data_6457 #Corrected using PDB structure: 2D3GB # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 2 Q HA 5.26 4.52 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.01 -0.14 0.11 -0.27 0.34 0.07 # #bmr6457.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6457.str file): #HA CA CB CO N HN #N/A -0.01 -0.01 -0.27 +0.34 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.13 +/-0.16 +/-0.16 +/-0.36 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.902 0.979 0.997 0.890 0.894 0.750 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.126 0.557 0.649 0.659 1.477 0.287 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu Gabriel . . 2 Marquardt John L. . 3 Ottiger Marcel . . 4 Bax Ad . . stop_ _BMRB_accession_number 6457 _BMRB_flat_file_name bmr6457.str _Entry_type new _Submission_date 2005-01-13 _Accession_date 2005-01-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 397 "13C chemical shifts" 342 "15N chemical shifts" 83 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase ; _Citation_status published _Citation_type journal _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu Gabriel . . 2 Marquardt John L. . 3 Ottiger Marcel . . 4 Bax Ad . . stop_ _Journal_abbreviation "J. Am. Chem. Soc." _Journal_volume 120 _Journal_issue ? _Page_first 6836 _Page_last 6837 _Year 1998 loop_ _Keyword Ubiquitin "Liquid Crystal" stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "Ubiqutin" _Abbreviation_common "Ubiqutin" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ubiquitin $Ub stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not present" save_ ######################## # Monomeric polymers # ######################## save_Ub _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ubiquitin _Name_variant Ubiquitin _Abbreviation_common Ubiquitin _Molecular_mass 8579.94 _Mol_thiol_state "not present" loop_ _Biological_function Protein stop_ ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ILE 4 PHE 5 VAL 6 LYS 7 THR 8 LEU 9 THR 10 GLY 11 LYS 12 THR 13 ILE 14 THR 15 LEU 16 GLU 17 VAL 18 GLU 19 PRO 20 SER 21 ASP 22 THR 23 ILE 24 GLU 25 ASN 26 VAL 27 LYS 28 ALA 29 LYS 30 ILE 31 GLN 32 ASP 33 LYS 34 GLU 35 GLY 36 ILE 37 PRO 38 PRO 39 ASP 40 GLN 41 GLN 42 ARG 43 LEU 44 ILE 45 PHE 46 ALA 47 GLY 48 LYS 49 GLN 50 LEU 51 GLU 52 ASP 53 GLY 54 ARG 55 THR 56 LEU 57 SER 58 ASP 59 TYR 60 ASN 61 ILE 62 GLN 63 LYS 64 GLU 65 SER 66 THR 67 LEU 68 HIS 69 LEU 70 VAL 71 LEU 72 ARG 73 LEU 74 ARG 75 GLY 76 GLY stop_ _Sequence_homology_query_date 2006-01-30 _Sequence_homology_query_revised_last_date 2006-01-24 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 4245 ubiquitin 100.00 76 100 100 6e-36 BMRB 4375 Ubiquitin 100.00 76 100 100 6e-36 BMRB 5387 ubiquitin 100.00 76 100 100 6e-36 BMRB 6470 Ubiquitin 100.00 76 100 100 6e-36 BMRB 68 ubiquitin 100.00 76 100 100 6e-36 PDB 1XD3 "B Chain B, Crystal Structure Of Uchl3-UbvmeComplex" 101.33 75 100 100 3e-35 PDB 1AAR "A Chain A, Di-Ubiquitin" 100.00 76 100 100 6e-36 PDB 1CMX "B Chain B, Structural Basis For TheSpecificity Of Ubiquitin C- Terminal Hydrolases" 100.00 76 100 100 3e-35 PDB 1D3Z "A Chain A, Ubiquitin Nmr Structure" 100.00 76 100 100 6e-36 PDB 1F9J "A Chain A, Structure Of A New Crystal FormOf Tetraubiquitin" 100.00 76 100 100 6e-36 PDB 1FXT "B Chain B, Structure Of A ConjugatingEnzyme-Ubiquitin Thiolester Complex" 100.00 76 100 100 6e-36 PDB 1G6J "A Chain A, Structure Of Recombinant HumanUbiquitin In Aot Reverse Micelles" 100.00 76 100 100 2e-35 PDB 1NBF "C Chain C, Crystal Structure Of A Ubp-FamilyDeubiquitinating Enzyme In Isolation And In ComplexWith Ubiquitin Aldehyde" 100.00 76 100 100 3e-35 PDB 1P3Q "U Chain U, Mechanism Of UbiquitinRecognition By The Cue Domain Of Vps9" 100.00 76 100 100 6e-36 PDB 1Q5W "B Chain B, Ubiquitin Recognition By Npl4Zinc-Fingers" 100.00 76 100 100 6e-36 PDB 1S1Q "B Chain B, Tsg101(Uev) Domain In ComplexWith Ubiquitin" 100.00 76 100 100 2e-35 PDB 1TBE "A Chain A, Tetraubiquitin" 100.00 76 100 100 6e-36 PDB 1UBI "Synthetic, Structural And Biological StudiesOf The Ubiquitin System: Chemically Synthesized AndNative Ubiquitin Fold Into Identical Three-DimensionalStructures." 