data_5590 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments of rice telomere binding domain from Oryza sativa ; _BMRB_accession_number 5590 _BMRB_flat_file_name bmr5590.str _Entry_type original _Submission_date 2002-11-15 _Accession_date 2002-11-15 _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 Ko Sung-gun . . 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" 425 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-11-24 original author . stop_ _Original_release_date 2003-11-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N Resonance Assignments of Rice Telomere Binding Domain from Oryza sativa ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22760842 _PubMed_ID 12878845 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ko Sung-gun . . 2 Shin Joon . . 3 Yu Eun Yong . 4 Chung In Kwon . 5 Tanaka Toshiyuki . . 6 Lee Weontae . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 89 _Page_last 90 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_Myb_RTBP1 _Saveframe_category molecular_system _Mol_system_name 'DNA-binding domain in RTBP1' _Abbreviation_common Myb_RTBP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DNA-binding domain in RTBP1' $Myb_RTBP1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'DNA binding protein as homodimer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Myb_RTBP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Telomere binding protein-1' _Abbreviation_common RTBP1 _Molecular_mass 13729.68 _Mol_thiol_state 'not present' _Details 'The pI of this protein is 10.32' ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; FPFADPNSLALANVPLSRSK RPDFGQRRIRRPFTVAEVEL LVEAVEHLGTGRWRDVKFRA FENVHHRTYVDLKDKWKTLV HTASIAPQQRRGAPVPQELL DRVLAAQAYWSVDSSGRIVT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 PHE 2 506 PRO 3 507 PHE 4 508 ALA 5 509 ASP 6 510 PRO 7 511 ASN 8 512 SER 9 513 LEU 10 514 ALA 11 515 LEU 12 516 ALA 13 517 ASN 14 518 VAL 15 519 PRO 16 520 LEU 17 521 SER 18 522 ARG 19 523 SER 20 524 LYS 21 525 ARG 22 526 PRO 23 527 ASP 24 528 PHE 25 529 GLY 26 530 GLN 27 531 ARG 28 532 ARG 29 533 ILE 30 534 ARG 31 535 ARG 32 536 PRO 33 537 PHE 34 538 THR 35 539 VAL 36 540 ALA 37 541 GLU 38 542 VAL 39 543 GLU 40 544 LEU 41 545 LEU 42 546 VAL 43 547 GLU 44 548 ALA 45 549 VAL 46 550 GLU 47 551 HIS 48 552 LEU 49 553 GLY 50 554 THR 51 