data_19240 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human FKBP12-Major Form ; _BMRB_accession_number 19240 _BMRB_flat_file_name bmr19240.str _Entry_type original _Submission_date 2013-05-14 _Accession_date 2013-05-14 _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 Mustafi Sourajit Mitra . 2 Chen Hui . . 3 Li Hongmin . . 4 LeMaster David M. . 5 Hernandez Griselda . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 627 "13C chemical shifts" 479 "15N chemical shifts" 105 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-06 update author 'update assignments' 2013-07-15 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16931 'Partial list of chemical shifts for Human FKBP12' 19241 'Analyzing the visible conformational substates of the FK506-binding protein FKBP12' 19323 'Human FKBP12.6-major form' 19324 'Human FKBP12.6-Minor Form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Analyzing the visible conformational substates of the FK506-binding protein FKBP12.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23688288 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mustafi Sourajit M. . 2 Chen Hui . . 3 Li Hongmin . . 4 Lemaster David M. . 5 Hernandez Griselda . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume 453 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 371 _Page_last 380 _Year 2013 _Details . loop_ _Keyword 'conformational dynamics' FKBP12 NMR 'slow exchange' 'X-ray structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FKBP12 _Enzyme_commission_number 5.2.1.8 loop_ _Mol_system_component_name _Mol_label FKBP12 $FKBP12 stop_ _System_molecular_weight 11819.5 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FKBP12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FKBP12 _Molecular_mass 11819.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'Immunophilin,Ryanodine binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; GVQVETISPGDGRTFPKRGQ TCVVHYTGMLEDGKKFDSSR DRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFD VELLKLE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 VAL 3 GLN 4 VAL 5 GLU 6 THR 7 ILE 8 SER 9 PRO 10 GLY 11 ASP 12 GLY 13 ARG 14 THR 15 PHE 16 PRO 17 LYS 18 ARG 19 GLY 20 GLN 21 THR 22 CYS 23 VAL 24 VAL 25 HIS 26 TYR 27 THR 28 GLY 29 MET 30 LEU 31 GLU 32 ASP 33 GLY 34 LYS 35 LYS 36 PHE 37 ASP 38 SER 39 SER 40 ARG 41 ASP 42 ARG 43 ASN 44 LYS 45 PRO 46 PHE 47 LYS 48 PHE 49 MET 50 LEU 51 GLY 52 LYS 53 GLN 54 GLU 55 VAL 56 ILE 57 ARG 58 GLY 59 TRP 60 GLU 61 GLU 62 GLY 63 VAL 64 ALA 65 GLN 66 MET 67 SER 68 VAL 69 GLY 70 GLN 71 ARG 72 ALA 73 LYS 74 LEU 75 THR 76 ILE 77 SER 78 PRO 79 ASP 80 TYR 81 ALA 82 TYR 83 GLY 84 ALA 85 THR 86 GLY 87 HIS 88 PRO 89 GLY 90 ILE 91 ILE 92 PRO 93 PRO 94 HIS 95 ALA 96 THR 97 LEU 98 VAL 99 PHE 100 ASP 101 VAL 102 GLU 103 LEU 104 LEU 105 LYS 106 LEU 107 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 11471 entity_1 100.00 107 100.00 100.00 3.18e-72 BMRB 16925 FKBP12 100.00 107 100.00 100.00 3.18e-72 BMRB 16931 FKBP12 100.00 107 100.00 100.00 3.18e-72 BMRB 16933 FKBP12 100.00 107 100.00 100.00 3.18e-72 BMRB 19241 FKBP12 100.00 107 100.00 100.00 3.18e-72 PDB 1A7X "Fkbp12-Fk1012 Complex" 100.00 107 100.00 100.00 3.18e-72 PDB 1B6C "Crystal Structure Of The Cytoplasmic Domain Of The Type I Tgf-Beta Receptor In Complex With Fkbp12" 100.00 107 100.00 100.00 3.18e-72 PDB 1BKF "Fk506 Binding Protein Fkbp Mutant R42kH87V COMPLEX WITH Immunosuppressant Fk506" 100.00 107 98.13 99.07 3.44e-70 PDB 1BL4 "Fkbp Mutant F36v Complexed With Remodeled Synthetic Ligand" 100.00 107 99.07 99.07 3.15e-71 PDB 1D6O "Native Fkbp" 100.00 107 100.00 100.00 3.18e-72 PDB 1D7H "Fkbp Complexed With Dmso" 100.00 107 100.00 100.00 3.18e-72 PDB 1D7I "Fkbp Complexed With Methyl Methylsulfinylmethyl Sulfide (Dss)" 100.00 107 100.00 100.00 3.18e-72 PDB 1D7J "Fkbp Complexed With 4-Hydroxy-2-Butanone" 100.00 107 100.00 100.00 3.18e-72 PDB 1EYM "Fk506 Binding Protein Mutant, Homodimeric Complex" 100.00 107 99.07 99.07 2.40e-71 PDB 1F40 "Solution Structure Of Fkbp12 Complexed With Gpi-1046, A Neurotrophic Ligand" 100.00 107 100.00 100.00 3.18e-72 PDB 1FAP "The Structure Of The Immunophilin-Immunosuppressant Fkbp12- Rapamycin Complex Interacting With Human Frap" 99.07 107 100.00 100.00 1.48e-71 PDB 1FKB "Atomic Structure Of The Rapamycin Human Immunophilin Fkbp- 12 Complex" 99.07 107 100.00 100.00 1.48e-71 PDB 1FKD "Fk-506 Binding Protein: Three-Dimensional Structure Of The Complex With The Antagonist L-685,818" 100.00 107 100.00 100.00 3.18e-72 PDB 1FKF "Atomic Structure Of Fkbp-Fk506, An Immunophilin-Immunosuppressant Complex" 100.00 107 100.00 100.00 3.18e-72 PDB 1FKG "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.48e-71 PDB 1FKH "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.48e-71 PDB 1FKI "Design, Synthesis, And Kinetic Evaluation Of High-Affinity Fkbp Ligands, And The X-Ray Crystal Structures Of Their Complexes Wi" 99.07 107 100.00 100.00 1.48e-71 PDB 1FKJ "Atomic Structure Of Fkbp12-Fk506, An Immunophilin Immunosuppressant Complex" 100.00 107 100.00 100.00 3.18e-72 PDB 1FKK "Atomic Structure Of Fkbp12, An Immunophilin Binding Protein" 100.00 107 97.20 100.00 1.82e-70 PDB 1FKL "Atomic Structure Of Fkbp12-Rapaymycin, An Immunophilin- Immunosuppressant Complex" 100.00 107 97.20 100.00 1.82e-70 PDB 1FKR "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.18e-72 PDB 1FKS "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.18e-72 PDB 1FKT "Solution Structure Of Fkbp, A Rotamase Enzyme And Receptor For Fk506 And Rapamycin" 100.00 107 100.00 100.00 3.18e-72 PDB 1J4H "Crystal Structure Analysis Of The Fkbp12 Complexed With 000107 Small Molecule" 100.00 107 100.00 100.00 3.18e-72 PDB 1J4I "Crystal Structure Analysis Of The Fkbp12 Complexed With 000308 Small Molecule" 100.00 107 100.00 100.00 3.18e-72 PDB 1J4R "Fk506 Binding Protein Complexed With Fkb-001" 100.00 107 100.00 100.00 3.18e-72 PDB 1NSG "The Structure Of The Immunophilin-immunosuppressant Fkbp12-rapamycin Complex