H H 7.860 0.02 1 85 . 9 GLN HA H 4.050 0.02 1 86 . 9 GLN HB2 H 2.140 0.02 2 87 . 9 GLN HG2 H 2.430 0.02 2 88 . 9 GLN HG3 H 2.360 0.02 2 89 . 9 GLN HE21 H 7.350 0.02 2 90 . 9 GLN HE22 H 6.770 0.02 2 91 . 10 ARG N N 121.100 0.15 1 92 . 10 ARG CA C 55.100 0.15 1 93 . 10 ARG C C 175.800 0.15 1 94 . 10 ARG CB C 28.100 0.15 1 95 . 10 ARG CG C 24.500 0.15 1 96 . 10 ARG CD C 41.800 0.15 1 97 . 10 ARG H H 8.120 0.02 1 98 . 10 ARG HA H 4.060 0.02 1 99 . 10 ARG HB2 H 2.000 0.02 2 100 . 10 ARG HG2 H 2.210 0.02 2 101 . 10 ARG HG3 H 2.110 0.02 2 102 . 10 ARG HD2 H 3.230 0.02 2 103 . 10 ARG HD3 H 3.060 0.02 2 104 . 11 LEU N N 119.500 0.15 1 105 . 11 LEU CA C 55.100 0.15 1 106 . 11 LEU C C 175.800 0.15 1 107 . 11 LEU CB C 38.500 0.15 1 108 . 11 LEU CG C 24.500 0.15 1 109 . 11 LEU CD1 C 21.300 0.15 2 110 . 11 LEU CD2 C 23.100 0.15 2 111 . 11 LEU H H 8.030 0.02 1 112 . 11 LEU HA H 3.700 0.02 1 113 . 11 LEU HB2 H 1.620 0.02 2 114 . 11 LEU HB3 H 1.450 0.02 2 115 . 11 LEU HG H 1.450 0.02 1 116 . 11 LEU HD1 H 0.560 0.02 4 117 . 11 LEU HD2 H 0.710 0.02 2 118 . 12 ALA N N 120.700 0.15 1 119 . 12 ALA CA C 52.800 0.15 1 120 . 12 ALA C C 178.000 0.15 1 121 . 12 ALA CB C 15.600 0.15 1 122 . 12 ALA H H 7.720 0.02 1 123 . 12 ALA HA H 3.980 0.02 1 124 . 12 ALA HB H 1.460 0.02 1 125 . 13 ALA N N 120.700 0.15 1 126 . 13 ALA CA C 52.700 0.15 1 127 . 13 ALA C C 178.400 0.15 1 128 . 13 ALA CB C 15.500 0.15 1 129 . 13 ALA H H 7.760 0.02 1 130 . 13 ALA HA H 4.190 0.02 1 131 . 13 ALA HB H 1.510 0.02 1 132 . 14 ILE N N 120.600 0.15 1 133 . 14 ILE CA C 63.700 0.15 1 134 . 14 ILE C C 175.000 0.15 1 135 . 14 ILE CB C 35.900 0.15 1 136 . 14 ILE CG1 C 27.600 0.15 2 137 . 14 ILE CG2 C 15.200 0.15 1 138 . 14 ILE CD1 C 11.000 0.15 1 139 . 14 ILE H H 7.840 0.02 1 140 . 14 ILE HA H 3.580 0.02 1 141 . 14 ILE HB H 1.880 0.02 1 142 . 14 ILE HG12 H 1.760 0.02 1 143 . 14 ILE HG13 H 0.810 0.02 1 144 . 14 ILE HG2 H 0.730 0.02 4 145 . 14 ILE HD1 H 0.510 0.02 1 146 . 15 LYS N N 119.300 0.15 1 147 . 15 LYS CA C 58.200 0.15 1 148 . 15 LYS C C 177.200 0.15 1 149 . 15 LYS CB C 30.000 0.15 1 150 . 15 LYS CG C 23.600 0.15 1 151 . 15 LYS CD C 27.200 0.15 1 152 . 15 LYS CE C 39.500 0.15 1 153 . 15 LYS H H 8.220 0.02 1 154 . 15 LYS HA H 3.770 0.02 1 155 . 15 LYS HB2 H 1.920 0.02 2 156 . 15 LYS HB3 H 1.800 0.02 2 157 . 15 LYS HG2 H 1.490 0.02 2 158 . 15 LYS HG3 H 1.360 0.02 2 159 . 15 LYS HD2 H 1.610 0.02 1 160 . 15 LYS HD3 H 1.610 0.02 1 161 . 15 LYS HE2 H 2.850 0.02 2 162 . 15 LYS HE3 H 2.840 0.02 2 163 . 16 THR N N 114.800 0.15 1 164 . 16 THR CA C 64.200 0.15 1 165 . 16 THR C C 174.400 0.15 1 166 . 16 THR CB C 66.400 0.15 1 167 . 16 THR CG2 C 19.400 0.15 1 168 . 16 THR H H 8.080 0.02 1 169 . 16 THR HA H 3.920 0.02 1 170 . 16 THR HB H 4.200 0.02 1 171 . 16 THR HG2 H 1.200 0.02 1 172 . 17 ARG N N 122.400 0.15 1 173 . 17 ARG CA C 56.800 0.15 1 174 . 17 ARG C C 176.500 0.15 1 175 . 