100.00 76 100 100 6e-36 PDB 1UBQ Ubiquitin 100.00 76 100 100 6e-36 PDB 1UZX "B Chain B, A Complex Of The Vps23 Uev WithUbiquitin" 100.00 76 100 100 6e-36 PDB 1V80 "A Chain A, Solution Structures Of UbiquitinAt 30 Bar And 3 Kbar" 100.00 76 100 100 6e-36 PDB 1V81 "A Chain A, Solution Structures Of UbiquitinAt 30 Bar And 3 Kbar" 100.00 76 100 100 6e-36 PDB 1WR6 "E Chain E, Crystal Structure Of Gga3 GatDomain In Complex With Ubiquitin" 100.00 76 100 100 6e-36 PDB 1WRD "B Chain B, Crystal Structure Of Tom1 GatDomain In Complex With Ubiquitin" 100.00 76 100 100 6e-36 PDB 1XQQ "A Chain A, Simultaneous Determination OfProtein Structure And Dynamics" 100.00 76 100 100 6e-36 PDB 1YD8 "U Chain U, Complex Of Human Gga3 Gat DomainAnd Ubiquitin" 100.00 76 100 100 6e-36 PDB 2AYO "B Chain B, Structure Of Usp14 Bound ToUbquitin Aldehyde" 100.00 76 100 100 3e-35 PDB 2BGF "A Chain A, Nmr Structure Of Lys48-LinkedDi-Ubiquitin Using Chemical Shift Perturbation DataTogether With Rdcs And 15n- Relaxation Data" 100.00 76 100 100 2e-35 PDB 1YIW "A Chain A, X-Ray Crystal Structure Of AChemically Synthesized Ubiquitin" 100.00 76 99 100 10e-36 PDB 1YX5 "B Chain B, Solution Structure Of S5aUim-1UBIQUITIN COMPLEX" 77.55 98 100 100 6e-36 PDB 1YX6 "B Chain B, Solution Structure Of S5aUim-2UBIQUITIN COMPLEX" 77.55 98 100 100 6e-36 DBJ BAA76676.1 "polyubiquitin [Bombyx mori]" 8.32 913 100 100 6e-36 DBJ BAA76676.1 "polyubiquitin [Bombyx mori]" 8.32 913 99 99 5e-35 DBJ BAA76676.1 "polyubiquitin [Bombyx mori]" 8.32 913 99 99 5e-35 DBJ BAA76676.1 "polyubiquitin [Bombyx mori]" 8.32 913 99 99 5e-35 DBJ BAA76676.1 "polyubiquitin [Bombyx mori]" 8.32 913 99 99 5e-35 EMBL CAA63349.1 "polyubiquitin [Rattus norvegicus]" 76.00 100 100 100 6e-36 EMBL CAA64326.1 "ubiquitin [Carabus alpestris]" 54.68 139 100 100 6e-36 EMBL CAA64326.1 "ubiquitin [Carabus alpestris]" 54.68 139 100 100 2e-28 EMBL CAA52416.1 "polyubiquitin [Artemia franciscana]" 10.90 697 100 100 6e-36 EMBL CAA52416.1 "polyubiquitin [Artemia franciscana]" 10.90 697 100 100 6e-36 GenBank AAV90707.1 "ribosomal protein S27a [Aedesalbopictus]" 48.72 156 100 100 6e-36 GenBank AAV84265.1 "ubiquitin [Culicoides sonorensis]" 45.51 167 100 100 6e-36 GenBank AAV84266.1 "ubiquitin [Culicoides sonorensis]" 39.79 191 100 100 6e-36 GenBank AAV84266.1 "ubiquitin [Culicoides sonorensis]" 39.79 191 100 100 6e-36 GenBank AAV84266.1 "ubiquitin [Culicoides sonorensis]" 39.79 191 100 100 7e-14 PIR I52328 "ubiquitin / ribosomal protein S27a,cytosolic [validated] - rat" 48.72 156 100 100 6e-36 PIR UQHUR7 "ubiquitin / ribosomal protein S27a,cytosolic [validated] - human" 48.72 156 100 100 6e-36 PIR S13928 "ubiquitin precursor - chicken" 33.19 229 100 100 6e-36 PIR I50437 "polyubiquitin 4 - chicken" 24.92 305 100 100 6e-36 PIR S21083 "polyubiquitin 5 - Chinese hamster" 19.95 381 100 100 6e-36 PRF 1212243A "ubiquitin S1" 100.00 76 100 100 6e-36 PRF 1212243C "ubiquitin S3" 100.00 76 100 100 6e-36 PRF 1212243J "ubiquitin S7(2)" 100.00 76 100 100 6e-36 PRF 1908225A ubiquitin 24.92 305 100 100 6e-36 PRF 1908225A ubiquitin 24.92 305 100 100 6e-36 REF NP_066289.2 "ubiquitin C [Homo sapiens]" 11.09 685 100 100 6e-36 REF NP_066289.2 "ubiquitin C [Homo sapiens]" 11.09 685 100 100 6e-36 REF NP_066289.2 "ubiquitin C [Homo sapiens]" 11.09 685 100 100 6e-36 REF NP_066289.2 "ubiquitin C [Homo sapiens]" 11.09 685 100 100 6e-36 REF NP_066289.2 "ubiquitin C [Homo sapiens]" 11.09 685 100 100 6e-36 SWISS-PROT P62972 "UBIQ_XENLA Ubiquitin" 100.00 76 100 100 6e-36 SWISS-PROT P62974 "UBIQ_PIG Ubiquitin" 100.00 76 100 100 6e-36 SWISS-PROT P62989 "UBIQ_RAT Ubiquitin" 100.00 76 100 100 6e-36 SWISS-PROT P68195 "UBIQ_SPOFR Ubiquitin" 100.00 76 100 100 6e-36 SWISS-PROT Q867C4 "UBIQ_PONPY Ubiquitin" 100.00 76 100 100 6e-36 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ub 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 $Ub "recombinant technology" "E. coli" Escherichia coli ? ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type bicelle _Details ; Using 5% w/v bicelles in 93% H2O, &% D2O, with a 3:1 ratio of DMPC:DHPC at 304 K. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ub 0.7 mM "[U-13C; U-15N]" phosphate 10 mM ? H20 93 % ? D20 7 % ? DMPC:DHPC(3:1) 5 "w/v %" ? stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model ? _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCO 1H-15N HSQC ; save_ ####################### # Sample conditions # ####################### save_conditions_292K _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0 pH temperature 292 0 K stop_ save_ save_conditions_298K _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0 pH temperature 298 0 K stop_ save_ save_conditions_304K _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0 pH temperature 304 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference 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 TSP H 1 protons ppm 0 direct internal ? ? ? 1.0 TSP C 13 "methyl carbon" ppm 1 direct internal ? ? ? ? stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_292K _Saveframe_category assigned_chemical_shifts loop_ _Experiment_label $1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_292K _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Ubiquitin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET HA H 4.23 . . 2 1 MET HB2 H 2.08 . . 3 1 MET HG2 H 2.02 . . 4 1 MET HE H 1.66 . . 5 1 MET C C 170.27 . . 6 1 MET CA C 54.44 . . 7 1 MET CB C 33.26 . . 8 1 MET CG C 30.94 . . 9 1 MET CE C 17.85 . . 10 2 GLN H H 8.90 . . 11 2 GLN HA H 5.25 . . 12 2 GLN HB2 H 1.87 . . 13 2 GLN HB3 H 1.69 . . 14 2 GLN HG2 H 1.81 . . 15 2 GLN HE21 H 7.65 . . 16 2 GLN HE22 H 6.79 . . 17 2 GLN C C 175.65 . . 18 2 GLN CA C 55.07 . . 19 2 GLN CB C 30.75 . . 20 2 GLN CG C 34.62 . . 21 2 GLN N N 123.56 . . 22 2 GLN NE2 N 111.95 . . 23 3 ILE H H 8.32 . . 24 3 ILE HA H 4.21 . . 25 3 ILE HB H 1.79 . . 26 3 ILE HG12 H 0.83 . . 27 3 ILE HG2 H 0.65 . . 28 3 ILE HD1 H 0.60 . . 29 3 ILE C C 172.18 . . 30 3 ILE CA C 59.56 . . 31 3 ILE CB C 42.20 . . 32 3 ILE CG1 C 25.16 . . 33 3 ILE CG2 C 17.97 . . 34 3 ILE CD1 C 14.32 . . 35 3 ILE N N 115.68 . . 36 4 PHE H H 8.61 . . 37 4 PHE HA H 5.63 . . 38 4 PHE HB2 H 2.88 . . 39 4 PHE HB3 H 3.06 . . 40 4 PHE HD1 H 7.08 . . 41 4 PHE HE1 H 7.25 . . 42 4 PHE C C 175.05 . . 43 4 PHE CA C 55.20 . . 44 4 PHE CB C 41.47 . . 45 4 PHE CD1 C 132.20 . . 46 4 PHE CE1 C 131.12 . . 47 4 PHE N N 118.45 . . 48 5 VAL H H 9.30 . . 49 5 VAL HA H 4.72 . . 50 5 VAL HB H 1.92 . . 51 5 VAL HG1 H 0.70 . . 52 5 VAL HG2 H 0.74 . . 53 5 VAL C C 174.60 . . 54 5 VAL CA C 60.61 . . 55 5 VAL CB C 34.22 . . 56 5 VAL CG1 C 22.48 . . 57 5 VAL CG2 C 20.92 . . 58 5 VAL N N 121.34 . . 59 6 LYS H H 8.82 . . 60 6 LYS HA H 5.37 . . 61 6 LYS HB2 H 1.35 . . 62 6 LYS HB3 H 1.67 . . 63 6 LYS HG2 H 1.29 . . 64 6 LYS HD2 H 1.58 . . 65 6 LYS HE2 H 2.91 . . 66 6 LYS C C 176.87 . . 67 6 LYS CA C 54.51 . . 68 6 LYS CB C 35.04 . . 69 6 LYS CG C 25.14 . . 70 6 LYS CD C 29.24 . . 71 6 LYS CE C 41.81 . . 72 6 LYS N N 127.86 . . 73 7 THR H H 8.73 . . 74 7 THR HA H 4.97 . . 75 7 THR HB H 4.82 . . 76 7 THR HG2 H 1.20 . . 77 7 THR C C 176.64 . . 78 7 THR CA C 60.46 . . 79 7 THR CB C 70.62 . . 80 7 THR CG2 C 21.56 . . 81 7 THR N N 115.74 . . 82 8 LEU H H 9.10 . . 83 8 LEU HA H 4.31 . . 84 8 LEU HB2 H 1.78 . . 