data_5221 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N resonance assignments for the C-Terminal Region of Ku86 (Ku86CTR) ; _BMRB_accession_number 5221 _BMRB_flat_file_name bmr5221.str _Entry_type original _Submission_date 2001-11-30 _Accession_date 2001-12-03 _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 Harris Richard . . 2 Maman Joseph D. . 3 Hinks John A. . 4 Sankar Andrew . . 5 Pearl Laurence H. . 6 Driscoll Paul C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 437 "13C chemical shifts" 448 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for the C-Terminal Region of Ku86 (Ku86CTR) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22012548 _PubMed_ID 12018486 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Harris Richard . . 2 Maman Joseph D. . 3 Hinks John A. . 4 Sankar Andrew . . 5 Pearl Laurence H. . 6 Driscoll Paul C. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 373 _Page_last 374 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_Ku86CTR _Saveframe_category molecular_system _Mol_system_name 'C-Terminal Region of Ku86' _Abbreviation_common Ku86CTR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ku86CTR $Ku86CTR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ku86CTR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminal region of Ku86' _Abbreviation_common Ku86CTR _Molecular_mass 20741 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 184 _Mol_residue_sequence ; MRGSHHHHHHGMASGTMKKK DQVTAQEIFQDNHEDGPTAK KLKTEQGGAHFSVSSLAEGS VTSVGSVNPAENFRVLVKQK KASFEEASNQLINHIEQFLD TNETPYFMKSIDCIRAFREE AIKFSEEQRFNNFLKALQEK VEIKQLNHFWEIVVQDGITL ITKEEASGSSVTAEEAKKFL APKD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ARG 3 3 GLY 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 GLY 12 12 MET 13 13 ALA 14 14 SER 15 15 GLY 16 16 THR 17 17 MET 18 543 LYS 19 544 LYS 20 545 LYS 21 546 ASP 22 547 GLN 23 548 VAL 24 549 THR 25 550 ALA 26 551 GLN 27 552 GLU 28 553 ILE 29 554 PHE 30 555 GLN 31 556 ASP 32 557 ASN 33 558 HIS 34 559 GLU 35 560 ASP 36 561 GLY 37 562 PRO 38 563 THR 39 564 ALA 40 565 LYS 41 566 LYS 42 567 LEU 43 568 LYS 44 569 THR 45 570 GLU 46 571 GLN 47 572 GLY 48 573 GLY 49 574 ALA 50 575 HIS 51 576 PHE 52 577 SER 53 578 VAL 54 579 SER 55 580 SER 56 581 LEU 57 582 ALA 58 583 GLU 59 584 GLY 60 585 SER 61 586 VAL 62 587 THR 63 588 SER 64 589 VAL 65 590 GLY 66 591 SER 67 592 VAL 68 593 ASN 69 594 PRO 70 595 ALA 71 596 GLU 72 597 ASN 73 598 PHE 74 599 ARG 75 600 VAL 76 601 LEU 77 602 VAL 78 603 LYS 79 604 GLN 80 605 LYS 81 606 LYS 82 607 ALA 83 608 SER 84 609 PHE 85 610 GLU 86 611 GLU 87 612 ALA 88 613 SER 89 614 ASN 90 615 GLN 91 616 LEU 92 617 ILE 93 618 ASN 94 619 HIS 95 620 ILE 96 621 GLU 97 622 GLN 98 623 PHE 99 624 LEU 100 625 ASP 101 626 THR 102 627 ASN 103 628 GLU 104 629 THR 105 630 PRO 106 631 TYR 107 632 PHE 108 633 MET 109 634 LYS 110 635 SER 111 636 ILE 112 637 ASP 113 638 CYS 114 639 ILE 115 640 ARG 116 641 ALA 117 642 PHE 118 643 ARG 119 644 GLU 120 645 GLU 121 646 ALA 122 647 ILE 123 648 LYS 124 649 PHE 125 650 SER 126 651 GLU 127 652 GLU 128 653 GLN 129 654 ARG 130 655 PHE 131 656 ASN 132 657 ASN 133 658 PHE 134 659 LEU 135 660 LYS 136 661 ALA 137 662 LEU 138 663 GLN 139 664 GLU 140 665 LYS 141 666 VAL 142 667 GLU 143 668 ILE 144 669 LYS 145 670 GLN 146 671 LEU 147 672 ASN 148 673 HIS 149 674 PHE 150 675 TRP 151 676 GLU 152 677 ILE 153 678 VAL 154 679 VAL 155 680 GLN 156 681 ASP 157 682 GLY 158 683 ILE 159 684 THR 160 685 LEU 161 686 ILE 162 687 THR 163 688 LYS 164 689 GLU 165 690 GLU 166 691 ALA 167 692 SER 168 693 GLY 169 694 SER 170 695 SER 171 696 VAL 172 697 THR 173 698 ALA 174 699 GLU 175 700 GLU 176 701 ALA 177 702 LYS 178 703 LYS 179 704 PHE 180 705 LEU 181 706 ALA 182 707 PRO 183 708 LYS 184 709 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5912 helicase_II 65.22 120 99.17 99.17 2.94e-79 PDB 1Q2Z "The 3d Solution Structure Of The C-Terminal Region Of Ku86" 65.22 120 99.17 99.17 2.94e-79 DBJ BAD96323 "ATP-dependent DNA helicase II variant [Homo sapiens]" 90.76 732 100.00 100.00 7.28e-109 DBJ BAE01114 "unnamed protein product [Macaca fascicularis]" 90.76 618 97.60 100.00 4.55e-108 DBJ BAF83429 "unnamed protein product [Homo sapiens]" 90.76 732 100.00 100.00 6.07e-109 DBJ BAH24115 "X-ray repair complementing defective repair in Chinese hamster cells 5 [synthetic construct]" 90.76 732 100.00 100.00 6.20e-109 EMBL CAA40736 "nuclear factor IV [Homo sapiens]" 90.76 628 100.00 100.00 5.39e-110 EMBL CAH92321 "hypothetical protein [Pongo abelii]" 90.76 732 97.60 100.00 3.25e-107 GB AAA36154 "Ku (p70/p80) subunit [Homo sapiens]" 90.76 732 100.00 100.00 6.20e-109 GB AAA59475 "Ku antigen [Homo sapiens]" 90.76 732 100.00 100.00 6.20e-109 GB AAH19027 "X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining) [Homo sapiens]" 90.76 732 100.00 100.00 6.20e-109 GB AAH95442 "X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining) [Homo sapiens]" 90.76 732 100.00 