data_4438 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical Shift Assignments for SCP2 ; _BMRB_accession_number 4438 _BMRB_flat_file_name bmr4438.str _Entry_type original _Submission_date 1999-10-14 _Accession_date 1999-10-14 _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 'Lopez Garcia' Francisco . . 2 Szyperski Thomas . . 3 Dyer James H. . 4 Choinowski Thomas . . 5 Seedorf Udo . . 6 Hauser Helmut . . 7 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 637 "13C chemical shifts" 301 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-23 original author . stop_ _Original_release_date 2000-03-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of the sterol carrier protein-2; implications for the biological role ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20090956 _PubMed_ID 10623549 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'Lopez Garcia' Francisco . . 2 Szyperski Thomas . . 3 Dyer James H. . 4 Choinowski Thomas . . 5 Seedorf Udo . . 6 Hauser Helmut . . 7 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 295 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 595 _Page_last 603 _Year 2000 _Details . loop_ _Keyword 'sterol carrier protein 2' 'protein structure' 'protein dynamics' 'nitroxide spin labels' 'lipid binding' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; Guntert, P., Dotsch, V., Wider, G., Wuthrich, K., Processing of multi-dimensional NMR data with the new software, J. Biomol. NMR 2, 619-629 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref2 _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T.H., Billeter, M., Buntert, P., Wuthrich, K., The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules, J. Biomol. NMR 6, 1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref3 _Saveframe_category citation _Citation_full ; Guntert, P., Mumenthaler, C., Wuthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. (1997) 273(1):283-98. ; _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P . . 2 Mumenthaler C . . 3 Wuthrich K . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ ################################## # Molecular system description # ################################## save_system_SCP-2 _Saveframe_category molecular_system _Mol_system_name 'Sterol carrier protein 2See' _Abbreviation_common SCP-2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SCP-2 $SCP-2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'See SWISS-PROT P22307' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SCP-2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sterol carrier protein 2' _Abbreviation_common SCP-2 _Molecular_mass 13242.3 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; SSASDGFKANLVFKEIEKKL EEEGEQFVKKIGGIFAFKVK DGPGGKEATWVVDVKNGKGS VLPNSDKKADCTITMADSDF LALMTGKMNPQSAFFQGKLK ITGNMGLAMKLQNLQLQPGN AKL ; loop_ _Residue_seq_code _Residue_label 1 SER 2 SER 3 ALA 4 SER 5 ASP 6 GLY 7 PHE 8 LYS 9 ALA 10 ASN 11 LEU 12 VAL 13 PHE 14 LYS 15 GLU 16 ILE 17 GLU 18 LYS 19 LYS 20 LEU 21 GLU 22 GLU 23 GLU 24 GLY 25 GLU 26 GLN 27 PHE 28 VAL 29 LYS 30 LYS 31 ILE 32 GLY 33 GLY 34 ILE 35 PHE 36 ALA 37 PHE 38 LYS 39 VAL 40 LYS 41 ASP 42 GLY 43 PRO 44 GLY 45 GLY 46 LYS 47 GLU 48 ALA 49 THR 50 TRP 51 VAL 52 VAL 53 ASP 54 VAL 55 LYS 56 ASN 57 GLY 58 LYS 59 GLY 60 SER 61 VAL 62 LEU 63 PRO 64 ASN 65 SER 66 ASP 67 LYS 68 LYS 69 ALA 70 ASP 71 CYS 72 THR 73 ILE 74 THR 75 MET 76 ALA 77 ASP 78 SER 79 ASP 80 PHE 81 LEU 82 ALA 83 LEU 84 MET 85 THR 86 GLY 87 LYS 88 MET 89 ASN 90 PRO 91 GLN 92 SER 93 ALA 94 PHE 95 PHE 96 GLN 97 GLY 98 LYS 99 LEU 100 LYS 101 ILE 102 THR 103 GLY 104 ASN 105 MET 106 GLY 107 LEU 108 ALA 109 MET 110 LYS 111 LEU 112 GLN 113 ASN 114 LEU 115 GLN 116 LEU 117 GLN 118 PRO 119 GLY 120 ASN 121 ALA 122 LYS 123 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-10 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 PDB 1C44 "Sterol Carrier Protein 2 (Scp2) From Rabbit" 100.00 123 97.56 97.56 8.95e-78 PDB 1QND "Sterol Carrier Protein-2, Nmr, 20 Structures" 99.19 123 100.00 100.00 1.20e-79 PDB 2C0L "Tpr Domain Of Human Pex5p In Complex With Human Mscp2" 99.19 122 100.00 100.00 1.16e-79 DBJ BAG35708 "unnamed protein product [Homo sapiens]" 100.00 547 100.00 100.00 1.79e-76 DBJ BAG57810 "unnamed protein product [Homo sapiens]" 100.00 523 100.00 100.00 1.12e-76 DBJ BAG58208 "unnamed protein product [Homo sapiens]" 100.00 466 100.00 100.00 3.43e-77 DBJ BAG64455 "unnamed protein product [Homo sapiens]" 74.80 121 100.00 100.00 2.68e-57 EMBL CAH91926 "hypothetical protein [Pongo abelii]" 100.00 547 99.19 100.00 4.20e-76 GB AAA03557 "sterol carrier