17 ARG CB C 27.800 0.15 1 176 . 17 ARG CG C 25.700 0.15 1 177 . 17 ARG CD C 41.100 0.15 1 178 . 17 ARG H H 7.790 0.02 1 179 . 17 ARG HA H 4.020 0.02 1 180 . 17 ARG HB2 H 1.990 0.02 1 181 . 17 ARG HB3 H 1.990 0.02 1 182 . 17 ARG HG2 H 1.740 0.02 2 183 . 17 ARG HG3 H 1.630 0.02 2 184 . 17 ARG HD2 H 3.190 0.02 2 185 . 17 ARG HD3 H 3.120 0.02 2 186 . 18 LEU N N 120.000 0.15 1 187 . 18 LEU CA C 55.200 0.15 1 188 . 18 LEU C C 176.000 0.15 1 189 . 18 LEU CB C 39.400 0.15 1 190 . 18 LEU CG C 24.300 0.15 1 191 . 18 LEU CD1 C 22.300 0.15 2 192 . 18 LEU CD2 C 23.100 0.15 2 193 . 18 LEU H H 8.100 0.02 1 194 . 18 LEU HA H 3.560 0.02 1 195 . 18 LEU HB2 H 1.700 0.02 2 196 . 18 LEU HB3 H 1.530 0.02 2 197 . 18 LEU HG H 1.470 0.02 1 198 . 18 LEU HD1 H 0.580 0.02 4 199 . 18 LEU HD2 H 0.580 0.02 4 200 . 19 GLN N N 114.500 0.15 1 201 . 19 GLN CA C 55.200 0.15 1 202 . 19 GLN C C 173.700 0.15 1 203 . 19 GLN CB C 26.100 0.15 1 204 . 19 GLN CG C 31.700 0.15 1 205 . 19 GLN NE2 N 111.900 0.15 1 206 . 19 GLN H H 7.370 0.02 1 207 . 19 GLN HA H 4.030 0.02 1 208 . 19 GLN HB2 H 2.140 0.02 2 209 . 19 GLN HG2 H 2.520 0.02 2 210 . 19 GLN HG3 H 2.430 0.02 2 211 . 19 GLN HE21 H 7.510 0.02 2 212 . 19 GLN HE22 H 6.910 0.02 2 213 . 20 ALA N N 120.000 0.15 1 214 . 20 ALA CA C 49.300 0.15 1 215 . 20 ALA C C 174.900 0.15 1 216 . 20 ALA CB C 17.200 0.15 1 217 . 20 ALA H H 7.380 0.02 1 218 . 20 ALA HA H 4.470 0.02 1 219 . 20 ALA HB H 1.390 0.02 1 220 . 21 LEU N N 120.200 0.15 1 221 . 21 LEU CA C 53.700 0.15 1 222 . 21 LEU C C 175.500 0.15 1 223 . 21 LEU CB C 40.500 0.15 1 224 . 21 LEU CG C 23.900 0.15 1 225 . 21 LEU CD1 C 22.800 0.15 1 226 . 21 LEU CD2 C 21.800 0.15 1 227 . 21 LEU H H 7.320 0.02 1 228 . 21 LEU HA H 4.090 0.02 1 229 . 21 LEU HB2 H 1.530 0.02 2 230 . 21 LEU HB3 H 1.420 0.02 2 231 . 21 LEU HG H 1.600 0.02 1 232 . 21 LEU HD1 H 0.580 0.02 4 233 . 21 LEU HD2 H 0.520 0.02 4 234 . 22 GLY N N 111.100 0.15 1 235 . 22 GLY CA C 43.200 0.15 1 236 . 22 GLY C C 171.800 0.15 1 237 . 22 GLY H H 8.730 0.02 1 238 . 22 GLY HA2 H 4.050 0.02 2 239 . 22 GLY HA3 H 3.910 0.02 2 240 . 23 GLY N N 105.500 0.15 1 241 . 23 GLY CA C 43.200 0.15 1 242 . 23 GLY C C 171.100 0.15 1 243 . 23 GLY H H 7.830 0.02 1 244 . 23 GLY HA2 H 3.950 0.02 2 245 . 23 GLY HA3 H 3.790 0.02 2 246 . 24 SER N N 115.900 0.15 1 247 . 24 SER CA C 55.500 0.15 1 248 . 24 SER C C 172.300 0.15 1 249 . 24 SER CB C 62.200 0.15 1 250 . 24 SER H H 8.130 0.02 1 251 . 24 SER HA H 4.550 0.02 1 252 . 24 SER HB2 H 4.190 0.02 2 253 . 24 SER HG H 4.000 0.02 1 254 . 25 GLU N N 124.200 0.15 1 255 . 25 GLU CA C 57.500 0.15 1 256 . 25 GLU C C 176.600 0.15 1 257 . 25 GLU CB C 26.900 0.15 1 258 . 25 GLU CG C 33.900 0.15 1 259 . 25 GLU H H 9.000 0.02 1 260 . 25 GLU HA H 4.000 0.02 1 261 . 25 GLU HB2 H 2.060 0.02 2 262 . 25 GLU HB3 H 2.050 0.02 2 263 . 25 GLU HG2 H 2.340 0.02 1 264 . 25 GLU HG3 H 2.340 0.02 1 265 . 