data_2208 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site ; _BMRB_accession_number 2208 _BMRB_flat_file_name bmr2208.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Neri Placido . . 2 Meadows Robert P. . 3 Gemmecker G. . . 4 Olejniczak E. T. . 5 Nettesheim David G. . 6 Logan Timothy . . 7 Simmer R. . . 8 Helfrich R. . . 9 Holzman Thomas F. . 10 Severin Jean . . 11 Fesik Stephen W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 323 "13C chemical shifts" 318 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Neri, Placido, Meadows, Robert P., Gemmecker, G., Olejniczak, E.T., Nettesheim, David G., Logan, Timothy, Simmer, R., Helfrich, R., Holzman, Thomas F., Severin, Jean, Fesik, Stephen W., "1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site," FEBS Lett. 294 (1-2), 81-88 (1991). ; _Citation_title ; 1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Neri Placido . . 2 Meadows Robert P. . 3 Gemmecker G. . . 4 Olejniczak E. T. . 5 Nettesheim David G. . 6 Logan Timothy . . 7 Simmer R. . . 8 Helfrich R. . . 9 Holzman Thomas F. . 10 Severin Jean . . 11 Fesik Stephen W. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 294 _Journal_issue 1-2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 81 _Page_last 88 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_cyclophilin _Saveframe_category molecular_system _Mol_system_name cyclophilin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cyclophilin $cyclophilin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyclophilin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common cyclophilin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; MVNPTVFFDIAVDGEPLGRV SFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGF MCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSM ANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVE AMERFGSRNGKTSKKITIAD CGQLE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 ASN 4 PRO 5 THR 6 VAL 7 PHE 8 PHE 9 ASP 10 ILE 11 ALA 12 VAL 13 ASP 14 GLY 15 GLU 16 PRO 17 LEU 18 GLY 19 ARG 20 VAL 21 SER 22 PHE 23 GLU 24 LEU 25 PHE 26 ALA 27 ASP 28 LYS 29 VAL 30 PRO 31 LYS 32 THR 33 ALA 34 GLU 35 ASN 36 PHE 37 ARG 38 ALA 39 LEU 40 SER 41 THR 42 GLY 43 GLU 44 LYS 45 GLY 46 PHE 47 GLY 48 TYR 49 LYS 50 GLY 51 SER 52 CYS 53 PHE 54 HIS 55 ARG 56 ILE 57 ILE 58 PRO 59 GLY 60 PHE 61 MET 62 CYS 63 GLN 64 GLY 65 GLY 66 ASP 67 PHE 68 THR 69 ARG 70 HIS 71 ASN 72 GLY 73 THR 74 GLY 75 GLY 76 LYS 77 SER 78 ILE 79 TYR 80 GLY 81 GLU 82 LYS 83 PHE 84 GLU 85 ASP 86 GLU 87 ASN 88 PHE 89 ILE 90 LEU 91 LYS 92 HIS 93 THR 94 GLY 95 PRO 96 GLY 97 ILE 98 LEU 99 SER 100 MET 101 ALA 102 ASN 103 ALA 104 GLY 105 PRO 106 ASN 107 THR 108 ASN 109 GLY 110 SER 111 GLN 112 PHE 113 PHE 114 ILE 115 CYS 116 THR 117 ALA 118 LYS 119 THR 120 GLU 121 TRP 122 LEU 123 ASP 124 GLY 125 LYS 126 HIS 127 VAL 128 VAL 129 PHE 130 GLY 131 LYS 132 VAL 133 LYS 134 GLU 135 GLY 136 MET 137 ASN 138 ILE 139 VAL 140 GLU 141 ALA 142 MET 143 GLU 144 ARG 145 PHE 146 GLY 147 SER 148 ARG 149 ASN 150 GLY 151 LYS 152 THR 153 SER 154 LYS 155 LYS 156 ILE 157 THR 158 ILE 159 ALA 160 ASP 161 CYS 162 GLY 163 GLN 164 LEU 165 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 17218 CypA 99.39 164 100.00 100.00 2.69e-115 BMRB 25104 entity_1 100.00 165 100.00 100.00 3.57e-116 BMRB 25337 CypA 100.00 165 100.00 100.00 3.57e-116 BMRB 25502 entity_1 100.00 165 100.00 100.00 3.57e-116 PDB 1AK4 "Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid" 100.00 165 100.00 100.00 3.57e-116 PDB 1AWQ "Cypa Complexed With Hagpia (Pseudo-Symmetric Monomer)" 99.39 164 100.00 100.00 2.69e-115 PDB 1AWR "Cypa Complexed With Hagpia" 99.39 164 100.00 100.00 2.69e-115 PDB 1AWS "Secypa Complexed With Hagpia (Pseudo-Symmetric Monomer)" 99.39 164 97.56 97.56 4.09e-111 PDB 1AWT "Secypa Complexed With Hagpia" 99.39 164 97.56 97.56 4.09e-111 PDB 1AWU "Cypa Complexed With Hvgpia (Pseudo-Symmetric Monomer)" 99.39 164 100.00 100.00 2.69e-115 PDB 1AWV "Cypa Complexed With Hvgpia" 99.39 164 100.00 100.00 2.69e-115 PDB 1BCK "Human Cyclophilin A Complexed With 2-Thr Cyclosporin" 99.39 165 100.00 100.00 2.78e-115 PDB 1CWA "X-Ray Structure Of A Monomeric Cyclophilin A-Cyclosporin A Crystal Complex At 2.1 Angstroms Resolution" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWB "The X-Ray Structure Of (Mebm2t)1-Cyclosporin Complexed With Cyclophilin A Provides An Explanation For Its Anomalously High Immu" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWC "Improved Binding Affinity For Cyclophilin A By A Cyclosporin Derivative Singly Modified At Its Effector Domain" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWF "Human Cyclophilin A Complexed With 2-Val Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWH "Human Cyclophilin A Complexed With 