protein-X/sterol carrier protein-2 [Homo sapiens]" 100.00 547 100.00 100.00 1.79e-76 GB AAA03558 "sterol carrier protein-2 [Homo sapiens]" 100.00 289 100.00 100.00 8.58e-79 GB AAA03559 "sterol carrier protein-2 [Homo sapiens]" 100.00 143 100.00 100.00 1.55e-80 GB AAB41286 "sterol carrier protein-X/sterol carrier protein-2 [Homo sapiens]" 100.00 547 100.00 100.00 1.85e-76 GB AAH05911 "Sterol carrier protein 2 [Homo sapiens]" 100.00 143 100.00 100.00 1.55e-80 REF NP_001007100 "non-specific lipid-transfer protein isoform 5 precursor [Homo sapiens]" 100.00 143 100.00 100.00 1.55e-80 REF NP_001007101 "non-specific lipid-transfer protein isoform 4 [Homo sapiens]" 100.00 140 100.00 100.00 1.60e-80 REF NP_001126116 "non-specific lipid-transfer protein [Pongo abelii]" 100.00 547 99.19 100.00 4.20e-76 REF NP_001180528 "non-specific lipid-transfer protein isoform 7 [Homo sapiens]" 100.00 523 100.00 100.00 1.27e-76 REF NP_001180529 "non-specific lipid-transfer protein isoform 6 [Homo sapiens]" 100.00 503 100.00 100.00 7.53e-77 SP P22307 "RecName: Full=Non-specific lipid-transfer protein; Short=NSL-TP; AltName: Full=Propanoyl-CoA C-acyltransferase; AltName: Full=S" 100.00 547 100.00 100.00 1.79e-76 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $SCP-2 Human 9606 Eukaryota Metazoa Homo sapiens liver stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $SCP-2 'recombinant technology' 'E. coli' Escherichia coli 'XJ-1 Blue' plasmid pGEX-2T/hSCP2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SCP-2 1.0 mM [U-15N] stop_ save_ save_sample2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SCP-2 1 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Saveframe_category software _Name PROSA _Version 4.3 loop_ _Task 'Processing of NMR data' stop_ _Details . _Citation_label $ref1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'NMR spectral analysis' stop_ _Details . _Citation_label $ref2 save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'Structure calculation' 'Torsion angle dynamics' stop_ _Details . _Citation_label $ref3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity+ _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCACBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACBCA(CO)NH _Sample_label . save_ save_1H-13C-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-NOESY _Sample_label . save_ save_HCCH-COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_four_channels,_Z-gradient,_triple_resonance_probe_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'four channels, Z-gradient, triple resonance probe' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'four channels, Z-gradient, triple resonance probe' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_set1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 309 1 K 'ionic strength' 0.45 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shiftset1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $conditions_set1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name SCP-2 _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 . 2 SER N N 117.4 . 1 2 . 2 SER H H 8.41 . 1 3 . 2 SER CA C 58.1 . 1 4 . 2 SER HA H 4.51 . 1 5 . 2 SER CB C 64.0 . 1 6 . 2 SER HB2 H 3.88 . 1 7 . 2 SER HB3 H 3.88 . 1 8 . 3 ALA N N 126.0 . 1 9 . 3 ALA H H 8.46 . 1 10 . 3 ALA CA C 53.6 . 1 11 . 3 ALA HA H 4.26 . 1 12 . 3 ALA HB H 1.39 . 1 13 . 3 ALA CB C 18.9 . 1 14 . 4 SER N N 112.2 . 1 15 . 4 SER H H 8.09 . 1 16 . 4 SER CA C 58.4 . 1 17 . 4 SER HA H 4.32 . 1 18 . 4 SER CB C 63.3 . 1 19 . 4 SER HB2 H 3.49 . 2 20 . 4 SER HB3 H 3.83 . 2 21 . 5 ASP N N 121.8 . 1 22 . 5 ASP H H 7.94 . 1 23 . 5 ASP CA C 55.8 . 1 24 . 5 ASP HA H 4.54 . 1 25 . 5 ASP CB C 40.9 . 1 26 . 5 ASP HB2 H 2.72 . 1 27 . 5 ASP HB3 H 2.72 . 1 28 . 6 GLY N N 107.6 . 1 29 . 6 GLY H H 8.49 . 1 30 . 6 GLY CA C 45.5 . 1 31 . 6 GLY HA2 H 4.02 . 1 32 . 6 GLY HA3 H 4.02 . 1 33 . 7 PHE N N 120.3 . 1 34 . 7 PHE H H 8.03 . 1 35 . 7 PHE CA C 58.4 . 1 36 . 7 PHE HA H 4.45 . 1 37 . 7 PHE CB C 38.0 . 1 38 . 7 PHE HB2 H 3.38 . 1 39 . 7 PHE HB3 H 3.38 . 1 40 . 7 PHE HD1 H 7.46 . 1 41 . 7 PHE HD2 H 7.46 . 1 42 . 7 PHE HE1 H 7.33 . 1 43 . 7 PHE HE2 H 7.33 . 1 44 . 7 PHE HZ H 6.85 . 1 45 . 8 LYS N N 133.6 . 1 46 . 8 LYS H H 12.22 . 1 47 . 8 LYS CA C 59.1 . 1 48 . 8 LYS HA H 4.11 . 1 49 . 8 LYS CB C 31.6 . 1 50 . 8 LYS HB2 H 1.80 . 1 51 . 8 LYS HB3 H 1.80 . 1 52 . 9 ALA N N 119.8 . 1 53 . 9 ALA H H 10.70 . 1 54 . 9 ALA CA C 54.5 . 1 55 . 9 ALA HA H 3.70 . 1 56 . 9 ALA HB H 1.29 . 1 57 . 9 ALA CB C 19.9 . 1 58 . 10 ASN N N 113.6 . 1 59 . 10 ASN H H 7.57 . 1 60 . 10 ASN CA C 57.1 . 1 61 . 10 ASN HA H 4.39 . 1 62 . 