data_4700 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of Cdc42 bound to the GTPase Binding Domain of PAK ; _BMRB_accession_number 4700 _BMRB_flat_file_name bmr4700.str _Entry_type original _Submission_date 2000-03-23 _Accession_date 2000-03-23 _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 Morreale Angela . . 2 Venkatesan Meenakshi . . 3 Mott Helen R. . 4 Owen Darerca . . 5 Nietlispach Daniel . . 6 Lowe Peter N. . 7 Laue Ernest D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1276 "13C chemical shifts" 741 "15N chemical shifts" 224 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-29 update BMRB 'Updating non-standard residue' 2000-12-18 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Morreale, A., Venkatesan, M., Mott, H.R., Owen, D., Nietlispach, D., Lowe, P.N., and Laue, E.D., "Structure of Cdc42 bound to the GTPase Binding Domain of PAK," Nat. Struct. Biol. 7, 384-388 (2000). ; _Citation_title 'Structure of Cdc42 bound to the GTPase Binding Domain of PAK' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20264518 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Morreale Angela . . 2 Venkatesan Meenakshi . . 3 Mott Helen R. . 4 Owen Darerca . . 5 Nietlispach Daniel . . 6 Lowe Peter N. . 7 Laue Ernest D. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 384 _Page_last 388 _Year 2000 _Details . loop_ _Keyword 'G protein' kinase stop_ save_ ################################## # Molecular system description # ################################## save_Cdc42_and_PAK _Saveframe_category molecular_system _Mol_system_name 'Cdc42 + fragment of PAK' _Abbreviation_common 'Cdc42 and PAK' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Cdc42 $Cdc42 PAK $PAK stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Cdc42: small GTPase involved in cytoskeletal regulation' 'PAK: Ser/Thr kinase Cdc42 binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cdc42 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Cdc42 _Name_variant Q61L _Abbreviation_common Cdc42 _Molecular_mass 20430.40 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MQTIKCVVVGDGAVGKTCLL ISYTTNKFPSEYVPTVFDNY AVTVMIGGEPYTLGLFDTAG LEDYDRLRPLSYPQTDVFLV CFSVVSPSSFENVKEKWVPE ITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPE TAEKLARDLKAVKYVECSAL TQKGLKNVFDEAILAALEPP EPKKX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLN 3 3 THR 4 4 ILE 5 5 LYS 6 6 CYS 7 7 VAL 8 8 VAL 9 9 VAL 10 10 GLY 11 11 ASP 12 12 GLY 13 13 ALA 14 14 VAL 15 15 GLY 16 16 LYS 17 17 THR 18 18 CYS 19 19 LEU 20 20 LEU 21 21 ILE 22 22 SER 23 23 TYR 24 24 THR 25 25 THR 26 26 ASN 27 27 LYS 28 28 PHE 29 29 PRO 30 30 SER 31 31 GLU 32 32 TYR 33 33 VAL 34 34 PRO 35 35 THR 36 36 VAL 37 37 PHE 38 38 ASP 39 39 ASN 40 40 TYR 41 41 ALA 42 42 VAL 43 43 THR 44 44 VAL 45 45 MET 46 46 ILE 47 47 GLY 48 48 GLY 49 49 GLU 50 50 PRO 51 51 TYR 52 52 THR 53 53 LEU 54 54 GLY 55 55 LEU 56 56 PHE 57 57 ASP 58 58 THR 59 59 ALA 60 60 GLY 61 61 LEU 62 62 GLU 63 63 ASP 64 64 TYR 65 65 ASP 66 66 ARG 67 67 LEU 68 68 ARG 69 69 PRO 70 70 LEU 71 71 SER 72 72 TYR 73 73 PRO 74 73 GLN 75 75 THR 76 76 ASP 77 77 VAL 78 78 PHE 79 79 LEU 80 80 VAL 81 81 CYS 82 82 PHE 83 83 SER 84 84 VAL 85 85 VAL 86 86 SER 87 87 PRO 88 88 SER 89 89 SER 90 90 PHE 91 91 GLU 92 92 ASN 93 93 VAL 94 94 LYS 95 95 GLU 96 96 LYS 97 97 TRP 98 98 VAL 99 99 PRO 100 100 GLU 101 101 ILE 102 102 THR 103 103 HIS 104 104 HIS 105 105 CYS 106 106 PRO 107 107 LYS 108 108 THR 109 109 PRO 110 110 PHE 111 111 LEU 112 112 LEU 113 113 VAL 114 114 GLY 115 115 THR 116 116 GLN 117 117 ILE 118 118 ASP 119 119 LEU 120 120 ARG 121 121 ASP 122 122 ASP 123 123 PRO 124 124 SER 125 125 THR 126 126 ILE 127 127 GLU 128 128 LYS 129 129 LEU 130 130 ALA 131 131 LYS 132 132 ASN 133 133 LYS 134 134 GLN 135 135 LYS 136 136 PRO 137 137 ILE 138 138 THR 139 139 PRO 140 140 GLU 141 141 THR 142 142 ALA 143 143 GLU 144 144 LYS 145 145 LEU 146 146 ALA 147 147 ARG 148 148 ASP 149 149 LEU 150 150 LYS 151 151 ALA 152 152 VAL 153 153 LYS 154 154 TYR 155 155 VAL 156 156 GLU 157 157 CYS 158 158 SER 159 159 ALA 160 160 LEU 161 161 THR 162 162 GLN 163 163 LYS 164 164 GLY 165 165 LEU 166 166 LYS 167 167 ASN 168 168 VAL 169 169 PHE 170 170 ASP 171 171 GLU 172 172 ALA 173 173 ILE 174 174 LEU 175 175 ALA 176 176 ALA 177 177 LEU 178 178 GLU 179 179 PRO 180 180 PRO 181 181 GLU 182 182 PRO 183 183 LYS 184 184 LYS 185 185 GNP 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 BMRB 15424 Cdc42(T35A) 96.22 178 98.88 98.88 2.09e-124 PDB 1A4R "G12v Mutant Of Human Placental Cdc42 Gtpase In The Gdp Form" 99.46 191 98.91 98.91 3.73e-128 PDB 1AJE "Cdc42 From Human, Nmr, 20 Structures" 99.46 194 99.46 99.46 5.52e-130 PDB 1AM4 "Complex Between Cdc42hs.Gmppnp And P50 Rhogap (H. Sapiens)" 95.14 177 98.86 99.43 1.00e-122 PDB 1AN0 "Cdc42hs-Gdp Complex" 98.92 190 98.91 98.91 2.87e-127 PDB 1CEE "Solution Structure Of Cdc42 In Complex With The Gtpase Binding Domain Of Wasp" 96.76 179 99.44 99.44 6.62e-126 PDB 1CF4 "Cdc42ACK GTPASE-Binding Domain Complex" 99.46 184 100.00 100.00 1.44e-130 PDB 1DOA "Structure Of The Rho Family Gtp-Binding Protein Cdc42 In Complex With The Multifunctional Regulator Rhogdi" 99.46 191 99.46 99.46 9.57e-130 PDB 1E0A "Cdc42 Complexed With The Gtpase Binding Domain Of P21 Activated Kinase" 99.46 184 100.00 100.00 1.44e-130 PDB 1EES "Solution Structure Of Cdc42hs Complexed With A Peptide Derived From P-21 Activated Kinase, Nmr, 20 Structures" 96.22 178 99.44 99.44 4.24e-125 PDB 1GRN "Crystal Structure Of The Cdc42CDC42GAPALF3 COMPLEX." 99.46 191 99.46 99.46 1.67e-129 PDB 1GZS "Crystal Structure Of The Complex Between The Gef Domain Of The Salmonella Typhimurium Sope Toxin And Human Cdc42" 96.22 180 99.44 99.44 4.80e-125 PDB 1KI1 "Guanine Nucleotide Exchange Region Of Intersectin In Complex With Cdc42" 99.46 188 99.46 99.46 6.35e-130 PDB 1KZ7 "Crystal Structure Of The DhPH FRAGMENT OF MURINE DBS IN Complex With The Placental Isoform Of Human Cdc42" 99.46 188 99.46 99.46 6.35e-130 PDB 1KZG Dbscdc42(Y889f) 99.46 188 99.46 99.46 6.35e-130 PDB 1NF3 "Structure Of Cdc42 In A Complex With The Gtpase-Binding Domain Of The Cell Polarity Protein, Par6" 99.46 195 99.46 100.00 1.27e-129 PDB 2ASE "Nmr Structure Of The F28l Mutant Of Cdc42hs" 96.22 178 98.88 98.88 2.90e-124 PDB 2DFK "Crystal Structure Of The Cdc42-Collybistin Ii Complex" 99.46 194 99.46 99.46 2.05e-129 PDB 2KB0 Cdc42(T35a) 96.22 178 98.88 98.88 2.09e-124 PDB 2NGR "Transition State Complex For Gtp Hydrolysis By Cdc42: Comparisons Of The High Resolution Structures For Cdc42 Bound To The Acti" 99.46 191 99.46 99.46 1.67e-129 PDB 2ODB "The Crystal Structure Of Human Cdc42 In Complex With The Crib Domain Of Human P21-Activated Kinase 6 (Pak6)" 99.46 192 99.46 99.46 1.36e-129 PDB 2QRZ "Cdc42 Bound To Gmp-Pcp: Induced Fit By Effector Is Required" 99.46 189 99.46 99.46 1.25e-129 PDB 2WM9 "Structure Of The Complex Between Dock9 And Cdc42." 99.46 190 99.46 99.46 1.02e-129 PDB 2WMN "Structure Of The Complex Between Dock9 And Cdc42-Gdp." 99.46 190 99.46 99.46 1.02e-129 PDB 2WMO "Structure Of The Complex Between Dock9 And Cdc42" 99.46 190 99.46 99.46 1.02e-129 PDB 3EG5 "Crystal Structure Of Mdia1-Tsh Gbd-Fh3 In Complex With Cdc42-Gmppnp" 96.22 178 98.88 99.44 7.99e-125 PDB 3GCG "Crystal Structure Of Map And Cdc42 Complex" 95.68 182 99.44 99.44 8.45e-124 PDB 3QBV "Structure Of Designed Orthogonal Interaction Between Cdc42 And Nucleotide Exchange Domains Of Intersectin" 96.22 178 98.88 98.88 8.20e-124 PDB 3VHL "Crystal Structure Of The Dhr-2 Domain Of Dock8 In Complex With Cdc42 (T17n Mutant)" 99.46 195 98.91 98.91 2.55e-129 PDB 4DID "Crystal Structure Of Salmonella Effector N-Terminal Domain Sopb In Complex With Cdc42" 98.92 193 99.45 99.45 3.61e-129 PDB 4ITR "Crystal Structure Of Ibpafic2-h3717a In Complex With Adenylylated Cdc42" 99.46 191 99.46 99.46 1.67e-129 PDB 4JS0 "Complex Of Cdc42 With The Crib-pr Domain Of Irsp53" 96.22 178 98.88 98.88 8.76e-124 PDB 4YC7 "Crystal Structure Of Human Fmnl2 Gbd-fh3 Domains Bound To Cdc42-gppnhp" 96.76 181 98.88 99.44 1.53e-125 PDB 4YDH "The Structure Of Human Fmnl1 N-terminal Domains Bound To Cdc42" 96.76 181 98.88 99.44 1.53e-125 DBJ BAB22563 "unnamed protein product [Mus musculus]" 99.46 191 99.46 99.46 1.67e-129 DBJ BAC16312 "Raichu-1054X [synthetic construct]" 94.59 762 98.86 99.43 4.26e-116 DBJ BAC34669 "unnamed protein product [Mus musculus]" 99.46 191 98.91 99.46 1.00e-128 DBJ BAC35825 "unnamed protein product [Mus musculus]" 99.46 191 99.46 99.46 1.67e-129 DBJ BAE01909 "unnamed protein product [Macaca fascicularis]" 99.46 191 98.91 99.46 5.44e-129 EMBL CAA90215 "CDC42 GTP-binding protein [Canis lupus familiaris]" 99.46 191 99.46 99.46 1.67e-129 EMBL CAB57325 "hypothetical protein [Homo sapiens]" 100.54 191 97.31 98.39 9.48e-127 EMBL CAB57326 "hypothetical protein [Homo sapiens]" 99.46 191 99.46 99.46 1.67e-129 EMBL CAB57327 "hypothetical protein [Homo sapiens]" 76.76 142 99.30 99.30 1.14e-97 EMBL CAB57328 "hypothetical protein [Homo sapiens]" 62.70 116 99.14 99.14 9.45e-78 GB AAA37410 "CDC42Mm, partial [Mus musculus]" 99.46 191 99.46 99.46 1.67e-129 GB AAA52494 "GTP-binding protein G25K [Homo sapiens]" 100.54 191 97.31 98.39 9.48e-127 GB AAA52592 "GTP-binding protein G25K [Homo sapiens]" 99.46 191 99.46 99.46 1.67e-129 GB AAB40051 "cdc42b [Mus musculus]" 100.54 191 97.31 98.39 9.48e-127 GB AAC00027 "CDC42 [Gallus gallus]" 99.46 191 99.46 99.46 1.95e-129 REF NP_001003254 "cell division control protein 42 homolog precursor [Canis lupus familiaris]" 99.46 191 99.46 99.46 1.67e-129 REF NP_001008027 "cell division control protein 42 homolog isoform 1 [Xenopus (Silurana) tropicalis]" 100.54 191 97.31 98.39 9.48e-127 REF NP_001017070 "cell division control protein 42 homolog isoform 2 [Xenopus (Silurana) tropicalis]" 99.46 191 99.46 99.46 1.99e-129 REF NP_001018130 "cell division control protein 42 homolog isoform 2 [Danio rerio]" 99.46 191 97.28 98.91 4.18e-127 REF NP_001034891 "cell division control protein 42 homolog isoform 1 precursor [Homo sapiens]" 99.46 191 99.46 99.46 1.67e-129 SP P60766 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 99.46 191 99.46 99.46 1.67e-129 SP P60952 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 99.46 191 99.46 99.46 1.67e-129 SP P60953 "RecName: Full=Cell division control protein 42 homolog; AltName: Full=G25K GTP-binding protein; Flags: Precursor" 99.46 191 99.46 99.46 1.67e-129 SP Q007T2 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor" 99.46 191 99.46 99.46 1.67e-129 SP Q2KJ93 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor" 99.46 191 99.46 99.46 1.67e-129 TPG DAA32122 "TPA: cell division control protein 42 homolog precursor [Bos taurus]" 89.19 165 99.39 99.39 3.73e-115 stop_ save_ save_PAK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'p21 activated kinase' _Abbreviation_common PAK _Molecular_mass 5127.64 _Mol_thiol_state 'not present' _Details . _Residue_count 46 _Mol_residue_sequence ; GSISLPSDFEHTIHVGFDAV TGEFTGMPEQWARLLQTSNI TKSEQK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1073 GLY 2 1074 SER 3 1075 ILE 4 1076 SER 5 1077 LEU 6 1078 PRO 7 1079 SER 8 1080 ASP 9 1081 PHE 10 1082 GLU 11 1083 HIS 12 1084 THR 13 1085 ILE 14 1086 HIS 15 1087 VAL 16 1088 GLY 17 1089 PHE 18 1090 ASP 19 1091 ALA 20 1092 VAL 21 1093 THR 22 1094 GLY 23 1095 GLU 24 