data_4100 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments of the Mrf-2 DNA-binding Domain ; _BMRB_accession_number 4100 _BMRB_flat_file_name bmr4100.str _Entry_type original _Submission_date 1998-01-23 _Accession_date 1998-01-23 _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 Yuan Yate-Ching . . 2 Whitson Robert H. . 3 Itakura Keiichi . . 4 Chen Yuan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 636 "13C chemical shifts" 349 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-03-22 original author . stop_ _Original_release_date 1999-03-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Yuan, Y-C., Whitson, R. H., Itakura, K., and Chen, Y., "Resonance Assignments of the Mrf-2 DNA-binding Domain," J. Biomol. NMR 11, 459-460 (1998). ; _Citation_title 'Resonance Assignments of the Mrf-2 DNA-binding Domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98356293 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuan Yate-Ching . . 2 Whitson Robert H. . 3 Itakura Keiichi . . 4 Chen Yuan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 11 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 459 _Page_last 460 _Year 1998 _Details . loop_ _Keyword 'DNA-binding domains' Mrf-2 'transcription factors' stop_ save_ ################################## # Molecular system description # ################################## save_system_Mrf-2 _Saveframe_category molecular_system _Mol_system_name Mrf-2 _Abbreviation_common Mrf-2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Mrf-2 $Mrf-2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Mrf-2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA-binding domain Mrf-2' _Abbreviation_common Mrf-2 _Molecular_mass 14000 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; MRGSHHHHHHGSRADEQAFL VALYKYMKERKTPIERIPYL GFKQINLWTMFQAAQKLGGY ETITARRQWKHIYDELGGNP GSTSAATCTRRHYERLILPY ERFIKGEEDKPLPPIKPRK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 ARG 14 ALA 15 ASP 16 GLU 17 GLN 18 ALA 19 PHE 20 LEU 21 VAL 22 ALA 23 LEU 24 TYR 25 LYS 26 TYR 27 MET 28 LYS 29 GLU 30 ARG 31 LYS 32 THR 33 PRO 34 ILE 35 GLU 36 ARG 37 ILE 38 PRO 39 TYR 40 LEU 41 GLY 42 PHE 43 LYS 44 GLN 45 ILE 46 ASN 47 LEU 48 TRP 49 THR 50 MET 51 PHE 52 GLN 53 ALA 54 ALA 55 GLN 56 LYS 57 LEU 58 GLY 59 GLY 60 TYR 61 GLU 62 THR 63 ILE 64 THR 65 ALA 66 ARG 67 ARG 68 GLN 69 TRP 70 LYS 71 HIS 72 ILE 73 TYR 74 ASP 75 GLU 76 LEU 77 GLY 78 GLY 79 ASN 80 PRO 81 GLY 82 SER 83 THR 84 SER 85 ALA 86 ALA 87 THR 88 CYS 89 THR 90 ARG 91 ARG 92 HIS 93 TYR 94 GLU 95 ARG 96 LEU 97 ILE 98 LEU 99 PRO 100 TYR 101 GLU 102 ARG 103 PHE 104 ILE 105 LYS 106 GLY 107 GLU 108 GLU 109 ASP 110 LYS 111 PRO 112 LEU 113 PRO 114 PRO 115 ILE 116 LYS 117 PRO 118 ARG 119 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1IG6 "Human Mrf-2 Domain, Nmr, 11 Structures" 89.92 107 100.00 100.00 2.74e-72 PDB 2OEH "Determination Of The Three-Dimensional Structure Of The Mrf2-Dna Complex Using Paramagnetic Spin Labeling" 89.92 107 100.00 100.00 2.74e-72 DBJ BAB15012 "unnamed protein product [Homo sapiens]" 89.92 214 100.00 100.00 2.13e-73 DBJ BAE37034 "unnamed protein product [Mus musculus]" 70.59 158 98.81 98.81 5.11e-54 DBJ BAI45553 "AT rich interactive domain 5B [synthetic construct]" 89.92 1188 100.00 100.00 4.41e-67 EMBL CAG32224 "hypothetical protein RCJMB04_20e24 [Gallus gallus]" 89.92 1185 99.07 100.00 2.96e-67 EMBL CAH89369 "hypothetical protein [Pongo abelii]" 89.92 944 100.00 100.00 3.16e-68 GB AAA59870 "modulator recognition factor 2 [Homo sapiens]" 89.92 246 100.00 100.00 2.80e-73 GB AAF89682 "DNA binding protein DESRT [Mus musculus]" 89.92 743 100.00 100.00 7.29e-68 GB AAH15120 "ARID5B protein, partial [Homo sapiens]" 89.92 217 99.07 99.07 1.38e-72 GB AAH66345 "ARID5B protein, partial [Homo sapiens]" 89.92 213 100.00 100.00 2.28e-73 GB AAI07801 "ARID5B protein, partial [Homo sapiens]" 90.76 458 99.07 99.07 1.67e-69 REF NP_001026391 "AT-rich interactive domain-containing protein 5B [Gallus gallus]" 89.92 1185 99.07 100.00 2.96e-67 REF NP_001101094 "AT-rich interactive domain-containing protein 5B [Rattus norvegicus]" 89.92 1184 100.00 100.00 2.95e-67 REF NP_001125269 "AT-rich interactive domain-containing protein 5B [Pongo abelii]" 89.92 944 100.00 100.00 3.16e-68 REF NP_001231567 "AT-rich interactive domain-containing protein 5B isoform 2 [Homo sapiens]" 89.92 945 100.00 100.00 3.23e-68 REF NP_076087 "AT-rich interactive domain-containing protein 5B [Mus musculus]" 89.92 1188 100.00 100.00 4.11e-67 SP E1BLP6 "RecName: Full=AT-rich interactive domain-containing protein 5B; Short=ARID domain-containing protein 5B" 89.92 1173 100.00 100.00 2.93e-67 SP E2R9X2 "RecName: Full=AT-rich interactive domain-containing protein 5B; Short=ARID domain-containing protein 5B" 89.92 1187 100.00 100.00 1.46e-66 SP Q14865 "RecName: Full=AT-rich interactive domain-containing protein 5B; Short=ARID domain-containing protein 5B; AltName: Full=MRF1-lik" 89.92 1188 100.00 100.00 4.41e-67 SP Q5ZJ69 "RecName: Full=AT-rich interactive domain-containing