26 ALA N N 120.500 0.15 1 266 . 26 ALA CA C 52.700 0.15 1 267 . 26 ALA C C 179.100 0.15 1 268 . 26 ALA CB C 16.000 0.15 1 269 . 26 ALA H H 8.480 0.02 1 270 . 26 ALA HA H 4.140 0.02 1 271 . 26 ALA HB H 1.380 0.02 1 272 . 27 GLU N N 118.600 0.15 1 273 . 27 GLU CA C 56.400 0.15 1 274 . 27 GLU C C 176.700 0.15 1 275 . 27 GLU CB C 28.000 0.15 1 276 . 27 GLU CG C 34.800 0.15 1 277 . 27 GLU H H 7.680 0.02 1 278 . 27 GLU HA H 4.010 0.02 1 279 . 27 GLU HB2 H 2.060 0.02 2 280 . 27 GLU HB3 H 1.960 0.02 2 281 . 27 GLU HG2 H 2.200 0.02 1 282 . 27 GLU HG3 H 2.200 0.02 1 283 . 28 LEU N N 120.400 0.15 1 284 . 28 LEU CA C 56.200 0.15 1 285 . 28 LEU C C 176.700 0.15 1 286 . 28 LEU CB C 39.000 0.15 1 287 . 28 LEU CG C 24.700 0.15 1 288 . 28 LEU CD1 C 23.200 0.15 1 289 . 28 LEU CD2 C 21.700 0.15 1 290 . 28 LEU H H 8.010 0.02 1 291 . 28 LEU HA H 4.010 0.02 1 292 . 28 LEU HB2 H 1.810 0.02 2 293 . 28 LEU HB3 H 1.530 0.02 2 294 . 28 LEU HG H 1.680 0.02 1 295 . 28 LEU HD1 H 0.790 0.02 4 296 . 28 LEU HD2 H 0.720 0.02 4 297 . 29 ALA N N 120.500 0.15 1 298 . 29 ALA CA C 52.600 0.15 1 299 . 29 ALA C C 179.000 0.15 1 300 . 29 ALA CB C 15.600 0.15 1 301 . 29 ALA H H 8.270 0.02 1 302 . 29 ALA HA H 4.180 0.02 1 303 . 29 ALA HB H 1.470 0.02 1 304 . 30 ALA N N 120.400 0.15 1 305 . 30 ALA CA C 52.700 0.15 1 306 . 30 ALA C C 179.000 0.15 1 307 . 30 ALA CB C 15.600 0.15 1 308 . 30 ALA H H 7.660 0.02 1 309 . 30 ALA HA H 4.120 0.02 1 310 . 30 ALA HB H 1.460 0.02 1 311 . 31 PHE N N 119.900 0.15 1 312 . 31 PHE CA C 58.500 0.15 1 313 . 31 PHE C C 175.600 0.15 1 314 . 31 PHE CB C 37.000 0.15 1 315 . 31 PHE CD1 C 131.250 0.15 1 316 . 31 PHE CD2 C 131.250 0.15 1 317 . 31 PHE CE1 C 130.930 0.15 1 318 . 31 PHE CE2 C 130.930 0.15 1 319 . 31 PHE CZ C 129.740 0.15 1 320 . 31 PHE H H 8.170 0.02 1 321 . 31 PHE HA H 4.380 0.02 1 322 . 31 PHE HB2 H 3.240 0.02 2 323 . 31 PHE HB3 H 3.050 0.02 2 324 . 31 PHE HD1 H 7.020 0.02 1 325 . 31 PHE HD2 H 7.020 0.02 1 326 . 31 PHE HE1 H 7.220 0.02 1 327 . 31 PHE HE2 H 7.220 0.02 1 328 . 31 PHE HZ H 7.200 0.02 1 329 . 32 GLU N N 119.200 0.15 1 330 . 32 GLU CA C 58.000 0.15 1 331 . 32 GLU C C 176.600 0.15 1 332 . 32 GLU CB C 26.900 0.15 1 333 . 32 GLU CG C 34.500 0.15 1 334 . 32 GLU H H 8.570 0.02 1 335 . 32 GLU HA H 3.740 0.02 1 336 . 32 GLU HB2 H 2.220 0.02 1 337 . 32 GLU HB3 H 2.220 0.02 1 338 . 32 GLU HG2 H 2.400 0.02 1 339 . 32 GLU HG3 H 2.400 0.02 1 340 . 33 LYS N N 117.700 0.15 1 341 . 33 LYS CA C 57.100 0.15 1 342 . 33 LYS C C 177.300 0.15 1 343 . 33 LYS CB C 30.000 0.15 1 344 . 33 LYS CG C 22.900 0.15 1 345 . 33 LYS CD C 27.000 0.15 1 346 . 33 LYS CE C 39.900 0.15 1 347 . 33 LYS H H 7.610 0.02 1 348 . 33 LYS HA H 4.030 0.02 1 349 . 33 LYS HB2 H 1.920 0.02 1 350 . 33 LYS HB3 H 1.920 0.02 1 351 . 33 LYS HG2 H 1.620 0.02 2 352 . 33 LYS HG3 H 1.430 0.02 2 353 . 33 LYS HD2 H 1.670 0.02 1 354 . 33 LYS HD3 H 1.670 0.02 1 355 . 