data_531 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A ; _BMRB_accession_number 531 _BMRB_flat_file_name bmr531.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Heald S. L. . 2 Harding Matthew W. . 3 Handschumacher R. E. . 4 Armitage Ian M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 10 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 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 ; Heald, S.L., Harding, Matthew W., Handschumacher, R.E., Armitage, Ian M., "1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A," Biochemistry 29, 4466-4478 (1990). ; _Citation_title ; 1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A ; _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 Heald S. L. . 2 Harding Matthew W. . 3 Handschumacher R. E. . 4 Armitage Ian M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4466 _Page_last 4478 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_peptidylprolyl_isomerase _Saveframe_category molecular_system _Mol_system_name 'peptidylprolyl isomerase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'peptidylprolyl isomerase' $peptidylprolyl_isomerase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_peptidylprolyl_isomerase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'peptidylprolyl isomerase' _Name_variant 'major isoform (non N-acetylated)' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 163 _Mol_residue_sequence ; VNPTVFFDIAVDGEPLGRVS FELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFM CQGGDFTRHNGTGGKSIYGE KFDDENFILKHTGPGILSMA NAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEA MERFGSRNGKTSKKITIADC GQI ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 ASN 3 PRO 4 THR 5 VAL 6 PHE 7 PHE 8 ASP 9 ILE 10 ALA 11 VAL 12 ASP 13 GLY 14 GLU 15 PRO 16 LEU 17 GLY 18 ARG 19 VAL 20 SER 21 PHE 22 GLU 23 LEU 24 PHE 25 ALA 26 ASP 27 LYS 28 VAL 29 PRO 30 LYS 31 THR 32 ALA 33 GLU 34 ASN 35 PHE 36 ARG 37 ALA 38 LEU 39 SER 40 THR 41 GLY 42 GLU 43 LYS 44 GLY 45 PHE 46 GLY 47 TYR 48 LYS 49 GLY 50 SER 51 CYS 52 PHE 53 HIS 54 ARG 55 ILE 56 ILE 57 PRO 58 GLY 59 PHE 60 MET 61 CYS 62 GLN 63 GLY 64 GLY 65 ASP 66 PHE 67 THR 68 ARG 69 HIS 70 ASN 71 GLY 72 THR 73 GLY 74 GLY 75 LYS 76 SER 77 ILE 78 TYR 79 GLY 80 GLU 81 LYS 82 PHE 83 ASP 84 ASP 85 GLU 86 ASN 87 PHE 88 ILE 89 LEU 90 LYS 91 HIS 92 THR 93 GLY 94 PRO 95 GLY 96 ILE 97 LEU 98 SER 99 MET 100 ALA 101 ASN 102 ALA 103 GLY 104 PRO 105 ASN 106 THR 107 ASN 108 GLY 109 SER 110 GLN 111 PHE 112 PHE 113 ILE 114 CYS 115 THR 116 ALA 117 LYS 118 THR 119 GLU 120 TRP 121 LEU 122 ASP 123 GLY 124 LYS 125 HIS 126 VAL 127 VAL 128 PHE 129 GLY 130 LYS 131 VAL 132 LYS 133 GLU 134 GLY 135 MET 136 ASN 137 ILE 138 VAL 139 GLU 140 ALA 141 MET 142 GLU 143 ARG 144 PHE 145 GLY 146 SER 147 ARG 148 ASN 149 GLY 150 LYS 151 THR 152 SER 153 LYS 154 LYS 155 ILE 156 THR 157 ILE 158 ALA 159 ASP 160 CYS 161 GLY 162 GLN 163 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 100.00 164 98.77 100.00 1.10e-113 BMRB 17461 CypA 100.00 165 98.77 100.00 6.73e-114 BMRB 2208 cyclophilin 100.00 165 98.77 100.00 6.73e-114 BMRB 25337 CypA 100.00 165 98.77 100.00 6.73e-114 BMRB 532 "peptidylprolyl isomerase" 100.00 163 100.00 100.00 1.32e-114 PDB 1AK4 "Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid" 100.00 165 98.77 100.00 6.73e-114 PDB 1AWQ "Cypa Complexed With Hagpia (Pseudo-Symmetric Monomer)" 100.00 164 98.77 100.00 1.10e-113 PDB 1AWR "Cypa Complexed With Hagpia" 100.00 164 98.77 100.00 1.10e-113 