protein 5B; Short=ARID domain-containing protein 5B" 89.92 1185 99.07 100.00 2.96e-67 SP Q8BM75 "RecName: Full=AT-rich interactive domain-containing protein 5B; Short=ARID domain-containing protein 5B; AltName: Full=Developm" 89.92 1188 100.00 100.00 4.11e-67 TPG DAA14307 "TPA: AT rich interactive domain 5B (MRF1-like) [Bos taurus]" 89.92 1130 100.00 100.00 2.43e-67 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Mrf-2 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 _Vector_type _Vector_name _Details $Mrf-2 'recombinant technology' 'E. coli' Escherichia coli M15PREP plasmid PQE30 ; native ( The modified plasmid has an open reading frame that encodes the sequence Met-Arg-Gly-Ser-(His)6-Gly-Ser, followed by the residues 13-119) ; 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 $Mrf-2 1.0 mM '[U-13C; U-15N]' H2O 90 % . D2O 10 % . KCL 100 mM . Na2S2O4 20 mM . NaN3 0.15 % . stop_ 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_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _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 0.0 . indirect . . . . DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name Mrf-2 _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 . 13 ARG H H 8.70 0.04 1 2 . 13 ARG HA H 4.38 0.04 1 3 . 13 ARG HB2 H 1.96 0.04 2 4 . 13 ARG HB3 H 1.88 0.04 2 5 . 13 ARG HG2 H 1.70 0.04 1 6 . 13 ARG HG3 H 1.70 0.04 1 7 . 13 ARG HD2 H 3.21 0.04 1 8 . 13 ARG HD3 H 3.21 0.04 1 9 . 13 ARG CA C 57.29 0.50 1 10 . 13 ARG CB C 30.40 0.50 1 11 . 13 ARG CG C 27.10 0.50 1 12 . 13 ARG CD C 43.40 0.50 1 13 . 13 ARG N N 123.12 0.50 1 14 . 14 ALA H H 8.23 0.04 1 15 . 14 ALA HA H 4.16 0.04 1 16 . 14 ALA HB H 1.44 0.04 1 17 . 14 ALA CA C 55.10 0.50 1 18 . 14 ALA CB C 18.52 0.50 1 19 . 14 ALA N N 122.91 0.50 1 20 . 15 ASP H H 8.09 0.04 1 21 . 15 ASP HA H 4.33 0.04 1 22 . 15 ASP HB2 H 2.75 0.04 1 23 . 15 ASP HB3 H 2.75 0.04 1 24 . 15 ASP CA C 56.10 0.50 1 25 . 15 ASP CB C 40.20 0.50 1 26 . 15 ASP N N 118.90 0.50 1 27 . 16 GLU H H 7.60 0.04 1 28 . 16 GLU HA H 2.28 0.04 1 29 . 16 GLU HB2 H 1.87 0.04 1 30 . 16 GLU HB3 H 1.87 0.04 1 31 . 16 GLU HG2 H 1.67 0.04 1 32 . 16 GLU HG3 H 1.67 0.04 1 33 . 16 GLU CA C 58.82 0.50 1 34 . 16 GLU CB C 29.60 0.50 1 35 . 16 GLU CG C 27.40 0.50 1 36 . 16 GLU N N 123.12 0.50 1 37 . 17 GLN H H 7.93 0.04 1 38 . 17 GLN HA H 3.92 0.04 1 39 . 17 GLN HB2 H 2.03 0.04 1 40 . 17 GLN HB3 H 2.03 0.04 1 41 . 17 GLN HG2 H 2.41 0.04 1 42 . 17 GLN HG3 H 2.41 0.04 1 43 . 17 GLN HE21 H 7.40 0.04 2 44 . 17 GLN HE22 H 6.82 0.04 2 45 . 17 GLN CA C 59.36 0.50 1 46 . 17 GLN CB C 28.10 0.50 1 47 . 17 GLN CG C 33.80 0.50 1 48 . 17 GLN N N 115.95 0.50 1 49 . 17 GLN NE2 N 111.69 0.50 1 50 . 18 ALA H H 7.94 0.50 1 51 . 18 ALA HA H 4.07 0.04 1 52 . 18 ALA HB H 1.50 0.04 1 53 . 18 ALA CA C 55.37 0.50 1 54 . 18 ALA CB C 17.90 0.50 1 55 . 18 ALA N N 120.17 0.50 1 56 . 19 PHE H H 7.82 0.04 1 57 . 19 PHE HA H 4.24 0.04 1 58 . 19 PHE HB2 H 3.23 0.04 2 59 . 19 PHE HB3 H 3.05 0.04 2 60 . 19 PHE CA C 61.50 0.50 1 61 . 19 PHE CB C 39.90 0.50 1 62 . 19 PHE N N 120.10 0.50 1 63 . 20 LEU H H 8.30 0.04 1 64 . 20 LEU HA H 3.62 0.04 1 65 . 20 LEU HB2 H 1.93 0.04 1 66 . 20 LEU HB3 H 1.93 0.04 1 67 . 20 LEU HG H 2.16 0.04 1 68 . 20 LEU HD1 H 1.03 0.04 2 69 . 20 LEU HD2 H 1.16 0.04 2 70 . 20 LEU CA C 57.97 0.50 1 71 . 20 LEU CB C 41.30 0.50 1 72 . 20 LEU CG C 27.15 0.50 1 73 . 20 LEU CD1 C 26.14 0.50 1 74 . 20 LEU CD2 C 22.59 0.50 1 75 . 20 LEU N N 119.10 0.50 1 76 . 21 VAL H H 8.01 0.04 1 77 . 21 VAL HA H 3.55 0.04 1 78 . 21 VAL HB H 2.00 0.04 1 79 . 21 VAL HG1 H 1.06 0.04 2 80 . 21 VAL HG2 H 0.95 0.04 2 81 . 21 VAL CA C 66.80 0.50 1 82 . 21 VAL CB C 31.80 0.50 1 83 . 21 VAL CG1 C 23.00 0.50 1 84 . 21 VAL CG2 C 21.00 0.50 1 85 . 21 VAL N N 117.19 0.50 1 86 . 22 ALA H H 7.49 0.04 1 87 . 22 ALA HA H 4.07 0.04 1 88 . 22 ALA HB H 1.54 0.04 1 89 . 22 ALA CA C 55.40 0.50 1 90 . 22 ALA CB C 19.23 0.50 1 91 . 22 ALA N N 122.40 0.50 1 92 . 23 LEU H H 8.77 0.04 1 93 . 23 LEU HA H 3.22 0.04 1 94 . 23 LEU HB2 H 1.19 0.04 2 95 . 23 LEU HB3 H 0.11 0.04 2 96 . 23 LEU HG H 1.04 0.04 1 97 . 23 LEU HD1 H 0.66 0.04 2 98 . 23 LEU HD2 H 0.79 0.04 2 99 . 23 LEU CA C 58.20 0.50 1 100 . 23 LEU CB C 41.30 0.50 1 101 . 23 LEU CG C 27.15 0.50 1 102 . 23 LEU CD1 C 26.64 0.50 1 103 . 23 LEU CD2 C 24.11 0.50 1 104 . 23 LEU N N 121.91 0.50 1 105 . 24 TYR H H 8.48 0.04 1 106 . 24 TYR HA H 3.99 0.04 1 107 . 24 TYR HB2 H 3.15 0.04 2 108 . 24 TYR HB3 H 2.87 0.04 2 109 . 24 TYR CA C 62.27 0.50 1 110 . 24 TYR CB C 37.40 0.50 1 111 . 24 TYR N N 116.90 0.50 1 112 . 25 LYS H H 7.91 0.04 1 113 . 25 LYS HA H 4.06 0.04 1 114 . 25 LYS HB2 H 1.96 0.04 1 115 . 25 LYS HB3 H 1.96 0.04 1 116 . 25 LYS HG2 H 1.47 0.04 2 117 . 25 LYS HG3 H 1.38 0.04 2 118 . 25 LYS HD2 H 1.72 0.04 1 119 . 25 LYS HD3 H 1.72 0.04 1 120 . 25 LYS HE2 H 3.02 0.04 1 121 . 25 LYS HE3 H 3.02 0.04 1 122 . 25 LYS CA C 60.20 0.50 1 123 . 25 LYS CB C 32.70 0.50 1 124 . 25 LYS CG C 24.71 0.50 1 125 . 25 LYS CD C 29.00 0.50 1 126 . 25 LYS CE C 41.93 0.50 1 127 . 25 LYS N N 120.17 0.50 1 128 . 