33 LYS HE2 H 2.940 0.02 1 356 . 33 LYS HE3 H 2.940 0.02 1 357 . 34 GLU N N 120.800 0.15 1 358 . 34 GLU CA C 57.300 0.15 1 359 . 34 GLU C C 177.800 0.15 1 360 . 34 GLU CB C 27.300 0.15 1 361 . 34 GLU CG C 33.900 0.15 1 362 . 34 GLU H H 7.780 0.02 1 363 . 34 GLU HA H 4.110 0.02 1 364 . 34 GLU HB2 H 2.100 0.02 1 365 . 34 GLU HB3 H 2.100 0.02 1 366 . 34 GLU HG2 H 2.310 0.02 1 367 . 34 GLU HG3 H 2.310 0.02 1 368 . 35 ILE N N 119.700 0.15 1 369 . 35 ILE CA C 61.500 0.15 1 370 . 35 ILE C C 174.800 0.15 1 371 . 35 ILE CB C 35.300 0.15 1 372 . 35 ILE CG1 C 26.800 0.15 2 373 . 35 ILE CG2 C 16.100 0.15 1 374 . 35 ILE CD1 C 11.500 0.15 1 375 . 35 ILE H H 8.250 0.02 1 376 . 35 ILE HA H 3.810 0.02 1 377 . 35 ILE HB H 1.730 0.02 1 378 . 35 ILE HG12 H 1.460 0.02 1 379 . 35 ILE HG13 H 1.460 0.02 1 380 . 35 ILE HG2 H 0.910 0.02 1 381 . 35 ILE HD1 H 0.680 0.02 1 382 . 36 ALA N N 123.400 0.15 1 383 . 36 ALA CA C 52.700 0.15 1 384 . 36 ALA C C 179.100 0.15 1 385 . 36 ALA CB C 15.600 0.15 1 386 . 36 ALA H H 8.240 0.02 1 387 . 36 ALA HA H 4.310 0.02 1 388 . 36 ALA HB H 1.470 0.02 1 389 . 37 ALA N N 121.100 0.15 1 390 . 37 ALA CA C 52.700 0.15 1 391 . 37 ALA C C 178.200 0.15 1 392 . 37 ALA CB C 15.600 0.15 1 393 . 37 ALA H H 7.960 0.02 1 394 . 37 ALA HA H 4.170 0.02 1 395 . 37 ALA HB H 1.520 0.02 1 396 . 38 PHE N N 120.400 0.15 1 397 . 38 PHE CA C 58.900 0.15 1 398 . 38 PHE C C 174.800 0.15 1 399 . 38 PHE CB C 36.600 0.15 1 400 . 38 PHE CD1 C 131.400 0.15 1 401 . 38 PHE CD2 C 131.400 0.15 1 402 . 38 PHE CE1 C 131.580 0.15 1 403 . 38 PHE CE2 C 131.580 0.15 1 404 . 38 PHE CZ C 129.480 0.15 1 405 . 38 PHE H H 7.850 0.02 1 406 . 38 PHE HA H 4.190 0.02 1 407 . 38 PHE HB2 H 3.290 0.02 2 408 . 38 PHE HB3 H 3.130 0.02 2 409 . 38 PHE HD1 H 7.190 0.02 1 410 . 38 PHE HD2 H 7.190 0.02 1 411 . 38 PHE HE1 H 7.210 0.02 1 412 . 38 PHE HE2 H 7.210 0.02 1 413 . 38 PHE HZ H 7.170 0.02 1 414 . 39 GLU N N 117.800 0.15 1 415 . 39 GLU CA C 58.200 0.15 1 416 . 39 GLU C C 177.500 0.15 1 417 . 39 GLU CB C 27.700 0.15 1 418 . 39 GLU CG C 35.300 0.15 1 419 . 39 GLU H H 8.800 0.02 1 420 . 39 GLU HA H 3.680 0.02 1 421 . 39 GLU HB2 H 2.100 0.02 1 422 . 39 GLU HB3 H 2.100 0.02 1 423 . 39 GLU HG2 H 2.550 0.02 2 424 . 39 GLU HG3 H 2.540 0.02 2 425 . 40 SER N N 114.400 0.15 1 426 . 40 SER CA C 59.500 0.15 1 427 . 40 SER C C 174.900 0.15 1 428 . 40 SER CB C 60.400 0.15 1 429 . 40 SER H H 8.190 0.02 1 430 . 40 SER HA H 4.190 0.02 1 431 . 40 SER HB2 H 4.000 0.02 2 432 . 40 SER HG H 4.000 0.02 1 433 . 41 GLU N N 122.600 0.15 1 434 . 41 GLU CA C 57.200 0.15 1 435 . 41 GLU C C 177.300 0.15 1 436 . 41 GLU CB C 27.300 0.15 1 437 . 41 GLU CG C 34.400 0.15 1 438 . 41 GLU H H 7.860 0.02 1 439 . 41 GLU HA H 4.090 0.02 1 440 . 41 GLU HB2 H 2.240 0.02 2 441 . 41 GLU HB3 H 2.180 0.02 2 442 . 41 GLU HG2 H 2.520 0.02 2 443 . 41 GLU HG3 H 2.260 0.02 2 444 . 42 LEU N N 118.500 0.15 1 445 . 