100.00 6.20e-109 GB AAR11279 "Ku autoantigen [Pan troglodytes]" 62.50 138 99.13 100.00 7.91e-75 REF NP_001126362 "X-ray repair cross-complementing protein 5 [Pongo abelii]" 90.76 732 97.60 100.00 3.25e-107 REF NP_001244295 "X-ray repair cross-complementing protein 5 [Macaca mulatta]" 90.76 732 97.60 100.00 6.30e-107 REF NP_066964 "X-ray repair cross-complementing protein 5 [Homo sapiens]" 90.76 732 100.00 100.00 6.20e-109 REF XP_001151873 "PREDICTED: X-ray repair cross-complementing protein 5 [Pan troglodytes]" 90.76 827 99.40 100.00 1.69e-107 REF XP_003254095 "PREDICTED: X-ray repair cross-complementing protein 5 [Nomascus leucogenys]" 90.76 732 98.20 100.00 1.99e-107 SP P13010 "RecName: Full=X-ray repair cross-complementing protein 5; AltName: Full=86 kDa subunit of Ku antigen; AltName: Full=ATP-depende" 90.76 732 100.00 100.00 6.20e-109 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ku86CTR 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 _Variant _Vector_type _Vector_name _Details $Ku86CTR 'recombinant technology' 'E. coli' Escherichia coli 'BL21 Star' DE3 plasmid pET ; Expressed construct contains an N-terminal hexahistidine purification tag: MGSSHHHHHHSSGLVPRGS before the initiating Met of GABARAP. ; 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Ku86CTR . mM 1.0 1.5 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPIPE _Saveframe_category software _Name nmrPIPE _Version . loop_ _Task 'data processing' stop_ _Details ; Delaglio et al. Journal of Biomolecular NMR (1995) 6, 277-293. ; save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version v3.3 loop_ _Task 'spectral analysis' stop_ _Details ; Kraulis et al. Biochemistry (1994) 33, 3315-3531 ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _Sample_label . save_ save_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_H(CCO)NH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label . save_ save_(H)C(CO)NH-TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 8.0 0.2 n/a temperature 298 0.2 K 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Ku86CTR _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 . 34 GLU N N 122.182 0.05 1 2 . 34 GLU H H 8.34 0.005 1 3 . 34 GLU CA C 56.7 0.05 1 4 . 34 GLU C C 176.362 0.05 1 5 . 34 GLU CB C 30.15 0.05 1 6 . 34 GLU HA H 4.246 0.005 1 7 . 34 GLU HB2 H 1.885 0.005 2 8 . 34 GLU HB3 H 2.016 0.005 2 9 . 34 GLU HG2 H 2.174 0.005 1 10 . 35 ASP N N 121.159 0.05 1 11 . 35 ASP H H 8.437 0.005 1 12 . 35 ASP CA C 54.219 0.05 1 13 . 35 ASP C C 176.606 0.05 1 14 . 35 ASP CB C 41.469 0.05 1 15 . 35 ASP HA H 4.665 0.005 1 16 . 35 ASP HB2 H 2.608 0.005 2 17 . 35 ASP HB3 H 2.701 0.005 2 18 . 36 GLY N N 108.816 0.05 1 19 . 36 GLY H H 8.112 0.005 1 20 . 36 GLY CA C 44.855 0.05 1 21 . 36 GLY HA2 H 4.108 0.005 1 22 . 69 PRO CA C 65.226 0.05 1 23 . 69 PRO C C 178.926 0.05 1 24 . 69 PRO CB C 31.168 0.05 1 25 . 69 PRO CG C 27.641 0.05 1 26 . 69 PRO HA H 4.222 0.005 1 27 . 70 ALA N N 120.431 0.05 1 28 . 70 ALA H H 8.22 0.005 1 29 . 70 ALA CA C 56.008 0.05 1 30 . 70 ALA C C 179.041 0.05 1 31 . 70 ALA CB C 18.459 0.05 1 32 . 70 ALA HA H 3.958 0.005 1 33 . 70 ALA HB H 1.517 0.005 1 34 . 71 GLU N N 116.52 0.05 1 35 . 71 GLU H H 7.553 0.005 1 36 . 71 GLU CA C 58.868 0.05 1 37 . 71 GLU C C 179.438 0.05 1 38 . 71 GLU CB C 29.485 0.05 1 39 . 71 GLU CG C 36.029 0.05 1 40 . 71 GLU HA H 4.112 0.005 1 41 . 71 GLU HB2 H 2.012 0.005 1 42 . 71 GLU HG2 H 2.347 0.005 1 43 . 72 ASN N N 116.71 0.05 1 44 . 72 ASN H H 8.308 0.005 1 45 . 72 ASN CA C 56.088 0.05 1 46 . 72 ASN C C 176.716 0.05 1 47 . 72 ASN CB C 39.3 0.05 1 48 . 72 ASN HA H 4.334 0.005 1 49 . 72 ASN HB2 H 2.867 0.005 1 50 . 73 PHE N N 118.556 0.05 1 51 . 73 PHE H H 8.155 0.005 1 52 . 73 PHE CA C 61.127 0.05 1 53 . 73 PHE C C 175.302 0.05 1 54 . 73 PHE CB C 39.436 0.05 1 55 . 73 PHE HA H 4.035 0.005 1 56 . 73 PHE HB2 H 3.131 0.005 2 57 . 73 PHE HB3 H 3.292 0.005 2 58 . 74 ARG N N 116.629 0.05 1 59 . 74 ARG H H 7.679 0.005 1 60 . 74 ARG CA C 60.438 0.05 1 61 . 74 ARG C C 178.957 0.05 1 62 . 74 ARG CB C 30.714 0.05 1 63 . 74 ARG CG C 29.329 0.05 1 64 . 74 ARG CD C 44.19 0.05 1 65 . 74 ARG HA H 3.393 0.005 1 66 . 74 ARG HB2 H 1.99 0.005 2 67 . 74 ARG HB3 H 2.229 0.005 2 68 . 74 ARG HG2 H 1.741 0.005 1 69 . 75 VAL N N 117.756 0.05 1 70 . 75 VAL H H 7.861 0.005 1 71 . 75 VAL CA C 66.58 0.05 1 72 . 75 VAL C C 178.198 0.05 1 73 . 75 VAL CB C 31.853 0.05 1 74 . 75 VAL CG1 C 21.047 0.05 2 75 . 75 VAL CG2 C 22.866 0.05 2 76 . 75 VAL HA H 3.575 0.005 1 77 . 75 VAL HB H 2.121 0.005 1 78 . 75 VAL HG1 H 0.876 0.005 2 79 . 75 VAL HG2 H 1.082 0.005 2 80 . 76 LEU N N 119.24 0.05 1 81 . 76 LEU H H 8.015 0.005 1 82 . 76 LEU CA C 58.427 0.05 1 83 . 76 LEU C C 180.2 0.05 1 84 . 76 LEU CB C 42.385 0.05 1 85 . 76 LEU CG C 25.49 0.05 1 86 . 76 LEU CD1 C 23.804 0.05 1 87 . 76 LEU HA H 3.76 0.005 1 88 . 76 LEU HB2 H 1.136 0.005 2 89 . 76 LEU HB3 H 1.675 0.005 2 90 . 76 LEU HD1 H 0.657 0.005 1 91 . 77 VAL N N 110.093 0.05 1 92 . 