555 GLY 52 556 ARG 53 557 TRP 54 558 ARG 55 559 ASP 56 560 VAL 57 561 LYS 58 562 PHE 59 563 ARG 60 564 ALA 61 565 PHE 62 566 GLU 63 567 ASN 64 568 VAL 65 569 HIS 66 570 HIS 67 571 ARG 68 572 THR 69 573 TYR 70 574 VAL 71 575 ASP 72 576 LEU 73 577 LYS 74 578 ASP 75 579 LYS 76 580 TRP 77 581 LYS 78 582 THR 79 583 LEU 80 584 VAL 81 585 HIS 82 586 THR 83 587 ALA 84 588 SER 85 589 ILE 86 590 ALA 87 591 PRO 88 592 GLN 89 593 GLN 90 594 ARG 91 595 ARG 92 596 GLY 93 597 ALA 94 598 PRO 95 599 VAL 96 600 PRO 97 601 GLN 98 602 GLU 99 603 LEU 100 604 LEU 101 605 ASP 102 606 ARG 103 607 VAL 104 608 LEU 105 609 ALA 106 610 ALA 107 611 GLN 108 612 ALA 109 613 TYR 110 614 TRP 111 615 SER 112 +1 VAL 113 +2 ASP 114 +3 SER 115 +4 SER 116 +5 GLY 117 +6 ARG 118 +7 ILE 119 +8 VAL 120 +9 THR 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 11038 "The DNA binding domain of RTBP1" 99.17 122 100.00 100.00 9.15e-80 PDB 2ROH "The Dna Binding Domain Of Rtbp1" 99.17 122 100.00 100.00 9.15e-80 GB AAF97508 "telomere binding protein-1 [Oryza sativa]" 91.67 633 100.00 100.00 2.30e-70 GB EAY88030 "hypothetical protein OsI_09453 [Oryza sativa Indica Group]" 91.67 633 99.09 99.09 6.32e-69 GB EAZ25089 "hypothetical protein OsJ_08881 [Oryza sativa Japonica Group]" 89.17 638 99.07 100.00 9.56e-67 SP Q9LL45 "RecName: Full=Telomere-binding protein 1; AltName: Full=Protein RTBP1 [Oryza sativa Japonica Group]" 91.67 633 100.00 100.00 2.01e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Myb_RTBP1 Rice 4530 Eukaryota Viridiplantae Oryza sativa stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Myb_RTBP1 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Myb_RTBP1 1 mM '[U-100% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Myb_RTBP1 1 mM '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_sparky _Saveframe_category software _Name SPARKY _Version 2.0 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-NOESY_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-NOESY HSQC' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_15N-edited_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_15N-edited_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _Sample_label . save_ save_13C-edited_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-NOESY HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _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 '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 303 1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'DNA-binding domain in RTBP1' _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 PRO HA H 4.44 0.0068 1 2 . 