Interacting With Human Frap" 100.00 107 100.00 100.00 3.18e-72 PDB 1QPF "Fk506 Binding Protein (12 Kda, Human) Complex With L-709,858" 100.00 107 100.00 100.00 3.18e-72 PDB 1QPL "Fk506 Binding Protein (12 Kda, Human) Complex With L-707,587" 100.00 107 100.00 100.00 3.18e-72 PDB 1TCO "Ternary Complex Of A Calcineurin A Fragment, Calcineurin B, Fkbp12 And The Immunosuppressant Drug Fk506 (tacrolimus)" 100.00 107 99.07 99.07 2.73e-71 PDB 2DG3 "Wildtype Fk506-Binding Protein Complexed With Rapamycin" 100.00 107 100.00 100.00 3.18e-72 PDB 2DG4 "Fk506-Binding Protein Mutant Wf59 Complexed With Rapamycin" 100.00 107 99.07 100.00 4.05e-71 PDB 2DG9 "Fk506-Binding Protein Mutant Wl59 Complexed With Rapamycin" 100.00 107 99.07 99.07 7.46e-71 PDB 2FAP "The Structure Of The Immunophilin-immunosuppressant Fkbp12-(c16)- Ethoxy Rapamycin Complex Interacting With Huma" 100.00 107 100.00 100.00 3.18e-72 PDB 2FKE "Fk-506-Binding Protein: Three-Dimensional Structure Of The Complex With The Antagonist L-685,818" 100.00 107 100.00 100.00 3.18e-72 PDB 2PPN "Crystal Structure Of Fkbp12" 100.00 107 100.00 100.00 3.18e-72 PDB 2PPO "Crystal Structure Of E60a Mutant Of Fkbp12" 100.00 107 99.07 99.07 1.64e-71 PDB 2PPP "Crystal Structure Of E60q Mutant Of Fkbp12" 100.00 107 99.07 100.00 9.18e-72 PDB 2RSE "Nmr Structure Of Fkbp12-Mtor Frb Domain-Rapamycin Complex Structure Determined Based On Pcs" 100.00 107 100.00 100.00 3.18e-72 PDB 3FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 107 100.00 100.00 3.18e-72 PDB 3H9R "Crystal Structure Of The Kinase Domain Of Type I Activin Receptor (Acvr1) In Complex With Fkbp12 And Dorsomorphin" 100.00 109 100.00 100.00 2.19e-72 PDB 3MDY "Crystal Structure Of The Cytoplasmic Domain Of The Bone Morp Protein Receptor Type-1b (Bmpr1b) In Complex With Fkbp12 An 193189" 100.00 109 100.00 100.00 2.19e-72 PDB 4DH0 "X-Ray Crystal Structure Of 28-O-Methylrapamycin Complexed With Fkbp12: Is The Cyclohexyl Moiety Part Of The Effector Domain Of " 100.00 107 100.00 100.00 3.18e-72 PDB 4FAP "Atomic Structures Of The Rapamycin Analogs In Complex With Both Human Fkbp12 And Frb Domain Of Frap" 100.00 107 100.00 100.00 3.18e-72 PDB 4IPX "Analyzing The Visible Conformational Substates Of The Fk506 Binding Protein Fkbp12" 100.00 107 98.13 98.13 2.08e-69 PDB 4N19 "Structural Basis Of Conformational Transitions In The Active Site And 80 S Loop In The Fk506 Binding Protein Fkbp12" 100.00 107 98.13 98.13 9.69e-70 DBJ BAB22351 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 DBJ BAB27125 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 DBJ BAB31680 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 DBJ BAE32804 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 DBJ BAE40271 "unnamed protein product [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 EMBL CAA36462 "FK-506 binding protein [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 EMBL CAA39272 "FKBP [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 EMBL CAA42762 "FK506-binding protein [Mus musculus]" 100.00 108 97.20 97.20 1.18e-69 EMBL CAG28541 "FKBP1A [Homo sapiens]" 100.00 108 98.13 99.07 2.15e-70 EMBL CAG46965 "FKBP1A [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 GB AAA19163 "immunophilin FKBP12 [Rattus norvegicus]" 100.00 108 97.20 97.20 1.18e-69 GB AAA31252 "binding protein [Oryctolagus cuniculus]" 100.00 108 100.00 100.00 3.47e-72 GB AAA35844 "FK506-binding protein (FKBP) [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 GB AAA58472 "FKBP-12 protein [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 GB AAA58476 "FK506-binding protein 12 [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 PRF 1613455A "FK506 binding protein FKBP" 100.00 108 100.00 100.00 3.47e-72 REF NP_000792 "peptidyl-prolyl cis-trans isomerase FKBP1A isoform a [Homo sapiens]" 100.00 108 100.00 100.00 3.47e-72 REF NP_001030533 "peptidyl-prolyl cis-trans isomerase FKBP1A [Bos taurus]" 100.00 108 97.20 100.00 1.58e-70 REF NP_001033089 "peptidyl-prolyl cis-trans isomerase FKBP1A [Sus scrofa]" 100.00 108 98.13 100.00 1.12e-70 REF NP_001164597 "peptidyl-prolyl cis-trans isomerase FKBP1A [Oryctolagus cuniculus]" 100.00 108 100.00 100.00 3.47e-72 REF NP_001239119 "peptidyl-prolyl cis-trans isomerase FKBP1A [Canis lupus familiaris]" 100.00 108 99.07 100.00 1.86e-71 SP P18203 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 100.00 1.58e-70 SP P26883 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 97.20 1.18e-69 SP P62942 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 100.00 100.00 3.47e-72 SP P62943 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 100.00 100.00 3.47e-72 SP Q62658 "RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; AltName: Full=12 kDa FK506-binding protein; Shor" 100.00 108 97.20 97.20 1.18e-69 TPG DAA23300 "TPA: peptidyl-prolyl cis-trans isomerase FKBP1A [Bos taurus]" 100.00 108 97.20 100.00 1.58e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FKBP12 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $FKBP12 'recombinant technology' . Escherichia coli BL21 pET11a 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 _Isotopic_labeling $FKBP12 1.5 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FKBP12 1.5 mM '[U-98% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_DQF-COSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ save_sample_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HCCH-TOCSY' '3D HNCO' '3D HCACO' '3D H(CCO)NH' '2D 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FKBP12 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 GLY HA2 H 3.211 . 1 2 1 1 GLY HA3 H 1.541 . 1 3 1 1 GLY C C 168.598 . 1 4 1 1 GLY CA C 42.246 . 1 5 2 2 VAL H H 8.491 . 1 6 2 2 VAL HA H 5.083 . 1 7 2 2 VAL HB H 1.756 . 1 8 2 2 VAL HG1 H 0.864 . 1 9 2 2 VAL HG2 H 0.770 . 1 10 2 2 VAL C C 172.931 . 1 11 2 2 VAL CA C 58.689 . 1 12 2 2 VAL CB C 34.596 . 1 13 2 2 VAL CG1 C 22.381 . 1 14 2 2 VAL CG2 C 18.647 . 1 15 2 2 VAL N N 120.857 . 1 16 3 3 GLN H H 8.526 . 