1096 PHE 25 1097 THR 26 1198 GLY 27 1099 MET 28 1100 PRO 29 1101 GLU 30 1102 GLN 31 1103 TRP 32 1104 ALA 33 1105 ARG 34 1106 LEU 35 1107 LEU 36 1108 GLN 37 1109 THR 38 1110 SER 39 1111 ASN 40 1112 ILE 41 1113 THR 42 1114 LYS 43 1115 SER 44 1116 GLU 45 1117 GLN 46 1118 LYS stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-03-03 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 SWISS-PROT Q13153 'PAK1_HUMAN Serine/threonine-protein kinasePAK 1 (p21-activated kinase 1) (PAK-1) (p65-PAK)(Alpha-PAK)' 8.44 545 100 100 3e-18 SWISS-PROT O88643 'PAK1_MOUSE Serine/threonine-protein kinase PAK1 (p21-activated kinase 1) (PAK-1) (p65-PAK) (Alpha-PAK)(CDC42/RAC effecto' 8.44 545 100 100 3e-18 SWISS-PROT Q08E52 'PAK1_BOVIN Serine/threonine-protein kinasePAK 1 (p21-activated kinase 1) (PAK-1) (p65-PAK)(Alpha-PAK)' 8.46 544 100 100 3e-18 SWISS-PROT P35465 'PAK1_RAT Serine/threonine-protein kinase PAK 1(p21-activated kinase 1) (PAK-1) (p68-PAK) (Alpha-PAK)(Protein kinase MUK2' 8.46 544 100 100 3e-18 REF XP_001363384.1 'PREDICTED: similar to p21(CDKN1A)-activated kinase 1 isoform 2 [Monodelphisdomestica]' 8.36 550 100 100 3e-18 REF XP_001363301.1 'PREDICTED: similar to p21(CDKN1A)-activated kinase 1 isoform 1 [Monodelphisdomestica]' 8.44 545 100 100 3e-18 REF NP_035165.2 'p21 (CDKN1A)-activated kinase 1 [Musmusculus]' 8.46 544 100 100 3e-18 REF NP_001070366.1 'p21/Cdc42/Rac1-activated kinase 1(STE20 homolog, yeast) [Bos taurus]' 8.46 544 100 100 3e-18 REF XP_508657.2 'PREDICTED: p21-activated kinase 1[Pan troglodytes]' 8.58 536 100 100 3e-18 PRF 2003404A 'Ser/Thr protein kinase' 8.46 544 98 98 10e-18 GenBank ACA13260.1 'dsRed1/Pak1/Rac1/ECFP fusion protein[synthetic construct]' 5.94 775 100 100 3e-18 GenBank ACA13261.1 'dsRed1/Pak1/Cdc42/ECFP fusion protein[synthetic construct]' 6.10 754 100 100 3e-18 GenBank EAW75028.1 'p21/Cdc42/Rac1-activated kinase 1(STE20 homolog, yeast), isoform CRA_b [Homo sapiens]' 8.32 553 100 100 3e-18 GenBank EDL16325.1 'p21 (CDKN1A)-activated kinase 1,isoform CRA_c [Mus musculus]' 8.66 531 100 100 3e-18 GenBank EDM18463.1 'p21 (CDKN1A)-activated kinase 1,isoform CRA_b [Rattus norvegicus]' 9.43 488 100 100 3e-18 EMBL CAF91245.1 'unnamed protein product [Tetraodonnigroviridis]' 7.99 576 98 98 2e-17 EMBL CAN87991.1 'novel protein similar to p21(CDKN1A)-activated kinase 2 (pak2, wu:fc52b03) [Daniorerio]' 8.57 537 98 98 2e-17 EMBL CAN87992.1 'novel protein similar to p21(CDKN1A)-activated kinase 2 (pak2, wu:fc52b03) [Daniorerio]' 18.11 254 98 98 2e-17 EMBL CAF94511.1 'unnamed protein product [Tetraodonnigroviridis]' 47.92 96 100 100 10e-06 DBJ BAC16311.1 'Raichu-1011X [synthetic construct]' 6.03 763 100 100 3e-18 DBJ BAC16312.1 'Raichu-1054X [synthetic construct]' 6.04 762 100 100 3e-18 DBJ BAF85787.1 'unnamed protein product [Homo sapiens]' 8.32 553 100 100 3e-18 PDB 1F3M 'A Chain A, Crystal Structure Of HumanSerineTHREONINE KINASE PAK1' 57.50 80 100 100 3e-18 PDB 1E0A 'B Chain B, Cdc42 Complexed With The GtpaseBinding Domain Of P21 Activated Kinase' 100.00 46 100 100 2e-19 PDB 2QME 'I Chain I, Crystal Structure Of Human Rac3In Complex With Crib Domain Of Human P21-ActivatedKinase 1 (Pak1)' 127.78 36 100 100 3e-13 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_GNP _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' _BMRB_code . _PDB_code GNP _Standard_residue_derivative . _Molecular_mass 522.196 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Aug 26 12:50:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P . 0 . ? O1G O1G O . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? N3B N3B N . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3A O3A O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? HNB3 HNB3 H . 0 . ? HOB2 HOB2 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'2 H5'2 H . 0 . ? H5'1 H5'1 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB PG O1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING PG N3B ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? SING N3B PB ? ? SING N3B HNB3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING O3A PA ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'2 ? ? SING C5' H5'1 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? DOUB C6 O6 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING N1 HN1 ? ? SING C2 N2 ? ? DOUB C2 N3 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING N3 C4 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $Cdc42 Human 9606 Eukaryota Metazoa Homo sapiens cytoplasm $PAK Rat 10116 Eukaryota Metazoa Rattus norvegicus . 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 'recombinant technology' . . . . . $PAK 'recombinant technology' . . . . . 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 . mM 0.7 1.0 '[U-13C; U-15N]' $PAK . mM 0.7 1.0 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version 3.3 loop_ _Task 'DATA PROCESSING' stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Task ASSIGNMENT stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-edited_NOESy_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESy' _Sample_label $sample_1 save_ save_13C-edited_NOEsy_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOEsy' _Sample_label $sample_1 save_ save_HCCH-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label $sample_1 save_ save_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HBHA(CBCACO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label $sample_1 save_ save_13C/15N-Xfiltered_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C/15N-Xfiltered NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 pH temperature 298 1 K 'ionic strength' 55 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; 2 sets of signals were observed for the C-terminal residues, probably due to cis-trans isomerization of the C-terminal prolines ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Cdc42 _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 MET CA C 55.83 0.00 1 2 . 1 MET HA H 4.419 0.002 1 3 . 1 MET CB C 33.14 0.00 1 4 . 1 MET CG C 31.59 0.00 1 5 . 1 MET CE C 16.75 0.06 1 6 . 1 MET HE H 2.089 0.009 1 7 . 1 MET HB2 H 2.044 0.009 1 8 . 1 MET HB3 H 2.044 0.009 1 9 . 1 MET HG2 H 2.539 0.006 1 10 . 1 MET HG3 H 2.539 0.006 1 11 . 2 GLN CA C 56.00 0.09 1 12 . 2 GLN HA H 4.342 0.017 1 13 . 2 GLN CB C 29.18 0.00 1 14 . 2 GLN CG C 34.14 0.00 1 15 . 2 GLN NE2 N 110.55 0.02 1 16 . 2 GLN HE21 H 6.870 0.004 2 17 . 2 GLN HE22 H 7.522 0.006 2 18 . 2 GLN HB2 H 1.793 0.005 1 19 . 2 GLN HB3 H 1.793 0.005 1 20 . 2 GLN HG2 H 2.212 0.016 1 21 . 2 GLN HG3 H 2.212 0.016 1 22 . 3 THR N N 114.56 0.04 1 23 . 3 THR H H 8.308 0.010 1 24 . 3 THR CA C 60.60 0.11 1 25 . 3 THR HA H 5.559 0.007 1 26 . 3 THR CB C 71.45 0.07 1 27 . 3 THR HB H 4.156 0.008 1 28 . 3 THR CG2 C 20.93 0.04 1 29 . 3 THR HG2 H 1.218 0.008 1 30 . 4 ILE N N 124.18 0.01 1 31 . 4 ILE H H 9.014 0.009 1 32 . 4 ILE CA C 60.27 0.07 1 33 . 4 ILE HA H 4.454 0.005 1 34 . 4 ILE HB H 1.752 0.006 1 35 . 4 ILE CG1 C 27.37 0.05 1 36 . 4 ILE HG12 H 1.051 0.017 2 37 . 4 ILE HG13 H 1.701 0.017 2 38 . 4 ILE CG2 C 17.39 0.03 1 39 . 4 ILE HG2 H 0.731 0.006 1 40 . 4 ILE CD1 C 14.84 0.04 1 41 . 4 ILE HD1 H 0.701 0.018 1 42 . 5 LYS N N 129.97 0.06 1 43 . 5 LYS H H 10.734 0.008 1 44 . 5 LYS CA C 55.83 0.09 1 45 . 5 LYS HA H 5.072 0.007 1 46 . 6 CYS N N 129.98 0.04 1 47 . 6 CYS H H 9.531 0.007 1 48 . 6 CYS CA C 55.97 0.04 1 49 . 6 CYS HA H 5.711 0.012 1 50 . 6 CYS CB C 29.18 0.00 1 51 . 6 CYS HB2 H 3.075 0.000 1 52 . 6 CYS HB3 H 3.075 0.000 1 53 . 7 VAL N N 128.74 0.09 1 54 . 7 VAL H H 7.993 0.006 1 55 . 7 VAL CA C 60.98 0.07 1 56 . 7 VAL HA H 5.092 0.010 1 57 . 7 VAL CB C 33.31 0.04 1 58 . 7 VAL HB H 1.835 0.016 1 59 . 7 VAL CG1 C 22.62 0.00 2 60 . 7 VAL HG1 H 0.840 0.017 2 61 . 7 VAL CG2 C 22.07 0.03 2 62 . 7 VAL HG2 H 1.307 0.011 2 63 . 8 VAL N N 126.04 0.03 1 64 . 8 VAL H H 8.630 0.005 1 65 . 8 VAL CA C 61.13 0.09 1 66 . 8 VAL HA H 5.186 0.012 1 67 . 8 VAL CB C 33.20 0.07 1 68 . 8 VAL HB H 2.351 0.010 1 69 . 8 VAL CG1 C 22.73 0.06 2 70 . 8 VAL HG1 H 1.038 0.013 2 71 . 8 VAL CG2 C 22.48 0.02 2 72 . 8 VAL HG2 H 1.178 0.005 2 73 . 9 VAL N N 117.24 0.05 1 74 . 9 VAL H H 9.011 0.003 1 75 . 9 VAL CA C 58.37 0.05 1 76 . 9 VAL HA H 4.608 0.002 1 77 . 9 VAL HB H 2.022 0.006 1 78 . 9 VAL CG1 C 19.90 0.04 2 79 . 9 VAL HG1 H 0.776 0.008 2 80 . 9 VAL CG2 C 21.12 0.01 2 81 . 9 VAL HG2 H 1.199 0.010 2 82 . 10 GLY N N 106.55 0.03 1 83 . 10 GLY H H 6.922 0.004 1 84 . 10 GLY CA C 43.14 0.04 1 85 . 10 GLY HA3 H 1.706 0.018 2 86 . 10 GLY HA2 H 4.100 0.005 2 87 . 11 ASP N N 116.92 0.07 1 88 . 11 ASP H H 8.361 0.009 1 89 . 11 ASP CA C 55.96 0.02 1 90 . 11 ASP HA H 4.855 0.012 1 91 . 11 ASP HB2 H 2.845 0.008 1 92 . 11 ASP HB3 H 2.845 0.008 1 93 . 12 GLY N N 104.01 0.08 1 94 . 12 GLY H H 8.711 0.003 1 95 . 12 GLY CA C 46.57 0.01 1 96 . 12 GLY HA2 H 3.587 0.009 1 97 . 12 GLY HA3 H 3.587 0.009 1 98 . 13 ALA N N 121.71 0.05 1 99 . 13 ALA H H 9.406 0.003 1 100 . 13 ALA CA C 52.83 0.04 1 101 . 13 ALA HA H 3.617 0.011 1 102 . 13 ALA CB C 16.31 0.02 1 103 . 13 ALA HB H 1.344 0.007 1 104 . 14 VAL CA C 63.37 0.00 1 105 . 15 GLY N N 108.42 0.02 1 106 . 15 GLY H H 8.647 0.019 1 107 . 15 GLY CA C 44.87 0.05 1 108 . 16 LYS N N 124.70 0.03 1 109 . 16 LYS H H 9.435 0.012 1 110 . 16 LYS CA C 60.69 0.03 1 111 . 16 LYS CB C 29.91 0.00 1 112 . 17 THR N N 118.65 0.05 1 113 . 17 THR H H 9.331 0.008 1 114 . 17 THR CA C 66.62 0.06 1 115 . 17 THR HA H 4.213 0.019 1 116 . 17 THR CB C 68.44 0.00 1 117 . 17 THR HB H 4.517 0.003 1 118 . 17 THR CG2 C 21.40 0.07 1 119 . 17 THR HG2 H 1.282 0.006 1 120 . 18 CYS N N 119.30 0.04 1 121 . 18 CYS H H 9.979 0.008 1 122 . 18 CYS CA C 65.52 0.06 1 123 . 18 CYS CB C 27.31 0.00 1 124 . 18 CYS HB3 H 2.140 0.000 2 125 . 19 LEU N N 119.63 0.04 1 126 . 19 LEU H H 8.227 0.009 1 127 . 19 LEU CA C 59.35 0.08 1 128 . 19 LEU HA H 4.038 0.016 1 129 . 19 LEU CB C 41.70 0.04 1 130 . 19 LEU HB3 H 1.778 0.007 2 131 . 19 LEU HB2 H 2.366 0.008 2 132 . 19 LEU CG C 25.92 0.01 1 133 . 19 LEU HG H 2.031 0.013 1 134 . 19 LEU CD1 C 27.09 0.06 2 135 . 19 LEU HD1 H 0.776 0.012 2 136 . 19 LEU CD2 C 27.25 0.07 2 137 . 19 LEU HD2 H 0.853 0.009 2 138 . 20 LEU N N 116.62 0.04 1 139 . 20 LEU H H 7.703 0.007 1 140 . 20 LEU CA C 57.99 0.02 1 141 . 20 LEU HA H 4.100 0.008 1 142 . 20 LEU CB C 42.94 0.00 1 143 . 20 LEU CG C 26.65 0.00 1 144 . 20 LEU HG H 2.231 0.009 1 145 . 20 LEU CD1 C 25.62 0.01 2 146 . 20 LEU HD1 H 1.117 0.004 2 147 . 20 LEU CD2 C 25.42 0.05 2 148 . 20 LEU HD2 H 1.203 0.009 2 149 . 20 LEU HB2 H 1.760 0.000 1 150 . 20 LEU HB3 H 1.760 0.000 1 151 . 21 ILE N N 120.97 0.06 1 152 . 21 ILE H H 9.297 0.008 1 153 . 21 ILE CA C 61.16 0.07 1 154 . 21 ILE HA H 3.444 0.016 1 155 . 21 ILE CB C 35.61 0.13 1 156 . 21 ILE HB H 1.735 0.011 1 157 . 21 ILE CG1 C 26.46 0.02 1 158 . 21 ILE HG13 H 1.156 0.017 2 159 . 21 ILE HG12 H 1.509 0.011 2 160 . 21 ILE CG2 C 16.83 0.05 1 161 . 21 ILE HG2 H 0.620 0.007 1 162 . 21 ILE CD1 C 6.73 0.03 1 163 . 21 ILE HD1 H 0.060 0.009 1 164 . 22 SER N N 118.30 0.02 1 165 . 22 SER H H 8.977 0.005 1 166 . 22 SER CA C 61.33 0.05 1 167 . 22 SER HA H 4.413 0.011 1 168 . 22 SER CB C 64.27 0.10 1 169 . 22 SER HB2 H 4.148 0.006 1 170 . 22 SER HB3 H 4.148 0.006 1 171 . 23 TYR N N 116.94 0.03 1 172 . 23 TYR H H 7.715 0.010 1 173 . 23 TYR CA C 60.09 0.03 1 174 . 23 TYR HA H 4.220 0.010 1 175 . 