3-D-Ser Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWI "Human Cyclophilin A Complexed With 2-Val 3-(N-Methyl)-D-Alanine Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWJ "Human Cyclophilin A Complexed With 2-Val 3-S-Methyl-Sarcosine Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWK "Human Cyclophilin A Complexed With 1-(6,7-Dihydro)mebmt 2-Val 3-D-(2- S-Methyl)sarcosine Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWL "Human Cyclophilin A Complexed With 4 4-Hydroxy-Meleu Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWM "Human Cyclophilin A Complexed With 4 Meile Cyclosporin" 100.00 165 100.00 100.00 3.57e-116 PDB 1CWO "Human Cyclophilin A Complexed With Thr2, Leu5, D-Hiv8, Leu10 Cyclosporin" 99.39 165 100.00 100.00 2.78e-115 PDB 1FGL "Cyclophilin A Complexed With A Fragment Of Hiv-1 Gag Protein" 100.00 165 100.00 100.00 3.57e-116 PDB 1M63 "Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition Of Immunophilin-Drug Complexes" 100.00 165 100.00 100.00 3.57e-116 PDB 1M9C "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex." 100.00 165 100.00 100.00 3.57e-116 PDB 1M9D "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) O-Type Chimera Complex." 100.00 165 100.00 100.00 3.57e-116 PDB 1M9E "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex" 99.39 164 100.00 100.00 1.68e-115 PDB 1M9F "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex." 100.00 165 100.00 100.00 3.57e-116 PDB 1M9X "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex." 100.00 165 100.00 100.00 3.57e-116 PDB 1M9Y "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex." 100.00 165 100.00 100.00 3.57e-116 PDB 1MF8 "Crystal Structure Of Human Calcineurin Complexed With Cyclosporin A And Human Cyclophilin" 100.00 165 100.00 100.00 3.57e-116 PDB 1MIK "The Role Of Water Molecules In The Structure-Based Design Of (5- Hydroxynorvaline)-2-Cyclosporin: Synthesis, Biological Activit" 100.00 165 100.00 100.00 3.57e-116 PDB 1NMK "The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-Ray Crystal Structure And Bindin" 100.00 165 100.00 100.00 3.57e-116 PDB 1OCA "Human Cyclophilin A, Unligated, Nmr, 20 Structures" 100.00 165 100.00 100.00 3.57e-116 PDB 1RMH "Recombinant Cyclophilin A From Human T Cell" 99.39 164 100.00 100.00 2.69e-115 PDB 1VBS "Structure Of Cyclophilin Complexed With (D)ala Containing Tetrapeptide" 100.00 165 100.00 100.00 3.57e-116 PDB 1VBT "Structure Of Cyclophilin Complexed With Sulfur-Substituted Tetrapeptide Aapf" 100.00 165 100.00 100.00 3.57e-116 PDB 1W8L "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 100.00 100.00 3.57e-116 PDB 1W8M "Enzymatic And Structural Characterisation Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 100.00 100.00 3.57e-116 PDB 1W8V "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 100.00 100.00 3.57e-116 PDB 1YND "Structure Of Human Cyclophilin A In Complex With The Novel Immunosuppressant Sanglifehrin A At 1.6a Resolution" 100.00 165 100.00 100.00 3.57e-116 PDB 1ZKF "Cyrstal Structure Of Human Cyclophilin-A In Complex With Suc-Agpf-Pna" 100.00 165 100.00 100.00 3.57e-116 PDB 2ALF "Crystal Structure Of Human Cypa Mutant K131a" 99.39 164 98.78 99.39 5.56e-114 PDB 2CPL "Similarities And Differences Between Human Cyclophilin A And Other Beta-Barrel Structures. Structural Refinement At 1.63 Angstr" 100.00 165 100.00 100.00 3.57e-116 PDB 2CYH "Cyclophilin A Complexed With Dipeptide Ala-Pro" 99.39 164 100.00 100.00 2.69e-115 PDB 2MS4 "Cyclophilin A Complexed With A Fragment Of Crk-ii" 100.00 165 100.00 100.00 3.57e-116 PDB 2MZU "Extending The Enoe Data Set Of Large Proteins By Evaluation Of Noes With Unresolved Diagonals" 100.00 165 100.00 100.00 3.57e-116 PDB 2N0T "Structural Ensemble Of The Enzyme Cyclophilin Reveals An Orchestrated Mode Of Action At Atomic Resolution" 100.00 165 100.00 100.00 3.57e-116 PDB 2RMA "Crystal Structures Of Cyclophilin A Complexed With Cyclosporin A And N-Methyl-4-[(E)-2-Butenyl]-4,4-Dimethylthreonine Cyclospor" 100.00 165 100.00 100.00 3.57e-116 PDB 2RMB "Crystal Structures Of Cyclophilin A Complexed With Cyclosporin A And N-Methyl-4-[(E)-2-Butenyl]-4,4-Dimethylthreonine Cyclospor" 100.00 165 100.00 100.00 3.57e-116 PDB 2WLW "Structure Of The N-Terminal Capsid Domain Of Hiv-2" 100.00 165 98.79 99.39 1.45e-114 PDB 2X25 "Free Acetyl-Cypa Orthorhombic Form" 99.39 169 98.78 99.39 9.99e-114 PDB 2X2A "Free Acetyl-Cypa Trigonal Form" 100.00 165 98.79 99.39 8.49e-115 PDB 2X2C "Acetyl-Cypa:cyclosporine Complex" 100.00 165 99.39 99.39 1.92e-115 PDB 2X2D "Acetyl-Cypa:hiv-1 N-Term Capsid Domain Complex" 100.00 165 99.39 99.39 1.92e-115 PDB 2X83 "Evolutionary Basis Of Hiv Restriction By The Antiretroviral Trimcyp" 98.79 163 98.77 99.39 5.27e-113 PDB 2XGY "Complex Of Rabbit Endogenous Lentivirus (Relik)capsid With Cyclophilin