1 17 3 3 GLN HA H 4.628 . 1 18 3 3 GLN HB2 H 2.03 . 1 19 3 3 GLN HB3 H 1.89 . 1 20 3 3 GLN HG3 H 2.228 . 1 21 3 3 GLN HE21 H 7.338 . 1 22 3 3 GLN HE22 H 6.768 . 1 23 3 3 GLN C C 174.462 . 1 24 3 3 GLN CA C 54.249 . 1 25 3 3 GLN CB C 31.221 . 1 26 3 3 GLN CG C 33.857 . 1 27 3 3 GLN N N 127.672 . 1 28 3 3 GLN NE2 N 111.315 . 1 29 4 4 VAL H H 8.803 . 1 30 4 4 VAL HA H 4.454 . 1 31 4 4 VAL HB H 1.955 . 1 32 4 4 VAL HG1 H 0.584 . 1 33 4 4 VAL HG2 H 0.744 . 1 34 4 4 VAL C C 175.255 . 1 35 4 4 VAL CA C 61.986 . 1 36 4 4 VAL CB C 32.907 . 1 37 4 4 VAL CG1 C 20.578 . 1 38 4 4 VAL CG2 C 21.150 . 1 39 4 4 VAL N N 125.506 . 1 40 5 5 GLU H H 8.993 . 1 41 5 5 GLU HA H 4.725 . 1 42 5 5 GLU HB2 H 1.878 . 1 43 5 5 GLU HB3 H 2.039 . 1 44 5 5 GLU HG2 H 2.1 . 1 45 5 5 GLU HG3 H 2.1 . 1 46 5 5 GLU C C 175.55 . 1 47 5 5 GLU CA C 54.16 . 1 48 5 5 GLU CB C 32.622 . 1 49 5 5 GLU CG C 36.417 . 1 50 5 5 GLU N N 128.8 . 1 51 6 6 THR H H 9.126 . 1 52 6 6 THR HA H 3.838 . 1 53 6 6 THR HB H 4.017 . 1 54 6 6 THR HG2 H 1.056 . 1 55 6 6 THR C C 173.493 . 1 56 6 6 THR CA C 66.671 . 1 57 6 6 THR CB C 68.824 . 1 58 6 6 THR CG2 C 22.278 . 1 59 6 6 THR N N 124.37 . 1 60 7 7 ILE H H 9.295 . 1 61 7 7 ILE HA H 4.005 . 1 62 7 7 ILE HB H 1.227 . 1 63 7 7 ILE HG12 H 0.988 . 1 64 7 7 ILE HG13 H 1.489 . 1 65 7 7 ILE HG2 H 0.797 . 1 66 7 7 ILE HD1 H 0.653 . 1 67 7 7 ILE C C 175.596 . 1 68 7 7 ILE CA C 63.216 . 1 69 7 7 ILE CB C 39.609 . 1 70 7 7 ILE CG1 C 27.647 . 1 71 7 7 ILE CG2 C 16.562 . 1 72 7 7 ILE CD1 C 13.418 . 1 73 7 7 ILE N N 129.531 . 1 74 8 8 SER H H 8.249 . 1 75 8 8 SER HA H 4.929 . 1 76 8 8 SER HB2 H 3.811 . 1 77 8 8 SER HB3 H 3.735 . 1 78 8 8 SER C C 171.717 . 1 79 8 8 SER CA C 55.548 . 1 80 8 8 SER CB C 64.276 . 1 81 8 8 SER N N 114.711 . 1 82 9 9 PRO HA H 4.276 . 1 83 9 9 PRO HB2 H 2.043 . 1 84 9 9 PRO HB3 H 2.228 . 1 85 9 9 PRO HG2 H 1.96 . 1 86 9 9 PRO HG3 H 1.96 . 1 87 9 9 PRO HD2 H 3.666 . 1 88 9 9 PRO HD3 H 3.745 . 1 89 9 9 PRO C C 177.48 . 1 90 9 9 PRO CA C 63.562 . 1 91 9 9 PRO CB C 32.572 . 1 92 9 9 PRO CG C 26.967 . 1 93 9 9 PRO CD C 51.054 . 1 94 10 10 GLY H H 8.425 . 1 95 10 10 GLY HA2 H 4.09 . 1 96 10 10 GLY HA3 H 3.464 . 1 97 10 10 GLY C C 173.999 . 1 98 10 10 GLY CA C 44.065 . 1 99 10 10 GLY N N 107.853 . 1 100 11 11 ASP H H 7.989 . 1 101 11 11 ASP HA H 4.232 . 1 102 11 11 ASP HB2 H 2.904 . 1 103 11 11 ASP HB3 H 2.663 . 1 104 11 11 ASP C C 178.158 . 1 105 11 11 ASP CA C 54.559 . 1 106 11 11 ASP CB C 39.051 . 1 107 11 11 ASP N N 118.815 . 1 108 12 12 GLY H H 8.675 . 1 109 12 12 GLY HA2 H 3.94 . 1 110 12 12 GLY HA3 H 3.399 . 1 111 12 12 GLY C C 173.093 . 1 112 12 12 GLY CA C 45.956 . 1 113 12 12 GLY N N 108.212 . 1 114 13 13 ARG H H 8.485 . 1 115 13 13 ARG HA H 4.653 . 1 116 13 13 ARG HB2 H 1.465 . 1 117 13 13 ARG HB3 H 1.662 . 1 118 13 13 ARG HG2 H 1.356 . 1 119 13 13 ARG HG3 H 1.465 . 1 120 13 13 ARG HD2 H 3.084 . 1 121 13 13 ARG HD3 H 3.084 . 1 122 13 13 ARG C C 174.856 . 1 123 13 13 ARG CA C 56.759 . 1 124 13 13 ARG CB C 34.039 . 1 125 13 13 ARG CG C 26.437 . 1 126 13 13 ARG CD C 43.137 . 1 127 13 13 ARG N N 117.596 . 1 128 14 14 THR H H 10.146 . 1 129 14 14 THR HA H 4.139 . 1 130 14 14 THR HB H 4.150 . 1 131 14 14 THR HG2 H 1.029 . 1 132 14 14 THR C C 172.087 . 1 133 14 14 THR CA C 61.986 . 1 134 14 14 THR CB C 66.340 . 1 135 14 14 THR CG2 C 22.386 . 1 136 14 14 THR N N 125.323 . 1 137 15 15 PHE H H 8.074 . 1 138 15 15 PHE HA H 5.176 . 1 139 15 15 PHE HB2 H 2.539 . 1 140 15 15 PHE HB3 H 3.009 . 1 141 15 15 PHE HD1 H 6.973 . 1 142 15 15 PHE HD2 H 6.973 . 1 143 15 15 PHE HE1 H 7.016 . 1 144 15 15 PHE HE2 H 7.016 . 1 145 15 15 PHE HZ H 6.994 . 1 146 15 15 PHE C C 174.243 . 1 147 15 15 PHE CA C 54.422 . 1 148 15 15 PHE CB C 39.594 . 1 149 15 15 PHE CD1 C 132.696 . 1 150 15 15 PHE CD2 C 132.696 . 1 151 15 15 PHE CE1 C 130.760 . 1 152 15 15 PHE CE2 C 130.760 . 1 153 15 15 PHE CZ C 128.688 . 1 154 15 15 PHE N N 124.798 . 1 155 16 16 PRO HA H 4.287 . 1 156 16 16 PRO HB2 H 1.585 . 1 157 16 16 PRO HB3 H 1.954 . 1 158 16 16 PRO HG2 H 1.725 . 1 159 16 16 PRO HG3 H 2.056 . 1 160 16 16 PRO HD2 H 3.971 . 1 161 16 16 PRO HD3 H 4.236 . 1 162 16 16 PRO C C 175.283 . 1 163 16 16 PRO CA C 62.984 . 1 164 16 16 PRO CB C 33.134 . 1 165 16 16 PRO CG C 28.149 . 1 166 16 16 PRO CD C 51.546 . 1 167 17 17 LYS H H 8.461 . 1 168 17 17 LYS HA H 4.532 . 1 169 17 17 LYS HB2 H 1.470 . 1 170 17 17 LYS HB3 H 1.748 . 1 171 17 17 LYS HG2 H 1.364 . 1 172 17 17 LYS HG3 H 1.435 . 1 173 17 17 LYS HD2 H 1.555 . 1 174 17 17 LYS HD3 H 1.555 . 1 175 17 17 LYS HE2 H 2.928 . 1 176 17 17 LYS HE3 H 2.906 . 1 177 17 17 LYS C C 175.859 . 1 178 17 17 LYS CA C 53.467 . 1 179 17 17 LYS CB C 34.615 . 1 180 17 17 LYS CG C 24.550 . 1 181 17 17 LYS CD C 28.649 . 1 182 17 17 LYS CE C 42.182 . 1 183 17 17 LYS N N 121.634 . 1 184 18 18 ARG H H 8.416 . 1 185 18 18 ARG HA H 3.557 . 1 186 18 18 ARG HB2 H 1.640 . 1 187 18 18 ARG HB3 H 1.699 . 1 188 18 18 ARG HG2 H 1.437 . 1 189 18 18 ARG HG3 H 1.640 . 1 190 18 18 ARG HD2 H 3.147 . 1 191 18 18 ARG HD3 H 3.147 . 1 192 18 18 ARG C C 177.195 . 1 193 18 18 ARG CA C 58.766 . 1 194 18 18 ARG CB C 29.385 . 1 195 18 18 ARG CG C 29.564 . 1 196 18 18 ARG CD C 43.234 . 1 197 18 18 ARG N N 120.434 . 1 198 19 19 GLY H H 8.643 . 1 199 19 19 GLY HA2 H 4.324 . 1 200 19 19 GLY HA3 H 3.580 . 1 201 19 19 GLY C C 174.015 . 1 202 19 19 GLY CA C 44.875 . 1 203 19 19 GLY N N 112.924 . 1 204 20 20 GLN H H 8.058 . 1 205 20 20 GLN HA H 4.433 . 1 206 20 20 GLN HB2 H 1.816 . 1 207 20 20 GLN HB3 H 2.209 . 1 208 20 20 GLN HG2 H 1.795 . 1 209 20 20 GLN HG3 H 1.916 . 1 210 20 20 GLN HE21 H 6.407 . 1 211 20 20 GLN HE22 H 7.515 . 1 212 20 20 GLN C C 174.813 . 1 213 20 20 GLN CA C 56.245 . 1 214 20 20 GLN CB C 30.551 . 1 215 20 20 GLN CG C 35.597 . 1 216 20 20 GLN N N 118.665 . 1 217 20 20 GLN NE2 N 110.599 . 1 218 21 21 THR H H 8.706 . 1 219 21 21 THR HA H 4.388 . 1 220 21 21 THR HB H 3.815 . 1 221 21 21 THR HG2 H 0.753 . 1 222 21 21 THR C C 173.613 . 1 223 21 21 THR CA C 63.003 . 1 224 21 21 THR CB C 68.744 . 