77 VAL H H 7.412 0.005 1 93 . 77 VAL CA C 64.344 0.05 1 94 . 77 VAL C C 179.069 0.05 1 95 . 77 VAL CB C 30.694 0.05 1 96 . 77 VAL CG1 C 19.505 0.05 2 97 . 77 VAL CG2 C 22.325 0.05 2 98 . 77 VAL HA H 3.789 0.005 1 99 . 78 LYS N N 121.041 0.05 1 100 . 78 LYS H H 7.963 0.005 1 101 . 78 LYS CA C 59.236 0.05 1 102 . 78 LYS C C 178.933 0.05 1 103 . 78 LYS CB C 32.684 0.05 1 104 . 78 LYS CG C 25.377 0.05 1 105 . 78 LYS CD C 29.329 0.05 1 106 . 78 LYS CE C 41.977 0.05 1 107 . 78 LYS HA H 4.213 0.005 1 108 . 78 LYS HB2 H 1.972 0.005 2 109 . 78 LYS HB3 H 2.011 0.005 2 110 . 78 LYS HD2 H 1.619 0.005 2 111 . 78 LYS HD3 H 1.737 0.005 2 112 . 79 GLN N N 114.663 0.05 1 113 . 79 GLN H H 8.04 0.005 1 114 . 79 GLN CA C 55.901 0.05 1 115 . 79 GLN C C 175.826 0.05 1 116 . 79 GLN CB C 28.481 0.05 1 117 . 79 GLN CG C 34.296 0.05 1 118 . 79 GLN HA H 4.317 0.005 1 119 . 79 GLN HG2 H 2.409 0.005 2 120 . 79 GLN HG3 H 2.574 0.005 2 121 . 80 LYS N N 115.519 0.05 1 122 . 80 LYS H H 7.69 0.005 1 123 . 80 LYS CA C 57.193 0.05 1 124 . 80 LYS C C 176.61 0.05 1 125 . 80 LYS CB C 29.606 0.05 1 126 . 80 LYS HA H 4.101 0.005 1 127 . 81 LYS C C 176.489 0.05 1 128 . 81 LYS CB C 33.141 0.05 1 129 . 81 LYS CA C 56.669 0.05 1 130 . 81 LYS CG C 25.32 0.05 1 131 . 81 LYS CD C 28.811 0.05 1 132 . 81 LYS CE C 42.092 0.05 1 133 . 81 LYS HA H 4.216 0.005 1 134 . 81 LYS HB2 H 1.67 0.005 2 135 . 81 LYS HB3 H 1.932 0.005 2 136 . 81 LYS HG2 H 1.372 0.005 2 137 . 81 LYS HG3 H 1.435 0.005 2 138 . 81 LYS HD3 H 1.655 0.005 1 139 . 82 ALA N N 119.813 0.05 1 140 . 82 ALA H H 7.674 0.005 1 141 . 82 ALA CA C 50.658 0.05 1 142 . 82 ALA C C 176.572 0.05 1 143 . 82 ALA CB C 21.954 0.05 1 144 . 82 ALA HA H 4.432 0.005 1 145 . 82 ALA HB H 1.227 0.005 1 146 . 83 SER N N 115.806 0.05 1 147 . 83 SER H H 8.662 0.005 1 148 . 83 SER CA C 57.185 0.05 1 149 . 83 SER C C 174.422 0.05 1 150 . 83 SER CB C 64.135 0.05 1 151 . 83 SER HA H 4.411 0.005 1 152 . 84 PHE CA C 62.26 0.05 1 153 . 84 PHE C C 179.803 0.05 1 154 . 84 PHE CB C 38.896 0.05 1 155 . 84 PHE HA H 3.627 0.005 1 156 . 85 GLU N N 121.389 0.05 1 157 . 85 GLU H H 9.2 0.005 1 158 . 85 GLU CA C 60.534 0.05 1 159 . 85 GLU C C 176.756 0.05 1 160 . 85 GLU CB C 30.116 0.05 1 161 . 85 GLU CG C 35.673 0.05 1 162 . 85 GLU HA H 3.656 0.005 1 163 . 85 GLU HB2 H 2.117 0.005 2 164 . 85 GLU HB3 H 2.175 0.005 2 165 . 86 GLU N N 119.598 0.05 1 166 . 86 GLU H H 7.951 0.005 1 167 . 86 GLU CA C 59.214 0.05 1 168 . 86 GLU C C 179.583 0.05 1 169 . 86 GLU CB C 29.606 0.05 1 170 . 86 GLU CG C 36.06 0.05 1 171 . 86 GLU HA H 4.003 0.005 1 172 . 86 GLU HB2 H 1.941 0.005 2 173 . 86 GLU HB3 H 2.118 0.005 2 174 . 86 GLU HG2 H 2.242 0.005 1 175 . 87 ALA N N 120.395 0.05 1 176 . 87 ALA H H 8.558 0.005 1 177 . 87 ALA CA C 54.819 0.05 1 178 . 87 ALA C C 180.735 0.05 1 179 . 87 ALA CB C 18.834 0.05 1 180 . 87 ALA HA H 3.859 0.005 1 181 . 87 ALA HB H 1.106 0.005 1 182 . 88 SER N N 113.5 0.05 1 183 . 88 SER H H 8.677 0.005 1 184 . 88 SER CA C 61.802 0.05 1 185 . 88 SER C C 175.667 0.05 1 186 . 88 SER CB C 63.13 0.05 1 187 . 88 SER HA H 4.407 0.005 1 188 . 88 SER HB2 H 3.111 0.005 2 189 . 88 SER HB3 H 3.359 0.005 2 190 . 89 ASN N N 123.339 0.05 1 191 . 89 ASN H H 8.214 0.005 1 192 . 89 ASN CA C 55.932 0.05 1 193 . 89 ASN C C 178.809 0.05 1 194 . 89 ASN CB C 37.143 0.05 1 195 . 89 ASN HA H 4.393 0.005 1 196 . 89 ASN HB2 H 2.705 0.005 2 197 . 89 ASN HB3 H 2.963 0.005 2 198 . 90 GLN N N 119.297 0.05 1 199 . 90 GLN H H 7.593 0.005 1 200 . 90 GLN CA C 58.652 0.05 1 201 . 90 GLN C C 178.643 0.05 1 202 . 90 GLN CB C 28.752 0.05 1 203 . 90 GLN HA H 3.98 0.005 1 204 . 90 GLN CG C 33.643 0.05 1 205 . 91 LEU N N 121.142 0.05 1 206 . 91 LEU H H 7.667 0.005 1 207 . 91 LEU CA C 58.284 0.05 1 208 . 91 LEU C C 178.597 0.05 1 209 . 91 LEU CB C 42.385 0.05 1 210 . 91 LEU HA H 3.936 0.005 1 211 . 91 LEU CD1 C 24.075 0.05 1 212 . 91 LEU HG H 1.423 0.005 1 213 . 91 LEU HD1 H -0.23 0.005 2 214 . 91 LEU HD2 H 0.676 0.005 2 215 . 91 LEU HB2 H 1.45 0.005 1 216 . 92 ILE N N 119.324 0.05 1 217 . 92 ILE H H 8.518 0.005 1 218 . 92 ILE CA C 66.123 0.05 1 219 . 92 ILE C C 177.505 0.05 1 220 . 92 ILE CB C 38.005 0.05 1 221 . 92 ILE CG1 C 29.078 0.05 1 222 . 92 ILE CG2 C 16.83 0.05 1 223 . 92 ILE CD1 C 13.685 0.05 1 224 . 92 ILE HA H 3.264 0.005 1 225 . 92 ILE HB H 1.728 0.005 1 226 . 92 ILE HG2 H 0.932 0.005 1 227 . 92 ILE HD1 H 0.781 0.005 1 228 . 93 ASN N N 117.456 0.05 1 229 . 93 ASN H H 7.436 0.005 1 230 . 93 ASN CA C 56.486 0.05 1 231 . 93 ASN C C 178.427 0.05 1 232 . 93 ASN CB C 37.988 0.05 1 233 . 93 ASN HA H 4.358 0.005 1 234 . 93 ASN HB2 H 2.593 0.005 2 235 . 93 ASN HB3 H 2.698 0.005 2 236 . 94 HIS N N 118.071 0.05 1 237 . 94 HIS H H 7.447 0.005 1 238 . 94 HIS CA C 60.213 0.05 1 239 . 94 HIS C C 176.913 0.05 1 240 . 94 HIS CB C 29.807 0.05 1 241 . 94 HIS HA H 3.975 0.005 1 242 . 94 HIS HB2 H 3.036 0.005 1 243 . 95 ILE N N 118.633 0.05 1 244 . 95 ILE H H 8.295 0.005 1 245 . 95 ILE CA C 66.44 0.05 1 246 . 