10 ASN CB C 39.4 . 1 63 . 10 ASN HB2 H 3.09 . 2 64 . 10 ASN HB3 H 2.98 . 2 65 . 10 ASN ND2 N 113.6 . 1 66 . 10 ASN HD21 H 7.85 . 1 67 . 10 ASN HD22 H 7.36 . 1 68 . 11 LEU N N 117.0 . 1 69 . 11 LEU H H 7.55 . 1 70 . 11 LEU CA C 57.7 . 1 71 . 11 LEU HA H 4.01 . 1 72 . 11 LEU CB C 41.5 . 1 73 . 11 LEU HB2 H 1.54 . 2 74 . 11 LEU HB3 H 1.90 . 2 75 . 11 LEU CG C 27.0 . 1 76 . 11 LEU HG H 1.76 . 1 77 . 11 LEU HD1 H 0.95 . 1 78 . 11 LEU HD2 H 0.85 . 1 79 . 11 LEU CD1 C 24.7 . 1 80 . 11 LEU CD2 C 23.6 . 1 81 . 12 VAL N N 117.0 . 1 82 . 12 VAL H H 6.75 . 1 83 . 12 VAL CA C 65.0 . 1 84 . 12 VAL HA H 3.32 . 1 85 . 12 VAL CB C 31.2 . 1 86 . 12 VAL HB H 1.68 . 1 87 . 12 VAL HG1 H 0.09 . 1 88 . 12 VAL HG2 H 0.56 . 1 89 . 12 VAL CG1 C 20.6 . 1 90 . 12 VAL CG2 C 21.9 . 1 91 . 13 PHE N N 116.5 . 1 92 . 13 PHE H H 7.62 . 1 93 . 13 PHE CA C 63.6 . 1 94 . 13 PHE HA H 3.89 . 1 95 . 13 PHE CB C 37.8 . 1 96 . 13 PHE HB2 H 2.28 . 2 97 . 13 PHE HB3 H 2.83 . 2 98 . 13 PHE HD1 H 5.89 . 1 99 . 13 PHE HD2 H 5.89 . 1 100 . 13 PHE HE1 H 7.06 . 1 101 . 13 PHE HE2 H 7.06 . 1 102 . 14 LYS N N 119.8 . 1 103 . 14 LYS H H 8.04 . 1 104 . 14 LYS CA C 59.1 . 1 105 . 14 LYS HA H 4.25 . 1 106 . 14 LYS CB C 31.5 . 1 107 . 14 LYS HB2 H 1.89 . 2 108 . 14 LYS HB3 H 1.99 . 2 109 . 14 LYS CG C 24.4 . 1 110 . 14 LYS HG2 H 1.57 . 1 111 . 14 LYS HG3 H 1.57 . 1 112 . 14 LYS CD C 28.6 . 1 113 . 14 LYS HD2 H 1.74 . 1 114 . 14 LYS HD3 H 1.74 . 1 115 . 14 LYS HE2 H 3.07 . 1 116 . 14 LYS HE3 H 3.07 . 1 117 . 15 GLU N N 118.9 . 1 118 . 15 GLU H H 7.32 . 1 119 . 15 GLU CA C 58.8 . 1 120 . 15 GLU HA H 4.16 . 1 121 . 15 GLU CB C 29.0 . 1 122 . 15 GLU HB2 H 2.05 . 1 123 . 15 GLU HB3 H 2.05 . 1 124 . 15 GLU CG C 35.8 . 1 125 . 15 GLU HG2 H 2.25 . 2 126 . 15 GLU HG3 H 2.33 . 2 127 . 16 ILE N N 120.8 . 1 128 . 16 ILE H H 8.37 . 1 129 . 16 ILE CA C 65.9 . 1 130 . 16 ILE HA H 3.43 . 1 131 . 16 ILE CB C 37.7 . 1 132 . 16 ILE HB H 1.82 . 1 133 . 16 ILE HG2 H 0.71 . 1 134 . 16 ILE CG2 C 17.0 . 1 135 . 16 ILE CG1 C 29.0 . 1 136 . 16 ILE HG12 H 0.79 . 1 137 . 16 ILE HG13 H 1.65 . 1 138 . 16 ILE HD1 H 0.38 . 1 139 . 16 ILE CD1 C 13.0 . 1 140 . 17 GLU N N 119.4 . 1 141 . 17 GLU H H 8.45 . 1 142 . 17 GLU CA C 60.3 . 1 143 . 17 GLU HA H 3.77 . 1 144 . 17 GLU CB C 29.9 . 1 145 . 17 GLU HB2 H 2.17 . 1 146 . 17 GLU HB3 H 2.29 . 1 147 . 17 GLU CG C 36.4 . 1 148 . 17 GLU HG2 H 2.44 . 1 149 . 17 GLU HG3 H 2.44 . 1 150 . 18 LYS N N 118.4 . 1 151 . 18 LYS H H 7.45 . 1 152 . 18 LYS CA C 59.0 . 1 153 . 18 LYS HA H 4.12 . 1 154 . 18 LYS CB C 32.2 . 1 155 . 18 LYS HB2 H 1.94 . 1 156 . 18 LYS HB3 H 1.94 . 1 157 . 19 LYS N N 119.4 . 1 158 . 19 LYS H H 7.91 . 1 159 . 19 LYS CA C 58.4 . 1 160 . 19 LYS HA H 4.16 . 1 161 . 19 LYS CB C 31.6 . 1 162 . 19 LYS HB2 H 1.79 . 2 163 . 19 LYS HB3 H 1.73 . 2 164 . 19 LYS HG2 H 1.38 . 1 165 . 19 LYS HG3 H 1.38 . 1 166 . 20 LEU N N 117.4 . 1 167 . 20 LEU H H 8.46 . 1 168 . 20 LEU CA C 56.8 . 1 169 . 20 LEU HA H 3.94 . 1 170 . 20 LEU CB C 39.6 . 1 171 . 20 LEU HB2 H 1.75 . 1 172 . 20 LEU HB3 H 1.87 . 1 173 . 20 LEU CG C 26.2 . 1 174 . 20 LEU HG H 1.84 . 1 175 . 20 LEU HD1 H 0.63 . 1 176 . 20 LEU HD2 H 0.65 . 1 177 . 20 LEU CD1 C 22.1 . 1 178 . 20 LEU CD2 C 25.8 . 1 179 . 21 GLU N N 120.5 . 1 180 . 21 GLU H H 8.05 . 1 181 . 21 GLU CA C 59.5 . 1 182 . 21 GLU HA H 4.04 . 1 183 . 21 GLU CB C 29.2 . 1 184 . 21 GLU HB2 H 2.20 . 1 185 . 21 GLU HB3 H 2.30 . 1 186 . 21 GLU CG C 36.1 . 1 187 . 21 GLU HG2 H 2.32 . 2 188 . 21 GLU HG3 H 2.48 . 2 189 . 22 GLU N N 116.2 . 1 190 . 22 GLU H H 7.70 . 1 191 . 22 GLU CA C 58.4 . 1 192 . 22 GLU HA H 4.30 . 1 193 . 22 GLU CB C 31.2 . 1 194 . 22 GLU HB2 H 2.17 . 1 195 . 22 GLU HB3 H 2.17 . 1 196 . 22 GLU CG C 36.1 . 1 197 . 22 GLU HG2 H 2.29 . 2 198 . 22 GLU HG3 H 2.52 . 2 199 . 23 GLU N N 116.0 . 1 200 . 23 GLU H H 8.63 . 1 201 . 23 GLU CA C 55.8 . 1 202 . 23 GLU HA H 4.87 . 1 203 . 23 GLU CB C 31.3 . 1 204 . 23 GLU HB2 H 1.93 . 2 205 . 23 GLU HB3 H 2.31 . 2 206 . 23 GLU HG2 H 2.22 . 1 207 . 23 GLU HG3 H 2.22 . 1 208 . 24 GLY N N 109.9 . 1 209 . 24 GLY H H 8.22 . 1 210 . 24 GLY CA C 49.9 . 1 211 . 24 GLY HA2 H 3.88 . 1 212 . 24 GLY HA3 H 5.16 . 1 213 . 25 GLU N N 119.4 . 1 214 . 25 GLU H H 9.38 . 1 215 . 25 GLU CA C 60.0 . 1 216 . 25 GLU HA H 4.08 . 1 217 . 25 GLU CB C 29.2 . 1 218 . 25 GLU HB2 H 2.02 . 1 219 . 25 GLU HB3 H 2.02 . 1 220 . 25 GLU CG C 36.7 . 1 221 . 25 GLU HG2 H 2.26 . 2 222 . 25 GLU HG3 H 2.34 . 2 223 . 26 GLN N N 116.3 . 1 224 . 26 GLN H H 8.00 . 1 225 . 26 GLN CA C 58.1 . 1 226 . 26 GLN HA H 4.10 . 1 227 . 26 GLN CB C 28.3 . 1 228 . 26 GLN HB2 H 2.15 . 1 229 . 26 GLN HB3 H 2.02 . 1 230 . 26 GLN CG C 33.8 . 1 231 . 26 GLN HG2 H 2.39 . 