23 TYR CB C 40.07 0.00 1 176 . 23 TYR HB3 H 2.547 0.000 2 177 . 23 TYR HB2 H 3.074 0.000 2 178 . 23 TYR HD1 H 6.793 0.014 1 179 . 23 TYR HD2 H 6.793 0.014 1 180 . 23 TYR CE1 C 118.42 0.00 1 181 . 23 TYR CE2 C 118.42 0.00 1 182 . 23 TYR HE1 H 6.907 0.000 1 183 . 23 TYR HE2 H 6.907 0.000 1 184 . 24 THR N N 102.13 0.04 1 185 . 24 THR H H 7.647 0.004 1 186 . 24 THR CA C 64.46 0.04 1 187 . 24 THR HA H 3.349 0.021 1 188 . 24 THR CB C 69.27 0.03 1 189 . 24 THR HB H 3.850 0.015 1 190 . 24 THR CG2 C 24.64 0.04 1 191 . 24 THR HG2 H 1.192 0.010 1 192 . 25 THR N N 106.51 0.05 1 193 . 25 THR H H 7.728 0.010 1 194 . 25 THR CA C 61.13 0.07 1 195 . 25 THR HA H 4.459 0.010 1 196 . 25 THR CB C 72.78 0.05 1 197 . 25 THR HB H 3.890 0.015 1 198 . 25 THR CG2 C 19.50 0.05 1 199 . 25 THR HG2 H 0.132 0.013 1 200 . 26 ASN N N 114.83 0.08 1 201 . 26 ASN H H 7.698 0.004 1 202 . 26 ASN CA C 55.15 0.02 1 203 . 26 ASN HA H 4.614 0.011 1 204 . 26 ASN CB C 37.37 0.10 1 205 . 26 ASN HB3 H 2.970 0.016 2 206 . 26 ASN HB2 H 3.103 0.022 2 207 . 26 ASN ND2 N 111.87 0.02 1 208 . 26 ASN HD21 H 6.875 0.009 2 209 . 26 ASN HD22 H 7.428 0.009 2 210 . 27 LYS N N 116.97 0.02 1 211 . 27 LYS H H 7.159 0.009 1 212 . 27 LYS CA C 54.58 0.05 1 213 . 27 LYS HA H 4.467 0.007 1 214 . 27 LYS CB C 34.40 0.04 1 215 . 27 LYS HB3 H 1.331 0.015 2 216 . 27 LYS HB2 H 1.520 0.007 2 217 . 27 LYS CG C 24.36 0.03 1 218 . 27 LYS CD C 28.51 0.01 1 219 . 27 LYS CE C 42.10 0.00 1 220 . 27 LYS HG2 H 1.226 0.012 1 221 . 27 LYS HG3 H 1.226 0.012 1 222 . 27 LYS HD2 H 1.565 0.015 1 223 . 27 LYS HD3 H 1.565 0.015 1 224 . 27 LYS HE2 H 2.913 0.008 1 225 . 27 LYS HE3 H 2.913 0.008 1 226 . 28 PHE N N 119.68 0.02 1 227 . 28 PHE H H 8.207 0.004 1 228 . 28 PHE CA C 54.73 0.00 1 229 . 28 PHE HA H 4.761 0.001 1 230 . 28 PHE CZ C 129.09 0.00 1 231 . 28 PHE HZ H 5.909 0.004 1 232 . 28 PHE HB2 H 2.909 0.003 1 233 . 28 PHE HB3 H 2.909 0.003 1 234 . 28 PHE CD1 C 131.71 0.06 1 235 . 28 PHE CD2 C 131.71 0.06 1 236 . 28 PHE HD1 H 6.865 0.015 1 237 . 28 PHE HD2 H 6.865 0.015 1 238 . 28 PHE CE1 C 130.22 0.08 1 239 . 28 PHE CE2 C 130.22 0.08 1 240 . 28 PHE HE1 H 6.674 0.011 1 241 . 28 PHE HE2 H 6.674 0.011 1 242 . 29 PRO CA C 62.47 0.07 1 243 . 29 PRO HA H 4.276 0.013 1 244 . 29 PRO CB C 30.88 0.07 1 245 . 29 PRO HB3 H 1.802 0.014 2 246 . 29 PRO HB2 H 2.163 0.008 2 247 . 30 SER N N 117.75 0.02 1 248 . 30 SER H H 8.280 0.007 1 249 . 30 SER CA C 59.75 0.04 1 250 . 30 SER HA H 4.144 0.016 1 251 . 30 SER CB C 63.63 0.01 1 252 . 30 SER HB3 H 3.912 0.018 2 253 . 30 SER HB2 H 4.025 0.003 2 254 . 31 GLU N N 119.04 0.05 1 255 . 31 GLU H H 7.781 0.007 1 256 . 31 GLU CA C 54.88 0.04 1 257 . 31 GLU HA H 4.530 0.013 1 258 . 31 GLU CB C 31.23 0.06 1 259 . 31 GLU HB3 H 1.888 0.004 2 260 . 31 GLU HB2 H 1.987 0.012 2 261 . 31 GLU CG C 35.48 0.01 1 262 . 31 GLU HG2 H 2.166 0.004 1 263 . 31 GLU HG3 H 2.166 0.004 1 264 . 32 TYR N N 122.06 0.06 1 265 . 32 TYR H H 8.873 0.004 1 266 . 32 TYR CA C 54.88 0.04 1 267 . 32 TYR HA H 5.121 0.007 1 268 . 32 TYR CB C 36.56 0.00 1 269 . 32 TYR HB2 H 3.096 0.018 1 270 . 32 TYR HB3 H 3.096 0.018 1 271 . 32 TYR CD1 C 132.90 0.06 1 272 . 32 TYR CD2 C 132.90 0.06 1 273 . 32 TYR HD1 H 7.295 0.007 1 274 . 32 TYR HD2 H 7.295 0.007 1 275 . 32 TYR CE1 C 116.78 0.00 1 276 . 32 TYR CE2 C 116.78 0.00 1 277 . 32 TYR HE1 H 7.033 0.015 1 278 . 32 TYR HE2 H 7.033 0.015 1 279 . 33 VAL N N 132.10 0.08 1 280 . 33 VAL H H 8.470 0.010 1 281 . 33 VAL CA C 59.31 0.03 1 282 . 33 VAL HA H 4.313 0.007 1 283 . 33 VAL CB C 33.41 0.02 1 284 . 33 VAL HB H 2.046 0.009 1 285 . 33 VAL CG1 C 20.54 0.01 2 286 . 33 VAL HG1 H 0.901 0.008 2 287 . 33 VAL CG2 C 20.33 0.05 2 288 . 33 VAL HG2 H 0.993 0.014 2 289 . 34 PRO CA C 63.87 0.00 1 290 . 34 PRO HA H 4.944 0.000 1 291 . 34 PRO HB2 H 2.433 0.000 2 292 . 34 PRO CD C 50.09 0.00 1 293 . 34 PRO HD2 H 3.600 0.017 1 294 . 34 PRO HD3 H 3.600 0.017 1 295 . 35 THR N N 126.67 0.06 1 296 . 35 THR H H 10.452 0.004 1 297 . 35 THR CA C 64.64 0.01 1 298 . 35 THR HA H 3.917 0.003 1 299 . 35 THR CB C 69.42 0.04 1 300 . 35 THR HB H 4.315 0.021 1 301 . 35 THR CG2 C 20.23 0.00 1 302 . 35 THR HG2 H 1.011 0.009 1 303 . 36 VAL N N 123.68 0.05 1 304 . 36 VAL H H 8.406 0.006 1 305 . 36 VAL CA C 64.72 0.08 1 306 . 36 VAL HA H 3.655 0.016 1 307 . 36 VAL HB H 1.867 0.019 1 308 . 36 VAL CG1 C 22.27 0.02 2 309 . 36 VAL HG1 H 0.444 0.010 2 310 . 36 VAL CG2 C 20.36 0.05 2 311 . 36 VAL HG2 H 0.615 0.014 2 312 . 37 PHE N N 111.29 0.03 1 313 . 37 PHE H H 7.233 0.009 1 314 . 37 PHE CA C 59.65 0.02 1 315 . 37 PHE HA H 4.644 0.003 1 316 . 37 PHE CB C 41.58 0.00 1 317 . 37 PHE HB3 H 2.113 0.003 2 318 . 37 PHE HZ H 7.026 0.000 1 319 . 37 PHE HD1 H 7.175 0.017 1 320 . 37 PHE HD2 H 7.175 0.017 1 321 . 37 PHE HE1 H 6.927 0.001 1 322 . 37 PHE HE2 H 6.927 0.001 1 323 . 38 ASP N N 124.60 0.06 1 324 . 38 ASP H H 7.843 0.004 1 325 . 38 ASP CA C 53.76 0.04 1 326 . 38 ASP HA H 4.975 0.018 1 327 . 38 ASP HB2 H 2.357 0.006 1 328 . 38 ASP HB3 H 2.357 0.006 1 329 . 39 ASN N N 115.68 0.04 1 330 . 39 ASN H H 8.198 0.009 1 331 . 39 ASN CA C 49.99 0.01 1 332 . 39 ASN HA H 5.002 0.003 1 333 . 39 ASN CB C 42.99 0.00 1 334 . 39 ASN HB3 H 2.110 0.018 2 335 . 39 ASN HB2 H 2.496 0.015 2 336 . 39 ASN ND2 N 106.53 0.05 1 337 . 39 ASN HD21 H 5.781 0.006 2 338 . 39 ASN HD22 H 5.927 0.013 2 339 . 40 TYR N N 123.49 0.11 1 340 . 40 TYR H H 8.871 0.013 1 341 . 40 TYR CA C 53.77 0.13 1 342 . 40 TYR HA H 5.526 0.017 1 343 . 40 TYR CB C 41.16 0.06 1 344 . 40 TYR HB2 H 3.543 0.000 1 345 . 40 TYR HB3 H 3.543 0.000 1 346 . 40 TYR CD1 C 132.50 0.06 1 347 . 40 TYR CD2 C 132.50 0.06 1 348 . 40 TYR HD1 H 6.698 0.005 1 349 . 40 TYR HD2 H 6.698 0.005 1 350 . 40 TYR CE1 C 117.53 0.03 1 351 . 40 TYR CE2 C 117.53 0.03 1 352 . 40 TYR HE1 H 6.142 0.003 1 353 . 40 TYR HE2 H 6.142 0.003 1 354 . 41 ALA N N 123.35 0.03 1 355 . 41 ALA H H 9.031 0.008 1 356 . 41 ALA CA C 51.26 0.05 1 357 . 41 ALA HA H 5.648 0.010 1 358 . 41 ALA CB C 22.11 0.07 1 359 . 41 ALA HB H 1.333 0.008 1 360 . 42 VAL N N 108.58 0.03 1 361 . 42 VAL H H 8.255 0.007 1 362 . 42 VAL CA C 58.83 0.06 1 363 . 42 VAL HA H 4.884 0.010 1 364 . 42 VAL CB C 36.61 0.00 1 365 . 42 VAL HB H 2.483 0.016 1 366 . 42 VAL CG1 C 18.88 0.05 2 367 . 42 VAL HG1 H 0.953 0.005 2 368 . 42 VAL CG2 C 24.34 0.00 2 369 . 42 VAL HG2 H 1.061 0.012 2 370 . 43 THR N N 116.97 0.02 1 371 . 43 THR H H 9.178 0.012 1 372 . 43 THR CA C 61.55 0.05 1 373 . 43 THR HA H 5.356 0.011 1 374 . 43 THR CB C 69.72 0.12 1 375 . 43 THR HB H 3.981 0.012 1 376 . 43 THR CG2 C 22.09 0.04 1 377 . 43 THR HG2 H 1.147 0.009 1 378 . 44 VAL N N 120.30 0.04 1 379 . 44 VAL H H 9.139 0.014 1 380 . 44 VAL CA C 60.54 0.01 1 381 . 44 VAL HA H 4.259 0.014 1 382 . 44 VAL CB C 35.48 0.07 1 383 . 44 VAL HB H 1.846 0.008 1 384 . 44 VAL CG1 C 22.20 0.03 2 385 . 44 VAL HG1 H 0.861 0.004 2 386 . 44 VAL CG2 C 19.89 0.04 2 387 . 44 VAL HG2 H 0.858 0.006 2 388 . 45 MET N N 120.44 0.05 1 389 . 45 MET H H 8.652 0.006 1 390 . 45 MET CA C 52.99 0.08 1 391 . 45 MET HA H 5.244 0.017 1 392 . 45 MET CG C 31.83 0.02 1 393 . 45 MET CE C 16.57 0.03 1 394 . 45 MET HE H 1.938 0.007 1 395 . 45 MET HB2 H 2.032 0.009 1 396 . 45 MET HB3 H 2.032 0.009 1 397 . 45 MET HG2 H 2.566 0.005 1 398 . 45 MET HG3 H 2.566 0.005 1 399 . 46 ILE N N 124.40 0.06 1 400 . 46 ILE H H 9.292 0.007 1 401 . 46 ILE CA C 60.87 0.07 1 402 . 46 ILE HA H 4.642 0.007 1 403 . 46 ILE CB C 38.13 0.07 1 404 . 46 ILE HB H 1.840 0.013 1 405 . 46 ILE CG1 C 26.94 0.02 1 406 . 46 ILE HG13 H 0.786 0.004 2 407 . 46 ILE HG12 H 1.422 0.012 2 408 . 46 ILE CG2 C 16.33 0.04 1 409 . 46 ILE HG2 H 0.597 0.007 1 410 . 46 ILE CD1 C 13.52 0.03 1 411 . 46 ILE HD1 H 0.109 0.016 1 412 . 47 GLY N N 118.11 0.01 1 413 . 47 GLY H H 9.417 0.012 1 414 . 47 GLY CA C 47.38 0.08 1 415 . 47 GLY HA2 H 3.979 0.004 1 416 . 47 GLY HA3 H 3.979 0.004 1 417 . 48 GLY N N 103.81 0.05 1 418 . 48 GLY H H 8.604 0.007 1 419 . 48 GLY CA C 44.79 0.08 1 420 . 48 GLY HA3 H 3.707 0.014 2 421 . 48 GLY HA2 H 4.213 0.009 2 422 . 49 GLU N N 119.99 0.02 1 423 . 49 GLU H H 7.785 0.005 1 424 . 49 GLU CA C 52.49 0.00 1 425 . 49 GLU HA H 5.046 0.008 1 426 . 49 GLU HB2 H 2.209 0.000 2 427 . 49 GLU CG C 35.28 0.04 1 428 . 49 GLU HG3 H 2.266 0.010 2 429 . 49 GLU HG2 H 2.374 0.006 2 430 . 50 PRO CA C 63.15 0.02 1 431 . 50 PRO HA H 5.059 0.009 1 432 . 50 PRO CB C 31.74 0.00 1 433 . 50 PRO HD2 H 3.835 0.000 1 434 . 50 PRO HD3 H 3.835 0.000 1 435 . 51 TYR N N 122.33 0.07 1 436 . 51 TYR H H 9.440 0.013 1 437 . 51 TYR CA C 56.69 0.08 1 438 . 51 TYR HA H 4.940 0.005 1 439 . 51 TYR CB C 41.64 0.00 1 440 . 51 TYR HB3 H 2.525 0.002 2 441 . 51 TYR HB2 H 2.986 0.030 2 442 . 51 TYR CD1 C 132.98 0.02 1 443 . 51 TYR CD2 C 132.98 0.02 1 444 . 51 TYR HD1 H 7.102 0.011 1 445 . 51 TYR HD2 H 7.102 0.011 1 446 . 51 TYR CE1 C 117.93 0.02 1 447 . 51 TYR CE2 C 117.93 0.02 1 448 . 51 TYR HE1 H 6.730 0.010 1 449 . 51 TYR HE2 H 6.730 0.010 1 450 . 52 THR N N 115.70 0.05 1 451 . 52 THR H H 8.813 0.009 1 452 . 52 THR CA C 62.25 0.11 1 453 . 52 THR HA H 5.038 0.017 1 454 . 52 THR CB C 69.89 0.08 1 455 . 52 THR HB H 4.116 0.014 1 456 . 52 THR CG2 C 21.63 0.09 1 457 . 52 THR HG2 H 1.239 0.012 1 458 . 53 LEU N N 130.46 0.04 1 459 . 53 LEU H H 9.729 0.007 1 460 . 53 LEU CA C 53.56 0.04 1 461 . 53 LEU HA H 5.158 0.008 1 462 . 53 LEU CB C 43.24 0.07 1 463 . 53 LEU HB3 H 1.252 0.009 2 464 . 53 LEU HB2 H 2.108 0.008 2 465 . 53 LEU CG C 27.12 0.00 1 466 . 53 LEU HG H 1.562 0.012 1 467 . 53 LEU CD1 C 23.58 0.02 2 468 . 53 LEU HD1 H 0.943 0.006 2 469 . 53 LEU CD2 C 26.40 0.02 2 470 . 53 LEU HD2 H 1.014 0.011 2 471 . 54 GLY N N 114.38 0.08 1 472 . 54 GLY H H 9.731 0.007 1 473 . 54 GLY CA C 45.39 0.01 1 474 . 54 GLY HA2 H 3.855 0.006 1 475 . 54 GLY HA3 H 3.855 0.006 1 476 . 55 LEU N N 124.39 0.08 1 477 . 55 LEU H H 9.326 0.007 1 478 . 55 LEU CA C 53.54 0.02 1 479 . 55 LEU HA H 5.470 0.011 1 480 . 55 LEU CG C 26.13 0.00 1 481 . 55 LEU HG H 1.854 0.008 1 482 . 55 LEU CD1 C 26.14 0.02 2 483 . 55 LEU HD1 H 0.988 0.005 2 484 . 55 LEU CD2 C 23.60 0.02 2 485 . 55 LEU HD2 H 1.093 0.011 2 486 . 55 LEU HB2 H 1.607 0.020 1 487 . 55 LEU HB3 H 1.607 0.020 1 488 . 56 PHE N N 127.12 0.06 1 489 . 56 PHE H H 9.535 0.006 1 490 . 56 PHE CA C 57.69 0.00 1 491 . 56 PHE HA H 4.640 0.003 1 492 . 56 PHE CB C 40.27 0.00 1 493 . 56 PHE HB2 H 2.982 0.000 1 494 . 56 PHE HB3 H 2.982 0.000 1 495 . 56 PHE CD1 C 131.95 0.00 1 496 . 56 PHE CD2 C 131.95 0.00 1 497 . 56 PHE HD1 H 7.683 0.010 1 498 . 56 PHE HD2 H 7.683 0.010 1 499 . 56 PHE CE1 C 131.94 0.00 1 500 . 56 PHE CE2 C 131.94 0.00 1 501 . 56 PHE HE1 H 7.536 0.019 1 502 . 56 PHE HE2 H 7.536 0.019 1 503 . 57 ASP N N 125.08 0.05 1 504 . 57 ASP H H 8.902 0.007 1 505 . 57 ASP CA C 53.30 0.01 1 506 . 57 ASP HA H 4.864 0.016 1 507 . 57 ASP CB C 42.85 0.00 1 508 . 57 ASP HB3 H 2.336 0.003 2 509 . 58 THR N N 108.86 0.08 1 510 . 58 THR H H 6.917 0.005 1 511 . 58 THR CA C 60.00 0.01 1 512 . 58 THR HA H 5.197 0.021 1 513 . 58 THR HB H 4.573 0.000 1 514 . 58 THR CG2 C 21.23 0.04 1 515 . 58 THR HG2 H 1.586 0.006 1 516 . 59 ALA N N 118.43 0.02 1 517 . 59 ALA H H 7.727 0.009 1 518 . 59 ALA CA C 52.24 0.02 1 519 . 59 ALA HA H 4.517 0.016 1 520 . 59 ALA CB C 22.61 0.04 1 521 . 59 ALA HB H 1.924 0.005 1 522 . 60 GLY CA C 46.25 0.00 1 523 . 61 LEU N N 120.61 0.07 1 524 . 61 LEU H H 8.548 0.001 1 525 . 61 LEU CA C 55.67 0.06 1 526 . 61 LEU HA H 4.470 0.012 1 527 . 