95 ILE C C 177.814 0.05 1 247 . 95 ILE CB C 38.051 0.05 1 248 . 95 ILE CG1 C 29.978 0.05 1 249 . 95 ILE CG2 C 16.438 0.05 1 250 . 95 ILE CD1 C 14.615 0.05 1 251 . 95 ILE HA H 3.607 0.005 1 252 . 95 ILE HB H 2.166 0.005 1 253 . 96 GLU N N 117.095 0.05 1 254 . 96 GLU H H 8.392 0.005 1 255 . 96 GLU CA C 60.581 0.05 1 256 . 96 GLU C C 179.166 0.05 1 257 . 96 GLU CB C 29.314 0.05 1 258 . 96 GLU CG C 37.195 0.05 1 259 . 96 GLU HA H 3.766 0.005 1 260 . 96 GLU HB2 H 2.012 0.005 2 261 . 96 GLU HB3 H 2.122 0.005 2 262 . 96 GLU HG2 H 2.548 0.005 1 263 . 97 GLN N N 118.34 0.05 1 264 . 97 GLN H H 7.606 0.005 1 265 . 97 GLN CA C 59.036 0.05 1 266 . 97 GLN C C 180.148 0.05 1 267 . 97 GLN CB C 28.31 0.05 1 268 . 97 GLN CG C 34.201 0.05 1 269 . 97 GLN HA H 4.047 0.005 1 270 . 97 GLN HG2 H 2.301 0.005 2 271 . 97 GLN HG3 H 2.476 0.005 2 272 . 97 GLN HB2 H 2.05 0.005 1 273 . 98 PHE N N 119.55 0.05 1 274 . 98 PHE H H 8.688 0.005 1 275 . 98 PHE CA C 57.19 0.05 1 276 . 98 PHE C C 180.091 0.05 1 277 . 98 PHE CB C 37.094 0.05 1 278 . 98 PHE HA H 4.558 0.005 1 279 . 98 PHE HB2 H 3.401 0.005 2 280 . 98 PHE HB3 H 3.783 0.005 2 281 . 99 LEU N N 121.01 0.05 1 282 . 99 LEU H H 8.667 0.005 1 283 . 99 LEU CA C 58.131 0.05 1 284 . 99 LEU C C 179.703 0.05 1 285 . 99 LEU CB C 40.858 0.05 1 286 . 99 LEU CG C 25.203 0.05 1 287 . 99 LEU CD1 C 21.847 0.05 1 288 . 99 LEU HA H 4.116 0.005 1 289 . 99 LEU HB2 H 1.315 0.005 2 290 . 99 LEU HB3 H 1.832 0.005 2 291 . 99 LEU HG H 0.416 0.005 1 292 . 99 LEU HD1 H -0.017 0.005 1 293 . 100 ASP N N 117.674 0.05 1 294 . 100 ASP H H 7.664 0.005 1 295 . 100 ASP CA C 56.187 0.05 1 296 . 100 ASP C C 178.088 0.05 1 297 . 100 ASP CB C 40.753 0.05 1 298 . 100 ASP HA H 4.587 0.005 1 299 . 100 ASP HB2 H 2.719 0.005 2 300 . 100 ASP HB3 H 2.779 0.005 2 301 . 101 THR N N 108.815 0.05 1 302 . 101 THR H H 7.392 0.005 1 303 . 101 THR CA C 64.277 0.05 1 304 . 101 THR C C 176.779 0.05 1 305 . 101 THR CB C 70.218 0.05 1 306 . 101 THR HA H 4.062 0.005 1 307 . 101 THR HB H 4.045 0.005 1 308 . 102 ASN N N 114.795 0.05 1 309 . 102 ASN H H 7.905 0.005 1 310 . 102 ASN CA C 54.494 0.05 1 311 . 102 ASN C C 174.484 0.05 1 312 . 102 ASN CB C 38.914 0.05 1 313 . 102 ASN HA H 4.622 0.005 1 314 . 102 ASN HB2 H 2.697 0.005 2 315 . 102 ASN HB3 H 3.389 0.005 2 316 . 103 GLU N N 116.416 0.05 1 317 . 103 GLU H H 7.436 0.005 1 318 . 103 GLU CA C 54.696 0.05 1 319 . 103 GLU C C 176.907 0.05 1 320 . 103 GLU CB C 33.141 0.05 1 321 . 103 GLU HA H 4.611 0.005 1 322 . 103 GLU HB2 H 2.075 0.005 1 323 . 105 PRO CA C 66.327 0.05 1 324 . 105 PRO C C 180.217 0.05 1 325 . 105 PRO CB C 30.909 0.05 1 326 . 105 PRO CG C 28.473 0.05 1 327 . 105 PRO HA H 4.271 0.005 1 328 . 105 PRO HB2 H 1.945 0.005 1 329 . 106 TYR N N 115.216 0.05 1 330 . 106 TYR H H 6.988 0.005 1 331 . 106 TYR CA C 61.594 0.05 1 332 . 106 TYR C C 179.887 0.05 1 333 . 106 TYR CB C 37.833 0.05 1 334 . 106 TYR HA H 4.025 0.005 1 335 . 106 TYR HB2 H 3.088 0.005 1 336 . 107 PHE N N 123.972 0.05 1 337 . 107 PHE H H 8.364 0.005 1 338 . 107 PHE CA C 57.821 0.05 1 339 . 107 PHE C C 179.449 0.05 1 340 . 107 PHE CB C 36.605 0.05 1 341 . 107 PHE HA H 4.74 0.005 1 342 . 107 PHE HB2 H 3.424 0.005 2 343 . 107 PHE HB3 H 3.997 0.005 2 344 . 108 MET N N 117.319 0.05 1 345 . 108 MET H H 8.406 0.005 1 346 . 108 MET CA C 57.628 0.05 1 347 . 108 MET C C 179.979 0.05 1 348 . 108 MET CB C 29.62 0.05 1 349 . 108 MET CG C 31.6 0.05 1 350 . 108 MET HA H 4.49 0.005 1 351 . 108 MET HB2 H 2.214 0.005 1 352 . 108 MET HG2 H 2.822 0.005 1 353 . 109 LYS N N 120.774 0.05 1 354 . 109 LYS H H 7.637 0.005 1 355 . 109 LYS CA C 59.714 0.05 1 356 . 109 LYS C C 180.303 0.05 1 357 . 109 LYS CB C 32.75 0.05 1 358 . 109 LYS CG C 25.17 0.05 1 359 . 109 LYS CD C 29.478 0.05 1 360 . 109 LYS CE C 41.777 0.05 1 361 . 109 LYS HA H 4.28 0.005 1 362 . 109 LYS HB2 H 1.497 0.005 2 363 . 109 LYS HB3 H 1.592 0.005 2 364 . 109 LYS HG2 H 1.122 0.005 2 365 . 109 LYS HG3 H 1.306 0.005 2 366 . 110 SER N N 116.374 0.05 1 367 . 110 SER H H 8.275 0.005 1 368 . 110 SER C C 176.71 0.05 1 369 . 110 SER CB C 64.512 0.05 1 370 . 110 SER HA H 4.436 0.005 1 371 . 111 ILE N N 123.599 0.05 1 372 . 111 ILE H H 8.237 0.005 1 373 . 111 ILE CA C 64.019 0.05 1 374 . 111 ILE C C 177.964 0.05 1 375 . 111 ILE CB C 35.588 0.05 1 376 . 111 ILE CG2 C 16.993 0.05 1 377 . 111 ILE CD1 C 11.12 0.05 1 378 . 111 ILE HA H 3.908 0.005 1 379 . 111 ILE HB H 2.427 0.005 1 380 . 111 ILE HG2 H 0.947 0.005 1 381 . 111 ILE HD1 H 0.586 0.005 1 382 . 112 ASP N N 120.568 0.05 1 383 . 112 ASP H H 7.794 0.005 1 384 . 112 ASP CA C 58.071 0.05 1 385 . 112 ASP C C 180.3 0.05 1 386 . 112 ASP CB C 40.396 0.05 1 387 . 112 ASP HA H 4.499 0.005 1 388 . 112 ASP HB2 H 2.811 0.005 2 389 . 112 ASP HB3 H 3.073 0.005 2 390 . 113 CYS N N 116.444 0.05 1 391 . 113 CYS H H 7.943 0.005 1 392 . 113 CYS CA C 64.521 0.05 1 393 . 113 CYS C C 176.323 0.05 1 394 . 113 CYS CB C 27.975 0.05 1 395 . 113 CYS HA H 4.088 0.005 1 396 . 114 ILE N N 121.631 0.05 1 397 . 