1 232 . 26 GLN HG3 H 2.39 . 1 233 . 26 GLN NE2 N 111.8 . 1 234 . 26 GLN HE21 H 7.51 . 1 235 . 26 GLN HE22 H 6.83 . 1 236 . 27 PHE N N 119.0 . 1 237 . 27 PHE H H 7.69 . 1 238 . 27 PHE CA C 62.1 . 1 239 . 27 PHE HA H 4.13 . 1 240 . 27 PHE CB C 39.3 . 1 241 . 27 PHE HB2 H 2.88 . 2 242 . 27 PHE HB3 H 3.12 . 2 243 . 27 PHE HD1 H 7.10 . 1 244 . 27 PHE HD2 H 7.10 . 1 245 . 27 PHE HE1 H 7.34 . 1 246 . 27 PHE HE2 H 7.34 . 1 247 . 28 VAL N N 119.8 . 1 248 . 28 VAL H H 8.49 . 1 249 . 28 VAL CA C 65.5 . 1 250 . 28 VAL HA H 3.87 . 1 251 . 28 VAL CB C 31.2 . 1 252 . 28 VAL HB H 2.00 . 1 253 . 28 VAL HG1 H 0.64 . 1 254 . 28 VAL HG2 H 0.70 . 1 255 . 28 VAL CG1 C 21.1 . 1 256 . 28 VAL CG2 C 21.9 . 1 257 . 29 LYS N N 117.2 . 1 258 . 29 LYS H H 7.51 . 1 259 . 29 LYS CA C 58.7 . 1 260 . 29 LYS HA H 3.99 . 1 261 . 29 LYS CB C 32.6 . 1 262 . 29 LYS HB2 H 1.87 . 1 263 . 29 LYS HB3 H 1.87 . 1 264 . 29 LYS HG2 H 1.44 . 2 265 . 29 LYS HG3 H 1.56 . 2 266 . 29 LYS HD2 H 1.65 . 1 267 . 29 LYS HD3 H 1.65 . 1 268 . 30 LYS N N 115.1 . 1 269 . 30 LYS H H 7.54 . 1 270 . 30 LYS CA C 58.0 . 1 271 . 30 LYS HA H 4.17 . 1 272 . 30 LYS CB C 33.8 . 1 273 . 30 LYS HB2 H 1.80 . 1 274 . 30 LYS HB3 H 1.80 . 1 275 . 30 LYS HG2 H 1.44 . 1 276 . 30 LYS HG3 H 1.55 . 1 277 . 31 ILE N N 117.4 . 1 278 . 31 ILE H H 8.11 . 1 279 . 31 ILE CA C 63.6 . 1 280 . 31 ILE HA H 4.12 . 1 281 . 31 ILE CB C 38.0 . 1 282 . 31 ILE HB H 2.13 . 1 283 . 31 ILE HG2 H 0.98 . 1 284 . 31 ILE CG2 C 18.9 . 1 285 . 31 ILE CG1 C 27.7 . 1 286 . 31 ILE HG12 H 1.01 . 2 287 . 31 ILE HG13 H 1.80 . 2 288 . 31 ILE HD1 H 0.89 . 1 289 . 31 ILE CD1 C 13.7 . 1 290 . 32 GLY N N 107.0 . 1 291 . 32 GLY H H 7.86 . 1 292 . 32 GLY CA C 48.7 . 1 293 . 32 GLY HA2 H 3.89 . 2 294 . 32 GLY HA3 H 4.24 . 2 295 . 33 GLY N N 102.7 . 1 296 . 33 GLY H H 6.98 . 1 297 . 33 GLY CA C 45.1 . 1 298 . 33 GLY HA2 H 3.44 . 2 299 . 33 GLY HA3 H 4.34 . 2 300 . 34 ILE N N 118.9 . 1 301 . 34 ILE H H 8.92 . 1 302 . 34 ILE CA C 60.9 . 1 303 . 34 ILE HA H 4.80 . 1 304 . 34 ILE CB C 39.9 . 1 305 . 34 ILE HB H 1.54 . 1 306 . 34 ILE HG2 H 0.76 . 1 307 . 34 ILE CG2 C 17.9 . 1 308 . 34 ILE CG1 C 28.4 . 1 309 . 34 ILE HG12 H 0.92 . 2 310 . 34 ILE HG13 H 1.57 . 2 311 . 34 ILE HD1 H 0.80 . 1 312 . 34 ILE CD1 C 13.8 . 1 313 . 35 PHE N N 126.0 . 1 314 . 35 PHE H H 9.19 . 1 315 . 35 PHE CA C 56.5 . 1 316 . 35 PHE HA H 5.05 . 1 317 . 35 PHE CB C 43.8 . 1 318 . 35 PHE HB2 H 2.25 . 1 319 . 35 PHE HB3 H 2.90 . 1 320 . 35 PHE HD1 H 7.00 . 1 321 . 35 PHE HD2 H 7.00 . 1 322 . 35 PHE HE1 H 6.93 . 1 323 . 35 PHE HE2 H 6.93 . 1 324 . 36 ALA N N 123.3 . 1 325 . 36 ALA H H 8.68 . 1 326 . 36 ALA CA C 50.6 . 1 327 . 36 ALA HA H 5.25 . 1 328 . 36 ALA HB H 1.33 . 1 329 . 36 ALA CB C 20.8 . 1 330 . 37 PHE N N 120.0 . 1 331 . 37 PHE H H 9.56 . 1 332 . 37 PHE CA C 56.4 . 1 333 . 37 PHE HA H 5.44 . 1 334 . 37 PHE CB C 41.2 . 1 335 . 37 PHE HB2 H 3.10 . 1 336 . 37 PHE HB3 H 2.72 . 1 337 . 37 PHE HD1 H 7.22 . 1 338 . 37 PHE HD2 H 7.22 . 1 339 . 37 PHE HE1 H 7.13 . 1 340 . 37 PHE HE2 H 7.13 . 1 341 . 37 PHE HZ H 6.71 . 1 342 . 38 LYS N N 126.2 . 1 343 . 38 LYS H H 9.33 . 1 344 . 38 LYS CA C 55.3 . 1 345 . 38 LYS HA H 4.82 . 1 346 . 38 LYS CB C 31.5 . 1 347 . 38 LYS HB2 H 1.79 . 2 348 . 38 LYS HB3 H 1.89 . 2 349 . 38 LYS HG2 H 1.21 . 1 350 . 38 LYS HG3 H 1.21 . 1 351 . 38 LYS HD2 H 1.48 . 1 352 . 38 LYS HD3 H 1.48 . 1 353 . 39 VAL N N 125.1 . 1 354 . 39 VAL H H 9.14 . 1 355 . 39 VAL CA C 61.4 . 1 356 . 39 VAL HA H 5.05 . 1 357 . 39 VAL CB C 32.3 . 1 358 . 39 VAL HB H 2.28 . 1 359 . 39 VAL HG1 H 1.29 . 1 360 . 39 VAL HG2 H 0.64 . 1 361 . 39 VAL CG1 C 22.7 . 1 362 . 39 VAL CG2 C 20.5 . 1 363 . 40 LYS N N 123.8 . 1 364 . 40 LYS H H 8.49 . 1 365 . 40 LYS CA C 53.9 . 1 366 . 40 LYS HA H 4.93 . 1 367 . 40 LYS CB C 34.7 . 1 368 . 40 LYS HB2 H 1.87 . 1 369 . 40 LYS HB3 H 1.69 . 1 370 . 40 LYS HG2 H 1.33 . 1 371 . 40 LYS HG3 H 1.33 . 1 372 . 40 LYS HD2 H 1.58 . 1 373 . 40 LYS HD3 H 1.58 . 1 374 . 41 ASP N N 117.0 . 1 375 . 41 ASP H H 9.25 . 1 376 . 41 ASP CA C 55.6 . 1 377 . 41 ASP HA H 4.24 . 1 378 . 41 ASP CB C 39.3 . 1 379 . 41 ASP HB2 H 3.02 . 1 380 . 41 ASP HB3 H 2.71 . 1 381 . 42 GLY N N 104.8 . 1 382 . 42 GLY H H 8.52 . 1 383 . 42 GLY CA C 44.2 . 1 384 . 42 GLY HA2 H 2.92 . 2 385 . 42 GLY HA3 H 3.86 . 2 386 . 43 PRO CD C 48.8 . 1 387 . 43 PRO CA C 63.5 . 1 388 . 43 PRO HA H 4.27 . 1 389 . 43 PRO CB C 30.9 . 1 390 . 43 PRO HB2 H 1.79 . 2 391 . 43 PRO HB3 H 2.15 . 2 392 . 43 PRO CG C 27.7 . 1 393 . 43 PRO HG2 H 1.72 . 2 394 . 43 PRO HG3 H 1.82 . 2 395 . 43 PRO HD2 H 2.27 . 2 396 . 43 PRO HD3 H 2.88 . 2 397 . 44 GLY N N 112.7 . 1 398 . 44 GLY H H 8.98 . 1 399 . 