A" 100.00 173 100.00 100.00 8.38e-116 PDB 3CYH "Cyclophilin A Complexed With Dipeptide Ser-Pro" 99.39 164 100.00 100.00 2.69e-115 PDB 3CYS "Determination Of The Nmr Solution Structure Of The Cyclophilin A- Cyclosporin A Complex" 100.00 165 100.00 100.00 3.57e-116 PDB 3K0M "Cryogenic Structure Of Cypa" 100.00 165 100.00 100.00 3.57e-116 PDB 3K0N "Room Temperature Structure Of Cypa" 100.00 165 100.00 100.00 3.57e-116 PDB 3K0O "Room Temperature Structure Of Cypa Mutant Ser99thr" 100.00 165 99.39 100.00 1.05e-115 PDB 3K0P "Cryogenic Structure Of Cypa Mutant Ser99thr" 100.00 165 99.39 100.00 1.05e-115 PDB 3K0Q "Cryogenic Structure Of Cypa Mutant Ser99thr (2)" 100.00 165 99.39 100.00 1.05e-115 PDB 3K0R "Cryogenic Structure Of Cypa Mutant Arg55lys" 100.00 165 99.39 100.00 1.28e-115 PDB 3ODI "Crystal Structure Of Cyclophilin A In Complex With Voclosporin E- Isa247" 100.00 165 100.00 100.00 3.57e-116 PDB 3ODL "Crystal Structure Of Cyclophilin A In Complex With Voclosporin Z- Isa247" 100.00 165 100.00 100.00 3.57e-116 PDB 3RDD "Human Cyclophilin A Complexed With An Inhibitor" 100.00 184 100.00 100.00 4.01e-116 PDB 4CYH "Cyclophilin A Complexed With Dipeptide His-Pro" 99.39 164 100.00 100.00 2.69e-115 PDB 4DGA "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-1 Ca(O-Loop) Complex" 100.00 165 98.79 99.39 1.45e-114 PDB 4DGB "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-2 Ca Cyclophilin- Binding Loop Complex" 100.00 165 98.79 99.39 1.45e-114 PDB 4DGC "Trimcyp Cyclophilin Domain From Macaca Mulatta: Cyclosporin A Complex" 100.00 165 98.79 99.39 1.45e-114 PDB 4DGD "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant" 100.00 165 98.18 98.79 7.75e-113 PDB 4DGE "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant, Hiv-1 Ca(O-Loop) Complex" 100.00 165 98.18 98.79 7.75e-113 PDB 4IPZ "Smbz Bound To Cyclophilin A" 100.00 165 100.00 100.00 3.57e-116 PDB 4N1M "Structure Of Cyclophilin A In Complex With Glypro" 100.00 168 100.00 100.00 3.14e-116 PDB 4N1N "Structure Of Cyclophilin A In Complex With Benzamide." 100.00 165 100.00 100.00 3.57e-116 PDB 4N1O "Structure Of Cyclophilin A In Complex With Saccharin." 100.00 165 100.00 100.00 3.57e-116 PDB 4N1P "Structure Of Cyclophilin A In Complex With Picolinamide." 100.00 165 100.00 100.00 3.57e-116 PDB 4N1Q "Structure Of Cyclophilin A In Complex With Cyclohexanecarboxamide." 100.00 165 100.00 100.00 3.57e-116 PDB 4N1R "Structure Of Cyclophilin A In Complex With Benzenesulfonohydrazide." 100.00 165 100.00 100.00 3.57e-116 PDB 4N1S "Structure Of Cyclophilin A In Complex With Benzohydrazide." 100.00 165 100.00 100.00 3.57e-116 PDB 4YUG "Multiconformer Synchrotron Model Of Cypa At 100 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUH "Multiconformer Synchrotron Model Of Cypa At 150 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUI "Multiconformer Synchrotron Model Of Cypa At 180 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUJ "Multiconformer Synchrotron Model Of Cypa At 240 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUK "Multiconformer Synchrotron Model Of Cypa At 260 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUL "Multiconformer Synchrotron Model Of Cypa At 280 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUM "Multiconformer Synchrotron Model Of Cypa At 300 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUN "Multiconformer Synchrotron Model Of Cypa At 310 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUO "High-resolution Multiconformer Synchrotron Model Of Cypa At 273 K" 100.00 165 100.00 100.00 3.57e-116 PDB 4YUP "Multiconformer Fixed-target X-ray Free Electron (xfel) Model Of Cypa At 273 K" 100.00 165 100.00 100.00 3.57e-116 PDB 5CYH "Cyclophilin A Complexed With Dipeptide Gly-Pro" 99.39 164 100.00 100.00 2.69e-115 DBJ BAE01146 "unnamed protein product [Macaca fascicularis]" 63.64 105 99.05 100.00 1.51e-68 DBJ BAE30323 "unnamed protein product [Mus musculus]" 99.39 164 96.95 97.56 9.05e-112 DBJ BAE87660 "unnamed protein product [Macaca fascicularis]" 100.00 165 100.00 100.00 3.57e-116 DBJ BAF82774 "unnamed protein product [Homo sapiens]" 100.00 165 100.00 100.00 3.57e-116 DBJ BAF83540 "unnamed protein product [Homo sapiens]" 100.00 165 99.39 100.00 1.37e-115 EMBL CAA34961 "unnamed protein product [Cricetulus longicaudatus]" 99.39 164 96.95 98.78 1.68e-112 EMBL CAA37039 "peptidylprolyl isomerase [Homo sapiens]" 100.00 165 100.00 100.00 3.57e-116 EMBL CAA68264 "unnamed protein product [Homo sapiens]" 100.00 165 100.00 100.00 3.57e-116 EMBL CAG32988 "PPIA [Homo sapiens]" 100.00 165 99.39 100.00 1.23e-115 EMBL CAH91833 "hypothetical protein [Pongo abelii]" 100.00 165 99.39 99.39 1.43e-115 GB AAB81959 "cyclophilin A [Papio hamadryas]" 100.00 165 100.00 100.00 3.57e-116 GB AAB81960 "cyclophilin