data_4375 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Assignments of Ubiquitin Unfolded in 8M Urea, pH2 and Analysis of Chemical shift Dispersion in Unfolded Proteins ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Peti Wolfgang . . 2 Smith Lorna J. . 3 Redfield Christina . . 4 Schwalbe Harald . . stop_ _BMRB_accession_number 4375 _BMRB_flat_file_name bmr4375.str _Entry_type new _Submission_date 1999-08-10 _Accession_date 1999-08-10 _Entry_origination author _NMR_STAR_version 2.1.1 _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' 379 '13C chemical shifts' 313 '15N chemical shifts' 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-12-08 update BMRB "update the relationship loop" 2001-02-27 original author "original release" stop_ loop_ _Related_BMRB_accession_number _Relationship 1520 ; Characterization of a Partially Denatured State of a Protein by Two-Dimensional NMR: Reduction of the Hydrophobic Interactions in Ubiquitin ; 2573 ; Fast Internal Main-Chain Dynamics of Human Ubiquitin ; 2574 ; Fast Internal Main-Chain Dynamics of Human Ubiquitin ; 68 ; Sequential 1H NMR Assignments and Secondary Structure Identification of Human Ubiquitin ; 15047 "chemical shifts of denatured ubiquitin" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Chemical Shifts in Denatured Proteins: Resonance Assignments for Denatured Ubiquitin and Comparisons with other Denatured Proteins ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21151318 _PubMed_ID 11256811 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Peti Wolfgang . . 2 Smith Lorna J. . 3 Redfield Christina . . 4 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 2 _Page_first 153 _Page_last 165 _Year 2001 loop_ _Keyword 'Unfolded proteins' Ubiquitin 'Resonance Assignment' 'Triple Resonance NMR' stop_ save_ ################################## # Molecular system description # ################################## save_system_GMH4CO _Saveframe_category molecular_system _Mol_system_name Ubiquitin _Abbreviation_common Ubiquitin loop_ _Mol_system_component_name _Mol_label Ubiquitin $Ubiquitin stop_ _System_molecular_weight 8668.31 _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' save_ ######################## # Monomeric polymers # ######################## save_Ubiquitin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ubiquitin _Abbreviation_common ubiquitin _Details ; 13C,15N, Ubiquitin ; ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ILE 4 PHE 5 VAL 6 LYS 7 THR 8 LEU 9 THR 10 GLY 11 LYS 12 THR 13 ILE 14 THR 15 LEU 16 GLU 17 VAL 18 GLU 19 PRO 20 SER 21 ASP 22 THR 23 ILE 24 GLU 25 ASN 26 VAL 27 LYS 28 ALA 29 LYS 30 ILE 31 GLN 32 ASP 33 LYS 34 GLU 35 GLY 36 ILE 37 PRO 38 PRO 39 ASP 40 GLN 41 GLN 42 ARG 43 LEU 44 ILE 45 PHE 46 ALA 47 GLY 48 LYS 49 GLN 50 LEU 51 GLU 52 ASP 53 GLY 54 ARG 55 THR 56 LEU 57 SER 58 ASP 59 TYR 60 ASN 61 ILE 62 GLN 63 LYS 64 GLU 65 SER 66 THR 67 LEU 68 HIS 69 LEU 70 VAL 71 LEU 72 ARG 73 LEU 74 ARG 75 GLY 76 GLY stop_ _Sequence_homology_query_date 2008-09-24 _Sequence_homology_query_revised_last_date 2008-09-24 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 1YX5 "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" 100.00 98 100.00 100.00 1.43e-36 PDB 1YX6 "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" 100.00 98 100.00 100.00 1.43e-36 DBJ BAA09860 "polyubiquitin [Homo sapiens]" 100.00 611 98.68 98.68 3.65e-35 DBJ BAA11842 "ubiquitin [Cavia porcellus]" 100.00 311 100.00 100.00 4.85e-36 DBJ BAA11843 "ubiquitin extention protein [Cavia porcellus]" 100.00 156 100.00 100.00 9.69e-37 DBJ BAA23632 "polyubiquitin UbC [Homo sapiens]" 100.00 