61 LEU CB C 42.25 0.03 1 528 . 61 LEU HB3 H 1.619 0.017 2 529 . 61 LEU HB2 H 2.058 0.021 2 530 . 61 LEU CG C 27.41 0.04 1 531 . 61 LEU HG H 2.106 0.010 1 532 . 61 LEU CD1 C 22.98 0.04 2 533 . 61 LEU HD1 H 1.052 0.004 2 534 . 61 LEU CD2 C 25.12 0.01 2 535 . 61 LEU HD2 H 1.099 0.007 2 536 . 62 GLU N N 121.29 0.05 1 537 . 62 GLU H H 9.049 0.005 1 538 . 62 GLU CA C 57.47 0.04 1 539 . 62 GLU HA H 4.258 0.006 1 540 . 62 GLU CB C 28.99 0.01 1 541 . 62 GLU HB3 H 2.070 0.006 2 542 . 62 GLU HB2 H 2.116 0.012 2 543 . 62 GLU CG C 35.50 0.03 1 544 . 62 GLU HG2 H 2.348 0.007 1 545 . 62 GLU HG3 H 2.348 0.007 1 546 . 63 ASP N N 116.04 0.05 1 547 . 63 ASP H H 8.478 0.010 1 548 . 63 ASP CA C 55.66 0.03 1 549 . 63 ASP HA H 4.057 0.009 1 550 . 63 ASP CB C 39.03 0.11 1 551 . 63 ASP HB3 H 1.163 0.018 2 552 . 63 ASP HB2 H 1.915 0.012 2 553 . 64 TYR N N 113.57 0.01 1 554 . 64 TYR H H 7.229 0.010 1 555 . 64 TYR CA C 55.19 0.04 1 556 . 64 TYR HA H 5.089 0.010 1 557 . 64 TYR CB C 37.07 0.06 1 558 . 64 TYR HB3 H 2.769 0.001 2 559 . 64 TYR HB2 H 3.569 0.019 2 560 . 64 TYR CD1 C 132.03 0.01 1 561 . 64 TYR CD2 C 132.03 0.01 1 562 . 64 TYR HD1 H 7.152 0.010 1 563 . 64 TYR HD2 H 7.152 0.010 1 564 . 64 TYR CE1 C 118.73 0.03 1 565 . 64 TYR CE2 C 118.73 0.03 1 566 . 64 TYR HE1 H 6.525 0.004 1 567 . 64 TYR HE2 H 6.525 0.004 1 568 . 65 ASP N N 121.51 0.03 1 569 . 65 ASP H H 8.003 0.006 1 570 . 65 ASP CA C 57.88 0.06 1 571 . 65 ASP HA H 4.454 0.005 1 572 . 65 ASP CB C 40.54 0.05 1 573 . 65 ASP HB2 H 2.765 0.013 1 574 . 65 ASP HB3 H 2.765 0.013 1 575 . 66 ARG N N 114.23 0.02 1 576 . 66 ARG H H 8.718 0.007 1 577 . 66 ARG CA C 57.99 0.06 1 578 . 66 ARG HA H 4.081 0.008 1 579 . 66 ARG CB C 29.74 0.02 1 580 . 66 ARG HB3 H 1.766 0.012 2 581 . 66 ARG HB2 H 1.827 0.010 2 582 . 66 ARG CG C 27.46 0.01 1 583 . 66 ARG CD C 43.27 0.03 1 584 . 66 ARG HG2 H 1.659 0.018 1 585 . 66 ARG HG3 H 1.659 0.018 1 586 . 66 ARG HD2 H 3.250 0.011 1 587 . 66 ARG HD3 H 3.250 0.011 1 588 . 67 LEU N N 115.02 0.03 1 589 . 67 LEU H H 7.244 0.005 1 590 . 67 LEU CA C 55.17 0.05 1 591 . 67 LEU HA H 3.985 0.013 1 592 . 67 LEU CB C 43.23 0.04 1 593 . 67 LEU HB3 H 1.447 0.012 2 594 . 67 LEU HB2 H 1.637 0.011 2 595 . 67 LEU CG C 27.00 0.00 1 596 . 67 LEU HG H 1.447 0.000 1 597 . 67 LEU CD1 C 26.19 0.05 2 598 . 67 LEU HD1 H 0.579 0.002 2 599 . 67 LEU CD2 C 24.87 0.02 2 600 . 67 LEU HD2 H 0.586 0.006 2 601 . 68 ARG N N 120.23 0.04 1 602 . 68 ARG H H 7.570 0.007 1 603 . 68 ARG CA C 61.21 0.00 1 604 . 68 ARG HB3 H 1.829 0.000 2 605 . 68 ARG HB2 H 2.038 0.000 2 606 . 68 ARG HD2 H 3.056 0.000 1 607 . 68 ARG HD3 H 3.056 0.000 1 608 . 69 PRO CA C 63.55 0.02 1 609 . 69 PRO HD2 H 3.811 0.000 1 610 . 69 PRO HD3 H 3.811 0.000 1 611 . 70 LEU N N 116.69 0.03 1 612 . 70 LEU H H 6.950 0.014 1 613 . 70 LEU CA C 56.33 0.08 1 614 . 70 LEU HA H 3.542 0.009 1 615 . 70 LEU CB C 37.92 0.00 1 616 . 70 LEU HB2 H 0.346 0.000 2 617 . 70 LEU CG C 26.70 0.02 1 618 . 70 LEU HG H 1.193 0.008 1 619 . 70 LEU CD1 C 24.61 0.02 2 620 . 70 LEU HD1 H 0.315 0.017 2 621 . 70 LEU CD2 C 22.27 0.02 2 622 . 70 LEU HD2 H 0.425 0.015 2 623 . 71 SER N N 108.96 0.05 1 624 . 71 SER H H 7.400 0.006 1 625 . 71 SER CA C 60.32 0.02 1 626 . 71 SER HA H 4.216 0.016 1 627 . 71 SER CB C 64.98 0.11 1 628 . 71 SER HB3 H 3.843 0.011 2 629 . 71 SER HB2 H 4.112 0.006 2 630 . 72 TYR N N 119.08 0.10 1 631 . 72 TYR H H 6.990 0.014 1 632 . 72 TYR CA C 56.41 0.00 1 633 . 72 TYR HA H 4.702 0.000 1 634 . 72 TYR HB2 H 3.246 0.000 1 635 . 72 TYR HB3 H 3.246 0.000 1 636 . 72 TYR HD1 H 6.737 0.010 1 637 . 72 TYR HD2 H 6.737 0.010 1 638 . 72 TYR CE1 C 117.52 0.03 1 639 . 72 TYR CE2 C 117.52 0.03 1 640 . 72 TYR HE1 H 6.560 0.011 1 641 . 72 TYR HE2 H 6.560 0.011 1 642 . 73 PRO CA C 65.83 0.13 1 643 . 73 PRO HA H 4.316 0.002 1 644 . 73 PRO CB C 30.31 0.00 1 645 . 73 PRO HB2 H 2.403 0.000 1 646 . 73 PRO HB3 H 2.403 0.000 1 647 . 74 GLN N N 114.27 0.06 1 648 . 74 GLN H H 9.153 0.006 1 649 . 74 GLN CA C 57.29 0.04 1 650 . 74 GLN HA H 3.861 0.012 1 651 . 74 GLN CB C 25.63 0.05 1 652 . 74 GLN HB3 H 2.300 0.011 2 653 . 74 GLN HB2 H 2.363 0.000 2 654 . 74 GLN CG C 34.89 0.07 1 655 . 74 GLN HG3 H 2.242 0.005 2 656 . 74 GLN HG2 H 2.367 0.007 2 657 . 74 GLN NE2 N 110.84 0.07 1 658 . 74 GLN HE21 H 6.881 0.009 2 659 . 74 GLN HE22 H 7.619 0.009 2 660 . 75 THR N N 116.14 0.06 1 661 . 75 THR H H 7.451 0.004 1 662 . 75 THR CA C 67.08 0.01 1 663 . 75 THR HA H 3.120 0.026 1 664 . 75 THR CB C 68.03 0.00 1 665 . 75 THR HB H 3.618 0.000 1 666 . 75 THR CG2 C 22.60 0.08 1 667 . 75 THR HG2 H 0.048 0.009 1 668 . 76 ASP N N 122.38 0.07 1 669 . 76 ASP H H 8.647 0.007 1 670 . 76 ASP CA C 56.38 0.08 1 671 . 76 ASP HA H 4.989 0.000 1 672 . 76 ASP CB C 43.50 0.00 1 673 . 76 ASP HB2 H 2.756 0.015 1 674 . 76 ASP HB3 H 2.756 0.015 1 675 . 77 VAL N N 115.09 0.08 1 676 . 77 VAL H H 7.641 0.011 1 677 . 77 VAL CA C 60.43 0.03 1 678 . 77 VAL HA H 4.762 0.006 1 679 . 77 VAL CB C 32.90 0.02 1 680 . 77 VAL HB H 2.162 0.013 1 681 . 77 VAL CG1 C 17.37 0.06 2 682 . 77 VAL HG1 H 0.781 0.006 2 683 . 77 VAL CG2 C 20.71 0.04 2 684 . 77 VAL HG2 H 0.979 0.005 2 685 . 78 PHE N N 121.65 0.02 1 686 . 78 PHE H H 8.474 0.004 1 687 . 78 PHE CA C 56.80 0.10 1 688 . 78 PHE HA H 5.808 0.007 1 689 . 78 PHE CB C 43.53 0.00 1 690 . 78 PHE HB2 H 3.011 0.009 1 691 . 78 PHE HB3 H 3.011 0.009 1 692 . 78 PHE CD1 C 132.32 0.01 1 693 . 78 PHE CD2 C 132.32 0.01 1 694 . 78 PHE HD1 H 7.016 0.014 1 695 . 78 PHE HD2 H 7.016 0.014 1 696 . 79 LEU N N 118.33 0.07 1 697 . 79 LEU H H 9.151 0.013 1 698 . 79 LEU CA C 53.82 0.04 1 699 . 79 LEU HA H 4.784 0.027 1 700 . 79 LEU HB3 H 1.165 0.017 2 701 . 79 LEU CG C 26.49 0.07 1 702 . 79 LEU HG H 1.382 0.008 1 703 . 79 LEU CD1 C 25.12 0.03 2 704 . 79 LEU HD1 H 0.324 0.012 2 705 . 79 LEU CD2 C 23.24 0.03 2 706 . 79 LEU HD2 H 0.541 0.013 2 707 . 80 VAL N N 124.00 0.07 1 708 . 80 VAL H H 8.883 0.019 1 709 . 80 VAL CA C 61.22 0.08 1 710 . 80 VAL HA H 4.393 0.015 1 711 . 80 VAL CB C 31.09 0.05 1 712 . 80 VAL HB H 2.384 0.013 1 713 . 80 VAL CG1 C 21.14 0.04 2 714 . 80 VAL HG1 H 0.736 0.009 2 715 . 80 VAL CG2 C 22.86 0.05 2 716 . 80 VAL HG2 H 0.921 0.014 2 717 . 81 CYS N N 122.95 0.07 1 718 . 81 CYS H H 9.068 0.010 1 719 . 81 CYS CA C 57.74 0.07 1 720 . 81 CYS HA H 5.844 0.012 1 721 . 81 CYS CB C 30.56 0.00 1 722 . 81 CYS HB3 H 2.212 0.000 2 723 . 81 CYS HB2 H 2.539 0.000 2 724 . 82 PHE N N 117.02 0.06 1 725 . 82 PHE H H 9.012 0.004 1 726 . 82 PHE CA C 56.49 0.08 1 727 . 82 PHE HA H 4.610 0.018 1 728 . 82 PHE CB C 39.56 0.00 1 729 . 82 PHE HB3 H 2.887 0.000 2 730 . 82 PHE CD1 C 132.77 0.03 1 731 . 82 PHE CD2 C 132.77 0.03 1 732 . 82 PHE HD1 H 7.224 0.015 1 733 . 82 PHE HD2 H 7.224 0.015 1 734 . 83 SER N N 112.53 0.02 1 735 . 83 SER H H 8.170 0.017 1 736 . 83 SER CA C 54.98 0.00 1 737 . 83 SER HA H 5.243 0.017 1 738 . 83 SER CB C 63.18 0.07 1 739 . 83 SER HB2 H 4.091 0.000 1 740 . 83 SER HB3 H 4.091 0.000 1 741 . 84 VAL N N 120.01 0.06 1 742 . 84 VAL H H 8.783 0.017 1 743 . 84 VAL CA C 63.72 0.07 1 744 . 84 VAL HA H 4.332 0.000 1 745 . 84 VAL CB C 30.34 0.08 1 746 . 84 VAL HB H 2.844 0.008 1 747 . 84 VAL CG1 C 20.20 0.02 2 748 . 84 VAL HG1 H 0.933 0.007 2 749 . 84 VAL CG2 C 20.54 0.01 2 750 . 84 VAL HG2 H 1.037 0.019 2 751 . 85 VAL N N 107.18 0.13 1 752 . 85 VAL H H 7.678 0.009 1 753 . 85 VAL CA C 60.21 0.10 1 754 . 85 VAL HA H 4.524 0.008 1 755 . 85 VAL CB C 30.02 0.03 1 756 . 85 VAL HB H 2.513 0.011 1 757 . 85 VAL CG1 C 21.29 0.02 2 758 . 85 VAL HG1 H 0.704 0.016 2 759 . 85 VAL CG2 C 18.38 0.06 2 760 . 85 VAL HG2 H 0.760 0.010 2 761 . 86 SER N N 111.60 0.03 1 762 . 86 SER H H 7.858 0.004 1 763 . 86 SER CA C 53.77 0.00 1 764 . 86 SER HA H 5.214 0.017 1 765 . 86 SER CB C 62.62 0.00 1 766 . 86 SER HB3 H 3.815 0.002 2 767 . 86 SER HB2 H 4.206 0.000 2 768 . 87 PRO CA C 65.59 0.11 1 769 . 87 PRO HA H 4.326 0.010 1 770 . 87 PRO CB C 32.24 0.00 1 771 . 87 PRO HB3 H 2.114 0.000 2 772 . 87 PRO HB2 H 2.116 0.000 2 773 . 88 SER N N 112.90 0.02 1 774 . 88 SER H H 9.008 0.006 1 775 . 88 SER CA C 61.55 0.09 1 776 . 88 SER HA H 4.322 0.006 1 777 . 88 SER CB C 61.86 0.00 1 778 . 88 SER HB2 H 3.992 0.007 1 779 . 88 SER HB3 H 3.992 0.007 1 780 . 89 SER N N 119.88 0.07 1 781 . 89 SER H H 8.128 0.006 1 782 . 89 SER CA C 61.41 0.02 1 783 . 89 SER HA H 5.125 0.024 1 784 . 89 SER CB C 63.80 0.00 1 785 . 89 SER HB2 H 4.461 0.000 1 786 . 89 SER HB3 H 4.461 0.000 1 787 . 90 PHE N N 124.51 0.01 1 788 . 90 PHE H H 7.529 0.004 1 789 . 90 PHE CA C 60.13 0.05 1 790 . 90 PHE HA H 3.985 0.018 1 791 . 90 PHE CB C 39.72 0.00 1 792 . 90 PHE HB3 H 2.886 0.008 2 793 . 90 PHE HB2 H 3.369 0.008 2 794 . 90 PHE HZ H 6.848 0.010 1 795 . 90 PHE CD1 C 131.48 0.01 1 796 . 90 PHE CD2 C 131.48 0.01 1 797 . 90 PHE HD1 H 6.077 0.012 1 798 . 90 PHE HD2 H 6.077 0.012 1 799 . 90 PHE CE1 C 129.66 0.04 1 800 . 90 PHE CE2 C 129.66 0.04 1 801 . 90 PHE HE1 H 6.815 0.013 1 802 . 90 PHE HE2 H 6.815 0.013 1 803 . 91 GLU N N 118.52 0.03 1 804 . 91 GLU H H 8.189 0.011 1 805 . 91 GLU CA C 58.80 0.03 1 806 . 91 GLU HA H 3.990 0.005 1 807 . 91 GLU CB C 28.76 0.06 1 808 . 91 GLU HB3 H 2.175 0.013 2 809 . 91 GLU HB2 H 2.243 0.000 2 810 . 91 GLU CG C 35.49 0.02 1 811 . 91 GLU HG2 H 2.434 0.012 1 812 . 91 GLU HG3 H 2.434 0.012 1 813 . 92 ASN N N 113.68 0.04 1 814 . 92 ASN H H 8.191 0.010 1 815 . 92 ASN CA C 54.75 0.04 1 816 . 92 ASN HA H 4.824 0.000 1 817 . 92 ASN CB C 38.07 0.00 1 818 . 92 ASN HB3 H 2.902 0.015 2 819 . 92 ASN HB2 H 3.370 0.003 2 820 . 92 ASN ND2 N 115.45 0.08 1 821 . 92 ASN HD21 H 6.807 0.012 2 822 . 92 ASN HD22 H 10.332 0.004 2 823 . 93 VAL N N 123.07 0.05 1 824 . 93 VAL H H 7.927 0.009 1 825 . 93 VAL CA C 68.34 0.14 1 826 . 93 VAL HA H 3.815 0.007 1 827 . 93 VAL CB C 30.83 0.01 1 828 . 93 VAL HB H 2.360 0.011 1 829 . 93 VAL CG1 C 22.59 0.07 2 830 . 93 VAL HG1 H 0.893 0.010 2 831 . 93 VAL CG2 C 22.73 0.07 2 832 . 93 VAL HG2 H 1.307 0.008 2 833 . 94 LYS N N 114.32 0.02 1 834 . 94 LYS H H 6.680 0.006 1 835 . 94 LYS CA C 58.03 0.07 1 836 . 94 LYS HA H 3.972 0.011 1 837 . 94 LYS CB C 33.43 0.03 1 838 . 94 LYS HB3 H 1.727 0.013 2 839 . 94 LYS HB2 H 1.938 0.008 2 840 . 94 LYS CG C 24.55 0.05 1 841 . 94 LYS CD C 29.28 0.03 1 842 . 94 LYS CE C 41.65 0.05 1 843 . 94 LYS HG2 H 1.343 0.008 1 844 . 94 LYS HG3 H 1.343 0.008 1 845 . 94 LYS HD2 H 1.628 0.007 1 846 . 94 LYS HD3 H 1.628 0.007 1 847 . 94 LYS HE2 H 2.885 0.009 1 848 . 94 LYS HE3 H 2.885 0.009 1 849 . 95 GLU N N 111.89 0.05 1 850 . 95 GLU H H 7.739 0.009 1 851 . 95 GLU CA C 57.51 0.08 1 852 . 95 GLU HA H 4.140 0.008 1 853 . 95 GLU CB C 30.52 0.04 1 854 . 95 GLU HB3 H 1.866 0.012 2 855 . 95 GLU HB2 H 2.125 0.007 2 856 . 95 GLU CG C 35.44 0.04 1 857 . 95 GLU HG3 H 2.279 0.005 2 858 . 95 GLU HG2 H 2.350 0.013 2 859 . 96 LYS N N 114.99 0.04 1 860 . 96 LYS H H 8.179 0.006 1 861 . 96 LYS CA C 57.49 0.03 1 862 . 96 LYS HA H 4.345 0.012 1 863 . 96 LYS CB C 35.29 0.12 1 864 . 96 LYS HB3 H 0.980 0.017 2 865 . 96 LYS HB2 H 1.275 0.018 2 866 . 96 LYS CG C 24.80 0.08 1 867 . 96 LYS HG2 H 0.661 0.026 2 868 . 96 LYS CD C 29.54 0.01 1 869 . 96 LYS HD3 H 0.689 0.016 2 870 . 96 LYS HD2 H 1.001 0.005 2 871 . 96 LYS CE C 41.42 0.00 1 872 . 96 LYS HE3 H 2.065 0.006 2 873 . 96 LYS HE2 H 2.329 0.024 2 874 . 97 TRP N N 118.91 0.04 1 875 . 97 TRP H H 7.762 0.005 1 876 . 97 TRP CA C 60.91 0.05 1 877 . 97 TRP HB3 H 3.012 0.009 2 878 . 97 TRP CD1 C 125.85 0.00 1 879 . 97 TRP HD1 H 6.755 0.005 1 880 . 