26 TYR H H 8.27 0.04 1 129 . 26 TYR HA H 4.00 0.04 1 130 . 26 TYR HB2 H 3.22 0.04 2 131 . 26 TYR HB3 H 3.22 0.04 2 132 . 26 TYR CA C 61.70 0.50 1 133 . 26 TYR CB C 39.20 0.50 1 134 . 26 TYR N N 120.40 0.50 1 135 . 27 MET H H 8.22 0.04 1 136 . 27 MET HA H 3.97 0.04 1 137 . 27 MET HB2 H 2.02 0.04 1 138 . 27 MET HB3 H 2.02 0.04 1 139 . 27 MET HG2 H 2.57 0.04 2 140 . 27 MET HG3 H 2.52 0.04 2 141 . 27 MET HE H 2.33 0.04 1 142 . 27 MET CA C 57.20 0.50 1 143 . 27 MET CB C 31.69 0.50 1 144 . 27 MET CG C 36.80 0.50 1 145 . 27 MET CE C 18.52 0.50 1 146 . 27 MET N N 115.10 0.50 1 147 . 28 LYS H H 8.07 0.04 1 148 . 28 LYS HA H 3.81 0.04 1 149 . 28 LYS HB2 H 2.05 0.04 2 150 . 28 LYS HB3 H 1.92 0.04 2 151 . 28 LYS HG2 H 1.48 0.04 2 152 . 28 LYS HG3 H 1.37 0.04 2 153 . 28 LYS HD2 H 1.62 0.04 1 154 . 28 LYS HD3 H 1.62 0.04 1 155 . 28 LYS HE2 H 2.86 0.04 1 156 . 28 LYS HE3 H 2.86 0.04 1 157 . 28 LYS CA C 60.15 0.50 1 158 . 28 LYS CB C 32.80 0.50 1 159 . 28 LYS CG C 25.10 0.50 1 160 . 28 LYS CD C 29.10 0.50 1 161 . 28 LYS CE C 41.90 0.50 1 162 . 28 LYS N N 120.11 0.50 1 163 . 29 GLU H H 8.32 0.04 1 164 . 29 GLU HA H 3.95 0.04 1 165 . 29 GLU HB2 H 2.04 0.04 1 166 . 29 GLU HB3 H 2.04 0.04 1 167 . 29 GLU HG2 H 2.27 0.04 1 168 . 29 GLU HG3 H 2.27 0.04 1 169 . 29 GLU CA C 59.40 0.50 1 170 . 29 GLU CB C 28.60 0.50 1 171 . 29 GLU CG C 36.30 0.50 1 172 . 29 GLU N N 121.91 0.50 1 173 . 30 ARG H H 7.45 0.04 1 174 . 30 ARG HA H 4.14 0.04 1 175 . 30 ARG HB2 H 1.54 0.04 1 176 . 30 ARG HB3 H 1.54 0.04 1 177 . 30 ARG HG2 H 1.70 0.04 1 178 . 30 ARG HG3 H 1.70 0.04 1 179 . 30 ARG HD2 H 3.00 0.04 1 180 . 30 ARG HD3 H 3.00 0.04 1 181 . 30 ARG CA C 55.80 0.50 1 182 . 30 ARG CB C 30.20 0.50 1 183 . 30 ARG CG C 30.70 0.50 1 184 . 30 ARG CD C 41.90 0.50 1 185 . 30 ARG N N 117.90 0.50 1 186 . 31 LYS H H 7.73 0.04 1 187 . 31 LYS HA H 3.89 0.04 1 188 . 31 LYS HB2 H 2.32 0.04 2 189 . 31 LYS HB3 H 2.04 0.04 2 190 . 31 LYS HG2 H 1.34 0.04 2 191 . 31 LYS HG3 H 1.30 0.04 2 192 . 31 LYS HD2 H 1.71 0.04 2 193 . 31 LYS HD3 H 1.64 0.04 2 194 . 31 LYS HE2 H 3.02 0.04 1 195 . 31 LYS HE3 H 3.02 0.04 1 196 . 31 LYS CA C 56.90 0.50 1 197 . 31 LYS CB C 28.60 0.50 1 198 . 31 LYS CG C 25.10 0.50 1 199 . 31 LYS CD C 29.00 0.50 1 200 . 31 LYS CE C 42.20 0.50 1 201 . 31 LYS N N 111.23 0.50 1 202 . 32 THR H H 8.19 0.04 1 203 . 32 THR HA H 4.70 0.04 1 204 . 32 THR HB H 4.36 0.04 1 205 . 32 THR HG2 H 1.03 0.04 1 206 . 32 THR CA C 57.50 0.50 1 207 . 32 THR CB C 70.00 0.50 1 208 . 32 THR CG2 C 19.40 0.50 1 209 . 32 THR N N 108.50 0.50 1 210 . 33 PRO HA H 4.45 0.04 1 211 . 33 PRO HB2 H 2.27 0.04 2 212 . 33 PRO HB3 H 1.87 0.04 2 213 . 33 PRO HG2 H 2.02 0.04 1 214 . 33 PRO HG3 H 2.02 0.04 1 215 . 33 PRO HD2 H 3.86 0.04 2 216 . 33 PRO HD3 H 3.64 0.04 2 217 . 33 PRO CA C 62.30 0.50 1 218 . 33 PRO CB C 32.40 0.50 1 219 . 33 PRO CG C 27.00 0.50 1 220 . 33 PRO CD C 51.00 0.50 1 221 . 34 ILE H H 8.33 0.04 1 222 . 34 ILE HA H 3.80 0.04 1 223 . 34 ILE HB H 1.39 0.04 1 224 . 34 ILE HG12 H 0.91 0.04 1 225 . 34 ILE HG13 H 0.91 0.04 1 226 . 34 ILE HG2 H 0.66 0.04 1 227 . 34 ILE HD1 H 0.58 0.04 1 228 . 34 ILE CA C 61.70 0.50 1 229 . 34 ILE CB C 36.80 0.50 1 230 . 34 ILE CG1 C 58.63 0.50 1 231 . 34 ILE CG2 C 17.50 0.50 1 232 . 34 ILE CD1 C 12.90 0.50 1 233 . 34 ILE N N 120.90 0.50 1 234 . 35 GLU H H 8.49 0.04 1 235 . 35 GLU HA H 4.39 0.04 1 236 . 35 GLU HB2 H 2.14 0.04 2 237 . 35 GLU HB3 H 1.91 0.04 2 238 . 35 GLU HG2 H 2.23 0.04 1 239 . 35 GLU HG3 H 2.23 0.04 1 240 . 35 GLU CA C 56.90 0.50 1 241 . 35 GLU CB C 31.50 0.50 1 242 . 35 GLU CG C 35.90 0.50 1 243 . 35 GLU N N 128.04 0.50 1 244 . 36 ARG H H 7.88 0.04 1 245 . 36 ARG HA H 4.43 0.04 1 246 . 36 ARG HB2 H 1.82 0.04 1 247 . 36 ARG HB3 H 1.82 0.04 1 248 . 36 ARG HG2 H 1.73 0.04 1 249 . 36 ARG HG3 H 1.73 0.04 1 250 . 36 ARG HD2 H 3.22 0.04 1 251 . 36 ARG HD3 H 3.22 0.04 1 252 . 36 ARG CA C 56.10 0.50 1 253 . 36 ARG CB C 31.20 0.50 1 254 . 36 ARG CG C 27.20 0.50 1 255 . 36 ARG CD C 43.40 0.50 1 256 . 36 ARG N N 117.70 0.50 1 257 . 37 ILE H H 8.70 0.04 1 258 . 37 ILE HA H 4.33 0.04 1 259 . 37 ILE HB H 1.73 0.04 1 260 . 37 ILE HG12 H 1.63 0.04 1 261 . 37 ILE HG13 H 1.63 0.04 1 262 . 37 ILE HG2 H 1.12 0.04 1 263 . 37 ILE HD1 H 0.99 0.04 1 264 . 37 ILE CA C 58.90 0.50 1 265 . 37 ILE CB C 38.83 0.50 1 266 . 37 ILE CG1 C 27.15 0.50 1 267 . 37 ILE CG2 C 18.50 0.50 1 268 . 37 ILE CD1 C 12.93 0.50 1 269 . 37 ILE N N 125.54 0.50 1 270 . 38 PRO HA H 4.64 0.04 1 271 . 38 PRO HB2 H 2.41 0.04 2 272 . 38 PRO HB3 H 2.27 0.04 2 273 . 38 PRO HG2 H 1.95 0.04 2 274 . 38 PRO HG3 H 1.87 0.04 2 275 . 38 PRO HD2 H 3.58 0.04 2 276 . 38 PRO HD3 H 3.52 0.04 2 277 . 38 PRO CA C 62.69 0.50 1 278 . 38 PRO CB C 30.20 0.50 1 279 . 38 PRO CG C 24.75 0.50 1 280 . 38 PRO CD C 50.55 0.50 1 281 . 39 TYR H H 8.48 0.04 1 282 . 39 TYR HA H 4.59 0.04 1 283 . 39 TYR HB2 H 2.57 0.04 1 284 . 39 TYR HB3 H 2.57 0.04 1 285 . 39 TYR CA C 57.60 0.50 1 286 . 39 TYR CB C 40.20 0.50 1 287 . 39 TYR N N 118.00 0.50 1 288 . 40 LEU H H 8.52 0.04 1 289 . 40 LEU HA H 4.60 0.04 1 290 . 40 LEU HB2 H 1.62 0.04 1 291 . 