44 GLY CA C 46.3 . 1 400 . 44 GLY HA2 H 3.90 . 1 401 . 44 GLY HA3 H 3.90 . 1 402 . 45 GLY N N 107.7 . 1 403 . 45 GLY H H 8.35 . 1 404 . 45 GLY CA C 45.5 . 1 405 . 45 GLY HA2 H 3.81 . 2 406 . 45 GLY HA3 H 4.18 . 2 407 . 46 LYS N N 120.4 . 1 408 . 46 LYS H H 6.99 . 1 409 . 46 LYS CA C 56.8 . 1 410 . 46 LYS HA H 4.28 . 1 411 . 46 LYS CB C 34.1 . 1 412 . 46 LYS HB2 H 1.75 . 1 413 . 46 LYS HB3 H 2.02 . 1 414 . 46 LYS CG C 25.7 . 1 415 . 46 LYS HG2 H 1.55 . 2 416 . 46 LYS HG3 H 1.63 . 2 417 . 47 GLU N N 117.0 . 1 418 . 47 GLU H H 8.18 . 1 419 . 47 GLU CA C 53.9 . 1 420 . 47 GLU HA H 5.70 . 1 421 . 47 GLU CB C 33.9 . 1 422 . 47 GLU HB2 H 2.02 . 1 423 . 47 GLU HB3 H 2.02 . 1 424 . 47 GLU CG C 36.2 . 1 425 . 47 GLU HG2 H 2.19 . 1 426 . 47 GLU HG3 H 2.19 . 1 427 . 48 ALA N N 125.1 . 1 428 . 48 ALA H H 8.91 . 1 429 . 48 ALA CA C 51.3 . 1 430 . 48 ALA HA H 4.46 . 1 431 . 48 ALA HB H 0.45 . 1 432 . 48 ALA CB C 22.5 . 1 433 . 49 THR N N 112.7 . 1 434 . 49 THR H H 7.96 . 1 435 . 49 THR CA C 60.4 . 1 436 . 49 THR HA H 5.70 . 1 437 . 49 THR CB C 71.7 . 1 438 . 49 THR HB H 3.84 . 1 439 . 49 THR HG2 H 1.03 . 1 440 . 49 THR CG2 C 21.2 . 1 441 . 50 TRP N N 125.1 . 1 442 . 50 TRP H H 9.00 . 1 443 . 50 TRP CA C 58.3 . 1 444 . 50 TRP HA H 4.70 . 1 445 . 50 TRP CB C 35.5 . 1 446 . 50 TRP HB2 H 2.01 . 2 447 . 50 TRP HB3 H 2.31 . 2 448 . 50 TRP NE1 N 128.0 . 1 449 . 50 TRP HD1 H 6.08 . 1 450 . 50 TRP HE3 H 7.06 . 1 451 . 50 TRP HE1 H 10.22 . 1 452 . 50 TRP HZ3 H 6.37 . 1 453 . 50 TRP HZ2 H 7.37 . 1 454 . 50 TRP HH2 H 6.44 . 1 455 . 51 VAL N N 121.3 . 1 456 . 51 VAL H H 8.50 . 1 457 . 51 VAL CA C 61.0 . 1 458 . 51 VAL HA H 5.17 . 1 459 . 51 VAL CB C 34.1 . 1 460 . 51 VAL HB H 2.03 . 1 461 . 51 VAL HG1 H 0.80 . 1 462 . 51 VAL HG2 H 0.95 . 1 463 . 51 VAL CG1 C 21.1 . 1 464 . 51 VAL CG2 C 22.4 . 1 465 . 52 VAL N N 126.5 . 1 466 . 52 VAL H H 9.64 . 1 467 . 52 VAL CA C 61.6 . 1 468 . 52 VAL HA H 4.89 . 1 469 . 52 VAL CB C 34.2 . 1 470 . 52 VAL HB H 2.38 . 1 471 . 52 VAL HG1 H 1.04 . 1 472 . 52 VAL HG2 H 1.25 . 1 473 . 52 VAL CG1 C 21.2 . 1 474 . 52 VAL CG2 C 22.8 . 1 475 . 53 ASP N N 129.0 . 1 476 . 53 ASP H H 9.28 . 1 477 . 53 ASP CA C 53.7 . 1 478 . 53 ASP HA H 4.77 . 1 479 . 53 ASP CB C 41.5 . 1 480 . 53 ASP HB2 H 2.23 . 2 481 . 53 ASP HB3 H 3.35 . 2 482 . 54 VAL N N 121.4 . 1 483 . 54 VAL H H 8.01 . 1 484 . 54 VAL CA C 60.1 . 1 485 . 54 VAL HA H 4.51 . 1 486 . 54 VAL CB C 29.6 . 1 487 . 54 VAL HB H 2.60 . 1 488 . 54 VAL HG1 H 0.99 . 1 489 . 54 VAL HG2 H 1.14 . 1 490 . 54 VAL CG1 C 25.4 . 1 491 . 54 VAL CG2 C 21.2 . 1 492 . 55 LYS N N 119.1 . 1 493 . 55 LYS H H 9.04 . 1 494 . 55 LYS CA C 57.2 . 1 495 . 55 LYS HA H 4.28 . 1 496 . 55 LYS CB C 37.6 . 1 497 . 55 LYS HB2 H 1.03 . 1 498 . 55 LYS HB3 H 1.68 . 1 499 . 55 LYS CG C 25.3 . 1 500 . 55 LYS HG2 H 1.06 . 2 501 . 55 LYS HG3 H 1.24 . 2 502 . 55 LYS HD2 H 1.54 . 1 503 . 55 LYS HD3 H 1.54 . 1 504 . 56 ASN N N 117.9 . 1 505 . 56 ASN H H 9.06 . 1 506 . 56 ASN CA C 52.9 . 1 507 . 56 ASN HA H 4.78 . 1 508 . 56 ASN CB C 41.0 . 1 509 . 56 ASN HB2 H 2.87 . 1 510 . 56 ASN HB3 H 2.47 . 1 511 . 56 ASN ND2 N 119.4 . 1 512 . 56 ASN HD21 H 9.39 . 1 513 . 56 ASN HD22 H 7.11 . 1 514 . 57 GLY N N 112.3 . 1 515 . 57 GLY H H 8.85 . 1 516 . 57 GLY CA C 47.5 . 1 517 . 57 GLY HA2 H 3.69 . 1 518 . 57 GLY HA3 H 3.80 . 1 519 . 58 LYS N N 124.7 . 1 520 . 58 LYS H H 8.55 . 1 521 . 58 LYS CA C 55.1 . 1 522 . 58 LYS HA H 4.23 . 1 523 . 58 LYS CB C 32.9 . 1 524 . 58 LYS HB2 H 1.76 . 1 525 . 58 LYS HB3 H 2.07 . 1 526 . 58 LYS HG2 H 1.45 . 2 527 . 58 LYS HG3 H 1.52 . 2 528 . 59 GLY N N 104.7 . 1 529 . 59 GLY H H 7.79 . 1 530 . 59 GLY CA C 44.5 . 1 531 . 59 GLY HA2 H 4.26 . 1 532 . 59 GLY HA3 H 4.26 . 1 533 . 60 SER N N 112.2 . 1 534 . 60 SER H H 9.00 . 1 535 . 60 SER CA C 58.3 . 1 536 . 60 SER HA H 4.71 . 1 537 . 60 SER CB C 66.2 . 1 538 . 60 SER HB2 H 3.71 . 2 539 . 60 SER HB3 H 3.98 . 2 540 . 61 VAL N N 122.2 . 1 541 . 61 VAL H H 9.01 . 1 542 . 61 VAL CA C 62.5 . 1 543 . 61 VAL HA H 4.65 . 1 544 . 61 VAL CB C 33.2 . 1 545 . 61 VAL HB H 2.13 . 1 546 . 61 VAL HG1 H 1.01 . 1 547 . 61 VAL HG2 H 1.07 . 1 548 . 61 VAL CG1 C 21.8 . 1 549 . 61 VAL CG2 C 21.9 . 1 550 . 62 LEU N N 128.5 . 1 551 . 62 LEU H H 9.51 . 1 552 . 62 LEU CA C 51.4 . 1 553 . 62 LEU HA H 5.09 . 1 554 . 62 LEU CB C 43.8 . 1 555 . 62 LEU HB2 H 1.94 . 2 556 . 62 LEU HB3 H 1.43 . 2 557 . 62 LEU CG C 26.1 . 1 558 . 62 LEU HG H 1.52 . 1 559 . 62 LEU HD1 H 0.90 . 1 560 . 62 LEU HD2 H 0.93 . 1 561 . 62 LEU CD1 C 25.9 . 1 562 . 62 LEU CD2 C 23.9 . 1 563 . 63 PRO CD C 51.1 . 1 564 . 63 PRO CA C 62.6 . 1 565 . 63 PRO HA H 3.95 . 1 566 . 63 PRO CB C 31.6 . 1 567 . 63 PRO HB2 H 1.56 . 