685 100.00 100.00 4.93e-36 DBJ BAA76675 "ubiquitin/79aa fusion protein [Bombyx mori]" 100.00 155 98.68 100.00 3.81e-36 EMBL CAA30815 "unnamed protein product [Cricetulus sp.]" 93.42 223 100.00 100.00 7.68e-33 EMBL CAA37227 "unnamed protein product [Drosophila melanogaster]" 100.00 128 100.00 100.00 1.36e-36 EMBL CAA37599 "unnamed protein product [Manduca sexta]" 100.00 155 100.00 100.00 1.30e-36 EMBL CAA40312 "ubiquitin-52 amino acid fusion protein [Homo sapiens]" 100.00 128 100.00 100.00 1.22e-36 EMBL CAA40313 "ubiquitin-52 amino acid fusion protein [Homo sapiens]" 100.00 128 100.00 100.00 1.22e-36 GenBank AAA28997 ubiquitin 100.00 231 100.00 100.00 4.73e-36 GenBank AAA28998 "ubiquitin-hybrid protein precursor" 100.00 156 100.00 100.00 1.56e-36 GenBank AAA36789 ubiquitin 100.00 685 100.00 100.00 4.93e-36 GenBank AAA53067 "p125 protein" 100.00 1054 100.00 100.00 1.46e-36 GenBank AAA56988 ubiquitin 100.00 128 100.00 100.00 1.22e-36 PIR I65237 "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" 100.00 128 100.00 100.00 1.22e-36 PIR UQHUR7 "ubiquitin / ribosomal protein S27a, cytosolic [validated] - human" 100.00 156 100.00 100.00 9.69e-37 REF NP_001005123 "ubiquitin A-52 residue ribosomal protein fusion product 1 [Xenopus tropicalis]" 100.00 128 100.00 100.00 1.22e-36 REF NP_001006688 "ubiquitin C [Xenopus tropicalis]" 100.00 609 100.00 100.00 5.01e-36 REF NP_001009202 "polyubiquitin [Ovis aries]" 100.00 305 98.68 100.00 7.87e-36 REF NP_001009286 "ubiqitin RPL40 fusion protein [Ovis aries]" 100.00 128 100.00 100.00 1.22e-36 REF NP_001013290 "ubiquitin C [Danio rerio]" 100.00 610 100.00 100.00 5.06e-36 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ubiquitin Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Organ _Tissue _Cell_line _Cell_type _ATCC_number _Vector_type _Vector_name _Vendor_name $Ubiquitin "recombinant technology" . . . . . . . . . . . . 'Sample from VLI Research, Inc. Laboratories, Malvern, PA' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details ; The volume used was 250?l in a 5mm microcell Shigemi tube. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Ubiquitin 5 mg . . "[U-15N; U-13C]" H2O 95 % . . . D2O 5 % . . . Urea 8 M . . . stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 0.02 n/a temperature 303 0.1 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details ; Internal reference with DSS and TSP, we found no difference. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _Indirect_shift_ratio DSS H 1 "methyl protons" ppm 0 internal direct . DSS C 13 "methyl protons" ppm 0 internal indirect .2514495192 DSS N 15 "methyl protons" ppm 0 internal indirect .1013290513 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts 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 Ubiquitin 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 MET CA C 54.747 0.05 1 2 1 MET C C 172.127 0.05 1 3 1 MET CB C 32.337 0.05 1 4 1 MET CG C 30.345 0.05 1 5 2 GLN H H 8.908 0.03 1 6 2 GLN HA H 4.371 0.03 1 7 2 GLN HB2 H 1.872 0.03 2 8 2 GLN HB3 H 1.908 0.03 2 9 2 GLN HG2 H 2.193 0.03 2 10 2 GLN HG3 H 2.229 0.03 2 11 2 GLN CA C 55.245 0.05 1 12 2 GLN C C 175.580 0.05 1 13 2 GLN CB C 29.349 0.05 1 14 2 GLN CG C 33.333 0.05 1 15 2 GLN N N 123.948 0.05 1 16 3 ILE H H 8.360 0.03 1 17 3 ILE HA H 4.157 0.03 1 18 3 ILE HB H 1.765 0.03 1 19 3 ILE HG12 H 1.372 0.03 2 20 3 ILE HG13 H 1.087 0.03 2 21 3 ILE HG2 H 0.837 0.03 1 22 3 ILE CA C 60.225 0.05 1 23 3 ILE C C 175.493 0.05 1 24 3 ILE CB C 38.811 0.05 1 25 3 ILE CG1 C 26.361 0.05 1 26 3 ILE CG2 C 16.899 0.05 1 27 3 ILE CD1 C 11.919 0.05 1 28 3 ILE N N 122.415 0.05 1 29 4 PHE H H 8.487 