42 LEU CA C 54.800 0.15 1 446 . 42 LEU C C 177.200 0.15 1 447 . 42 LEU CB C 39.300 0.15 1 448 . 42 LEU CG C 23.900 0.15 1 449 . 42 LEU CD1 C 23.000 0.15 1 450 . 42 LEU CD2 C 21.300 0.15 1 451 . 42 LEU H H 7.910 0.02 1 452 . 42 LEU HA H 3.850 0.02 1 453 . 42 LEU HB2 H 1.510 0.02 2 454 . 42 LEU HB3 H 1.310 0.02 2 455 . 42 LEU HG H 1.310 0.02 1 456 . 42 LEU HD1 H 0.460 0.02 4 457 . 42 LEU HD2 H 0.310 0.02 4 458 . 43 GLN N N 117.700 0.15 1 459 . 43 GLN CA C 55.900 0.15 1 460 . 43 GLN C C 174.600 0.15 1 461 . 43 GLN CB C 26.100 0.15 1 462 . 43 GLN CG C 31.500 0.15 1 463 . 43 GLN NE2 N 111.400 0.15 1 464 . 43 GLN H H 7.870 0.02 1 465 . 43 GLN HA H 3.980 0.02 1 466 . 43 GLN HB2 H 2.140 0.02 2 467 . 43 GLN HB3 H 2.130 0.02 2 468 . 43 GLN HG2 H 2.460 0.02 1 469 . 43 GLN HG3 H 2.460 0.02 1 470 . 43 GLN HE21 H 7.460 0.02 2 471 . 43 GLN HE22 H 6.830 0.02 2 472 . 44 ALA N N 119.300 0.15 1 473 . 44 ALA CA C 50.800 0.15 1 474 . 44 ALA C C 175.400 0.15 1 475 . 44 ALA CB C 16.400 0.15 1 476 . 44 ALA H H 7.390 0.02 1 477 . 44 ALA HA H 4.160 0.02 1 478 . 44 ALA HB H 1.360 0.02 1 479 . 45 TYR N N 118.000 0.15 1 480 . 45 TYR CA C 56.400 0.15 1 481 . 45 TYR C C 173.200 0.15 1 482 . 45 TYR CB C 36.400 0.15 1 483 . 45 TYR CD1 C 133.430 0.15 1 484 . 45 TYR CD2 C 133.430 0.15 1 485 . 45 TYR CE1 C 118.310 0.15 1 486 . 45 TYR CE2 C 118.310 0.15 1 487 . 45 TYR H H 7.450 0.02 1 488 . 45 TYR HA H 4.390 0.02 1 489 . 45 TYR HB2 H 3.110 0.02 2 490 . 45 TYR HB3 H 3.020 0.02 2 491 . 45 TYR HD1 H 7.220 0.02 1 492 . 45 TYR HD2 H 7.220 0.02 1 493 . 45 TYR HE1 H 6.830 0.02 1 494 . 45 TYR HE2 H 6.830 0.02 1 495 . 46 LYS N N 123.900 0.15 1 496 . 46 LYS CA C 54.300 0.15 1 497 . 46 LYS C C 174.400 0.15 1 498 . 46 LYS CB C 30.400 0.15 1 499 . 46 LYS CG C 22.200 0.15 1 500 . 46 LYS CD C 26.600 0.15 1 501 . 46 LYS CE C 39.500 0.15 1 502 . 46 LYS H H 7.930 0.02 1 503 . 46 LYS HA H 4.190 0.02 1 504 . 46 LYS HB2 H 1.790 0.02 2 505 . 46 LYS HB3 H 1.690 0.02 2 506 . 46 LYS HG2 H 1.380 0.02 2 507 . 46 LYS HG3 H 1.340 0.02 2 508 . 46 LYS HD2 H 1.610 0.02 1 509 . 46 LYS HD3 H 1.610 0.02 1 510 . 46 LYS HE2 H 2.910 0.02 1 511 . 46 LYS HE3 H 2.910 0.02 1 512 . 47 GLY N N 108.500 0.15 1 513 . 47 GLY CA C 43.200 0.15 1 514 . 47 GLY C C 171.000 0.15 1 515 . 47 GLY H H 7.600 0.02 1 516 . 47 GLY HA2 H 3.950 0.02 2 517 . 47 GLY HA3 H 3.800 0.02 2 518 . 48 LYS N N 119.600 0.15 1 519 . 48 LYS CA C 54.000 0.15 1 520 . 48 LYS C C 174.900 0.15 1 521 . 48 LYS CB C 30.500 0.15 1 522 . 48 LYS CG C 22.300 0.15 1 523 . 48 LYS CD C 26.600 0.15 1 524 . 48 LYS CE C 39.900 0.15 1 525 . 48 LYS H H 8.110 0.02 1 526 . 48 LYS HA H 4.330 0.02 1 527 . 48 LYS HB2 H 1.890 0.02 2 528 . 48 LYS HB3 H 1.740 0.02 2 529 . 48 LYS HG2 H 1.390 0.02 1 530 . 48 LYS HG3 H 1.390 0.02 1 531 . 48 LYS HD2 H 1.640 0.02 1 532 . 48 LYS HD3 H 1.640 0.02 1 533 . 48 LYS HE2 H 2.940 0.02 1 534 . 48 LYS HE3 H 2.940 0.02 1 535 . 