data_15424 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignment of Cdc42(T35A), and Active Switch I mutant of Cdc42 ; _BMRB_accession_number 15424 _BMRB_flat_file_name bmr15424.str _Entry_type original _Submission_date 2007-08-08 _Accession_date 2007-08-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '13N-15N backbone and sidechain assignments of the protein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oswald Robert E . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 700 "13C chemical shifts" 643 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-12 update BMRB 'added PubMed ID' 2008-01-30 update BMRB 'complete entry citation' 2007-08-16 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR assignment of Cdc42(T35A), an active Switch I mutant of Cdc42' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636871 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Adams Paul D. . 2 Oswald Robert E. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 225 _Page_last 227 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Cdc42(T35A) monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Cdc42(T35A) monomer' $Cdc42(T35A) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cdc42(T35A) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Cdc42(T35A) _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 178 _Mol_residue_sequence ; MQTIKCVVVGDGAVGKTCLL ISYTTNKFPSEYVPAVFDNY AVTVMIGGEPYTLGLFDTAG QEDYDRLRPLSYPQTDVFLV CFSVVSPSSFENVKEKWVPE ITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPE TAEKLARDLKAVKYVECSAL TQKGLKNVFDEAILAALE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 THR 4 ILE 5 LYS 6 CYS 7 VAL 8 VAL 9 VAL 10 GLY 11 ASP 12 GLY 13 ALA 14 VAL 15 GLY 16 LYS 17 THR 18 CYS 19 LEU 20 LEU 21 ILE 22 SER 23 TYR 24 THR 25 THR 26 ASN 27 LYS 28 PHE 29 PRO 30 SER 31 GLU 32 TYR 33 VAL 34 PRO 35 ALA 36 VAL 37 PHE 38 ASP 39 ASN 40 TYR 41 ALA 42 VAL 43 THR 44 VAL 45 MET 46 ILE 47 GLY 48 GLY 49 GLU 50 PRO 51 TYR 52 THR 53 LEU 54 GLY 55 LEU 56 PHE 57 ASP 58 THR 59 ALA 60 GLY 61 GLN 62 GLU 63 ASP 64 TYR 65 ASP 66 ARG 67 LEU 68 ARG 69 PRO 70 LEU 71 SER 72 TYR 73 PRO 74 GLN 75 THR 76 ASP 77 VAL 78 PHE 79 LEU 80 VAL 81 CYS 82 PHE 83 SER 84 VAL 85 VAL 86 SER 87 PRO 88 SER 89 SER 90 PHE 91 GLU 92 ASN 93 VAL 94 LYS 95 GLU 96 LYS 97 TRP 98 VAL 99 PRO 100 GLU 101 ILE 102 THR 103 HIS 104 HIS 105 CYS 106 PRO 107 LYS 108 THR 109 PRO 110 PHE 111 LEU 112 LEU 113 VAL 114 GLY 115 THR 116 GLN 117 ILE 118 ASP 119 LEU 120 ARG 121 ASP 122 ASP 123 PRO 124 SER 125 THR 126 ILE 127 GLU 128 LYS 129 LEU 130 ALA 131 LYS 132 ASN 133 LYS 134 GLN 135 LYS 136 PRO 137 ILE 138 THR 139 PRO 140 GLU 141 THR 142 ALA 143 GLU 144 LYS 145 LEU 146 ALA 147 ARG 148 ASP 149 LEU 150 LYS 151 ALA 152 VAL 153 LYS 154 TYR 155 VAL 156 GLU 157 CYS 158 SER 159 ALA 160 LEU 161 THR 162 GLN 163 LYS 164 GLY 165 LEU 166 LYS 167 ASN 168 VAL 169 PHE 170 ASP 171 GLU 172 ALA 173 ILE 174 LEU 175 ALA 176 ALA 177 LEU 178 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 BMRB 4700 Cdc42 100.00 185 98.88 98.88 2.01e-124 PDB 1A4R "G12v Mutant Of Human Placental Cdc42 Gtpase In The Gdp Form" 100.00 191 98.88 98.88 3.15e-124 PDB 1AJE "Cdc42 From Human, Nmr, 20 Structures" 100.00 194 99.44 99.44 6.07e-126 PDB 1AM4 "Complex Between Cdc42hs.Gmppnp And P50 Rhogap (H. Sapiens)" 98.88 177 98.86 99.43 8.86e-124 PDB 1AN0 "Cdc42hs-Gdp Complex" 99.44 190 98.87 98.87 2.48e-123 PDB 1CEE "Solution Structure Of Cdc42 In Complex With The Gtpase Binding Domain Of Wasp" 100.00 179 99.44 99.44 7.32e-126 PDB 1CF4 "Cdc42ACK GTPASE-Binding Domain Complex" 100.00 184 98.88 98.88 1.94e-124 PDB 1DOA "Structure Of The Rho Family Gtp-Binding Protein Cdc42 In Complex With The Multifunctional Regulator Rhogdi" 100.00 191 99.44 99.44 1.09e-125 PDB 1E0A "Cdc42 Complexed With The Gtpase Binding Domain Of P21 Activated Kinase" 100.00 184 98.88 98.88 1.94e-124 PDB 1EES "Solution Structure Of Cdc42hs Complexed With A Peptide Derived From P-21 Activated Kinase, Nmr, 20 Structures" 100.00 178 99.44 99.44 4.57e-126 PDB 1GRN "Crystal Structure Of The Cdc42CDC42GAPALF3 COMPLEX." 100.00 191 99.44 99.44 1.38e-125 PDB 1GZS "Crystal Structure Of The Complex Between The Gef Domain Of The Salmonella Typhimurium Sope Toxin And Human Cdc42" 100.00 180 99.44 99.44 4.90e-126 PDB 1KI1 "Guanine Nucleotide Exchange Region Of Intersectin In Complex With Cdc42" 100.00 188 99.44 99.44 7.46e-126 PDB 1KZ7 "Crystal Structure Of The DhPH FRAGMENT OF MURINE DBS IN Complex With The Placental Isoform Of Human Cdc42" 100.00 188 99.44 99.44 7.46e-126 PDB 1KZG Dbscdc42(Y889f) 100.00 188 99.44 99.44 7.46e-126 PDB 1NF3 "Structure Of Cdc42 In A Complex With The Gtpase-Binding Domain Of The Cell Polarity Protein, Par6" 100.00 195 98.31 98.88 1.64e-123 PDB 2ASE "Nmr Structure Of The F28l Mutant Of Cdc42hs" 100.00 178 98.88 98.88 3.13e-125 PDB 2DFK "Crystal Structure Of The Cdc42-Collybistin Ii Complex" 100.00 194 99.44 99.44 1.47e-125 PDB 2KB0 Cdc42(T35a) 100.00 178 100.00 100.00 9.36e-127 PDB 2NGR "Transition State Complex For Gtp Hydrolysis By Cdc42: Comparisons Of The High Resolution Structures For Cdc42 Bound To The Acti" 100.00 191 99.44 99.44 1.38e-125 PDB 2ODB "The Crystal Structure Of Human Cdc42 In Complex With The Crib Domain Of Human P21-Activated Kinase 6 (Pak6)" 100.00 192 99.44 99.44 1.11e-125 PDB 2QRZ "Cdc42 Bound To Gmp-Pcp: Induced Fit By Effector Is Required" 100.00 189 99.44 99.44 1.44e-125 PDB 2WM9 "Structure Of The Complex Between Dock9 And Cdc42." 100.00 190 99.44 99.44 1.46e-125 PDB 2WMN "Structure Of The Complex Between Dock9 And Cdc42-Gdp." 100.00 190 99.44 99.44 1.46e-125 PDB 2WMO "Structure Of The Complex Between Dock9 And Cdc42" 100.00 190 99.44 99.44 1.46e-125 PDB 3EG5 "Crystal Structure Of Mdia1-Tsh Gbd-Fh3 In Complex With Cdc42-Gmppnp" 100.00 178 98.88 99.44 9.30e-126 PDB 3GCG "Crystal Structure Of Map And Cdc42 Complex" 99.44 182 99.44 99.44 7.01e-125 PDB 3QBV "Structure Of Designed Orthogonal Interaction Between Cdc42 And Nucleotide Exchange Domains Of Intersectin" 100.00 178 98.88 98.88 8.65e-125 PDB 3VHL "Crystal Structure Of The Dhr-2 Domain Of Dock8 In Complex With Cdc42 (T17n Mutant)" 100.00 195 98.88 98.88 2.00e-125 PDB 4DID "Crystal Structure Of Salmonella Effector N-Terminal Domain Sopb In Complex With Cdc42" 100.00 193 99.44 99.44 7.13e-126 PDB 4ITR "Crystal Structure Of Ibpafic2-h3717a In Complex With Adenylylated Cdc42" 100.00 191 99.44 99.44 1.38e-125 PDB 4JS0 "Complex Of Cdc42 With The Crib-pr Domain Of Irsp53" 100.00 178 98.88 98.88 9.54e-125 PDB 4YC7 "Crystal Structure Of Human Fmnl2 Gbd-fh3 Domains Bound To Cdc42-gppnhp" 100.00 181 98.88 99.44 1.27e-125 PDB 4YDH "The Structure Of Human Fmnl1 N-terminal Domains Bound To Cdc42" 100.00 181 98.88 99.44 1.27e-125 DBJ BAB22563 "unnamed protein product [Mus musculus]" 100.00 191 99.44 99.44 1.38e-125 DBJ BAC16312 "Raichu-1054X [synthetic construct]" 98.31 762 98.86 99.43 8.00e-117 DBJ BAC34669 "unnamed protein product [Mus musculus]" 100.00 191 98.88 99.44 8.40e-125 DBJ BAC35825 "unnamed protein product [Mus musculus]" 100.00 191 99.44 99.44 1.38e-125 DBJ BAE01909 "unnamed protein product [Macaca fascicularis]" 100.00 191 98.88 99.44 5.03e-125 EMBL CAA90215 "CDC42 GTP-binding protein [Canis lupus familiaris]" 100.00 191 99.44 99.44 1.38e-125 EMBL CAB57325 "hypothetical protein [Homo sapiens]" 100.00 191 98.88 99.44 5.86e-125 EMBL CAB57326 "hypothetical protein [Homo sapiens]" 100.00 191 99.44 99.44 1.38e-125 EMBL CAB57327 "hypothetical protein [Homo sapiens]" 79.78 142 99.30 99.30 9.83e-99 EMBL