114 ILE H H 8.851 0.005 1 398 . 114 ILE CA C 67.009 0.05 1 399 . 114 ILE C C 177.72 0.05 1 400 . 114 ILE CB C 38.306 0.05 1 401 . 114 ILE CG1 C 30.616 0.05 1 402 . 114 ILE CG2 C 18.979 0.05 1 403 . 114 ILE CD1 C 13.76 0.05 1 404 . 114 ILE HA H 3.789 0.005 1 405 . 114 ILE HB H 2.226 0.005 1 406 . 114 ILE HG2 H 1.155 0.005 1 407 . 114 ILE HG12 H 1.345 0.005 1 408 . 115 ARG N N 119.56 0.05 1 409 . 115 ARG H H 8.917 0.005 1 410 . 115 ARG CA C 60.548 0.05 1 411 . 115 ARG C C 178.848 0.05 1 412 . 115 ARG CB C 30.595 0.05 1 413 . 115 ARG CG C 28.383 0.05 1 414 . 115 ARG CD C 43.645 0.05 1 415 . 115 ARG HA H 3.902 0.005 1 416 . 115 ARG HB2 H 1.933 0.005 1 417 . 115 ARG HG2 H 1.594 0.005 1 418 . 115 ARG HD2 H 3.246 0.005 1 419 . 116 ALA N N 120.74 0.05 1 420 . 116 ALA H H 7.783 0.005 1 421 . 116 ALA CA C 55.614 0.05 1 422 . 116 ALA C C 179.322 0.05 1 423 . 116 ALA CB C 18.591 0.05 1 424 . 116 ALA HA H 4.296 0.005 1 425 . 117 PHE N N 117.998 0.05 1 426 . 117 PHE H H 8.206 0.005 1 427 . 117 PHE CA C 57.392 0.05 1 428 . 117 PHE C C 177.523 0.05 1 429 . 117 PHE CB C 38.005 0.05 1 430 . 117 PHE HA H 4.541 0.005 1 431 . 117 PHE HB2 H 3.076 0.005 1 432 . 118 ARG N N 120.595 0.05 1 433 . 118 ARG H H 8.42 0.005 1 434 . 118 ARG CA C 60.393 0.05 1 435 . 118 ARG C C 177.614 0.05 1 436 . 118 ARG CB C 30.942 0.05 1 437 . 118 ARG CG C 28.186 0.05 1 438 . 118 ARG CD C 43.165 0.05 1 439 . 119 GLU N N 114.894 0.05 1 440 . 119 GLU H H 8.048 0.005 1 441 . 119 GLU CA C 59.267 0.05 1 442 . 119 GLU C C 181.543 0.05 1 443 . 119 GLU CB C 30.464 0.05 1 444 . 119 GLU CG C 36.434 0.05 1 445 . 119 GLU HA H 3.9 0.005 1 446 . 119 GLU HB2 H 2.092 0.005 2 447 . 119 GLU HB3 H 2.281 0.005 2 448 . 119 GLU HG2 H 2.295 0.005 2 449 . 119 GLU HG3 H 2.603 0.005 2 450 . 120 GLU N N 116.399 0.05 1 451 . 120 GLU H H 8.694 0.005 1 452 . 120 GLU CA C 57.597 0.05 1 453 . 120 GLU C C 179.35 0.05 1 454 . 120 GLU CB C 29.062 0.05 1 455 . 120 GLU CG C 35.568 0.05 1 456 . 120 GLU HA H 4.772 0.005 1 457 . 121 ALA N N 122.246 0.05 1 458 . 121 ALA H H 9.315 0.005 1 459 . 121 ALA CA C 55.852 0.05 1 460 . 121 ALA C C 180.602 0.05 1 461 . 121 ALA CB C 18.263 0.05 1 462 . 121 ALA HA H 3.955 0.005 1 463 . 121 ALA HB H 1.482 0.005 1 464 . 122 ILE N N 116.576 0.05 1 465 . 122 ILE H H 7.514 0.005 1 466 . 122 ILE CA C 66.215 0.05 1 467 . 122 ILE C C 179.338 0.05 1 468 . 122 ILE CB C 38.578 0.05 1 469 . 122 ILE CG1 C 30.757 0.05 1 470 . 122 ILE CG2 C 16.641 0.05 1 471 . 122 ILE CD1 C 13.847 0.05 1 472 . 122 ILE HA H 3.596 0.005 1 473 . 122 ILE HB H 1.907 0.005 1 474 . 122 ILE HG2 H 0.944 0.005 1 475 . 123 LYS N N 119.805 0.05 1 476 . 123 LYS H H 7.311 0.005 1 477 . 123 LYS CA C 59.37 0.05 1 478 . 123 LYS C C 178.779 0.05 1 479 . 123 LYS CB C 32.537 0.05 1 480 . 123 LYS CG C 24.927 0.05 1 481 . 123 LYS CD C 29.126 0.05 1 482 . 123 LYS CE C 41.825 0.05 1 483 . 123 LYS HA H 3.944 0.005 1 484 . 123 LYS HB2 H 1.695 0.005 2 485 . 123 LYS HB3 H 1.923 0.005 2 486 . 123 LYS HG2 H 1.251 0.005 2 487 . 123 LYS HG3 H 1.466 0.005 2 488 . 123 LYS HD3 H 1.687 0.005 1 489 . 124 PHE N N 114.777 0.05 1 490 . 124 PHE H H 8.23 0.005 1 491 . 124 PHE CA C 58.741 0.05 1 492 . 124 PHE C C 174.613 0.05 1 493 . 124 PHE CB C 38.296 0.05 1 494 . 124 PHE HA H 4.525 0.005 1 495 . 124 PHE HB2 H 2.428 0.005 2 496 . 124 PHE HB3 H 3.346 0.005 2 497 . 125 SER N N 112.944 0.05 1 498 . 125 SER H H 7.573 0.005 1 499 . 125 SER CA C 59.6 0.05 1 500 . 125 SER C C 175.551 0.05 1 501 . 125 SER CB C 60.873 0.05 1 502 . 125 SER HA H 4.46 0.005 1 503 . 125 SER HB2 H 4.271 0.005 1 504 . 126 GLU N N 120.33 0.05 1 505 . 126 GLU H H 8.91 0.005 1 506 . 126 GLU CA C 54.316 0.05 1 507 . 126 GLU C C 177.294 0.05 1 508 . 126 GLU CB C 29.511 0.05 1 509 . 126 GLU CG C 32.933 0.05 1 510 . 126 GLU HA H 4.633 0.005 1 511 . 126 GLU HG2 H 0.915 0.005 2 512 . 126 GLU HG3 H 1.847 0.005 2 513 . 126 GLU HB2 H 2.454 0.005 1 514 . 127 GLU N N 121.583 0.05 1 515 . 127 GLU H H 10.072 0.005 1 516 . 127 GLU CA C 60.013 0.05 1 517 . 127 GLU C C 178.108 0.05 1 518 . 127 GLU CB C 28.428 0.05 1 519 . 127 GLU CG C 35.032 0.05 1 520 . 127 GLU HA H 3.805 0.005 1 521 . 128 GLN N N 119.319 0.05 1 522 . 128 GLN H H 8.597 0.005 1 523 . 128 GLN CA C 59.13 0.05 1 524 . 128 GLN C C 178.129 0.05 1 525 . 128 GLN CB C 28.187 0.05 1 526 . 128 GLN CG C 34.05 0.05 1 527 . 128 GLN HA H 4.115 0.005 1 528 . 129 ARG N N 119.722 0.05 1 529 . 129 ARG H H 7.847 0.005 1 530 . 129 ARG CA C 59.513 0.05 1 531 . 129 ARG C C 180.433 0.05 1 532 . 129 ARG CB C 30.776 0.05 1 533 . 129 ARG CG C 27.941 0.05 1 534 . 129 ARG CD C 43.477 0.05 1 535 . 129 ARG HA H 4.217 0.005 1 536 . 129 ARG HB2 H 2.24 0.005 2 537 . 129 ARG HB3 H 2.3 0.005 2 538 . 129 ARG HG2 H 1.764 0.005 2 539 . 129 ARG HG3 H 2.124 0.005 2 540 . 130 PHE N N 118.427 0.05 1 541 . 130 PHE H H 7.64 0.005 1 542 . 130 PHE CA C 62.146 0.05 1 543 . 130 PHE C C 175.992 0.05 1 544 . 130 PHE CB C 38.735 0.05 1 545 . 130 PHE HA H 3.586 0.005 1 546 . 