A [Chlorocebus aethiops]" 100.00 165 100.00 100.00 3.57e-116 GB AAB81961 "cyclophilin A [Macaca mulatta]" 100.00 165 100.00 100.00 3.57e-116 GB AAF69142 "cyclophilin I [Bos taurus]" 56.97 94 98.94 100.00 5.64e-60 GB AAF78600 "cyclophilin A [Canis lupus familiaris]" 94.55 156 98.72 100.00 4.51e-108 PIR CSHYAC "peptidylprolyl isomerase (EC 5.2.1.8) A - Chinese hamster" 99.39 164 96.95 98.78 1.68e-112 PRF 1503232A "peptidyl-Pro cis trans isomerase" 99.39 164 98.78 100.00 1.28e-114 REF NP_001009370 "peptidyl-prolyl cis-trans isomerase A [Felis catus]" 99.39 164 96.95 98.78 1.96e-112 REF NP_001027981 "peptidyl-prolyl cis-trans isomerase A [Macaca mulatta]" 100.00 165 100.00 100.00 3.57e-116 REF NP_001126060 "peptidyl-prolyl cis-trans isomerase A [Pongo abelii]" 100.00 165 99.39 99.39 1.43e-115 REF NP_001270275 "uncharacterized protein LOC101866023 [Macaca fascicularis]" 63.64 105 99.05 100.00 1.51e-68 REF NP_001271703 "uncharacterized protein LOC101925040 [Macaca fascicularis]" 100.00 165 100.00 100.00 3.57e-116 SP P14851 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 99.39 164 96.95 98.78 1.68e-112 SP P62935 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 99.39 164 98.78 100.00 1.28e-114 SP P62936 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 99.39 164 98.78 100.00 1.28e-114 SP P62937 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 100.00 165 100.00 100.00 3.57e-116 SP P62938 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 100.00 165 100.00 100.00 3.57e-116 TPG DAA25853 "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" 99.39 164 97.56 98.78 4.73e-113 TPG DAA25854 "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" 99.39 164 97.56 98.78 4.73e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $cyclophilin human 9606 Eukaryota Metazoa Homo sapiens generic 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 $cyclophilin 'not available' . Escherichia coli DL-39 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . na temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP C . . . 0 . . . . . $entry_citation $entry_citation TSP H . . . 0 . . . . . $entry_citation $entry_citation NH4[15]NO3 N . . . 376.25 . . . . . $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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name cyclophilin _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 . 4 PRO CA C 56.9 . 1 2 . 4 PRO C C 174.5 . 1 3 . 5 THR H H 8.79 . 1 4 . 5 THR CA C 60.4 . 1 5 . 5 THR HA H 5.71 . 1 6 . 5 THR C C 174.8 . 1 7 . 5 THR N N 114.4 . 1 8 . 6 VAL H H 8.72 . 1 9 . 6 VAL CA C 58.5 . 1 10 . 6 VAL HA H 5.31 . 1 11 . 6 VAL C C 173.1 . 1 12 . 6 VAL N N 120 . 1 13 . 7 PHE H H 8.96 . 1 14 . 7 PHE CA C 54.9 . 1 15 . 7 PHE HA H 5.88 . 1 16 . 7 PHE C C 172 . 1 17 . 7 PHE N N 118.9 . 1 18 . 8 PHE H H 9.54 . 1 19 . 8 PHE CA C 53 . 1 20 . 8 PHE HA H 5.32 . 1 21 . 8 PHE C C 174.4 . 1 22 . 8 PHE N N 117 . 1 23 . 9 ASP H H 9.27 . 1 24 . 9 ASP CA C 54.4 . 1 25 . 9 ASP HA H 5.52 . 1 26 . 9 ASP C C 176.6 . 1 27 . 9 ASP N N 123.7 . 1 28 . 10 ILE H H 9.06 . 1 29 . 10 ILE CA C 57.7 . 1 30 . 10 ILE HA H 5.2 . 1 31 . 10 ILE C C 175.4 . 1 32 . 10 ILE N N 123.7 . 1 33 . 11 ALA H H 9.65 . 1 34 . 11 ALA CA C 50.5 . 1 35 . 11 ALA HA H 5.15 . 1 36 . 11 ALA C C 174.2 . 1 37 . 11 ALA N N 131.9 . 1 38 . 12 VAL H H 8.93 . 1 39 . 12 VAL CA C 60.1 . 1 40 . 12 VAL HA H 4.5 . 1 41 . 12 VAL C C 175.9 . 1 42 . 12 VAL N N 117.8 . 1 43 . 13 ASP H H 9.87 . 1 44 . 13 ASP CA C 54.5 . 1 45 . 13 ASP HA H 4.32 . 1 46 . 13 ASP C C 175.2 . 1 47 . 13 ASP N N 130.4 . 1 48 . 14 GLY H H 8.58 . 1 49 . 14 GLY CA C 45 . 1 50 . 14 GLY HA2 H 3.41 . 2 51 . 14 GLY C C 173.1 . 1 52 . 14 GLY HA3 H 4.19 . 2 53 . 14 GLY N N 101.1 . 1 54 . 15 GLU H H 8.06 . 1 55 . 15 GLU CA C 52.5 . 1 56 . 15 GLU HA H 4.78 . 1 57 . 15 GLU N N 122.9 . 1 58 . 16 PRO CA C 64.4 . 1 59 . 16 PRO C C 175.4 . 1 60 . 17 LEU H H 9.19 . 1 61 . 17 LEU CA C 55.2 . 1 62 . 17 LEU HA H 4.7 . 1 63 . 17 LEU C C 175.3 . 1 64 . 17 LEU N N 125.6 . 1 65 . 18 GLY H H 7.24 . 1 66 . 18 GLY CA C 44.9 . 1 67 . 18 GLY HA2 H 3.95 . 2 68 . 18 GLY C C 169.4 . 1 69 . 18 GLY HA3 H 4.21 . 2 70 . 18 GLY N N 101.6 . 1 71 . 19 ARG H H 8.39 . 1 72 . 19 ARG CA C 54.7 . 1 73 . 19 ARG HA H 5.63 . 1 74 . 19 ARG C C 174.4 . 1 75 . 19 ARG N N 120.4 . 1 76 . 20 VAL H H 9.39 . 1 77 . 20 VAL CA C 59.6 . 1 78 . 20 VAL HA H 4.58 . 1 79 . 20 VAL C C 173.2 . 1 80 . 20 VAL N N 126.3 . 1 81 . 21 SER H H 8.78 . 1 82 . 21 SER CA C 55.1 . 1 83 . 21 SER HA H 5.53 . 1 84 . 21 SER C C 173.1 . 1 85 . 21 SER N N 120 . 1 86 . 22 PHE H H 9.49 . 1 87 . 22 PHE CA C 55.4 . 1 88 . 22 PHE HA H 5.21 . 1 89 . 22 PHE C C 174.8 . 1 90 . 22 PHE N N 118.5 . 1 91 . 23 GLU H H 8.71 . 1 92 . 23 GLU CA C 54.7 . 1 93 . 23 GLU HA H 4.7 . 1 94 . 23 GLU C C 174 . 1 95 . 23 GLU N N 122.6 . 