0.03 1 30 4 PHE HA H 4.728 0.03 1 31 4 PHE HB2 H 3.086 0.03 2 32 4 PHE HB3 H 2.943 0.03 2 33 4 PHE HE1 H 7.191 0.03 3 34 4 PHE CA C 56.241 0.05 1 35 4 PHE C C 174.976 0.05 1 36 4 PHE CB C 39.309 0.05 1 37 4 PHE N N 124.494 0.05 1 38 5 VAL H H 8.334 0.03 1 39 5 VAL HA H 4.157 0.03 1 40 5 VAL HB H 1.979 0.03 1 41 5 VAL HG2 H 0.873 0.03 2 42 5 VAL CA C 61.719 0.05 1 43 5 VAL C C 175.580 0.05 1 44 5 VAL CB C 32.835 0.05 1 45 5 VAL CG1 C 20.385 0.05 1 46 5 VAL CG2 C 20.385 0.05 1 47 5 VAL N N 122.410 0.05 1 48 6 LYS H H 8.452 0.03 1 49 6 LYS HA H 4.371 0.03 1 50 6 LYS HB2 H 1.836 0.03 2 51 6 LYS HB3 H 1.729 0.03 2 52 6 LYS HG2 H 1.444 0.03 2 53 6 LYS HD2 H 1.622 0.03 2 54 6 LYS HE2 H 3.015 0.03 2 55 6 LYS HE3 H 2.979 0.03 2 56 6 LYS CA C 55.743 0.05 1 57 6 LYS C C 176.788 0.05 1 58 6 LYS CB C 32.835 0.05 1 59 6 LYS CG C 24.369 0.05 1 60 6 LYS CD C 28.851 0.05 1 61 6 LYS CE C 41.799 0.05 1 62 6 LYS N N 125.102 0.05 1 63 7 THR H H 8.335 0.03 1 64 7 THR HA H 4.406 0.03 1 65 7 THR HB H 4.086 0.03 1 66 7 THR HG2 H 1.230 0.03 1 67 7 THR CA C 61.221 0.05 1 68 7 THR C C 174.889 0.05 1 69 7 THR CB C 69.687 0.05 1 70 7 THR CG2 C 20.883 0.05 1 71 7 THR N N 115.893 0.05 1 72 8 LEU H H 8.509 0.03 1 73 8 LEU HA H 4.443 0.03 1 74 8 LEU HB2 H 1.658 0.03 1 75 8 LEU HB3 H 1.658 0.03 1 76 8 LEU HG H 1.551 0.03 1 77 8 LEU HD2 H 0.908 0.03 2 78 8 LEU CA C 55.245 0.05 1 79 8 LEU C C 177.651 0.05 1 80 8 LEU CB C 41.799 0.05 1 81 8 LEU CG C 26.361 0.05 1 82 8 LEU CD1 C 24.369 0.05 1 83 8 LEU CD2 C 22.875 0.05 1 84 8 LEU N N 124.205 0.05 1 85 9 THR H H 8.093 0.03 1 86 9 THR HA H 4.371 0.03 1 87 9 THR HB H 4.264 0.03 1 88 9 THR HG2 H 1.230 0.03 1 89 9 THR CA C 61.221 0.05 1 90 9 THR C C 175.148 0.05 1 91 9 THR CB C 69.687 0.05 1 92 9 THR CG2 C 20.883 0.05 1 93 9 THR N N 112.630 0.05 1 94 10 GLY H H 8.316 0.03 1 95 10 GLY HA2 H 3.943 0.03 2 96 10 GLY HA3 H 4.014 0.03 2 97 10 GLY CA C 44.787 0.05 1 98 10 GLY C C 173.940 0.05 1 99 10 GLY N N 110.301 0.05 1 100 11 LYS H H 8.100 0.03 1 101 11 LYS HA H 4.086 0.03 1 102 11 LYS HB2 H 1.836 0.03 2 103 11 LYS HB3 H 1.729 0.03 2 104 11 LYS HG2 H 1.408 0.03 2 105 11 LYS HG3 H 1.372 0.03 2 106 11 LYS HD2 H 1.694 0.03 2 107 11 LYS HE2 H 3.050 0.03 2 108 11 LYS HE3 H 2.907 0.03 2 109 11 LYS CA C 55.743 0.05 1 110 11 LYS C C 176.788 0.05 1 111 11 LYS CB C 32.835 0.05 1 112 11 LYS CG C 24.369 0.05 1 113 11 LYS CD C 28.353 0.05 1 114 11 LYS CE C 41.799 0.05 1 115 11 LYS N N 120.482 0.05 1 116 12 THR H H 8.377 0.03 1 117 12 THR HA H 4.371 0.03 1 118 12 THR HB H 4.157 0.03 1 119 12 THR HG2 H 1.194 0.03 1 120 12 THR CA C 61.719 0.05 1 121 12 THR C C 174.544 0.05 1 122 12 THR CB C 69.687 0.05 1 123 12 THR CG2 C 20.883 0.05 1 124 12 THR N N 116.610 0.05 1 125 13 ILE H H 8.441 0.03 1 126 13 ILE HA H 4.330 0.03 1 127 13 ILE HB H 1.872 0.03 1 128 13 ILE HG12 H 1.158 0.03 2 129 13 ILE HG13 H 1.444 0.03 2 130 13 ILE HG2 H 0.908 0.03 1 131 13 ILE CA C 60.225 0.05 1 132 13 ILE C C 176.011 0.05 1 133 13 ILE CB C 38.811 0.05 1 134 13 ILE CG1 C 26.361 0.05 1 135 13 ILE CG2 C 16.899 0.05 1 136 13 ILE CD1 C 12.417 0.05 1 137 13 ILE N N 123.520 0.05 1 138 14 THR H H 8.312 0.03 1 139 14 THR HA H 4.371 0.03 1 140 14 THR HB H 4.121 0.03 1 141 14 THR HG2 H 1.158 0.03 1 142 14 THR CA C 61.221 0.05 1 143 14 THR C C 174.199 0.05 1 144 14 THR CB C 69.687 0.05 1 145 14 THR CG2 C 20.883 0.05 1 146 14 THR N N 118.645 0.05 1 147 15 LEU H H 8.390 0.03 1 148 15 LEU HA H 4.407 0.03 1 149 15 LEU HB2 H 1.587 0.03 2 150 15 LEU HB3 H 1.551 0.03 2 151 15 LEU HG H 1.444 0.03 1 152 15 LEU HD2 H 0.908 0.03 2 153 15 LEU CA C 54.249 0.05 1 154 15 LEU C C 176.874 0.05 1 155 15 LEU CB C 42.297 0.05 