97 TRP NE1 N 132.30 0.06 1 881 . 97 TRP HE1 H 11.702 0.004 1 882 . 97 TRP CZ2 C 116.00 0.00 1 883 . 97 TRP HZ2 H 7.695 0.001 1 884 . 98 VAL N N 115.68 0.04 1 885 . 98 VAL H H 8.682 0.013 1 886 . 98 VAL CA C 68.14 0.12 1 887 . 98 VAL HA H 3.588 0.025 1 888 . 98 VAL CB C 28.65 0.00 1 889 . 98 VAL HB H 2.206 0.009 1 890 . 98 VAL CG1 C 25.31 0.07 2 891 . 98 VAL HG1 H 0.694 0.002 1 892 . 98 VAL CG2 C 21.54 0.03 2 893 . 98 VAL HG2 H 0.778 0.014 1 894 . 99 PRO CA C 66.78 0.00 1 895 . 99 PRO CB C 30.44 0.00 1 896 . 99 PRO HD2 H 3.500 0.000 1 897 . 99 PRO HD3 H 3.500 0.000 1 898 . 100 GLU N N 115.90 0.02 1 899 . 100 GLU H H 7.592 0.004 1 900 . 100 GLU CA C 60.83 0.02 1 901 . 100 GLU HA H 4.227 0.010 1 902 . 100 GLU CB C 29.98 0.00 1 903 . 100 GLU HB2 H 2.276 0.022 1 904 . 100 GLU HB3 H 2.276 0.022 1 905 . 100 GLU HG2 H 2.536 0.002 1 906 . 100 GLU HG3 H 2.536 0.002 1 907 . 101 ILE N N 112.48 0.05 1 908 . 101 ILE H H 8.300 0.008 1 909 . 101 ILE CA C 65.87 0.12 1 910 . 101 ILE HA H 3.556 0.015 1 911 . 101 ILE CB C 36.09 0.00 1 912 . 101 ILE HB H 0.408 0.006 1 913 . 101 ILE CG1 C 25.19 0.00 1 914 . 101 ILE HG13 H 1.034 0.012 2 915 . 101 ILE HG12 H 1.167 0.001 2 916 . 101 ILE CG2 C 18.56 0.04 1 917 . 101 ILE HG2 H 0.217 0.008 1 918 . 101 ILE CD1 C 14.24 0.04 1 919 . 102 THR N N 111.85 0.08 1 920 . 102 THR H H 7.940 0.006 1 921 . 102 THR CA C 64.76 0.08 1 922 . 102 THR HA H 3.831 0.014 1 923 . 102 THR CB C 69.46 0.06 1 924 . 102 THR HB H 4.214 0.021 1 925 . 102 THR CG2 C 21.74 0.12 1 926 . 102 THR HG2 H 1.282 0.009 1 927 . 103 HIS N N 117.89 0.08 1 928 . 103 HIS H H 7.672 0.009 1 929 . 103 HIS CA C 58.28 0.05 1 930 . 103 HIS HA H 4.324 0.011 1 931 . 103 HIS CB C 28.43 0.00 1 932 . 103 HIS CD2 C 118.89 0.07 1 933 . 103 HIS HD2 H 5.979 0.011 1 934 . 103 HIS CE1 C 136.92 0.00 1 935 . 103 HIS HE1 H 8.370 0.025 1 936 . 103 HIS HB2 H 3.312 0.010 1 937 . 103 HIS HB3 H 3.312 0.010 1 938 . 104 HIS N N 112.92 0.02 1 939 . 104 HIS H H 7.271 0.004 1 940 . 104 HIS CA C 59.48 0.04 1 941 . 104 HIS HA H 4.294 0.014 1 942 . 104 HIS CB C 33.56 0.00 1 943 . 104 HIS HB3 H 3.041 0.000 2 944 . 104 HIS HB2 H 3.559 0.000 2 945 . 105 CYS N N 116.44 0.02 1 946 . 105 CYS H H 8.559 0.005 1 947 . 105 CYS CA C 56.23 0.00 1 948 . 105 CYS HA H 5.057 0.010 1 949 . 105 CYS HB3 H 3.035 0.031 2 950 . 105 CYS HB2 H 3.589 0.025 2 951 . 106 PRO CA C 64.70 0.09 1 952 . 106 PRO HA H 4.552 0.010 1 953 . 106 PRO CB C 32.11 0.00 1 954 . 106 PRO HB3 H 1.997 0.000 2 955 . 106 PRO HB2 H 2.578 0.014 2 956 . 107 LYS N N 115.28 0.01 1 957 . 107 LYS H H 8.863 0.012 1 958 . 107 LYS CA C 55.69 0.09 1 959 . 107 LYS HA H 4.459 0.013 1 960 . 107 LYS CB C 31.82 0.08 1 961 . 107 LYS HB3 H 1.948 0.016 2 962 . 107 LYS HB2 H 2.110 0.020 2 963 . 107 LYS CG C 25.02 0.07 1 964 . 107 LYS CD C 28.75 0.00 1 965 . 107 LYS CE C 42.08 0.01 1 966 . 107 LYS HG2 H 1.478 0.008 1 967 . 107 LYS HG3 H 1.478 0.008 1 968 . 107 LYS HD2 H 1.759 0.022 1 969 . 107 LYS HD3 H 1.759 0.022 1 970 . 107 LYS HE2 H 3.052 0.006 1 971 . 107 LYS HE3 H 3.052 0.006 1 972 . 108 THR N N 119.32 0.01 1 973 . 108 THR H H 7.588 0.004 1 974 . 108 THR CA C 61.37 0.00 1 975 . 108 THR HA H 4.782 0.009 1 976 . 108 THR HB H 4.138 0.015 1 977 . 108 THR CG2 C 22.02 0.04 1 978 . 108 THR HG2 H 1.366 0.015 1 979 . 109 PRO CA C 62.71 0.01 1 980 . 109 PRO HA H 4.629 0.015 1 981 . 109 PRO CB C 33.38 0.02 1 982 . 109 PRO HB3 H 1.786 0.017 2 983 . 109 PRO HB2 H 2.349 0.002 2 984 . 109 PRO HG2 H 2.184 0.016 1 985 . 109 PRO HG3 H 2.184 0.016 1 986 . 110 PHE N N 112.22 0.07 1 987 . 110 PHE H H 8.292 0.007 1 988 . 110 PHE CA C 54.90 0.37 1 989 . 110 PHE HA H 6.026 0.003 1 990 . 110 PHE CB C 44.01 0.00 1 991 . 110 PHE HB3 H 2.923 0.000 2 992 . 110 PHE HB2 H 3.033 0.015 2 993 . 110 PHE HZ H 7.307 0.000 1 994 . 110 PHE CD1 C 132.67 0.03 1 995 . 110 PHE CD2 C 132.67 0.03 1 996 . 110 PHE HD1 H 7.046 0.015 1 997 . 110 PHE HD2 H 7.046 0.015 1 998 . 110 PHE HE1 H 7.040 0.000 1 999 . 110 PHE HE2 H 7.040 0.000 1 1000 . 111 LEU N N 120.07 0.07 1 1001 . 111 LEU H H 8.788 0.006 1 1002 . 111 LEU CA C 54.59 0.10 1 1003 . 111 LEU HA H 4.754 0.010 1 1004 . 111 LEU CB C 43.76 0.00 1 1005 . 111 LEU HB3 H 1.359 0.000 2 1006 . 111 LEU HB2 H 1.517 0.000 2 1007 . 111 LEU CG C 30.51 0.05 1 1008 . 111 LEU HG H 1.507 0.006 1 1009 . 111 LEU CD1 C 24.87 0.04 2 1010 . 111 LEU HD1 H 0.681 0.007 2 1011 . 111 LEU CD2 C 26.41 0.02 2 1012 . 111 LEU HD2 H 0.630 0.001 2 1013 . 112 LEU N N 121.33 0.02 1 1014 . 112 LEU H H 8.127 0.007 1 1015 . 112 LEU CA C 53.61 0.08 1 1016 . 112 LEU HA H 5.431 0.012 1 1017 . 112 LEU CB C 44.37 0.10 1 1018 . 112 LEU HB3 H 1.556 0.011 2 1019 . 112 LEU HB2 H 2.184 0.012 2 1020 . 112 LEU CG C 27.99 0.04 1 1021 . 112 LEU HG H 2.093 0.013 1 1022 . 112 LEU CD1 C 25.86 0.06 2 1023 . 112 LEU HD1 H 1.118 0.014 2 1024 . 112 LEU CD2 C 25.61 0.04 2 1025 . 112 LEU HD2 H 1.262 0.011 2 1026 . 113 VAL N N 125.19 0.06 1 1027 . 113 VAL H H 9.328 0.011 1 1028 . 113 VAL CA C 59.60 0.10 1 1029 . 113 VAL HA H 4.958 0.022 1 1030 . 113 VAL CB C 33.91 0.08 1 1031 . 113 VAL HB H 2.176 0.013 1 1032 . 113 VAL CG1 C 20.80 0.05 2 1033 . 113 VAL HG1 H 0.496 0.014 2 1034 . 113 VAL CG2 C 21.73 0.04 2 1035 . 113 VAL HG2 H 0.558 0.015 2 1036 . 114 GLY N N 114.41 0.06 1 1037 . 114 GLY H H 8.853 0.005 1 1038 . 114 GLY CA C 44.08 0.06 1 1039 . 114 GLY HA3 H 3.345 0.000 2 1040 . 114 GLY HA2 H 3.760 0.000 2 1041 . 115 THR N N 114.86 0.05 1 1042 . 115 THR H H 9.269 0.011 1 1043 . 115 THR CA C 59.25 0.04 1 1044 . 115 THR HA H 5.066 0.017 1 1045 . 115 THR CB C 70.75 0.00 1 1046 . 115 THR CG2 C 22.63 0.00 1 1047 . 115 THR HG2 H 0.708 0.015 1 1048 . 116 GLN N N 107.83 0.05 1 1049 . 116 GLN H H 9.533 0.009 1 1050 . 116 GLN CA C 56.42 0.00 1 1051 . 116 GLN HA H 4.097 0.004 1 1052 . 116 GLN CB C 24.20 0.00 1 1053 . 117 ILE N N 105.47 0.06 1 1054 . 117 ILE H H 7.738 0.008 1 1055 . 117 ILE CA C 64.70 0.03 1 1056 . 117 ILE HA H 3.899 0.015 1 1057 . 117 ILE CB C 36.54 0.06 1 1058 . 117 ILE HB H 2.081 0.012 1 1059 . 117 ILE CG1 C 25.16 0.06 1 1060 . 117 ILE CG2 C 16.54 0.03 1 1061 . 117 ILE HG2 H 0.858 0.013 1 1062 . 117 ILE CD1 C 13.23 0.03 1 1063 . 117 ILE HD1 H 0.595 0.012 1 1064 . 117 ILE HG12 H 1.254 0.008 1 1065 . 117 ILE HG13 H 1.254 0.008 1 1066 . 118 ASP N N 118.15 0.03 1 1067 . 118 ASP H H 8.828 0.008 1 1068 . 118 ASP CA C 55.40 0.03 1 1069 . 118 ASP HA H 4.531 0.004 1 1070 . 118 ASP CB C 40.37 0.00 1 1071 . 118 ASP HB2 H 2.728 0.012 1 1072 . 118 ASP HB3 H 2.728 0.012 1 1073 . 119 LEU N N 116.99 0.07 1 1074 . 119 LEU H H 7.988 0.007 1 1075 . 119 LEU CA C 55.30 0.02 1 1076 . 119 LEU HA H 4.441 0.017 1 1077 . 119 LEU CB C 41.97 0.00 1 1078 . 119 LEU CG C 26.54 0.00 1 1079 . 119 LEU HG H 1.678 0.015 1 1080 . 119 LEU CD1 C 21.37 0.04 2 1081 . 119 LEU HD1 H 0.825 0.007 2 1082 . 119 LEU CD2 C 25.57 0.07 2 1083 . 119 LEU HD2 H 0.972 0.008 2 1084 . 119 LEU HB2 H 2.110 0.008 1 1085 . 119 LEU HB3 H 2.110 0.008 1 1086 . 120 ARG N N 116.08 0.05 1 1087 . 120 ARG H H 7.353 0.005 1 1088 . 120 ARG CA C 60.06 0.13 1 1089 . 120 ARG HA H 3.654 0.011 1 1090 . 120 ARG CB C 30.25 0.07 1 1091 . 120 ARG HB3 H 1.680 0.012 2 1092 . 120 ARG HB2 H 1.855 0.007 2 1093 . 120 ARG HG2 H 1.429 0.000 1 1094 . 120 ARG HG3 H 1.429 0.000 1 1095 . 121 ASP N N 110.83 0.06 1 1096 . 121 ASP H H 7.185 0.007 1 1097 . 121 ASP CA C 52.74 0.03 1 1098 . 121 ASP HA H 4.864 0.020 1 1099 . 121 ASP CB C 41.41 0.03 1 1100 . 121 ASP HB3 H 2.516 0.006 2 1101 . 121 ASP HB2 H 2.943 0.005 2 1102 . 122 ASP N N 121.41 0.05 1 1103 . 122 ASP H H 7.326 0.003 1 1104 . 122 ASP CA C 51.60 0.00 1 1105 . 122 ASP HA H 5.054 0.014 1 1106 . 122 ASP HB3 H 2.833 0.000 2 1107 . 122 ASP HB2 H 3.135 0.000 2 1108 . 123 PRO CA C 65.69 0.10 1 1109 . 123 PRO HA H 4.235 0.013 1 1110 . 123 PRO CB C 32.11 0.03 1 1111 . 123 PRO HB3 H 2.062 0.008 2 1112 . 123 PRO HB2 H 2.456 0.011 2 1113 . 123 PRO CG C 27.45 0.00 1 1114 . 123 PRO CD C 51.27 0.01 1 1115 . 123 PRO HD3 H 3.964 0.011 2 1116 . 123 PRO HD2 H 4.465 0.010 2 1117 . 123 PRO HG2 H 2.252 0.008 1 1118 . 123 PRO HG3 H 2.252 0.008 1 1119 . 124 SER N N 111.74 0.07 1 1120 . 124 SER H H 8.402 0.013 1 1121 . 124 SER CA C 61.90 0.12 1 1122 . 124 SER HA H 4.327 0.009 1 1123 . 124 SER CB C 62.23 0.05 1 1124 . 124 SER HB3 H 4.025 0.011 2 1125 . 124 SER HB2 H 4.105 0.006 2 1126 . 125 THR N N 121.06 0.06 1 1127 . 125 THR H H 7.994 0.010 1 1128 . 125 THR CA C 67.79 0.04 1 1129 . 125 THR HA H 4.765 0.001 1 1130 . 125 THR CB C 67.66 0.07 1 1131 . 125 THR HB H 3.943 0.013 1 1132 . 125 THR CG2 C 21.22 0.04 1 1133 . 125 THR HG2 H 1.295 0.014 1 1134 . 126 ILE N N 120.65 0.03 1 1135 . 126 ILE H H 8.304 0.009 1 1136 . 126 ILE CA C 64.84 0.08 1 1137 . 126 ILE HA H 3.622 0.017 1 1138 . 126 ILE CB C 37.12 0.08 1 1139 . 126 ILE HB H 2.008 0.014 1 1140 . 126 ILE CG1 C 28.51 0.03 1 1141 . 126 ILE HG13 H 1.278 0.016 2 1142 . 126 ILE HG12 H 1.605 0.011 2 1143 . 126 ILE CG2 C 17.13 0.03 1 1144 . 126 ILE HG2 H 0.994 0.007 1 1145 . 126 ILE CD1 C 12.00 0.04 1 1146 . 126 ILE HD1 H 0.850 0.009 1 1147 . 127 GLU N N 119.49 0.02 1 1148 . 127 GLU H H 8.324 0.006 1 1149 . 127 GLU CA C 59.16 0.10 1 1150 . 127 GLU HA H 4.207 0.011 1 1151 . 127 GLU CB C 29.27 0.04 1 1152 . 127 GLU CG C 35.97 0.05 1 1153 . 127 GLU HG3 H 2.301 0.009 2 1154 . 127 GLU HG2 H 2.401 0.008 2 1155 . 127 GLU HB2 H 2.159 0.019 1 1156 . 127 GLU HB3 H 2.159 0.019 1 1157 . 128 LYS N N 119.97 0.02 1 1158 . 128 LYS H H 7.981 0.013 1 1159 . 128 LYS CA C 59.88 0.02 1 1160 . 128 LYS HA H 4.035 0.010 1 1161 . 128 LYS CB C 32.09 0.08 1 1162 . 128 LYS CG C 25.09 0.04 1 1163 . 128 LYS HG3 H 1.473 0.014 2 1164 . 128 LYS HG2 H 1.687 0.017 2 1165 . 128 LYS CD C 29.06 0.00 1 1166 . 128 LYS HD3 H 1.733 0.004 2 1167 . 128 LYS HD2 H 1.775 0.007 2 1168 . 128 LYS CE C 42.10 0.00 1 1169 . 128 LYS HB2 H 2.092 0.015 1 1170 . 128 LYS HB3 H 2.092 0.015 1 1171 . 128 LYS HE2 H 3.036 0.008 1 1172 . 128 LYS HE3 H 3.036 0.008 1 1173 . 129 LEU N N 117.79 0.01 1 1174 . 129 LEU H H 8.203 0.008 1 1175 . 129 LEU CA C 57.94 0.08 1 1176 . 129 LEU HA H 4.183 0.014 1 1177 . 129 LEU CB C 41.69 0.06 1 1178 . 129 LEU HB3 H 1.113 0.018 2 1179 . 129 LEU HB2 H 1.913 0.010 2 1180 . 129 LEU CG C 27.05 0.07 1 1181 . 129 LEU HG H 1.910 0.010 1 1182 . 129 LEU CD1 C 25.13 0.02 2 1183 . 129 LEU HD1 H 0.732 0.008 2 1184 . 129 LEU CD2 C 22.43 0.04 2 1185 . 129 LEU HD2 H 0.862 0.007 2 1186 . 130 ALA N N 121.72 0.08 1 1187 . 130 ALA H H 8.575 0.006 1 1188 . 130 ALA CA C 55.28 0.04 1 1189 . 130 ALA HA H 4.346 0.006 1 1190 . 130 ALA CB C 17.64 0.08 1 1191 . 130 ALA HB H 1.651 0.004 1 1192 . 131 LYS N N 119.65 0.03 1 1193 . 131 LYS H H 8.146 0.008 1 1194 . 131 LYS CA C 59.03 0.07 1 1195 . 131 LYS HA H 4.170 0.009 1 1196 . 131 LYS CB C 32.14 0.03 1 1197 . 131 LYS HB3 H 2.013 0.006 2 1198 . 131 LYS HB2 H 2.069 0.002 2 1199 . 131 LYS CG C 25.18 0.06 1 1200 . 131 LYS HG3 H 1.602 0.007 2 1201 . 131 LYS HG2 H 1.770 0.007 2 1202 . 131 LYS CD C 29.01 0.00 1 1203 . 131 LYS CE C 42.25 0.01 1 1204 . 131 LYS HD2 H 1.764 0.000 1 1205 . 131 LYS HD3 H 1.764 0.000 1 1206 . 131 LYS HE2 H 3.059 0.010 1 1207 . 131 LYS HE3 H 3.059 0.010 1 1208 . 132 ASN N N 114.93 0.02 1 1209 . 132 ASN H H 7.487 0.006 1 1210 . 132 ASN CA C 52.07 0.09 1 1211 . 132 ASN HA H 5.052 0.013 1 1212 . 132 ASN CB C 39.18 0.09 1 1213 . 132 ASN HB3 H 2.656 0.011 2 1214 . 132 ASN HB2 H 3.097 0.013 2 1215 . 132 ASN ND2 N 111.35 0.06 1 1216 . 