85 8 LEU HB3 H 1.94 . . 86 8 LEU HG H 1.88 . . 87 8 LEU HD1 H 1.05 . . 88 8 LEU HD2 H 0.99 . . 89 8 LEU C C 178.53 . . 90 8 LEU CA C 57.57 . . 91 8 LEU CB C 41.96 . . 92 8 LEU CG C 27.37 . . 93 8 LEU CD1 C 25.32 . . 94 8 LEU CD2 C 23.91 . . 95 8 LEU N N 121.67 . . 96 9 THR H H 7.63 . . 97 9 THR HA H 4.43 . . 98 9 THR HB H 4.59 . . 99 9 THR HG2 H 1.27 . . 100 9 THR C C 175.25 . . 101 9 THR CA C 61.39 . . 102 9 THR CB C 69.13 . . 103 9 THR CG2 C 21.88 . . 104 9 THR N N 105.93 . . 105 10 GLY H H 7.81 . . 106 10 GLY HA2 H 3.61 . . 107 10 GLY C C 173.80 . . 108 10 GLY CA C 45.45 . . 109 10 GLY N N 109.23 . . 110 11 LYS H H 7.28 . . 111 11 LYS HA H 4.36 . . 112 11 LYS HB2 H 1.72 . . 113 11 LYS HB3 H 1.82 . . 114 11 LYS HG2 H 1.27 . . 115 11 LYS HD2 H 1.65 . . 116 11 LYS HE2 H 2.94 . . 117 11 LYS C C 175.67 . . 118 11 LYS CA C 56.27 . . 119 11 LYS CB C 33.19 . . 120 11 LYS CG C 25.08 . . 121 11 LYS CD C 29.20 . . 122 11 LYS CE C 41.87 . . 123 11 LYS N N 121.94 . . 124 12 THR H H 8.65 . . 125 12 THR HA H 5.05 . . 126 12 THR HB H 3.95 . . 127 12 THR HG2 H 1.10 . . 128 12 THR C C 174.05 . . 129 12 THR CA C 62.38 . . 130 12 THR CB C 69.90 . . 131 12 THR CG2 C 22.04 . . 132 12 THR N N 120.78 . . 133 13 ILE H H 9.45 . . 134 13 ILE HA H 4.54 . . 135 13 ILE HB H 1.88 . . 136 13 ILE HG12 H 1.10 . . 137 13 ILE HG2 H 0.88 . . 138 13 ILE HD1 H 0.73 . . 139 13 ILE C C 174.95 . . 140 13 ILE CA C 59.97 . . 141 13 ILE CB C 40.94 . . 142 13 ILE CG1 C 27.00 . . 143 13 ILE CG2 C 17.88 . . 144 13 ILE CD1 C 14.47 . . 145 13 ILE N N 127.45 . . 146 14 THR H H 8.71 . . 147 14 THR HA H 4.96 . . 148 14 THR HB H 4.03 . . 149 14 THR HG2 H 1.13 . . 150 14 THR C C 173.52 . . 151 14 THR CA C 61.93 . . 152 14 THR CB C 69.64 . . 153 14 THR CG2 C 21.86 . . 154 14 THR N N 121.86 . . 155 15 LEU H H 8.71 . . 156 15 LEU HA H 4.78 . . 157 15 LEU HB2 H 1.22 . . 158 15 LEU HB3 H 1.36 . . 159 15 LEU HG H 1.43 . . 160 15 LEU HD1 H 0.71 . . 161 15 LEU HD2 H 0.78 . . 162 15 LEU C C 174.40 . . 163 15 LEU CA C 52.82 . . 164 15 LEU CB C 47.06 . . 165 15 LEU CG C 26.85 . . 166 15 LEU CD1 C 27.16 . . 167 15 LEU CD2 C 24.26 . . 168 15 LEU N N 125.14 . . 169 16 GLU H H 8.14 . . 170 16 GLU HA H 4.92 . . 171 16 GLU HB2 H 1.94 . . 172 16 GLU HB3 H 1.85 . . 173 16 GLU HG2 H 2.16 . . 174 16 GLU C C 175.59 . . 175 16 GLU CA C 54.81 . . 176 16 GLU CB C 29.44 . . 177 16 GLU CG C 34.90 . . 178 16 GLU N N 122.50 . . 179 17 VAL H H 8.90 . . 180 17 VAL HA H 4.71 . . 181 17 VAL HB H 2.33 . . 182 17 VAL HG1 H 0.72 . . 183 17 VAL HG2 H 0.45 . . 184 17 VAL C C 173.89 . . 185 17 VAL CA C 58.42 . . 186 17 VAL CB C 36.39 . . 187 17 VAL CG1 C 22.33 . . 188 17 VAL CG2 C 19.60 . . 189 17 VAL N N 117.55 . . 190 18 GLU H H 8.64 . . 191 18 GLU HA H 5.08 . . 192 18 GLU HB2 H 2.20 . . 193 18 GLU HB3 H 1.63 . . 194 18 GLU HG2 H 2.31 . . 195 18 GLU C C 175.89 . . 196 18 GLU CA C 52.71 . . 197 18 GLU CB C 30.30 . . 198 18 GLU CG C 34.28 . . 199 18 GLU N N 119.33 . . 200 19 PRO HA H 4.14 . . 201 19 PRO HB2 H 2.45 . . 202 19 PRO HB3 H 2.02 . . 203 19 PRO HG2 H 2.08 . . 204 19 PRO HD2 H 3.82 . . 205 19 PRO C C 175.04 . . 206 19 PRO CA C 65.46 . . 207 19 PRO CB C 31.94 . . 208 19 PRO CG C 28.02 . . 209 19 PRO CD C 50.57 . . 210 19 PRO N N 134.12 . . 211 20 SER H H 7.04 . . 212 20 SER HA H 4.37 . . 213 20 SER HB2 H 3.79 . . 214 20 SER HB3 H 4.15 . . 215 20 SER C C 174.39 . . 216 20 SER CA C 57.39 . . 217 20 SER CB C 63.36 . . 218 20 SER N N 103.74 . . 219 21 ASP H H 8.03 . . 220 21 ASP HA H 4.70 . . 221 21 ASP HB2 H 2.54 . . 222 21 ASP HB3 H 2.96 . . 223 21 ASP C C 176.09 . . 224 21 ASP CA C 55.69 . . 225 21 ASP CB C 40.79 . . 226 21 ASP N N 123.82 . . 227 22 THR H H 7.90 . . 228 22 THR HA H 4.92 . . 229 22 THR HB H 4.83 . . 230 22 THR HG2 H 1.28 . . 231 22 THR C C 176.48 . . 232 22 THR CA C 59.68 . . 233 22 THR CB C 71.19 . . 