1 156 15 LEU CG C 26.361 0.05 1 157 15 LEU CD1 C 24.369 0.05 1 158 15 LEU CD2 C 22.875 0.05 1 159 15 LEU N N 125.138 0.05 1 160 16 GLU H H 8.460 0.03 1 161 16 GLU HA H 4.371 0.03 1 162 16 GLU HB2 H 1.979 0.03 2 163 16 GLU HB3 H 2.051 0.03 2 164 16 GLU HG2 H 2.443 0.03 1 165 16 GLU HG3 H 2.443 0.03 1 166 16 GLU CA C 55.245 0.05 1 167 16 GLU C C 175.839 0.05 1 168 16 GLU CB C 28.353 0.05 1 169 16 GLU CG C 32.337 0.05 1 170 16 GLU N N 121.515 0.05 1 171 17 VAL H H 8.254 0.03 1 172 17 VAL HA H 4.156 0.03 1 173 17 VAL HB H 2.015 0.03 1 174 17 VAL HG1 H 0.908 0.03 1 175 17 VAL HG2 H 0.908 0.03 1 176 17 VAL CA C 61.719 0.05 1 177 17 VAL C C 175.925 0.05 1 178 17 VAL CB C 32.337 0.05 1 179 17 VAL CG1 C 20.385 0.05 1 180 17 VAL CG2 C 20.883 0.05 1 181 17 VAL N N 121.457 0.05 1 182 18 GLU H H 8.454 0.03 1 183 18 GLU HA H 4.728 0.03 1 184 18 GLU HB2 H 2.122 0.03 2 185 18 GLU HB3 H 1.908 0.03 2 186 18 GLU HG2 H 2.122 0.03 2 187 18 GLU HG3 H 2.515 0.03 2 188 18 GLU CA C 55.245 0.05 1 189 18 GLU CB C 28.851 0.05 1 190 18 GLU N N 124.448 0.05 1 191 19 PRO CA C 62.715 0.05 1 192 19 PRO C C 176.961 0.05 1 193 19 PRO CB C 31.839 0.05 1 194 19 PRO CG C 26.859 0.05 1 195 19 PRO CD C 50.265 0.05 1 196 20 SER H H 8.430 0.03 1 197 20 SER HA H 4.440 0.03 1 198 20 SER HB2 H 3.907 0.03 1 199 20 SER HB3 H 3.907 0.03 1 200 20 SER CA C 58.233 0.05 1 201 20 SER C C 174.717 0.05 1 202 20 SER CB C 63.711 0.05 1 203 20 SER N N 115.309 0.05 1 204 21 ASP H H 8.529 0.03 1 205 21 ASP HA H 4.728 0.03 1 206 21 ASP HB2 H 2.836 0.03 2 207 21 ASP HB3 H 2.943 0.03 2 208 21 ASP CA C 52.755 0.05 1 209 21 ASP C C 175.321 0.05 1 210 21 ASP CB C 37.815 0.05 1 211 21 ASP N N 120.466 0.05 1 212 22 THR H H 8.117 0.03 1 213 22 THR HA H 4.371 0.03 1 214 22 THR HB H 4.228 0.03 1 215 22 THR HG2 H 1.194 0.03 1 216 22 THR CA C 61.719 0.05 1 217 22 THR C C 174.544 0.05 1 218 22 THR CB C 69.687 0.05 1 219 22 THR CG2 C 20.883 0.05 1 220 22 THR N N 114.056 0.05 1 221 23 ILE H H 8.139 0.03 1 222 23 ILE HA H 4.157 0.03 1 223 23 ILE HB H 1.872 0.03 1 224 23 ILE HG12 H 1.158 0.03 2 225 23 ILE HG13 H 1.479 0.03 2 226 23 ILE HG2 H 0.908 0.03 1 227 23 ILE CA C 60.723 0.05 1 228 23 ILE C C 176.270 0.05 1 229 23 ILE CB C 38.313 0.05 1 230 23 ILE CG1 C 26.859 0.05 1 231 23 ILE CG2 C 16.899 0.05 1 232 23 ILE CD1 C 11.919 0.05 1 233 23 ILE N N 122.722 0.05 1 234 24 GLU H H 8.541 0.03 1 235 24 GLU HA H 4.300 0.03 1 236 24 GLU HB2 H 1.979 0.03 2 237 24 GLU HB3 H 2.086 0.03 2 238 24 GLU HG2 H 2.372 0.03 2 239 24 GLU CA C 55.245 0.05 1 240 24 GLU C C 175.666 0.05 1 241 24 GLU CB C 29.349 0.05 1 242 24 GLU CG C 33.333 0.05 1 243 24 GLU N N 124.467 0.05 1 244 25 ASN H H 8.560 0.03 1 245 25 ASN HA H 4.730 0.03 1 246 25 ASN HB2 H 2.872 0.03 2 247 25 ASN HB3 H 2.943 0.03 2 248 25 ASN CA C 52.755 0.05 1 249 25 ASN CB C 37.815 0.05 1 250 25 ASN N N 120.723 0.05 1 251 26 VAL H H 8.097 0.03 1 252 26 VAL HA H 4.192 0.03 1 253 26 VAL HB H 2.301 0.03 1 254 26 VAL HG1 H 0.873 0.03 1 255 26 VAL HG2 H 0.873 0.03 1 256 26 VAL CA C 61.719 0.05 1 257 26 VAL C C 176.184 0.05 1 258 26 VAL CB C 32.337 0.05 1 259 26 VAL CG1 C 19.887 0.05 1 260 26 VAL CG2 C 20.883 0.05 1 261 26 VAL N N 120.095 0.05 1 262 27 LYS H H 8.346 0.03 1 263 27 LYS HA H 4.300 0.03 1 264 27 LYS HB2 H 1.836 0.03 1 265 27 LYS HB3 H 1.836 0.03 1 266 27 LYS HG2 H 1.444 0.03 2 267 27 LYS HG3 H 1.301 0.03 2 268 27 LYS HD2 H 1.587 0.03 2 269 27 LYS HD3 H 1.729 0.03 2 270 27 LYS HE3 H 2.872 0.03 2 271 27 LYS CA C 55.743 0.05 1 272 27 LYS C C 176.357 0.05 1 273 27 LYS CB C 32.337 0.05 1 274 27 LYS CG C 24.369 0.05 1 275 27 LYS CD C 28.851 0.05 1 276 27 LYS CE C 41.799 0.05 1 277 27 LYS N N 