1 225 21 21 THR CG2 C 21.448 . 1 226 21 21 THR N N 119.664 . 1 227 22 22 CYS H H 8.78 . 1 228 22 22 CYS HA H 4.206 . 1 229 22 22 CYS HB2 H 1.728 . 1 230 22 22 CYS HB3 H 1.624 . 1 231 22 22 CYS C C 172.236 . 1 232 22 22 CYS CA C 57.974 . 1 233 22 22 CYS CB C 28.426 . 1 234 22 22 CYS N N 125.936 . 1 235 23 23 VAL H H 7.941 . 1 236 23 23 VAL HA H 4.535 . 1 237 23 23 VAL HB H 1.929 . 1 238 23 23 VAL HG1 H 0.526 . 1 239 23 23 VAL HG2 H 0.659 . 1 240 23 23 VAL C C 175.714 . 1 241 23 23 VAL CA C 61.449 . 1 242 23 23 VAL CB C 30.989 . 1 243 23 23 VAL CG1 C 19.691 . 1 244 23 23 VAL CG2 C 21.254 . 1 245 23 23 VAL N N 123.375 . 1 246 24 24 VAL H H 9.558 . 1 247 24 24 VAL HA H 5.798 . 1 248 24 24 VAL HB H 2.297 . 1 249 24 24 VAL HG1 H 1.209 . 1 250 24 24 VAL HG2 H 0.836 . 1 251 24 24 VAL C C 175.400 . 1 252 24 24 VAL CA C 57.891 . 1 253 24 24 VAL CB C 35.533 . 1 254 24 24 VAL CG1 C 20.045 . 1 255 24 24 VAL CG2 C 21.727 . 1 256 24 24 VAL N N 117.997 . 1 257 25 25 HIS H H 8.511 . 1 258 25 25 HIS HA H 5.809 . 1 259 25 25 HIS HB2 H 2.778 . 1 260 25 25 HIS HB3 H 2.651 . 1 261 25 25 HIS HD2 H 6.906 . 1 262 25 25 HIS HE1 H 7.037 . 1 263 25 25 HIS C C 176.535 . 1 264 25 25 HIS CA C 54.391 . 1 265 25 25 HIS CB C 35.229 . 1 266 25 25 HIS CD2 C 136.901 . 1 267 25 25 HIS CE1 C 117.435 . 1 268 25 25 HIS N N 118.688 . 1 269 26 26 TYR H H 9.891 . 1 270 26 26 TYR HA H 6.405 . 1 271 26 26 TYR HB2 H 2.918 . 1 272 26 26 TYR HB3 H 2.840 . 1 273 26 26 TYR HD1 H 6.903 . 1 274 26 26 TYR HD2 H 6.903 . 1 275 26 26 TYR HE1 H 6.512 . 1 276 26 26 TYR HE2 H 6.512 . 1 277 26 26 TYR C C 173.681 . 1 278 26 26 TYR CA C 55.898 . 1 279 26 26 TYR CB C 44.356 . 1 280 26 26 TYR CD1 C 132.667 . 1 281 26 26 TYR CD2 C 132.667 . 1 282 26 26 TYR CE1 C 117.807 . 1 283 26 26 TYR CE2 C 117.807 . 1 284 26 26 TYR N N 118.481 . 1 285 27 27 THR H H 8.680 . 1 286 27 27 THR HA H 4.476 . 1 287 27 27 THR HB H 3.916 . 1 288 27 27 THR HG2 H 1.149 . 1 289 27 27 THR C C 172.587 . 1 290 27 27 THR CA C 63.001 . 1 291 27 27 THR CB C 72.204 . 1 292 27 27 THR CG2 C 22.076 . 1 293 27 27 THR N N 116.790 . 1 294 28 28 GLY H H 9.216 . 1 295 28 28 GLY HA2 H 3.959 . 1 296 28 28 GLY HA3 H 2.113 . 1 297 28 28 GLY C C 170.807 . 1 298 28 28 GLY CA C 45.405 . 1 299 28 28 GLY N N 115.190 . 1 300 29 29 MET H H 9.120 . 1 301 29 29 MET HA H 5.193 . 1 302 29 29 MET HB2 H 1.788 . 1 303 29 29 MET HB3 H 1.872 . 1 304 29 29 MET HG2 H 1.903 . 1 305 29 29 MET HG3 H 2.275 . 1 306 29 29 MET C C 175.317 . 1 307 29 29 MET CA C 54.185 . 1 308 29 29 MET CB C 37.485 . 1 309 29 29 MET CE C 16.611 . 1 310 29 29 MET N N 125.529 . 1 311 30 30 LEU H H 8.421 . 1 312 30 30 LEU HA H 4.698 . 1 313 30 30 LEU HB2 H 1.827 . 1 314 30 30 LEU HB3 H 2.146 . 1 315 30 30 LEU HG H 1.832 . 1 316 30 30 LEU HD1 H 0.771 . 1 317 30 30 LEU HD2 H 0.977 . 1 318 30 30 LEU C C 179.13 . 1 319 30 30 LEU CA C 53.963 . 1 320 30 30 LEU CB C 41.507 . 1 321 30 30 LEU CG C 28.159 . 1 322 30 30 LEU CD1 C 23.020 . 1 323 30 30 LEU CD2 C 25.669 . 1 324 30 30 LEU N N 119.043 . 1 325 31 31 GLU H H 8.991 . 1 326 31 31 GLU HA H 3.753 . 1 327 31 31 GLU HB2 H 1.98 . 1 328 31 31 GLU HB3 H 2.043 . 1 329 31 31 GLU HG2 H 2.183 . 1 330 31 31 GLU HG3 H 2.183 . 1 331 31 31 GLU C C 176.387 . 1 332 31 31 GLU CA C 59.697 . 1 333 31 31 GLU CB C 29.514 . 1 334 31 31 GLU CG C 36.742 . 1 335 31 31 GLU N N 120.632 . 1 336 32 32 ASP H H 7.778 . 1 337 32 32 ASP HA H 4.356 . 1 338 32 32 ASP HB2 H 2.919 . 1 339 32 32 ASP HB3 H 2.500 . 1 340 32 32 ASP C C 177.037 . 1 341 32 32 ASP CA C 53.499 . 1 342 32 32 ASP CB C 39.683 . 1 343 32 32 ASP N N 115.330 . 1 344 33 33 GLY H H 8.159 . 1 345 33 33 GLY HA2 H 4.208 . 1 346 33 33 GLY HA3 H 3.580 . 1 347 33 33 GLY C C 174.083 . 1 348 33 33 GLY CA C 44.800 . 1 349 33 33 GLY N N 108.474 . 1 350 34 34 LYS H H 7.802 . 1 351 34 34 LYS HA H 4.037 . 1 352 34 34 LYS HB2 H 1.729 . 1 353 34 34 LYS HB3 H 1.846 . 1 354 34 34 LYS HG2 H 1.245 . 1 355 34 34 LYS HG3 H 1.384 . 1 356 34 34 LYS HD2 H 1.600 . 1 357 34 34 LYS HD3 H 1.600 . 1 358 34 34 LYS HE2 H 2.920 . 1 359 34 34 LYS HE3 H 2.920 . 1 360 34 34 LYS C C 176.144 . 1 361 34 34 LYS CA C 57.245 . 1 362 34 34 LYS CB C 32.382 . 1 363 34 34 LYS CG C 24.889 . 1 364 34 34 LYS CD C 29.020 . 1 365 34 34 LYS CE C 42.063 . 1 366 34 34 LYS N N 121.762 . 1 367 35 35 LYS H H 8.503 . 1 368 35 35 LYS HA H 4.429 . 1 369 35 35 LYS HB2 H 1.624 . 1 370 35 35 LYS HB3 H 1.624 . 1 371 35 35 LYS HG2 H 1.045 . 1 372 35 35 LYS HG3 H 1.340 . 1 373 35 35 LYS HD2 H 1.547 . 1 374 35 35 LYS HD3 H 1.547 . 1 375 35 35 LYS HE2 H 2.798 . 1 376 35 35 LYS HE3 H 2.797 . 1 377 35 35 LYS C C 176.517 . 1 378 35 35 LYS CA C 56.587 . 1 379 35 35 LYS CB C 32.628 . 1 380 35 35 LYS CG C 24.136 . 1 381 35 35 LYS CD C 29.291 . 1 382 35 35 LYS CE C 41.229 . 1 383 35 35 LYS N N 127.503 . 1 384 36 36 PHE H H 8.459 . 1 385 36 36 PHE HA H 5.054 . 1 386 36 36 PHE HB2 H 2.568 . 1 387 36 36 PHE HB3 H 3.237 . 1 388 36 36 PHE HD1 H 6.896 . 1 389 36 36 PHE HD2 H 6.896 . 1 390 36 36 PHE HE1 H 7.176 . 1 391 36 36 PHE HE2 H 7.176 . 1 392 36 36 PHE HZ H 6.944 . 1 393 36 36 PHE C C 174.294 . 1 394 36 36 PHE CA C 56.216 . 1 395 36 36 PHE CB C 41.092 . 1 396 36 36 PHE CD1 C 132.663 . 1 397 36 36 PHE CD2 C 132.663 . 1 398 36 36 PHE CE1 C 131.137 . 1 399 36 36 PHE CE2 C 131.137 . 1 400 36 36 PHE CZ C 129.949 . 1 401 36 36 PHE N N 120.998 . 1 402 37 37 ASP H H 6.750 . 1 403 37 37 ASP HA H 4.775 . 1 404 37 37 ASP HB2 H 3.287 . 1 405 37 37 ASP HB3 H 2.105 . 1 406 37 37 ASP C C 174.605 . 1 407 37 37 ASP CA C 54.401 . 1 408 37 37 ASP CB C 44.275 . 1 409 37 37 ASP N N 118.728 . 1 410 38 38 SER H H 8.168 . 1 411 38 38 SER HA H 4.568 . 1 412 38 38 SER HB2 H 3.925 . 1 413 38 38 SER HB3 H 3.534 . 1 414 38 38 SER C C 174.736 . 1 415 38 38 SER CA C 56.889 . 1 416 38 38 SER CB C 64.794 . 1 417 38 38 SER N N 118.281 . 1 418 39 39 SER H H 7.908 . 1 419 39 39 SER HA H 4.085 . 1 420 39 39 SER HB2 H 4.961 . 1 421 39 39 SER HB3 H 3.715 . 1 422 39 39 SER C C 176.870 . 1 423 39 39 SER CA C 61.525 . 1 424 39 39 SER CB C 61.659 . 1 425 39 39 SER N N 124.643 . 