49 GLY N N 109.700 0.15 1 536 . 49 GLY CA C 43.600 0.15 1 537 . 49 GLY C C 171.500 0.15 1 538 . 49 GLY H H 8.640 0.02 1 539 . 49 GLY HA2 H 3.910 0.02 3 540 . 49 GLY HA3 H 3.810 0.02 2 541 . 50 ASN N N 119.400 0.15 1 542 . 50 ASN CA C 49.200 0.15 1 543 . 50 ASN C C 171.700 0.15 1 544 . 50 ASN CB C 36.700 0.15 1 545 . 50 ASN ND2 N 112.400 0.15 1 546 . 50 ASN H H 8.130 0.02 1 547 . 50 ASN HA H 4.980 0.02 1 548 . 50 ASN HB2 H 2.800 0.02 2 549 . 50 ASN HB3 H 2.700 0.02 2 550 . 50 ASN HD21 H 7.530 0.02 2 551 . 50 ASN HD22 H 6.610 0.02 2 552 . 51 PRO CA C 62.900 0.15 1 553 . 51 PRO C C 176.900 0.15 1 554 . 51 PRO CB C 29.700 0.15 1 555 . 51 PRO CG C 25.100 0.15 1 556 . 51 PRO CD C 48.800 0.15 1 557 . 51 PRO HA H 4.260 0.02 1 558 . 51 PRO HB2 H 2.330 0.02 2 559 . 51 PRO HB3 H 1.920 0.02 2 560 . 51 PRO HG2 H 2.040 0.02 1 561 . 51 PRO HG3 H 2.040 0.02 1 562 . 51 PRO HD2 H 3.920 0.02 2 563 . 51 PRO HD3 H 3.830 0.02 2 564 . 52 GLU N N 118.300 0.15 1 565 . 52 GLU CA C 57.000 0.15 1 566 . 52 GLU C C 176.600 0.15 1 567 . 52 GLU CB C 26.700 0.15 1 568 . 52 GLU CG C 34.400 0.15 1 569 . 52 GLU H H 8.290 0.02 1 570 . 52 GLU HA H 4.050 0.02 1 571 . 52 GLU HB2 H 1.930 0.02 1 572 . 52 GLU HB3 H 1.930 0.02 1 573 . 52 GLU HG2 H 2.100 0.02 1 574 . 52 GLU HG3 H 2.100 0.02 1 575 . 53 VAL N N 119.100 0.15 1 576 . 53 VAL CA C 63.800 0.15 1 577 . 53 VAL C C 175.500 0.15 1 578 . 53 VAL CB C 29.200 0.15 1 579 . 53 VAL CG1 C 18.800 0.15 1 580 . 53 VAL CG2 C 20.000 0.15 1 581 . 53 VAL H H 7.280 0.02 1 582 . 53 VAL HA H 3.420 0.02 1 583 . 53 VAL HB H 1.900 0.02 1 584 . 53 VAL HG1 H 0.760 0.02 4 585 . 53 VAL HG2 H 0.390 0.02 4 586 . 54 GLU N N 118.800 0.15 1 587 . 54 GLU CA C 56.600 0.15 1 588 . 54 GLU C C 176.800 0.15 1 589 . 54 GLU CB C 26.500 0.15 1 590 . 54 GLU CG C 33.400 0.15 1 591 . 54 GLU H H 7.840 0.02 1 592 . 54 GLU HA H 4.050 0.02 1 593 . 54 GLU HB2 H 1.960 0.02 1 594 . 54 GLU HB3 H 1.960 0.02 1 595 . 54 GLU HG2 H 2.280 0.02 1 596 . 54 GLU HG3 H 2.280 0.02 1 597 . 55 ALA N N 120.600 0.15 1 598 . 55 ALA CA C 52.900 0.15 1 599 . 55 ALA C C 179.100 0.15 1 600 . 55 ALA CB C 15.500 0.15 1 601 . 55 ALA H H 7.730 0.02 1 602 . 55 ALA HA H 4.140 0.02 1 603 . 55 ALA HB H 1.490 0.02 1 604 . 56 LEU N N 119.400 0.15 1 605 . 56 LEU CA C 55.600 0.15 1 606 . 56 LEU C C 176.500 0.15 1 607 . 56 LEU CB C 40.000 0.15 1 608 . 56 LEU CG C 24.700 0.15 1 609 . 56 LEU CD1 C 24.500 0.15 1 610 . 56 LEU CD2 C 21.700 0.15 1 611 . 56 LEU H H 7.670 0.02 1 612 . 56 LEU HA H 4.140 0.02 1 613 . 56 LEU HB2 H 2.030 0.02 2 614 . 56 LEU HB3 H 1.470 0.02 2 615 . 56 LEU HG H 1.960 0.02 1 616 . 56 LEU HD1 H 0.880 0.02 4 617 . 56 LEU HD2 H 0.890 0.02 4 618 . 57 ARG N N 119.100 0.15 1 619 . 57 ARG CA C 57.900 0.15 1 620 . 57 ARG C C 177.700 0.15 1 621 . 57 ARG CB C 27.600 0.15 1 622 . 57 ARG CG C 25.900 0.15 1 623 . 57 ARG CD C 40.900 0.15 1 624 . 57 ARG H H 8.390 0.02 1 625 . 