234 22 THR CG2 C 22.18 . . 235 22 THR N N 109.14 . . 236 23 ILE H H 8.56 . . 237 23 ILE HA H 3.66 . . 238 23 ILE HB H 2.57 . . 239 23 ILE HG12 H 1.29 . . 240 23 ILE HG2 H 0.79 . . 241 23 ILE HD1 H 0.58 . . 242 23 ILE C C 178.77 . . 243 23 ILE CA C 62.25 . . 244 23 ILE CB C 34.34 . . 245 23 ILE CG1 C 27.93 . . 246 23 ILE CG2 C 18.11 . . 247 23 ILE CD1 C 9.47 . . 248 23 ILE N N 121.53 . . 249 24 GLU H H 9.76 . . 250 24 GLU HA H 3.92 . . 251 24 GLU HB2 H 2.06 . . 252 24 GLU HG2 H 2.39 . . 253 24 GLU C C 178.37 . . 254 24 GLU CA C 60.21 . . 255 24 GLU CB C 28.27 . . 256 24 GLU CG C 34.66 . . 257 24 GLU N N 121.17 . . 258 25 ASN H H 7.92 . . 259 25 ASN HA H 4.53 . . 260 25 ASN HB2 H 2.87 . . 261 25 ASN HB3 H 3.21 . . 262 25 ASN HD21 H 7.82 . . 263 25 ASN HD22 H 6.89 . . 264 25 ASN C C 178.11 . . 265 25 ASN CA C 56.05 . . 266 25 ASN CB C 38.44 . . 267 25 ASN N N 120.91 . . 268 25 ASN ND2 N 109.70 . . 269 26 VAL H H 8.07 . . 270 26 VAL HA H 3.40 . . 271 26 VAL HB H 2.36 . . 272 26 VAL HG1 H 0.70 . . 273 26 VAL HG2 H 0.99 . . 274 26 VAL C C 177.68 . . 275 26 VAL CA C 67.65 . . 276 26 VAL CB C 30.83 . . 277 26 VAL CG1 C 21.55 . . 278 26 VAL CG2 C 23.67 . . 279 26 VAL N N 122.05 . . 280 27 LYS H H 8.56 . . 281 27 LYS HA H 4.58 . . 282 27 LYS HB2 H 1.44 . . 283 27 LYS HB3 H 2.05 . . 284 27 LYS HG2 H 1.39 . . 285 27 LYS HD2 H 1.66 . . 286 27 LYS HE2 H 2.64 . . 287 27 LYS C C 180.28 . . 288 27 LYS CA C 59.24 . . 289 27 LYS CB C 33.72 . . 290 27 LYS CG C 26.27 . . 291 27 LYS CD C 30.39 . . 292 27 LYS CE C 42.38 . . 293 27 LYS N N 119.20 . . 294 28 ALA H H 8.06 . . 295 28 ALA HA H 4.16 . . 296 28 ALA HB H 1.64 . . 297 28 ALA C C 180.03 . . 298 28 ALA CA C 55.36 . . 299 28 ALA CB C 17.70 . . 300 28 ALA N N 123.78 . . 301 29 LYS H H 7.85 . . 302 29 LYS HA H 4.21 . . 303 29 LYS HB2 H 1.94 . . 304 29 LYS HB3 H 2.15 . . 305 29 LYS HG2 H 1.60 . . 306 29 LYS HD2 H 1.48 . . 307 29 LYS HE2 H 2.99 . . 308 29 LYS C C 180.05 . . 309 29 LYS CA C 59.64 . . 310 29 LYS CB C 33.28 . . 311 29 LYS CG C 26.47 . . 312 29 LYS CD C 30.06 . . 313 29 LYS CE C 42.31 . . 314 29 LYS N N 120.28 . . 315 30 ILE H H 8.28 . . 316 30 ILE HA H 3.51 . . 317 30 ILE HB H 2.37 . . 318 30 ILE HG12 H 0.71 . . 319 30 ILE HG2 H 0.71 . . 320 30 ILE HD1 H 0.90 . . 321 30 ILE C C 178.04 . . 322 30 ILE CA C 66.14 . . 323 30 ILE CB C 36.79 . . 324 30 ILE CG1 C 31.12 . . 325 30 ILE CG2 C 17.09 . . 326 30 ILE CD1 C 15.30 . . 327 30 ILE N N 121.42 . . 328 31 GLN H H 8.58 . . 329 31 GLN HA H 3.83 . . 330 31 GLN HB2 H 2.51 . . 331 31 GLN HB3 H 1.95 . . 332 31 GLN HG2 H 2.27 . . 333 31 GLN HE21 H 7.63 . . 334 31 GLN HE22 H 6.80 . . 335 31 GLN C C 178.62 . . 336 31 GLN CA C 59.99 . . 337 31 GLN CB C 27.71 . . 338 31 GLN CG C 33.72 . . 339 31 GLN N N 123.83 . . 340 31 GLN NE2 N 109.85 . . 341 32 ASP H H 8.01 . . 342 32 ASP HA H 4.35 . . 343 32 ASP HB2 H 2.81 . . 344 32 ASP HB3 H 2.89 . . 345 32 ASP C C 176.98 . . 346 32 ASP CA C 57.18 . . 347 32 ASP CB C 40.57 . . 348 32 ASP N N 119.70 . . 349 33 LYS H H 7.43 . . 350 33 LYS HA H 4.34 . . 351 33 LYS HB2 H 1.99 . . 352 33 LYS HB3 H 1.85 . . 353 33 LYS HG2 H 1.61 . . 354 33 LYS HD2 H 1.71 . . 355 33 LYS HE2 H 3.11 . . 356 33 LYS C C 177.60 . . 357 33 LYS CA C 58.04 . . 358 33 LYS CB C 34.16 . . 359 33 LYS CG C 25.36 . . 360 33 LYS CD C 28.86 . . 361 33 LYS CE C 42.02 . . 362 33 LYS N N 115.47 . . 363 34 GLU H H 8.74 . . 364 34 GLU HA H 4.62 . . 365 34 GLU HB2 H 1.72 . . 366 34 GLU HB3 H 2.27 . . 367 34 GLU HG2 H 2.20 . . 368 34 GLU C C 177.57 . . 369 34 GLU CA C 55.16 . . 370 34 GLU CB C 32.65 . . 371 34 GLU CG C 35.18 . . 372 34 GLU N N 114.21 . . 373 35 GLY H H 8.53 . . 374 35 GLY HA2 H 3.93 . . 375 35 GLY C C 173.69 . . 376 35 GLY CA C 46.07 . . 377 35 GLY N N 108.99 . . 378 36 ILE H H 6.15 . . 379 36 ILE HA H 4.45 . . 380 36 ILE HB H 1.41 . . 381 36 ILE HG12 H 1.10 . . 