40 LEU HB3 H 1.62 0.04 1 292 . 40 LEU HG H 1.77 0.04 1 293 . 40 LEU HD1 H 0.98 0.04 2 294 . 40 LEU HD2 H 0.94 0.04 2 295 . 40 LEU CA C 53.80 0.50 1 296 . 40 LEU CB C 41.60 0.50 1 297 . 40 LEU CG C 27.60 0.50 1 298 . 40 LEU CD1 C 25.10 0.50 1 299 . 40 LEU CD2 C 23.09 0.50 1 300 . 40 LEU N N 123.00 0.50 1 301 . 41 GLY H H 9.07 0.04 1 302 . 41 GLY HA2 H 4.04 0.04 2 303 . 41 GLY HA3 H 3.72 0.04 2 304 . 41 GLY CA C 47.40 0.50 1 305 . 41 GLY N N 115.70 0.50 1 306 . 42 PHE H H 8.72 0.04 1 307 . 42 PHE HA H 4.44 0.04 1 308 . 42 PHE HB2 H 3.49 0.04 2 309 . 42 PHE HB3 H 3.26 0.04 2 310 . 42 PHE HD1 H 7.33 0.04 1 311 . 42 PHE HD2 H 7.33 0.04 1 312 . 42 PHE HE1 H 7.40 0.04 1 313 . 42 PHE HE2 H 7.40 0.04 1 314 . 42 PHE CA C 59.14 0.50 1 315 . 42 PHE CB C 38.03 0.50 1 316 . 42 PHE N N 116.41 0.50 1 317 . 43 LYS H H 7.68 0.04 1 318 . 43 LYS HA H 4.70 0.04 1 319 . 43 LYS HB2 H 1.76 0.04 1 320 . 43 LYS HB3 H 1.76 0.04 1 321 . 43 LYS HG2 H 1.42 0.04 1 322 . 43 LYS HG3 H 1.42 0.04 1 323 . 43 LYS HD2 H 1.72 0.04 2 324 . 43 LYS HD3 H 1.86 0.04 2 325 . 43 LYS HE2 H 3.09 0.04 1 326 . 43 LYS HE3 H 3.09 0.04 1 327 . 43 LYS CA C 55.30 0.50 1 328 . 43 LYS CB C 28.66 0.50 1 329 . 43 LYS CG C 24.62 0.50 1 330 . 43 LYS CD C 35.08 0.50 1 331 . 43 LYS CE C 41.80 0.50 1 332 . 43 LYS N N 119.71 0.50 1 333 . 44 GLN H H 8.72 0.04 1 334 . 44 GLN HA H 3.58 0.04 1 335 . 44 GLN HB2 H 1.64 0.04 1 336 . 44 GLN HB3 H 1.64 0.04 1 337 . 44 GLN HG2 H 1.94 0.04 2 338 . 44 GLN HG3 H 1.65 0.04 2 339 . 44 GLN HE21 H 7.16 0.04 2 340 . 44 GLN HE22 H 6.38 0.04 2 341 . 44 GLN CA C 56.60 0.50 1 342 . 44 GLN CB C 29.70 0.50 1 343 . 44 GLN CG C 34.77 0.50 1 344 . 44 GLN N N 126.53 0.50 1 345 . 44 GLN NE2 N 108.65 0.50 1 346 . 45 ILE H H 8.04 0.04 1 347 . 45 ILE HA H 3.75 0.04 1 348 . 45 ILE HB H 1.55 0.04 1 349 . 45 ILE HG12 H 1.50 0.04 1 350 . 45 ILE HG13 H 1.50 0.04 1 351 . 45 ILE HG2 H 0.86 0.04 1 352 . 45 ILE HD1 H 0.58 0.04 1 353 . 45 ILE CA C 63.70 0.50 1 354 . 45 ILE CB C 39.80 0.50 1 355 . 45 ILE CG1 C 27.15 0.50 1 356 . 45 ILE CG2 C 18.00 0.50 1 357 . 45 ILE CD1 C 13.90 0.50 1 358 . 45 ILE N N 125.55 0.50 1 359 . 46 ASN H H 7.86 0.04 1 360 . 46 ASN HA H 3.90 0.04 1 361 . 46 ASN HB2 H 3.32 0.04 1 362 . 46 ASN HB3 H 3.32 0.04 1 363 . 46 ASN HD21 H 7.58 0.04 1 364 . 46 ASN HD22 H 6.86 0.04 1 365 . 46 ASN CA C 62.30 0.50 1 366 . 46 ASN CB C 37.16 0.50 1 367 . 46 ASN N N 120.50 0.50 1 368 . 46 ASN ND2 N 111.73 0.50 1 369 . 47 LEU H H 8.96 0.04 1 370 . 47 LEU HA H 4.00 0.04 1 371 . 47 LEU HB2 H 2.06 0.04 1 372 . 47 LEU HB3 H 2.06 0.04 1 373 . 47 LEU HG H 1.95 0.04 1 374 . 47 LEU HD1 H 1.06 0.04 2 375 . 47 LEU HD2 H 0.92 0.04 2 376 . 47 LEU CA C 58.30 0.50 1 377 . 47 LEU CB C 42.40 0.50 1 378 . 47 LEU CG C 27.15 0.50 1 379 . 47 LEU CD1 C 26.14 0.50 1 380 . 47 LEU CD2 C 23.60 0.50 1 381 . 47 LEU N N 126.15 0.50 1 382 . 48 TRP H H 8.28 0.04 1 383 . 48 TRP HA H 4.50 0.04 1 384 . 48 TRP HB2 H 3.28 0.04 1 385 . 48 TRP HB3 H 3.28 0.04 1 386 . 48 TRP HE1 H 9.97 0.04 1 387 . 48 TRP CA C 59.10 0.50 1 388 . 48 TRP CB C 43.02 0.50 1 389 . 48 TRP N N 118.60 0.50 1 390 . 48 TRP NE1 N 128.69 0.50 1 391 . 49 THR H H 8.17 0.04 1 392 . 49 THR HA H 3.58 0.04 1 393 . 49 THR HB H 4.13 0.04 1 394 . 49 THR HG2 H 1.20 0.04 1 395 . 49 THR CA C 66.78 0.50 1 396 . 49 THR CB C 68.60 0.50 1 397 . 49 THR CG2 C 22.57 0.50 1 398 . 49 THR N N 115.90 0.50 1 399 . 50 MET H H 8.47 0.04 1 400 . 50 MET HA H 3.84 0.04 1 401 . 50 MET HB2 H 2.16 0.04 1 402 . 50 MET HB3 H 2.16 0.04 1 403 . 50 MET HG2 H 2.61 0.04 1 404 . 50 MET HG3 H 2.61 0.04 1 405 . 50 MET HE H 2.30 0.04 1 406 . 50 MET CA C 61.40 0.50 1 407 . 50 MET CB C 28.68 0.50 1 408 . 50 MET CG C 37.31 0.50 1 409 . 50 MET CE C 20.04 0.50 1 410 . 50 MET N N 120.17 0.50 1 411 . 51 PHE H H 8.48 0.04 1 412 . 51 PHE HA H 4.52 0.04 1 413 . 51 PHE HB2 H 3.35 0.04 2 414 . 51 PHE HB3 H 2.84 0.04 2 415 . 51 PHE CA C 62.50 0.50 1 416 . 51 PHE CB C 40.30 0.50 1 417 . 51 PHE N N 118.46 0.50 1 418 . 52 GLN H H 8.70 0.04 1 419 . 52 GLN HA H 3.36 0.04 1 420 . 52 GLN HB2 H 1.05 0.04 1 421 . 52 GLN HB3 H 1.05 0.04 1 422 . 52 GLN HG2 H 1.42 0.04 2 423 . 52 GLN HG3 H 1.34 0.04 2 424 . 52 GLN HE21 H 6.63 0.04 2 425 . 52 GLN HE22 H 5.86 0.04 2 426 . 52 GLN CA C 58.63 0.50 1 427 . 52 GLN CB C 32.70 0.50 1 428 . 52 GLN CG C 29.18 0.50 1 429 . 52 GLN N N 117.70 0.50 1 430 . 52 GLN NE2 N 110.79 0.50 1 431 . 53 ALA H H 8.48 0.04 1 432 . 53 ALA HA H 3.94 0.04 1 433 . 53 ALA HB H 1.37 0.04 1 434 . 53 ALA CA C 55.10 0.50 1 435 . 53 ALA CB C 17.70 0.50 1 436 . 53 ALA N N 121.65 0.50 1 437 . 54 ALA H H 7.78 0.04 1 438 . 54 ALA HA H 3.89 0.04 1 439 . 54 ALA HB H 1.40 0.04 1 440 . 54 ALA CA C 54.00 0.50 1 441 . 54 ALA CB C 19.50 0.50 1 442 . 54 ALA N N 117.70 0.50 1 443 . 55 GLN H H 8.38 0.04 1 444 . 55 GLN HA H 3.63 0.04 1 445 . 55 GLN HB2 H 1.84 0.04 1 446 . 55 GLN HB3 H 1.84 0.04 1 447 . 55 GLN HG2 H 1.64 0.04 2 448 . 55 GLN HG3 H 1.54 0.04 2 449 . 55 GLN HE21 H 6.91 0.04 2 450 . 55 GLN HE22 H 6.44 0.04 2 451 . 55 GLN CA C 58.55 0.50 1 452 . 55 GLN CB C 27.52 0.50 1 453 . 