CAB57328 "hypothetical protein [Homo sapiens]" 65.17 116 99.14 99.14 1.06e-78 GB AAA37410 "CDC42Mm, partial [Mus musculus]" 100.00 191 99.44 99.44 1.38e-125 GB AAA52494 "GTP-binding protein G25K [Homo sapiens]" 100.00 191 98.88 99.44 5.86e-125 GB AAA52592 "GTP-binding protein G25K [Homo sapiens]" 100.00 191 99.44 99.44 1.38e-125 GB AAB40051 "cdc42b [Mus musculus]" 100.00 191 98.88 99.44 5.86e-125 GB AAC00027 "CDC42 [Gallus gallus]" 100.00 191 99.44 99.44 1.32e-125 REF NP_001003254 "cell division control protein 42 homolog precursor [Canis lupus familiaris]" 100.00 191 99.44 99.44 1.38e-125 REF NP_001008027 "cell division control protein 42 homolog isoform 1 [Xenopus (Silurana) tropicalis]" 100.00 191 98.88 99.44 5.86e-125 REF NP_001017070 "cell division control protein 42 homolog isoform 2 [Xenopus (Silurana) tropicalis]" 100.00 191 99.44 99.44 1.70e-125 REF NP_001018130 "cell division control protein 42 homolog isoform 2 [Danio rerio]" 100.00 191 98.88 99.44 3.82e-125 REF NP_001034891 "cell division control protein 42 homolog isoform 1 precursor [Homo sapiens]" 100.00 191 99.44 99.44 1.38e-125 SP P60766 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 100.00 191 99.44 99.44 1.38e-125 SP P60952 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 100.00 191 99.44 99.44 1.38e-125 SP P60953 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 100.00 191 99.44 99.44 1.38e-125 SP Q007T2 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor" 100.00 191 99.44 99.44 1.38e-125 SP Q2KJ93 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor" 100.00 191 99.44 99.44 1.38e-125 TPG DAA32122 "TPA: cell division control protein 42 homolog precursor [Bos taurus]" 92.70 165 99.39 99.39 3.61e-116 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cdc42(T35A) 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Cdc42(T35A) 'recombinant technology' . Escherichia coli . pET-15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Cdc42(T35A) . mM 0.3 0.5 '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.3 . mM pH 5.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label water C 13 protons ppm 0 na indirect . . . 0.251449530 $entry_citation $entry_citation water H 1 protons ppm 0 na indirect . . . 1.0 $entry_citation $entry_citation water N 15 protons ppm 0 na indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Cdc42(T35A) monomer' _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 1 1 MET H H 8.233 0.02 1 2 1 1 MET HA H 4.309 0.02 1 3 1 1 MET HB2 H 2.324 0.02 1 4 1 1 MET C C 174.6 0.4 1 5 1 1 MET CA C 55.864 0.4 1 6 1 1 MET CB C 30.062 0.4 1 7 1 1 MET CG C 33.053 0.4 1 8 1 1 MET N N 118.273 0.4 1 9 2 2 GLN H H 8.458 0.02 1 10 2 2 GLN HA H 4.33 0.02 1 11 2 2 GLN HB2 H 1.978 0.02 2 12 2 2 GLN HB3 H 1.68 0.02 2 13 2 2 GLN HE21 H 6.81 0.02 2 14 2 2 GLN HE22 H 7.544 0.02 2 15 2 2 GLN HG2 H 1.382 0.02 2 16 2 2 GLN HG3 H 2.973 0.02 2 17 2 2 GLN C C 176.274 0.4 1 18 2 2 GLN CA C 55.806 0.4 1 19 2 2 GLN CB C 32.011 0.4 1 20 2 2 GLN CG C 41.951 0.4 1 21 2 2 GLN N N 121.53 0.4 1 22 2 2 GLN NE2 N 111.257 0.4 1 23 3 3 THR H H 7.618 0.02 1 24 3 3 THR HA H 4.683 0.02 1 25 3 3 THR HB H 4.1 0.02 1 26 3 3 THR HG2 H 1.288 0.02 2 27 3 3 THR C C 173.331 0.4 1 28 3 3 THR CA C 61.64 0.4 1 29 3 3 THR CB C 70.16 0.4 1 30 3 3 THR CG2 C 21.242 0.4 1 31 3 3 THR N N 120.51 0.4 1 32 4 4 ILE H H 9.077 0.02 1 33 4 4 ILE HA H 4.418 0.02 1 34 4 4 ILE HB H 1.825 0.02 1 35 4 4 ILE HG12 H 0.611 0.02 1 36 4 4 ILE C C 173.824 0.4 1 37 4 4 ILE CA C 59.775 0.4 1 38 4 4 ILE CB C 40.441 0.4 1 39 4 4 ILE CD1 C 14.429 0.4 1 40 4 4 ILE CG1 C 27.691 0.4 2 41 4 4 ILE CG2 C 18.244 0.4 2 42 4 4 ILE N N 127.486 0.4 1 43 5 5 LYS H H 10.666 0.02 1 44 5 5 LYS HA H 4.773 0.02 1 45 5 5 LYS C C 174.398 0.4 1 46 5 5 LYS CA C 56.175 0.4 1 47 5 5 LYS CB C 31.965 0.4 1 48 5 5 LYS CD C 32.596 0.4 1 49 5 5 LYS CG C 29.144 0.4 1 50 5 5 LYS N N 131.626 0.4 1 51 6 6 CYS H H 9.473 0.02 1 52 6 6 CYS HA H 5.58 0.02 1 53 6 6 CYS HB2 H 3.022 0.02 2 54 6 6 CYS HB3 H 2.231 0.02 2 55 6 6 CYS C C 172.21 0.4 1 56 6 6 CYS CA C 56.195 0.4 1 57 6 6 CYS CB C 28.604 0.4 1 58 6 6 CYS N N 131.522 0.4 1 59 7 7 VAL H H 7.607 0.02 1 60 7 7 VAL HA H 5.014 0.02 1 61 7 7 VAL HB H 1.633 0.02 1 62 7 7 VAL HG1 H 1.019 0.02 2 63 7 7 VAL HG2 H 0.697 0.02 2 64 7 7 VAL C C 174.077 0.4 1 65 7 7 VAL CA C 60.575 0.4 1 66 7 7 VAL CB C 33.1 0.4 1 67 7 7 VAL CG2 C 21.968 0.4 1 68 7 7 VAL N N 128.326 0.4 1 69 8 8 VAL H H 8.566 0.02 1 70 8 8 VAL HA H 4.784 0.02 1 71 8 8 VAL HB H 2.234 0.02 1 72 8 8 VAL HG1 H 0.87 0.02 2 73 8 8 VAL HG2 H 1.018 0.02 2 74 8 8 VAL C C 174.443 0.4 1 75 8 8 VAL CA C 61.573 0.4 1 76 8 8 VAL CB C 32.367 0.4 1 77 8 8 VAL CG2 C 22.422 0.4 1 78 8 8 VAL N N 127.481 0.4 1 79 9 9 VAL H H 8.923 0.02 1 80 9 9 VAL HA H 4.419 0.02 1 81 9 9 VAL HB H 1.739 0.02 1 82 9 9 VAL HG1 H 0.991 0.02 2 83 9 9 VAL HG2 H 0.609 0.02 2 84 9 9 VAL C C 173.171 0.4 1 85 9 9 VAL CA C 58.397 0.4 1 86 9 9 VAL CB C 35.085 0.4 1 87 9 9 VAL CG2 C 20.651 0.4 1 88 9 9 VAL N N 116.9 0.4 1 89 10 10 GLY H H 6.267 0.02 1 90 10 10 GLY HA2 H 4.159 0.02 2 91 10 10 GLY HA3 H 1.722 0.02 2 92 10 10 GLY C C 172.378 0.4 1 93 10 10 GLY CA C 42.935 0.4 1 94 10 10 GLY N N 106.077 0.4 1 95 11 11 ASP H H 8.399 0.02 1 96 11 11 ASP HA H 4.737 0.02 1 97 11 11 ASP HB2 H 2.736 0.02 1 98 11 11 ASP C C 177.486 0.4 1 99 11 11 ASP CA C 55.635 0.4 1 100 11 11 ASP CB C 41.076 0.4 1 101 11 11 ASP N N 119.142 0.4 1 102 12 12 GLY H H 8.902 0.02 1 103 12 12 GLY HA2 H 3.954 0.02 2 104 12 12 GLY HA3 H 3.718 0.02 2 105 12 12 GLY C C 173.624 0.4 1 106 12 12 GLY CA C 46.955 0.4 1 107 12 12 GLY N N 104.688 0.4 1 108 13 13 ALA H H 10.666 0.02 1 109 13 13 ALA HA H 4.067 0.02 1 110 13 13 ALA HB H 1.567 0.02 1 111 13 13 ALA CA C 53.455 0.4 1 112 13 13 ALA CB C 15.706 0.4 1 113 13 13 ALA N N 123.135 0.4 1 114 14 14 VAL H H 7.663 0.02 1 115 14 14 VAL HA H 4.146 0.02 1 116 14 14 VAL C C 175.007 0.4 1 117 14 14 VAL CA C 62.015 0.4 1 118 14 14 VAL N N 118.803 0.4 1 119 15 15 GLY H H 8.686 0.02 1 120 15 15 GLY HA2 H 4.838 0.02 2 121 15 15 GLY HA3 H 4.312 0.02 2 122 15 15 GLY C C 175.934 0.4 1 123 15 15 GLY CA C 44.835 0.4 1 124 15 15 GLY N N 110.36 0.4 1 125 16 16 LYS H H 10.352 0.02 1 126 16 16 LYS HA H 3.575 0.02 1 127 16 16 LYS C C 176.582 0.4 1 128 16 16 LYS CA C 60.695 0.4 1 129 16 16 LYS CB C 29.661 0.4 1 130 16 16 LYS N N 125.835 0.4 1 131 17 17 THR H H 9.024 0.02 1 132 17 17 THR HA H 3.93 0.02 1 133 17 17 THR HB H 4.39 0.02 1 134 17 17 THR HG2 H 1.159 0.02 1 135 17 17 THR C C 177.493 0.4 1 136 17 17 THR CA C 66.984 0.4 1 137 17 17 THR CB C 67.298 0.4 1 138 17 17 THR CG2 C 22.423 0.4 1 139 17 17 THR N N 118.089 0.4 1 140 18 18 CYS H H 9.773 0.02 1 141 18 18 CYS HA H 3.58 0.02 1 142 18 18 CYS HB2 H 2.814 0.02 2 143 18 18 CYS HB3 H 2.066 0.02 2 144 18 18 CYS C C 176.716 0.4 1 145 18 18 CYS CA C 65.816 0.4 1 146 18 18 CYS CB C 27.655 0.4 1 147 18 18 CYS N N 119.747 0.4 1 148 19 19 LEU H H 8.195 0.02 1 149 19 19 LEU HA H 3.94 0.02 1 150 19 19 LEU HB2 H 2.29 0.02 2 151 19 19 LEU HB3 H 2.473 0.02 2 152 19 19 LEU HD2 H 0.682 0.02 1 153 19 19 LEU HG H 1.754 0.02 1 154 19 19 LEU C C 177.177 0.4 1 155 19 19 LEU CA C 59.366 0.4 1 156 19 19 LEU CB C 41.377 0.4 1 157 19 19 LEU CG C 26.782 0.4 1 158 19 19 LEU N N 121.557 0.4 1 159 20 20 LEU H H 7.27 0.02 1 160 20 20 LEU HA H 3.84 0.02 1 161 20 20 LEU HB2 H 1.661 0.02 1 162 20 20 LEU HD1 H 0.693 0.02 1 163 20 20 LEU HD2 H 0.914 0.02 1 164 20 20 LEU HG H 2.283 0.02 1 165 20 20 LEU C C 180.155 0.4 1 166 20 20 LEU CA C 57.629 0.4 1 167 20 20 LEU CB C 41.498 0.4 1 168 20 20 LEU CD2 C 24.571 