1 426 40 40 ARG H H 7.557 . 1 427 40 40 ARG HA H 3.530 . 1 428 40 40 ARG HB2 H 1.296 . 1 429 40 40 ARG HG2 H 1.022 . 1 430 40 40 ARG HD2 H 2.692 . 1 431 40 40 ARG HD3 H 2.692 . 1 432 40 40 ARG C C 179.659 . 1 433 40 40 ARG CA C 58.884 . 1 434 40 40 ARG CB C 28.444 . 1 435 40 40 ARG CD C 43.137 . 1 436 40 40 ARG N N 124.034 . 1 437 41 41 ASP H H 7.131 . 1 438 41 41 ASP HA H 4.244 . 1 439 41 41 ASP HB2 H 2.717 . 1 440 41 41 ASP HB3 H 2.547 . 1 441 41 41 ASP C C 176.644 . 1 442 41 41 ASP CA C 56.417 . 1 443 41 41 ASP CB C 39.868 . 1 444 41 41 ASP N N 118.552 . 1 445 42 42 ARG H H 6.845 . 1 446 42 42 ARG HA H 4.366 . 1 447 42 42 ARG HB2 H 1.926 . 1 448 42 42 ARG HB3 H 1.926 . 1 449 42 42 ARG HG2 H 1.604 . 1 450 42 42 ARG HG3 H 1.690 . 1 451 42 42 ARG HD2 H 3.162 . 1 452 42 42 ARG HD3 H 3.416 . 1 453 42 42 ARG C C 175.262 . 1 454 42 42 ARG CA C 55.993 . 1 455 42 42 ARG CB C 31.087 . 1 456 42 42 ARG CG C 28.389 . 1 457 42 42 ARG CD C 43.461 . 1 458 42 42 ARG N N 114.890 . 1 459 43 43 ASN H H 7.760 . 1 460 43 43 ASN HA H 4.347 . 1 461 43 43 ASN HB2 H 3.123 . 1 462 43 43 ASN HB3 H 2.617 . 1 463 43 43 ASN HD21 H 7.521 . 1 464 43 43 ASN HD22 H 6.778 . 1 465 43 43 ASN C C 173.928 . 1 466 43 43 ASN CA C 54.035 . 1 467 43 43 ASN CB C 37.317 . 1 468 43 43 ASN N N 115.563 . 1 469 43 43 ASN ND2 N 112.326 . 1 470 44 44 LYS H H 7.338 . 1 471 44 44 LYS HA H 4.852 . 1 472 44 44 LYS HB2 H 1.678 . 1 473 44 44 LYS HB3 H 1.741 . 1 474 44 44 LYS HG2 H 1.417 . 1 475 44 44 LYS HG3 H 1.417 . 1 476 44 44 LYS HD2 H 1.67 . 1 477 44 44 LYS HD3 H 1.67 . 1 478 44 44 LYS HE2 H 2.99 . 1 479 44 44 LYS HE3 H 2.99 . 1 480 44 44 LYS C C 172.152 . 1 481 44 44 LYS CA C 53.490 . 1 482 44 44 LYS CB C 35.117 . 1 483 44 44 LYS CG C 24.185 . 1 484 44 44 LYS CD C 29.293 . 1 485 44 44 LYS CE C 42.052 . 1 486 44 44 LYS N N 115.634 . 1 487 45 45 PRO HA H 3.865 . 1 488 45 45 PRO HB2 H 1.327 . 1 489 45 45 PRO HB3 H 1.327 . 1 490 45 45 PRO HG2 H 1.182 . 1 491 45 45 PRO HG3 H 1.634 . 1 492 45 45 PRO HD2 H 3.565 . 1 493 45 45 PRO HD3 H 3.525 . 1 494 45 45 PRO C C 174.075 . 1 495 45 45 PRO CA C 62.940 . 1 496 45 45 PRO CB C 32.122 . 1 497 45 45 PRO CG C 26.396 . 1 498 45 45 PRO CD C 50.632 . 1 499 46 46 PHE H H 9.146 . 1 500 46 46 PHE HA H 4.882 . 1 501 46 46 PHE HB2 H 3.539 . 1 502 46 46 PHE HB3 H 3.136 . 1 503 46 46 PHE HD1 H 7.236 . 1 504 46 46 PHE HD2 H 7.236 . 1 505 46 46 PHE HE1 H 7.032 . 1 506 46 46 PHE HE2 H 7.032 . 1 507 46 46 PHE HZ H 7.065 . 1 508 46 46 PHE C C 172.781 . 1 509 46 46 PHE CA C 56.687 . 1 510 46 46 PHE CB C 42.721 . 1 511 46 46 PHE CD1 C 131.470 . 1 512 46 46 PHE CD2 C 131.470 . 1 513 46 46 PHE CE1 C 131.738 . 1 514 46 46 PHE CE2 C 131.738 . 1 515 46 46 PHE CZ C 130.110 . 1 516 46 46 PHE N N 124.293 . 1 517 47 47 LYS H H 7.366 . 1 518 47 47 LYS HA H 5.520 . 1 519 47 47 LYS HB2 H 1.172 . 1 520 47 47 LYS HB3 H 1.404 . 1 521 47 47 LYS HG2 H 0.964 . 1 522 47 47 LYS HG3 H 1.231 . 1 523 47 47 LYS HD2 H 1.327 . 1 524 47 47 LYS HD3 H 1.404 . 1 525 47 47 LYS HE2 H 2.534 . 1 526 47 47 LYS HE3 H 2.749 . 1 527 47 47 LYS C C 174.571 . 1 528 47 47 LYS CA C 54.087 . 1 529 47 47 LYS CB C 35.165 . 1 530 47 47 LYS CG C 25.299 . 1 531 47 47 LYS CD C 29.427 . 1 532 47 47 LYS CE C 41.540 . 1 533 47 47 LYS N N 124.383 . 1 534 48 48 PHE H H 7.942 . 1 535 48 48 PHE HA H 4.640 . 1 536 48 48 PHE HB2 H 2.840 . 1 537 48 48 PHE HB3 H 2.734 . 1 538 48 48 PHE HD1 H 6.871 . 1 539 48 48 PHE HD2 H 6.871 . 1 540 48 48 PHE HE1 H 6.944 . 1 541 48 48 PHE HE2 H 6.944 . 1 542 48 48 PHE HZ H 6.782 . 1 543 48 48 PHE C C 171.512 . 1 544 48 48 PHE CA C 55.651 . 1 545 48 48 PHE CB C 41.218 . 1 546 48 48 PHE CD1 C 132.892 . 1 547 48 48 PHE CD2 C 132.892 . 1 548 48 48 PHE CE1 C 129.949 . 1 549 48 48 PHE CE2 C 129.949 . 1 550 48 48 PHE CZ C 127.781 . 1 551 48 48 PHE N N 115.417 . 1 552 49 49 MET H H 9.138 . 1 553 49 49 MET HA H 4.609 . 1 554 49 49 MET HB2 H 1.733 . 1 555 49 49 MET HB3 H 1.747 . 1 556 49 49 MET HG2 H 2.040 . 1 557 49 49 MET C C 176.278 . 1 558 49 49 MET CA C 54.249 . 1 559 49 49 MET CB C 33.403 . 1 560 49 49 MET CG C 31.179 . 1 561 49 49 MET CE C 16.826 . 1 562 49 49 MET N N 122.850 . 1 563 50 50 LEU H H 8.570 . 1 564 50 50 LEU HA H 4.168 . 1 565 50 50 LEU HB2 H 1.297 . 1 566 50 50 LEU HB3 H 1.883 . 1 567 50 50 LEU HG H 1.541 . 1 568 50 50 LEU HD1 H 0.986 . 1 569 50 50 LEU HD2 H 0.663 . 1 570 50 50 LEU C C 177.649 . 1 571 50 50 LEU CA C 57.166 . 1 572 50 50 LEU CB C 41.737 . 1 573 50 50 LEU CG C 27.087 . 1 574 50 50 LEU CD1 C 25.548 . 1 575 50 50 LEU CD2 C 24.895 . 1 576 50 50 LEU N N 131.410 . 1 577 51 51 GLY H H 10.000 . 1 578 51 51 GLY HA2 H 4.260 . 1 579 51 51 GLY HA3 H 3.767 . 1 580 51 51 GLY C C 174.344 . 1 581 51 51 GLY CA C 45.395 . 1 582 51 51 GLY N N 118.418 . 1 583 52 52 LYS H H 7.513 . 1 584 52 52 LYS HA H 4.389 . 1 585 52 52 LYS HB2 H 1.668 . 1 586 52 52 LYS HB3 H 2.029 . 1 587 52 52 LYS HG2 H 1.258 . 1 588 52 52 LYS HG3 H 1.487 . 1 589 52 52 LYS HD2 H 1.605 . 1 590 52 52 LYS HD3 H 1.617 . 1 591 52 52 LYS HE2 H 2.889 . 1 592 52 52 LYS HE3 H 2.946 . 1 593 52 52 LYS C C 175.243 . 1 594 52 52 LYS CA C 54.790 . 1 595 52 52 LYS CB C 32.978 . 1 596 52 52 LYS CG C 25.117 . 1 597 52 52 LYS CD C 28.517 . 1 598 52 52 LYS CE C 41.997 . 1 599 52 52 LYS N N 119.181 . 1 600 53 53 GLN H H 8.993 . 1 601 53 53 GLN HA H 3.884 . 1 602 53 53 GLN HB2 H 2.140 . 1 603 53 53 GLN HB3 H 2.160 . 1 604 53 53 GLN HG2 H 2.100 . 1 605 53 53 GLN HG3 H 2.195 . 1 606 53 53 GLN HE21 H 6.580 . 1 607 53 53 GLN HE22 H 7.463 . 1 608 53 53 GLN C C 175.840 . 1 609 53 53 GLN CA C 57.114 . 1 610 53 53 GLN CB C 25.778 . 1 611 53 53 GLN CG C 34.527 . 1 612 53 53 GLN N N 116.855 . 1 613 53 53 GLN NE2 N 111.950 . 1 614 54 54 GLU H H 9.336 . 1 615 54 54 GLU HA H 4.153 . 1 616 54 54 GLU HB2 H 1.999 . 1 617 54 54 GLU HB3 H 2.069 . 1 618 54 54 GLU HG2 H 2.206 . 1 619 54 54 GLU HG3 H 2.206 . 1 620 54 54 GLU C C 176.046 . 1 621 54 54 GLU CA C 57.317 . 1 622 54 54 GLU CB C 30.786 . 1 623 54 54 GLU CG C 37.025 . 1 624 54 54 GLU N N 117.407 . 1 625 55 55 VAL H H 6.770 . 