382 36 ILE HG2 H 0.95 . . 383 36 ILE HD1 H 0.79 . . 384 36 ILE C C 173.32 . . 385 36 ILE CA C 57.74 . . 386 36 ILE CB C 40.57 . . 387 36 ILE CG1 C 27.00 . . 388 36 ILE CG2 C 17.86 . . 389 36 ILE CD1 C 13.58 . . 390 36 ILE N N 120.22 . . 391 37 PRO HA H 4.63 . . 392 37 PRO HB2 H 1.97 . . 393 37 PRO HG2 H 2.05 . . 394 37 PRO HD2 H 3.58 . . 395 37 PRO C C 176.67 . . 396 37 PRO CA C 61.65 . . 397 37 PRO CB C 31.84 . . 398 37 PRO CG C 28.26 . . 399 37 PRO CD C 51.14 . . 400 37 PRO N N 141.58 . . 401 38 PRO HA H 4.12 . . 402 38 PRO HB2 H 2.23 . . 403 38 PRO HB3 H 2.06 . . 404 38 PRO HG2 H 1.62 . . 405 38 PRO HD2 H 3.76 . . 406 38 PRO C C 178.05 . . 407 38 PRO CA C 66.25 . . 408 38 PRO CB C 32.88 . . 409 38 PRO CG C 27.66 . . 410 38 PRO CD C 51.16 . . 411 38 PRO N N 135.27 . . 412 39 ASP H H 8.55 . . 413 39 ASP HA H 4.43 . . 414 39 ASP HB2 H 2.72 . . 415 39 ASP HB3 H 2.80 . . 416 39 ASP C C 176.82 . . 417 39 ASP CA C 55.63 . . 418 39 ASP CB C 39.53 . . 419 39 ASP N N 113.72 . . 420 40 GLN H H 7.82 . . 421 40 GLN HA H 4.46 . . 422 40 GLN HB2 H 2.46 . . 423 40 GLN HB3 H 1.84 . . 424 40 GLN HG2 H 2.41 . . 425 40 GLN HE21 H 7.63 . . 426 40 GLN HE22 H 6.74 . . 427 40 GLN C C 175.11 . . 428 40 GLN CA C 55.63 . . 429 40 GLN CB C 30.13 . . 430 40 GLN CG C 34.45 . . 431 40 GLN N N 117.12 . . 432 40 GLN NE2 N 110.75 . . 433 41 GLN H H 7.48 . . 434 41 GLN HA H 4.24 . . 435 41 GLN HB2 H 1.92 . . 436 41 GLN HG2 H 1.66 . . 437 41 GLN HE21 H 6.22 . . 438 41 GLN HE22 H 6.52 . . 439 41 GLN C C 176.03 . . 440 41 GLN CA C 56.46 . . 441 41 GLN CB C 31.64 . . 442 41 GLN CG C 33.47 . . 443 41 GLN N N 118.06 . . 444 41 GLN NE2 N 104.17 . . 445 42 ARG H H 8.53 . . 446 42 ARG HA H 4.50 . . 447 42 ARG HB2 H 1.64 . . 448 42 ARG HB3 H 1.73 . . 449 42 ARG HG2 H 1.42 . . 450 42 ARG HD2 H 3.06 . . 451 42 ARG C C 173.78 . . 452 42 ARG CA C 55.04 . . 453 42 ARG CB C 31.74 . . 454 42 ARG CG C 27.10 . . 455 42 ARG CD C 43.60 . . 456 42 ARG N N 123.02 . . 457 43 LEU H H 8.82 . . 458 43 LEU HA H 5.36 . . 459 43 LEU HB2 H 1.16 . . 460 43 LEU HB3 H 1.57 . . 461 43 LEU HG H 1.48 . . 462 43 LEU HD1 H 0.78 . . 463 43 LEU HD2 H 0.81 . . 464 43 LEU C C 175.02 . . 465 43 LEU CA C 52.97 . . 466 43 LEU CB C 45.78 . . 467 43 LEU CG C 27.27 . . 468 43 LEU CD1 C 26.54 . . 469 43 LEU CD2 C 24.30 . . 470 43 LEU N N 124.38 . . 471 44 ILE H H 9.03 . . 472 44 ILE HA H 4.99 . . 473 44 ILE HB H 1.69 . . 474 44 ILE HG12 H 1.06 . . 475 44 ILE HG2 H 0.69 . . 476 44 ILE HD1 H 0.69 . . 477 44 ILE C C 175.79 . . 478 44 ILE CA C 58.97 . . 479 44 ILE CB C 41.41 . . 480 44 ILE CG1 C 27.95 . . 481 44 ILE CG2 C 17.56 . . 482 44 ILE CD1 C 12.85 . . 483 44 ILE N N 122.26 . . 484 45 PHE H H 8.83 . . 485 45 PHE HA H 5.04 . . 486 45 PHE HB2 H 2.81 . . 487 45 PHE HB3 H 3.05 . . 488 45 PHE HD1 H 7.36 . . 489 45 PHE HE1 H 7.54 . . 490 45 PHE HZ H 7.49 . . 491 45 PHE C C 174.20 . . 492 45 PHE CA C 57.01 . . 493 45 PHE CB C 43.75 . . 494 45 PHE CD1 C 132.21 . . 495 45 PHE CE1 C 132.27 . . 496 45 PHE CZ C 130.25 . . 497 45 PHE N N 125.73 . . 498 46 ALA H H 8.81 . . 499 46 ALA HA H 3.69 . . 500 46 ALA HB H 0.91 . . 501 46 ALA C C 177.02 . . 502 46 ALA CA C 52.53 . . 503 46 ALA CB C 16.56 . . 504 46 ALA N N 132.54 . . 505 47 GLY H H 8.13 . . 506 47 GLY HA2 H 3.48 . . 507 47 GLY C C 173.54 . . 508 47 GLY CA C 45.34 . . 509 47 GLY N N 102.68 . . 510 48 LYS H H 7.98 . . 511 48 LYS HA H 4.62 . . 512 48 LYS HB2 H 1.87 . . 513 48 LYS HG2 H 1.53 . . 514 48 LYS HD2 H 1.87 . . 515 48 LYS HE2 H 3.17 . . 516 48 LYS C C 174.43 . . 517 48 LYS CA C 54.54 . . 518 48 LYS CB C 34.52 . . 519 48 LYS CG C 24.55 . . 520 48 LYS CD C 29.12 . . 521 48 LYS CE C 42.10 . . 522 48 LYS N N 121.91 . . 523 49 GLN H H 8.60 . . 524 49 GLN HA H 4.56 . . 525 49 GLN HB2 H 2.00 . . 526 49 GLN HG2 H 2.25 . . 527 49 GLN HE21 H 7.63 . . 528 49 GLN HE22 H 6.82 . . 