0.4 1 169 20 20 LEU CG C 25.571 0.4 1 170 20 20 LEU N N 117.986 0.4 1 171 21 21 ILE H H 8.619 0.02 1 172 21 21 ILE HA H 3.09 0.02 1 173 21 21 ILE HB H 1.269 0.02 1 174 21 21 ILE HD1 H 0.124 0.02 1 175 21 21 ILE HG12 H 0.662 0.02 1 176 21 21 ILE C C 179.125 0.4 1 177 21 21 ILE CA C 66.129 0.4 1 178 21 21 ILE CB C 38.338 0.4 1 179 21 21 ILE CD1 C 14.611 0.4 1 180 21 21 ILE CG1 C 28.236 0.4 2 181 21 21 ILE CG2 C 17.599 0.4 2 182 21 21 ILE N N 121.078 0.4 1 183 22 22 SER H H 8.899 0.02 1 184 22 22 SER HA H 4.517 0.02 1 185 22 22 SER HB2 H 4.123 0.02 2 186 22 22 SER HB3 H 3.974 0.02 2 187 22 22 SER C C 176.876 0.4 1 188 22 22 SER CA C 61.38 0.4 1 189 22 22 SER CB C 63.882 0.4 1 190 22 22 SER N N 118.286 0.4 1 191 23 23 TYR H H 7.951 0.02 1 192 23 23 TYR HA H 4.264 0.02 1 193 23 23 TYR HB2 H 2.485 0.02 2 194 23 23 TYR HB3 H 3.012 0.02 2 195 23 23 TYR HD2 H 6.352 0.02 1 196 23 23 TYR HE2 H 6.644 0.02 1 197 23 23 TYR C C 176.82 0.4 1 198 23 23 TYR CA C 60.474 0.4 1 199 23 23 TYR CB C 39.531 0.4 1 200 23 23 TYR N N 117.292 0.4 1 201 24 24 THR H H 7.702 0.02 1 202 24 24 THR HA H 3.614 0.02 1 203 24 24 THR HB H 3.757 0.02 1 204 24 24 THR HG2 H 1.069 0.02 1 205 24 24 THR C C 176.5 0.4 1 206 24 24 THR CA C 64.095 0.4 1 207 24 24 THR CB C 70.437 0.4 1 208 24 24 THR CG2 C 23.149 0.4 1 209 24 24 THR N N 105.659 0.4 1 210 25 25 THR H H 8.08 0.02 1 211 25 25 THR HA H 4.556 0.02 1 212 25 25 THR HB H 4.25 0.02 1 213 25 25 THR HG2 H 1.211 0.02 1 214 25 25 THR C C 175.025 0.4 1 215 25 25 THR CA C 61.975 0.4 1 216 25 25 THR CB C 72.012 0.4 1 217 25 25 THR CG2 C 20.788 0.4 1 218 25 25 THR N N 109.689 0.4 1 219 26 26 ASN H H 7.603 0.02 1 220 26 26 ASN HA H 4.501 0.02 1 221 26 26 ASN HB2 H 3.137 0.02 1 222 26 26 ASN HB3 H 2.885 0.02 2 223 26 26 ASN C C 173.259 0.4 2 224 26 26 ASN CA C 55.218 0.4 1 225 26 26 ASN CB C 38.009 0.4 1 226 26 26 ASN N N 115.569 0.4 1 227 27 27 LYS H H 7.698 0.02 1 228 27 27 LYS HA H 4.431 0.02 1 229 27 27 LYS HB2 H 1.531 0.02 1 230 27 27 LYS HG2 H 1.323 0.02 1 231 27 27 LYS C C 173.5 0.4 1 232 27 27 LYS CA C 55.163 0.4 1 233 27 27 LYS CB C 35.034 0.4 1 234 27 27 LYS CD C 28.962 0.4 1 235 27 27 LYS CE C 42.133 0.4 1 236 27 27 LYS CG C 24.33 0.4 1 237 27 27 LYS N N 118.253 0.4 1 238 28 28 PHE H H 8.554 0.02 1 239 28 28 PHE CA C 55.575 0.4 1 240 28 28 PHE CB C 39.322 0.4 1 241 28 28 PHE N N 125.682 0.4 1 242 29 29 PRO HA H 4.373 0.02 1 243 29 29 PRO HB2 H 1.877 0.02 1 244 29 29 PRO C C 173.611 0.4 1 245 29 29 PRO CA C 61.978 0.4 1 246 29 29 PRO CB C 30.039 0.4 1 247 29 29 PRO CD C 48.673 0.4 1 248 29 29 PRO CG C 28.327 0.4 1 249 30 30 SER H H 7.993 0.02 1 250 30 30 SER HA H 4.285 0.02 1 251 30 30 SER HB2 H 3.948 0.02 2 252 30 30 SER HB3 H 3.826 0.02 2 253 30 30 SER C C 174.665 0.4 1 254 30 30 SER CA C 58.948 0.4 1 255 30 30 SER CB C 64.019 0.4 1 256 30 30 SER N N 116.682 0.4 1 257 31 31 GLU H H 8.198 0.02 1 258 31 31 GLU HA H 4.308 0.02 1 259 31 31 GLU HB2 H 2.116 0.02 2 260 31 31 GLU HB3 H 1.895 0.02 2 261 31 31 GLU HG2 H 1.895 0.02 1 262 31 31 GLU C C 175.157 0.4 1 263 31 31 GLU CA C 56.846 0.4 1 264 31 31 GLU CB C 30.113 0.4 1 265 31 31 GLU CG C 36.276 0.4 1 266 31 31 GLU N N 120.151 0.4 1 267 32 32 TYR H H 7.714 0.02 1 268 32 32 TYR HA H 4.407 0.02 1 269 32 32 TYR HB2 H 3.061 0.02 2 270 32 32 TYR HB3 H 2.718 0.02 2 271 32 32 TYR HD1 H 6.987 0.02 1 272 32 32 TYR C C 173.544 0.4 1 273 32 32 TYR CA C 58.368 0.4 1 274 32 32 TYR CB C 38.614 0.4 1 275 32 32 TYR N N 118.548 0.4 1 276 33 33 VAL H H 7.764 0.02 1 277 33 33 VAL HA H 4.048 0.02 1 278 33 33 VAL HB H 1.738 0.02 1 279 33 33 VAL HG1 H 0.842 0.02 2 280 33 33 VAL HG2 H 0.631 0.02 2 281 33 33 VAL CA C 58.575 0.4 1 282 33 33 VAL CB C 33.6 0.4 1 283 33 33 VAL N N 125.992 0.4 1 284 34 34 PRO HA H 4.215 0.02 1 285 34 34 PRO HB2 H 2.159 0.02 1 286 34 34 PRO C C 175.627 0.4 1 287 34 34 PRO CA C 61.655 0.4 1 288 34 34 PRO CB C 31.965 0.4 1 289 34 34 PRO CD C 49.944 0.4 1 290 34 34 PRO CG C 26.328 0.4 1 291 35 35 ALA H H 8.503 0.02 1 292 35 35 ALA HA H 4.19 0.02 1 293 35 35 ALA HB H 1.434 0.02 1 294 35 35 ALA C C 178.295 0.4 1 295 35 35 ALA CA C 54.499 0.4 1 296 35 35 ALA CB C 18.235 0.4 1 297 35 35 ALA N N 123.063 0.4 1 298 36 36 VAL H H 8.032 0.02 1 299 36 36 VAL HA H 4.258 0.02 1 300 36 36 VAL HB H 1.777 0.02 1 301 36 36 VAL HG1 H 0.631 0.02 1 302 36 36 VAL CA C 60.2 0.4 1 303 36 36 VAL CB C 29.879 0.4 1 304 36 36 VAL N N 116.77 0.4 1 305 37 37 PHE HB2 H 3.05 0.02 1 306 37 37 PHE C C 174.502 0.4 1 307 37 37 PHE CA C 56.175 0.4 1 308 37 37 PHE CB C 40.231 0.4 1 309 38 38 ASP H H 7.602 0.02 1 310 38 38 ASP HA H 4.343 0.02 1 311 38 38 ASP HB2 H 2.456 0.02 1 312 38 38 ASP HB3 H 2.182 0.02 1 313 38 38 ASP C C 174.386 0.4 1 314 38 38 ASP CA C 54.323 0.4 1 315 38 38 ASP CB C 40.815 0.4 1 316 38 38 ASP N N 125.774 0.4 1 317 39 39 ASN H H 7.917 0.02 1 318 39 39 ASN HA H 4.303 0.02 1 319 39 39 ASN HB2 H 2.129 0.02 1 320 39 39 ASN HD21 H 7.305 0.02 2 321 39 39 ASN HD22 H 6.667 0.02 2 322 39 39 ASN C C 173.897 0.4 1 323 39 39 ASN CA C 54.317 0.4 1 324 39 39 ASN CB C 38.18 0.4 1 325 39 39 ASN N N 117.429 0.4 1 326 39 39 ASN ND2 N 112.368 0.4 1 327 40 40 TYR H H 7.726 0.02 1 328 40 40 TYR HA H 4.513 0.02 1 329 40 40 TYR HB2 H 2.754 0.02 2 330 40 40 TYR HB3 H 2.827 0.02 2 331 40 40 TYR HD2 H 6.911 0.02 1 332 40 40 TYR C C 172.772 0.4 1 333 40 40 TYR CA C 57.335 0.4 1 334 40 40 TYR CB C 42.956 0.4 1 335 40 40 TYR N N 122.998 0.4 1 336 41 41 ALA H H 7.651 0.02 1 337 41 41 ALA HA H 5.636 0.02 1 338 41 41 ALA HB H 1.09 0.02 1 339 41 41 ALA C C 175.778 0.4 1 340 41 41 ALA CA C 50.456 0.4 1 341 41 41 ALA CB C 20.492 0.4 1 342 41 41 ALA N N 127.028 0.4 1 343 42 42 VAL H H 8.781 0.02 1 344 42 42 VAL HA H 4.564 0.02 1 345 42 42 VAL HB H 2.122 0.02 1 346 42 42 VAL HG1 H 0.968 0.02 1 347 42 42 VAL C C 173.852 0.4 1 348 42 42 VAL CA C 59.278 0.4 1 349 42 42 VAL CB C 35.342 0.4 1 350 42 42 VAL CG2 C 20.899 0.4 1 351 42 42 VAL N N 117.471 0.4 1 352 43 43 THR H H 8.566 0.02 1 353 43 43 THR HA H 5.124 0.02 1 354 43 43 THR HB H 3.932 0.02 1 355 43 43 THR HG2 H 1.077 0.02 1 356 43 43 THR C C 174.21 0.4 1 357 43 43 THR CA C 62.434 0.4 1 358 43 43 THR CB C 69.296 0.4 1 359 43 43 THR CG2 C 21.878 0.4 1 360 43 43 THR N N 120.85 0.4 1 361 44 44 VAL H H 9.442 0.02 1 362 44 44 VAL HA H 4.367 0.02 1 363 44 44 VAL HB H 1.956 0.02 1 364 44 44 VAL HG1 H 0.941 0.02 1 365 44 44 VAL C C 174.061 0.4 1 366 44 44 VAL CA C 60.639 0.4 1 367 44 44 VAL CB C 35.053 0.4 1 368 44 44 VAL CG2 C 21.423 0.4 1 369 44 44 VAL N N 127.764 0.4 1 370 45 45 MET H H 8.513 0.02 1 371 45 45 MET HA H 5.272 0.02 1 372 45 45 MET HB2 H 1.974 0.02 2 373 45 45 MET HB3 H 1.756 0.02 2 374 45 45 MET HG2 H 2.408 0.02 1 375 45 45 MET C C 176.395 0.4 1 376 45 45 MET CA C 53.264 0.4 1 377 45 45 MET CB C 31.692 0.4 1 378 45 45 MET N N 123.063 0.4 1 379 46 46 ILE H H 9.103 0.02 1 380 46 46 ILE HA H 4.382 0.02 1 381 46 46 ILE HB H 1.972 0.02 1 382 46 46 ILE HD1 H 0.702 0.02 1 383 46 46 ILE HG2 H 1.127 0.02 1 384 46 46 ILE C C 177.661 0.4 1 385 46 46 ILE CA C 59.755 0.4 1 386 46 46 ILE CB C 38.913 0.4 1 387 46 46 ILE CD1 C 11.886 0.4 1 388 46 46 ILE CG1 C 26.601 0.4 2 389 46 46 ILE CG2 C 16.518 0.4 2 390 46 46 ILE N N 125.267 0.4 1 391 47 47 GLY H H 9.385 0.02 1 392 47 47 GLY HA2 H 4.755 0.02 2 393 47 47 GLY HA3 H 3.851 0.02 2 394 47 47 GLY C C 175.195 0.4 1 395 47 47 GLY CA C 47.015 0.4 1 396 47 47 GLY N N 119.278 0.4 1 397 48 48 GLY H H 8.606 0.02 1 398 48 48 GLY HA2 H 4.14 0.02 2 399 48 48 GLY HA3 H 3.623 0.02 2 400 48 48 GLY C C 172.844 0.4 1 401 48 48 GLY CA C 44.889 0.4 1 402 48 48 GLY N N 104.656 0.4 1 403 