130 PHE HB2 H 2.387 0.005 2 547 . 130 PHE HB3 H 2.892 0.005 2 548 . 131 ASN N N 120.456 0.05 1 549 . 131 ASN H H 8.71 0.005 1 550 . 131 ASN CA C 55.53 0.05 1 551 . 131 ASN C C 178.017 0.05 1 552 . 131 ASN CB C 36.799 0.05 1 553 . 131 ASN HA H 4.183 0.005 1 554 . 131 ASN HB2 H 2.643 0.005 2 555 . 131 ASN HB3 H 2.914 0.005 2 556 . 132 ASN N N 117.946 0.05 1 557 . 132 ASN H H 8.595 0.005 1 558 . 132 ASN CA C 55.661 0.05 1 559 . 132 ASN C C 178.842 0.05 1 560 . 132 ASN CB C 37.425 0.05 1 561 . 132 ASN HA H 4.397 0.005 1 562 . 132 ASN HB2 H 2.832 0.005 2 563 . 132 ASN HB3 H 2.947 0.005 2 564 . 133 PHE N N 122.515 0.05 1 565 . 133 PHE H H 7.568 0.005 1 566 . 133 PHE CA C 60.023 0.05 1 567 . 133 PHE C C 176.271 0.05 1 568 . 133 PHE CB C 37.746 0.05 1 569 . 133 PHE HA H 4.476 0.005 1 570 . 133 PHE HB2 H 3.134 0.005 2 571 . 133 PHE HB3 H 3.478 0.005 2 572 . 134 LEU N N 122.984 0.05 1 573 . 134 LEU H H 8.366 0.005 1 574 . 134 LEU CA C 57.48 0.05 1 575 . 134 LEU C C 179.511 0.05 1 576 . 134 LEU CB C 40.846 0.05 1 577 . 134 LEU CG C 25.325 0.05 1 578 . 134 LEU CD1 C 23.089 0.05 1 579 . 134 LEU HA H 3.336 0.005 1 580 . 134 LEU HG H 0.886 0.005 1 581 . 134 LEU HD1 H 0.682 0.005 2 582 . 134 LEU HD2 H 0.74 0.005 2 583 . 134 LEU HB2 H 1.434 0.005 1 584 . 135 LYS N N 117.098 0.05 1 585 . 135 LYS H H 7.833 0.005 1 586 . 135 LYS CA C 60.005 0.05 1 587 . 135 LYS C C 179.26 0.05 1 588 . 135 LYS CB C 32.597 0.05 1 589 . 135 LYS CG C 25.957 0.05 1 590 . 135 LYS CD C 29.503 0.05 1 591 . 135 LYS HA H 4.133 0.005 1 592 . 135 LYS HB2 H 1.806 0.005 2 593 . 135 LYS HB3 H 1.92 0.005 2 594 . 135 LYS HG2 H 1.425 0.005 1 595 . 135 LYS HD3 H 1.664 0.005 1 596 . 135 LYS HE2 H 2.89 0.005 1 597 . 136 ALA N N 122.141 0.05 1 598 . 136 ALA H H 7.592 0.005 1 599 . 136 ALA CA C 54.589 0.05 1 600 . 136 ALA C C 180.914 0.05 1 601 . 136 ALA CB C 17.692 0.05 1 602 . 136 ALA HA H 4.155 0.005 1 603 . 136 ALA HB H 1.469 0.005 1 604 . 137 LEU N N 121.953 0.05 1 605 . 137 LEU H H 8.631 0.005 1 606 . 137 LEU CA C 57.385 0.05 1 607 . 137 LEU C C 178.085 0.05 1 608 . 137 LEU CB C 41.05 0.05 1 609 . 137 LEU CG C 26.284 0.05 1 610 . 137 LEU CD1 C 22.731 0.05 1 611 . 137 LEU HA H 3.904 0.005 1 612 . 137 LEU HG H 1.105 0.005 1 613 . 137 LEU HB2 H 1.832 0.005 1 614 . 137 LEU HD1 H 0.92 0.005 1 615 . 138 GLN N N 118.803 0.05 1 616 . 138 GLN H H 7.963 0.005 1 617 . 138 GLN CA C 59.474 0.05 1 618 . 138 GLN C C 177.954 0.05 1 619 . 138 GLN CB C 28.07 0.05 1 620 . 138 GLN CG C 33.485 0.05 1 621 . 139 GLU N N 116.873 0.05 1 622 . 139 GLU H H 7.238 0.005 1 623 . 139 GLU CA C 59.154 0.05 1 624 . 139 GLU C C 178.821 0.05 1 625 . 139 GLU CB C 29.682 0.05 1 626 . 139 GLU CG C 36.399 0.05 1 627 . 139 GLU HA H 3.872 0.005 1 628 . 140 LYS N N 119.64 0.05 1 629 . 140 LYS H H 7.85 0.005 1 630 . 140 LYS CA C 58.957 0.05 1 631 . 140 LYS C C 178.623 0.05 1 632 . 140 LYS CB C 32.597 0.05 1 633 . 140 LYS CG C 24.929 0.05 1 634 . 140 LYS CD C 29.302 0.05 1 635 . 140 LYS CE C 41.744 0.05 1 636 . 140 LYS HA H 4.032 0.005 1 637 . 140 LYS HB2 H 1.814 0.005 2 638 . 140 LYS HB3 H 1.949 0.005 2 639 . 140 LYS HG2 H 1.387 0.005 2 640 . 140 LYS HG3 H 1.54 0.005 2 641 . 140 LYS HD2 H 1.558 0.005 2 642 . 140 LYS HD3 H 1.634 0.005 2 643 . 141 VAL N N 117.905 0.05 1 644 . 141 VAL H H 8.34 0.005 1 645 . 141 VAL CA C 66.538 0.05 1 646 . 141 VAL C C 178.157 0.05 1 647 . 141 VAL CB C 31.134 0.05 1 648 . 141 VAL CG1 C 21.463 0.05 2 649 . 141 VAL CG2 C 23.068 0.05 2 650 . 141 VAL HA H 3.465 0.005 1 651 . 141 VAL HB H 2.05 0.005 1 652 . 141 VAL HG1 H 0.907 0.005 2 653 . 141 VAL HG2 H 1.077 0.005 2 654 . 142 GLU N N 119.412 0.05 1 655 . 142 GLU H H 7.662 0.005 1 656 . 142 GLU CA C 59.16 0.05 1 657 . 142 GLU C C 180.444 0.05 1 658 . 142 GLU CB C 29.062 0.05 1 659 . 142 GLU HA H 4.036 0.005 1 660 . 142 GLU CG C 36.039 0.05 1 661 . 143 ILE N N 120.577 0.05 1 662 . 143 ILE H H 7.953 0.005 1 663 . 143 ILE CA C 64.429 0.05 1 664 . 143 ILE C C 178.708 0.05 1 665 . 143 ILE CB C 38.186 0.05 1 666 . 143 ILE CG1 C 28.944 0.05 1 667 . 143 ILE CG2 C 17.104 0.05 1 668 . 143 ILE CD1 C 13.227 0.05 1 669 . 143 ILE HA H 3.873 0.005 1 670 . 143 ILE HB H 1.914 0.005 1 671 . 143 ILE HG12 H 1.253 0.005 2 672 . 143 ILE HG13 H 1.681 0.005 2 673 . 143 ILE HG2 H 0.963 0.005 1 674 . 143 ILE HD1 H 0.859 0.005 1 675 . 144 LYS N N 117.314 0.05 1 676 . 144 LYS H H 8.108 0.005 1 677 . 144 LYS CA C 56.261 0.05 1 678 . 144 LYS C C 175.275 0.05 1 679 . 144 LYS CB C 32.614 0.05 1 680 . 144 LYS CG C 25.709 0.05 1 681 . 144 LYS CD C 28.975 0.05 1 682 . 144 LYS CE C 41.674 0.05 1 683 . 144 LYS HA H 4.27 0.005 1 684 . 144 LYS HB2 H 1.656 0.005 2 685 . 144 LYS HB3 H 2.048 0.005 2 686 . 144 LYS HG2 H 1.504 0.005 1 687 . 144 LYS HD3 H 1.609 0.005 1 688 . 144 LYS HE2 H 2.981 0.005 1 689 . 145 GLN N N 115.362 0.05 1 690 . 145 GLN H H 7.758 0.005 1 691 . 145 GLN CA C 56.698 0.05 1 692 . 145 GLN C C 176.951 0.05 1 693 . 145 GLN CB C 25.902 0.05 1 694 . 145 GLN CG C 34.32 0.05 1 695 . 