1 626 55 55 VAL HA H 4.257 . 1 627 55 55 VAL HB H 1.380 . 1 628 55 55 VAL HG1 H 0.042 . 1 629 55 55 VAL HG2 H 0.016 . 1 630 55 55 VAL C C 175.038 . 1 631 55 55 VAL CA C 57.376 . 1 632 55 55 VAL CB C 35.211 . 1 633 55 55 VAL CG1 C 17.876 . 1 634 55 55 VAL CG2 C 21.526 . 1 635 55 55 VAL N N 108.277 . 1 636 56 56 ILE H H 7.369 . 1 637 56 56 ILE HA H 3.780 . 1 638 56 56 ILE HB H 2.104 . 1 639 56 56 ILE HG12 H 0.772 . 1 640 56 56 ILE HG13 H 1.080 . 1 641 56 56 ILE HG2 H 0.148 . 1 642 56 56 ILE HD1 H 0.679 . 1 643 56 56 ILE C C 177.090 . 1 644 56 56 ILE CA C 61.836 . 1 645 56 56 ILE CB C 38.386 . 1 646 56 56 ILE CG1 C 24.911 . 1 647 56 56 ILE CG2 C 17.394 . 1 648 56 56 ILE CD1 C 14.344 . 1 649 56 56 ILE N N 111.410 . 1 650 57 57 ARG H H 8.576 . 1 651 57 57 ARG HA H 3.977 . 1 652 57 57 ARG HB2 H 1.283 . 1 653 57 57 ARG HB3 H 1.700 . 1 654 57 57 ARG HG2 H 1.036 . 1 655 57 57 ARG HG3 H 1.509 . 1 656 57 57 ARG HD2 H 2.038 . 1 657 57 57 ARG HD3 H 2.719 . 1 658 57 57 ARG C C 179.179 . 1 659 57 57 ARG CA C 59.782 . 1 660 57 57 ARG CB C 30.150 . 1 661 57 57 ARG CG C 26.501 . 1 662 57 57 ARG CD C 43.313 . 1 663 57 57 ARG N N 124.697 . 1 664 58 58 GLY H H 9.528 . 1 665 58 58 GLY HA2 H 3.868 . 1 666 58 58 GLY HA3 H 3.731 . 1 667 58 58 GLY C C 175.021 . 1 668 58 58 GLY CA C 47.642 . 1 669 58 58 GLY N N 100.975 . 1 670 59 59 TRP H H 7.460 . 1 671 59 59 TRP HA H 4.176 . 1 672 59 59 TRP HB2 H 2.659 . 1 673 59 59 TRP HB3 H 2.715 . 1 674 59 59 TRP HD1 H 6.308 . 1 675 59 59 TRP HE1 H 5.763 . 1 676 59 59 TRP HE3 H 6.557 . 1 677 59 59 TRP HZ2 H 6.114 . 1 678 59 59 TRP HZ3 H 6.591 . 1 679 59 59 TRP HH2 H 5.641 . 1 680 59 59 TRP C C 177.180 . 1 681 59 59 TRP CA C 59.749 . 1 682 59 59 TRP CB C 28.940 . 1 683 59 59 TRP CD1 C 121.076 . 1 684 59 59 TRP CE3 C 120.114 . 1 685 59 59 TRP CZ2 C 111.895 . 1 686 59 59 TRP CZ3 C 121.268 . 1 687 59 59 TRP CH2 C 124.135 . 1 688 59 59 TRP N N 119.870 . 1 689 59 59 TRP NE1 N 117.833 . 1 690 60 60 GLU H H 7.304 . 1 691 60 60 GLU HA H 3.844 . 1 692 60 60 GLU HB2 H 2.000 . 1 693 60 60 GLU HB3 H 2.100 . 1 694 60 60 GLU HG2 H 2.278 . 1 695 60 60 GLU HG3 H 2.278 . 1 696 60 60 GLU C C 178.236 . 1 697 60 60 GLU CA C 60.999 . 1 698 60 60 GLU CB C 29.046 . 1 699 60 60 GLU CG C 37.155 . 1 700 60 60 GLU N N 118.501 . 1 701 61 61 GLU H H 8.360 . 1 702 61 61 GLU HA H 4.106 . 1 703 61 61 GLU HB2 H 1.833 . 1 704 61 61 GLU HB3 H 2.103 . 1 705 61 61 GLU HG2 H 2.274 . 1 706 61 61 GLU HG3 H 2.373 . 1 707 61 61 GLU C C 179.095 . 1 708 61 61 GLU CA C 58.664 . 1 709 61 61 GLU CB C 29.558 . 1 710 61 61 GLU CG C 36.767 . 1 711 61 61 GLU N N 113.496 . 1 712 62 62 GLY H H 7.799 . 1 713 62 62 GLY HA2 H 3.571 . 1 714 62 62 GLY HA3 H 3.663 . 1 715 62 62 GLY C C 174.326 . 1 716 62 62 GLY CA C 47.107 . 1 717 62 62 GLY N N 107.130 . 1 718 63 63 VAL H H 8.660 . 1 719 63 63 VAL HA H 3.865 . 1 720 63 63 VAL HB H 2.200 . 1 721 63 63 VAL HG1 H 0.936 . 1 722 63 63 VAL HG2 H 1.017 . 1 723 63 63 VAL C C 177.199 . 1 724 63 63 VAL CA C 65.365 . 1 725 63 63 VAL CB C 30.772 . 1 726 63 63 VAL CG1 C 23.688 . 1 727 63 63 VAL CG2 C 22.580 . 1 728 63 63 VAL N N 120.613 . 1 729 64 64 ALA H H 7.033 . 1 730 64 64 ALA HA H 3.964 . 1 731 64 64 ALA HB H 1.512 . 1 732 64 64 ALA C C 177.601 . 1 733 64 64 ALA CA C 54.485 . 1 734 64 64 ALA CB C 18.672 . 1 735 64 64 ALA N N 116.893 . 1 736 65 65 GLN H H 7.079 . 1 737 65 65 GLN HA H 4.308 . 1 738 65 65 GLN HB2 H 2.325 . 1 739 65 65 GLN HB3 H 2.079 . 1 740 65 65 GLN HG2 H 2.478 . 1 741 65 65 GLN HE21 H 7.159 . 1 742 65 65 GLN HE22 H 6.999 . 1 743 65 65 GLN C C 175.365 . 1 744 65 65 GLN CA C 55.419 . 1 745 65 65 GLN CB C 29.710 . 1 746 65 65 GLN CG C 34.218 . 1 747 65 65 GLN N N 112.174 . 1 748 65 65 GLN NE2 N 111.291 . 1 749 66 66 MET H H 7.917 . 1 750 66 66 MET HA H 4.722 . 1 751 66 66 MET HB2 H 1.886 . 1 752 66 66 MET HB3 H 2.079 . 1 753 66 66 MET HG2 H 2.664 . 1 754 66 66 MET HE H 1.809 . 1 755 66 66 MET C C 172.272 . 1 756 66 66 MET CA C 54.825 . 1 757 66 66 MET CB C 35.282 . 1 758 66 66 MET CE C 17.500 . 1 759 66 66 MET N N 122.473 . 1 760 67 67 SER H H 8.143 . 1 761 67 67 SER HA H 4.772 . 1 762 67 67 SER HB2 H 3.681 . 1 763 67 67 SER HB3 H 2.295 . 1 764 67 67 SER C C 176.107 . 1 765 67 67 SER CA C 54.385 . 1 766 67 67 SER CB C 65.898 . 1 767 67 67 SER N N 107.582 . 1 768 68 68 VAL H H 7.601 . 1 769 68 68 VAL HA H 3.041 . 1 770 68 68 VAL HB H 1.724 . 1 771 68 68 VAL HG1 H 0.772 . 1 772 68 68 VAL HG2 H 0.807 . 1 773 68 68 VAL C C 176.249 . 1 774 68 68 VAL CA C 67.005 . 1 775 68 68 VAL CB C 31.270 . 1 776 68 68 VAL CG1 C 21.485 . 1 777 68 68 VAL CG2 C 23.135 . 1 778 68 68 VAL N N 119.172 . 1 779 69 69 GLY H H 8.799 . 1 780 69 69 GLY HA2 H 4.349 . 1 781 69 69 GLY HA3 H 3.775 . 1 782 69 69 GLY C C 173.696 . 1 783 69 69 GLY CA C 44.359 . 1 784 69 69 GLY N N 116.861 . 1 785 70 70 GLN H H 8.562 . 1 786 70 70 GLN HA H 3.978 . 1 787 70 70 GLN HB2 H 2.106 . 1 788 70 70 GLN HB3 H 2.106 . 1 789 70 70 GLN HG2 H 2.895 . 1 790 70 70 GLN HG3 H 2.895 . 1 791 70 70 GLN HE21 H 7.553 . 1 792 70 70 GLN HE22 H 6.438 . 1 793 70 70 GLN C C 173.408 . 1 794 70 70 GLN CA C 55.736 . 1 795 70 70 GLN CB C 30.161 . 1 796 70 70 GLN CG C 33.338 . 1 797 70 70 GLN N N 123.160 . 1 798 70 70 GLN NE2 N 108.549 . 1 799 71 71 ARG H H 8.746 . 1 800 71 71 ARG HA H 5.615 . 1 801 71 71 ARG HB2 H 1.485 . 1 802 71 71 ARG HB3 H 1.796 . 1 803 71 71 ARG HG2 H 1.335 . 1 804 71 71 ARG HG3 H 1.485 . 1 805 71 71 ARG HD2 H 2.835 . 1 806 71 71 ARG HD3 H 2.915 . 1 807 71 71 ARG C C 175.388 . 1 808 71 71 ARG CA C 53.880 . 1 809 71 71 ARG CB C 33.426 . 1 810 71 71 ARG CG C 26.947 . 1 811 71 71 ARG CD C 44.227 . 1 812 71 71 ARG N N 124.610 . 1 813 72 72 ALA H H 9.882 . 1 814 72 72 ALA HA H 5.059 . 1 815 72 72 ALA HB H 1.224 . 1 816 72 72 ALA C C 172.868 . 1 817 72 72 ALA CA C 51.054 . 1 818 72 72 ALA CB C 23.545 . 1 819 72 72 ALA N N 131.011 . 1 820 73 73 LYS H H 9.171 . 1 821 73 73 LYS HA H 5.200 . 1 822 73 73 LYS HB2 H 1.525 . 1 823 73 73 LYS HB3 H 1.676 . 1 824 73 73 LYS HG2 H 1.047 . 1 825 73 73 LYS HG3 H 1.354 . 