49 49 GLU H H 7.722 0.02 1 404 49 49 GLU HA H 4.182 0.02 1 405 49 49 GLU HB2 H 1.953 0.02 1 406 49 49 GLU HG2 H 2.147 0.02 1 407 49 49 GLU CA C 52.336 0.4 1 408 49 49 GLU CB C 31.16 0.4 1 409 49 49 GLU N N 120.543 0.4 1 410 50 50 PRO HA H 4.977 0.02 1 411 50 50 PRO HB2 H 1.823 0.02 1 412 50 50 PRO C C 177.922 0.4 1 413 50 50 PRO CA C 62.08 0.4 1 414 50 50 PRO CB C 32.147 0.4 1 415 51 51 TYR H H 9.148 0.02 1 416 51 51 TYR HA H 4.683 0.02 1 417 51 51 TYR HB2 H 2.725 0.02 1 418 51 51 TYR HD2 H 6.72 0.02 1 419 51 51 TYR HE2 H 7.044 0.02 1 420 51 51 TYR C C 176.4 0.4 1 421 51 51 TYR CA C 57.344 0.4 1 422 51 51 TYR CB C 41.669 0.4 1 423 51 51 TYR N N 121.3 0.4 1 424 52 52 THR H H 8.889 0.02 1 425 52 52 THR HA H 4.113 0.02 1 426 52 52 THR HB H 4.007 0.02 1 427 52 52 THR C C 172.149 0.4 1 428 52 52 THR CA C 62.4 0.4 1 429 52 52 THR CB C 69.447 0.4 1 430 52 52 THR CG2 C 22.059 0.4 1 431 52 52 THR N N 119.482 0.4 1 432 53 53 LEU H H 9.48 0.02 1 433 53 53 LEU HA H 5.03 0.02 1 434 53 53 LEU HB2 H 2.117 0.02 1 435 53 53 LEU HD1 H 0.904 0.02 1 436 53 53 LEU HD2 H 1.135 0.02 1 437 53 53 LEU C C 174.307 0.4 1 438 53 53 LEU CA C 53.375 0.4 1 439 53 53 LEU CB C 44.216 0.4 1 440 53 53 LEU CD2 C 23.694 0.4 1 441 53 53 LEU CG C 26.964 0.4 1 442 53 53 LEU N N 131.364 0.4 1 443 54 54 GLY H H 9.749 0.02 1 444 54 54 GLY HA2 H 4.571 0.02 2 445 54 54 GLY HA3 H 3.577 0.02 2 446 54 54 GLY C C 171.929 0.4 1 447 54 54 GLY CA C 45.195 0.4 1 448 54 54 GLY N N 115.64 0.4 1 449 55 55 LEU H H 8.623 0.02 1 450 55 55 LEU HA H 5.104 0.02 1 451 55 55 LEU HB2 H 2.02 0.02 1 452 55 55 LEU HD2 H 0.755 0.02 1 453 55 55 LEU HG H 1.319 0.02 1 454 55 55 LEU C C 176 0.4 1 455 55 55 LEU CA C 54.202 0.4 1 456 55 55 LEU CB C 44.057 0.4 1 457 55 55 LEU CD2 C 24.875 0.4 1 458 55 55 LEU CG C 26.601 0.4 1 459 55 55 LEU N N 125.141 0.4 1 460 56 56 PHE H H 8.735 0.02 1 461 56 56 PHE HA H 4.821 0.02 1 462 56 56 PHE HB2 H 3.287 0.02 2 463 56 56 PHE HB3 H 2.977 0.02 2 464 56 56 PHE HD2 H 7.389 0.02 1 465 56 56 PHE C C 173.13 0.4 1 466 56 56 PHE CA C 56.833 0.4 1 467 56 56 PHE CB C 40.776 0.4 1 468 56 56 PHE N N 122.065 0.4 1 469 57 57 ASP H H 9.093 0.02 1 470 57 57 ASP HA H 4.877 0.02 1 471 57 57 ASP HB2 H 3.001 0.02 2 472 57 57 ASP HB3 H 2.777 0.02 2 473 57 57 ASP C C 175.941 0.4 1 474 57 57 ASP CA C 51.755 0.4 1 475 57 57 ASP CB C 43.082 0.4 1 476 57 57 ASP N N 124.05 0.4 1 477 58 58 THR H H 8.621 0.02 1 478 58 58 THR HA H 3.905 0.02 1 479 58 58 THR C C 172.124 0.4 1 480 58 58 THR CA C 60.335 0.4 1 481 58 58 THR CB C 74.469 0.4 1 482 58 58 THR N N 109.327 0.4 1 483 59 59 ALA H H 8.695 0.02 1 484 59 59 ALA HA H 4.565 0.02 1 485 59 59 ALA HB H 0.777 0.02 1 486 59 59 ALA CA C 50.475 0.4 1 487 59 59 ALA CB C 18.224 0.4 1 488 59 59 ALA N N 123.129 0.4 1 489 60 60 GLY H H 8.63 0.02 1 490 60 60 GLY HA2 H 4.42 0.02 2 491 60 60 GLY HA3 H 3.902 0.02 2 492 60 60 GLY C C 173.122 0.4 1 493 60 60 GLY CA C 46.178 0.4 1 494 60 60 GLY N N 109.449 0.4 1 495 61 61 GLN H H 8.553 0.02 1 496 61 61 GLN HA H 4.492 0.02 1 497 61 61 GLN HB2 H 2.348 0.02 2 498 61 61 GLN HB3 H 2.673 0.02 2 499 61 61 GLN HE21 H 8.019 0.02 2 500 61 61 GLN HE22 H 6.965 0.02 2 501 61 61 GLN HG2 H 2.65 0.02 1 502 61 61 GLN C C 177.014 0.4 1 503 61 61 GLN CA C 56.895 0.4 1 504 61 61 GLN CB C 28.863 0.4 1 505 61 61 GLN CG C 34.412 0.4 1 506 61 61 GLN N N 118.471 0.4 1 507 61 61 GLN NE2 N 111.812 0.4 1 508 62 62 GLU H H 9.082 0.02 1 509 62 62 GLU HA H 4.292 0.02 1 510 62 62 GLU HB2 H 2.03 0.02 1 511 62 62 GLU HG2 H 2.346 0.02 1 512 62 62 GLU C C 178.273 0.4 1 513 62 62 GLU CA C 58.361 0.4 1 514 62 62 GLU CB C 28.579 0.4 1 515 62 62 GLU CG C 36.047 0.4 1 516 62 62 GLU N N 122.087 0.4 1 517 63 63 ASP H H 8.636 0.02 1 518 63 63 ASP HA H 4.348 0.02 1 519 63 63 ASP HB2 H 2.415 0.02 1 520 63 63 ASP HB3 H 2.191 0.02 1 521 63 63 ASP C C 176.712 0.4 1 522 63 63 ASP CA C 55.587 0.4 1 523 63 63 ASP CB C 39.571 0.4 1 524 63 63 ASP N N 117.009 0.4 1 525 64 64 TYR H H 8.061 0.02 1 526 64 64 TYR HA H 4.609 0.02 1 527 64 64 TYR HB2 H 3.44 0.02 2 528 64 64 TYR HB3 H 2.828 0.02 2 529 64 64 TYR C C 176.254 0.4 1 530 64 64 TYR CA C 58.231 0.4 1 531 64 64 TYR CB C 38.65 0.4 1 532 64 64 TYR N N 117.063 0.4 1 533 65 65 ASP H H 8.064 0.02 1 534 65 65 ASP HA H 4.439 0.02 1 535 65 65 ASP HB2 H 2.138 0.02 1 536 65 65 ASP C C 175.163 0.4 1 537 65 65 ASP CA C 57.971 0.4 1 538 65 65 ASP N N 122.196 0.4 1 539 66 66 ARG H H 8.537 0.02 1 540 66 66 ARG HA H 4.345 0.02 1 541 66 66 ARG C C 175.009 0.4 1 542 66 66 ARG CA C 56.217 0.4 1 543 66 66 ARG N N 122.224 0.4 1 544 67 67 LEU H H 8.336 0.02 1 545 67 67 LEU HA H 4.037 0.02 1 546 67 67 LEU CA C 61.694 0.4 1 547 67 67 LEU N N 117.734 0.4 1 548 69 69 PRO HB2 H 2.342 0.02 1 549 69 69 PRO C C 178.122 0.4 1 550 69 69 PRO CA C 63.575 0.4 1 551 69 69 PRO CD C 47.674 0.4 1 552 69 69 PRO CG C 27.872 0.4 1 553 70 70 LEU H H 7.47 0.02 1 554 70 70 LEU HA H 4.031 0.02 1 555 70 70 LEU HB2 H 1.883 0.02 2 556 70 70 LEU HB3 H 1.527 0.02 2 557 70 70 LEU HD1 H 0.93 0.02 1 558 70 70 LEU HD2 H 0.808 0.02 1 559 70 70 LEU C C 178.756 0.4 1 560 70 70 LEU CA C 56.944 0.4 1 561 70 70 LEU CB C 40.002 0.4 1 562 70 70 LEU CD2 C 22.059 0.4 1 563 70 70 LEU CG C 25.329 0.4 1 564 70 70 LEU N N 118.335 0.4 1 565 71 71 SER H H 7.882 0.02 1 566 71 71 SER HA H 4.461 0.02 1 567 71 71 SER HB2 H 3.89 0.02 1 568 71 71 SER C C 179.2 0.4 1 569 71 71 SER CA C 59.71 0.4 1 570 71 71 SER CB C 63.841 0.4 1 571 71 71 SER N N 111.784 0.4 1 572 72 72 TYR H H 7.362 0.02 1 573 72 72 TYR CA C 56.002 0.4 1 574 72 72 TYR CB C 35.144 0.4 1 575 72 72 TYR N N 119.959 0.4 1 576 73 73 PRO HA H 4.231 0.02 1 577 73 73 PRO C C 176.096 0.4 1 578 73 73 PRO CA C 66.055 0.4 1 579 73 73 PRO CB C 35.726 0.4 1 580 74 74 GLN H H 8.995 0.02 1 581 74 74 GLN HA H 3.79 0.02 1 582 74 74 GLN HB2 H 2.265 0.02 1 583 74 74 GLN HE21 H 7.649 0.02 2 584 74 74 GLN HE22 H 6.846 0.02 2 585 74 74 GLN C C 174.686 0.4 1 586 74 74 GLN CA C 57.416 0.4 1 587 74 74 GLN CB C 25.352 0.4 1 588 74 74 GLN CG C 34.866 0.4 1 589 74 74 GLN N N 114.768 0.4 1 590 74 74 GLN NE2 N 111.257 0.4 1 591 75 75 THR H H 7.504 0.02 1 592 75 75 THR HA H 3.172 0.02 1 593 75 75 THR HB H 3.523 0.02 1 594 75 75 THR HG2 H 0.232 0.02 2 595 75 75 THR C C 173.589 0.4 1 596 75 75 THR CA C 67.162 0.4 1 597 75 75 THR CB C 61.122 0.4 1 598 75 75 THR CG2 C 22.695 0.4 1 599 75 75 THR N N 116.725 0.4 1 600 76 76 ASP H H 8.865 0.02 1 601 76 76 ASP HA H 4.873 0.02 1 602 76 76 ASP HB2 H 2.664 0.02 2 603 76 76 ASP HB3 H 2.563 0.02 2 604 76 76 ASP C C 177.6 0.4 1 605 76 76 ASP CA C 56.105 0.4 1 606 76 76 ASP CB C 44.016 0.4 1 607 76 76 ASP N N 124.192 0.4 1 608 77 77 VAL H H 7.578 0.02 1 609 77 77 VAL HA H 4.706 0.02 1 610 77 77 VAL HB H 2.12 0.02 1 611 77 77 VAL HG1 H 0.84 0.02 2 612 77 77 VAL HG2 H -0.041 0.02 2 613 77 77 VAL C C 171.266 0.4 1 614 77 77 VAL CA C 60.346 0.4 1 615 77 77 VAL CB C 32.362 0.4 1 616 77 77 VAL CG2 C 19.107 0.4 1 617 77 77 VAL N N 116.06 0.4 1 618 78 78 PHE H H 8.287 0.02 1 619 78 78 PHE HA H 5.646 0.02 1 620 78 78 PHE HB2 H 2.725 0.02 2 621 78 78 PHE HB3 H 2.841 0.02 2 622 78 78 PHE C C 175.799 0.4 1 623 78 78 PHE CA C 56.686 0.4 1 624 78 78 PHE CB C 43.413 0.4 1 625 78 78 PHE N N 121.935 0.4 1 626 79 79 LEU H H 8.937 0.02 1 627 79 79 LEU HA H 4.691 0.02 1 628 79 79 LEU HB2 H 1.783 0.02 1 629 79 79 LEU HD2 H 0.369 0.02 1 630 79 79 LEU HG H 1.006 0.02 1 631 79 79 LEU C C 174.059 0.4 1 632 79 79 LEU CA C 53.575 0.4 1 633 79 79 LEU CB C 41.184 0.4 1 634 79 79 LEU CD2 C 23.24 0.4 1 635 79 79 LEU CG C 25.783 0.4 1 636 79 79 LEU N N 119.06 0.4 1 637 80 80 VAL H H 8.828 0.02 1 638 