PDB 1AWU "Cypa Complexed With Hvgpia (Pseudo-Symmetric Monomer)" 100.00 164 98.77 100.00 1.10e-113 PDB 1AWV "Cypa Complexed With Hvgpia" 100.00 164 98.77 100.00 1.10e-113 PDB 1BCK "Human Cyclophilin A Complexed With 2-Thr Cyclosporin" 100.00 165 98.77 100.00 1.14e-113 PDB 1CWA "X-Ray Structure Of A Monomeric Cyclophilin A-Cyclosporin A Crystal Complex At 2.1 Angstroms Resolution" 100.00 165 98.77 100.00 6.73e-114 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 98.77 100.00 6.73e-114 PDB 1CWC "Improved Binding Affinity For Cyclophilin A By A Cyclosporin Derivative Singly Modified At Its Effector Domain" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWF "Human Cyclophilin A Complexed With 2-Val Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWH "Human Cyclophilin A Complexed With 3-D-Ser Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWI "Human Cyclophilin A Complexed With 2-Val 3-(N-Methyl)-D-Alanine Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWJ "Human Cyclophilin A Complexed With 2-Val 3-S-Methyl-Sarcosine Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWK "Human Cyclophilin A Complexed With 1-(6,7-Dihydro)mebmt 2-Val 3-D-(2- S-Methyl)sarcosine Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWL "Human Cyclophilin A Complexed With 4 4-Hydroxy-Meleu Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWM "Human Cyclophilin A Complexed With 4 Meile Cyclosporin" 100.00 165 98.77 100.00 6.73e-114 PDB 1CWO "Human Cyclophilin A Complexed With Thr2, Leu5, D-Hiv8, Leu10 Cyclosporin" 100.00 165 98.77 100.00 1.14e-113 PDB 1FGL "Cyclophilin A Complexed With A Fragment Of Hiv-1 Gag Protein" 100.00 165 98.77 100.00 6.73e-114 PDB 1M63 "Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition Of Immunophilin-Drug Complexes" 100.00 165 98.77 100.00 6.73e-114 PDB 1M9C "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex." 100.00 165 98.77 100.00 6.73e-114 PDB 1M9D "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) O-Type Chimera Complex." 100.00 165 98.77 100.00 6.73e-114 PDB 1M9E "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex" 100.00 164 98.77 100.00 7.58e-114 PDB 1M9F "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex." 100.00 165 98.77 100.00 6.73e-114 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 98.77 100.00 6.73e-114 PDB 1M9Y "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex." 100.00 165 98.77 100.00 6.73e-114 PDB 1MF8 "Crystal Structure Of Human Calcineurin Complexed With Cyclosporin A And Human Cyclophilin" 100.00 165 98.77 100.00 6.73e-114 PDB 1MIK "The Role Of Water Molecules In The Structure-Based Design Of (5- Hydroxynorvaline)-2-Cyclosporin: Synthesis, Biological Activit" 100.00 165 98.77 100.00 6.73e-114 PDB 1NMK "The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-Ray Crystal Structure And Bindin" 100.00 165 98.77 100.00 6.73e-114 PDB 1OCA "Human Cyclophilin A, Unligated, Nmr, 20 Structures" 100.00 165 98.77 100.00 6.73e-114 PDB 1RMH "Recombinant Cyclophilin A From Human T Cell" 100.00 164 98.77 100.00 1.10e-113 PDB 1VBS "Structure Of Cyclophilin Complexed With (D)ala Containing Tetrapeptide" 100.00 165 98.77 100.00 6.73e-114 PDB 1VBT "Structure Of Cyclophilin Complexed With Sulfur-Substituted Tetrapeptide Aapf" 100.00 165 98.77 100.00 6.73e-114 PDB 1W8L "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 98.77 100.00 6.73e-114 PDB 1W8M "Enzymatic And Structural Characterisation Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 