2 PRO HB2 H 2.25 0.0068 2 3 . 2 PRO HG2 H 2.02 0.0068 2 4 . 2 PRO HD2 H 3.86 0.0068 2 5 . 2 PRO C C 176.52 0.156 1 6 . 2 PRO CA C 61.25 0.156 1 7 . 2 PRO CB C 29.67 0.156 1 8 . 2 PRO CG C 25.5 0.156 1 9 . 2 PRO CD C 49.39 0.156 1 10 . 3 PHE H H 8.017 0.0068 1 11 . 3 PHE HA H 4.6 0.0068 1 12 . 3 PHE HB2 H 3.13 0.0068 2 13 . 3 PHE C C 176.2 0.156 1 14 . 3 PHE CA C 55.3 0.156 1 15 . 3 PHE CB C 36.81 0.156 1 16 . 3 PHE N N 119.19 0.158 1 17 . 4 ALA H H 7.96 0.0068 1 18 . 4 ALA HA H 4.27 0.0068 1 19 . 4 ALA HB H 1.28 0.0068 1 20 . 4 ALA C C 175.56 0.156 1 21 . 4 ALA CA C 50.1 0.156 1 22 . 4 ALA CB C 17.26 0.156 1 23 . 4 ALA N N 125.33 0.158 1 24 . 5 ASP H H 7.96 0.156 1 25 . 5 ASP HA H 4.76 0.156 1 26 . 5 ASP HB2 H 2.53 0.156 2 27 . 5 ASP CA C 49.84 0.156 1 28 . 5 ASP CB C 39.33 0.156 1 29 . 5 ASP N N 121.17 0.158 1 30 . 6 PRO HA H 4.37 0.0068 1 31 . 6 PRO HB2 H 2.15 0.0068 2 32 . 6 PRO HG2 H 1.95 0.0068 2 33 . 6 PRO HD2 H 3.47 0.0068 2 34 . 6 PRO C C 177.53 0.156 1 35 . 6 PRO CA C 62.02 0.156 1 36 . 6 PRO CB C 29.95 0.156 1 37 . 6 PRO CG C 25.59 0.156 1 38 . 6 PRO CD C 48.59 0.156 1 39 . 7 ASN H H 8.52 0.0068 1 40 . 7 ASN HA H 5.128 0.0068 1 41 . 7 ASN HB2 H 2.74 0.0068 2 42 . 7 ASN HD22 H 6.9 0.0068 1 43 . 7 ASN HD21 H 7.567 0.0068 1 44 . 7 ASN C C 175.81 0.156 1 45 . 7 ASN CA C 51.94 0.156 1 46 . 7 ASN CB C 36.46 0.156 1 47 . 7 ASN N N 116.98 0.158 1 48 . 7 ASN ND2 N 113.5 0.158 2 49 . 8 SER H H 7.95 0.0068 1 50 . 8 SER HA H 4.54 0.0068 1 51 . 8 SER HB2 H 4.07 0.0068 2 52 . 8 SER C C 174.75 0.156 1 53 . 8 SER CA C 57.4 0.156 1 54 . 8 SER CB C 61.4 0.156 1 55 . 8 SER N N 115.57 0.158 1 56 . 9 LEU H H 8 0.0068 1 57 . 9 LEU HA H 4.31 0.0068 1 58 . 9 LEU HB2 H 1.52 0.0068 2 59 . 9 LEU HD1 H 0.9 0.0068 2 60 . 9 LEU C C 177.48 0.156 1 61 . 9 LEU CA C 53.35 0.156 1 62 . 9 LEU CB C 40.43 0.156 1 63 . 9 LEU CD1 C 22.59 0.156 2 64 . 9 LEU N N 123.31 0.158 1 65 . 10 ALA H H 8.02 0.0068 1 66 . 10 ALA HA H 4.05 0.0068 1 67 . 10 ALA HB H 1.46 0.0068 1 68 . 10 ALA C C 178.01 0.156 1 69 . 10 ALA CA C 50.04 0.156 1 70 . 10 ALA CB C 16.8 0.156 1 71 . 