80 80 VAL HA H 4.138 0.02 1 639 80 80 VAL HB H 2.367 0.02 1 640 80 80 VAL HG1 H 0.839 0.02 1 641 80 80 VAL HG2 H 0.657 0.02 1 642 80 80 VAL C C 174.535 0.4 1 643 80 80 VAL CA C 61.395 0.4 1 644 80 80 VAL CB C 30.602 0.4 1 645 80 80 VAL CG1 C 21.06 0.4 2 646 80 80 VAL CG2 C 24.875 0.4 2 647 80 80 VAL N N 124.677 0.4 1 648 81 81 CYS H H 8.795 0.02 1 649 81 81 CYS HA H 5.758 0.02 1 650 81 81 CYS HB2 H 2.52 0.02 2 651 81 81 CYS HB3 H 2.172 0.02 2 652 81 81 CYS C C 173.98 0.4 1 653 81 81 CYS CA C 57.821 0.4 1 654 81 81 CYS CB C 30.043 0.4 1 655 81 81 CYS N N 123.745 0.4 1 656 82 82 PHE H H 8.873 0.02 1 657 82 82 PHE HA H 4.532 0.02 1 658 82 82 PHE HB2 H 3.415 0.02 2 659 82 82 PHE HB3 H 2.725 0.02 2 660 82 82 PHE HD2 H 7.18 0.02 3 661 82 82 PHE C C 171.09 0.4 1 662 82 82 PHE CA C 56.367 0.4 1 663 82 82 PHE CB C 40.091 0.4 1 664 82 82 PHE N N 117.718 0.4 1 665 83 83 SER H H 8.038 0.02 1 666 83 83 SER HA H 5.204 0.02 1 667 83 83 SER HB2 H 3.584 0.02 2 668 83 83 SER HB3 H 3.788 0.02 2 669 83 83 SER C C 178.547 0.4 1 670 83 83 SER CA C 55 0.4 1 671 83 83 SER CB C 63.051 0.4 1 672 83 83 SER N N 113.246 0.4 1 673 84 84 VAL H H 8.609 0.02 1 674 84 84 VAL HA H 4.261 0.02 1 675 84 84 VAL HB H 2.799 0.02 1 676 84 84 VAL HG1 H 0.905 0.02 2 677 84 84 VAL HG2 H 0.981 0.02 2 678 84 84 VAL C C 175.783 0.4 1 679 84 84 VAL CA C 63.745 0.4 1 680 84 84 VAL CB C 29.811 0.4 1 681 84 84 VAL CG2 C 20.648 0.4 1 682 84 84 VAL N N 120.609 0.4 1 683 85 85 VAL H H 7.653 0.02 1 684 85 85 VAL HA H 4.508 0.02 1 685 85 85 VAL HB H 2.447 0.02 1 686 85 85 VAL HG1 H 0.667 0.02 1 687 85 85 VAL C C 173.401 0.4 1 688 85 85 VAL CA C 59.998 0.4 1 689 85 85 VAL CB C 29.718 0.4 1 690 85 85 VAL CG1 C 21.333 0.4 2 691 85 85 VAL CG2 C 18.335 0.4 2 692 85 85 VAL N N 107.92 0.4 1 693 86 86 SER H H 7.792 0.02 1 694 86 86 SER HA H 5.2 0.02 1 695 86 86 SER HB2 H 4.11 0.02 2 696 86 86 SER HB3 H 3.766 0.02 2 697 86 86 SER CA C 53.848 0.4 1 698 86 86 SER CB C 62.72 0.4 1 699 86 86 SER N N 112.608 0.4 1 700 87 87 PRO C C 178.275 0.4 1 701 87 87 PRO CA C 65.655 0.4 1 702 87 87 PRO CB C 31.961 0.4 1 703 88 88 SER H H 8.928 0.02 1 704 88 88 SER HA H 4.783 0.02 1 705 88 88 SER HB2 H 4.238 0.02 2 706 88 88 SER HB3 H 3.891 0.02 2 707 88 88 SER C C 176.192 0.4 1 708 88 88 SER CA C 61.63 0.4 1 709 88 88 SER CB C 71.811 0.4 1 710 88 88 SER N N 113.475 0.4 1 711 89 89 SER H H 8.022 0.02 1 712 89 89 SER HA H 5.047 0.02 1 713 89 89 SER HB2 H 4.332 0.02 2 714 89 89 SER HB3 H 4.597 0.02 2 715 89 89 SER C C 176.417 0.4 1 716 89 89 SER CA C 61.352 0.4 1 717 89 89 SER CB C 63.93 0.4 1 718 89 89 SER N N 120.789 0.4 1 719 90 90 PHE H H 7.454 0.02 1 720 90 90 PHE HA H 3.967 0.02 1 721 90 90 PHE HB2 H 3.286 0.02 2 722 90 90 PHE HB3 H 2.841 0.02 2 723 90 90 PHE HD2 H 6.014 0.02 3 724 90 90 PHE C C 177.387 0.4 1 725 90 90 PHE CA C 59.945 0.4 1 726 90 90 PHE CB C 39.365 0.4 1 727 90 90 PHE N N 124.95 0.4 1 728 91 91 GLU H H 8.245 0.02 1 729 91 91 GLU HA H 3.921 0.02 1 730 91 91 GLU HB2 H 2.128 0.02 1 731 91 91 GLU C C 179.695 0.4 1 732 91 91 GLU CA C 59.102 0.4 1 733 91 91 GLU CB C 28.437 0.4 1 734 91 91 GLU CG C 35.775 0.4 1 735 91 91 GLU N N 119.953 0.4 1 736 92 92 ASN H H 8.106 0.02 1 737 92 92 ASN HA H 4.76 0.02 1 738 92 92 ASN HB2 H 3.301 0.02 2 739 92 92 ASN HB3 H 2.794 0.02 2 740 92 92 ASN HD22 H 6.758 0.02 2 741 92 92 ASN C C 178.593 0.4 1 742 92 92 ASN CA C 54.635 0.4 1 743 92 92 ASN CB C 37.879 0.4 1 744 92 92 ASN N N 114.315 0.4 1 745 92 92 ASN ND2 N 115.423 0.4 1 746 93 93 VAL H H 7.883 0.02 1 747 93 93 VAL HA H 3.738 0.02 1 748 93 93 VAL HB H 2.276 0.02 1 749 93 93 VAL HG1 H 1.219 0.02 2 750 93 93 VAL HG2 H 0.877 0.02 2 751 93 93 VAL C C 174.932 0.4 1 752 93 93 VAL CA C 68.395 0.4 1 753 93 93 VAL CB C 30.596 0.4 1 754 93 93 VAL CG2 C 22.604 0.4 1 755 93 93 VAL N N 124.067 0.4 1 756 94 94 LYS H H 6.59 0.02 1 757 94 94 LYS HA H 3.902 0.02 1 758 94 94 LYS HB2 H 1.887 0.02 2 759 94 94 LYS HB3 H 1.644 0.02 2 760 94 94 LYS HE2 H 2.732 0.02 1 761 94 94 LYS HG2 H 1.281 0.02 1 762 94 94 LYS C C 176.885 0.4 1 763 94 94 LYS CA C 58.135 0.4 1 764 94 94 LYS CB C 33.163 0.4 1 765 94 94 LYS CE C 41.679 0.4 1 766 94 94 LYS CG C 24.603 0.4 1 767 94 94 LYS N N 115.269 0.4 1 768 95 95 GLU H H 7.719 0.02 1 769 95 95 GLU HA H 4.089 0.02 1 770 95 95 GLU HB2 H 1.792 0.02 2 771 95 95 GLU HB3 H 2.076 0.02 2 772 95 95 GLU HG2 H 2.214 0.02 1 773 95 95 GLU C C 176.252 0.4 1 774 95 95 GLU CA C 57.564 0.4 1 775 95 95 GLU CB C 30.353 0.4 1 776 95 95 GLU CG C 39.862 0.4 1 777 95 95 GLU N N 112.466 0.4 1 778 96 96 LYS H H 8.063 0.02 1 779 96 96 LYS HA H 4.25 0.02 1 780 96 96 LYS HB2 H 1.181 0.02 1 781 96 96 LYS HE2 H 3.986 0.02 1 782 96 96 LYS HG2 H 0.962 0.02 1 783 96 96 LYS C C 177.781 0.4 1 784 96 96 LYS CA C 57.343 0.4 1 785 96 96 LYS CB C 35.19 0.4 1 786 96 96 LYS CD C 29.292 0.4 1 787 96 96 LYS CE C 39.408 0.4 1 788 96 96 LYS CG C 24.744 0.4 1 789 96 96 LYS N N 115.613 0.4 1 790 97 97 TRP H H 7.786 0.02 1 791 97 97 TRP HA H 4.39 0.02 1 792 97 97 TRP HB2 H 3.009 0.02 2 793 97 97 TRP HB3 H 3.19 0.02 2 794 97 97 TRP HE1 H 11.443 0.02 1 795 97 97 TRP C C 178.5 0.4 1 796 97 97 TRP CA C 60.831 0.4 1 797 97 97 TRP CB C 30.818 0.4 1 798 97 97 TRP N N 119.643 0.4 1 799 97 97 TRP NE1 N 132.366 0.4 1 800 98 98 VAL H H 8.604 0.02 1 801 98 98 VAL HA H 3.542 0.02 1 802 98 98 VAL HB H 2.108 0.02 1 803 98 98 VAL HG1 H 0.631 0.02 1 804 98 98 VAL CA C 68.434 0.4 1 805 98 98 VAL CB C 28.357 0.4 1 806 98 98 VAL N N 116.894 0.4 1 807 99 99 PRO HA H 3.932 0.02 1 808 99 99 PRO HB2 H 1.583 0.02 1 809 99 99 PRO C C 177.438 0.4 1 810 99 99 PRO CA C 66.615 0.4 1 811 99 99 PRO CB C 30.6 0.4 1 812 99 99 PRO CG C 28.236 0.4 1 813 100 100 GLU H H 7.538 0.02 1 814 100 100 GLU HA H 4.219 0.02 1 815 100 100 GLU HB2 H 2.221 0.02 1 816 100 100 GLU C C 178.891 0.4 1 817 100 100 GLU CA C 60.795 0.4 1 818 100 100 GLU CB C 29.919 0.4 1 819 100 100 GLU CG C 38.409 0.4 1 820 100 100 GLU N N 116.622 0.4 1 821 101 101 ILE H H 8.331 0.02 1 822 101 101 ILE HA H 3.598 0.02 1 823 101 101 ILE C C 177.812 0.4 1 824 101 101 ILE CA C 66.106 0.4 1 825 101 101 ILE CB C 35.806 0.4 1 826 101 101 ILE CG2 C 17.881 0.4 1 827 101 101 ILE N N 113.806 0.4 1 828 102 102 THR H H 7.881 0.02 1 829 102 102 THR HA H 3.849 0.02 1 830 102 102 THR HB H 4.148 0.02 1 831 102 102 THR C C 175.953 0.4 1 832 102 102 THR CA C 64.979 0.4 1 833 102 102 THR CB C 69.609 0.4 1 834 102 102 THR N N 112.542 0.4 1 835 103 103 HIS H H 7.598 0.02 1 836 103 103 HIS HA H 4.217 0.02 1 837 103 103 HIS HB2 H 3.143 0.02 1 838 103 103 HIS C C 176.414 0.4 1 839 103 103 HIS CA C 58.531 0.4 1 840 103 103 HIS CB C 28.397 0.4 1 841 103 103 HIS N N 118.843 0.4 1 842 104 104 HIS H H 7.405 0.02 1 843 104 104 HIS HA H 4.164 0.02 1 844 104 104 HIS HB2 H 3.525 0.02 2 845 104 104 HIS HB3 H 3.065 0.02 2 846 104 104 HIS C C 176.66 0.4 1 847 104 104 HIS CA C 59.641 0.4 1 848 104 104 HIS CB C 33.363 0.4 1 849 104 104 HIS N N 113.791 0.4 1 850 105 105 CYS H H 8.53 0.02 1 851 105 105 CYS HA H 5.015 0.02 1 852 105 105 CYS HB2 H 3.562 0.02 2 853 105 105 CYS HB3 H 3.077 0.02 2 854 105 105 CYS CA C 56.219 0.4 1 855 105 105 CYS N N 117.178 0.4 1 856 106 106 PRO HA H 4.477 0.02 1 857 106 106 PRO HB2 H 2.463 0.02 1 858 106 106 PRO HG2 H 1.888 0.02 1 859 106 106 PRO C C 177.961 0.4 1 860 106 106 PRO CA C 64.735 0.4 1 861 106 106 PRO CB C 31.961 0.4 1 862 106 106 PRO CG C 27.327 0.4 1 863 107 107 LYS H H 8.769 0.02 1 864 107 107 LYS HA H 4.771 0.02 1 865 107 107 LYS HB2 H 2.053 0.02 2 866 107 107 LYS HB3 H 1.875 0.02 2 867 107 107 LYS HE2 H 4.361 0.02 1 868 107 107 LYS HG2 H 1.399 0.02 1 