1 96 . 24 LEU H H 8.16 . 1 97 . 24 LEU CA C 51.4 . 1 98 . 24 LEU HA H 4.71 . 1 99 . 24 LEU C C 176.5 . 1 100 . 24 LEU N N 121.9 . 1 101 . 25 PHE H H 8.91 . 1 102 . 25 PHE CA C 54.3 . 1 103 . 25 PHE HA H 5.13 . 1 104 . 25 PHE C C 175.9 . 1 105 . 25 PHE N N 124.1 . 1 106 . 26 ALA H H 8.47 . 1 107 . 26 ALA CA C 54.1 . 1 108 . 26 ALA HA H 3.75 . 1 109 . 26 ALA C C 175.6 . 1 110 . 26 ALA N N 128.5 . 1 111 . 27 ASP H H 8.97 . 1 112 . 27 ASP CA C 54.9 . 1 113 . 27 ASP HA H 4.27 . 1 114 . 27 ASP C C 176.3 . 1 115 . 27 ASP N N 112.9 . 1 116 . 28 LYS H H 7.54 . 1 117 . 28 LYS CA C 56.2 . 1 118 . 28 LYS HA H 4.56 . 1 119 . 28 LYS C C 176.2 . 1 120 . 28 LYS N N 117.4 . 1 121 . 29 VAL H H 8.36 . 1 122 . 29 VAL CA C 57.9 . 1 123 . 29 VAL HA H 4.41 . 1 124 . 29 VAL N N 114.4 . 1 125 . 30 PRO CA C 65.9 . 1 126 . 30 PRO C C 180.2 . 1 127 . 31 LYS H H 10.71 . 1 128 . 31 LYS CA C 60.1 . 1 129 . 31 LYS HA H 4 . 1 130 . 31 LYS C C 181 . 1 131 . 31 LYS N N 123.3 . 1 132 . 32 THR H H 10.28 . 1 133 . 32 THR CA C 66.9 . 1 134 . 32 THR HA H 3.98 . 1 135 . 32 THR C C 177 . 1 136 . 32 THR N N 123.7 . 1 137 . 33 ALA H H 9.23 . 1 138 . 33 ALA CA C 55.6 . 1 139 . 33 ALA HA H 4.03 . 1 140 . 33 ALA C C 177.4 . 1 141 . 33 ALA N N 124.8 . 1 142 . 34 GLU H H 8.03 . 1 143 . 34 GLU CA C 57.6 . 1 144 . 34 GLU HA H 4.49 . 1 145 . 34 GLU C C 176.7 . 1 146 . 34 GLU N N 117.4 . 1 147 . 35 ASN H H 7.13 . 1 148 . 35 ASN CA C 56.4 . 1 149 . 35 ASN HA H 4.03 . 1 150 . 35 ASN C C 174 . 1 151 . 35 ASN N N 115.2 . 1 152 . 36 PHE H H 7.02 . 1 153 . 36 PHE CA C 61.1 . 1 154 . 36 PHE HA H 4.11 . 1 155 . 36 PHE C C 178.1 . 1 156 . 36 PHE N N 116.6 . 1 157 . 37 ARG H H 8.96 . 1 158 . 37 ARG CA C 60.1 . 1 159 . 37 ARG C C 177.3 . 1 160 . 37 ARG N N 120.4 . 1 161 . 38 ALA H H 8.67 . 1 162 . 38 ALA CA C 53.9 . 1 163 . 38 ALA HA H 4.04 . 1 164 . 38 ALA C C 181.7 . 1 165 . 38 ALA N N 118.5 . 1 166 . 39 LEU H H 8.22 . 1 167 . 39 LEU CA C 56.9 . 1 168 . 39 LEU HA H 3.75 . 1 169 . 39 LEU C C 178.8 . 1 170 . 39 LEU N N 120.4 . 1 171 . 40 SER H H 7.91 . 1 172 . 40 SER CA C 62.2 . 1 173 . 40 SER HA H 4.44 . 1 174 . 40 SER C C 173.8 . 1 175 . 40 SER N N 118.9 . 1 176 . 41 THR H H 7.99 . 1 177 . 41 THR CA C 62.6 . 1 178 . 41 THR HA H 4.27 . 1 179 . 41 THR C C 177.5 . 1 180 . 41 THR N N 107.7 . 1 181 . 42 GLY H H 7.58 . 1 182 . 42 GLY CA C 45.4 . 1 183 . 42 GLY HA2 H 3.46 . 2 184 . 42 GLY C C 177 . 1 185 . 42 GLY HA3 H 3.87 . 2 186 . 42 GLY N N 107.7 . 1 187 . 43 GLU H H 8 . 1 188 . 43 GLU CA C 58.2 . 1 189 . 43 GLU C C 175.8 . 1 190 . 43 GLU N N 117.8 . 1 191 . 44 LYS H H 9.13 . 1 192 . 44 LYS CA C 53.9 . 1 193 . 44 LYS HA H 4.28 . 1 194 . 44 LYS C C 175.9 . 1 195 . 44 LYS N N 117.8 . 1 196 . 45 GLY H H 7.94 . 1 197 . 45 GLY CA C 44.3 . 1 198 . 45 GLY HA2 H 3.55 . 2 199 . 45 GLY C C 171.9 . 1 200 . 45 GLY HA3 H 4.28 . 2 201 . 45 GLY N N 104.8 . 1 202 . 46 PHE H H 6.42 . 1 203 . 46 PHE CA C 53.7 . 1 204 . 46 PHE HA H 4.6 . 1 205 . 46 PHE C C 172.1 . 1 206 . 46 PHE N N 113.3 . 1 207 . 47 GLY H H 7.74 . 1 208 . 47 GLY CA C 45.2 . 1 209 . 47 GLY HA2 H 4.34 . 2 210 . 47 GLY C C 170.9 . 1 211 . 47 GLY HA3 H 2.5 . 2 212 . 47 GLY N N 104 . 1 213 . 48 TYR H H 6.86 . 1 214 . 48 TYR CA C 57.1 . 1 215 . 48 TYR HA H 4.2 . 1 216 . 48 TYR C C 177.3 . 1 217 . 48 TYR N N 113.3 . 1 218 . 49 LYS H H 8.47 . 1 219 . 49 LYS CA C 60.8 . 1 220 . 49 LYS C C 176.8 . 1 221 . 49 LYS N N 124.5 . 1 222 . 50 GLY H H 9.52 . 1 223 . 50 GLY CA C 44.9 . 1 224 . 50 GLY HA2 H 4.8 . 2 225 . 50 GLY C C 173.7 . 1 226 . 50 GLY HA3 H 4.41 . 2 227 . 50 GLY N N 116.7 . 1 228 . 51 SER H H 8.41 . 1 229 . 51 SER CA C 58.7 . 1 230 . 51 SER HA H 4.63 . 1 231 . 51 SER C C 171.1 . 1 232 . 51 SER N N 116.3 . 1 233 . 52 CYS H H 9.96 . 1 234 . 52 CYS CA C 55.6 . 1 235 . 52 CYS HA H 5.94 . 1 236 . 52 CYS C C 175.6 . 1 237 . 52 CYS N N 114.4 . 1 238 . 53 PHE H H 8.68 . 1 239 . 53 PHE CA C 57.7 . 1 240 . 53 PHE HA H 4.87 . 1 241 . 53 PHE C C 174.4 . 1 242 . 53 PHE N N 122.6 . 1 243 . 54 HIS H H 7.49 . 1 244 . 54 HIS CA C 57 . 1 245 . 54 HIS HA H 4.66 . 1 246 . 54 HIS C C 174.8 . 1 247 . 54 HIS N N 118.8 . 1 248 . 55 ARG H H 6.89 . 1 249 . 55 ARG CA C 54.6 . 1 250 . 55 ARG HA H 5.09 . 1 251 . 55 ARG C C 172.5 . 1 252 . 55 ARG N N 123.7 . 1 253 . 56 ILE H H 9.15 . 1 254 . 56 ILE CA C 61.2 . 1 255 . 56 ILE HA H 4.6 . 1 256 . 56 ILE C C 173.1 . 1 257 . 56 ILE N N 126.7 . 1 258 . 57 ILE H H 8.49 . 1 259 . 57 ILE CA C 57.2 . 1 260 . 57 ILE HA H 5.28 . 1 261 . 57 ILE N N 126.7 . 1 262 . 58 PRO CA C 62.5 . 1 263 . 58 PRO C C 177 . 1 264 . 59 GLY H H 9.83 . 1 265 . 59 GLY CA C 44.8 . 1 266 . 59 GLY HA2 H 4.04 . 1 267 . 59 GLY C C 171.5 . 1 268 . 59 GLY HA3 H 4.04 . 1 269 . 59 GLY N N 113.7 . 1 270 . 60 PHE H H 8.11 . 1 271 . 60 PHE CA C 56.1 . 1 272 . 60 PHE HA H 5.19 . 1 273 . 60 PHE C C 172 . 1 274 . 