124.410 0.05 1 278 28 ALA H H 8.228 0.03 1 279 28 ALA HA H 4.260 0.03 1 280 28 ALA HB H 1.372 0.03 1 281 28 ALA CA C 52.257 0.05 1 282 28 ALA C C 177.651 0.05 1 283 28 ALA CB C 18.891 0.05 1 284 28 ALA N N 124.955 0.05 1 285 29 LYS H H 8.329 0.03 1 286 29 LYS HA H 4.299 0.03 1 287 29 LYS HB2 H 1.729 0.03 2 288 29 LYS HB3 H 1.765 0.03 2 289 29 LYS HG2 H 1.479 0.03 2 290 29 LYS HG3 H 1.444 0.03 2 291 29 LYS HE2 H 2.979 0.03 1 292 29 LYS HE3 H 2.979 0.03 1 293 29 LYS CA C 56.241 0.05 1 294 29 LYS C C 176.702 0.05 1 295 29 LYS CB C 32.835 0.05 1 296 29 LYS CG C 24.369 0.05 1 297 29 LYS CD C 28.851 0.05 1 298 29 LYS CE C 41.799 0.05 1 299 29 LYS N N 121.002 0.05 1 300 30 ILE H H 8.255 0.03 1 301 30 ILE HA H 4.157 0.03 1 302 30 ILE HB H 1.836 0.03 1 303 30 ILE HG12 H 1.194 0.03 2 304 30 ILE HG13 H 1.479 0.03 2 305 30 ILE HG2 H 0.908 0.03 1 306 30 ILE CA C 60.723 0.05 1 307 30 ILE C C 176.270 0.05 1 308 30 ILE CB C 38.313 0.05 1 309 30 ILE CG1 C 26.361 0.05 1 310 30 ILE CG2 C 16.899 0.05 1 311 30 ILE CD1 C 12.417 0.05 1 312 30 ILE N N 122.422 0.05 1 313 31 GLN H H 8.408 0.03 1 314 31 GLN HA H 4.335 0.03 1 315 31 GLN HB2 H 2.086 0.03 2 316 31 GLN HB3 H 1.979 0.03 2 317 31 GLN HG2 H 2.443 0.03 2 318 31 GLN HG3 H 2.372 0.03 2 319 31 GLN CA C 55.245 0.05 1 320 31 GLN C C 175.666 0.05 1 321 31 GLN CB C 28.353 0.05 1 322 31 GLN CG C 32.337 0.05 1 323 31 GLN N N 123.618 0.05 1 324 32 ASP H H 8.501 0.03 1 325 32 ASP HA H 4.657 0.03 1 326 32 ASP HB2 H 2.765 0.03 2 327 32 ASP HB3 H 2.836 0.03 2 328 32 ASP CA C 52.755 0.05 1 329 32 ASP C C 175.235 0.05 1 330 32 ASP CB C 37.815 0.05 1 331 32 ASP N N 120.303 0.05 1 332 33 LYS H H 8.446 0.03 1 333 33 LYS HA H 4.300 0.03 1 334 33 LYS HB2 H 1.872 0.03 2 335 33 LYS HB3 H 1.765 0.03 2 336 33 LYS HG2 H 1.408 0.03 2 337 33 LYS HG3 H 1.444 0.03 2 338 33 LYS HD3 H 1.729 0.03 2 339 33 LYS HE2 H 3.514 0.03 2 340 33 LYS HE3 H 3.443 0.03 2 341 33 LYS CA C 56.241 0.05 1 342 33 LYS C C 176.443 0.05 1 343 33 LYS CB C 32.337 0.05 1 344 33 LYS CG C 24.369 0.05 1 345 33 LYS CD C 28.353 0.05 1 346 33 LYS CE C 41.799 0.05 1 347 33 LYS N N 121.987 0.05 1 348 34 GLU H H 8.334 0.03 1 349 34 GLU HA H 4.300 0.03 1 350 34 GLU HB2 H 2.015 0.03 2 351 34 GLU HB3 H 2.158 0.03 2 352 34 GLU HG2 H 2.479 0.03 2 353 34 GLU HG3 H 2.515 0.03 2 354 34 GLU CA C 55.245 0.05 1 355 34 GLU C C 176.443 0.05 1 356 34 GLU CB C 28.353 0.05 1 357 34 GLU CG C 32.337 0.05 1 358 34 GLU N N 120.286 0.05 1 359 35 GLY H H 8.352 0.03 1 360 35 GLY HA2 H 3.907 0.03 2 361 35 GLY HA3 H 3.978 0.03 2 362 35 GLY CA C 44.787 0.05 1 363 35 GLY C C 170.508 0.05 1 364 35 GLY N N 109.472 0.05 1 365 36 ILE H H 8.046 0.03 1 366 36 ILE HA H 4.371 0.03 1 367 36 ILE HB H 1.836 0.03 1 368 36 ILE HG12 H 1.158 0.03 2 369 36 ILE HG13 H 1.479 0.03 2 370 36 ILE CA C 58.233 0.05 1 371 36 ILE CB C 38.313 0.05 1 372 36 ILE N N 120.914 0.05 1 373 38 PRO CA C 63.213 0.05 1 374 38 PRO C C 177.047 0.05 1 375 38 PRO CB C 31.839 0.05 1 376 38 PRO CG C 26.859 0.05 1 377 38 PRO CD C 50.265 0.05 1 378 39 ASP H H 8.486 0.03 1 379 39 ASP HA H 4.657 0.03 1 380 39 ASP HB2 H 2.907 0.03 2 381 39 ASP HB3 H 2.943 0.03 2 382 39 ASP CA C 52.755 0.05 1 383 39 ASP C C 175.407 0.05 1 384 39 ASP CB C 37.317 0.05 1 385 39 ASP N N 117.154 0.05 1 386 40 GLN H H 8.321 0.03 1 387 40 GLN HA H 4.335 0.03 1 388 40 GLN HB2 H 1.944 0.03 2 389 40 GLN HB3 H 2.122 0.03 2 390 40 GLN HG2 H 2.336 0.03 2 391 40 GLN HG3 H 2.372 0.03 2 392 40 GLN CA C 55.743 0.05 1 393 40 GLN C C 176.011 0.05 1 394 40 GLN CB C 29.349 0.05 1 395 40 GLN CG C 33.333 0.05 1 396 40 GLN N N 120.173 0.05 1 397 41 GLN H H 8.280 0.03 1 398 41 GLN HA H 4.299 0.03 1 399 41 