132 ASN HD21 H 6.986 0.005 2 1217 . 132 ASN HD22 H 7.500 0.007 2 1218 . 133 LYS N N 113.25 0.03 1 1219 . 133 LYS H H 8.176 0.012 1 1220 . 133 LYS CA C 57.17 0.06 1 1221 . 133 LYS HA H 3.996 0.009 1 1222 . 133 LYS CB C 28.50 0.02 1 1223 . 133 LYS HB3 H 2.066 0.015 2 1224 . 133 LYS HB2 H 2.156 0.013 2 1225 . 133 LYS CG C 25.14 0.01 1 1226 . 133 LYS CD C 29.01 0.00 1 1227 . 133 LYS HD3 H 1.726 0.023 2 1228 . 133 LYS HD2 H 1.770 0.005 2 1229 . 133 LYS CE C 42.14 0.00 1 1230 . 133 LYS HG2 H 1.450 0.011 1 1231 . 133 LYS HG3 H 1.450 0.011 1 1232 . 133 LYS HE2 H 3.061 0.014 1 1233 . 133 LYS HE3 H 3.061 0.014 1 1234 . 134 GLN N N 115.26 0.03 1 1235 . 134 GLN H H 8.187 0.005 1 1236 . 134 GLN CA C 53.82 0.00 1 1237 . 134 GLN HA H 4.825 0.015 1 1238 . 134 GLN NE2 N 109.25 0.03 1 1239 . 134 GLN HE21 H 6.882 0.006 2 1240 . 134 GLN HE22 H 7.528 0.003 2 1241 . 134 GLN HB2 H 2.099 0.010 1 1242 . 134 GLN HB3 H 2.099 0.010 1 1243 . 134 GLN HG2 H 2.441 0.014 1 1244 . 134 GLN HG3 H 2.441 0.014 1 1245 . 135 LYS N N 117.94 0.04 1 1246 . 135 LYS H H 8.046 0.004 1 1247 . 135 LYS CA C 54.02 0.01 1 1248 . 135 LYS HA H 4.823 0.016 1 1249 . 135 LYS CB C 34.17 0.01 1 1250 . 135 LYS HB3 H 1.676 0.017 2 1251 . 135 LYS HB2 H 1.939 0.009 2 1252 . 135 LYS CG C 24.52 0.01 1 1253 . 135 LYS HG3 H 1.413 0.009 2 1254 . 135 LYS HG2 H 1.483 0.001 2 1255 . 135 LYS CE C 42.07 0.00 1 1256 . 135 LYS HE2 H 3.014 0.005 1 1257 . 135 LYS HE3 H 3.014 0.005 1 1258 . 136 PRO CA C 62.38 0.00 1 1259 . 136 PRO HA H 4.485 0.000 1 1260 . 136 PRO CB C 32.30 0.00 1 1261 . 136 PRO HB2 H 2.103 0.000 1 1262 . 136 PRO HB3 H 2.103 0.000 1 1263 . 136 PRO HD2 H 3.757 0.015 1 1264 . 136 PRO HD3 H 3.757 0.015 1 1265 . 137 ILE N N 121.45 0.05 1 1266 . 137 ILE H H 9.214 0.004 1 1267 . 137 ILE CA C 59.78 0.04 1 1268 . 137 ILE HA H 3.976 0.008 1 1269 . 137 ILE CB C 36.85 0.10 1 1270 . 137 ILE HB H 1.917 0.018 1 1271 . 137 ILE CG1 C 27.09 0.05 1 1272 . 137 ILE HG13 H 0.971 0.015 2 1273 . 137 ILE HG12 H 1.317 0.011 2 1274 . 137 ILE CG2 C 17.15 0.03 1 1275 . 137 ILE HG2 H 0.323 0.009 1 1276 . 137 ILE CD1 C 10.39 0.05 1 1277 . 137 ILE HD1 H 0.535 0.005 1 1278 . 138 THR N N 117.66 0.02 1 1279 . 138 THR H H 8.072 0.007 1 1280 . 138 THR CA C 59.00 0.06 1 1281 . 138 THR HA H 4.639 0.005 1 1282 . 138 THR HB H 4.763 0.009 1 1283 . 138 THR CG2 C 22.25 0.04 1 1284 . 138 THR HG2 H 1.355 0.005 1 1285 . 139 PRO CA C 65.44 0.09 1 1286 . 139 PRO HA H 4.156 0.015 1 1287 . 139 PRO CB C 31.52 0.07 1 1288 . 139 PRO HB3 H 2.044 0.000 2 1289 . 139 PRO HB2 H 2.566 0.007 2 1290 . 139 PRO HD3 H 3.876 0.000 2 1291 . 140 GLU N N 113.95 0.02 1 1292 . 140 GLU H H 8.644 0.010 1 1293 . 140 GLU CA C 60.08 0.06 1 1294 . 140 GLU HA H 4.056 0.012 1 1295 . 140 GLU CB C 28.59 0.05 1 1296 . 140 GLU HB3 H 1.954 0.009 2 1297 . 140 GLU HB2 H 2.093 0.009 2 1298 . 140 GLU CG C 36.49 0.01 1 1299 . 140 GLU HG3 H 2.331 0.005 1 1300 . 140 GLU HG2 H 2.388 0.012 1 1301 . 141 THR N N 117.55 0.09 1 1302 . 141 THR H H 7.651 0.010 1 1303 . 141 THR CA C 66.00 0.07 1 1304 . 141 THR HA H 3.887 0.013 1 1305 . 141 THR CB C 68.40 0.03 1 1306 . 141 THR HB H 4.087 0.010 1 1307 . 141 THR CG2 C 22.19 0.03 1 1308 . 141 THR HG2 H 1.207 0.011 1 1309 . 142 ALA N N 124.73 0.05 1 1310 . 142 ALA H H 7.625 0.005 1 1311 . 142 ALA CA C 55.13 0.08 1 1312 . 142 ALA HA H 3.936 0.013 1 1313 . 142 ALA CB C 17.07 0.04 1 1314 . 142 ALA HB H 0.681 0.008 1 1315 . 143 GLU N N 117.29 0.02 1 1316 . 143 GLU H H 8.862 0.008 1 1317 . 143 GLU CA C 59.44 0.05 1 1318 . 143 GLU HA H 3.816 0.009 1 1319 . 143 GLU CB C 29.31 0.09 1 1320 . 143 GLU HB3 H 2.038 0.012 2 1321 . 143 GLU HB2 H 2.170 0.021 2 1322 . 143 GLU CG C 36.78 0.03 1 1323 . 143 GLU HG3 H 2.416 0.012 2 1324 . 143 GLU HG2 H 2.581 0.006 2 1325 . 144 LYS N N 118.16 0.07 1 1326 . 144 LYS H H 7.381 0.003 1 1327 . 144 LYS CA C 59.35 0.04 1 1328 . 144 LYS HA H 4.016 0.010 1 1329 . 144 LYS CB C 31.87 0.08 1 1330 . 144 LYS HB3 H 1.926 0.006 2 1331 . 144 LYS HB2 H 2.036 0.006 2 1332 . 144 LYS CG C 25.15 0.00 1 1333 . 144 LYS HG3 H 1.481 0.005 2 1334 . 144 LYS HG2 H 1.586 0.013 2 1335 . 144 LYS CD C 28.76 0.00 1 1336 . 144 LYS HD3 H 1.713 0.004 2 1337 . 144 LYS HD2 H 1.774 0.003 2 1338 . 144 LYS CE C 42.12 0.00 1 1339 . 144 LYS HE2 H 3.042 0.004 1 1340 . 144 LYS HE3 H 3.042 0.004 1 1341 . 145 LEU N N 118.88 0.05 1 1342 . 145 LEU H H 7.383 0.007 1 1343 . 145 LEU CA C 57.73 0.04 1 1344 . 145 LEU HA H 4.213 0.017 1 1345 . 145 LEU CB C 40.72 0.00 1 1346 . 145 LEU HB3 H 1.543 0.000 2 1347 . 145 LEU HB2 H 1.864 0.016 2 1348 . 145 LEU CG C 26.63 0.05 1 1349 . 145 LEU HG H 1.433 0.017 1 1350 . 145 LEU CD1 C 25.90 0.01 2 1351 . 145 LEU HD1 H 0.167 0.012 2 1352 . 145 LEU CD2 C 23.23 0.04 2 1353 . 145 LEU HD2 H 0.830 0.009 2 1354 . 146 ALA N N 118.11 0.05 1 1355 . 146 ALA H H 8.545 0.008 1 1356 . 146 ALA CA C 55.42 0.03 1 1357 . 146 ALA HA H 3.785 0.012 1 1358 . 146 ALA CB C 18.17 0.04 1 1359 . 146 ALA HB H 1.509 0.005 1 1360 . 147 ARG N N 115.39 0.01 1 1361 . 147 ARG H H 7.802 0.009 1 1362 . 147 ARG CA C 59.00 0.04 1 1363 . 147 ARG HA H 4.221 0.016 1 1364 . 147 ARG CB C 29.98 0.04 1 1365 . 147 ARG HB3 H 1.997 0.001 2 1366 . 147 ARG CG C 27.49 0.03 1 1367 . 147 ARG HG3 H 1.673 0.015 2 1368 . 147 ARG HG2 H 1.916 0.010 2 1369 . 147 ARG CD C 43.39 0.06 1 1370 . 147 ARG HD3 H 3.259 0.001 2 1371 . 147 ARG HD2 H 3.333 0.013 2 1372 . 147 ARG HB2 H 2.034 0.008 1 1373 . 148 ASP N N 121.34 0.03 1 1374 . 148 ASP H H 8.538 0.012 1 1375 . 148 ASP CA C 57.46 0.05 1 1376 . 148 ASP HA H 4.395 0.015 1 1377 . 148 ASP CB C 40.24 0.08 1 1378 . 148 ASP HB3 H 2.709 0.006 2 1379 . 148 ASP HB2 H 2.897 0.006 2 1380 . 149 LEU N N 114.58 0.05 1 1381 . 149 LEU H H 8.450 0.003 1 1382 . 149 LEU CA C 54.27 0.06 1 1383 . 149 LEU HA H 4.422 0.015 1 1384 . 149 LEU CB C 41.74 0.02 1 1385 . 149 LEU HB3 H 1.803 0.014 2 1386 . 149 LEU CG C 25.89 0.00 1 1387 . 149 LEU HG H 1.940 0.005 1 1388 . 149 LEU CD1 C 26.92 0.02 2 1389 . 149 LEU HD1 H 0.784 0.008 2 1390 . 149 LEU CD2 C 21.68 0.04 2 1391 . 149 LEU HD2 H 0.862 0.012 2 1392 . 150 LYS N N 110.99 0.02 1 1393 . 150 LYS H H 7.700 0.007 1 1394 . 150 LYS CA C 57.27 0.08 1 1395 . 150 LYS HA H 3.842 0.012 1 1396 . 150 LYS CB C 27.92 0.05 1 1397 . 150 LYS HB3 H 1.917 0.010 2 1398 . 150 LYS HB2 H 2.309 0.016 2 1399 . 150 LYS CG C 24.81 0.04 1 1400 . 150 LYS CD C 28.99 0.03 1 1401 . 150 LYS CE C 42.10 0.01 1 1402 . 150 LYS HG2 H 1.403 0.010 1 1403 . 150 LYS HG3 H 1.403 0.010 1 1404 . 150 LYS HD2 H 1.743 0.004 1 1405 . 150 LYS HD3 H 1.743 0.004 1 1406 . 150 LYS HE2 H 3.078 0.004 1 1407 . 150 LYS HE3 H 3.078 0.004 1 1408 . 151 ALA N N 118.95 0.06 1 1409 . 151 ALA H H 8.292 0.007 1 1410 . 151 ALA CA C 51.13 0.08 1 1411 . 151 ALA HA H 3.040 0.009 1 1412 . 151 ALA CB C 20.12 0.01 1 1413 . 151 ALA HB H 1.134 0.007 1 1414 . 152 VAL N N 119.67 0.05 1 1415 . 152 VAL H H 8.840 0.007 1 1416 . 152 VAL CA C 65.95 0.07 1 1417 . 152 VAL HA H 3.558 0.007 1 1418 . 152 VAL CB C 32.61 0.07 1 1419 . 152 VAL HB H 1.723 0.012 1 1420 . 152 VAL CG1 C 21.23 0.06 2 1421 . 152 VAL HG1 H 0.963 0.004 2 1422 . 152 VAL CG2 C 22.68 0.04 2 1423 . 152 VAL HG2 H 1.056 0.011 2 1424 . 153 LYS N N 107.23 0.06 1 1425 . 153 LYS H H 6.953 0.006 1 1426 . 153 LYS CA C 54.93 0.06 1 1427 . 153 LYS HA H 4.408 0.009 1 1428 . 153 LYS CB C 34.18 0.04 1 1429 . 153 LYS HB3 H 1.777 0.008 2 1430 . 153 LYS HB2 H 2.112 0.015 2 1431 . 153 LYS CG C 23.13 0.06 1 1432 . 153 LYS CD C 28.47 0.01 1 1433 . 153 LYS CE C 41.19 0.00 1 1434 . 153 LYS HE3 H 2.820 0.001 2 1435 . 153 LYS HE2 H 2.930 0.003 2 1436 . 153 LYS HG2 H 1.245 0.013 1 1437 . 153 LYS HG3 H 1.245 0.013 1 1438 . 153 LYS HD2 H 1.528 0.011 1 1439 . 153 LYS HD3 H 1.528 0.011 1 1440 . 154 TYR N N 119.31 0.03 1 1441 . 154 TYR H H 8.703 0.008 1 1442 . 154 TYR CA C 55.98 0.03 1 1443 . 154 TYR HA H 5.848 0.006 1 1444 . 154 TYR CB C 40.36 0.00 1 1445 . 154 TYR HB2 H 2.840 0.007 1 1446 . 154 TYR HB3 H 2.840 0.007 1 1447 . 154 TYR HD1 H 7.077 0.011 1 1448 . 154 TYR HD2 H 7.077 0.011 1 1449 . 154 TYR CE1 C 118.05 0.02 1 1450 . 154 TYR CE2 C 118.05 0.02 1 1451 . 154 TYR HE1 H 6.810 0.002 1 1452 . 154 TYR HE2 H 6.810 0.002 1 1453 . 155 VAL N N 120.85 0.05 1 1454 . 155 VAL H H 8.331 0.005 1 1455 . 155 VAL CA C 58.32 0.05 1 1456 . 155 VAL HA H 4.182 0.009 1 1457 . 155 VAL CB C 34.95 0.08 1 1458 . 155 VAL HB H 2.007 0.003 1 1459 . 155 VAL CG1 C 21.23 0.05 2 1460 . 155 VAL HG1 H 0.693 0.007 2 1461 . 155 VAL CG2 C 22.81 0.02 2 1462 . 155 VAL HG2 H 0.700 0.015 2 1463 . 156 GLU N N 112.43 0.07 1 1464 . 156 GLU H H 8.125 0.006 1 1465 . 156 GLU CA C 53.65 0.03 1 1466 . 156 GLU HA H 5.494 0.017 1 1467 . 156 GLU CB C 31.59 0.00 1 1468 . 156 GLU CG C 34.12 0.00 1 1469 . 156 GLU HG3 H 1.880 0.021 2 1470 . 156 GLU HG2 H 2.297 0.009 2 1471 . 156 GLU HB2 H 2.027 0.000 1 1472 . 156 GLU HB3 H 2.027 0.000 1 1473 . 157 CYS N N 110.98 0.03 1 1474 . 157 CYS H H 8.846 0.004 1 1475 . 157 CYS CA C 55.83 0.02 1 1476 . 157 CYS HA H 5.369 0.007 1 1477 . 157 CYS CB C 32.10 0.00 1 1478 . 157 CYS HB3 H 2.472 0.000 2 1479 . 157 CYS HB2 H 2.902 0.000 2 1480 . 158 SER N N 109.22 0.04 1 1481 . 158 SER H H 8.303 0.004 1 1482 . 158 SER CA C 55.86 0.02 1 1483 . 158 SER HA H 5.326 0.001 1 1484 . 158 SER CB C 64.62 0.00 1 1485 . 158 SER HB2 H 4.107 0.003 1 1486 . 158 SER HB3 H 4.107 0.003 1 1487 . 159 ALA N N 131.66 0.07 1 1488 . 159 ALA H H 9.429 0.008 1 1489 . 159 ALA CA C 54.39 0.05 1 1490 . 159 ALA HA H 4.270 0.009 1 1491 . 159 ALA CB C 19.86 0.04 1 1492 . 159 ALA HB H 1.782 0.011 1 1493 . 160 LEU N N 117.50 0.06 1 1494 . 160 LEU H H 7.503 0.007 1 1495 . 160 LEU CA C 57.07 0.07 1 1496 . 160 LEU HA H 3.354 0.011 1 1497 . 160 LEU HB2 H 1.210 0.023 2 1498 . 160 LEU CG C 26.36 0.06 1 1499 . 160 LEU HG H 0.938 0.008 1 1500 . 160 LEU CD1 C 21.99 0.02 2 1501 . 160 LEU CD2 C 25.62 0.04 2 1502 . 160 LEU HD2 H 0.605 0.012 2 1503 . 161 THR N N 105.46 0.06 1 1504 . 161 THR H H 8.108 0.008 1 1505 . 161 THR CA C 61.40 0.05 1 1506 . 161 THR HA H 4.233 0.012 1 1507 . 161 THR CB C 69.55 0.07 1 1508 . 161 THR HB H 4.497 0.013 1 1509 . 161 THR CG2 C 21.31 0.03 1 1510 . 161 THR HG1 H 5.466 0.001 1 1511 . 161 THR HG2 H 1.180 0.006 1 1512 . 162 GLN N N 111.37 0.05 1 1513 . 162 GLN H H 7.494 0.008 1 1514 . 162 GLN CA C 58.75 0.10 1 1515 . 162 GLN HA H 4.024 0.011 1 1516 . 162 GLN CB C 25.74 0.00 1 1517 . 162 GLN HB3 H 2.234 0.005 2 1518 . 162 GLN HB2 H 2.735 0.014 2 1519 . 162 GLN CG C 34.28 0.00 1 1520 . 162 GLN HG2 H 2.213 0.016 2 1521 . 162 GLN NE2 N 112.76 0.08 1 1522 . 162 GLN HE21 H 7.159 0.006 2 1523 . 162 GLN HE22 H 7.483 0.007 2 1524 . 163 LYS N N 123.36 0.09 1 1525 . 163 LYS H H 7.933 0.006 1 1526 . 163 LYS CA C 58.04 0.03 1 1527 . 163 LYS HA H 4.235 0.009 1 1528 . 163 LYS CB C 32.11 0.07 1 1529 . 163 LYS HB3 H 1.647 0.011 2 1530 . 163 LYS HB2 H 1.829 0.011 2 1531 . 163 LYS CG C 24.62 0.01 1 1532 . 163 LYS CD C 29.08 0.01 1 1533 . 163 LYS CE C 42.02 0.04 1 1534 . 163 LYS HG2 H 1.437 0.008 1 1535 . 163 LYS HG3 H 1.437 0.008 1 1536 . 163 LYS HD2 H 1.726 0.015 1 1537 . 163 LYS HD3 H 1.726 0.015 1 1538 . 163 LYS HE2 H 2.974 0.011 1 1539 . 163 LYS HE3 H 2.974 0.011 1 1540 . 164 GLY N N 113.92 0.02 1 1541 . 164 GLY H H 9.224 0.006 1 1542 . 164 GLY CA C 46.18 0.06 1 1543 . 164 GLY HA3 H 3.909 0.006 2 1544 . 164 GLY HA2 H 4.339 0.018 2 1545 . 165 LEU N N 120.42 0.06 1 1546 . 165 LEU H H 7.481 0.007 1 1547 . 165 LEU CA C 58.57 0.13 1 1548 . 