60 PHE N N 118.9 . 1 275 . 61 MET H H 7.85 . 1 276 . 61 MET CA C 54.3 . 1 277 . 61 MET HA H 5.15 . 1 278 . 61 MET C C 173.7 . 1 279 . 61 MET N N 109.6 . 1 280 . 62 CYS H H 8.32 . 1 281 . 62 CYS CA C 57.3 . 1 282 . 62 CYS HA H 4.81 . 1 283 . 62 CYS C C 172.2 . 1 284 . 62 CYS N N 112.6 . 1 285 . 63 GLN H H 9.33 . 1 286 . 63 GLN CA C 54.3 . 1 287 . 63 GLN HA H 5.13 . 1 288 . 63 GLN C C 173.5 . 1 289 . 63 GLN N N 127.1 . 1 290 . 64 GLY H H 7.47 . 1 291 . 64 GLY CA C 44.5 . 1 292 . 64 GLY C C 172.2 . 1 293 . 64 GLY N N 110 . 1 294 . 65 GLY H H 9.11 . 1 295 . 65 GLY CA C 46.4 . 1 296 . 65 GLY C C 174.8 . 1 297 . 65 GLY N N 104.8 . 1 298 . 66 ASP H H 9.99 . 1 299 . 66 ASP CA C 51.2 . 1 300 . 66 ASP HA H 4.25 . 1 301 . 66 ASP C C 175.8 . 1 302 . 66 ASP N N 123.7 . 1 303 . 67 PHE H H 6.73 . 1 304 . 67 PHE CA C 55.8 . 1 305 . 67 PHE HA H 4.61 . 1 306 . 67 PHE C C 173.5 . 1 307 . 67 PHE N N 115.5 . 1 308 . 68 THR H H 7.25 . 1 309 . 68 THR CA C 61.4 . 1 310 . 68 THR HA H 4.62 . 1 311 . 68 THR C C 175.1 . 1 312 . 68 THR N N 108.1 . 1 313 . 69 ARG H H 8.7 . 1 314 . 69 ARG CA C 54.6 . 1 315 . 69 ARG HA H 4.38 . 1 316 . 69 ARG C C 175.6 . 1 317 . 69 ARG N N 121.5 . 1 318 . 70 HIS H H 6.58 . 1 319 . 70 HIS CA C 56.8 . 1 320 . 70 HIS HA H 4.42 . 1 321 . 70 HIS C C 173.6 . 1 322 . 70 HIS N N 110.7 . 1 323 . 71 ASN H H 7.44 . 1 324 . 71 ASN CA C 52.1 . 1 325 . 71 ASN HA H 4.51 . 1 326 . 71 ASN C C 175.1 . 1 327 . 71 ASN N N 111.8 . 1 328 . 72 GLY H H 9.66 . 1 329 . 72 GLY CA C 44.8 . 1 330 . 72 GLY HA2 H 4.47 . 1 331 . 72 GLY C C 174.5 . 1 332 . 72 GLY HA3 H 4.47 . 1 333 . 72 GLY N N 110.7 . 1 334 . 73 THR H H 7.87 . 1 335 . 73 THR CA C 61.9 . 1 336 . 73 THR HA H 4.15 . 1 337 . 73 THR C C 175.6 . 1 338 . 73 THR N N 109.2 . 1 339 . 74 GLY H H 8.8 . 1 340 . 74 GLY CA C 44.8 . 1 341 . 74 GLY HA2 H 4.46 . 2 342 . 74 GLY C C 174.5 . 1 343 . 74 GLY HA3 H 3.45 . 2 344 . 74 GLY N N 113.3 . 1 345 . 75 GLY H H 8.09 . 1 346 . 75 GLY CA C 42.9 . 1 347 . 75 GLY HA2 H 4.57 . 2 348 . 75 GLY C C 171.5 . 1 349 . 75 GLY HA3 H 2.64 . 2 350 . 75 GLY N N 108.5 . 1 351 . 76 LYS H H 6.95 . 1 352 . 76 LYS CA C 55.6 . 1 353 . 76 LYS HA H 4.66 . 1 354 . 76 LYS C C 171.8 . 1 355 . 76 LYS N N 115.2 . 1 356 . 77 SER H H 7.79 . 1 357 . 77 SER CA C 56.7 . 1 358 . 77 SER HA H 5.21 . 1 359 . 77 SER C C 175.1 . 1 360 . 77 SER N N 114.1 . 1 361 . 78 ILE H H 8.57 . 1 362 . 78 ILE CA C 63.3 . 1 363 . 78 ILE HA H 4.2 . 1 364 . 78 ILE C C 175.5 . 1 365 . 78 ILE N N 110.3 . 1 366 . 79 TYR H H 8.08 . 1 367 . 79 TYR CA C 56 . 1 368 . 79 TYR HA H 4.66 . 1 369 . 79 TYR C C 174.8 . 1 370 . 79 TYR N N 120.4 . 1 371 . 80 GLY H H 7.12 . 1 372 . 80 GLY CA C 42.7 . 1 373 . 80 GLY HA2 H 4.65 . 2 374 . 80 GLY C C 173.4 . 1 375 . 80 GLY HA3 H 3.8 . 2 376 . 80 GLY N N 105.9 . 1 377 . 81 GLU H H 8.97 . 1 378 . 81 GLU CA C 60.2 . 1 379 . 81 GLU HA H 4.49 . 1 380 . 81 GLU C C 175.2 . 1 381 . 81 GLU N N 122.6 . 1 382 . 82 LYS H H 7.89 . 1 383 . 82 LYS CA C 53.5 . 1 384 . 82 LYS HA H 5.54 . 1 385 . 82 LYS C C 174.8 . 1 386 . 82 LYS N N 112.2 . 1 387 . 83 PHE H H 9.2 . 1 388 . 83 PHE CA C 55.6 . 1 389 . 83 PHE HA H 4.96 . 1 390 . 83 PHE C C 172.9 . 1 391 . 83 PHE N N 115.9 . 1 392 . 84 GLU H H 9.25 . 1 393 . 84 GLU CA C 56.2 . 1 394 . 84 GLU HA H 3.78 . 1 395 . 84 GLU C C 175.6 . 1 396 . 84 GLU N N 118.9 . 1 397 . 85 ASP H H 8.66 . 1 398 . 85 ASP CA C 54.2 . 1 399 . 85 ASP HA H 4.28 . 1 400 . 85 ASP C C 175.5 . 1 401 . 85 ASP N N 118.5 . 1 402 . 86 GLU H H 9.56 . 1 403 . 86 GLU CA C 60 . 1 404 . 86 GLU C C 175.6 . 1 405 . 86 GLU N N 131.5 . 1 406 . 87 ASN H H 7.07 . 1 407 . 87 ASN CA C 52.4 . 1 408 . 87 ASN HA H 4.12 . 1 409 . 87 ASN C C 170 . 1 410 . 87 ASN N N 106.3 . 1 411 . 88 PHE H H 8.33 . 1 412 . 88 PHE CA C 55.5 . 1 413 . 88 PHE HA H 5.96 . 1 414 . 88 PHE C C 177 . 1 415 . 88 PHE N N 112.2 . 1 416 . 89 ILE H H 8.31 . 1 417 . 89 ILE CA C 64.6 . 1 418 . 89 ILE HA H 3.74 . 1 419 . 89 ILE C C 177 . 1 420 . 89 ILE N N 119.3 . 1 421 . 90 LEU H H 7.79 . 1 422 . 90 LEU CA C 53.7 . 1 423 . 90 LEU HA H 4.45 . 1 424 . 90 LEU C C 175.6 . 1 425 . 90 LEU N N 117 . 1 426 . 91 LYS H H 8.09 . 1 427 . 91 LYS CA C 54.1 . 1 428 . 91 LYS HA H 4.6 . 1 429 . 91 LYS C C 175.6 . 1 430 . 91 LYS N N 118.5 . 1 431 . 92 HIS H H 10.58 . 1 432 . 92 HIS CA C 56.3 . 1 433 . 92 HIS HA H 4.34 . 1 434 . 92 HIS C C 177 . 1 435 . 92 HIS N N 121.9 . 1 436 . 93 THR H H 7.24 . 1 437 . 93 THR CA C 62.9 . 1 438 . 93 THR HA H 4 . 1 439 . 93 THR C C 174.8 . 1 440 . 93 THR N N 109.6 . 1 441 . 94 GLY H H 7.54 . 1 442 . 94 GLY CA C 45.3 . 1 443 . 94 GLY HA2 H 4.75 . 2 444 . 94 GLY HA3 H 4.44 . 2 445 . 94 GLY N N 106.6 . 1 446 . 95 PRO CA C 62.4 . 1 447 . 95 PRO C C 176.4 . 1 448 . 96 GLY H H 9.24 . 1 449 . 96 GLY CA C 44.7 . 1 450 . 96 GLY HA2 H 4.6 . 2 451 . 96 GLY C C 172.5 . 1 452 . 96 GLY HA3 H 3.35 . 