10 ALA N N 123.45 0.158 1 72 . 11 LEU H H 7.91 0.0068 1 73 . 11 LEU HA H 4.31 0.0068 1 74 . 11 LEU HB2 H 1.59 0.0068 2 75 . 11 LEU HD1 H 0.84 0.0068 2 76 . 11 LEU C C 177.31 0.156 1 77 . 11 LEU CA C 52.5 0.156 1 78 . 11 LEU CB C 39.9 0.156 1 79 . 11 LEU CD1 C 22.59 0.156 2 80 . 11 LEU N N 120.1 0.158 1 81 . 12 ALA H H 8.01 0.0068 1 82 . 12 ALA HA H 4.28 0.0068 1 83 . 12 ALA HB H 1.27 0.0068 1 84 . 12 ALA C C 177.5 0.156 1 85 . 12 ALA CA C 49.28 0.156 1 86 . 12 ALA CB C 17.85 0.156 1 87 . 12 ALA N N 123.17 0.158 1 88 . 13 ASN H H 8.24 0.0068 1 89 . 13 ASN HA H 5.082 0.0068 1 90 . 13 ASN HB2 H 2.58 0.0068 2 91 . 13 ASN HD22 H 6.964 0.0068 1 92 . 13 ASN HD21 H 7.641 0.0068 1 93 . 13 ASN C C 174.71 0.156 1 94 . 13 ASN CA C 51.17 0.156 1 95 . 13 ASN CB C 36.74 0.156 1 96 . 13 ASN N N 117.11 0.158 1 97 . 13 ASN ND2 N 112.3 0.158 1 98 . 14 VAL H H 7.87 0.0068 1 99 . 14 VAL HA H 4.23 0.0068 1 100 . 14 VAL HB H 2.15 0.0068 1 101 . 14 VAL HG1 H 0.9 0.0068 2 102 . 14 VAL CA C 57.42 0.156 1 103 . 14 VAL CB C 30.26 0.156 1 104 . 14 VAL CG1 C 19.59 0.156 2 105 . 14 VAL N N 121.33 0.158 1 106 . 15 PRO HA H 4.38 0.0068 1 107 . 15 PRO HB2 H 2.15 0.0068 2 108 . 15 PRO HG2 H 1.93 0.0068 2 109 . 15 PRO HD2 H 3.32 0.0068 2 110 . 15 PRO C C 176.79 0.156 1 111 . 15 PRO CA C 60.89 0.156 1 112 . 15 PRO CB C 29.99 0.156 1 113 . 15 PRO CG C 25.59 0.156 1 114 . 15 PRO CD C 48.01 0.156 1 115 . 16 LEU H H 8.29 0.0068 1 116 . 16 LEU HA H 3.93 0.0068 1 117 . 16 LEU HB2 H 1.69 0.0068 2 118 . 16 LEU HD1 H 0.92 0.0068 2 119 . 16 LEU C C 177.43 0.156 1 120 . 16 LEU CA C 52.5 0.156 1 121 . 16 LEU CB C 40.37 0.156 1 122 . 16 LEU CD1 C 22.76 0.156 2 123 . 16 LEU N N 122.46 0.158 1 124 . 17 SER H H 8.23 0.0068 1 125 . 17 SER HA H 4.44 0.0068 1 126 . 17 SER HB2 H 3.82 0.0068 2 127 . 17 SER C C 173.51 0.156 1 128 . 17 SER CA C 56.07 0.156 1 129 . 17 SER CB C 61.52 0.156 1 130 . 17 SER N N 117.02 0.158 1 131 . 18 ARG H H 7.97 0.0068 1 132 . 18 ARG N N 128.1 0.158 1 133 . 20 LYS C C 176.36 0.156 1 134 . 21 ARG H H 8.4 0.0068 1 135 . 21 ARG HA H 4.56 0.0068 1 136 . 21 ARG HB2 H 1.81 0.0068 2 137 . 21 ARG HD2 H 3.17 0.0068 2 138 . 21 ARG CA C 52.67 0.156 1 139 . 21 ARG CB C 27.94 0.156 1 140 . 21 ARG CD C 41.42 0.156 1 141 . 21 ARG N N 123.95 0.158 1 142 . 22 PRO HA H 3.39 0.0068 1 143 . 22 PRO HB2 H 2.13 0.0068 2 144 . 22 PRO HG2 H 1.97 0.0068 2 145 . 