55 GLN CG C 33.20 0.50 1 454 . 55 GLN N N 118.65 0.50 1 455 . 55 GLN NE2 N 113.73 0.50 1 456 . 56 LYS H H 7.68 0.04 1 457 . 56 LYS HA H 3.95 0.04 1 458 . 56 LYS HB2 H 1.79 0.04 1 459 . 56 LYS HB3 H 1.79 0.04 1 460 . 56 LYS HG2 H 1.47 0.04 1 461 . 56 LYS HG3 H 1.47 0.04 1 462 . 56 LYS HD2 H 1.76 0.04 1 463 . 56 LYS HD3 H 1.76 0.04 1 464 . 56 LYS HE2 H 3.00 0.04 1 465 . 56 LYS HE3 H 3.00 0.04 1 466 . 56 LYS CA C 58.80 0.50 1 467 . 56 LYS CB C 31.80 0.50 1 468 . 56 LYS CG C 25.10 0.50 1 469 . 56 LYS CD C 29.10 0.50 1 470 . 56 LYS CE C 42.10 0.50 1 471 . 56 LYS N N 120.17 0.50 1 472 . 57 LEU H H 6.72 0.04 1 473 . 57 LEU HA H 4.28 0.04 1 474 . 57 LEU HB2 H 1.53 0.04 2 475 . 57 LEU HB3 H 1.39 0.04 2 476 . 57 LEU HG H 1.55 0.04 1 477 . 57 LEU HD1 H 0.60 0.04 1 478 . 57 LEU HD2 H 0.60 0.04 1 479 . 57 LEU CA C 54.30 0.50 1 480 . 57 LEU CB C 42.12 0.50 1 481 . 57 LEU CG C 26.64 0.50 1 482 . 57 LEU CD1 C 25.10 0.50 1 483 . 57 LEU CD2 C 22.59 0.50 1 484 . 57 LEU N N 116.35 0.50 1 485 . 58 GLY H H 7.32 0.04 1 486 . 58 GLY HA2 H 4.38 0.04 2 487 . 58 GLY HA3 H 3.65 0.04 2 488 . 58 GLY CA C 45.56 0.50 1 489 . 58 GLY N N 103.88 0.50 1 490 . 59 GLY H H 7.97 0.04 1 491 . 59 GLY HA2 H 4.48 0.04 1 492 . 59 GLY HA3 H 4.48 0.04 1 493 . 59 GLY CA C 44.76 0.50 1 494 . 59 GLY N N 108.66 0.50 1 495 . 60 TYR H H 9.63 0.04 1 496 . 60 TYR HA H 3.83 0.04 1 497 . 60 TYR HB2 H 3.14 0.04 2 498 . 60 TYR HB3 H 3.06 0.04 2 499 . 60 TYR CA C 63.33 0.50 1 500 . 60 TYR CB C 41.60 0.50 1 501 . 60 TYR N N 118.90 0.50 1 502 . 61 GLU H H 9.44 0.04 1 503 . 61 GLU HA H 3.83 0.04 1 504 . 61 GLU HB2 H 2.16 0.04 2 505 . 61 GLU HB3 H 2.02 0.04 2 506 . 61 GLU HG2 H 2.36 0.04 1 507 . 61 GLU HG3 H 2.36 0.04 1 508 . 61 GLU CA C 60.60 0.50 1 509 . 61 GLU CB C 28.32 0.50 1 510 . 61 GLU CG C 33.25 0.50 1 511 . 61 GLU N N 120.71 0.50 1 512 . 62 THR H H 8.00 0.04 1 513 . 62 THR HA H 3.87 0.04 1 514 . 62 THR HB H 3.85 0.04 1 515 . 62 THR HG2 H 1.19 0.04 1 516 . 62 THR CA C 66.60 0.50 1 517 . 62 THR CB C 68.60 0.50 1 518 . 62 THR CG2 C 22.10 0.50 1 519 . 62 THR N N 118.90 0.50 1 520 . 63 ILE H H 7.96 0.04 1 521 . 63 ILE HA H 3.12 0.04 1 522 . 63 ILE HB H 0.53 0.04 1 523 . 63 ILE HG12 H 1.27 0.04 2 524 . 63 ILE HG13 H 0.16 0.04 2 525 . 63 ILE HG2 H -1.34 0.04 1 526 . 63 ILE HD1 H 0.15 0.04 1 527 . 63 ILE CA C 64.70 0.50 1 528 . 63 ILE CB C 38.70 0.50 1 529 . 63 ILE CG1 C 29.20 0.50 1 530 . 63 ILE CG2 C 14.90 0.50 1 531 . 63 ILE CD1 C 14.50 0.50 1 532 . 63 ILE N N 121.65 0.50 1 533 . 64 THR H H 7.83 0.04 1 534 . 64 THR HA H 4.03 0.04 1 535 . 64 THR HB H 4.03 0.04 1 536 . 64 THR HG2 H 1.28 0.04 1 537 . 64 THR CA C 67.00 0.50 1 538 . 64 THR CB C 68.60 0.50 1 539 . 64 THR CG2 C 21.08 0.50 1 540 . 64 THR N N 114.90 0.50 1 541 . 65 ALA H H 8.24 0.04 1 542 . 65 ALA HA H 4.11 0.04 1 543 . 65 ALA HB H 1.55 0.04 1 544 . 65 ALA CA C 55.90 0.50 1 545 . 65 ALA CB C 17.90 0.50 1 546 . 65 ALA N N 125.52 0.50 1 547 . 66 ARG H H 8.05 0.04 1 548 . 66 ARG HA H 4.20 0.04 1 549 . 66 ARG HB2 H 1.52 0.04 1 550 . 66 ARG HB3 H 1.52 0.04 1 551 . 66 ARG HG2 H 1.73 0.04 1 552 . 66 ARG HG3 H 1.73 0.04 1 553 . 66 ARG HD2 H 3.00 0.04 1 554 . 66 ARG HD3 H 3.00 0.04 1 555 . 66 ARG CA C 56.60 0.50 1 556 . 66 ARG CB C 29.90 0.50 1 557 . 66 ARG CG C 29.20 0.50 1 558 . 66 ARG CD C 41.88 0.50 1 559 . 66 ARG N N 113.70 0.50 1 560 . 67 ARG H H 7.82 0.04 1 561 . 67 ARG HA H 4.26 0.04 1 562 . 67 ARG HB2 H 2.15 0.04 2 563 . 67 ARG HB3 H 1.99 0.04 2 564 . 67 ARG HG2 H 1.69 0.04 1 565 . 67 ARG HG3 H 1.69 0.04 1 566 . 67 ARG HD2 H 3.31 0.04 1 567 . 67 ARG HD3 H 3.31 0.04 1 568 . 67 ARG CA C 57.40 0.50 1 569 . 67 ARG CB C 26.60 0.50 1 570 . 67 ARG CG C 27.50 0.50 1 571 . 67 ARG CD C 43.38 0.50 1 572 . 67 ARG N N 117.60 0.50 1 573 . 68 GLN H H 8.12 0.04 1 574 . 68 GLN HA H 4.65 0.04 1 575 . 68 GLN HB2 H 1.74 0.04 1 576 . 68 GLN HB3 H 1.74 0.04 1 577 . 68 GLN HG2 H 2.25 0.04 1 578 . 68 GLN HG3 H 2.25 0.04 1 579 . 68 GLN HE21 H 7.55 0.04 2 580 . 68 GLN HE22 H 6.94 0.04 2 581 . 68 GLN CA C 55.37 0.50 1 582 . 68 GLN CB C 29.10 0.50 1 583 . 68 GLN CG C 32.67 0.50 1 584 . 68 GLN N N 115.37 0.50 1 585 . 68 GLN NE2 N 112.55 0.50 1 586 . 69 TRP H H 7.99 0.04 1 587 . 69 TRP HA H 4.04 0.04 1 588 . 69 TRP HB2 H 3.46 0.04 1 589 . 69 TRP HB3 H 3.46 0.04 1 590 . 69 TRP HE1 H 10.01 0.04 1 591 . 69 TRP CA C 61.70 0.50 1 592 . 69 TRP CB C 28.70 0.50 1 593 . 69 TRP N N 120.90 0.50 1 594 . 69 TRP NE1 N 128.69 0.50 1 595 . 70 LYS H H 9.07 0.04 1 596 . 70 LYS HA H 4.00 0.04 1 597 . 70 LYS HB2 H 2.01 0.04 1 598 . 70 LYS HB3 H 2.01 0.04 1 599 . 70 LYS HG2 H 1.58 0.04 1 600 . 70 LYS HG3 H 1.58 0.04 1 601 . 70 LYS HD2 H 1.84 0.04 1 602 . 70 LYS HD3 H 1.84 0.04 1 603 . 70 LYS HE2 H 3.01 0.04 1 604 . 70 LYS HE3 H 3.01 0.04 1 605 . 70 LYS CA C 59.30 0.50 1 606 . 70 LYS CB C 32.20 0.50 1 607 . 70 LYS CG C 25.12 0.50 1 608 . 70 LYS CD C 32.20 0.50 1 609 . 70 LYS CE C 41.90 0.50 1 610 . 70 LYS N N 119.50 0.50 1 611 . 71 HIS H H 7.68 0.04 1 612 . 71 HIS HA H 4.48 0.04 1 613 . 71 HIS HB2 H 3.28 0.04 1 614 . 71 HIS HB3 H 3.28 0.04 1 615 . 71 HIS HD2 H 6.92 0.04 1 616 . 