2 568 . 63 PRO HB3 H 1.72 . 2 569 . 63 PRO CG C 27.3 . 1 570 . 63 PRO HG2 H 1.91 . 2 571 . 63 PRO HG3 H 2.06 . 2 572 . 63 PRO HD2 H 3.81 . 1 573 . 63 PRO HD3 H 3.81 . 1 574 . 64 ASN N N 117.7 . 1 575 . 64 ASN H H 8.32 . 1 576 . 64 ASN CA C 53.9 . 1 577 . 64 ASN HA H 4.08 . 1 578 . 64 ASN CB C 37.3 . 1 579 . 64 ASN HB2 H 2.57 . 2 580 . 64 ASN HB3 H 2.78 . 2 581 . 64 ASN ND2 N 114.0 . 1 582 . 64 ASN HD21 H 7.48 . 1 583 . 64 ASN HD22 H 6.75 . 1 584 . 65 SER N N 109.6 . 1 585 . 65 SER H H 6.56 . 1 586 . 65 SER CA C 57.5 . 1 587 . 65 SER HA H 4.30 . 1 588 . 65 SER CB C 65.0 . 1 589 . 65 SER HB2 H 3.31 . 2 590 . 65 SER HB3 H 3.69 . 2 591 . 66 ASP N N 125.1 . 1 592 . 66 ASP H H 8.16 . 1 593 . 66 ASP CA C 52.9 . 1 594 . 66 ASP HA H 4.59 . 1 595 . 66 ASP CB C 40.6 . 1 596 . 66 ASP HB2 H 2.54 . 2 597 . 66 ASP HB3 H 2.74 . 2 598 . 67 LYS N N 121.9 . 1 599 . 67 LYS H H 7.97 . 1 600 . 67 LYS CA C 57.1 . 1 601 . 67 LYS HA H 3.88 . 1 602 . 67 LYS CB C 33.0 . 1 603 . 67 LYS HB2 H 1.60 . 1 604 . 67 LYS HB3 H 1.60 . 1 605 . 67 LYS CG C 24.8 . 1 606 . 67 LYS HG2 H 1.39 . 1 607 . 67 LYS HG3 H 1.39 . 1 608 . 68 LYS N N 122.8 . 1 609 . 68 LYS H H 7.96 . 1 610 . 68 LYS CA C 57.1 . 1 611 . 68 LYS HA H 3.93 . 1 612 . 68 LYS CB C 32.1 . 1 613 . 68 LYS HB2 H 1.65 . 1 614 . 68 LYS HB3 H 1.65 . 1 615 . 68 LYS HG2 H 1.39 . 1 616 . 68 LYS HG3 H 1.31 . 1 617 . 69 ALA N N 126.0 . 1 618 . 69 ALA H H 8.26 . 1 619 . 69 ALA CA C 50.1 . 1 620 . 69 ALA HA H 4.22 . 1 621 . 69 ALA HB H 1.18 . 1 622 . 69 ALA CB C 23.1 . 1 623 . 70 ASP N N 118.9 . 1 624 . 70 ASP H H 8.46 . 1 625 . 70 ASP CA C 56.4 . 1 626 . 70 ASP HA H 4.44 . 1 627 . 70 ASP CB C 43.4 . 1 628 . 70 ASP HB2 H 2.58 . 1 629 . 70 ASP HB3 H 2.45 . 1 630 . 71 CYS N N 115.7 . 1 631 . 71 CYS H H 7.51 . 1 632 . 71 CYS CA C 57.1 . 1 633 . 71 CYS HA H 5.01 . 1 634 . 71 CYS CB C 30.3 . 1 635 . 71 CYS HB2 H 2.55 . 2 636 . 71 CYS HB3 H 2.71 . 2 637 . 72 THR N N 121.7 . 1 638 . 72 THR H H 8.78 . 1 639 . 72 THR CA C 61.8 . 1 640 . 72 THR HA H 5.28 . 1 641 . 72 THR CB C 70.2 . 1 642 . 72 THR HB H 3.92 . 1 643 . 72 THR HG2 H 0.99 . 1 644 . 72 THR CG2 C 20.2 . 1 645 . 73 ILE N N 130.3 . 1 646 . 73 ILE H H 9.28 . 1 647 . 73 ILE CA C 59.7 . 1 648 . 73 ILE HA H 4.93 . 1 649 . 73 ILE CB C 40.0 . 1 650 . 73 ILE HB H 1.83 . 1 651 . 73 ILE HG2 H 1.00 . 1 652 . 73 ILE CG2 C 18.3 . 1 653 . 73 ILE CG1 C 29.0 . 1 654 . 73 ILE HG12 H 1.17 . 2 655 . 73 ILE HG13 H 1.51 . 2 656 . 73 ILE HD1 H 0.86 . 1 657 . 73 ILE CD1 C 14.6 . 1 658 . 74 THR N N 124.1 . 1 659 . 74 THR H H 9.01 . 1 660 . 74 THR CA C 61.7 . 1 661 . 74 THR HA H 5.80 . 1 662 . 74 THR CB C 70.2 . 1 663 . 74 THR HB H 3.92 . 1 664 . 74 THR HG2 H 1.20 . 1 665 . 74 THR CG2 C 20.5 . 1 666 . 75 MET N N 123.6 . 1 667 . 75 MET H H 8.69 . 1 668 . 75 MET CA C 55.6 . 1 669 . 75 MET HA H 4.79 . 1 670 . 75 MET CB C 40.2 . 1 671 . 75 MET HB2 H 2.10 . 2 672 . 75 MET HB3 H 2.46 . 2 673 . 75 MET CG C 32.6 . 1 674 . 75 MET HG2 H 2.67 . 2 675 . 75 MET HG3 H 3.08 . 2 676 . 76 ALA N N 123.2 . 1 677 . 76 ALA H H 9.63 . 1 678 . 76 ALA CA C 52.1 . 1 679 . 76 ALA HA H 4.62 . 1 680 . 76 ALA HB H 1.64 . 1 681 . 76 ALA CB C 19.3 . 1 682 . 77 ASP N N 123.6 . 1 683 . 77 ASP H H 9.06 . 1 684 . 77 ASP CA C 59.0 . 1 685 . 77 ASP HA H 4.55 . 1 686 . 77 ASP CB C 42.9 . 1 687 . 77 ASP HB2 H 2.63 . 1 688 . 77 ASP HB3 H 2.69 . 1 689 . 78 SER N N 110.3 . 1 690 . 78 SER H H 9.05 . 1 691 . 78 SER CA C 62.3 . 1 692 . 78 SER HA H 3.99 . 1 693 . 78 SER CB C 62.3 . 1 694 . 78 SER HB2 H 3.92 . 1 695 . 78 SER HB3 H 3.92 . 1 696 . 79 ASP N N 121.4 . 1 697 . 79 ASP H H 6.98 . 1 698 . 79 ASP CA C 56.8 . 1 699 . 79 ASP HA H 4.53 . 1 700 . 79 ASP CB C 41.0 . 1 701 . 79 ASP HB2 H 2.51 . 2 702 . 79 ASP HB3 H 2.93 . 2 703 . 80 PHE N N 122.7 . 1 704 . 80 PHE H H 9.05 . 1 705 . 80 PHE CA C 61.7 . 1 706 . 80 PHE HA H 4.33 . 1 707 . 80 PHE CB C 38.7 . 1 708 . 80 PHE HB2 H 3.12 . 2 709 . 80 PHE HB3 H 3.19 . 2 710 . 80 PHE HD1 H 7.09 . 1 711 . 80 PHE HD2 H 7.09 . 1 712 . 80 PHE HE1 H 6.54 . 1 713 . 80 PHE HE2 H 6.54 . 1 714 . 80 PHE HZ H 5.87 . 1 715 . 81 LEU N N 117.9 . 1 716 . 81 LEU H H 7.89 . 1 717 . 81 LEU CA C 58.1 . 1 718 . 81 LEU HA H 3.59 . 1 719 . 81 LEU CB C 41.2 . 1 720 . 81 LEU HB2 H 1.31 . 2 721 . 81 LEU HB3 H 1.86 . 2 722 . 81 LEU CG C 27.0 . 1 723 . 81 LEU HG H 1.45 . 1 724 . 81 LEU HD1 H 0.75 . 1 725 . 81 LEU HD2 H 0.89 . 1 726 . 81 LEU CD1 C 23.5 . 1 727 . 81 LEU CD2 C 25.4 . 1 728 . 82 ALA N N 120.8 . 1 729 . 82 ALA H H 7.39 . 1 730 . 82 ALA CA C 55.1 . 1 731 . 82 ALA HA H 3.80 . 1 732 . 82 ALA HB H 1.47 . 1 733 . 82 ALA CB C 18.3 . 1 734 . 83 LEU N N 118.4 . 1 735 . 83 LEU H H 8.50 . 1 736 . 