GLN HB2 H 1.979 0.03 2 400 41 GLN HB3 H 2.086 0.03 2 401 41 GLN HG2 H 2.336 0.03 2 402 41 GLN HG3 H 2.372 0.03 2 403 41 GLN CA C 55.743 0.05 1 404 41 GLN C C 175.925 0.05 1 405 41 GLN CB C 28.851 0.05 1 406 41 GLN CG C 33.333 0.05 1 407 41 GLN N N 120.938 0.05 1 408 42 ARG H H 8.397 0.03 1 409 42 ARG HA H 4.335 0.03 1 410 42 ARG HB2 H 2.051 0.03 2 411 42 ARG HB3 H 1.944 0.03 2 412 42 ARG HG2 H 1.587 0.03 2 413 42 ARG HG3 H 1.765 0.03 2 414 42 ARG HD2 H 3.193 0.03 2 415 42 ARG HD3 H 3.157 0.03 2 416 42 ARG CA C 55.743 0.05 1 417 42 ARG C C 176.011 0.05 1 418 42 ARG CB C 30.345 0.05 1 419 42 ARG CG C 27.357 0.05 1 420 42 ARG CD C 43.293 0.05 1 421 42 ARG N N 122.016 0.05 1 422 43 LEU H H 8.324 0.03 1 423 43 LEU HA H 4.335 0.03 1 424 43 LEU HB2 H 1.765 0.03 2 425 43 LEU HB3 H 1.587 0.03 2 426 43 LEU HG H 1.408 0.03 1 427 43 LEU HD2 H 0.837 0.03 2 428 43 LEU CA C 54.747 0.05 1 429 43 LEU C C 176.788 0.05 1 430 43 LEU CB C 42.297 0.05 1 431 43 LEU CG C 26.361 0.05 1 432 43 LEU CD1 C 24.369 0.05 1 433 43 LEU CD2 C 22.875 0.05 1 434 43 LEU N N 123.797 0.05 1 435 44 ILE H H 8.181 0.03 1 436 44 ILE HA H 4.120 0.03 1 437 44 ILE HB H 1.729 0.03 1 438 44 ILE HG12 H 1.087 0.03 2 439 44 ILE HG13 H 1.372 0.03 2 440 44 ILE HG2 H 0.801 0.03 1 441 44 ILE CA C 60.225 0.05 1 442 44 ILE C C 175.925 0.05 1 443 44 ILE CB C 38.313 0.05 1 444 44 ILE CG1 C 26.361 0.05 1 445 44 ILE CG2 C 16.899 0.05 1 446 44 ILE CD1 C 11.919 0.05 1 447 44 ILE N N 121.791 0.05 1 448 45 PHE H H 8.421 0.03 1 449 45 PHE HA H 4.585 0.03 1 450 45 PHE HB2 H 2.979 0.03 2 451 45 PHE HB3 H 3.122 0.03 2 452 45 PHE HE1 H 7.226 0.03 3 453 45 PHE CA C 57.237 0.05 1 454 45 PHE C C 175.407 0.05 1 455 45 PHE CB C 39.309 0.05 1 456 45 PHE N N 124.480 0.05 1 457 46 ALA H H 8.340 0.03 1 458 46 ALA HA H 4.300 0.03 1 459 46 ALA HB H 1.372 0.03 1 460 46 ALA CA C 51.759 0.05 1 461 46 ALA C C 177.738 0.05 1 462 46 ALA CB C 18.891 0.05 1 463 46 ALA N N 125.963 0.05 1 464 47 GLY H H 7.870 0.03 1 465 47 GLY HA2 H 3.943 0.03 2 466 47 GLY HA3 H 3.907 0.03 2 467 47 GLY CA C 44.787 0.05 1 468 47 GLY C C 174.026 0.05 1 469 47 GLY N N 107.253 0.05 1 470 48 LYS H H 8.236 0.03 1 471 48 LYS HA H 4.335 0.03 1 472 48 LYS HB2 H 1.836 0.03 2 473 48 LYS HB3 H 1.729 0.03 2 474 48 LYS HG2 H 1.408 0.03 2 475 48 LYS HG3 H 1.444 0.03 2 476 48 LYS HE2 H 2.979 0.03 2 477 48 LYS HE3 H 3.122 0.03 2 478 48 LYS CA C 56.241 0.05 1 479 48 LYS C C 176.702 0.05 1 480 48 LYS CB C 32.835 0.05 1 481 48 LYS CG C 24.369 0.05 1 482 48 LYS CD C 28.851 0.05 1 483 48 LYS CE C 41.799 0.05 1 484 48 LYS N N 120.443 0.05 1 485 49 GLN H H 8.514 0.03 1 486 49 GLN HA H 4.335 0.03 1 487 49 GLN HB2 H 2.086 0.03 2 488 49 GLN HB3 H 1.979 0.03 2 489 49 GLN HG2 H 2.336 0.03 2 490 49 GLN HG3 H 2.372 0.03 2 491 49 GLN CA C 55.743 0.05 1 492 49 GLN C C 176.011 0.05 1 493 49 GLN CB C 28.851 0.05 1 494 49 GLN CG C 32.835 0.05 1 495 49 GLN N N 121.372 0.05 1 496 50 LEU H H 8.354 0.03 1 497 50 LEU HA H 4.371 0.03 1 498 50 LEU HB2 H 1.622 0.03 2 499 50 LEU HB3 H 1.587 0.03 2 500 50 LEU HG H 1.551 0.03 1 501 50 LEU HD2 H 0.873 0.03 2 502 50 LEU CA C 54.747 0.05 1 503 50 LEU C C 177.392 0.05 1 504 50 LEU CB C 42.297 0.05 1 505 50 LEU CG C 26.361 0.05 1 506 50 LEU CD1 C 24.369 0.05 1 507 50 LEU CD2 C 22.875 0.05 1 508 50 LEU N N 123.626 0.05 1 509 51 GLU H H 8.457 0.03 1 510 51 GLU HA H 4.371 0.03 1 511 51 GLU HB2 H 2.122 0.03 2 512 51 GLU HB3 H 1.979 0.03 2 513 51 GLU HG2 H 2.443 0.03 2 514 51 GLU HG3 H 2.479 0.03 2 515 51 GLU CA C 55.245 0.05 1 516 51 GLU C C 175.925 0.05 1 517 51 GLU CB C 28.353 0.05 1 518 51 GLU CG C 32.337 0.05 1 519 51 GLU N N 120.514 0.05 1 520 52 ASP H H 8.531 0.03 