1 826 73 73 LYS HD2 H 1.612 . 1 827 73 73 LYS HD3 H 1.612 . 1 828 73 73 LYS HE2 H 2.705 . 1 829 73 73 LYS HE3 H 2.705 . 1 830 73 73 LYS C C 175.888 . 1 831 73 73 LYS CA C 54.652 . 1 832 73 73 LYS CB C 34.136 . 1 833 73 73 LYS CG C 24.450 . 1 834 73 73 LYS CD C 28.647 . 1 835 73 73 LYS CE C 42.177 . 1 836 73 73 LYS N N 120.697 . 1 837 74 74 LEU H H 9.929 . 1 838 74 74 LEU HA H 5.442 . 1 839 74 74 LEU HB2 H 1.233 . 1 840 74 74 LEU HB3 H 1.751 . 1 841 74 74 LEU HG H 1.573 . 1 842 74 74 LEU HD1 H 0.629 . 1 843 74 74 LEU HD2 H 0.644 . 1 844 74 74 LEU C C 175.935 . 1 845 74 74 LEU CA C 53.187 . 1 846 74 74 LEU CB C 43.736 . 1 847 74 74 LEU CG C 28.262 . 1 848 74 74 LEU CD1 C 25.471 . 1 849 74 74 LEU CD2 C 25.126 . 1 850 74 74 LEU N N 130.072 . 1 851 75 75 THR H H 8.821 . 1 852 75 75 THR HA H 5.021 . 1 853 75 75 THR HB H 3.945 . 1 854 75 75 THR HG2 H 1.008 . 1 855 75 75 THR C C 175.225 . 1 856 75 75 THR CA C 63.347 . 1 857 75 75 THR CB C 68.765 . 1 858 75 75 THR CG2 C 20.823 . 1 859 75 75 THR N N 121.362 . 1 860 76 76 ILE H H 9.834 . 1 861 76 76 ILE HA H 4.516 . 1 862 76 76 ILE HB H 1.763 . 1 863 76 76 ILE HG12 H 0.706 . 1 864 76 76 ILE HG13 H 1.694 . 1 865 76 76 ILE HG2 H 1.008 . 1 866 76 76 ILE HD1 H 0.790 . 1 867 76 76 ILE C C 173.537 . 1 868 76 76 ILE CA C 61.373 . 1 869 76 76 ILE CB C 41.514 . 1 870 76 76 ILE CG1 C 27.680 . 1 871 76 76 ILE CG2 C 20.823 . 1 872 76 76 ILE CD1 C 14.999 . 1 873 76 76 ILE N N 130.012 . 1 874 77 77 SER H H 8.226 . 1 875 77 77 SER HA H 4.660 . 1 876 77 77 SER HB2 H 3.870 . 1 877 77 77 SER HB3 H 4.330 . 1 878 77 77 SER CA C 57.683 . 1 879 77 77 SER CB C 61.618 . 1 880 77 77 SER N N 121.965 . 1 881 78 78 PRO HA H 4.419 . 1 882 78 78 PRO HB2 H 1.986 . 1 883 78 78 PRO HB3 H 2.043 . 1 884 78 78 PRO HG2 H 1.714 . 1 885 78 78 PRO HG3 H 1.986 . 1 886 78 78 PRO HD2 H 3.752 . 1 887 78 78 PRO HD3 H 3.752 . 1 888 78 78 PRO C C 179.670 . 1 889 78 78 PRO CA C 65.889 . 1 890 78 78 PRO CB C 30.505 . 1 891 78 78 PRO CG C 27.628 . 1 892 78 78 PRO CD C 49.890 . 1 893 79 79 ASP H H 9.443 . 1 894 79 79 ASP HA H 4.343 . 1 895 79 79 ASP HB2 H 2.748 . 1 896 79 79 ASP HB3 H 2.657 . 1 897 79 79 ASP C C 176.402 . 1 898 79 79 ASP CA C 55.127 . 1 899 79 79 ASP CB C 37.711 . 1 900 79 79 ASP N N 114.415 . 1 901 80 80 TYR H H 8.063 . 1 902 80 80 TYR HA H 4.338 . 1 903 80 80 TYR HB2 H 2.721 . 1 904 80 80 TYR HB3 H 2.888 . 1 905 80 80 TYR HD1 H 6.611 . 1 906 80 80 TYR HD2 H 6.611 . 1 907 80 80 TYR HE1 H 6.742 . 1 908 80 80 TYR HE2 H 6.742 . 1 909 80 80 TYR C C 173.129 . 1 910 80 80 TYR CA C 57.673 . 1 911 80 80 TYR CB C 38.860 . 1 912 80 80 TYR CD1 C 130.618 . 1 913 80 80 TYR CD2 C 130.618 . 1 914 80 80 TYR CE1 C 118.732 . 1 915 80 80 TYR CE2 C 118.732 . 1 916 80 80 TYR N N 123.197 . 1 917 81 81 ALA H H 7.787 . 1 918 81 81 ALA HA H 4.350 . 1 919 81 81 ALA HB H 1.375 . 1 920 81 81 ALA C C 175.711 . 1 921 81 81 ALA CA C 51.702 . 1 922 81 81 ALA CB C 19.378 . 1 923 81 81 ALA N N 125.424 . 1 924 82 82 TYR H H 9.195 . 1 925 82 82 TYR HA H 4.494 . 1 926 82 82 TYR HB2 H 2.617 . 1 927 82 82 TYR HB3 H 3.132 . 1 928 82 82 TYR HD1 H 7.008 . 1 929 82 82 TYR HD2 H 7.008 . 1 930 82 82 TYR HE1 H 6.476 . 1 931 82 82 TYR HE2 H 6.476 . 1 932 82 82 TYR C C 176.498 . 1 933 82 82 TYR CA C 58.855 . 1 934 82 82 TYR CB C 37.569 . 1 935 82 82 TYR CD1 C 132.859 . 1 936 82 82 TYR CD2 C 132.859 . 1 937 82 82 TYR CE1 C 117.957 . 1 938 82 82 TYR CE2 C 117.957 . 1 939 82 82 TYR N N 121.991 . 1 940 83 83 GLY H H 8.546 . 1 941 83 83 GLY HA2 H 3.557 . 1 942 83 83 GLY HA3 H 3.833 . 1 943 83 83 GLY C C 174.969 . 1 944 83 83 GLY CA C 46.645 . 1 945 83 83 GLY N N 108.368 . 1 946 84 84 ALA HA H 3.212 . 1 947 84 84 ALA HB H 1.360 . 1 948 84 84 ALA C C 177.435 . 1 949 84 84 ALA CA C 53.522 . 1 950 84 84 ALA CB C 19.286 . 1 951 85 85 THR H H 7.893 . 1 952 85 85 THR HA H 3.976 . 1 953 85 85 THR HB H 4.181 . 1 954 85 85 THR HG2 H 1.160 . 1 955 85 85 THR C C 176.945 . 1 956 85 85 THR CA C 64.002 . 1 957 85 85 THR CB C 69.368 . 1 958 85 85 THR CG2 C 21.793 . 1 959 85 85 THR N N 109.321 . 1 960 86 86 GLY H H 7.278 . 1 961 86 86 GLY HA2 H 3.620 . 1 962 86 86 GLY HA3 H 3.430 . 1 963 86 86 GLY C C 171.499 . 1 964 86 86 GLY CA C 45.086 . 1 965 86 86 GLY N N 106.827 . 1 966 87 87 HIS H H 8.732 . 1 967 87 87 HIS HA H 4.930 . 1 968 87 87 HIS HB2 H 2.492 . 1 969 87 87 HIS HE1 H 7.796 . 1 970 87 87 HIS C C 172.330 . 1 971 87 87 HIS CA C 52.621 . 1 972 87 87 HIS CB C 31.680 . 1 973 87 87 HIS CE1 C 138.302 . 1 974 87 87 HIS N N 121.653 . 1 975 88 88 PRO HA H 4.084 . 1 976 88 88 PRO HB2 H 1.766 . 1 977 88 88 PRO HB3 H 2.101 . 1 978 88 88 PRO HG2 H 1.852 . 1 979 88 88 PRO HG3 H 1.852 . 1 980 88 88 PRO HD2 H 3.198 . 1 981 88 88 PRO HD3 H 3.438 . 1 982 88 88 PRO C C 176.115 . 1 983 88 88 PRO CA C 65.069 . 1 984 88 88 PRO CB C 31.586 . 1 985 88 88 PRO CG C 26.601 . 1 986 88 88 PRO CD C 50.982 . 1 987 89 89 GLY H H 8.519 . 1 988 89 89 GLY HA2 H 4.179 . 1 989 89 89 GLY HA3 H 3.544 . 1 990 89 89 GLY C C 173.752 . 1 991 89 89 GLY CA C 45.180 . 1 992 89 89 GLY N N 113.486 . 1 993 90 90 ILE H H 8.047 . 1 994 90 90 ILE HA H 4.198 . 1 995 90 90 ILE HB H 1.349 . 1 996 90 90 ILE HG12 H 0.879 . 1 997 90 90 ILE HG13 H 1.219 . 1 998 90 90 ILE HG2 H 0.796 . 1 999 90 90 ILE HD1 H 0.591 . 1 1000 90 90 ILE C C 174.272 . 1 1001 90 90 ILE CA C 62.777 . 1 1002 90 90 ILE CB C 41.507 . 1 1003 90 90 ILE CG1 C 26.885 . 1 1004 90 90 ILE CG2 C 17.681 . 1 1005 90 90 ILE CD1 C 12.584 . 1 1006 90 90 ILE N N 118.011 . 1 1007 91 91 ILE H H 8.186 . 1 1008 91 91 ILE HA H 4.419 . 1 1009 91 91 ILE HB H 1.211 . 1 1010 91 91 ILE HG12 H 0.229 . 1 1011 91 91 ILE HG13 H 0.670 . 1 1012 91 91 ILE HG2 H 0.796 . 1 1013 91 91 ILE HD1 H -0.218 . 1 1014 91 91 ILE C C 174.157 . 1 1015 91 91 ILE CA C 56.559 . 1 1016 91 91 ILE CB C 40.807 . 1 1017 91 91 ILE CG1 C 26.024 . 1 1018 91 91 ILE CG2 C 17.681 . 1 1019 91 91 ILE CD1 C 11.896 . 1 1020 91 91 ILE N N 119.489 . 1 1021 92 92 PRO HG2 H 1.886 . 1 1022 92 92 PRO HG3 H 1.886 . 1 1023 92 92 PRO HD2 H 3.292 . 1 1024 92 92 PRO HD3 H 3.671 . 