83 LEU CA C 58.2 . 1 737 . 83 LEU HA H 4.12 . 1 738 . 83 LEU CB C 42.3 . 1 739 . 83 LEU HB2 H 1.47 . 2 740 . 83 LEU HB3 H 1.65 . 2 741 . 84 MET N N 113.8 . 1 742 . 84 MET H H 8.06 . 1 743 . 84 MET CA C 55.3 . 1 744 . 84 MET HA H 4.33 . 1 745 . 84 MET HB2 H 1.36 . 2 746 . 84 MET HB3 H 1.57 . 2 747 . 84 MET HE H 1.43 . 1 748 . 84 MET CE C 15.4 . 1 749 . 85 THR N N 105.6 . 1 750 . 85 THR H H 7.38 . 1 751 . 85 THR CA C 61.3 . 1 752 . 85 THR HA H 4.55 . 1 753 . 85 THR CB C 69.4 . 1 754 . 85 THR HB H 4.43 . 1 755 . 85 THR HG2 H 1.07 . 1 756 . 85 THR CG2 C 21.6 . 1 757 . 86 GLY N N 107.1 . 1 758 . 86 GLY H H 7.51 . 1 759 . 86 GLY CA C 46.2 . 1 760 . 86 GLY HA2 H 3.86 . 2 761 . 86 GLY HA3 H 4.09 . 2 762 . 87 LYS N N 117.9 . 1 763 . 87 LYS H H 8.30 . 1 764 . 87 LYS CA C 56.5 . 1 765 . 87 LYS HA H 4.24 . 1 766 . 87 LYS CB C 32.3 . 1 767 . 87 LYS HB2 H 1.92 . 1 768 . 87 LYS HB3 H 1.60 . 1 769 . 88 MET N N 116.1 . 1 770 . 88 MET H H 7.23 . 1 771 . 88 MET CA C 54.3 . 1 772 . 88 MET HA H 4.49 . 1 773 . 88 MET CB C 36.5 . 1 774 . 88 MET HB2 H 1.65 . 2 775 . 88 MET HB3 H 1.79 . 2 776 . 88 MET CG C 31.3 . 1 777 . 88 MET HG2 H 2.25 . 2 778 . 88 MET HG3 H 2.32 . 2 779 . 89 ASN CA C 51.0 . 1 780 . 89 ASN HA H 5.05 . 1 781 . 89 ASN CB C 39.1 . 1 782 . 89 ASN HB2 H 2.83 . 2 783 . 89 ASN HB3 H 2.99 . 2 784 . 89 ASN ND2 N 114.2 . 1 785 . 89 ASN HD21 H 7.80 . 1 786 . 89 ASN HD22 H 7.10 . 1 787 . 90 PRO CD C 50.6 . 1 788 . 90 PRO CA C 65.8 . 1 789 . 90 PRO HA H 4.01 . 1 790 . 90 PRO CB C 32.0 . 1 791 . 90 PRO HB2 H 2.12 . 1 792 . 90 PRO HB3 H 2.12 . 1 793 . 90 PRO CG C 27.7 . 1 794 . 90 PRO HG2 H 1.83 . 2 795 . 90 PRO HG3 H 2.20 . 2 796 . 90 PRO HD2 H 3.91 . 1 797 . 90 PRO HD3 H 3.91 . 1 798 . 91 GLN CA C 45.4 . 1 799 . 91 GLN HA H 3.93 . 1 800 . 92 SER N N 115.1 . 1 801 . 92 SER H H 8.12 . 1 802 . 92 SER CA C 61.1 . 1 803 . 92 SER HA H 4.37 . 1 804 . 92 SER CB C 62.6 . 1 805 . 92 SER HB2 H 3.95 . 2 806 . 92 SER HB3 H 4.00 . 2 807 . 93 ALA N N 122.2 . 1 808 . 93 ALA H H 8.25 . 1 809 . 93 ALA CA C 55.1 . 1 810 . 93 ALA HA H 4.01 . 1 811 . 93 ALA HB H 1.37 . 1 812 . 93 ALA CB C 19.2 . 1 813 . 94 PHE N N 119.4 . 1 814 . 94 PHE H H 8.46 . 1 815 . 94 PHE HA H 4.61 . 1 816 . 94 PHE HB2 H 3.13 . 2 817 . 94 PHE HB3 H 3.23 . 2 818 . 94 PHE HD1 H 7.02 . 1 819 . 94 PHE HD2 H 7.02 . 1 820 . 94 PHE HE1 H 7.36 . 1 821 . 94 PHE HE2 H 7.36 . 1 822 . 95 PHE N N 121.4 . 1 823 . 95 PHE H H 8.58 . 1 824 . 95 PHE CA C 60.8 . 1 825 . 95 PHE HA H 4.31 . 1 826 . 95 PHE CB C 38.7 . 1 827 . 95 PHE HB2 H 3.33 . 1 828 . 95 PHE HB3 H 3.33 . 1 829 . 95 PHE HD1 H 7.39 . 1 830 . 95 PHE HD2 H 7.39 . 1 831 . 95 PHE HE1 H 7.44 . 1 832 . 95 PHE HE2 H 7.44 . 1 833 . 96 GLN N N 114.1 . 1 834 . 96 GLN H H 8.12 . 1 835 . 96 GLN CA C 56.4 . 1 836 . 96 GLN HA H 4.26 . 1 837 . 96 GLN CB C 29.9 . 1 838 . 96 GLN HB2 H 1.97 . 2 839 . 96 GLN HB3 H 2.31 . 2 840 . 96 GLN CG C 34.4 . 1 841 . 96 GLN HG2 H 2.47 . 2 842 . 96 GLN HG3 H 2.73 . 2 843 . 96 GLN NE2 N 109.8 . 1 844 . 96 GLN HE21 H 7.27 . 1 845 . 96 GLN HE22 H 6.74 . 1 846 . 97 GLY N N 107.0 . 1 847 . 97 GLY H H 7.75 . 1 848 . 97 GLY CA C 45.9 . 1 849 . 97 GLY HA2 H 3.87 . 2 850 . 97 GLY HA3 H 4.09 . 2 851 . 98 LYS N N 116.0 . 1 852 . 98 LYS H H 8.06 . 1 853 . 98 LYS CA C 56.4 . 1 854 . 98 LYS HA H 4.30 . 1 855 . 98 LYS CB C 34.2 . 1 856 . 98 LYS HB2 H 1.58 . 1 857 . 98 LYS HB3 H 1.81 . 1 858 . 98 LYS HG2 H 1.31 . 2 859 . 98 LYS HG3 H 1.39 . 2 860 . 99 LEU N N 119.4 . 1 861 . 99 LEU H H 7.08 . 1 862 . 99 LEU CA C 54.2 . 1 863 . 99 LEU HA H 4.81 . 1 864 . 99 LEU CB C 45.8 . 1 865 . 99 LEU HB2 H 1.34 . 2 866 . 99 LEU HB3 H 1.55 . 2 867 . 99 LEU HG H 1.59 . 1 868 . 99 LEU HD1 H 0.88 . 2 869 . 99 LEU HD2 H 0.96 . 2 870 . 99 LEU CD1 C 47.4 . 1 871 . 100 LYS N N 125.1 . 1 872 . 100 LYS H H 8.13 . 1 873 . 100 LYS CA C 55.0 . 1 874 . 100 LYS HA H 4.83 . 1 875 . 100 LYS CB C 34.5 . 1 876 . 100 LYS HB2 H 1.88 . 1 877 . 100 LYS HB3 H 1.77 . 1 878 . 100 LYS HG2 H 1.35 . 2 879 . 100 LYS HG3 H 1.40 . 2 880 . 101 ILE N N 123.4 . 1 881 . 101 ILE H H 8.69 . 1 882 . 101 ILE CA C 60.1 . 1 883 . 101 ILE HA H 5.12 . 1 884 . 101 ILE CB C 41.9 . 1 885 . 101 ILE HB H 1.59 . 1 886 . 101 ILE HG2 H 0.71 . 1 887 . 101 ILE CG2 C 17.9 . 1 888 . 101 ILE CG1 C 28.0 . 1 889 . 101 ILE HG12 H 0.89 . 2 890 . 101 ILE HG13 H 1.56 . 2 891 . 101 ILE HD1 H 0.65 . 1 892 . 101 ILE CD1 C 14.5 . 1 893 . 102 THR N N 118.9 . 1 894 . 102 THR H H 8.86 . 1 895 . 102 THR CA C 60.4 . 1 896 . 102 THR HA H 4.64 . 1 897 . 102 THR CB C 71.0 . 1 898 . 102 THR HB H 4.18 . 1 899 . 102 THR HG2 H 1.19 . 1 900 . 102 THR CG2 C 21.5 . 1 901 . 103 GLY N N 110.3 . 1 902 . 103 GLY H H 8.72 . 1 903 . 