22 PRO HD2 H 3.82 0.0068 2 146 . 22 PRO C C 176.24 0.156 1 147 . 22 PRO CA C 61.03 0.156 1 148 . 22 PRO CB C 29.99 0.156 1 149 . 22 PRO CG C 25.89 0.156 1 150 . 22 PRO CD C 49.39 0.156 1 151 . 23 ASP H H 8.28 0.0068 1 152 . 23 ASP HA H 5.07 0.0068 1 153 . 23 ASP HB2 H 2.47 0.0068 2 154 . 23 ASP C C 176.17 0.156 1 155 . 23 ASP CA C 51.14 0.156 1 156 . 23 ASP CB C 39.11 0.156 1 157 . 23 ASP N N 119.82 0.158 1 158 . 24 PHE H H 8.15 0.0068 1 159 . 24 PHE HA H 4.53 0.0068 1 160 . 24 PHE HB2 H 3.01 0.0068 2 161 . 24 PHE C C 176.5 0.156 1 162 . 24 PHE CA C 55.86 0.156 1 163 . 24 PHE CB C 37.59 0.156 1 164 . 24 PHE N N 120.89 0.158 1 165 . 25 GLY H H 8.43 0.0068 1 166 . 25 GLY HA2 H 3.88 0.0068 2 167 . 25 GLY C C 174.31 0.156 1 168 . 25 GLY CA C 43.14 0.156 1 169 . 25 GLY N N 110.04 0.158 1 170 . 26 GLN H H 8.14 0.0068 1 171 . 26 GLN HA H 4.343 0.0068 1 172 . 26 GLN HB2 H 2.111 0.0068 2 173 . 26 GLN HG2 H 2.365 0.0068 2 174 . 26 GLN HE22 H 6.964 0.0068 1 175 . 26 GLN HE21 H 7.794 0.0068 1 176 . 26 GLN C C 176.17 0.156 1 177 . 26 GLN CA C 53.91 0.156 1 178 . 26 GLN CB C 27.11 0.156 1 179 . 26 GLN CG C 32.59 0.156 1 180 . 26 GLN N N 119.76 0.158 1 181 . 26 GLN NE2 N 114 0.158 1 182 . 27 ARG H H 8.31 0.0068 1 183 . 27 ARG HA H 4.16 0.0068 1 184 . 27 ARG HB2 H 1.72 0.0068 2 185 . 27 ARG HG2 H 1.6 0.0068 2 186 . 27 ARG HD2 H 3.13 0.0068 2 187 . 27 ARG C C 176.13 0.156 1 188 . 27 ARG CA C 54.8 0.156 1 189 . 27 ARG CB C 28.56 0.156 1 190 . 27 ARG CG C 26.11 0.156 1 191 . 27 ARG CD C 41.41 0.156 1 192 . 27 ARG N N 121.94 0.158 1 193 . 28 ARG H H 8.35 0.0068 1 194 . 28 ARG HA H 4.31 0.0068 1 195 . 28 ARG HB2 H 1.73 0.0068 2 196 . 28 ARG HG2 H 1.59 0.0068 2 197 . 28 ARG HD2 H 3.1 0.0068 2 198 . 28 ARG C C 175.93 0.156 1 199 . 28 ARG CA C 53.91 0.156 1 200 . 28 ARG CB C 28.71 0.156 1 201 . 28 ARG CG C 25.78 0.156 1 202 . 28 ARG CD C 41.43 0.156 1 203 . 28 ARG N N 122.59 0.158 1 204 . 29 ILE H H 8.21 0.0068 1 205 . 29 ILE HA H 4.37 0.0068 1 206 . 29 ILE HB H 1.78 0.0068 1 207 . 29 ILE HG12 H 1.38 0.0068 2 208 . 29 ILE HD1 H 0.8 0.0068 1 209 . 29 ILE C C 176.01 0.156 1 210 . 29 ILE CA C 58.72 0.156 1 211 . 29 ILE CB C 36.21 0.156 1 212 . 29 ILE CD1 C 16.22 0.156 2 213 . 29 ILE N N 122.7 0.158 1 214 . 30 ARG H H 8.48 0.0068 1 215 . 30 ARG HA H 4.44 0.0068 1 216 . 30 ARG HB2 H 1.792 0.0068 2 217 . 