57 ARG HA H 3.810 0.02 1 626 . 57 ARG HB2 H 1.880 0.02 2 627 . 57 ARG HB3 H 1.810 0.02 2 628 . 57 ARG HG2 H 1.930 0.02 2 629 . 57 ARG HG3 H 1.810 0.02 2 630 . 57 ARG HD2 H 3.110 0.02 2 631 . 57 ARG HD3 H 3.090 0.02 2 632 . 58 LYS N N 119.400 0.15 1 633 . 58 LYS CA C 57.300 0.15 1 634 . 58 LYS C C 176.900 0.15 1 635 . 58 LYS CB C 30.100 0.15 1 636 . 58 LYS CG C 23.100 0.15 1 637 . 58 LYS CD C 27.000 0.15 1 638 . 58 LYS CE C 39.800 0.15 1 639 . 58 LYS H H 7.970 0.02 1 640 . 58 LYS HA H 4.030 0.02 1 641 . 58 LYS HB2 H 1.920 0.02 1 642 . 58 LYS HB3 H 1.920 0.02 1 643 . 58 LYS HG2 H 1.610 0.02 2 644 . 58 LYS HG3 H 1.430 0.02 2 645 . 58 LYS HD2 H 1.670 0.02 1 646 . 58 LYS HD3 H 1.670 0.02 1 647 . 58 LYS HE2 H 2.930 0.02 1 648 . 58 LYS HE3 H 2.930 0.02 1 649 . 60 ALA N N 121.100 0.15 1 650 . 60 ALA CA C 53.200 0.15 1 651 . 60 ALA C C 176.500 0.15 1 652 . 60 ALA CB C 15.300 0.15 1 653 . 60 ALA H H 8.500 0.02 1 654 . 60 ALA HA H 3.930 0.02 1 655 . 60 ALA HB H 1.500 0.02 1 656 . 61 ALA N N 119.100 0.15 1 657 . 61 ALA CA C 52.600 0.15 1 658 . 61 ALA C C 177.700 0.15 1 659 . 61 ALA CB C 15.600 0.15 1 660 . 61 ALA H H 7.860 0.02 1 661 . 61 ALA HA H 4.020 0.02 1 662 . 61 ALA HB H 1.490 0.02 1 663 . 62 ALA N N 120.400 0.15 1 664 . 62 ALA CA C 52.600 0.15 1 665 . 62 ALA C C 179.300 0.15 1 666 . 62 ALA CB C 15.600 0.15 1 667 . 62 ALA H H 7.760 0.02 1 668 . 62 ALA HA H 4.200 0.02 1 669 . 62 ALA HB H 1.530 0.02 1 670 . 63 ILE N N 120.000 0.15 1 671 . 63 ILE CA C 62.600 0.15 1 672 . 63 ILE C C 175.300 0.15 1 673 . 63 ILE CB C 35.300 0.15 1 674 . 63 ILE CG1 C 26.800 0.15 2 675 . 63 ILE CG2 C 15.400 0.15 1 676 . 63 ILE CD1 C 12.200 0.15 1 677 . 63 ILE H H 7.890 0.02 1 678 . 63 ILE HA H 3.730 0.02 1 679 . 63 ILE HB H 1.960 0.02 1 680 . 63 ILE HG12 H 1.840 0.02 1 681 . 63 ILE HG13 H 1.840 0.02 1 682 . 63 ILE HG2 H 0.850 0.02 4 683 . 63 ILE HD1 H 0.770 0.02 1 684 . 64 ARG N N 119.700 0.15 1 685 . 64 ARG CA C 58.100 0.15 1 686 . 64 ARG C C 176.900 0.15 1 687 . 64 ARG CB C 27.200 0.15 1 688 . 64 ARG CG C 25.600 0.15 1 689 . 64 ARG CD C 40.700 0.15 1 690 . 64 ARG H H 8.010 0.02 1 691 . 64 ARG HA H 3.830 0.02 1 692 . 64 ARG HB2 H 2.030 0.02 2 693 . 64 ARG HB3 H 1.920 0.02 2 694 . 64 ARG HG2 H 1.720 0.02 2 695 . 64 ARG HG3 H 1.590 0.02 2 696 . 64 ARG HD2 H 3.220 0.02 1 697 . 64 ARG HD3 H 3.220 0.02 1 698 . 65 ASP N N 119.000 0.15 1 699 . 65 ASP CA C 55.300 0.15 1 700 . 65 ASP C C 177.000 0.15 1 701 . 65 ASP CB C 37.900 0.15 1 702 . 65 ASP H H 8.120 0.02 1 703 . 65 ASP HA H 4.390 0.02 1 704 . 65 ASP HB2 H 2.790 0.02 2 705 . 65 ASP HB3 H 2.650 0.02 2 706 . 66 GLU N N 121.400 0.15 1 707 . 66 GLU CA C 56.800 0.15 1 708 . 66 GLU C C 176.700 0.15 1 709 . 66 GLU CB C 26.900 0.15 1 710 . 66 GLU CG C 33.500 0.15 1 711 . 66 GLU H H 7.900 0.02 1 712 . 66 GLU HA H 4.050 0.02 1 713 . 66 GLU HB2 H 2.240 0.02 2 714 . 66 GLU HB3 H 2.140 0.02 2 715 . 66 GLU HG2 H 2.420 0.02 2 716 . 