1 1025 92 92 PRO CA C 61.646 . 1 1026 92 92 PRO CB C 30.840 . 1 1027 92 92 PRO CG C 26.596 . 1 1028 92 92 PRO CD C 51.700 . 1 1029 93 93 PRO HA H 3.576 . 1 1030 93 93 PRO HB2 H 1.479 . 1 1031 93 93 PRO HB3 H 2.152 . 1 1032 93 93 PRO HG2 H 1.639 . 1 1033 93 93 PRO HG3 H 1.951 . 1 1034 93 93 PRO HD2 H 3.390 . 1 1035 93 93 PRO HD3 H 3.703 . 1 1036 93 93 PRO C C 175.585 . 1 1037 93 93 PRO CA C 63.497 . 1 1038 93 93 PRO CB C 32.855 . 1 1039 93 93 PRO CG C 27.738 . 1 1040 93 93 PRO CD C 50.767 . 1 1041 94 94 HIS H H 7.898 . 1 1042 94 94 HIS HA H 3.755 . 1 1043 94 94 HIS HB2 H 3.115 . 1 1044 94 94 HIS HB3 H 3.151 . 1 1045 94 94 HIS HD2 H 6.889 . 1 1046 94 94 HIS HE1 H 7.796 . 1 1047 94 94 HIS C C 173.566 . 1 1048 94 94 HIS CA C 56.998 . 1 1049 94 94 HIS CB C 27.968 . 1 1050 94 94 HIS CD2 C 119.647 . 1 1051 94 94 HIS CE1 C 138.302 . 1 1052 94 94 HIS N N 115.741 . 1 1053 95 95 ALA H H 7.654 . 1 1054 95 95 ALA HA H 4.414 . 1 1055 95 95 ALA HB H 1.193 . 1 1056 95 95 ALA C C 177.121 . 1 1057 95 95 ALA CA C 52.613 . 1 1058 95 95 ALA CB C 20.539 . 1 1059 95 95 ALA N N 121.864 . 1 1060 96 96 THR H H 8.431 . 1 1061 96 96 THR HA H 4.554 . 1 1062 96 96 THR HB H 3.899 . 1 1063 96 96 THR HG2 H 0.968 . 1 1064 96 96 THR C C 173.585 . 1 1065 96 96 THR CA C 63.718 . 1 1066 96 96 THR CB C 69.512 . 1 1067 96 96 THR CG2 C 20.875 . 1 1068 96 96 THR N N 123.977 . 1 1069 97 97 LEU H H 8.637 . 1 1070 97 97 LEU HA H 5.058 . 1 1071 97 97 LEU HB2 H 1.463 . 1 1072 97 97 LEU HB3 H 1.693 . 1 1073 97 97 LEU HG H 1.767 . 1 1074 97 97 LEU HD1 H 0.748 . 1 1075 97 97 LEU HD2 H 1.158 . 1 1076 97 97 LEU C C 174.829 . 1 1077 97 97 LEU CA C 52.810 . 1 1078 97 97 LEU CB C 46.469 . 1 1079 97 97 LEU CG C 26.991 . 1 1080 97 97 LEU CD1 C 23.600 . 1 1081 97 97 LEU CD2 C 26.991 . 1 1082 97 97 LEU N N 124.657 . 1 1083 98 98 VAL H H 8.657 . 1 1084 98 98 VAL HA H 5.185 . 1 1085 98 98 VAL HB H 1.682 . 1 1086 98 98 VAL HG1 H 0.744 . 1 1087 98 98 VAL HG2 H 0.831 . 1 1088 98 98 VAL C C 175.008 . 1 1089 98 98 VAL CA C 60.606 . 1 1090 98 98 VAL CB C 34.035 . 1 1091 98 98 VAL CG1 C 21.150 . 1 1092 98 98 VAL CG2 C 20.852 . 1 1093 98 98 VAL N N 121.211 . 1 1094 99 99 PHE H H 9.640 . 1 1095 99 99 PHE HA H 5.721 . 1 1096 99 99 PHE HB2 H 2.698 . 1 1097 99 99 PHE HB3 H 2.621 . 1 1098 99 99 PHE HD1 H 6.994 . 1 1099 99 99 PHE HD2 H 6.994 . 1 1100 99 99 PHE HE1 H 7.141 . 1 1101 99 99 PHE HE2 H 7.141 . 1 1102 99 99 PHE HZ H 7.545 . 1 1103 99 99 PHE C C 174.049 . 1 1104 99 99 PHE CA C 55.122 . 1 1105 99 99 PHE CB C 43.179 . 1 1106 99 99 PHE CD1 C 131.430 . 1 1107 99 99 PHE CD2 C 131.430 . 1 1108 99 99 PHE CE1 C 132.018 . 1 1109 99 99 PHE CE2 C 132.018 . 1 1110 99 99 PHE CZ C 130.698 . 1 1111 99 99 PHE N N 123.247 . 1 1112 100 100 ASP H H 8.730 . 1 1113 100 100 ASP HA H 5.095 . 1 1114 100 100 ASP HB2 H 2.387 . 1 1115 100 100 ASP HB3 H 2.760 . 1 1116 100 100 ASP C C 176.700 . 1 1117 100 100 ASP CA C 52.725 . 1 1118 100 100 ASP CB C 41.940 . 1 1119 100 100 ASP N N 124.300 . 1 1120 101 101 VAL H H 9.471 . 1 1121 101 101 VAL HA H 4.968 . 1 1122 101 101 VAL HB H 1.700 . 1 1123 101 101 VAL HG1 H 0.612 . 1 1124 101 101 VAL HG2 H 0.650 . 1 1125 101 101 VAL C C 172.409 . 1 1126 101 101 VAL CA C 61.058 . 1 1127 101 101 VAL CB C 35.109 . 1 1128 101 101 VAL CG1 C 22.561 . 1 1129 101 101 VAL CG2 C 21.031 . 1 1130 101 101 VAL N N 126.301 . 1 1131 102 102 GLU H H 9.224 . 1 1132 102 102 GLU HA H 5.334 . 1 1133 102 102 GLU HB2 H 1.543 . 1 1134 102 102 GLU HB3 H 1.975 . 1 1135 102 102 GLU HG2 H 1.815 . 1 1136 102 102 GLU HG3 H 1.815 . 1 1137 102 102 GLU C C 174.986 . 1 1138 102 102 GLU CA C 53.911 . 1 1139 102 102 GLU CB C 33.527 . 1 1140 102 102 GLU CG C 35.608 . 1 1141 102 102 GLU N N 128.307 . 1 1142 103 103 LEU H H 8.561 . 1 1143 103 103 LEU HA H 4.608 . 1 1144 103 103 LEU HB2 H 0.973 . 1 1145 103 103 LEU HB3 H 2.156 . 1 1146 103 103 LEU HG H 1.210 . 1 1147 103 103 LEU HD1 H 0.709 . 1 1148 103 103 LEU HD2 H 0.573 . 1 1149 103 103 LEU C C 174.076 . 1 1150 103 103 LEU CA C 53.897 . 1 1151 103 103 LEU CB C 41.366 . 1 1152 103 103 LEU CG C 28.205 . 1 1153 103 103 LEU CD1 C 23.101 . 1 1154 103 103 LEU CD2 C 26.014 . 1 1155 103 103 LEU N N 128.227 . 1 1156 104 104 LEU H H 8.967 . 1 1157 104 104 LEU HA H 4.122 . 1 1158 104 104 LEU HB2 H 1.379 . 1 1159 104 104 LEU HB3 H 1.411 . 1 1160 104 104 LEU HG H 1.636 . 1 1161 104 104 LEU HD1 H 0.609 . 1 1162 104 104 LEU HD2 H 0.746 . 1 1163 104 104 LEU C C 177.774 . 1 1164 104 104 LEU CA C 57.195 . 1 1165 104 104 LEU CB C 42.871 . 1 1166 104 104 LEU CG C 26.856 . 1 1167 104 104 LEU CD1 C 26.165 . 1 1168 104 104 LEU CD2 C 22.378 . 1 1169 104 104 LEU N N 128.654 . 1 1170 105 105 LYS H H 7.581 . 1 1171 105 105 LYS HA H 4.259 . 1 1172 105 105 LYS HB2 H 1.610 . 1 1173 105 105 LYS HB3 H 1.692 . 1 1174 105 105 LYS HG2 H 1.147 . 1 1175 105 105 LYS HG3 H 1.077 . 1 1176 105 105 LYS HD2 H 1.496 . 1 1177 105 105 LYS HD3 H 1.496 . 1 1178 105 105 LYS HE2 H 2.789 . 1 1179 105 105 LYS HE3 H 2.849 . 1 1180 105 105 LYS C C 175.010 . 1 1181 105 105 LYS CA C 55.423 . 1 1182 105 105 LYS CB C 34.919 . 1 1183 105 105 LYS CG C 23.927 . 1 1184 105 105 LYS CD C 29.208 . 1 1185 105 105 LYS CE C 41.897 . 1 1186 105 105 LYS N N 112.127 . 1 1187 106 106 LEU H H 8.155 . 1 1188 106 106 LEU HA H 5.162 . 1 1189 106 106 LEU HB2 H 1.101 . 1 1190 106 106 LEU HB3 H 1.466 . 1 1191 106 106 LEU HG H 1.261 . 1 1192 106 106 LEU HD1 H 0.777 . 1 1193 106 106 LEU HD2 H 0.569 . 1 1194 106 106 LEU C C 175.828 . 1 1195 106 106 LEU CA C 53.074 . 1 1196 106 106 LEU CB C 44.248 . 1 1197 106 106 LEU CG C 25.683 . 1 1198 106 106 LEU CD1 C 25.644 . 1 1199 106 106 LEU CD2 C 25.684 . 1 1200 106 106 LEU N N 120.474 . 1 1201 107 107 GLU H H 8.924 . 1 1202 107 107 GLU HA H 4.229 . 1 1203 107 107 GLU HB2 H 1.586 . 1 1204 107 107 GLU HB3 H 1.919 . 1 1205 107 107 GLU HG2 H 1.803 . 1 1206 107 107 GLU HG3 H 1.876 . 1 1207 107 107 GLU C C 180.442 . 1 1208 107 107 GLU CA C 56.514 . 1 1209 107 107 GLU CB C 32.217 . 1 1210 107 107 GLU CG C 36.557 . 1 1211 107 107 GLU N N 126.905 . 1 stop_ save_