1 521 52 ASP HA H 4.728 0.03 1 522 52 ASP HB2 H 2.907 0.03 2 523 52 ASP HB3 H 2.979 0.03 2 524 52 ASP CA C 52.755 0.05 1 525 52 ASP C C 175.580 0.05 1 526 52 ASP CB C 37.815 0.05 1 527 52 ASP N N 119.578 0.05 1 528 53 GLY H H 8.376 0.03 1 529 53 GLY HA2 H 3.943 0.03 2 530 53 GLY HA3 H 3.978 0.03 2 531 53 GLY CA C 45.285 0.05 1 532 53 GLY C C 174.026 0.05 1 533 53 GLY N N 108.578 0.05 1 534 54 ARG H H 8.151 0.03 1 535 54 ARG HA H 4.371 0.03 1 536 54 ARG HB2 H 1.872 0.03 2 537 54 ARG HB3 H 1.765 0.03 2 538 54 ARG HG2 H 1.658 0.03 2 539 54 ARG HG3 H 1.622 0.03 2 540 54 ARG HD2 H 3.193 0.03 1 541 54 ARG HD3 H 3.193 0.03 1 542 54 ARG CA C 55.743 0.05 1 543 54 ARG C C 176.615 0.05 1 544 54 ARG CB C 30.843 0.05 1 545 54 ARG CG C 26.361 0.05 1 546 54 ARG CD C 42.795 0.05 1 547 54 ARG N N 119.912 0.05 1 548 55 THR H H 8.272 0.03 1 549 55 THR HA H 4.371 0.03 1 550 55 THR HB H 4.228 0.03 1 551 55 THR HG2 H 1.230 0.03 1 552 55 THR CA C 61.719 0.05 1 553 55 THR C C 174.630 0.05 1 554 55 THR CB C 69.687 0.05 1 555 55 THR CG2 C 20.883 0.05 1 556 55 THR N N 115.318 0.05 1 557 56 LEU H H 8.368 0.03 1 558 56 LEU HA H 4.300 0.03 1 559 56 LEU HB2 H 1.658 0.03 2 560 56 LEU HB3 H 1.622 0.03 2 561 56 LEU HG H 1.587 0.03 1 562 56 LEU HD2 H 0.873 0.03 2 563 56 LEU CA C 55.245 0.05 1 564 56 LEU C C 177.392 0.05 1 565 56 LEU CB C 42.297 0.05 1 566 56 LEU CG C 26.361 0.05 1 567 56 LEU CD1 C 24.369 0.05 1 568 56 LEU CD2 C 22.875 0.05 1 569 56 LEU N N 124.446 0.05 1 570 57 SER H H 8.356 0.03 1 571 57 SER HA H 4.407 0.03 1 572 57 SER HB2 H 3.800 0.03 2 573 57 SER HB3 H 3.836 0.03 2 574 57 SER CA C 58.233 0.05 1 575 57 SER C C 174.458 0.05 1 576 57 SER CB C 63.711 0.05 1 577 57 SER N N 115.958 0.05 1 578 58 ASP H H 8.436 0.03 1 579 58 ASP HA H 4.657 0.03 1 580 58 ASP HB2 H 2.836 0.03 2 581 58 ASP HB3 H 2.800 0.03 2 582 58 ASP CA C 52.755 0.05 1 583 58 ASP C C 175.235 0.05 1 584 58 ASP CB C 37.815 0.05 1 585 58 ASP N N 120.435 0.05 1 586 59 TYR H H 8.097 0.03 1 587 59 TYR HA H 4.371 0.03 1 588 59 TYR HD1 H 7.048 0.03 3 589 59 TYR CA C 57.735 0.05 1 590 59 TYR C C 175.407 0.05 1 591 59 TYR CB C 38.313 0.05 1 592 59 TYR N N 120.095 0.05 1 593 60 ASN H H 8.360 0.03 1 594 60 ASN HA H 4.692 0.03 1 595 60 ASN HB2 H 2.800 0.03 2 596 60 ASN HB3 H 2.658 0.03 2 597 60 ASN CA C 52.755 0.05 1 598 60 ASN C C 175.062 0.05 1 599 60 ASN CB C 38.313 0.05 1 600 60 ASN N N 120.088 0.05 1 601 61 ILE H H 8.000 0.03 1 602 61 ILE HA H 4.121 0.03 1 603 61 ILE HB H 1.836 0.03 1 604 61 ILE HG12 H 1.158 0.03 2 605 61 ILE HG13 H 1.444 0.03 2 606 61 ILE HG2 H 0.908 0.03 1 607 61 ILE CA C 60.723 0.05 1 608 61 ILE C C 176.184 0.05 1 609 61 ILE CB C 38.313 0.05 1 610 61 ILE CG1 C 26.859 0.05 1 611 61 ILE CG2 C 16.899 0.05 1 612 61 ILE CD1 C 12.417 0.05 1 613 61 ILE N N 120.618 0.05 1 614 62 GLN H H 8.377 0.03 1 615 62 GLN HA H 4.371 0.03 1 616 62 GLN HB2 H 1.944 0.03 2 617 62 GLN HB3 H 2.086 0.03 2 618 62 GLN HG2 H 2.479 0.03 2 619 62 GLN HG3 H 2.443 0.03 2 620 62 GLN CA C 55.245 0.05 1 621 62 GLN C C 176.270 0.05 1 622 62 GLN CB C 30.345 0.05 1 623 62 GLN N N 123.650 0.05 1 624 63 LYS H H 8.358 0.03 1 625 63 LYS HA H 4.300 0.03 1 626 63 LYS HB2 H 1.622 0.03 2 627 63 LYS HB3 H 1.658 0.03 2 628 63 LYS HG2 H 1.230 0.03 1 629 63 LYS HG3 H 1.230 0.03 1 630 63 LYS HD2 H 1.515 0.03 2 631 63 LYS HD3 H 1.587 0.03 2 632 63 LYS HE3 H 2.907 0.03 2 633 63 LYS CA C 56.241 0.05 1 634 63 LYS C C 176.702 0.05 1 635 63 LYS CB C 32.835 0.05 1 636 63 LYS CG C 24.369 0.05 1 637 63 LYS CD C 28.353 0.05 1 638 63 LYS CE C 41.799 0.05 1 639 63 LYS N N 123.890 0.05 1 640 64 GLU H H 8.410 0.03 1 641 64 GLU HA H 4.300 0.03 1 642 64 GLU HB2 H 2.122 