145 GLN HA H 4.014 0.005 1 696 . 145 GLN HB2 H 2.307 0.005 2 697 . 145 GLN HB3 H 2.432 0.005 2 698 . 146 LEU N N 120.522 0.05 1 699 . 146 LEU H H 8.372 0.005 1 700 . 146 LEU CA C 52.859 0.05 1 701 . 146 LEU C C 178.516 0.05 1 702 . 146 LEU CB C 41.925 0.05 1 703 . 146 LEU CG C 26.217 0.05 1 704 . 146 LEU CD1 C 23.637 0.05 1 705 . 146 LEU HA H 4.965 0.005 1 706 . 146 LEU HB2 H 1.654 0.005 2 707 . 146 LEU HB3 H 1.868 0.005 2 708 . 146 LEU HD1 H 0.88 0.005 2 709 . 146 LEU HD2 H 0.975 0.005 2 710 . 147 ASN N N 120.008 0.05 1 711 . 147 ASN H H 8.43 0.005 1 712 . 147 ASN CA C 57.401 0.05 1 713 . 147 ASN C C 177.239 0.05 1 714 . 147 ASN CB C 37.888 0.05 1 715 . 147 ASN HA H 4.3 0.005 1 716 . 148 HIS CA C 58.534 0.05 1 717 . 148 HIS C C 177.995 0.05 1 718 . 148 HIS CB C 29.4 0.05 1 719 . 148 HIS HA H 4.622 0.005 1 720 . 148 HIS HB2 H 3.302 0.005 1 721 . 149 PHE N N 119.067 0.05 1 722 . 149 PHE H H 7.203 0.005 1 723 . 149 PHE CA C 60.093 0.05 1 724 . 149 PHE C C 176.492 0.05 1 725 . 149 PHE CB C 38.288 0.05 1 726 . 149 PHE HA H 3.943 0.005 1 727 . 149 PHE HB2 H 2.667 0.005 1 728 . 150 TRP N N 120.245 0.05 1 729 . 150 TRP H H 7.902 0.005 1 730 . 150 TRP CA C 59.277 0.05 1 731 . 150 TRP C C 176.753 0.05 1 732 . 150 TRP CB C 29.802 0.05 1 733 . 150 TRP NE1 N 129.492 0.05 1 734 . 150 TRP HE1 H 10.111 0.005 1 735 . 150 TRP HA H 3.862 0.005 1 736 . 150 TRP HB2 H 3.18 0.005 2 737 . 150 TRP HB3 H 3.327 0.005 2 738 . 151 GLU N N 114.38 0.05 1 739 . 151 GLU H H 7.89 0.005 1 740 . 151 GLU CA C 59.333 0.05 1 741 . 151 GLU C C 179.059 0.05 1 742 . 151 GLU CB C 29.627 0.05 1 743 . 151 GLU CG C 36.485 0.05 1 744 . 151 GLU HA H 3.846 0.005 1 745 . 151 GLU HB2 H 2.019 0.005 2 746 . 151 GLU HB3 H 2.137 0.005 2 747 . 151 GLU HG2 H 2.314 0.005 2 748 . 151 GLU HG3 H 2.469 0.005 2 749 . 152 ILE N N 119.383 0.05 1 750 . 152 ILE H H 7.141 0.005 1 751 . 152 ILE CA C 64.909 0.05 1 752 . 152 ILE C C 178.063 0.05 1 753 . 152 ILE CB C 37.693 0.05 1 754 . 152 ILE CG1 C 28.133 0.05 1 755 . 152 ILE CG2 C 17.91 0.05 1 756 . 152 ILE HA H 3.546 0.005 1 757 . 152 ILE HB H 1.775 0.005 1 758 . 153 VAL N N 121.648 0.05 1 759 . 153 VAL H H 6.706 0.005 1 760 . 153 VAL CA C 67.162 0.05 1 761 . 153 VAL C C 177.817 0.05 1 762 . 153 VAL CB C 31.015 0.05 1 763 . 153 VAL CG1 C 20.264 0.05 2 764 . 153 VAL CG2 C 23.239 0.05 2 765 . 153 VAL HA H 3.858 0.005 1 766 . 153 VAL HB H 2.901 0.005 1 767 . 153 VAL HG2 H 0.069 0.005 1 768 . 154 VAL N N 116.876 0.05 1 769 . 154 VAL H H 7.763 0.005 1 770 . 154 VAL CA C 65.968 0.05 1 771 . 154 VAL C C 180.714 0.05 1 772 . 154 VAL CB C 31.938 0.05 1 773 . 154 VAL CG1 C 21.048 0.05 2 774 . 154 VAL CG2 C 22.361 0.05 2 775 . 154 VAL HA H 3.346 0.005 1 776 . 154 VAL HB H 1.82 0.005 1 777 . 154 VAL HG1 H 0.61 0.005 2 778 . 154 VAL HG2 H 0.821 0.005 2 779 . 155 GLN N N 120.671 0.05 1 780 . 155 GLN H H 8.108 0.005 1 781 . 155 GLN CA C 58.542 0.05 1 782 . 155 GLN C C 178.178 0.05 1 783 . 155 GLN CB C 28.247 0.05 1 784 . 155 GLN CG C 34.03 0.05 1 785 . 155 GLN HA H 3.933 0.005 1 786 . 155 GLN HB2 H 2.132 0.005 1 787 . 155 GLN HG2 H 2.452 0.005 1 788 . 156 ASP N N 118.827 0.05 1 789 . 156 ASP H H 8.029 0.005 1 790 . 156 ASP CA C 55.373 0.05 1 791 . 156 ASP C C 177.273 0.05 1 792 . 156 ASP CB C 41.782 0.05 1 793 . 156 ASP HA H 4.55 0.005 1 794 . 156 ASP HB2 H 2.489 0.005 2 795 . 156 ASP HB3 H 2.552 0.005 2 796 . 157 GLY N N 106.87 0.05 1 797 . 157 GLY H H 7.884 0.005 1 798 . 157 GLY CA C 45.573 0.05 1 799 . 157 GLY C C 175.607 0.05 1 800 . 157 GLY HA2 H 3.523 0.005 1 801 . 157 GLY HA3 H 3.911 0.005 1 802 . 158 ILE N N 122.008 0.05 1 803 . 158 ILE H H 7.205 0.005 1 804 . 158 ILE CA C 62.378 0.05 1 805 . 158 ILE C C 172.053 0.05 1 806 . 158 ILE CB C 37.219 0.05 1 807 . 158 ILE HA H 3.666 0.005 1 808 . 158 ILE HB H 1.832 0.005 1 809 . 159 THR N N 115.832 0.05 1 810 . 159 THR H H 7.327 0.005 1 811 . 159 THR CA C 57.016 0.05 1 812 . 159 THR C C 174.859 0.05 1 813 . 159 THR CB C 71.337 0.05 1 814 . 159 THR HA H 4.842 0.005 1 815 . 159 THR HB H 4.099 0.005 1 816 . 160 LEU N N 121.396 0.05 1 817 . 160 LEU H H 8.074 0.005 1 818 . 160 LEU CA C 54.726 0.05 1 819 . 160 LEU C C 176.539 0.05 1 820 . 160 LEU CB C 43.495 0.05 1 821 . 160 LEU HA H 4.101 0.005 1 822 . 161 ILE N N 122.835 0.05 1 823 . 161 ILE H H 9.948 0.005 1 824 . 161 ILE CA C 61.916 0.05 1 825 . 161 ILE C C 179.013 0.05 1 826 . 161 ILE CB C 39.103 0.05 1 827 . 161 ILE CG2 C 19.314 0.05 1 828 . 161 ILE HA H 4.173 0.005 1 829 . 161 ILE HB H 1.629 0.005 1 830 . 161 ILE HG2 H 0.935 0.005 1 831 . 161 ILE HD1 H 0.787 0.005 1 832 . 162 THR N N 122.064 0.05 1 833 . 162 THR H H 8.791 0.005 1 834 . 162 THR CA C 60.992 0.05 1 835 . 162 THR C C 175.904 0.05 1 836 . 162 THR CB C 72.738 0.05 1 837 . 162 THR HA H 4.527 0.005 1 838 . 162 THR HB H 4.568 0.005 1 839 . 162 THR HG2 H 1.114 0.005 1 840 . 163 LYS N N 119.984 0.05 1 841 . 163 LYS H H 8.692 0.005 1 842 . 163 LYS CA C 57.828 0.05 1 843 . 163 LYS C C 177.842 0.05 1 844 . 163 LYS CB C 32.597 0.05 1 845 . 