529 49 GLN C C 175.40 . . 530 49 GLN CA C 55.73 . . 531 49 GLN CB C 28.99 . . 532 49 GLN CG C 34.62 . . 533 49 GLN N N 122.75 . . 534 49 GLN NE2 N 111.92 . . 535 50 LEU H H 8.53 . . 536 50 LEU HA H 4.09 . . 537 50 LEU HB2 H 1.03 . . 538 50 LEU HB3 H 1.50 . . 539 50 LEU HG H 1.50 . . 540 50 LEU HD1 H 0.53 . . 541 50 LEU HD2 H -0.15 . . 542 50 LEU C C 176.39 . . 543 50 LEU CA C 54.23 . . 544 50 LEU CB C 41.56 . . 545 50 LEU CG C 25.84 . . 546 50 LEU CD1 C 26.02 . . 547 50 LEU CD2 C 19.68 . . 548 50 LEU N N 125.86 . . 549 51 GLU H H 8.40 . . 550 51 GLU HA H 4.49 . . 551 51 GLU HB2 H 2.25 . . 552 51 GLU HB3 H 2.00 . . 553 51 GLU HG2 H 2.39 . . 554 51 GLU C C 175.60 . . 555 51 GLU CA C 55.95 . . 556 51 GLU CB C 31.56 . . 557 51 GLU CG C 36.00 . . 558 51 GLU N N 123.28 . . 559 52 ASP H H 8.16 . . 560 52 ASP HA H 4.36 . . 561 52 ASP HB2 H 2.68 . . 562 52 ASP HB3 H 2.57 . . 563 52 ASP C C 177.06 . . 564 52 ASP CA C 56.95 . . 565 52 ASP CB C 40.84 . . 566 52 ASP N N 120.37 . . 567 53 GLY H H 9.39 . . 568 53 GLY HA2 H 3.93 . . 569 53 GLY C C 174.60 . . 570 53 GLY CA C 45.16 . . 571 53 GLY N N 107.00 . . 572 54 ARG H H 7.46 . . 573 54 ARG HA H 4.70 . . 574 54 ARG HB2 H 2.08 . . 575 54 ARG HB3 H 2.23 . . 576 54 ARG HG2 H 1.63 . . 577 54 ARG HD2 H 3.08 . . 578 54 ARG C C 175.08 . . 579 54 ARG CA C 54.38 . . 580 54 ARG CB C 32.64 . . 581 54 ARG CG C 27.57 . . 582 54 ARG CD C 42.86 . . 583 54 ARG N N 119.39 . . 584 55 THR H H 8.73 . . 585 55 THR HA H 5.24 . . 586 55 THR HB H 4.55 . . 587 55 THR HG2 H 1.13 . . 588 55 THR C C 176.29 . . 589 55 THR CA C 59.68 . . 590 55 THR CB C 72.25 . . 591 55 THR CG2 C 22.26 . . 592 55 THR N N 108.74 . . 593 56 LEU H H 8.14 . . 594 56 LEU HA H 4.06 . . 595 56 LEU HB2 H 1.23 . . 596 56 LEU HB3 H 2.12 . . 597 56 LEU HG H 1.72 . . 598 56 LEU HD1 H 0.76 . . 599 56 LEU HD2 H 0.63 . . 600 56 LEU C C 180.54 . . 601 56 LEU CA C 58.70 . . 602 56 LEU CB C 40.36 . . 603 56 LEU CG C 26.92 . . 604 56 LEU CD1 C 26.86 . . 605 56 LEU CD2 C 23.36 . . 606 56 LEU N N 118.26 . . 607 57 SER H H 8.47 . . 608 57 SER HA H 4.27 . . 609 57 SER HB2 H 3.75 . . 610 57 SER HB3 H 3.85 . . 611 57 SER C C 178.04 . . 612 57 SER CA C 61.07 . . 613 57 SER CB C 62.52 . . 614 57 SER N N 113.67 . . 615 58 ASP H H 7.93 . . 616 58 ASP HA H 4.30 . . 617 58 ASP HB2 H 2.31 . . 618 58 ASP HB3 H 3.02 . . 619 58 ASP C C 177.13 . . 620 58 ASP CA C 57.17 . . 621 58 ASP CB C 40.09 . . 622 58 ASP N N 124.53 . . 623 59 TYR H H 7.25 . . 624 59 TYR HA H 4.67 . . 625 59 TYR HB2 H 3.47 . . 626 59 TYR HB3 H 2.54 . . 627 59 TYR HD1 H 7.26 . . 628 59 TYR HE1 H 6.90 . . 629 59 TYR C C 174.43 . . 630 59 TYR CA C 58.24 . . 631 59 TYR CB C 40.06 . . 632 59 TYR CD1 C 133.66 . . 633 59 TYR CE1 C 118.55 . . 634 59 TYR N N 115.85 . . 635 60 ASN H H 8.15 . . 636 60 ASN HA H 4.36 . . 637 60 ASN HB2 H 2.79 . . 638 60 ASN HB3 H 3.31 . . 639 60 ASN HD21 H 7.53 . . 640 60 ASN HD22 H 6.81 . . 641 60 ASN C C 174.07 . . 642 60 ASN CA C 54.11 . . 643 60 ASN CB C 37.40 . . 644 60 ASN N N 116.24 . . 645 60 ASN ND2 N 111.15 . . 646 61 ILE H H 7.25 . . 647 61 ILE HA H 3.39 . . 648 61 ILE HB H 1.41 . . 649 61 ILE HG12 H -0.30 . . 650 61 ILE HG2 H 0.49 . . 651 61 ILE HD1 H 0.42 . . 652 61 ILE C C 174.34 . . 653 61 ILE CA C 62.41 . . 654 61 ILE CB C 36.73 . . 655 61 ILE CG1 C 28.33 . . 656 61 ILE CG2 C 17.36 . . 657 61 ILE CD1 C 14.37 . . 658 61 ILE N N 118.94 . . 659 62 GLN H H 7.61 . . 660 62 GLN HA H 4.51 . . 661 62 GLN HB2 H 2.26 . . 662 62 GLN HB3 H 1.90 . . 663 62 GLN HG2 H 2.37 . . 664 62 GLN HE21 H 7.28 . . 665 62 GLN HE22 H 6.81 . . 666 62 GLN C C 175.70 . . 667 62 GLN CA C 53.65 . . 668 62 GLN CB C 31.64 . . 669 62 GLN CG C 33.42 . . 670 62 GLN N N 125.08 . . 671 62 GLN NE2 N 112.15 . . 672 63 LYS H H 8.49 . . 673 63 LYS HA H 4.00 . . 674 63 LYS HB2 H 1.91 . . 675 63 LYS HB3 H 2.06 . . 