0.03 2 643 64 GLU HB3 H 2.015 0.03 2 644 64 GLU HG2 H 2.479 0.03 2 645 64 GLU HG3 H 2.515 0.03 2 646 64 GLU CA C 55.245 0.05 1 647 64 GLU C C 176.270 0.05 1 648 64 GLU CB C 28.353 0.05 1 649 64 GLU CG C 32.337 0.05 1 650 64 GLU N N 120.949 0.05 1 651 65 SER H H 8.442 0.03 1 652 65 SER HA H 4.513 0.03 1 653 65 SER HB2 H 3.907 0.03 1 654 65 SER HB3 H 3.907 0.03 1 655 65 SER CA C 58.233 0.05 1 656 65 SER C C 175.062 0.05 1 657 65 SER CB C 63.711 0.05 1 658 65 SER N N 116.679 0.05 1 659 66 THR H H 8.241 0.03 1 660 66 THR HA H 4.371 0.03 1 661 66 THR HB H 4.050 0.03 1 662 66 THR HG2 H 1.194 0.03 1 663 66 THR CA C 61.719 0.05 1 664 66 THR C C 174.544 0.05 1 665 66 THR CB C 69.189 0.05 1 666 66 THR CG2 C 20.883 0.05 1 667 66 THR N N 115.491 0.05 1 668 67 LEU H H 8.129 0.03 1 669 67 LEU HA H 4.300 0.03 1 670 67 LEU HB2 H 1.551 0.03 2 671 67 LEU HB3 H 1.515 0.03 2 672 67 LEU HG H 1.479 0.03 1 673 67 LEU HD2 H 0.837 0.03 2 674 67 LEU CA C 54.747 0.05 1 675 67 LEU C C 177.047 0.05 1 676 67 LEU CB C 42.297 0.05 1 677 67 LEU CG C 26.361 0.05 1 678 67 LEU CD1 C 23.871 0.05 1 679 67 LEU CD2 C 22.377 0.05 1 680 67 LEU N N 123.757 0.05 1 681 68 HIS H H 8.650 0.03 1 682 68 HIS HA H 4.760 0.03 1 683 68 HIS HB2 H 3.157 0.03 2 684 68 HIS HB3 H 3.264 0.03 2 685 68 HIS CA C 54.249 0.05 1 686 68 HIS C C 174.113 0.05 1 687 68 HIS CB C 28.353 0.05 1 688 68 HIS N N 119.824 0.05 1 689 69 LEU H H 8.304 0.03 1 690 69 LEU HA H 4.300 0.03 1 691 69 LEU HB2 H 1.729 0.03 2 692 69 LEU HB3 H 1.765 0.03 2 693 69 LEU HG H 1.515 0.03 1 694 69 LEU HD2 H 0.873 0.03 2 695 69 LEU CA C 54.747 0.05 1 696 69 LEU C C 176.874 0.05 1 697 69 LEU CB C 42.297 0.05 1 698 69 LEU CG C 26.361 0.05 1 699 69 LEU CD1 C 23.871 0.05 1 700 69 LEU N N 124.029 0.05 1 701 70 VAL H H 8.390 0.03 1 702 70 VAL HA H 4.080 0.03 1 703 70 VAL HB H 2.015 0.03 1 704 70 VAL HG2 H 0.908 0.03 2 705 70 VAL CA C 61.719 0.05 1 706 70 VAL C C 175.925 0.05 1 707 70 VAL CB C 32.337 0.05 1 708 70 VAL CG1 C 20.385 0.05 1 709 70 VAL N N 122.524 0.05 1 710 71 LEU H H 8.383 0.03 1 711 71 LEU HA H 4.300 0.03 1 712 71 LEU HB2 H 1.551 0.03 2 713 71 LEU HB3 H 1.515 0.03 2 714 71 LEU HG H 1.587 0.03 1 715 71 LEU HD2 H 0.837 0.03 2 716 71 LEU CA C 54.747 0.05 1 717 71 LEU C C 176.961 0.05 1 718 71 LEU CB C 42.297 0.05 1 719 71 LEU CG C 26.361 0.05 1 720 71 LEU CD1 C 23.871 0.05 1 721 71 LEU CD2 C 22.875 0.05 1 722 71 LEU N N 126.751 0.05 1 723 72 ARG H H 8.489 0.03 1 724 72 ARG HA H 4.371 0.03 1 725 72 ARG HB2 H 1.765 0.03 2 726 72 ARG HB3 H 1.622 0.03 2 727 72 ARG HG2 H 1.587 0.03 2 728 72 ARG HG3 H 1.515 0.03 2 729 72 ARG HD2 H 2.979 0.03 2 730 72 ARG HD3 H 3.193 0.03 2 731 72 ARG CA C 55.245 0.05 1 732 72 ARG CB C 30.345 0.05 1 733 72 ARG N N 122.663 0.05 1 734 73 LEU CA C 54.747 0.05 1 735 73 LEU C C 177.479 0.05 1 736 73 LEU CB C 42.297 0.05 1 737 73 LEU CG C 26.361 0.05 1 738 73 LEU CD1 C 24.369 0.05 1 739 74 ARG H H 8.566 0.03 1 740 74 ARG HA H 4.335 0.03 1 741 74 ARG HB2 H 1.872 0.03 2 742 74 ARG HB3 H 1.801 0.03 2 743 74 ARG HG2 H 1.658 0.03 2 744 74 ARG HG3 H 1.515 0.03 2 745 74 ARG HD2 H 3.229 0.03 2 746 74 ARG HD3 H 3.193 0.03 2 747 74 ARG CA C 56.241 0.05 1 748 74 ARG C C 176.874 0.05 1 749 74 ARG CB C 30.345 0.05 1 750 74 ARG CG C 26.361 0.05 1 751 74 ARG CD C 43.293 0.05 1 752 74 ARG N N 121.985 0.05 1 753 75 GLY H H 8.448 0.03 1 754 75 GLY HA2 H 3.943 0.03 2 755 75 GLY HA3 H 4.010 0.03 2 756 75 GLY CA C 44.787 0.05 1 757 75 GLY C C 174.285 0.05 1 758 75 GLY N N 109.911 0.05 1 759 76 GLY H H 8.200 0.03 1 760 76 GLY HA2 H 3.943 0.03 2 761 76 GLY HA3 H 4.010 0.03 2 762 76 GLY CA C 43.791 0.05 1 763 76 GLY N N 108.828 0.05 1 stop_ save_