163 LYS HA H 4.624 0.005 1 846 . 164 GLU CA C 58.497 0.05 1 847 . 164 GLU C C 178.076 0.05 1 848 . 164 GLU CB C 29.427 0.05 1 849 . 164 GLU CG C 37.244 0.05 1 850 . 164 GLU HA H 4.053 0.005 1 851 . 164 GLU HB2 H 2.256 0.005 2 852 . 164 GLU HB3 H 2.353 0.005 2 853 . 165 GLU N N 117.993 0.05 1 854 . 165 GLU H H 7.447 0.005 1 855 . 165 GLU CA C 57.317 0.05 1 856 . 165 GLU C C 176.786 0.05 1 857 . 165 GLU CB C 32.597 0.05 1 858 . 165 GLU CG C 37.664 0.05 1 859 . 165 GLU HA H 4.133 0.005 1 860 . 166 ALA N N 121.866 0.05 1 861 . 166 ALA H H 8.018 0.005 1 862 . 166 ALA CA C 52.091 0.05 1 863 . 166 ALA CB C 21.45 0.05 1 864 . 166 ALA HA H 4.533 0.005 1 865 . 166 ALA HB H 1.304 0.005 1 866 . 167 SER CA C 61.028 0.05 1 867 . 167 SER C C 175.623 0.05 1 868 . 167 SER CB C 63.408 0.05 1 869 . 167 SER HA H 4.336 0.005 1 870 . 167 SER HB2 H 3.959 0.005 1 871 . 168 GLY N N 109.522 0.05 1 872 . 168 GLY H H 8.46 0.005 1 873 . 168 GLY CA C 45.367 0.05 1 874 . 168 GLY C C 175.414 0.05 1 875 . 168 GLY HA2 H 3.826 0.005 1 876 . 168 GLY HA3 H 4.121 0.005 1 877 . 169 SER N N 113.335 0.05 1 878 . 169 SER H H 7.728 0.005 1 879 . 169 SER CA C 56.119 0.05 1 880 . 169 SER CB C 63.819 0.05 1 881 . 169 SER HA H 4.512 0.005 1 882 . 169 SER HB2 H 3.725 0.005 1 883 . 170 SER CA C 57.908 0.05 1 884 . 170 SER C C 174.967 0.05 1 885 . 170 SER CB C 64.141 0.05 1 886 . 170 SER HA H 4.618 0.005 1 887 . 170 SER HB2 H 3.932 0.005 2 888 . 170 SER HB3 H 4.025 0.005 2 889 . 171 VAL N N 125.625 0.05 1 890 . 171 VAL H H 8.378 0.005 1 891 . 171 VAL CA C 62.973 0.05 1 892 . 171 VAL C C 176.531 0.05 1 893 . 171 VAL CB C 32.869 0.05 1 894 . 171 VAL CG1 C 21.799 0.05 1 895 . 171 VAL HA H 4.043 0.005 1 896 . 171 VAL HB H 1.992 0.005 1 897 . 171 VAL HG2 H 0.941 0.005 1 898 . 172 THR N N 118.146 0.05 1 899 . 172 THR H H 8.302 0.005 1 900 . 172 THR CA C 60.556 0.05 1 901 . 172 THR C C 175.945 0.05 1 902 . 172 THR CB C 71.476 0.05 1 903 . 172 THR HA H 4.207 0.005 1 904 . 173 ALA CA C 55.634 0.05 1 905 . 173 ALA C C 180.993 0.05 1 906 . 173 ALA CB C 18.072 0.05 1 907 . 173 ALA HA H 4.155 0.005 1 908 . 173 ALA HB H 1.505 0.005 1 909 . 174 GLU N N 117.747 0.05 1 910 . 174 GLU H H 8.604 0.005 1 911 . 174 GLU CA C 59.797 0.05 1 912 . 174 GLU C C 179.353 0.05 1 913 . 174 GLU CB C 29.273 0.05 1 914 . 174 GLU CG C 36.545 0.05 1 915 . 174 GLU HA H 4.032 0.005 1 916 . 175 GLU N N 121.452 0.05 1 917 . 175 GLU H H 7.87 0.005 1 918 . 175 GLU CA C 59.103 0.05 1 919 . 175 GLU C C 179.888 0.05 1 920 . 175 GLU CB C 29.924 0.05 1 921 . 175 GLU CG C 36.803 0.05 1 922 . 175 GLU HA H 3.96 0.005 1 923 . 176 ALA N N 122.666 0.05 1 924 . 176 ALA H H 8.305 0.005 1 925 . 176 ALA CA C 54.79 0.05 1 926 . 176 ALA C C 180.155 0.05 1 927 . 176 ALA CB C 18.592 0.05 1 928 . 176 ALA HA H 3.965 0.005 1 929 . 176 ALA HB H 1.439 0.005 1 930 . 177 LYS N N 119.835 0.05 1 931 . 177 LYS H H 7.961 0.005 1 932 . 177 LYS CA C 59.091 0.05 1 933 . 177 LYS C C 179.637 0.05 1 934 . 177 LYS CB C 32.451 0.05 1 935 . 177 LYS CG C 25.01 0.05 1 936 . 177 LYS CD C 29.265 0.05 1 937 . 177 LYS CE C 41.184 0.05 1 938 . 177 LYS HA H 4.192 0.005 1 939 . 178 LYS N N 120.439 0.05 1 940 . 178 LYS H H 8.103 0.005 1 941 . 178 LYS CA C 58.273 0.05 1 942 . 178 LYS C C 178.556 0.05 1 943 . 178 LYS CB C 32.309 0.05 1 944 . 178 LYS CG C 25.194 0.05 1 945 . 178 LYS CD C 29.247 0.05 1 946 . 178 LYS HA H 4.056 0.005 1 947 . 178 LYS HG2 H 1.496 0.005 2 948 . 178 LYS HG3 H 1.582 0.005 2 949 . 178 LYS HB2 H 1.9 0.005 1 950 . 178 LYS HD3 H 1.685 0.005 1 951 . 179 PHE N N 119.28 0.05 1 952 . 179 PHE H H 7.85 0.005 1 953 . 179 PHE CA C 60.947 0.05 1 954 . 179 PHE C C 176.132 0.05 1 955 . 179 PHE CB C 38.675 0.05 1 956 . 179 PHE HA H 4.261 0.005 1 957 . 180 LEU N N 124.403 0.05 1 958 . 180 LEU H H 8.302 0.005 1 959 . 180 LEU CA C 57.542 0.05 1 960 . 180 LEU C C 175.748 0.05 1 961 . 180 LEU CB C 39.83 0.05 1 962 . 180 LEU HA H 4.646 0.005 1 963 . 182 PRO CA C 63.166 0.05 1 964 . 182 PRO C C 177.547 0.05 1 965 . 182 PRO CB C 32.169 0.05 1 966 . 182 PRO CG C 27.289 0.05 1 967 . 182 PRO CD C 50.237 0.05 1 968 . 182 PRO HA H 4.466 0.005 1 969 . 182 PRO HB2 H 1.933 0.005 2 970 . 182 PRO HB3 H 2.318 0.005 2 971 . 182 PRO HD2 H 3.617 0.005 2 972 . 182 PRO HD3 H 3.746 0.005 2 973 . 182 PRO HG2 H 2.011 0.005 1 974 . 183 LYS N N 121.743 0.05 1 975 . 183 LYS H H 8.453 0.005 1 976 . 183 LYS CA C 56.105 0.05 1 977 . 183 LYS C C 175.916 0.05 1 978 . 183 LYS CB C 32.963 0.05 1 979 . 183 LYS CG C 24.6 0.05 1 980 . 183 LYS CD C 28.886 0.05 1 981 . 183 LYS CE C 42.074 0.05 1 982 . 183 LYS HA H 4.285 0.005 1 983 . 183 LYS HD2 H 1.625 0.005 2 984 . 183 LYS HD3 H 1.71 0.005 2 985 . 183 LYS HB2 H 1.851 0.005 1 986 . 183 LYS HG2 H 1.429 0.005 1 987 . 183 LYS HE2 H 2.93 0.005 1 988 . 184 ASP N N 126.758 0.05 1 989 . 184 ASP H H 7.86 0.005 1 990 . 184 ASP CA C 55.807 0.05 1 991 . 184 ASP CB C 32.869 0.05 1 992 . 184 ASP HA H 4.344 0.005 1 993 . 184 ASP HB2 H 2.583 0.005 1 stop_ save_