30 ARG HG2 H 1.68 0.0068 2 218 . 30 ARG HD2 H 3.23 0.0068 2 219 . 30 ARG C C 184.26 0.156 1 220 . 30 ARG CA C 53.58 0.156 1 221 . 30 ARG CB C 28.79 0.156 1 222 . 30 ARG CG C 25 0.156 1 223 . 30 ARG CD C 41.12 0.156 1 224 . 30 ARG N N 126.63 0.158 1 225 . 31 ARG H H 8.55 0.0068 1 226 . 31 ARG HA H 4.269 0.0068 1 227 . 31 ARG HB2 H 2.17 0.0068 2 228 . 31 ARG HG2 H 1.868 0.0068 2 229 . 31 ARG HD2 H 3.4 0.0068 2 230 . 31 ARG C C 184.286 0.156 1 231 . 31 ARG CA C 53.36 0.156 1 232 . 31 ARG CB C 28.76 0.156 1 233 . 31 ARG CG C 25 0.156 1 234 . 31 ARG CD C 41.12 0.156 1 235 . 31 ARG N N 115.67 0.158 1 236 . 32 PRO HA H 4.4 0.0068 1 237 . 32 PRO HB2 H 2.17 0.0068 2 238 . 32 PRO HG2 H 1.97 0.0068 2 239 . 32 PRO HD2 H 3.76 0.0068 2 240 . 32 PRO C C 177.17 0.156 1 241 . 32 PRO CA C 61.18 0.156 1 242 . 32 PRO CB C 30.58 0.156 1 243 . 32 PRO CG C 25 0.156 1 244 . 32 PRO CD C 48.48 0.156 1 245 . 33 PHE H H 9.35 0.0068 1 246 . 33 PHE HA H 4.58 0.0068 1 247 . 33 PHE HB2 H 3.15 0.0068 2 248 . 33 PHE C C 178.21 0.156 1 249 . 33 PHE CA C 56.09 0.156 1 250 . 33 PHE CB C 37.79 0.156 1 251 . 33 PHE N N 124.34 0.158 1 252 . 34 THR H H 9.11 0.0068 1 253 . 34 THR HA H 4.36 0.0068 1 254 . 34 THR HB H 4.27 0.0068 1 255 . 34 THR HG2 H 1.4 0.0068 1 256 . 34 THR C C 176 0.156 1 257 . 34 THR CA C 58.43 0.156 1 258 . 34 THR CB C 68.69 0.156 1 259 . 34 THR CG2 C 22.34 0.156 2 260 . 34 THR N N 116.04 0.158 1 261 . 35 VAL H H 8.89 0.0068 1 262 . 35 VAL HA H 4.36 0.0068 1 263 . 35 VAL HB H 2.17 0.0068 1 264 . 35 VAL HG1 H 1.18 0.0068 2 265 . 35 VAL C C 177.84 0.156 1 266 . 35 VAL CA C 64.38 0.156 1 267 . 35 VAL CB C 29.17 0.156 1 268 . 35 VAL CG1 C 22.69 0.156 2 269 . 35 VAL N N 121.85 0.158 1 270 . 36 ALA H H 8.21 0.0068 1 271 . 36 ALA HA H 4.27 0.0068 1 272 . 36 ALA HB H 1.15 0.0068 1 273 . 36 ALA C C 181.23 0.156 1 274 . 36 ALA CA C 53.7 0.156 1 275 . 36 ALA CB C 16.21 0.156 1 276 . 36 ALA N N 121.72 0.158 1 277 . 37 GLU H H 7.928 0.0068 1 278 . 37 GLU HA H 4.39 0.0068 1 279 . 37 GLU HB2 H 1.92 0.0068 2 280 . 37 GLU HG2 H 1.93 0.0068 2 281 . 37 GLU C C 179.24 0.156 1 282 . 37 GLU CA C 57.6 0.156 1 283 . 37 GLU CB C 30.1 0.156 1 284 . 37 GLU CG C 33 0.156 1 285 . 37 GLU N N 117.14 0.158 1 286 . 38 VAL H H 8.54 0.0068 1 287 . 38 VAL HA H 3.67 0.0068 1 288 . 38 VAL HB H 2.11 0.0068 1 289 . 38 VAL HG1 H 0.98 0.0068 2 290 . 