71 HIS HE1 H 8.25 0.04 1 617 . 71 HIS CA C 59.30 0.50 1 618 . 71 HIS CB C 28.00 0.50 1 619 . 71 HIS N N 116.60 0.50 1 620 . 72 ILE H H 7.18 0.04 1 621 . 72 ILE HA H 3.67 0.04 1 622 . 72 ILE HB H 2.63 0.04 1 623 . 72 ILE HG12 H 1.25 0.04 1 624 . 72 ILE HG13 H 1.25 0.04 1 625 . 72 ILE HG2 H 1.06 0.04 1 626 . 72 ILE HD1 H 0.50 0.04 1 627 . 72 ILE CA C 62.70 0.50 1 628 . 72 ILE CB C 36.00 0.50 1 629 . 72 ILE CG1 C 27.15 0.50 1 630 . 72 ILE CG2 C 17.50 0.50 1 631 . 72 ILE CD1 C 9.88 0.50 1 632 . 72 ILE N N 117.60 0.50 1 633 . 73 TYR H H 7.84 0.04 1 634 . 73 TYR HA H 3.91 0.04 1 635 . 73 TYR HB2 H 3.59 0.04 2 636 . 73 TYR HB3 H 3.36 0.04 2 637 . 73 TYR CA C 62.50 0.50 1 638 . 73 TYR CB C 37.07 0.50 1 639 . 73 TYR N N 120.66 0.50 1 640 . 74 ASP H H 8.69 0.04 1 641 . 74 ASP HA H 4.33 0.04 1 642 . 74 ASP HB2 H 2.73 0.04 1 643 . 74 ASP HB3 H 2.73 0.04 1 644 . 74 ASP CA C 56.96 0.50 1 645 . 74 ASP CB C 40.30 0.50 1 646 . 74 ASP N N 119.50 0.50 1 647 . 75 GLU H H 8.01 0.04 1 648 . 75 GLU HA H 4.07 0.04 1 649 . 75 GLU HB2 H 2.12 0.04 2 650 . 75 GLU HB3 H 2.00 0.04 2 651 . 75 GLU HG2 H 2.20 0.04 1 652 . 75 GLU HG3 H 2.20 0.04 1 653 . 75 GLU CA C 59.35 0.50 1 654 . 75 GLU CB C 29.30 0.50 1 655 . 75 GLU CG C 35.70 0.50 1 656 . 75 GLU N N 121.90 0.50 1 657 . 76 LEU H H 7.74 0.04 1 658 . 76 LEU HA H 4.24 0.04 1 659 . 76 LEU HB2 H 1.84 0.04 1 660 . 76 LEU HB3 H 1.84 0.04 1 661 . 76 LEU HG H 1.93 0.04 1 662 . 76 LEU HD1 H 0.95 0.04 2 663 . 76 LEU HD2 H 0.93 0.04 2 664 . 76 LEU CA C 55.30 0.50 1 665 . 76 LEU CB C 41.80 0.50 1 666 . 76 LEU CG C 27.66 0.50 1 667 . 76 LEU CD1 C 26.50 0.50 1 668 . 76 LEU CD2 C 23.09 0.50 1 669 . 76 LEU N N 117.40 0.50 1 670 . 77 GLY H H 7.70 0.04 1 671 . 77 GLY HA2 H 4.01 0.04 2 672 . 77 GLY HA3 H 3.77 0.04 2 673 . 77 GLY CA C 45.80 0.50 1 674 . 77 GLY N N 105.28 0.50 1 675 . 78 GLY H H 7.71 0.04 1 676 . 78 GLY HA2 H 3.54 0.04 2 677 . 78 GLY HA3 H 2.42 0.04 2 678 . 78 GLY CA C 45.00 0.50 1 679 . 78 GLY N N 106.27 0.50 1 680 . 79 ASN H H 8.47 0.04 1 681 . 79 ASN HA H 4.32 0.04 1 682 . 79 ASN HB2 H 2.80 0.04 2 683 . 79 ASN HB3 H 2.66 0.04 2 684 . 79 ASN HD21 H 7.69 0.04 2 685 . 79 ASN HD22 H 6.99 0.04 2 686 . 79 ASN CA C 57.10 0.50 1 687 . 79 ASN CB C 39.30 0.50 1 688 . 79 ASN N N 120.80 0.50 1 689 . 79 ASN ND2 N 112.85 0.50 1 690 . 80 PRO HA H 4.69 0.04 1 691 . 80 PRO HB2 H 2.45 0.04 2 692 . 80 PRO HB3 H 2.04 0.04 2 693 . 80 PRO HG2 H 2.10 0.04 1 694 . 80 PRO HG3 H 2.10 0.04 1 695 . 80 PRO HD2 H 4.03 0.04 2 696 . 80 PRO HD3 H 3.79 0.04 2 697 . 80 PRO CA C 64.40 0.50 1 698 . 80 PRO CB C 32.83 0.50 1 699 . 80 PRO CG C 27.70 0.50 1 700 . 80 PRO CD C 51.00 0.50 1 701 . 81 GLY H H 8.65 0.04 1 702 . 81 GLY HA2 H 3.95 0.04 1 703 . 81 GLY HA3 H 3.95 0.04 1 704 . 81 GLY CA C 45.30 0.50 1 705 . 81 GLY N N 107.76 0.50 1 706 . 82 SER H H 7.58 0.04 1 707 . 82 SER HA H 4.64 0.04 1 708 . 82 SER HB2 H 3.98 0.04 2 709 . 82 SER HB3 H 3.80 0.04 2 710 . 82 SER CA C 57.90 0.50 1 711 . 82 SER CB C 64.20 0.50 1 712 . 82 SER N N 114.40 0.50 1 713 . 83 THR H H 8.83 0.04 1 714 . 83 THR HA H 4.27 0.04 1 715 . 83 THR HB H 4.38 0.04 1 716 . 83 THR HG2 H 1.33 0.04 1 717 . 83 THR CA C 63.60 0.50 1 718 . 83 THR CB C 68.90 0.50 1 719 . 83 THR CG2 C 21.57 0.50 1 720 . 83 THR N N 120.05 0.50 1 721 . 84 SER H H 8.26 0.04 1 722 . 84 SER HA H 4.60 0.04 1 723 . 84 SER HB2 H 4.06 0.04 2 724 . 84 SER HB3 H 3.95 0.04 2 725 . 84 SER CA C 58.30 0.50 1 726 . 84 SER CB C 63.60 0.50 1 727 . 84 SER N N 115.60 0.50 1 728 . 85 ALA H H 7.12 0.04 1 729 . 85 ALA HA H 3.55 0.04 1 730 . 85 ALA HB H 0.36 0.04 1 731 . 85 ALA CA C 55.60 0.50 1 732 . 85 ALA CB C 17.50 0.50 1 733 . 85 ALA N N 123.89 0.50 1 734 . 86 ALA H H 8.77 0.04 1 735 . 86 ALA HA H 3.77 0.04 1 736 . 86 ALA HB H 1.57 0.04 1 737 . 86 ALA CA C 56.40 0.50 1 738 . 86 ALA CB C 19.00 0.50 1 739 . 86 ALA N N 121.91 0.50 1 740 . 87 THR H H 8.02 0.04 1 741 . 87 THR HA H 3.77 0.04 1 742 . 87 THR HB H 4.09 0.04 1 743 . 87 THR HG2 H 1.20 0.04 1 744 . 87 THR CA C 66.78 0.50 1 745 . 87 THR CB C 68.90 0.50 1 746 . 87 THR CG2 C 21.57 0.50 1 747 . 87 THR N N 115.20 0.50 1 748 . 88 CYS H H 8.58 0.04 1 749 . 88 CYS HA H 4.46 0.04 1 750 . 88 CYS HB2 H 3.46 0.04 2 751 . 88 CYS HB3 H 3.30 0.04 2 752 . 88 CYS CA C 58.90 0.50 1 753 . 88 CYS CB C 37.80 0.50 1 754 . 88 CYS N N 118.30 0.50 1 755 . 89 THR H H 8.04 0.04 1 756 . 89 THR HA H 3.77 0.04 1 757 . 89 THR HB H 4.40 0.04 1 758 . 89 THR HG2 H 1.58 0.04 1 759 . 89 THR CA C 68.78 0.50 1 760 . 89 THR CB C 67.77 0.50 1 761 . 89 THR CG2 C 22.08 0.50 1 762 . 89 THR N N 116.94 0.50 1 763 . 90 ARG H H 7.41 0.04 1 764 . 90 ARG HB2 H 2.06 0.04 1 765 . 90 ARG HB3 H 2.06 0.04 1 766 . 90 ARG CA C 59.60 0.50 1 767 . 90 ARG CB C 29.60 0.50 1 768 . 90 ARG N N 121.50 0.50 1 769 . 91 ARG H H 7.93 0.04 1 770 . 91 ARG HA H 3.97 0.04 1 771 . 91 ARG HB2 H 1.96 0.04 1 772 . 91 ARG HB3 H 1.96 0.04 1 773 . 91 ARG HG2 H 1.72 0.04 1 774 . 91 ARG HG3 H 1.72 0.04 1 775 . 91 ARG HD2 H 3.03 0.04 1 776 . 91 ARG HD3 H 3.03 0.04 1 777 . 91 ARG CA C 59.35 0.50 1 778 . 91 ARG CB C 28.60 0.50 1 779 . 