2 453 . 96 GLY N N 110.3 . 1 454 . 97 ILE H H 6.78 . 1 455 . 97 ILE CA C 59.2 . 1 456 . 97 ILE HA H 4.02 . 1 457 . 97 ILE C C 172.1 . 1 458 . 97 ILE N N 120.7 . 1 459 . 98 LEU H H 7.82 . 1 460 . 98 LEU CA C 53 . 1 461 . 98 LEU HA H 4.81 . 1 462 . 98 LEU C C 173 . 1 463 . 98 LEU N N 129.3 . 1 464 . 99 SER H H 7.96 . 1 465 . 99 SER CA C 54.1 . 1 466 . 99 SER HA H 5.21 . 1 467 . 99 SER C C 173.4 . 1 468 . 99 SER N N 118.9 . 1 469 . 100 MET H H 8.29 . 1 470 . 100 MET CA C 53.5 . 1 471 . 100 MET HA H 5.51 . 1 472 . 100 MET C C 178.4 . 1 473 . 100 MET N N 122.6 . 1 474 . 101 ALA H H 8.23 . 1 475 . 101 ALA CA C 51.4 . 1 476 . 101 ALA HA H 4.72 . 1 477 . 101 ALA C C 174.5 . 1 478 . 101 ALA N N 126.3 . 1 479 . 102 ASN H H 7.7 . 1 480 . 102 ASN CA C 53.4 . 1 481 . 102 ASN HA H 4.71 . 1 482 . 102 ASN C C 172.3 . 1 483 . 102 ASN N N 113.3 . 1 484 . 103 ALA H H 9.26 . 1 485 . 103 ALA CA C 50.1 . 1 486 . 103 ALA HA H 4.73 . 1 487 . 103 ALA C C 175.9 . 1 488 . 103 ALA N N 120.7 . 1 489 . 104 GLY H H 8.24 . 1 490 . 104 GLY CA C 43.1 . 1 491 . 104 GLY HA2 H 4.68 . 2 492 . 104 GLY HA3 H 3.72 . 2 493 . 104 GLY N N 107.7 . 1 494 . 105 PRO CA C 63.7 . 1 495 . 105 PRO C C 175.5 . 1 496 . 106 ASN H H 8.86 . 1 497 . 106 ASN CA C 54 . 1 498 . 106 ASN HA H 4.11 . 1 499 . 106 ASN C C 174.4 . 1 500 . 106 ASN N N 118.9 . 1 501 . 107 THR H H 10.31 . 1 502 . 107 THR CA C 59.9 . 1 503 . 107 THR HA H 4.44 . 1 504 . 107 THR C C 172.9 . 1 505 . 107 THR N N 110 . 1 506 . 108 ASN H H 7.43 . 1 507 . 108 ASN CA C 55.5 . 1 508 . 108 ASN HA H 4.2 . 1 509 . 108 ASN C C 173.4 . 1 510 . 108 ASN N N 120 . 1 511 . 109 GLY H H 9.15 . 1 512 . 109 GLY CA C 45.5 . 1 513 . 109 GLY HA2 H 4.62 . 1 514 . 109 GLY C C 170.4 . 1 515 . 109 GLY HA3 H 4.62 . 1 516 . 109 GLY N N 110.3 . 1 517 . 110 SER H H 8.77 . 1 518 . 110 SER CA C 57.1 . 1 519 . 110 SER HA H 4.78 . 1 520 . 110 SER C C 175.3 . 1 521 . 110 SER N N 116.7 . 1 522 . 111 GLN H H 8.42 . 1 523 . 111 GLN CA C 57.9 . 1 524 . 111 GLN HA H 4.29 . 1 525 . 111 GLN C C 175.5 . 1 526 . 111 GLN N N 124.5 . 1 527 . 112 PHE H H 8.17 . 1 528 . 112 PHE CA C 55 . 1 529 . 112 PHE HA H 6.05 . 1 530 . 112 PHE C C 171.4 . 1 531 . 112 PHE N N 117 . 1 532 . 113 PHE H H 9.83 . 1 533 . 113 PHE CA C 54.7 . 1 534 . 113 PHE HA H 5.85 . 1 535 . 113 PHE C C 172.1 . 1 536 . 113 PHE N N 114.4 . 1 537 . 114 ILE H H 9.03 . 1 538 . 114 ILE CA C 58.7 . 1 539 . 114 ILE HA H 4.86 . 1 540 . 114 ILE C C 176.7 . 1 541 . 114 ILE N N 117 . 1 542 . 115 CYS H H 9.5 . 1 543 . 115 CYS CA C 61.1 . 1 544 . 115 CYS HA H 4.58 . 1 545 . 115 CYS C C 175.9 . 1 546 . 115 CYS N N 124.1 . 1 547 . 116 THR H H 9.05 . 1 548 . 116 THR CA C 60.3 . 1 549 . 116 THR HA H 4.4 . 1 550 . 116 THR C C 171.9 . 1 551 . 116 THR N N 115.2 . 1 552 . 117 ALA H H 7.62 . 1 553 . 117 ALA CA C 50.4 . 1 554 . 117 ALA HA H 4.37 . 1 555 . 117 ALA C C 174.5 . 1 556 . 117 ALA N N 121.9 . 1 557 . 118 LYS H H 8.73 . 1 558 . 118 LYS CA C 57.3 . 1 559 . 118 LYS HA H 3.79 . 1 560 . 118 LYS C C 175.6 . 1 561 . 118 LYS N N 119.3 . 1 562 . 119 THR H H 7.38 . 1 563 . 119 THR CA C 56.7 . 1 564 . 119 THR HA H 3.55 . 1 565 . 119 THR C C 174.5 . 1 566 . 119 THR N N 117.4 . 1 567 . 120 GLU H H 9.09 . 1 568 . 120 GLU CA C 59 . 1 569 . 120 GLU HA H 5.19 . 1 570 . 120 GLU C C 176.6 . 1 571 . 120 GLU N N 124.1 . 1 572 . 121 TRP H H 7.31 . 1 573 . 121 TRP CA C 59.7 . 1 574 . 121 TRP HA H 4.72 . 1 575 . 121 TRP C C 175.5 . 1 576 . 121 TRP N N 117.8 . 1 577 . 122 LEU H H 7.06 . 1 578 . 122 LEU CA C 54 . 1 579 . 122 LEU HA H 4.32 . 1 580 . 122 LEU C C 176.5 . 1 581 . 122 LEU N N 120.4 . 1 582 . 123 ASP H H 7.59 . 1 583 . 123 ASP CA C 55.4 . 1 584 . 123 ASP HA H 5.18 . 1 585 . 123 ASP C C 177.5 . 1 586 . 123 ASP N N 121.9 . 1 587 . 124 GLY H H 9.58 . 1 588 . 124 GLY CA C 44.7 . 1 589 . 124 GLY C C 171.5 . 1 590 . 124 GLY N N 110.7 . 1 591 . 125 LYS H H 7.59 . 1 592 . 125 LYS CA C 55.9 . 1 593 . 125 LYS HA H 4.06 . 1 594 . 125 LYS C C 174.4 . 1 595 . 125 LYS N N 114.1 . 1 596 . 126 HIS H H 7.44 . 1 597 . 126 HIS CA C 54.7 . 1 598 . 126 HIS HA H 4.8 . 1 599 . 126 HIS C C 173.2 . 1 600 . 126 HIS N N 120 . 1 601 . 127 VAL H H 8.25 . 1 602 . 127 VAL CA C 63.4 . 1 603 . 127 VAL HA H 4.24 . 1 604 . 127 VAL C C 174.1 . 1 605 . 127 VAL N N 124.1 . 1 606 . 128 VAL H H 9.45 . 1 607 . 128 VAL CA C 62.9 . 1 608 . 128 VAL HA H 3.98 . 1 609 . 128 VAL C C 174.4 . 1 610 . 128 VAL N N 132.6 . 1 611 . 129 PHE H H 8.12 . 1 612 . 129 PHE CA C 55.6 . 1 613 . 129 PHE HA H 5.24 . 1 614 . 129 PHE C C 172.1 . 1 615 . 129 PHE N N 116.7 . 1 616 . 130 GLY H H 7.37 . 1 617 . 130 GLY CA C 46.2 . 1 618 . 130 GLY HA2 H 3.08 . 1 619 . 130 GLY C C 170.1 . 1 620 . 130 GLY HA3 H 3.08 . 1 621 . 130 GLY N N 110 . 1 622 . 131 LYS H H 8.3 . 1 623 . 131 LYS CA C 54.5 . 1 624 . 131 LYS HA H 5.16 . 1 625 . 131 LYS C C 174.4 . 