869 107 107 LYS CA C 55.895 0.4 1 870 107 107 LYS CB C 31.16 0.4 1 871 107 107 LYS N N 116.131 0.4 1 872 108 108 THR H H 7.586 0.02 1 873 108 108 THR N N 121.415 0.4 1 874 109 109 PRO HA H 4.529 0.02 1 875 109 109 PRO HB2 H 2.209 0.02 1 876 109 109 PRO HG2 H 1.622 0.02 1 877 109 109 PRO C C 174.846 0.4 1 878 109 109 PRO CA C 62.495 0.4 1 879 109 109 PRO CB C 33.563 0.4 1 880 109 109 PRO CD C 51.307 0.4 1 881 109 109 PRO CG C 26.964 0.4 1 882 110 110 PHE H H 8.165 0.02 1 883 110 110 PHE HA H 5.929 0.02 1 884 110 110 PHE HB2 H 3.006 0.02 1 885 110 110 PHE C C 172.666 0.4 1 886 110 110 PHE CA C 54.448 0.4 1 887 110 110 PHE CB C 43.554 0.4 1 888 110 110 PHE N N 112.128 0.4 1 889 111 111 LEU H H 8.633 0.02 1 890 111 111 LEU HA H 4.694 0.02 1 891 111 111 LEU HB2 H 1.343 0.02 1 892 111 111 LEU HG H 0.529 0.02 1 893 111 111 LEU C C 175.472 0.4 1 894 111 111 LEU CA C 54.212 0.4 1 895 111 111 LEU CB C 43.831 0.4 1 896 111 111 LEU CD2 C 25.602 0.4 1 897 111 111 LEU CG C 29.689 0.4 1 898 111 111 LEU N N 119.654 0.4 1 899 112 112 LEU H H 8.061 0.02 1 900 112 112 LEU HA H 5.363 0.02 1 901 112 112 LEU HB2 H 2.11 0.02 2 902 112 112 LEU HB3 H 1.546 0.02 2 903 112 112 LEU HD2 H 1.076 0.02 2 904 112 112 LEU C C 173.631 0.4 1 905 112 112 LEU CA C 53.826 0.4 1 906 112 112 LEU CB C 44.182 0.4 1 907 112 112 LEU CG C 25.693 0.4 1 908 112 112 LEU N N 121.946 0.4 1 909 113 113 VAL H H 9.178 0.02 1 910 113 113 VAL HA H 4.878 0.02 1 911 113 113 VAL HB H 2.091 0.02 1 912 113 113 VAL HG1 H 0.396 0.02 1 913 113 113 VAL HG2 H 0.445 0.02 1 914 113 113 VAL C C 174.3 0.4 1 915 113 113 VAL CA C 59.695 0.4 1 916 113 113 VAL CB C 33.323 0.4 1 917 113 113 VAL CG1 C 20.42 0.4 2 918 113 113 VAL CG2 C 21.197 0.4 2 919 113 113 VAL N N 125.807 0.4 1 920 114 114 GLY H H 8.731 0.02 1 921 114 114 GLY HA2 H 3.688 0.02 2 922 114 114 GLY HA3 H 3.27 0.02 2 923 114 114 GLY C C 173.36 0.4 1 924 114 114 GLY CA C 44.195 0.4 1 925 114 114 GLY N N 115.079 0.4 1 926 115 115 THR H H 9.181 0.02 1 927 115 115 THR HA H 4.969 0.02 1 928 115 115 THR HB H 4.554 0.02 1 929 115 115 THR HG2 H 0.631 0.02 1 930 115 115 THR C C 175.355 0.4 1 931 115 115 THR CA C 59.375 0.4 1 932 115 115 THR CB C 70.53 0.4 1 933 115 115 THR CG2 C 22.604 0.4 1 934 115 115 THR N N 115.613 0.4 1 935 116 116 GLN H H 9.38 0.02 1 936 116 116 GLN HA H 3.983 0.02 1 937 116 116 GLN HB2 H 2.509 0.02 1 938 116 116 GLN HG2 H 1.138 0.02 1 939 116 116 GLN C C 179.11 0.4 1 940 116 116 GLN CA C 56.195 0.4 1 941 116 116 GLN CB C 23.911 0.4 1 942 116 116 GLN CG C 32.505 0.4 1 943 116 116 GLN N N 108.468 0.4 1 944 117 117 ILE H H 7.635 0.02 1 945 117 117 ILE HA H 3.814 0.02 1 946 117 117 ILE HB H 2.017 0.02 1 947 117 117 ILE HG12 H 0.763 0.02 1 948 117 117 ILE C C 178.002 0.4 1 949 117 117 ILE CA C 64.828 0.4 1 950 117 117 ILE CB C 36.327 0.4 1 951 117 117 ILE CD1 C 13.43 0.4 1 952 117 117 ILE CG2 C 16.7 0.4 2 953 118 118 ASP H H 8.732 0.02 1 954 118 118 ASP HA H 4.468 0.02 1 955 118 118 ASP HB2 H 2.638 0.02 2 956 118 118 ASP HB3 H 2.128 0.02 2 957 118 118 ASP C C 176.888 0.4 1 958 118 118 ASP CA C 55.527 0.4 1 959 118 118 ASP CB C 40.482 0.4 1 960 118 118 ASP N N 119.049 0.4 1 961 119 119 LEU H H 7.914 0.02 1 962 119 119 LEU HA H 4.332 0.02 1 963 119 119 LEU HB2 H 2.031 0.02 2 964 119 119 LEU HB3 H 1.73 0.02 2 965 119 119 LEU HD1 H 0.817 0.02 1 966 119 119 LEU HD2 H 0.686 0.02 1 967 119 119 LEU HG H 1.273 0.02 1 968 119 119 LEU C C 178.015 0.4 1 969 119 119 LEU CA C 55.388 0.4 1 970 119 119 LEU CB C 41.573 0.4 1 971 119 119 LEU CD2 C 21.333 0.4 1 972 119 119 LEU CG C 25.602 0.4 1 973 119 119 LEU N N 117.783 0.4 1 974 120 120 ARG H H 7.256 0.02 1 975 120 120 ARG HA H 3.561 0.02 1 976 120 120 ARG HB2 H 1.615 0.02 1 977 120 120 ARG HG2 H 1.782 0.02 1 978 120 120 ARG C C 174.671 0.4 1 979 120 120 ARG CA C 60.041 0.4 1 980 120 120 ARG CB C 30.079 0.4 1 981 120 120 ARG CD C 43.949 0.4 1 982 120 120 ARG CG C 28.962 0.4 1 983 120 120 ARG N N 116.747 0.4 1 984 121 121 ASP H H 7.078 0.02 1 985 121 121 ASP HA H 4.802 0.02 1 986 121 121 ASP HB2 H 2.887 0.02 2 987 121 121 ASP HB3 H 2.441 0.02 2 988 121 121 ASP C C 175.364 0.4 1 989 121 121 ASP CA C 52.775 0.4 1 990 121 121 ASP CB C 41.372 0.4 1 991 121 121 ASP N N 111.544 0.4 1 992 122 122 ASP H H 7.246 0.02 1 993 122 122 ASP HA H 4.983 0.02 1 994 122 122 ASP HB2 H 3.074 0.02 2 995 122 122 ASP HB3 H 2.769 0.02 2 996 122 122 ASP CA C 51.575 0.4 1 997 122 122 ASP CB C 43.576 0.4 1 998 122 122 ASP N N 122.169 0.4 1 999 123 123 PRO HA H 4.132 0.02 1 1000 123 123 PRO HB2 H 2.352 0.02 2 1001 123 123 PRO HB3 H 1.971 0.02 2 1002 123 123 PRO C C 178.982 0.4 1 1003 123 123 PRO CA C 65.824 0.4 1 1004 123 123 PRO CB C 32.041 0.4 1 1005 123 123 PRO CG C 27.418 0.4 1 1006 124 124 SER H H 8.333 0.02 1 1007 124 124 SER HA H 4.762 0.02 1 1008 124 124 SER HB2 H 4.263 0.02 2 1009 124 124 SER HB3 H 4.007 0.02 2 1010 124 124 SER C C 176.716 0.4 1 1011 124 124 SER CA C 62.073 0.4 1 1012 124 124 SER CB C 62.373 0.4 1 1013 124 124 SER N N 112.482 0.4 1 1014 125 125 THR H H 7.921 0.02 1 1015 125 125 THR HA H 4.658 0.02 1 1016 125 125 THR HB H 3.87 0.02 1 1017 125 125 THR HG2 H 1.26 0.02 1 1018 125 125 THR C C 175.789 0.4 1 1019 125 125 THR CA C 67.686 0.4 1 1020 125 125 THR CG2 C 21.242 0.4 1 1021 125 125 THR N N 121.82 0.4 1 1022 126 126 ILE H H 8.234 0.02 1 1023 126 126 ILE HA H 3.55 0.02 1 1024 126 126 ILE HB H 1.92 0.02 1 1025 126 126 ILE HG12 H 0.87 0.02 1 1026 126 126 ILE C C 179.057 0.4 1 1027 126 126 ILE CA C 65.032 0.4 1 1028 126 126 ILE CB C 37.064 0.4 1 1029 126 126 ILE CD1 C 12.431 0.4 1 1030 126 126 ILE CG1 C 28.508 0.4 1 1031 126 126 ILE CG2 C 17.4 0.4 1 1032 126 126 ILE N N 121.486 0.4 1 1033 127 127 GLU H H 8.24 0.02 1 1034 127 127 GLU HA H 4.165 0.02 1 1035 127 127 GLU HB2 H 2.104 0.02 1 1036 127 127 GLU C C 177.025 0.4 1 1037 127 127 GLU CA C 59.326 0.4 1 1038 127 127 GLU CB C 29.33 0.4 1 1039 127 127 GLU CG C 36.028 0.4 1 1040 127 127 GLU N N 120.249 0.4 1 1041 128 128 LYS H H 7.919 0.02 1 1042 128 128 LYS HA H 3.978 0.02 1 1043 128 128 LYS HB2 H 2.026 0.02 1 1044 128 128 LYS HD2 H 1.633 0.02 1 1045 128 128 LYS HG2 H 1.39 0.02 1 1046 128 128 LYS C C 179.838 0.4 1 1047 128 128 LYS CA C 59.938 0.4 1 1048 128 128 LYS CB C 31.691 0.4 1 1049 128 128 LYS CD C 29.748 0.4 1 1050 128 128 LYS CE C 42.06 0.4 1 1051 128 128 LYS CG C 25.204 0.4 1 1052 128 128 LYS N N 120.679 0.4 1 1053 129 129 LEU H H 8.142 0.02 1 1054 129 129 LEU HA H 4.128 0.02 1 1055 129 129 LEU HB2 H 1.835 0.02 1 1056 129 129 LEU HD2 H 0.973 0.02 1 1057 129 129 LEU HG H 2.262 0.02 1 1058 129 129 LEU C C 179.701 0.4 1 1059 129 129 LEU CA C 57.904 0.4 1 1060 129 129 LEU CB C 41.674 0.4 1 1061 129 129 LEU CD2 C 21.923 0.4 1 1062 129 129 LEU CG C 25.238 0.4 1 1063 129 129 LEU N N 118.553 0.4 1 1064 130 130 ALA H H 8.493 0.02 1 1065 130 130 ALA HA H 4.286 0.02 1 1066 130 130 ALA HB H 1.588 0.02 1 1067 130 130 ALA C C 182.027 0.4 1 1068 130 130 ALA CA C 55.358 0.4 1 1069 130 130 ALA CB C 17.069 0.4 1 1070 130 130 ALA N N 122.578 0.4 1 1071 131 131 LYS H H 8.065 0.02 1 1072 131 131 LYS HA H 4.124 0.02 1 1073 131 131 LYS HB2 H 1.958 0.02 1 1074 131 131 LYS HE2 H 3.543 0.02 1 1075 131 131 LYS HG2 H 1.626 0.02 1 1076 131 131 LYS C C 177.085 0.4 1 1077 131 131 LYS CA C 59.093 0.4 1 1078 131 131 LYS CB C 31.782 0.4 1 1079 131 131 LYS CD C 28.962 0.4 1 1080 131 131 LYS CE C 42.042 0.4 1 1081 131 131 LYS CG C 25.238 0.4 1 1082 131 131 LYS N N 120.347 0.4 1 1083 132 132 ASN H H 7.414 0.02 1 1084 132 132 ASN HA H 4.983 0.02 1 1085 132 132 ASN HB2 H 3.041 0.02 2 1086 132 132 ASN HB3 H 2.595 0.02 2 1087 132 