91 ARG CG C 29.60 0.50 1 780 . 91 ARG CD C 41.70 0.50 1 781 . 91 ARG N N 117.10 0.50 1 782 . 92 HIS H H 8.16 0.04 1 783 . 92 HIS HA H 4.67 0.04 1 784 . 92 HIS HB2 H 2.88 0.04 1 785 . 92 HIS HB3 H 2.88 0.04 1 786 . 92 HIS CA C 59.60 0.50 1 787 . 92 HIS CB C 30.40 0.50 1 788 . 92 HIS N N 117.10 0.50 1 789 . 93 TYR H H 8.59 0.04 1 790 . 93 TYR HA H 3.99 0.04 1 791 . 93 TYR HB2 H 3.26 0.04 2 792 . 93 TYR HB3 H 3.12 0.04 2 793 . 93 TYR CA C 63.30 0.50 1 794 . 93 TYR CB C 39.85 0.50 1 795 . 93 TYR N N 121.65 0.50 1 796 . 94 GLU H H 8.99 0.04 1 797 . 94 GLU HA H 3.94 0.04 1 798 . 94 GLU HB2 H 1.97 0.04 1 799 . 94 GLU HB3 H 1.97 0.04 1 800 . 94 GLU HG2 H 2.30 0.04 1 801 . 94 GLU HG3 H 2.30 0.04 1 802 . 94 GLU CA C 59.10 0.50 1 803 . 94 GLU CB C 29.90 0.50 1 804 . 94 GLU CG C 36.05 0.50 1 805 . 94 GLU N N 119.19 0.50 1 806 . 95 ARG H H 7.47 0.04 1 807 . 95 ARG HA H 4.23 0.04 1 808 . 95 ARG HB2 H 1.98 0.04 1 809 . 95 ARG HB3 H 1.98 0.04 1 810 . 95 ARG HG2 H 1.76 0.04 2 811 . 95 ARG HG3 H 1.69 0.04 2 812 . 95 ARG HD2 H 3.22 0.04 1 813 . 95 ARG HD3 H 3.22 0.04 1 814 . 95 ARG CA C 58.20 0.50 1 815 . 95 ARG CB C 31.80 0.50 1 816 . 95 ARG CG C 27.60 0.50 1 817 . 95 ARG CD C 43.32 0.50 1 818 . 95 ARG N N 114.40 0.50 1 819 . 96 LEU H H 8.12 0.04 1 820 . 96 LEU HA H 4.40 0.04 1 821 . 96 LEU HB2 H 1.36 0.04 1 822 . 96 LEU HB3 H 1.36 0.04 1 823 . 96 LEU HG H 1.75 0.04 1 824 . 96 LEU HD1 H 1.02 0.04 2 825 . 96 LEU HD2 H 0.97 0.04 2 826 . 96 LEU CA C 57.20 0.50 1 827 . 96 LEU CB C 44.90 0.50 1 828 . 96 LEU CG C 24.60 0.50 1 829 . 96 LEU CD1 C 25.10 0.50 1 830 . 96 LEU CD2 C 23.60 0.50 1 831 . 96 LEU N N 114.40 0.50 1 832 . 97 ILE H H 7.91 0.04 1 833 . 97 ILE HA H 4.34 0.04 1 834 . 97 ILE HB H 0.64 0.04 1 835 . 97 ILE HG12 H 1.33 0.04 1 836 . 97 ILE HG13 H 1.33 0.04 1 837 . 97 ILE HG2 H 1.16 0.04 1 838 . 97 ILE HD1 H 1.03 0.04 1 839 . 97 ILE CA C 60.20 0.50 1 840 . 97 ILE CB C 39.30 0.50 1 841 . 97 ILE CG1 C 28.68 0.50 1 842 . 97 ILE CG2 C 21.06 0.50 1 843 . 97 ILE CD1 C 12.90 0.50 1 844 . 97 ILE N N 113.40 0.50 1 845 . 98 LEU H H 8.04 0.04 1 846 . 98 LEU HA H 4.40 0.04 1 847 . 98 LEU HB2 H 1.24 0.04 1 848 . 98 LEU HB3 H 1.24 0.04 1 849 . 98 LEU HG H 1.45 0.04 1 850 . 98 LEU HD1 H 0.33 0.04 2 851 . 98 LEU HD2 H 0.89 0.04 2 852 . 98 LEU CA C 59.33 0.50 1 853 . 98 LEU CB C 41.37 0.50 1 854 . 98 LEU CG C 27.60 0.50 1 855 . 98 LEU CD1 C 25.12 0.50 1 856 . 98 LEU CD2 C 24.61 0.50 1 857 . 98 LEU N N 119.80 0.50 1 858 . 99 PRO HA H 4.31 0.04 1 859 . 99 PRO HB2 H 1.97 0.04 1 860 . 99 PRO HB3 H 1.97 0.04 1 861 . 99 PRO HG2 H 2.07 0.04 1 862 . 99 PRO HG3 H 2.07 0.04 1 863 . 99 PRO HD2 H 4.00 0.04 1 864 . 99 PRO HD3 H 4.00 0.04 1 865 . 99 PRO CA C 66.70 0.50 1 866 . 99 PRO CB C 32.23 0.50 1 867 . 99 PRO CG C 29.69 0.50 1 868 . 99 PRO CD C 51.02 0.50 1 869 . 100 TYR H H 8.08 0.04 1 870 . 100 TYR HA H 3.80 0.04 1 871 . 100 TYR HB2 H 3.05 0.04 2 872 . 100 TYR HB3 H 3.00 0.04 2 873 . 100 TYR CA C 61.20 0.50 1 874 . 100 TYR CB C 40.30 0.50 1 875 . 100 TYR N N 119.39 0.50 1 876 . 101 GLU H H 8.69 0.04 1 877 . 101 GLU HA H 3.86 0.04 1 878 . 101 GLU HB2 H 2.40 0.04 1 879 . 101 GLU HB3 H 2.40 0.04 1 880 . 101 GLU HG2 H 2.60 0.04 1 881 . 101 GLU HG3 H 2.60 0.04 1 882 . 101 GLU CA C 60.70 0.50 1 883 . 101 GLU CB C 30.70 0.50 1 884 . 101 GLU CG C 36.80 0.50 1 885 . 101 GLU N N 120.65 0.50 1 886 . 102 ARG H H 8.65 0.04 1 887 . 102 ARG HA H 3.99 0.04 1 888 . 102 ARG HB2 H 1.74 0.04 1 889 . 102 ARG HB3 H 1.74 0.04 1 890 . 102 ARG HG2 H 1.72 0.04 1 891 . 102 ARG HG3 H 1.72 0.04 1 892 . 102 ARG HD2 H 3.02 0.04 1 893 . 102 ARG HD3 H 3.02 0.04 1 894 . 102 ARG CA C 59.35 0.50 1 895 . 102 ARG CB C 30.40 0.50 1 896 . 102 ARG CG C 29.70 0.50 1 897 . 102 ARG CD C 41.80 0.50 1 898 . 102 ARG N N 115.45 0.50 1 899 . 103 PHE H H 7.87 0.04 1 900 . 103 PHE HA H 4.36 0.04 1 901 . 103 PHE HB2 H 3.11 0.04 2 902 . 103 PHE HB3 H 2.81 0.04 2 903 . 103 PHE CA C 60.40 0.50 1 904 . 103 PHE CB C 39.20 0.50 1 905 . 103 PHE N N 120.66 0.50 1 906 . 104 ILE H H 8.45 0.04 1 907 . 104 ILE HA H 3.55 0.04 1 908 . 104 ILE HB H 1.84 0.04 1 909 . 104 ILE HG12 H 1.36 0.04 2 910 . 104 ILE HG13 H 1.25 0.04 2 911 . 104 ILE HG2 H 0.61 0.04 1 912 . 104 ILE HD1 H 0.88 0.04 1 913 . 104 ILE CA C 63.60 0.50 1 914 . 104 ILE CB C 37.60 0.50 1 915 . 104 ILE CG1 C 26.64 0.50 1 916 . 104 ILE CG2 C 18.00 0.50 1 917 . 104 ILE CD1 C 13.45 0.50 1 918 . 104 ILE N N 117.10 0.50 1 919 . 105 LYS H H 7.57 0.04 1 920 . 105 LYS HA H 4.29 0.04 1 921 . 105 LYS HB2 H 2.06 0.04 2 922 . 105 LYS HB3 H 1.91 0.04 2 923 . 105 LYS HG2 H 1.46 0.04 1 924 . 105 LYS HG3 H 1.46 0.04 1 925 . 105 LYS HD2 H 1.73 0.04 1 926 . 105 LYS HD3 H 1.73 0.04 1 927 . 105 LYS HE2 H 3.03 0.04 1 928 . 105 LYS HE3 H 3.03 0.04 1 929 . 105 LYS CA C 57.20 0.50 1 930 . 105 LYS CB C 32.80 0.50 1 931 . 105 LYS CG C 25.12 0.50 1 932 . 105 LYS CD C 29.70 0.50 1 933 . 105 LYS CE C 42.00 0.50 1 934 . 105 LYS N N 119.64 0.50 1 935 . 106 GLY H H 7.77 0.04 1 936 . 106 GLY HA2 H 3.99 0.04 1 937 . 106 GLY HA3 H 3.99 0.04 1 938 . 106 GLY CA C 46.60 0.50 1 939 . 106 GLY N N 108.47 0.50 1 940 . 