1 626 . 131 LYS N N 114.4 . 1 627 . 132 VAL H H 9.01 . 1 628 . 132 VAL CA C 63.7 . 1 629 . 132 VAL C C 174.8 . 1 630 . 132 VAL N N 123.3 . 1 631 . 133 LYS H H 9.45 . 1 632 . 133 LYS CA C 56.4 . 1 633 . 133 LYS HA H 4.42 . 1 634 . 133 LYS C C 174.8 . 1 635 . 133 LYS N N 131.1 . 1 636 . 134 GLU H H 7.54 . 1 637 . 134 GLU CA C 55 . 1 638 . 134 GLU HA H 4.55 . 1 639 . 134 GLU C C 174.3 . 1 640 . 134 GLU N N 117.7 . 1 641 . 135 GLY H H 8.7 . 1 642 . 135 GLY CA C 46.1 . 1 643 . 135 GLY HA2 H 4.8 . 2 644 . 135 GLY C C 176.5 . 1 645 . 135 GLY HA3 H 3.97 . 2 646 . 135 GLY N N 107.4 . 1 647 . 136 MET H H 8.88 . 1 648 . 136 MET CA C 56.5 . 1 649 . 136 MET HA H 4.46 . 1 650 . 136 MET C C 177 . 1 651 . 136 MET N N 122.9 . 1 652 . 137 ASN H H 8.92 . 1 653 . 137 ASN CA C 55.7 . 1 654 . 137 ASN HA H 4.44 . 1 655 . 137 ASN C C 176.8 . 1 656 . 137 ASN N N 113.7 . 1 657 . 138 ILE H H 7.65 . 1 658 . 138 ILE CA C 61.1 . 1 659 . 138 ILE HA H 3.75 . 1 660 . 138 ILE C C 177 . 1 661 . 138 ILE N N 123.7 . 1 662 . 139 VAL H H 7.28 . 1 663 . 139 VAL CA C 65.7 . 1 664 . 139 VAL HA H 3.86 . 1 665 . 139 VAL C C 177.4 . 1 666 . 139 VAL N N 121.5 . 1 667 . 140 GLU H H 8.31 . 1 668 . 140 GLU CA C 58.9 . 1 669 . 140 GLU HA H 4.67 . 1 670 . 140 GLU C C 178.7 . 1 671 . 140 GLU N N 117.4 . 1 672 . 141 ALA H H 7.51 . 1 673 . 141 ALA CA C 54.5 . 1 674 . 141 ALA HA H 4.09 . 1 675 . 141 ALA C C 179.9 . 1 676 . 141 ALA N N 120.7 . 1 677 . 142 MET H H 8.31 . 1 678 . 142 MET CA C 59.3 . 1 679 . 142 MET HA H 3.96 . 1 680 . 142 MET C C 177.2 . 1 681 . 142 MET N N 116.6 . 1 682 . 143 GLU H H 7.89 . 1 683 . 143 GLU CA C 58.7 . 1 684 . 143 GLU HA H 3.74 . 1 685 . 143 GLU C C 177.3 . 1 686 . 143 GLU N N 115.9 . 1 687 . 144 ARG H H 7.01 . 1 688 . 144 ARG CA C 57.3 . 1 689 . 144 ARG HA H 3.92 . 1 690 . 144 ARG C C 176.6 . 1 691 . 144 ARG N N 114.1 . 1 692 . 145 PHE H H 7.63 . 1 693 . 145 PHE CA C 57.7 . 1 694 . 145 PHE HA H 4.79 . 1 695 . 145 PHE C C 175.2 . 1 696 . 145 PHE N N 114.8 . 1 697 . 146 GLY H H 7.57 . 1 698 . 146 GLY CA C 43.7 . 1 699 . 146 GLY HA2 H 4.59 . 2 700 . 146 GLY C C 171.2 . 1 701 . 146 GLY HA3 H 3.61 . 2 702 . 146 GLY N N 104.4 . 1 703 . 147 SER H H 8.21 . 1 704 . 147 SER CA C 57.8 . 1 705 . 147 SER HA H 4.8 . 1 706 . 147 SER C C 174.8 . 1 707 . 147 SER N N 109.2 . 1 708 . 148 ARG H H 8.93 . 1 709 . 148 ARG CA C 59.4 . 1 710 . 148 ARG C C 176.2 . 1 711 . 148 ARG N N 120 . 1 712 . 149 ASN H H 7.87 . 1 713 . 149 ASN CA C 52.1 . 1 714 . 149 ASN HA H 4.83 . 1 715 . 149 ASN C C 176.2 . 1 716 . 149 ASN N N 110.7 . 1 717 . 150 GLY H H 8.07 . 1 718 . 150 GLY CA C 44.6 . 1 719 . 150 GLY HA2 H 4 . 2 720 . 150 GLY C C 172.7 . 1 721 . 150 GLY HA3 H 4.17 . 2 722 . 150 GLY N N 110.3 . 1 723 . 151 LYS H H 7.56 . 1 724 . 151 LYS CA C 56.8 . 1 725 . 151 LYS HA H 4.4 . 1 726 . 151 LYS C C 178 . 1 727 . 151 LYS N N 119.3 . 1 728 . 152 THR H H 8.88 . 1 729 . 152 THR CA C 59.5 . 1 730 . 152 THR HA H 5.57 . 1 731 . 152 THR C C 175.4 . 1 732 . 152 THR N N 116.7 . 1 733 . 153 SER H H 9.47 . 1 734 . 153 SER CA C 58.7 . 1 735 . 153 SER HA H 4.42 . 1 736 . 153 SER C C 174 . 1 737 . 153 SER N N 117.4 . 1 738 . 154 LYS H H 7.54 . 1 739 . 154 LYS CA C 54.3 . 1 740 . 154 LYS HA H 4.53 . 1 741 . 154 LYS C C 173.8 . 1 742 . 154 LYS N N 118.5 . 1 743 . 155 LYS H H 8.8 . 1 744 . 155 LYS CA C 56.2 . 1 745 . 155 LYS HA H 4.3 . 1 746 . 155 LYS C C 175.5 . 1 747 . 155 LYS N N 121.1 . 1 748 . 156 ILE H H 9.63 . 1 749 . 156 ILE CA C 58.8 . 1 750 . 156 ILE HA H 5.08 . 1 751 . 156 ILE C C 175.8 . 1 752 . 156 ILE N N 133.7 . 1 753 . 157 THR H H 9.23 . 1 754 . 157 THR CA C 59.1 . 1 755 . 157 THR HA H 5.3 . 1 756 . 157 THR C C 173 . 1 757 . 157 THR N N 117 . 1 758 . 158 ILE H H 8.58 . 1 759 . 158 ILE CA C 60.5 . 1 760 . 158 ILE HA H 4.22 . 1 761 . 158 ILE C C 174 . 1 762 . 158 ILE N N 121.1 . 1 763 . 159 ALA H H 8.86 . 1 764 . 159 ALA CA C 53.9 . 1 765 . 159 ALA HA H 4.12 . 1 766 . 159 ALA C C 177.9 . 1 767 . 159 ALA N N 131.9 . 1 768 . 160 ASP H H 8.06 . 1 769 . 160 ASP CA C 52.4 . 1 770 . 160 ASP HA H 4.87 . 1 771 . 160 ASP C C 172.2 . 1 772 . 160 ASP N N 110.7 . 1 773 . 161 CYS H H 8.59 . 1 774 . 161 CYS CA C 55 . 1 775 . 161 CYS HA H 4.53 . 1 776 . 161 CYS C C 171.9 . 1 777 . 161 CYS N N 115.5 . 1 778 . 162 GLY H H 6.85 . 1 779 . 162 GLY CA C 45.1 . 1 780 . 162 GLY HA2 H 3.51 . 1 781 . 162 GLY C C 169.6 . 1 782 . 162 GLY HA3 H 3.51 . 1 783 . 162 GLY N N 104 . 1 784 . 163 GLN H H 9.09 . 1 785 . 163 GLN CA C 54.8 . 1 786 . 163 GLN HA H 5.05 . 1 787 . 163 GLN C C 174.8 . 1 788 . 163 GLN N N 120.4 . 1 789 . 164 LEU H H 8.59 . 1 790 . 164 LEU CA C 54.5 . 1 791 . 164 LEU HA H 4.62 . 1 792 . 164 LEU C C 175.5 . 1 793 . 164 LEU N N 125.6 . 1 794 . 165 GLU H H 8.15 . 1 795 . 165 GLU CA C 57.8 . 1 796 . 165 GLU HA H 4.15 . 1 797 . 165 GLU N N 125.6 . 1 stop_ save_