38 VAL C C 177.65 0.156 1 291 . 38 VAL CA C 65.94 0.156 1 292 . 38 VAL CB C 30.07 0.156 1 293 . 38 VAL CG1 C 20.17 0.156 2 294 . 38 VAL N N 120.85 0.158 1 295 . 39 GLU H H 8.63 0.0068 1 296 . 39 GLU HA H 4.27 0.0068 1 297 . 39 GLU HB2 H 2.31 0.0068 2 298 . 39 GLU HG2 H 2.01 0.0068 2 299 . 39 GLU C C 178.51 0.156 1 300 . 39 GLU CA C 58.25 0.156 1 301 . 39 GLU CB C 26.7 0.156 1 302 . 39 GLU CG C 30.83 0.156 1 303 . 39 GLU N N 119.96 0.158 1 304 . 40 LEU H H 7.81 0.0068 1 305 . 40 LEU HA H 4.13 0.0068 1 306 . 40 LEU HB2 H 1.56 0.0068 2 307 . 40 LEU HG H 1.88 0.0068 1 308 . 40 LEU HD1 H 0.87 0.0068 1 309 . 40 LEU HD2 H 1.195 0.0068 1 310 . 40 LEU C C 180.07 0.156 1 311 . 40 LEU CA C 56.11 0.156 1 312 . 40 LEU CB C 40.73 0.156 1 313 . 40 LEU CG C 24.71 0.156 1 314 . 40 LEU CD1 C 21.59 0.156 2 315 . 40 LEU CD2 C 20.92 0.156 2 316 . 40 LEU N N 118.4 0.158 1 317 . 41 LEU H H 8.39 0.0068 1 318 . 41 LEU HA H 4.15 0.0068 1 319 . 41 LEU HB2 H 1.54 0.0068 2 320 . 41 LEU HD1 H 0.82 0.0068 2 321 . 41 LEU C C 177.15 0.156 1 322 . 41 LEU CA C 56.11 0.156 1 323 . 41 LEU CB C 40.73 0.156 1 324 . 41 LEU CD1 C 22.76 0.156 2 325 . 41 LEU N N 120.73 0.158 1 326 . 42 VAL H H 8.99 0.0068 1 327 . 42 VAL HA H 3.77 0.0068 1 328 . 42 VAL HB H 2.18 0.0068 1 329 . 42 VAL HG1 H 0.97 0.0068 2 330 . 42 VAL C C 177.15 0.156 1 331 . 42 VAL CA C 65.38 0.156 1 332 . 42 VAL CB C 29.67 0.156 1 333 . 42 VAL CG1 C 18 0.156 2 334 . 42 VAL N N 118.41 0.158 1 335 . 43 GLU H H 8.46 0.0068 1 336 . 43 GLU HA H 4.27 0.0068 1 337 . 43 GLU HB2 H 2.02 0.0068 2 338 . 43 GLU HG2 H 2.29 0.0068 2 339 . 43 GLU C C 179.31 0.156 1 340 . 43 GLU CA C 57.61 0.156 1 341 . 43 GLU CB C 27.15 0.156 1 342 . 43 GLU CG C 34 0.156 1 343 . 43 GLU N N 119.64 0.158 1 344 . 44 ALA H H 7.93 0.0068 1 345 . 44 ALA HA H 4.02 0.0068 1 346 . 44 ALA HB H 1.48 0.0068 1 347 . 44 ALA C C 179.48 0.156 1 348 . 44 ALA CA C 53.2 0.156 1 349 . 44 ALA CB C 16.82 0.156 1 350 . 44 ALA N N 120.11 0.158 1 351 . 45 VAL H H 8.37 0.0068 1 352 . 45 VAL HA H 4.33 0.0068 1 353 . 45 VAL HB H 2.12 0.0068 1 354 . 45 VAL HG1 H 1.18 0.0068 2 355 . 45 VAL C C 179.52 0.156 1 356 . 45 VAL CA C 63.35 0.156 1 357 . 45 VAL CB C 29.04 0.156 1 358 . 45 VAL CG1 C 21.51 0.156 2 359 . 45 VAL N N 120.83 0.158 1 360 . 46 GLU H H 9.1 0.0068 1 361 . 46 GLU HA H 3.97 0.0068 1 362 . 46 GLU HB2 H 1.79 0.0068 2 363 . 