107 GLU H H 8.26 0.04 1 941 . 107 GLU HA H 4.46 0.04 1 942 . 107 GLU HB2 H 2.16 0.04 2 943 . 107 GLU HB3 H 1.84 0.04 2 944 . 107 GLU HG2 H 2.16 0.04 1 945 . 107 GLU HG3 H 2.16 0.04 1 946 . 107 GLU CA C 56.10 0.50 1 947 . 107 GLU CB C 30.70 0.50 1 948 . 107 GLU CG C 36.20 0.50 1 949 . 107 GLU N N 119.48 0.50 1 950 . 108 GLU H H 8.49 0.04 1 951 . 108 GLU HA H 4.23 0.04 1 952 . 108 GLU HB2 H 2.08 0.04 1 953 . 108 GLU HB3 H 2.08 0.04 1 954 . 108 GLU HG2 H 2.38 0.04 2 955 . 108 GLU HG3 H 2.31 0.04 2 956 . 108 GLU CA C 56.96 0.50 1 957 . 108 GLU CB C 30.70 0.50 1 958 . 108 GLU CG C 36.40 0.50 1 959 . 108 GLU N N 120.71 0.50 1 960 . 109 ASP H H 8.52 0.04 1 961 . 109 ASP HA H 4.65 0.04 1 962 . 109 ASP HB2 H 2.74 0.04 2 963 . 109 ASP HB3 H 2.68 0.04 2 964 . 109 ASP CA C 54.05 0.50 1 965 . 109 ASP CB C 41.30 0.50 1 966 . 109 ASP N N 120.71 0.50 1 967 . 110 LYS H H 7.92 0.04 1 968 . 110 LYS HA H 4.68 0.04 1 969 . 110 LYS HB2 H 1.85 0.04 2 970 . 110 LYS HB3 H 1.77 0.04 2 971 . 110 LYS HG2 H 1.50 0.04 1 972 . 110 LYS HG3 H 1.50 0.04 1 973 . 110 LYS HD2 H 1.72 0.04 1 974 . 110 LYS HD3 H 1.72 0.04 1 975 . 110 LYS HE2 H 3.03 0.04 1 976 . 110 LYS HE3 H 3.03 0.04 1 977 . 110 LYS CA C 54.05 0.50 1 978 . 110 LYS CB C 32.80 0.50 1 979 . 110 LYS CG C 24.60 0.50 1 980 . 110 LYS CD C 29.00 0.50 1 981 . 110 LYS CE C 42.00 0.50 1 982 . 110 LYS N N 122.90 0.50 1 983 . 111 PRO HA H 4.45 0.04 1 984 . 111 PRO HB2 H 2.29 0.04 2 985 . 111 PRO HB3 H 1.88 0.04 2 986 . 111 PRO HG2 H 2.02 0.04 1 987 . 111 PRO HG3 H 2.02 0.04 1 988 . 111 PRO HD2 H 3.86 0.04 2 989 . 111 PRO HD3 H 3.66 0.04 2 990 . 111 PRO CA C 63.00 0.50 1 991 . 111 PRO CB C 31.90 0.50 1 992 . 111 PRO CG C 27.50 0.50 1 993 . 111 PRO CD C 50.40 0.50 1 994 . 112 LEU H H 8.46 0.04 1 995 . 112 LEU HA H 4.63 0.04 1 996 . 112 LEU HB2 H 1.60 0.04 1 997 . 112 LEU HB3 H 1.60 0.04 1 998 . 112 LEU HG H 1.71 0.04 1 999 . 112 LEU HD1 H 0.97 0.04 2 1000 . 112 LEU HD2 H 0.94 0.04 2 1001 . 112 LEU CA C 53.25 0.50 1 1002 . 112 LEU CB C 41.90 0.50 1 1003 . 112 LEU CG C 29.10 0.50 1 1004 . 112 LEU CD1 C 25.10 0.50 1 1005 . 112 LEU CD2 C 23.60 0.50 1 1006 . 112 LEU N N 124.56 0.50 1 1007 . 113 PRO HA H 4.73 0.04 1 1008 . 113 PRO HB2 H 2.37 0.04 2 1009 . 113 PRO HB3 H 1.88 0.04 2 1010 . 113 PRO HG2 H 2.05 0.04 1 1011 . 113 PRO HG3 H 2.05 0.04 1 1012 . 113 PRO HD2 H 3.87 0.04 2 1013 . 113 PRO HD3 H 3.64 0.04 2 1014 . 113 PRO CA C 61.20 0.50 1 1015 . 113 PRO CB C 30.70 0.50 1 1016 . 113 PRO CG C 27.30 0.50 1 1017 . 113 PRO CD C 50.40 0.50 1 1018 . 114 PRO HA H 4.48 0.04 1 1019 . 114 PRO HB2 H 2.28 0.04 2 1020 . 114 PRO HB3 H 1.88 0.04 2 1021 . 114 PRO HG2 H 2.03 0.04 1 1022 . 114 PRO HG3 H 2.03 0.04 1 1023 . 114 PRO HD2 H 3.84 0.04 2 1024 . 114 PRO HD3 H 3.67 0.04 2 1025 . 114 PRO CA C 62.80 0.50 1 1026 . 114 PRO CB C 32.30 0.50 1 1027 . 114 PRO CG C 27.40 0.50 1 1028 . 114 PRO CD C 50.40 0.50 1 1029 . 115 ILE H H 8.24 0.04 1 1030 . 115 ILE HA H 4.13 0.04 1 1031 . 115 ILE HB H 1.83 0.04 1 1032 . 115 ILE HG12 H 1.50 0.04 2 1033 . 115 ILE HG13 H 1.19 0.04 2 1034 . 115 ILE HG2 H 0.91 0.04 1 1035 . 115 ILE HD1 H 0.88 0.04 1 1036 . 115 ILE CA C 61.20 0.50 1 1037 . 115 ILE CB C 38.90 0.50 1 1038 . 115 ILE CG1 C 27.15 0.50 1 1039 . 115 ILE CG2 C 17.51 0.50 1 1040 . 115 ILE CD1 C 12.94 0.50 1 1041 . 115 ILE N N 121.31 0.50 1 1042 . 116 LYS H H 8.38 0.04 1 1043 . 116 LYS HA H 4.65 0.04 1 1044 . 116 LYS HB2 H 1.86 0.04 2 1045 . 116 LYS HB3 H 1.76 0.04 2 1046 . 116 LYS HG2 H 1.46 0.04 1 1047 . 116 LYS HG3 H 1.46 0.04 1 1048 . 116 LYS HD2 H 1.72 0.04 1 1049 . 116 LYS HD3 H 1.72 0.04 1 1050 . 116 LYS HE2 H 3.01 0.04 1 1051 . 116 LYS HE3 H 3.01 0.04 1 1052 . 116 LYS CA C 54.00 0.50 1 1053 . 116 LYS CB C 32.80 0.50 1 1054 . 116 LYS CG C 24.40 0.50 1 1055 . 116 LYS CD C 29.20 0.50 1 1056 . 116 LYS CE C 42.00 0.50 1 1057 . 116 LYS N N 126.73 0.50 1 1058 . 117 PRO HA H 4.44 0.04 1 1059 . 117 PRO HB2 H 2.32 0.04 2 1060 . 117 PRO HB3 H 1.88 0.04 2 1061 . 117 PRO HG2 H 2.03 0.04 1 1062 . 117 PRO HG3 H 2.03 0.04 1 1063 . 117 PRO HD2 H 3.85 0.04 2 1064 . 117 PRO HD3 H 3.65 0.04 2 1065 . 117 PRO CA C 63.10 0.50 1 1066 . 117 PRO CB C 32.00 0.50 1 1067 . 117 PRO CG C 27.50 0.50 1 1068 . 117 PRO CD C 50.80 0.50 1 1069 . 118 ARG H H 8.45 0.04 1 1070 . 118 ARG HA H 4.33 0.04 1 1071 . 118 ARG HB2 H 1.84 0.04 1 1072 . 118 ARG HB3 H 1.84 0.04 1 1073 . 118 ARG HD2 H 3.21 0.04 1 1074 . 118 ARG HD3 H 3.21 0.04 1 1075 . 118 ARG CA C 56.40 0.50 1 1076 . 118 ARG CB C 31.20 0.50 1 1077 . 118 ARG CG C 27.40 0.50 1 1078 . 118 ARG CD C 43.40 0.50 1 1079 . 118 ARG N N 121.65 0.50 1 1080 . 119 LYS H H 8.43 0.04 1 1081 . 119 LYS HA H 4.36 0.04 1 1082 . 119 LYS HB2 H 1.88 0.04 2 1083 . 119 LYS HB3 H 1.82 0.04 2 1084 . 119 LYS HD2 H 1.72 0.04 1 1085 . 119 LYS HD3 H 1.72 0.04 1 1086 . 119 LYS HE2 H 3.00 0.04 1 1087 . 119 LYS HE3 H 3.00 0.04 1 1088 . 119 LYS CA C 56.70 0.50 1 1089 . 119 LYS CB C 33.40 0.50 1 1090 . 119 LYS CG C 24.62 0.50 1 1091 . 119 LYS CD C 28.68 0.50 1 1092 . 119 LYS CE C 41.87 0.50 1 1093 . 119 LYS N N 123.60 0.50 1 stop_ save_