98.77 100.00 6.73e-114 PDB 1W8V "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" 100.00 165 98.77 100.00 6.73e-114 PDB 1YND "Structure Of Human Cyclophilin A In Complex With The Novel Immunosuppressant Sanglifehrin A At 1.6a Resolution" 100.00 165 98.77 100.00 6.73e-114 PDB 1ZKF "Cyrstal Structure Of Human Cyclophilin-A In Complex With Suc-Agpf-Pna" 100.00 165 98.77 100.00 6.73e-114 PDB 2ALF "Crystal Structure Of Human Cypa Mutant K131a" 100.00 164 97.55 99.39 2.82e-112 PDB 2CPL "Similarities And Differences Between Human Cyclophilin A And Other Beta-Barrel Structures. Structural Refinement At 1.63 Angstr" 100.00 165 98.77 100.00 6.73e-114 PDB 2CYH "Cyclophilin A Complexed With Dipeptide Ala-Pro" 100.00 164 98.77 100.00 1.10e-113 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 98.77 100.00 6.73e-114 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 98.77 100.00 6.73e-114 PDB 2WLW "Structure Of The N-Terminal Capsid Domain Of Hiv-2" 100.00 165 97.55 99.39 3.64e-112 PDB 2X25 "Free Acetyl-Cypa Orthorhombic Form" 100.00 169 97.55 99.39 3.70e-112 PDB 2X2A "Free Acetyl-Cypa Trigonal Form" 100.00 165 97.55 99.39 2.20e-112 PDB 2X2C "Acetyl-Cypa:cyclosporine Complex" 100.00 165 98.16 99.39 5.43e-113 PDB 2X2D "Acetyl-Cypa:hiv-1 N-Term Capsid Domain Complex" 100.00 165 98.16 99.39 5.43e-113 PDB 2X83 "Evolutionary Basis Of Hiv Restriction By The Antiretroviral Trimcyp" 100.00 163 97.55 99.39 4.09e-112 PDB 2XGY "Complex Of Rabbit Endogenous Lentivirus (Relik)capsid With Cyclophilin A" 100.00 173 98.77 100.00 1.88e-113 PDB 3CYH "Cyclophilin A Complexed With Dipeptide Ser-Pro" 100.00 164 98.77 100.00 1.10e-113 PDB 3CYS "Determination Of The Nmr Solution Structure Of The Cyclophilin A- Cyclosporin A Complex" 100.00 165 98.77 100.00 6.73e-114 PDB 3K0M "Cryogenic Structure Of Cypa" 100.00 165 98.77 100.00 6.73e-114 PDB 3K0N "Room Temperature Structure Of Cypa" 100.00 165 98.77 100.00 6.73e-114 PDB 3K0O "Room Temperature Structure Of Cypa Mutant Ser99thr" 100.00 165 98.16 100.00 1.76e-113 PDB 3K0P "Cryogenic Structure Of Cypa Mutant Ser99thr" 100.00 165 98.16 100.00 1.76e-113 PDB 3K0Q "Cryogenic Structure Of Cypa Mutant Ser99thr (2)" 100.00 165 98.16 100.00 1.76e-113 PDB 3K0R "Cryogenic Structure Of Cypa Mutant Arg55lys" 100.00 165 98.16 100.00 2.47e-113 PDB 3ODI "Crystal Structure Of Cyclophilin A In Complex With Voclosporin E- Isa247" 100.00 165 98.77 100.00 6.73e-114 PDB 3ODL "Crystal Structure Of Cyclophilin A In Complex With Voclosporin Z- Isa247" 100.00 165 98.77 100.00 6.73e-114 PDB 3RDD "Human Cyclophilin A Complexed With An Inhibitor" 100.00 184 98.77 100.00 1.16e-113 PDB 4CYH "Cyclophilin A Complexed With Dipeptide His-Pro" 100.00 164 98.77 100.00 1.10e-113 PDB 4DGA "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-1 Ca(O-Loop) Complex" 100.00 165 97.55 99.39 3.64e-112 PDB 4DGB "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-2 Ca Cyclophilin- Binding Loop Complex" 100.00 165 97.55 99.39 3.64e-112 PDB 4DGC "Trimcyp Cyclophilin Domain From Macaca Mulatta: Cyclosporin A Complex" 100.00 165 97.55 99.39 3.64e-112 PDB 4DGD "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant" 100.00 165 96.93 98.77 1.68e-110 PDB 4DGE "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant, Hiv-1 Ca(O-Loop) Complex" 100.00 165 96.93 98.77 1.68e-110 PDB 4IPZ "Smbz Bound To Cyclophilin A" 100.00 165 98.77 100.00 6.73e-114 PDB 5CYH "Cyclophilin A Complexed With Dipeptide