165 LEU HA H 3.890 0.018 1 1549 . 165 LEU CB C 43.73 0.04 1 1550 . 165 LEU HB3 H 1.211 0.000 2 1551 . 165 LEU HB2 H 2.098 0.017 2 1552 . 165 LEU CG C 27.08 0.00 1 1553 . 165 LEU HG H 1.749 0.017 1 1554 . 165 LEU CD1 C 26.52 0.06 2 1555 . 165 LEU HD1 H 1.148 0.012 2 1556 . 165 LEU CD2 C 25.37 0.03 2 1557 . 165 LEU HD2 H 1.282 0.005 2 1558 . 166 LYS N N 117.28 0.04 1 1559 . 166 LYS H H 8.732 0.006 1 1560 . 166 LYS CA C 60.47 0.03 1 1561 . 166 LYS HA H 4.071 0.000 1 1562 . 166 LYS HB2 H 2.078 0.016 2 1563 . 166 LYS HD3 H 1.868 0.004 2 1564 . 167 ASN N N 112.45 0.05 1 1565 . 167 ASN H H 8.072 0.010 1 1566 . 167 ASN CA C 57.02 0.09 1 1567 . 167 ASN HA H 4.331 0.006 1 1568 . 167 ASN CB C 38.64 0.05 1 1569 . 167 ASN ND2 N 113.17 0.02 1 1570 . 167 ASN HD21 H 7.350 0.004 2 1571 . 167 ASN HD22 H 8.004 0.001 2 1572 . 167 ASN HB2 H 2.706 0.014 1 1573 . 167 ASN HB3 H 2.706 0.014 1 1574 . 168 VAL N N 115.60 0.02 1 1575 . 168 VAL H H 7.384 0.008 1 1576 . 168 VAL CA C 67.03 0.10 1 1577 . 168 VAL HA H 3.018 0.010 1 1578 . 168 VAL CB C 31.06 0.01 1 1579 . 168 VAL HB H 2.074 0.011 1 1580 . 168 VAL CG1 C 20.88 0.06 2 1581 . 168 VAL HG1 H 0.055 0.013 2 1582 . 168 VAL CG2 C 21.33 0.03 2 1583 . 168 VAL HG2 H 0.888 0.011 2 1584 . 169 PHE N N 114.28 0.02 1 1585 . 169 PHE H H 6.621 0.010 1 1586 . 169 PHE CA C 62.70 0.05 1 1587 . 169 PHE HA H 3.679 0.010 1 1588 . 169 PHE CB C 39.15 0.02 1 1589 . 169 PHE HB3 H 2.337 0.023 2 1590 . 169 PHE HB2 H 2.715 0.001 2 1591 . 169 PHE CZ C 127.32 0.00 1 1592 . 169 PHE HZ H 6.743 0.010 1 1593 . 169 PHE CD1 C 130.76 0.00 1 1594 . 169 PHE CD2 C 130.76 0.00 1 1595 . 169 PHE HD1 H 6.657 0.006 1 1596 . 169 PHE HD2 H 6.657 0.006 1 1597 . 169 PHE HE1 H 6.811 0.000 1 1598 . 169 PHE HE2 H 6.811 0.000 1 1599 . 170 ASP N N 120.99 0.04 1 1600 . 170 ASP H H 9.028 0.010 1 1601 . 170 ASP CA C 57.42 0.03 1 1602 . 170 ASP HA H 4.275 0.017 1 1603 . 170 ASP CB C 39.71 0.00 1 1604 . 170 ASP HB3 H 2.535 0.000 2 1605 . 170 ASP HB2 H 2.736 0.011 2 1606 . 171 GLU N N 114.30 0.04 1 1607 . 171 GLU H H 8.087 0.008 1 1608 . 171 GLU CA C 58.25 0.02 1 1609 . 171 GLU HA H 4.067 0.018 1 1610 . 171 GLU CB C 28.00 0.00 1 1611 . 171 GLU HG3 H 2.059 0.011 2 1612 . 171 GLU HG2 H 2.524 0.000 2 1613 . 171 GLU HB2 H 1.822 0.025 1 1614 . 171 GLU HB3 H 1.822 0.025 1 1615 . 172 ALA N N 123.56 0.05 1 1616 . 172 ALA H H 8.104 0.007 1 1617 . 172 ALA CA C 55.21 0.07 1 1618 . 172 ALA HA H 3.848 0.013 1 1619 . 172 ALA CB C 17.82 0.03 1 1620 . 172 ALA HB H 1.386 0.006 1 1621 . 173 ILE N N 117.35 0.04 1 1622 . 173 ILE H H 8.554 0.009 1 1623 . 173 ILE CA C 66.01 0.07 1 1624 . 173 ILE HA H 3.332 0.012 1 1625 . 173 ILE CB C 37.72 0.03 1 1626 . 173 ILE HB H 2.057 0.019 1 1627 . 173 ILE CG2 C 17.79 0.03 1 1628 . 173 ILE HG2 H 0.686 0.014 1 1629 . 173 ILE CD1 C 14.51 0.02 1 1630 . 173 ILE HD1 H 0.991 0.005 1 1631 . 173 ILE HG12 H 1.391 0.000 1 1632 . 173 ILE HG13 H 1.391 0.000 1 1633 . 174 LEU N N 116.57 0.04 1 1634 . 174 LEU H H 8.200 0.012 1 1635 . 174 LEU CA C 57.94 0.03 1 1636 . 174 LEU HA H 3.897 0.015 1 1637 . 174 LEU CB C 41.02 0.09 1 1638 . 174 LEU HB3 H 1.453 0.008 2 1639 . 174 LEU HB2 H 1.819 0.010 2 1640 . 174 LEU CG C 26.23 0.08 1 1641 . 174 LEU HG H 1.847 0.012 1 1642 . 174 LEU CD1 C 22.27 0.03 2 1643 . 174 LEU HD1 H 0.813 0.008 2 1644 . 174 LEU CD2 C 24.88 0.03 2 1645 . 174 LEU HD2 H 0.799 0.002 2 1646 . 175 ALA N N 118.67 0.04 1 1647 . 175 ALA H H 7.910 0.011 1 1648 . 175 ALA CA C 54.18 0.06 1 1649 . 175 ALA HA H 4.122 0.011 1 1650 . 175 ALA CB C 18.28 0.05 1 1651 . 175 ALA HB H 1.433 0.006 1 1652 . 176 ALA N N 116.57 0.05 1 1653 . 176 ALA H H 7.898 0.004 1 1654 . 176 ALA CA C 53.62 0.03 1 1655 . 176 ALA HA H 4.056 0.014 1 1656 . 176 ALA CB C 19.55 0.05 1 1657 . 176 ALA HB H 1.406 0.009 1 1658 . 177 LEU N N 114.30 0.03 1 1659 . 177 LEU H H 7.769 0.014 1 1660 . 177 LEU CA C 55.33 0.05 1 1661 . 177 LEU HA H 4.293 0.010 1 1662 . 177 LEU CB C 42.93 0.02 1 1663 . 177 LEU HB3 H 1.575 0.010 2 1664 . 177 LEU HB2 H 1.716 0.012 2 1665 . 177 LEU CG C 26.19 0.06 1 1666 . 177 LEU HG H 1.801 0.015 1 1667 . 177 LEU CD1 C 25.28 0.10 2 1668 . 177 LEU HD1 H 0.600 0.011 2 1669 . 177 LEU CD2 C 22.15 0.03 2 1670 . 177 LEU HD2 H 0.785 0.007 2 1671 . 178 GLU N N 119.70 0.06 1 1672 . 178 GLU H H 7.739 0.006 1 1673 . 178 GLU CA C 54.09 0.01 1 1674 . 178 GLU HA H 4.638 0.004 1 1675 . 178 GLU CB C 29.80 0.02 1 1676 . 178 GLU CG C 35.41 0.00 1 1677 . 178 GLU HB2 H 2.039 0.007 1 1678 . 178 GLU HB3 H 2.039 0.007 1 1679 . 178 GLU HG2 H 2.349 0.008 1 1680 . 178 GLU HG3 H 2.349 0.008 1 1681 . 179 PRO CA C 61.48 0.04 1 1682 . 179 PRO HA H 4.823 0.022 1 1683 . 179 PRO CB C 30.80 0.02 1 1684 . 179 PRO HB3 H 2.020 0.006 2 1685 . 179 PRO HB2 H 2.428 0.007 2 1686 . 179 PRO CG C 27.22 0.03 1 1687 . 179 PRO CD C 50.22 0.00 1 1688 . 179 PRO HD3 H 3.662 0.002 2 1689 . 179 PRO HD2 H 3.759 0.001 2 1690 . 179 PRO HG2 H 2.110 0.007 1 1691 . 179 PRO HG3 H 2.110 0.007 1 1692 . 180 PRO CA C 62.88 0.03 1 1693 . 180 PRO HA H 4.503 0.003 1 1694 . 180 PRO CB C 31.81 0.04 1 1695 . 180 PRO HB3 H 1.970 0.004 2 1696 . 180 PRO HB2 H 2.360 0.010 2 1697 . 180 PRO CG C 27.28 0.00 1 1698 . 180 PRO CD C 50.22 0.00 1 1699 . 180 PRO HD3 H 3.750 0.005 2 1700 . 180 PRO HD2 H 3.934 0.013 2 1701 . 180 PRO HG2 H 2.096 0.002 1 1702 . 180 PRO HG3 H 2.096 0.002 1 1703 . 181 GLU N N 120.05 0.02 1 1704 . 181 GLU H H 8.320 0.011 1 1705 . 181 GLU CA C 53.93 0.08 1 1706 . 181 GLU HA H 4.646 0.006 1 1707 . 181 GLU CB C 29.96 0.00 1 1708 . 181 GLU HB3 H 1.978 0.014 2 1709 . 181 GLU HB2 H 2.073 0.013 2 1710 . 181 GLU CG C 35.75 0.02 1 1711 . 181 GLU HG2 H 2.341 0.006 1 1712 . 181 GLU HG3 H 2.341 0.006 1 1713 . 182 PRO CA C 62.91 0.04 1 1714 . 182 PRO HA H 4.455 0.006 1 1715 . 182 PRO CB C 31.95 0.04 1 1716 . 182 PRO HB3 H 1.941 0.009 2 1717 . 182 PRO HB2 H 2.348 0.007 2 1718 . 182 PRO CG C 27.21 0.00 1 1719 . 182 PRO CD C 50.55 0.02 1 1720 . 182 PRO HD3 H 3.725 0.006 2 1721 . 182 PRO HD2 H 3.898 0.007 2 1722 . 182 PRO HG2 H 2.071 0.009 1 1723 . 182 PRO HG3 H 2.071 0.009 1 1724 . 183 LYS N N 121.21 0.06 1 1725 . 183 LYS H H 8.501 0.006 1 1726 . 183 LYS CA C 56.15 0.02 1 1727 . 183 LYS HA H 4.344 0.006 1 1728 . 183 LYS CB C 32.91 0.02 1 1729 . 183 LYS HB3 H 1.815 0.006 2 1730 . 183 LYS HB2 H 1.911 0.007 2 1731 . 183 LYS CG C 24.62 0.01 1 1732 . 183 LYS CD C 28.97 0.00 1 1733 . 183 LYS CE C 42.10 0.00 1 1734 . 183 LYS HG2 H 1.547 0.009 1 1735 . 183 LYS HG3 H 1.547 0.009 1 1736 . 183 LYS HD2 H 1.752 0.002 1 1737 . 183 LYS HD3 H 1.752 0.002 1 1738 . 183 LYS HE2 H 3.063 0.004 1 1739 . 183 LYS HE3 H 3.063 0.004 1 1740 . 184 LYS N N 127.07 0.05 1 1741 . 184 LYS H H 8.045 0.012 1 1742 . 184 LYS CA C 57.54 0.02 1 1743 . 184 LYS HA H 4.196 0.011 1 1744 . 184 LYS CB C 33.61 0.05 1 1745 . 184 LYS HB3 H 1.754 0.009 2 1746 . 184 LYS HB2 H 1.861 0.008 2 1747 . 184 LYS CG C 24.37 0.02 1 1748 . 184 LYS CD C 29.01 0.00 1 1749 . 184 LYS CE C 42.05 0.00 1 1750 . 184 LYS HG2 H 1.439 0.025 1 1751 . 184 LYS HG3 H 1.439 0.025 1 1752 . 184 LYS HD2 H 1.703 0.004 1 1753 . 184 LYS HD3 H 1.703 0.004 1 1754 . 184 LYS HE2 H 3.035 0.003 1 1755 . 184 LYS HE3 H 3.035 0.003 1 1756 . 185 GNP HN1 H 10.733 0.001 1 1757 . 185 GNP H8 H 8.091 0.000 1 1758 . 185 GNP H1' H 6.033 0.005 1 1759 . 185 GNP H2' H 4.904 0.000 1 1760 . 185 GNP H3' H 4.722 0.000 1 1761 . 185 GNP HN21 H 12.781 0.029 1 1762 . 185 GNP HN22 H 12.781 0.029 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name PAK _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 GLY CA C 43.19 0.07 1 2 . 1 GLY HA3 H 3.836 0.031 2 3 . 1 GLY HA2 H 3.944 0.016 2 4 . 2 SER N N 115.49 0.04 1 5 . 2 SER H H 8.751 0.015 1 6 . 2 SER CA C 58.11 0.03 1 7 . 2 SER HA H 4.540 0.012 1 8 . 2 SER CB C 63.58 0.09 1 9 . 2 SER HB2 H 3.894 0.017 1 10 . 2 SER HB3 H 3.894 0.017 1 11 . 3 ILE N N 124.45 0.06 1 12 . 3 ILE H H 8.500 0.012 1 13 . 3 ILE CA C 60.75 0.05 1 14 . 3 ILE HA H 4.801 0.011 1 15 . 3 ILE CB C 39.19 0.08 1 16 . 3 ILE HB H 1.616 0.011 1 17 . 3 ILE CG1 C 28.21 0.11 1 18 . 3 ILE HG13 H 0.923 0.002 2 19 . 3 ILE HG12 H 1.643 0.010 2 20 . 3 ILE CG2 C 17.96 0.05 1 21 . 3 ILE HG2 H 1.036 0.019 1 22 . 3 ILE CD1 C 13.65 0.05 1 23 . 3 ILE HD1 H 0.840 0.013 1 24 . 4 SER N N 125.93 0.04 1 25 . 4 SER H H 8.932 0.018 1 26 . 4 SER CA C 59.02 0.05 1 27 . 4 SER HA H 4.544 0.004 1 28 . 4 SER CB C 65.76 0.03 1 29 . 4 SER HB2 H 4.002 0.010 1 30 . 4 SER HB3 H 4.002 0.010 1 31 . 5 LEU N N 117.35 0.02 1 32 . 5 LEU H H 8.234 0.011 1 33 . 5 LEU CA C 62.56 0.00 1 34 . 5 LEU HA H 4.496 0.013 1 35 . 5 LEU CB C 40.85 0.05 1 36 . 5 LEU HB3 H 1.693 0.013 2 37 . 5 LEU HB2 H 1.746 0.018 2 38 . 5 LEU CG C 27.59 0.08 1 39 . 5 LEU HG H 1.802 0.008 1 40 . 5 LEU CD1 C 25.04 0.08 2 41 . 5 LEU HD1 H 1.060 0.003 2 42 . 5 LEU CD2 C 22.70 0.09 2 43 . 5 LEU HD2 H 1.133 0.002 2 44 . 6 PRO CA C 62.56 0.04 1 45 . 6 PRO HA H 5.067 0.005 1 46 . 6 PRO CB C 32.22 0.09 1 47 . 6 PRO HB3 H 1.595 0.014 2 48 . 6 PRO HB2 H 1.827 0.018 2 49 . 6 PRO CG C 26.70 0.09 1 50 . 6 PRO HG3 H 0.745 0.022 2 51 . 6 PRO HG2 H 1.412 0.002 2 52 . 6 PRO CD C 50.05 0.05 1 53 . 6 PRO HD3 H 3.333 0.019 2 54 . 6 PRO HD2 H 3.487 0.021 2 55 . 7 SER N N 115.25 0.02 1 56 . 7 SER H H 9.163 0.015 1 57 . 7 SER CA C 57.03 0.06 1 58 . 7 SER HA H 4.787 0.007 1 59 . 7 SER CB C 66.27 0.08 1 60 . 7 SER HB3 H 3.746 0.009 2 61 . 7 SER HB2 H 3.932 0.013 2 62 . 8 ASP N N 115.82 0.04 1 63 . 8 ASP H H 8.796 0.013 1 64 . 8 ASP CA C 54.93 0.09 1 65 . 8 ASP HA H 4.337 0.008 1 66 . 8 ASP CB C 38.73 0.06 1 67 . 8 ASP HB2 H 2.879 0.017 1 68 . 8 ASP HB3 H 2.879 0.017 1 69 . 9 PHE N N 116.56 0.05 1 70 . 9 PHE H H 8.117 0.013 1 71 . 9 PHE CA C 59.44 0.03 1 72 . 9 PHE HA H 4.883 0.009 1 73 . 9 PHE CB C 39.45 0.01 1 74 . 9 PHE HB3 H 2.730 0.014 2 75 . 9 PHE HB2 H 2.903 0.029 2 76 . 9 PHE CZ C 128.47 0.08 1 77 . 9 PHE HZ H 6.834 0.011 1 78 . 9 PHE CD1 C 131.27 0.02 1 79 . 9 PHE CD2 C 131.27 0.02 1 80 . 9 PHE HD1 H 6.910 0.011 1 81 . 9 PHE HD2 H 6.910 0.011 1 82 . 9 PHE CE1 C 131.24 0.05 1 83 . 9 PHE CE2 C 131.24 0.05 1 84 . 9 PHE HE1 H 7.015 0.009 1 85 . 9 PHE HE2 H 7.015 0.009 1 86 . 10 GLU N N 126.68 0.08 1 87 . 10 GLU H H 8.676 0.015 1 88 . 10 GLU CA C 54.62 0.06 1 89 . 10 GLU HA H 4.201 0.014 1 90 . 10 GLU CB C 33.41 0.05 1 91 . 10 GLU HB3 H 1.749 0.011 2 92 . 10 GLU HB2 H 1.859 0.015 2 93 . 10 GLU CG C 35.50 0.05 1 94 . 10 GLU HG3 H 2.044 0.015 2 95 . 10 GLU HG2 H 2.211 0.016 2 96 . 11 HIS N N 124.38 0.15 1 97 . 11 HIS H H 8.998 0.014 1 98 . 11 HIS CA C 51.74 0.01 1 99 . 11 HIS HA H 5.061 0.016 1 100 . 11 HIS CB C 29.40 0.07 1 101 . 11 HIS HB3 H 2.891 0.016 2 102 . 11 HIS HB2 H 3.525 0.022 2 103 . 11 HIS CD2 C 116.65 0.05 1 104 . 11 HIS HD2 H 7.018 0.021 1 105 . 11 HIS CE1 C 136.12 0.00 1 106 . 11 HIS HE1 H 8.667 0.000 1 107 . 12 THR N N 119.09 0.12 1 108 . 12 THR H H 8.066 0.021 1 109 . 12 THR CA C 64.64 0.03 1 110 . 12 THR HA H 4.013 0.019 1 111 . 12 THR CB C 68.44 0.07 1 112 . 12 THR HB H 3.955 0.013 1 113 . 12 THR CG2 C 22.36 0.06 1 114 . 12 THR HG2 H 1.090 0.018 1 115 . 13 ILE N N 117.85 0.05 1 116 . 13 ILE H H 7.370 0.021 1 117 . 13 ILE CA C 59.89 0.05 1 118 . 13 ILE HA H 4.370 0.018 1 119 . 13 ILE CB C 41.76 0.07 1 120 . 13 ILE HB H 1.605 0.010 1 121 . 13 ILE CG1 C 26.71 0.07 1 122 . 13 ILE HG13 H 1.093 0.021 2 123 . 13 ILE HG12 H 1.522 0.018 2 124 . 13 ILE CG2 C 17.40 0.02 1 125 . 13 ILE HG2 H 0.866 0.014 1 126 . 13 ILE CD1 C 12.15 0.05 1 127 . 13 ILE HD1 H 0.755 0.015 1 128 . 