103 GLY CA C 44.9 . 1 904 . 103 GLY HA2 H 3.67 . 2 905 . 103 GLY HA3 H 4.44 . 2 906 . 104 ASN N N 120.3 . 1 907 . 104 ASN H H 8.28 . 1 908 . 104 ASN CA C 53.3 . 1 909 . 104 ASN HA H 4.50 . 1 910 . 104 ASN CB C 40.9 . 1 911 . 104 ASN HB2 H 2.73 . 1 912 . 104 ASN HB3 H 2.73 . 1 913 . 106 GLY N N 106.5 . 1 914 . 106 GLY H H 8.29 . 1 915 . 106 GLY CA C 46.9 . 1 916 . 106 GLY HA2 H 3.80 . 1 917 . 106 GLY HA3 H 3.80 . 1 918 . 107 LEU N N 121.3 . 1 919 . 107 LEU H H 7.38 . 1 920 . 107 LEU CA C 56.8 . 1 921 . 107 LEU HA H 4.09 . 1 922 . 107 LEU CB C 41.2 . 1 923 . 107 LEU HB2 H 1.44 . 1 924 . 107 LEU HB3 H 1.44 . 1 925 . 107 LEU HG H 1.37 . 1 926 . 107 LEU HD1 H 0.66 . 2 927 . 107 LEU HD2 H 0.69 . 2 928 . 107 LEU CD1 C 24.8 . 1 929 . 108 ALA N N 119.8 . 1 930 . 108 ALA H H 7.54 . 1 931 . 108 ALA CA C 55.6 . 1 932 . 108 ALA HA H 4.08 . 1 933 . 108 ALA HB H 1.51 . 1 934 . 108 ALA CB C 18.7 . 1 935 . 109 MET N N 112.4 . 1 936 . 109 MET H H 7.62 . 1 937 . 109 MET CA C 49.1 . 1 938 . 109 MET HA H 4.37 . 1 939 . 109 MET CB C 31.9 . 1 940 . 109 MET HB2 H 2.18 . 1 941 . 109 MET HB3 H 2.18 . 1 942 . 109 MET CG C 32.6 . 1 943 . 109 MET HG2 H 2.64 . 2 944 . 109 MET HG3 H 2.82 . 2 945 . 109 MET HE H 1.95 . 1 946 . 109 MET CE C 17.3 . 1 947 . 110 LYS N N 120.8 . 1 948 . 110 LYS H H 7.87 . 1 949 . 110 LYS CA C 57.8 . 1 950 . 110 LYS HA H 3.81 . 1 951 . 110 LYS HB2 H 1.63 . 2 952 . 110 LYS HB3 H 1.75 . 2 953 . 111 LEU N N 117.4 . 1 954 . 111 LEU H H 8.02 . 1 955 . 111 LEU HA H 4.40 . 1 956 . 111 LEU HB2 H 2.12 . 1 957 . 111 LEU HB3 H 2.29 . 1 958 . 112 GLN N N 115.9 . 1 959 . 112 GLN H H 7.99 . 1 960 . 112 GLN CA C 58.3 . 1 961 . 112 GLN HA H 4.10 . 1 962 . 113 ASN N N 115.1 . 1 963 . 113 ASN H H 7.83 . 1 964 . 113 ASN CA C 55.7 . 1 965 . 113 ASN HA H 4.54 . 1 966 . 113 ASN CB C 38.1 . 1 967 . 113 ASN HB2 H 2.68 . 2 968 . 113 ASN HB3 H 2.76 . 2 969 . 114 LEU N N 117.4 . 1 970 . 114 LEU H H 7.82 . 1 971 . 114 LEU CA C 54.5 . 1 972 . 114 LEU HA H 4.19 . 1 973 . 114 LEU CB C 42.6 . 1 974 . 114 LEU HB2 H 1.48 . 1 975 . 114 LEU HB3 H 1.48 . 1 976 . 114 LEU HD1 H 0.58 . 1 977 . 114 LEU HD2 H 0.51 . 1 978 . 114 LEU CD1 C 25.1 . 1 979 . 114 LEU CD2 C 23.0 . 1 980 . 115 GLN N N 115.1 . 1 981 . 115 GLN H H 6.96 . 1 982 . 115 GLN CA C 56.4 . 1 983 . 115 GLN HA H 4.00 . 1 984 . 116 LEU N N 122.2 . 1 985 . 116 LEU H H 8.26 . 1 986 . 116 LEU CA C 54.9 . 1 987 . 116 LEU HA H 4.22 . 1 988 . 116 LEU CB C 41.9 . 1 989 . 116 LEU HB2 H 1.47 . 1 990 . 116 LEU HB3 H 1.47 . 1 991 . 116 LEU HG H 1.56 . 1 992 . 116 LEU HD1 H 0.72 . 1 993 . 116 LEU HD2 H 0.69 . 1 994 . 116 LEU CD1 C 25.4 . 1 995 . 116 LEU CD2 C 23.4 . 1 996 . 117 GLN N N 119.8 . 1 997 . 117 GLN H H 8.24 . 1 998 . 117 GLN CA C 53.2 . 1 999 . 117 GLN HA H 4.57 . 1 1000 . 117 GLN CB C 29.0 . 1 1001 . 117 GLN HB2 H 1.86 . 1 1002 . 117 GLN HB3 H 2.03 . 1 1003 . 117 GLN CG C 33.1 . 1 1004 . 117 GLN HG2 H 2.30 . 1 1005 . 117 GLN HG3 H 2.30 . 1 1006 . 117 GLN NE2 N 111.6 . 1 1007 . 117 GLN HE21 H 7.46 . 1 1008 . 117 GLN HE22 H 6.78 . 1 1009 . 118 PRO CD C 50.3 . 1 1010 . 118 PRO CA C 63.4 . 1 1011 . 118 PRO HA H 4.36 . 1 1012 . 118 PRO CB C 31.9 . 1 1013 . 118 PRO HB2 H 1.93 . 2 1014 . 118 PRO HB3 H 2.23 . 2 1015 . 118 PRO CG C 27.3 . 1 1016 . 118 PRO HG2 H 1.94 . 2 1017 . 118 PRO HG3 H 2.02 . 2 1018 . 118 PRO HD2 H 3.65 . 2 1019 . 118 PRO HD3 H 3.71 . 2 1020 . 119 GLY N N 108.4 . 1 1021 . 119 GLY H H 8.44 . 1 1022 . 119 GLY CA C 45.1 . 1 1023 . 119 GLY HA2 H 3.90 . 1 1024 . 119 GLY HA3 H 3.90 . 1 1025 . 120 ASN N N 118.4 . 1 1026 . 120 ASN H H 8.21 . 1 1027 . 120 ASN CA C 53.2 . 1 1028 . 120 ASN HA H 4.70 . 1 1029 . 120 ASN CB C 39.0 . 1 1030 . 120 ASN HB2 H 2.71 . 2 1031 . 120 ASN HB3 H 2.80 . 2 1032 . 120 ASN ND2 N 112.2 . 1 1033 . 120 ASN HD21 H 7.55 . 1 1034 . 120 ASN HD22 H 6.87 . 1 1035 . 121 ALA N N 123.6 . 1 1036 . 121 ALA H H 8.15 . 1 1037 . 121 ALA CA C 52.2 . 1 1038 . 121 ALA HA H 4.26 . 1 1039 . 121 ALA HB H 1.32 . 1 1040 . 121 ALA CB C 19.3 . 1 1041 . 122 LYS N N 120.3 . 1 1042 . 122 LYS H H 8.19 . 1 1043 . 122 LYS CA C 55.9 . 1 1044 . 122 LYS HA H 4.28 . 1 1045 . 122 LYS CB C 32.8 . 1 1046 . 122 LYS HB2 H 1.71 . 2 1047 . 122 LYS HB3 H 1.81 . 2 1048 . 122 LYS HG2 H 1.41 . 1 1049 . 122 LYS HG3 H 1.41 . 1 1050 . 123 LEU N N 128.9 . 1 1051 . 123 LEU H H 7.78 . 1 1052 . 123 LEU CA C 56.8 . 1 1053 . 123 LEU HA H 4.14 . 1 1054 . 123 LEU CB C 43.4 . 1 1055 . 123 LEU HB2 H 1.53 . 1 1056 . 123 LEU HB3 H 1.53 . 1 1057 . 123 LEU CG C 27.3 . 1 1058 . 123 LEU HG H 1.54 . 1 1059 . 123 LEU HD1 H 0.83 . 1 1060 . 123 LEU HD2 H 0.80 . 1 1061 . 123 LEU CD1 C 25.3 . 1 1062 . 123 LEU CD2 C 23.6 . 1 stop_ save_