Gly-Pro" 100.00 164 98.77 100.00 1.10e-113 DBJ BAE01146 "unnamed protein product [Macaca fascicularis]" 63.80 105 97.12 100.00 5.37e-67 DBJ BAE87660 "unnamed protein product [Macaca fascicularis]" 100.00 165 98.77 100.00 6.73e-114 DBJ BAF82774 "unnamed protein product [Homo sapiens]" 100.00 165 98.77 100.00 6.73e-114 DBJ BAF83540 "unnamed protein product [Homo sapiens]" 100.00 165 98.16 100.00 2.58e-113 DBJ BAF85692 "unnamed protein product [Homo sapiens]" 63.80 105 98.08 100.00 1.08e-67 EMBL CAA37039 "peptidylprolyl isomerase [Homo sapiens]" 100.00 165 98.77 100.00 6.73e-114 EMBL CAA68264 "unnamed protein product [Homo sapiens]" 100.00 165 98.77 100.00 6.73e-114 EMBL CAG32988 "PPIA [Homo sapiens]" 100.00 165 98.77 100.00 9.04e-114 EMBL CAH91833 "hypothetical protein [Pongo abelii]" 100.00 165 98.16 99.39 3.11e-113 EMBL CAZ64804 "peptidylprolyl isomerase A (cyclophilin A) [Sus scrofa]" 100.00 164 100.00 100.00 1.18e-114 GB AAB81959 "cyclophilin A [Papio hamadryas]" 100.00 165 98.77 100.00 6.73e-114 GB AAB81960 "cyclophilin A [Chlorocebus aethiops]" 100.00 165 98.77 100.00 6.73e-114 GB AAB81961 "cyclophilin A [Macaca mulatta]" 100.00 165 98.77 100.00 6.73e-114 GB AAF69142 "cyclophilin I [Bos taurus]" 57.06 94 100.00 100.00 8.89e-60 GB AAF78600 "cyclophilin A [Canis lupus familiaris]" 95.71 156 100.00 100.00 3.88e-109 PRF 1503232A "peptidyl-Pro cis trans isomerase" 100.00 164 100.00 100.00 1.18e-114 REF NP_001009370 "peptidyl-prolyl cis-trans isomerase A [Felis catus]" 100.00 164 98.16 98.77 2.06e-112 REF NP_001027981 "peptidyl-prolyl cis-trans isomerase A [Macaca mulatta]" 100.00 165 98.77 100.00 6.73e-114 REF NP_001126060 "peptidyl-prolyl cis-trans isomerase A [Pongo abelii]" 100.00 165 98.16 99.39 3.11e-113 REF NP_001270275 "uncharacterized protein LOC101866023 [Macaca fascicularis]" 63.80 105 97.12 100.00 5.37e-67 REF NP_001271703 "uncharacterized protein LOC101925040 [Macaca fascicularis]" 100.00 165 98.77 100.00 6.73e-114 SP P62935 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 100.00 164 100.00 100.00 1.18e-114 SP P62936 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 100.00 164 100.00 100.00 1.18e-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 98.77 100.00 6.73e-114 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 98.77 100.00 6.73e-114 SP P62940 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" 100.00 165 98.77 100.00 6.73e-114 TPG DAA25853 "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" 100.00 164 98.77 98.77 3.43e-113 TPG DAA25854 "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" 100.00 164 98.77 98.77 3.43e-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 _Tissue $peptidylprolyl_isomerase cow 9909 Eukaryota Metazoa Bos primigenius generic thymus 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 $peptidylprolyl_isomerase 'not available' . . . . . 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 6.8 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details 'The chemical shift reference is not available at this time.' 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 'peptidylprolyl isomerase' _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 . 120 TRP H H 7.3 . 1 2 . 120 TRP HA H 4.72 . 1 3 . 120 TRP HB2 H 3.42 . 2 4 . 120 TRP HB3 H 3.38 . 2 5 . 120 TRP HD1 H 7.06 . 1 6 . 120 TRP HE1 H 9.83 . 1 7 . 120 TRP HE3 H 6.68 . 1 8 . 120 TRP HZ2 H 7.71 . 1 9 . 120 TRP HZ3 H 7.16 . 1 10 . 120 TRP HH2 H 7.38 . 1 stop_ save_