132 ASN HD21 H 6.916 0.02 2 1088 132 132 ASN HD22 H 7.41 0.02 2 1089 132 132 ASN C C 173.584 0.4 1 1090 132 132 ASN CA C 52.195 0.4 1 1091 132 132 ASN CB C 39.21 0.4 1 1092 132 132 ASN N N 115.667 0.4 1 1093 132 132 ASN ND2 N 112.09 0.4 1 1094 133 133 LYS H H 8.105 0.02 1 1095 133 133 LYS HA H 3.956 0.02 1 1096 133 133 LYS HB2 H 2.074 0.02 1 1097 133 133 LYS HD2 H 1.65 0.02 1 1098 133 133 LYS HE2 H 2.588 0.02 1 1099 133 133 LYS HG2 H 1.407 0.02 1 1100 133 133 LYS C C 175.311 0.4 1 1101 133 133 LYS CA C 57.317 0.4 1 1102 133 133 LYS CB C 28.397 0.4 1 1103 133 133 LYS CD C 29.326 0.4 1 1104 133 133 LYS CE C 42.224 0.4 1 1105 133 133 LYS CG C 25.148 0.4 1 1106 133 133 LYS N N 113.9 0.4 1 1107 134 134 GLN H H 8.107 0.02 1 1108 134 134 GLN HA H 4.777 0.02 1 1109 134 134 GLN HB2 H 2.005 0.02 1 1110 134 134 GLN HB3 H 1.869 0.02 1 1111 134 134 GLN HE21 H 7.466 0.02 2 1112 134 134 GLN HE22 H 6.817 0.02 2 1113 134 134 GLN HG2 H 2.385 0.02 1 1114 134 134 GLN C C 174.87 0.4 1 1115 134 134 GLN CA C 53.89 0.4 1 1116 134 134 GLN CB C 33.095 0.4 1 1117 134 134 GLN CG C 33.715 0.4 1 1118 134 134 GLN N N 116.006 0.4 1 1119 134 134 GLN NE2 N 110.146 0.4 1 1120 135 135 LYS H H 7.974 0.02 1 1121 135 135 LYS CA C 54.077 0.4 1 1122 135 135 LYS CB C 33.433 0.4 1 1123 135 135 LYS N N 118.646 0.4 1 1124 136 136 PRO HA H 4.378 0.02 1 1125 136 136 PRO HB2 H 2.157 0.02 2 1126 136 136 PRO HB3 H 1.98 0.02 2 1127 136 136 PRO HG2 H 1.695 0.02 1 1128 136 136 PRO C C 174.976 0.4 1 1129 136 136 PRO CA C 62.255 0.4 1 1130 136 136 PRO CB C 32.147 0.4 1 1131 136 136 PRO CD C 50.217 0.4 1 1132 136 136 PRO CG C 27.418 0.4 1 1133 137 137 ILE H H 9.147 0.02 1 1134 137 137 ILE HA H 3.918 0.02 1 1135 137 137 ILE HB H 1.842 0.02 1 1136 137 137 ILE HD1 H 0.479 0.02 1 1137 137 137 ILE HG12 H 1.204 0.02 2 1138 137 137 ILE HG13 H 0.221 0.02 2 1139 137 137 ILE C C 176.126 0.4 1 1140 137 137 ILE CA C 59.969 0.4 1 1141 137 137 ILE CB C 36.848 0.4 1 1142 137 137 ILE N N 122.234 0.4 1 1143 138 138 THR H H 7.993 0.02 1 1144 138 138 THR HA H 4.765 0.02 1 1145 138 138 THR HB H 4.54 0.02 1 1146 138 138 THR HG2 H 1.36 0.02 1 1147 138 138 THR CA C 59.171 0.4 1 1148 138 138 THR CB C 68.488 0.4 1 1149 138 138 THR N N 118.389 0.4 1 1150 139 139 PRO HA H 4.071 0.02 1 1151 139 139 PRO HB2 H 2.42 0.02 1 1152 139 139 PRO HG2 H 1.885 0.02 1 1153 139 139 PRO C C 177.838 0.4 1 1154 139 139 PRO CA C 65.575 0.4 1 1155 139 139 PRO CB C 31.401 0.4 1 1156 139 139 PRO CG C 27.907 0.4 1 1157 140 140 GLU H H 8.569 0.02 1 1158 140 140 GLU HA H 3 0.02 1 1159 140 140 GLU HB2 H 2.044 0.02 2 1160 140 140 GLU HB3 H 1.909 0.02 2 1161 140 140 GLU HG2 H 2.232 0.02 1 1162 140 140 GLU C C 179.357 0.4 1 1163 140 140 GLU CA C 60.137 0.4 1 1164 140 140 GLU CB C 28.357 0.4 1 1165 140 140 GLU N N 114.648 0.4 1 1166 141 141 THR H H 7.579 0.02 1 1167 141 141 THR HA H 3.811 0.02 1 1168 141 141 THR HB H 4.023 0.02 1 1169 141 141 THR HG2 H 1.145 0.02 1 1170 141 141 THR C C 176.395 0.4 1 1171 141 141 THR CA C 66.113 0.4 1 1172 141 141 THR CB C 68.569 0.4 1 1173 141 141 THR CG2 C 22.241 0.4 1 1174 141 141 THR N N 118.215 0.4 1 1175 142 142 ALA H H 7.562 0.02 1 1176 142 142 ALA HA H 3.866 0.02 1 1177 142 142 ALA HB H 0.638 0.02 1 1178 142 142 ALA C C 178.302 0.4 1 1179 142 142 ALA CA C 55.332 0.4 1 1180 142 142 ALA CB C 16.606 0.4 1 1181 142 142 ALA N N 125.491 0.4 1 1182 143 143 GLU H H 8.787 0.02 1 1183 143 143 GLU HA H 3.742 0.02 1 1184 143 143 GLU HB2 H 2.1 0.02 1 1185 143 143 GLU HG2 H 2.413 0.02 1 1186 143 143 GLU C C 179.077 0.4 1 1187 143 143 GLU CA C 59.59 0.4 1 1188 143 143 GLU CB C 28.998 0.4 1 1189 143 143 GLU CG C 36.865 0.4 1 1190 143 143 GLU N N 117.991 0.4 1 1191 144 144 LYS H H 7.313 0.02 1 1192 144 144 LYS HA H 3.95 0.02 1 1193 144 144 LYS HB2 H 1.916 0.02 1 1194 144 144 LYS HG2 H 1.454 0.02 1 1195 144 144 LYS C C 177.781 0.4 1 1196 144 144 LYS CA C 59.37 0.4 1 1197 144 144 LYS CB C 31.718 0.4 1 1198 144 144 LYS CD C 25.057 0.4 1 1199 144 144 LYS CE C 42.315 0.4 1 1200 144 144 LYS CG C 28.872 0.4 1 1201 144 144 LYS N N 118.815 0.4 1 1202 145 145 LEU H H 7.326 0.02 1 1203 145 145 LEU HA H 4.153 0.02 1 1204 145 145 LEU HB2 H 1.79 0.02 1 1205 145 145 LEU HD1 H 0.723 0.02 1 1206 145 145 LEU HD2 H 0.083 0.02 1 1207 145 145 LEU HG H 1.49 0.02 1 1208 145 145 LEU C C 178.162 0.4 1 1209 145 145 LEU CA C 57.834 0.4 1 1210 145 145 LEU CB C 40.432 0.4 1 1211 145 145 LEU CD2 C 23.513 0.4 1 1212 145 145 LEU CG C 26.147 0.4 1 1213 145 145 LEU N N 119.589 0.4 1 1214 146 146 ALA H H 8.482 0.02 1 1215 146 146 ALA HA H 3.705 0.02 1 1216 146 146 ALA HB H 1.452 0.02 1 1217 146 146 ALA C C 178.574 0.4 1 1218 146 146 ALA CA C 55.543 0.4 1 1219 146 146 ALA CB C 17.663 0.4 1 1220 146 146 ALA N N 118.809 0.4 1 1221 147 147 ARG H H 7.714 0.02 1 1222 147 147 ARG HA H 4.175 0.02 1 1223 147 147 ARG HB2 H 1.958 0.02 1 1224 147 147 ARG HD2 H 3.201 0.02 1 1225 147 147 ARG HG2 H 1.589 0.02 1 1226 147 147 ARG C C 180.165 0.4 1 1227 147 147 ARG CA C 58.995 0.4 1 1228 147 147 ARG CB C 29.657 0.4 1 1229 147 147 ARG CD C 43.495 0.4 1 1230 147 147 ARG CG C 27.418 0.4 1 1231 147 147 ARG N N 116.011 0.4 1 1232 148 148 ASP H H 8.461 0.02 1 1233 148 148 ASP HA H 4.324 0.02 1 1234 148 148 ASP HB2 H 2.838 0.02 2 1235 148 148 ASP HB3 H 2.651 0.02 2 1236 148 148 ASP C C 178.284 0.4 1 1237 148 148 ASP CA C 57.501 0.4 1 1238 148 148 ASP CB C 40.172 0.4 1 1239 148 148 ASP N N 121.913 0.4 1 1240 149 149 LEU H H 8.364 0.02 1 1241 149 149 LEU HA H 4.365 0.02 1 1242 149 149 LEU HB2 H 1.876 0.02 1 1243 149 149 LEU HB3 H 1.748 0.02 1 1244 149 149 LEU HD1 H 0.685 0.02 2 1245 149 149 LEU HD2 H 0.768 0.02 2 1246 149 149 LEU C C 174.985 0.4 1 1247 149 149 LEU CA C 54.315 0.4 1 1248 149 149 LEU CB C 41.373 0.4 1 1249 149 149 LEU CD2 C 21.858 0.4 1 1250 149 149 LEU CG C 27.055 0.4 1 1251 149 149 LEU N N 115.324 0.4 1 1252 150 150 LYS H H 7.624 0.02 1 1253 150 150 LYS HA H 3.783 0.02 1 1254 150 150 LYS HB2 H 2.24 0.02 1 1255 150 150 LYS HD2 H 1.876 0.02 1 1256 150 150 LYS HG2 H 1.345 0.02 1 1257 150 150 LYS C C 177.003 0.4 1 1258 150 150 LYS CA C 57.457 0.4 1 1259 150 150 LYS CB C 27.73 0.4 1 1260 150 150 LYS CD C 29.417 0.4 1 1261 150 150 LYS CE C 42.405 0.4 1 1262 150 150 LYS CG C 24.875 0.4 1 1263 150 150 LYS N N 111.768 0.4 1 1264 151 151 ALA H H 8.248 0.02 1 1265 151 151 ALA HA H 2.979 0.02 1 1266 151 151 ALA HB H 1.079 0.02 1 1267 151 151 ALA C C 177.944 0.4 1 1268 151 151 ALA CA C 51.231 0.4 1 1269 151 151 ALA CB C 19.707 0.4 1 1270 151 151 ALA N N 119.649 0.4 1 1271 152 152 VAL H H 8.684 0.02 1 1272 152 152 VAL HA H 3.478 0.02 1 1273 152 152 VAL HB H 1.63 0.02 1 1274 152 152 VAL HG1 H 0.932 0.02 2 1275 152 152 VAL HG2 H 1.028 0.02 2 1276 152 152 VAL C C 176.367 0.4 1 1277 152 152 VAL CA C 66.127 0.4 1 1278 152 152 VAL CB C 32.285 0.4 1 1279 152 152 VAL CG1 C 20.85 0.4 2 1280 152 152 VAL CG2 C 22.059 0.4 2 1281 152 152 VAL N N 120.805 0.4 1 1282 153 153 LYS H H 6.865 0.02 1 1283 153 153 LYS HA H 4.344 0.02 1 1284 153 153 LYS HB2 H 2.027 0.02 2 1285 153 153 LYS HB3 H 1.677 0.02 2 1286 153 153 LYS HG2 H 1.153 0.02 2 1287 153 153 LYS HG3 H 1.53 0.02 2 1288 153 153 LYS C C 172.951 0.4 1 1289 153 153 LYS CA C 55.049 0.4 1 1290 153 153 LYS CB C 34.332 0.4 1 1291 153 153 LYS CD C 28.599 0.4 1 1292 153 153 LYS CE C 43.495 0.4 1 1293 153 153 LYS CG C 23.513 0.4 1 1294 153 153 LYS N N 108.179 0.4 1 1295 154 154 TYR H H 8.606 0.02 1 1296 154 154 TYR HA H 5.761 0.02 1 1297 154 154 TYR HB2 H 2.745 0.02 1 1298 154 154 TYR C C 174.216 0.4 1 1299 154 154 TYR CA C 55.91 0.4 1 1300 154 154 TYR CB C 40.457 0.4 1 1301 154 154 TYR N N 