14 HIS N N 125.58 0.01 1 129 . 14 HIS H H 8.876 0.013 1 130 . 14 HIS CA C 55.00 0.05 1 131 . 14 HIS HA H 5.474 0.005 1 132 . 14 HIS CB C 31.01 0.01 1 133 . 14 HIS HB3 H 2.551 0.020 2 134 . 14 HIS HB2 H 3.025 0.022 2 135 . 14 HIS CD2 C 120.17 0.10 1 136 . 14 HIS HD2 H 7.128 0.014 1 137 . 14 HIS CE1 C 137.57 0.03 1 138 . 14 HIS HE1 H 8.415 0.000 1 139 . 15 VAL N N 127.78 0.07 1 140 . 15 VAL H H 8.383 0.012 1 141 . 15 VAL CA C 60.14 0.06 1 142 . 15 VAL HA H 4.910 0.014 1 143 . 15 VAL CB C 32.15 0.02 1 144 . 15 VAL HB H 2.099 0.017 1 145 . 15 VAL CG1 C 22.93 0.03 2 146 . 15 VAL HG1 H 1.018 0.016 2 147 . 15 VAL CG2 C 22.45 0.06 2 148 . 15 VAL HG2 H 1.145 0.016 2 149 . 16 GLY N N 114.32 0.03 1 150 . 16 GLY H H 8.647 0.014 1 151 . 16 GLY CA C 43.00 0.05 1 152 . 16 GLY HA3 H 3.557 0.013 2 153 . 16 GLY HA2 H 4.641 0.005 2 154 . 17 PHE N N 119.22 0.01 1 155 . 17 PHE H H 8.605 0.013 1 156 . 17 PHE CA C 57.19 0.10 1 157 . 17 PHE HA H 4.930 0.009 1 158 . 17 PHE CB C 42.26 0.05 1 159 . 17 PHE HB3 H 2.818 0.016 2 160 . 17 PHE HB2 H 2.848 0.003 2 161 . 17 PHE CZ C 128.98 0.01 1 162 . 17 PHE HZ H 7.143 0.011 1 163 . 17 PHE CD1 C 131.47 0.02 1 164 . 17 PHE CD2 C 131.47 0.02 1 165 . 17 PHE HD1 H 6.490 0.007 1 166 . 17 PHE HD2 H 6.490 0.007 1 167 . 17 PHE CE1 C 130.43 0.02 1 168 . 17 PHE CE2 C 130.43 0.02 1 169 . 17 PHE HE1 H 6.935 0.002 1 170 . 17 PHE HE2 H 6.935 0.002 1 171 . 18 ASP N N 128.17 0.05 1 172 . 18 ASP H H 7.982 0.015 1 173 . 18 ASP CA C 52.08 0.04 1 174 . 18 ASP HA H 4.588 0.007 1 175 . 18 ASP CB C 41.73 0.05 1 176 . 18 ASP HB3 H 2.237 0.011 2 177 . 18 ASP HB2 H 2.899 0.015 2 178 . 19 ALA N N 126.35 0.02 1 179 . 19 ALA H H 8.571 0.014 1 180 . 19 ALA CA C 53.74 0.03 1 181 . 19 ALA HA H 3.867 0.011 1 182 . 19 ALA CB C 18.45 0.07 1 183 . 19 ALA HB H 1.523 0.012 1 184 . 20 VAL N N 117.67 0.05 1 185 . 20 VAL H H 8.265 0.015 1 186 . 20 VAL CA C 65.40 0.07 1 187 . 20 VAL HA H 3.743 0.013 1 188 . 20 VAL CB C 31.13 0.04 1 189 . 20 VAL HB H 2.323 0.011 1 190 . 20 VAL CG1 C 20.66 0.07 2 191 . 20 VAL HG1 H 0.926 0.014 2 192 . 20 VAL CG2 C 22.07 0.05 2 193 . 20 VAL HG2 H 1.034 0.010 2 194 . 21 THR N N 107.33 0.06 1 195 . 21 THR H H 7.363 0.016 1 196 . 21 THR CA C 61.64 0.03 1 197 . 21 THR HA H 4.291 0.023 1 198 . 21 THR CB C 69.90 0.02 1 199 . 21 THR HB H 4.251 0.027 1 200 . 21 THR CG2 C 21.51 0.07 1 201 . 21 THR HG2 H 1.177 0.011 1 202 . 22 GLY N N 111.68 0.05 1 203 . 22 GLY H H 8.407 0.013 1 204 . 22 GLY CA C 45.95 0.09 1 205 . 22 GLY HA3 H 3.545 0.012 2 206 . 22 GLY HA2 H 4.022 0.013 2 207 . 23 GLU N N 117.37 0.02 1 208 . 23 GLU H H 7.126 0.011 1 209 . 23 GLU CA C 54.49 0.04 1 210 . 23 GLU HA H 4.498 0.015 1 211 . 23 GLU CB C 32.10 0.03 1 212 . 23 GLU HB3 H 1.705 0.015 2 213 . 23 GLU HB2 H 2.055 0.015 2 214 . 23 GLU CG C 35.52 0.04 1 215 . 23 GLU HG3 H 2.138 0.015 2 216 . 23 GLU HG2 H 2.228 0.018 2 217 . 24 PHE N N 118.85 0.04 1 218 . 24 PHE H H 8.790 0.012 1 219 . 24 PHE CA C 57.80 0.03 1 220 . 24 PHE HA H 5.477 0.009 1 221 . 24 PHE CB C 40.92 0.05 1 222 . 24 PHE HB3 H 3.012 0.011 2 223 . 24 PHE HB2 H 3.145 0.019 2 224 . 24 PHE CZ C 129.30 0.04 1 225 . 24 PHE HZ H 7.320 0.014 1 226 . 24 PHE CD1 C 131.99 0.01 1 227 . 24 PHE CD2 C 131.99 0.01 1 228 . 24 PHE HD1 H 7.502 0.012 1 229 . 24 PHE HD2 H 7.502 0.012 1 230 . 24 PHE CE1 C 131.13 0.10 1 231 . 24 PHE CE2 C 131.13 0.10 1 232 . 24 PHE HE1 H 7.302 0.011 1 233 . 24 PHE HE2 H 7.302 0.011 1 234 . 25 THR N N 114.56 0.06 1 235 . 25 THR H H 8.977 0.015 1 236 . 25 THR CA C 59.73 0.04 1 237 . 25 THR HA H 4.690 0.008 1 238 . 25 THR CB C 70.21 0.03 1 239 . 25 THR HB H 4.241 0.009 1 240 . 25 THR CG2 C 21.05 0.05 1 241 . 25 THR HG2 H 1.135 0.013 1 242 . 26 GLY N N 109.88 0.05 1 243 . 26 GLY H H 8.786 0.010 1 244 . 26 GLY CA C 45.71 0.06 1 245 . 26 GLY HA3 H 3.755 0.013 2 246 . 26 GLY HA2 H 4.451 0.013 2 247 . 27 MET N N 118.09 0.04 1 248 . 27 MET H H 8.133 0.011 1 249 . 27 MET CA C 53.39 0.08 1 250 . 27 MET HA H 4.307 0.018 1 251 . 27 MET CB C 33.08 0.04 1 252 . 27 MET HB3 H 1.946 0.020 2 253 . 27 MET HB2 H 2.038 0.019 2 254 . 27 MET CG C 31.87 0.06 1 255 . 27 MET HG3 H 2.469 0.012 2 256 . 27 MET HG2 H 2.593 0.017 2 257 . 27 MET CE C 17.20 0.05 1 258 . 27 MET HE H 1.656 0.015 1 259 . 28 PRO CA C 62.76 0.08 1 260 . 28 PRO HA H 4.251 0.011 1 261 . 28 PRO CB C 31.84 0.02 1 262 . 28 PRO HB3 H 1.028 0.020 2 263 . 28 PRO HB2 H 2.037 0.022 2 264 . 28 PRO CG C 26.85 0.05 1 265 . 28 PRO HG3 H 0.464 0.027 2 266 . 28 PRO HG2 H 1.320 0.018 2 267 . 28 PRO CD C 50.29 0.07 1 268 . 28 PRO HD3 H 3.022 0.013 2 269 . 28 PRO HD2 H 3.607 0.017 2 270 . 29 GLU N N 127.11 0.04 1 271 . 29 GLU H H 9.063 0.016 1 272 . 29 GLU CA C 59.83 0.05 1 273 . 29 GLU HA H 4.022 0.009 1 274 . 29 GLU CB C 29.11 0.03 1 275 . 29 GLU HB3 H 2.032 0.010 2 276 . 29 GLU HB2 H 2.132 0.014 2 277 . 29 GLU CG C 35.68 0.05 1 278 . 29 GLU HG3 H 2.320 0.013 2 279 . 29 GLU HG2 H 2.385 0.008 2 280 . 30 GLN N N 115.80 0.06 1 281 . 30 GLN H H 9.128 0.019 1 282 . 30 GLN CA C 58.55 0.02 1 283 . 30 GLN HA H 4.122 0.014 1 284 . 30 GLN CB C 27.80 0.02 1 285 . 30 GLN CG C 33.54 0.03 1 286 . 30 GLN HG3 H 2.494 0.012 2 287 . 30 GLN HG2 H 2.568 0.012 2 288 . 30 GLN NE2 N 111.60 0.03 1 289 . 30 GLN HE21 H 6.991 0.005 2 290 . 30 GLN HE22 H 7.595 0.003 2 291 . 30 GLN HB2 H 2.138 0.017 1 292 . 30 GLN HB3 H 2.138 0.017 1 293 . 31 TRP N N 117.85 0.04 1 294 . 31 TRP H H 7.279 0.013 1 295 . 31 TRP CA C 58.09 0.03 1 296 . 31 TRP HA H 4.568 0.014 1 297 . 31 TRP CB C 29.41 0.01 1 298 . 31 TRP HB3 H 3.113 0.017 2 299 . 31 TRP HB2 H 3.260 0.024 2 300 . 31 TRP CD1 C 123.17 0.02 1 301 . 31 TRP HD1 H 6.907 0.005 1 302 . 31 TRP NE1 N 127.27 0.01 1 303 . 31 TRP HE1 H 9.778 0.003 1 304 . 31 TRP CE3 C 119.80 0.06 1 305 . 31 TRP HE3 H 7.268 0.017 1 306 . 31 TRP CZ2 C 113.31 0.06 1 307 . 31 TRP HZ2 H 6.901 0.008 1 308 . 31 TRP CZ3 C 119.70 0.08 1 309 . 31 TRP HZ3 H 6.042 0.010 1 310 . 31 TRP CH2 C 123.41 0.04 1 311 . 31 TRP HH2 H 5.415 0.017 1 312 . 32 ALA N N 121.03 0.04 1 313 . 32 ALA H H 8.128 0.013 1 314 . 32 ALA CA C 55.25 0.05 1 315 . 32 ALA HA H 4.044 0.015 1 316 . 32 ALA CB C 17.73 0.05 1 317 . 32 ALA HB H 1.503 0.020 1 318 . 33 ARG N N 115.10 0.02 1 319 . 33 ARG H H 7.893 0.012 1 320 . 33 ARG CA C 58.42 0.08 1 321 . 33 ARG HA H 4.188 0.011 1 322 . 33 ARG CB C 29.90 0.06 1 323 . 33 ARG CG C 27.19 0.06 1 324 . 33 ARG HG3 H 1.731 0.009 2 325 . 33 ARG HG2 H 1.815 0.010 2 326 . 33 ARG CD C 43.14 0.05 1 327 . 33 ARG NE N 84.04 0.02 1 328 . 33 ARG HE H 7.457 0.017 1 329 . 33 ARG HB2 H 1.950 0.015 1 330 . 33 ARG HB3 H 1.950 0.015 1 331 . 33 ARG HD2 H 3.270 0.015 1 332 . 33 ARG HD3 H 3.270 0.015 1 333 . 34 LEU N N 119.60 0.04 1 334 . 34 LEU H H 7.616 0.012 1 335 . 34 LEU CA C 56.89 0.06 1 336 . 34 LEU HA H 4.225 0.018 1 337 . 34 LEU CB C 41.98 0.06 1 338 . 34 LEU HB3 H 1.540 0.017 2 339 . 34 LEU HB2 H 1.912 0.018 2 340 . 34 LEU CG C 26.79 0.15 1 341 . 34 LEU HG H 1.884 0.004 1 342 . 34 LEU CD1 C 22.64 0.06 2 343 . 34 LEU HD1 H 0.904 0.011 2 344 . 34 LEU CD2 C 25.41 0.04 2 345 . 34 LEU HD2 H 0.910 0.000 2 346 . 35 LEU N N 118.50 0.01 1 347 . 35 LEU H H 7.996 0.014 1 348 . 35 LEU CA C 55.95 0.04 1 349 . 35 LEU HA H 4.232 0.013 1 350 . 35 LEU CB C 42.08 0.05 1 351 . 35 LEU HB3 H 1.659 0.011 2 352 . 35 LEU HB2 H 1.781 0.012 2 353 . 35 LEU CG C 26.48 0.01 1 354 . 35 LEU HG H 1.737 0.007 1 355 . 35 LEU CD1 C 22.67 0.06 2 356 . 35 LEU HD1 H 0.744 0.010 2 357 . 35 LEU CD2 C 25.28 0.04 2 358 . 35 LEU HD2 H 0.767 0.014 2 359 . 36 GLN N N 117.83 0.03 1 360 . 36 GLN H H 7.759 0.012 1 361 . 36 GLN CA C 56.73 0.04 1 362 . 36 GLN HA H 4.382 0.008 1 363 . 36 GLN CB C 28.60 0.04 1 364 . 36 GLN CG C 33.67 0.02 1 365 . 36 GLN HG3 H 2.514 0.012 2 366 . 36 GLN HG2 H 2.577 0.015 2 367 . 36 GLN NE2 N 111.39 0.04 1 368 . 36 GLN HE21 H 6.942 0.003 2 369 . 36 GLN HE22 H 7.574 0.011 2 370 . 36 GLN HB2 H 2.252 0.016 1 371 . 36 GLN HB3 H 2.252 0.016 1 372 . 37 THR N N 112.80 0.04 1 373 . 37 THR H H 8.074 0.014 1 374 . 37 THR CA C 62.39 0.10 1 375 . 37 THR HA H 4.418 0.028 1 376 . 37 THR CB C 69.50 0.14 1 377 . 37 THR HB H 4.400 0.006 1 378 . 37 THR CG2 C 21.41 0.05 1 379 . 37 THR HG2 H 1.306 0.018 1 380 . 38 SER N N 116.96 0.05 1 381 . 38 SER H H 8.226 0.014 1 382 . 38 SER CA C 58.46 0.02 1 383 . 38 SER HA H 4.548 0.012 1 384 . 38 SER CB C 63.55 0.04 1 385 . 38 SER HB3 H 3.945 0.016 2 386 . 38 SER HB2 H 3.971 0.015 2 387 . 39 ASN N N 120.37 0.02 1 388 . 39 ASN H H 8.449 0.014 1 389 . 39 ASN CA C 53.26 0.07 1 390 . 39 ASN HA H 4.798 0.012 1 391 . 39 ASN CB C 38.60 0.07 1 392 . 39 ASN HB3 H 2.831 0.007 2 393 . 39 ASN HB2 H 2.912 0.009 2 394 . 39 ASN ND2 N 112.18 0.02 1 395 . 39 ASN HD21 H 6.968 0.012 2 396 . 39 ASN HD22 H 7.647 0.015 2 397 . 40 ILE N N 120.33 0.01 1 398 . 40 ILE H H 8.127 0.013 1 399 . 40 ILE CA C 61.28 0.06 1 400 . 40 ILE HA H 4.269 0.008 1 401 . 40 ILE CB C 38.46 0.03 1 402 . 40 ILE HB H 1.942 0.014 1 403 . 40 ILE CG1 C 27.05 0.03 1 404 . 40 ILE HG13 H 1.236 0.015 2 405 . 40 ILE HG12 H 1.511 0.016 2 406 . 40 ILE CG2 C 17.34 0.05 1 407 . 40 ILE HG2 H 0.956 0.012 1 408 . 40 ILE CD1 C 12.84 0.04 1 409 . 40 ILE HD1 H 0.902 0.014 1 410 . 41 THR N N 118.12 0.03 1 411 . 41 THR H H 8.274 0.012 1 412 . 41 THR CA C 61.85 0.03 1 413 . 41 THR HA H 4.380 0.011 1 414 . 41 THR CB C 69.71 0.15 1 415 . 41 THR HB H 4.241 0.008 1 416 . 41 THR CG2 C 21.46 0.03 1 417 . 41 THR HG2 H 1.255 0.010 1 418 . 42 LYS N N 123.86 0.06 1 419 . 42 LYS H H 8.404 0.013 1 420 . 42 LYS CA C 56.21 0.03 1 421 . 42 LYS HA H 4.407 0.017 1 422 . 42 LYS CB C 32.84 0.05 1 423 . 42 LYS HB3 H 1.820 0.010 2 424 . 42 LYS HB2 H 1.909 0.014 2 425 . 42 LYS CG C 24.47 0.02 1 426 . 42 LYS HG3 H 1.454 0.015 2 427 . 42 LYS HG2 H 1.490 0.019 2 428 . 42 LYS CD C 28.84 0.02 1 429 . 42 LYS CE C 41.93 0.05 1 430 . 42 LYS HD2 H 1.729 0.018 1 431 . 42 LYS HD3 H 1.729 0.018 1 432 . 42 LYS HE2 H 3.048 0.018 1 433 . 42 LYS HE3 H 3.048 0.018 1 434 . 43 SER N N 117.03 0.01 1 435 . 43 SER H H 8.417 0.016 1 436 . 43 SER CA C 58.25 0.07 1 437 . 43 SER HA H 4.514 0.025 1 438 . 43 SER CB C 63.71 0.02 1 439 . 43 SER HB2 H 3.901 0.012 1 440 . 43 SER HB3 H 3.901 0.012 1 441 . 44 GLU N N 122.49 0.08 1 442 . 44 GLU H H 8.523 0.014 1 443 . 44 GLU CA C 56.26 0.04 1 444 . 44 GLU HA H 4.359 0.012 1 445 . 44 GLU CB C 30.17 0.04 1 446 . 44 GLU HB3 H 1.976 0.007 2 447 . 44 GLU HB2 H 2.119 0.007 2 448 . 44 GLU CG C 35.99 0.10 1 449 . 44 GLU HG2 H 2.310 0.012 1 450 . 44 GLU HG3 H 2.310 0.012 1 451 . 45 GLN N N 121.82 0.02 1 452 . 45 GLN H H 8.402 0.013 1 453 . 45 GLN CA C 55.68 0.06 1 454 . 45 GLN HA H 4.366 0.012 1 455 . 45 GLN CB C 29.28 0.06 1 456 . 45 GLN HB3 H 2.033 0.015 2 457 . 45 GLN HB2 H 2.157 0.007 2 458 . 45 GLN CG C 33.66 0.08 1 459 . 45 GLN NE2 N 112.58 0.01 1 460 . 45 GLN HE21 H 6.912 0.001 2 461 . 45 GLN HE22 H 7.678 0.001 2 462 . 45 GLN HG2 H 2.387 0.019 1 463 . 45 GLN HG3 H 2.387 0.019 1 464 . 46 LYS N N 128.51 0.02 1 465 . 46 LYS H H 8.092 0.021 1 466 . 46 LYS CA C 57.30 0.08 1 467 . 46 LYS HA H 4.213 0.018 1 468 . 46 LYS CB C 33.50 0.06 1 469 . 46 LYS HB3 H 1.743 0.011 2 470 . 46 LYS HB2 H 1.867 0.009 2 471 . 46 LYS CG C 24.52 0.02 1 472 . 46 LYS CD C 28.83 0.00 1 473 . 46 LYS CE C 41.94 0.01 1 474 . 46 LYS HG2 H 1.427 0.004 1 475 . 46 LYS HG3 H 1.427 0.004 1 476 . 46 LYS HD2 H 1.706 0.008 1 477 . 46 LYS HD3 H 1.706 0.008 1 478 . 46 LYS HE2 H 3.031 0.013 1 479 . 46 LYS HE3 H 3.031 0.013 1 stop_ save_