66 GLU HG3 H 2.270 0.02 2 717 . 67 LEU N N 118.700 0.15 1 718 . 67 LEU CA C 55.300 0.15 1 719 . 67 LEU C C 176.700 0.15 1 720 . 67 LEU CB C 39.400 0.15 1 721 . 67 LEU CG C 24.500 0.15 1 722 . 67 LEU CD1 C 23.300 0.15 1 723 . 67 LEU CD2 C 22.700 0.15 1 724 . 67 LEU H H 8.130 0.02 1 725 . 67 LEU HA H 4.050 0.02 1 726 . 67 LEU HB2 H 1.840 0.02 2 727 . 67 LEU HB3 H 1.770 0.02 2 728 . 67 LEU HG H 1.670 0.02 1 729 . 67 LEU HD1 H 0.890 0.02 4 730 . 67 LEU HD2 H 0.850 0.02 2 731 . 68 GLN N N 116.000 0.15 1 732 . 68 GLN CA C 55.800 0.15 1 733 . 68 GLN C C 175.500 0.15 1 734 . 68 GLN CB C 25.900 0.15 1 735 . 68 GLN CG C 31.500 0.15 1 736 . 68 GLN NE2 N 111.100 0.15 1 737 . 68 GLN H H 7.860 0.02 1 738 . 68 GLN HA H 4.020 0.02 1 739 . 68 GLN HB2 H 2.150 0.02 2 740 . 68 GLN HB3 H 1.970 0.02 2 741 . 68 GLN HG2 H 2.520 0.02 1 742 . 68 GLN HG3 H 2.520 0.02 1 743 . 68 GLN HE21 H 7.420 0.02 2 744 . 68 GLN HE22 H 6.790 0.02 2 745 . 69 ALA N N 120.400 0.15 1 746 . 69 ALA CA C 51.400 0.15 1 747 . 69 ALA C C 176.500 0.15 1 748 . 69 ALA CB C 15.900 0.15 1 749 . 69 ALA H H 7.580 0.02 1 750 . 69 ALA HA H 4.140 0.02 1 751 . 69 ALA HB H 1.320 0.02 1 752 . 70 TYR N N 116.500 0.15 1 753 . 70 TYR CA C 56.800 0.15 1 754 . 70 TYR C C 173.700 0.15 1 755 . 70 TYR CB C 36.400 0.15 1 756 . 70 TYR CD1 C 133.010 0.15 1 757 . 70 TYR CD2 C 133.010 0.15 1 758 . 70 TYR CE1 C 118.230 0.15 1 759 . 70 TYR CE2 C 118.230 0.15 1 760 . 70 TYR H H 7.660 0.02 1 761 . 70 TYR HA H 4.290 0.02 1 762 . 70 TYR HB2 H 3.120 0.02 2 763 . 70 TYR HB3 H 3.020 0.02 2 764 . 70 TYR HD1 H 7.190 0.02 1 765 . 70 TYR HD2 H 7.190 0.02 1 766 . 70 TYR HE1 H 6.760 0.02 1 767 . 70 TYR HE2 H 6.760 0.02 1 768 . 71 ARG N N 119.000 0.15 1 769 . 71 ARG CA C 54.000 0.15 1 770 . 71 ARG C C 172.900 0.15 1 771 . 71 ARG CB C 28.500 0.15 1 772 . 71 ARG CG C 25.200 0.15 1 773 . 71 ARG CD C 41.100 0.15 1 774 . 71 ARG H H 7.550 0.02 1 775 . 71 ARG HA H 4.240 0.02 1 776 . 71 ARG HB2 H 1.820 0.02 2 777 . 71 ARG HB3 H 1.760 0.02 2 778 . 71 ARG HG2 H 1.680 0.02 2 779 . 71 ARG HG3 H 1.560 0.02 2 780 . 71 ARG HD2 H 3.140 0.02 1 781 . 71 ARG HD3 H 3.140 0.02 1 782 . 72 HIS N N 118.700 0.15 1 783 . 72 HIS CA C 52.900 0.15 1 784 . 72 HIS C C 170.300 0.15 1 785 . 72 HIS CB C 26.800 0.15 1 786 . 72 HIS CD2 C 120.300 0.15 1 787 . 72 HIS CE1 C 136.350 0.15 1 788 . 72 HIS H H 8.190 0.02 1 789 . 72 HIS HA H 4.690 0.02 1 790 . 72 HIS HB2 H 3.290 0.02 2 791 . 72 HIS HB3 H 3.190 0.02 2 792 . 72 HIS HD2 H 7.330 0.02 3 793 . 72 HIS HE1 H 8.550 0.02 1 794 . 73 ASN N N 125.100 0.15 1 795 . 73 ASN CA C 52.500 0.15 1 796 . 73 ASN C C 177.700 0.15 1 797 . 73 ASN CB C 37.800 0.15 1 798 . 73 ASN ND2 N 112.000 0.15 1 799 . 73 ASN H H 8.160 0.02 1 800 . 73 ASN HA H 4.480 0.02 1 801 . 73 ASN HB2 H 2.760 0.02 2 802 . 73 ASN HB3 H 2.660 0.02 2 803 . 73 ASN HD21 H 7.450 0.02 2 804 . 73 ASN HD22 H 6.760 0.02 2 stop_ save_