120.249 0.4 1 1302 155 155 VAL H H 8.271 0.02 1 1303 155 155 VAL HA H 4.138 0.02 1 1304 155 155 VAL HB H 1.88 0.02 1 1305 155 155 VAL HG1 H 0.571 0.02 1 1306 155 155 VAL HG2 H 0.638 0.02 1 1307 155 155 VAL C C 171.653 0.4 1 1308 155 155 VAL CA C 58.344 0.4 1 1309 155 155 VAL CB C 34.645 0.4 1 1310 155 155 VAL CG1 C 20.85 0.4 1 1311 155 155 VAL CG2 C 22.014 0.4 1 1312 155 155 VAL N N 121.448 0.4 1 1313 156 156 GLU H H 8.03 0.02 1 1314 156 156 GLU HA H 5.393 0.02 1 1315 156 156 GLU HB2 H 1.725 0.02 1 1316 156 156 GLU HG2 H 2.027 0.02 1 1317 156 156 GLU C C 175.89 0.4 1 1318 156 156 GLU CA C 53.775 0.4 1 1319 156 156 GLU CB C 31.521 0.4 1 1320 156 156 GLU CG C 34.321 0.4 1 1321 156 156 GLU N N 113.147 0.4 1 1322 157 157 CYS H H 8.838 0.02 1 1323 157 157 CYS HA H 5.324 0.02 1 1324 157 157 CYS HB2 H 2.714 0.02 2 1325 157 157 CYS HB3 H 2.334 0.02 2 1326 157 157 CYS C C 171.554 0.4 1 1327 157 157 CYS CA C 55.749 0.4 1 1328 157 157 CYS CB C 32.041 0.4 1 1329 157 157 CYS N N 111.91 0.4 1 1330 158 158 SER H H 8.277 0.02 1 1331 158 158 SER HA H 5.211 0.02 1 1332 158 158 SER HB2 H 3.879 0.02 2 1333 158 158 SER HB3 H 4.025 0.02 2 1334 158 158 SER C C 176.246 0.4 1 1335 158 158 SER CA C 55.892 0.4 1 1336 158 158 SER CB C 65.035 0.4 1 1337 158 158 SER N N 110.284 0.4 1 1338 159 159 ALA H H 9.297 0.02 1 1339 159 159 ALA HA H 4.21 0.02 1 1340 159 159 ALA HB H 1.735 0.02 1 1341 159 159 ALA C C 177.03 0.4 1 1342 159 159 ALA CA C 54.522 0.4 1 1343 159 159 ALA CB C 18.828 0.4 1 1344 159 159 ALA N N 132.318 0.4 1 1345 160 160 LEU H H 7.361 0.02 1 1346 160 160 LEU HA H 3.307 0.02 1 1347 160 160 LEU HB2 H 1.12 0.02 1 1348 160 160 LEU HD1 H 0.139 0.02 1 1349 160 160 LEU C C 177.619 0.4 1 1350 160 160 LEU CA C 57.497 0.4 1 1351 160 160 LEU CB C 43.255 0.4 1 1352 160 160 LEU CD2 C 23.24 0.4 1 1353 160 160 LEU CG C 25.783 0.4 1 1354 160 160 LEU N N 118.308 0.4 1 1355 161 161 THR H H 8.109 0.02 1 1356 161 161 THR HA H 4.218 0.02 1 1357 161 161 THR HB H 4.447 0.02 1 1358 161 161 THR HG2 H 1.157 0.02 1 1359 161 161 THR C C 176.064 0.4 1 1360 161 161 THR CA C 61.435 0.4 1 1361 161 161 THR CB C 69.809 0.4 1 1362 161 161 THR CG2 C 21.605 0.4 1 1363 161 161 THR N N 106.273 0.4 1 1364 162 162 GLN H H 7.457 0.02 1 1365 162 162 GLN HA H 3.923 0.02 1 1366 162 162 GLN HB2 H 2.643 0.02 1 1367 162 162 GLN HE21 H 7.248 0.02 2 1368 162 162 GLN HE22 H 6.418 0.02 2 1369 162 162 GLN HG2 H 2.281 0.02 2 1370 162 162 GLN HG3 H 2.088 0.02 2 1371 162 162 GLN C C 174.988 0.4 1 1372 162 162 GLN CA C 59.015 0.4 1 1373 162 162 GLN CB C 25.425 0.4 1 1374 162 162 GLN CG C 34.412 0.4 1 1375 162 162 GLN N N 112.744 0.4 1 1376 162 162 GLN NE2 N 110.979 0.4 1 1377 163 163 LYS H H 7.831 0.02 1 1378 163 163 LYS HA H 4.163 0.02 1 1379 163 163 LYS HB2 H 1.587 0.02 1 1380 163 163 LYS HG2 H 1.384 0.02 1 1381 163 163 LYS C C 177.322 0.4 1 1382 163 163 LYS CA C 58.055 0.4 1 1383 163 163 LYS CB C 32.041 0.4 1 1384 163 163 LYS CD C 28.872 0.4 1 1385 163 163 LYS CE C 42.133 0.4 1 1386 163 163 LYS CG C 24.693 0.4 1 1387 163 163 LYS N N 124.132 0.4 1 1388 164 164 GLY H H 9.133 0.02 1 1389 164 164 GLY HA2 H 4.293 0.02 2 1390 164 164 GLY HA3 H 3.86 0.02 2 1391 164 164 GLY C C 174.825 0.4 1 1392 164 164 GLY CA C 46.375 0.4 1 1393 164 164 GLY N N 114.473 0.4 1 1394 165 165 LEU H H 7.4 0.02 1 1395 165 165 LEU HA H 3.792 0.02 1 1396 165 165 LEU HB2 H 2.026 0.02 1 1397 165 165 LEU HD2 H 1.149 0.02 1 1398 165 165 LEU C C 176.722 0.4 1 1399 165 165 LEU CA C 58.737 0.4 1 1400 165 165 LEU CB C 43.498 0.4 1 1401 165 165 LEU CD2 C 25.874 0.4 1 1402 165 165 LEU CG C 27.237 0.4 1 1403 165 165 LEU N N 121.187 0.4 1 1404 166 166 LYS H H 8.58 0.02 1 1405 166 166 LYS HA H 4.151 0.02 1 1406 166 166 LYS HB2 H 2.058 0.02 1 1407 166 166 LYS HG2 H 1.642 0.02 1 1408 166 166 LYS C C 179.204 0.4 1 1409 166 166 LYS CA C 60.208 0.4 1 1410 166 166 LYS CB C 31.801 0.4 1 1411 166 166 LYS CD C 29.417 0.4 1 1412 166 166 LYS CE C 41.86 0.4 1 1413 166 166 LYS CG C 25.238 0.4 1 1414 166 166 LYS N N 116.769 0.4 1 1415 167 167 ASN H H 8.125 0.02 1 1416 167 167 ASN HA H 4.349 0.02 1 1417 167 167 ASN HB2 H 2.677 0.02 2 1418 167 167 ASN HB3 H 2.581 0.02 2 1419 167 167 ASN C C 175.612 0.4 1 1420 167 167 ASN CA C 56.686 0.4 1 1421 167 167 ASN CB C 38.65 0.4 1 1422 167 167 ASN N N 114.773 0.4 1 1423 168 168 VAL H H 7.365 0.02 1 1424 168 168 VAL HA H 2.91 0.02 1 1425 168 168 VAL HB H 1.811 0.02 1 1426 168 168 VAL HG1 H 0.792 0.02 1 1427 168 168 VAL C C 175.77 0.4 1 1428 168 168 VAL CA C 67.103 0.4 1 1429 168 168 VAL CB C 30.845 0.4 1 1430 168 168 VAL CG1 C 20.61 0.4 2 1431 168 168 VAL CG2 C 21.424 0.4 2 1432 168 168 VAL N N 117.042 0.4 1 1433 169 169 PHE H H 6.368 0.02 1 1434 169 169 PHE HA H 3.751 0.02 1 1435 169 169 PHE HB2 H 2.692 0.02 2 1436 169 169 PHE HB3 H 2.335 0.02 2 1437 169 169 PHE C C 178.202 0.4 1 1438 169 169 PHE CA C 61.975 0.4 1 1439 169 169 PHE CB C 38.99 0.4 1 1440 169 169 PHE N N 113.983 0.4 1 1441 170 170 ASP H H 7.906 0.02 1 1442 170 170 ASP HA H 4.338 0.02 1 1443 170 170 ASP HB2 H 2.684 0.02 1 1444 170 170 ASP C C 178.596 0.4 1 1445 170 170 ASP CA C 57.54 0.4 1 1446 170 170 ASP CB C 39.481 0.4 1 1447 170 170 ASP N N 120.793 0.4 1 1448 171 171 GLU H H 8.048 0.02 1 1449 171 171 GLU HA H 3.989 0.02 1 1450 171 171 GLU HB2 H 1.738 0.02 1 1451 171 171 GLU HG2 H 2.37 0.02 1 1452 171 171 GLU C C 179.405 0.4 1 1453 171 171 GLU CA C 58.13 0.4 1 1454 171 171 GLU CB C 27.546 0.4 1 1455 171 171 GLU CG C 35.048 0.4 1 1456 171 171 GLU N N 115.893 0.4 1 1457 172 172 ALA H H 7.937 0.02 1 1458 172 172 ALA HA H 3.759 0.02 1 1459 172 172 ALA HB H 1.372 0.02 1 1460 172 172 ALA C C 177.968 0.4 1 1461 172 172 ALA CA C 55.395 0.4 1 1462 172 172 ALA CB C 17.084 0.4 1 1463 172 172 ALA N N 123.733 0.4 1 1464 173 173 ILE H H 7.645 0.02 1 1465 173 173 ILE HA H 3.314 0.02 1 1466 173 173 ILE HB H 1.834 0.02 1 1467 173 173 ILE HD1 H 0.87 0.02 1 1468 173 173 ILE HG12 H 0.318 0.02 1 1469 173 173 ILE C C 177.082 0.4 1 1470 173 173 ILE CA C 65.755 0.4 1 1471 173 173 ILE CB C 37.448 0.4 1 1472 173 173 ILE CD1 C 14.066 0.4 1 1473 173 173 ILE CG1 C 30.143 0.4 2 1474 173 173 ILE CG2 C 18.154 0.4 2 1475 173 173 ILE N N 116.213 0.4 1 1476 174 174 LEU H H 7.703 0.02 1 1477 174 174 LEU HA H 3.76 0.02 1 1478 174 174 LEU HB2 H 1.697 0.02 2 1479 174 174 LEU HB3 H 1.362 0.02 2 1480 174 174 LEU HD2 H 0.738 0.02 1 1481 174 174 LEU C C 179.847 0.4 1 1482 174 174 LEU CA C 58.049 0.4 1 1483 174 174 LEU CB C 40.973 0.4 1 1484 174 174 LEU CD2 C 23.739 0.4 1 1485 174 174 LEU CG C 26.51 0.4 1 1486 174 174 LEU N N 116.496 0.4 1 1487 175 175 ALA H H 7.927 0.02 1 1488 175 175 ALA HA H 4.057 0.02 1 1489 175 175 ALA HB H 1.356 0.02 1 1490 175 175 ALA C C 178.605 0.4 1 1491 175 175 ALA CA C 54.004 0.4 1 1492 175 175 ALA CB C 18.464 0.4 1 1493 175 175 ALA N N 118.76 0.4 1 1494 176 176 ALA H H 7.647 0.02 1 1495 176 176 ALA HA H 4.035 0.02 1 1496 176 176 ALA HB H 1.328 0.02 1 1497 176 176 ALA C C 178.284 0.4 1 1498 176 176 ALA CA C 53.335 0.4 1 1499 176 176 ALA CB C 18.985 0.4 1 1500 176 176 ALA N N 117.532 0.4 1 1501 177 177 LEU H H 7.419 0.02 1 1502 177 177 LEU HA H 4.21 0.02 1 1503 177 177 LEU HB2 H 1.649 0.02 2 1504 177 177 LEU HB3 H 1.433 0.02 2 1505 177 177 LEU HG H 0.468 0.02 1 1506 177 177 LEU C C 174.091 0.4 1 1507 177 177 LEU CA C 55.035 0.4 1 1508 177 177 LEU CB C 42.34 0.4 1 1509 177 177 LEU CD2 C 21.968 0.4 1 1510 177 177 LEU CG C 25.42 0.4 1 1511 177 177 LEU N N 115.22 0.4 1 1512 178 178 GLU H H 7.524 0.02 1 1513 178 178 GLU CA C 54.575 0.4 1 1514 178 178 GLU CB C 29.165 0.4 1 1515 178 178 GLU N N 120.848 0.4 1 stop_ save_