676 63 LYS HG2 H 1.49 . . 677 63 LYS HD2 H 1.75 . . 678 63 LYS HE2 H 3.04 . . 679 63 LYS C C 175.54 . . 680 63 LYS CA C 57.78 . . 681 63 LYS CB C 32.64 . . 682 63 LYS CG C 24.00 . . 683 63 LYS CD C 29.76 . . 684 63 LYS CE C 41.95 . . 685 63 LYS N N 120.64 . . 686 64 GLU H H 9.28 . . 687 64 GLU HA H 3.46 . . 688 64 GLU HB2 H 2.59 . . 689 64 GLU HB3 H 2.45 . . 690 64 GLU HG2 H 2.26 . . 691 64 GLU C C 174.98 . . 692 64 GLU CA C 57.88 . . 693 64 GLU CB C 25.89 . . 694 64 GLU CG C 35.94 . . 695 64 GLU N N 114.29 . . 696 65 SER H H 7.67 . . 697 65 SER HA H 4.64 . . 698 65 SER HB2 H 3.89 . . 699 65 SER HB3 H 3.65 . . 700 65 SER C C 171.89 . . 701 65 SER CA C 60.88 . . 702 65 SER CB C 64.90 . . 703 65 SER N N 115.07 . . 704 66 THR H H 8.73 . . 705 66 THR HA H 5.27 . . 706 66 THR HB H 4.08 . . 707 66 THR HG2 H 0.94 . . 708 66 THR C C 173.68 . . 709 66 THR CA C 62.33 . . 710 66 THR CB C 70.07 . . 711 66 THR CG2 C 21.56 . . 712 66 THR N N 117.45 . . 713 67 LEU H H 9.41 . . 714 67 LEU HA H 5.06 . . 715 67 LEU HB2 H 1.62 . . 716 67 LEU HG H 1.78 . . 717 67 LEU HD1 H 0.71 . . 718 67 LEU HD2 H 0.67 . . 719 67 LEU C C 175.50 . . 720 67 LEU CA C 53.89 . . 721 67 LEU CB C 44.25 . . 722 67 LEU CG C 29.52 . . 723 67 LEU CD1 C 25.00 . . 724 67 LEU CD2 C 25.20 . . 725 67 LEU N N 127.45 . . 726 68 HIS H H 9.23 . . 727 68 HIS HA H 5.24 . . 728 68 HIS HB2 H 3.23 . . 729 68 HIS HB3 H 3.03 . . 730 68 HIS HE1 H 7.23 . . 731 68 HIS C C 172.88 . . 732 68 HIS CA C 54.99 . . 733 68 HIS CB C 30.52 . . 734 68 HIS CE1 C 119.47 . . 735 68 HIS N N 118.72 . . 736 69 LEU H H 8.34 . . 737 69 LEU HA H 5.19 . . 738 69 LEU HB2 H 1.61 . . 739 69 LEU HB3 H 1.10 . . 740 69 LEU HG H 1.34 . . 741 69 LEU HD1 H 0.87 . . 742 69 LEU HD2 H 0.74 . . 743 69 LEU C C 175.00 . . 744 69 LEU CA C 53.88 . . 745 69 LEU CB C 44.37 . . 746 69 LEU CG C 27.66 . . 747 69 LEU CD1 C 23.97 . . 748 69 LEU CD2 C 26.16 . . 749 69 LEU N N 124.80 . . 750 70 VAL H H 9.20 . . 751 70 VAL HA H 4.35 . . 752 70 VAL HB H 2.02 . . 753 70 VAL HG1 H 0.95 . . 754 70 VAL HG2 H 0.85 . . 755 70 VAL C C 173.73 . . 756 70 VAL CA C 60.79 . . 757 70 VAL CB C 34.90 . . 758 70 VAL CG1 C 21.47 . . 759 70 VAL CG2 C 20.85 . . 760 70 VAL N N 127.28 . . 761 71 LEU H H 8.12 . . 762 71 LEU HA H 5.06 . . 763 71 LEU HB2 H 1.54 . . 764 71 LEU HB3 H 1.68 . . 765 71 LEU HG H 1.68 . . 766 71 LEU HD1 H 0.97 . . 767 71 LEU HD2 H 0.87 . . 768 71 LEU C C 177.56 . . 769 71 LEU CA C 53.93 . . 770 71 LEU CB C 42.84 . . 771 71 LEU CG C 27.67 . . 772 71 LEU CD1 C 24.99 . . 773 71 LEU CD2 C 24.03 . . 774 71 LEU N N 123.47 . . 775 72 ARG H H 8.58 . . 776 72 ARG HA H 4.30 . . 777 72 ARG HB2 H 1.55 . . 778 72 ARG HB3 H 1.78 . . 779 72 ARG HG2 H 1.54 . . 780 72 ARG HD2 H 3.16 . . 781 72 ARG C C 175.08 . . 782 72 ARG CA C 55.60 . . 783 72 ARG CB C 31.34 . . 784 72 ARG CG C 27.25 . . 785 72 ARG CD C 43.43 . . 786 72 ARG N N 123.83 . . 787 73 LEU H H 8.32 . . 788 73 LEU HA H 4.39 . . 789 73 LEU HB2 H 1.58 . . 790 73 LEU HB3 H 1.64 . . 791 73 LEU HG H 1.64 . . 792 73 LEU HD1 H 0.93 . . 793 73 LEU HD2 H 0.88 . . 794 73 LEU C C 177.18 . . 795 73 LEU CA C 54.92 . . 796 73 LEU CB C 42.52 . . 797 73 LEU CG C 27.19 . . 798 73 LEU CD1 C 25.02 . . 799 73 LEU CD2 C 23.37 . . 800 73 LEU N N 124.56 . . 801 74 ARG H H 8.39 . . 802 74 ARG HA H 4.31 . . 803 74 ARG HB2 H 1.80 . . 804 74 ARG HB3 H 1.88 . . 805 74 ARG HG2 H 1.65 . . 806 74 ARG HD2 H 3.22 . . 807 74 ARG C C 176.60 . . 808 74 ARG CA C 56.45 . . 809 74 ARG CB C 30.71 . . 810 74 ARG CG C 27.10 . . 811 74 ARG CD C 43.32 . . 812 74 ARG N N 121.79 . . 813 75 GLY H H 8.45 . . 814 75 GLY HA2 H 3.98 . . 815 75 GLY C C 173.41 . . 816 75 GLY CA C 45.34 . . 817 75 GLY N N 111.12 . . 818 76 GLY H H 7.92 . . 819 76 GLY HA2 H 3.75 . . 820 76 GLY C C 178.88 . . 821 76 GLY CA C 46.09 . . 822 76 GLY N N 115.02 . . stop_ save_