46 GLU HG2 H 2.32 0.0068 2 364 . 46 GLU C C 179.07 0.156 1 365 . 46 GLU CA C 58.52 0.156 1 366 . 46 GLU CB C 28.53 0.156 1 367 . 46 GLU CG C 32 0.156 1 368 . 46 GLU N N 120.41 0.158 1 369 . 47 HIS H H 7.06 0.0068 1 370 . 47 HIS HA H 4.5 0.0068 1 371 . 47 HIS HB2 H 3.16 0.0068 2 372 . 47 HIS C C 176.36 0.156 1 373 . 47 HIS CA C 57.33 0.156 1 374 . 47 HIS CB C 31.6 0.156 1 375 . 47 HIS N N 113.49 0.158 1 376 . 48 LEU H H 8.5 0.0068 1 377 . 48 LEU HA H 4.13 0.0068 1 378 . 48 LEU HB2 H 1.54 0.0068 2 379 . 48 LEU HD1 H 0.88 0.0068 2 380 . 48 LEU C C 176.88 0.156 1 381 . 48 LEU CA C 53.13 0.156 1 382 . 48 LEU CB C 42.41 0.156 1 383 . 48 LEU CD1 C 22 0.156 2 384 . 48 LEU N N 116.72 0.158 1 385 . 49 GLY H H 8.31 0.0068 1 386 . 49 GLY HA2 H 3.17 0.0068 2 387 . 49 GLY C C 173.36 0.156 1 388 . 49 GLY CA C 39.12 0.156 1 389 . 49 GLY N N 111.12 0.158 1 390 . 50 THR H H 6.35 0.0068 1 391 . 50 THR HA H 4.39 0.0068 1 392 . 50 THR HB H 4.26 0.0068 1 393 . 50 THR HG2 H 0.98 0.0068 1 394 . 50 THR C C 173.93 0.156 1 395 . 50 THR CA C 58.73 0.156 1 396 . 50 THR CB C 66.71 0.156 1 397 . 50 THR CG2 C 19.41 0.156 2 398 . 50 THR N N 103.09 0.158 1 399 . 51 GLY H H 7.65 0.0068 1 400 . 51 GLY HA2 H 3.52 0.0068 2 401 . 51 GLY C C 173.95 0.156 1 402 . 51 GLY CA C 43.25 0.156 1 403 . 51 GLY N N 108.74 0.158 1 404 . 52 ARG H H 7.96 0.0068 1 405 . 52 ARG HA H 4.33 0.0068 1 406 . 52 ARG HB2 H 1.79 0.0068 2 407 . 52 ARG HG2 H 1.54 0.0068 2 408 . 52 ARG HD2 H 3.13 0.0068 2 409 . 52 ARG C C 175.96 0.156 1 410 . 52 ARG CA C 54.49 0.156 1 411 . 52 ARG CB C 29.04 0.156 1 412 . 52 ARG CG C 25.59 0.156 1 413 . 52 ARG CD C 41 0.156 1 414 . 52 ARG N N 120.58 0.158 1 415 . 53 TRP H H 8.8 0.0068 1 416 . 53 TRP HA H 4.71 0.0068 1 417 . 53 TRP HB2 H 2.91 0.0068 2 418 . 53 TRP HE1 H 10.42 0.0068 2 419 . 53 TRP C C 176.59 0.156 1 420 . 53 TRP CA C 51.57 0.156 1 421 . 53 TRP CB C 27.87 0.156 1 422 . 53 TRP N N 124.4 0.158 1 423 . 53 TRP NE1 N 130.4 0.158 1 424 . 54 ARG H H 7.26 0.0068 1 425 . 54 ARG HA H 4.22 0.0068 1 426 . 54 ARG HB2 H 1.56 0.0068 2 427 . 54 ARG HG2 H 1.31 0.0068 2 428 . 54 ARG HD2 H 2.96 0.0068 2 429 . 54 ARG C C 178.58 0.156 1 430 . 54 ARG CA C 58.12 0.156 1 431 . 54 ARG CB C 26.5 0.156 1 432 . 54 ARG CG C 22.98 0.156 1 433 . 54 ARG CD C 41 0.156 1 434 . 54 ARG N N 121.06 0.158 1 435 . 55 ASP H H 7.45 0.0068 1 436 . 55 ASP HA H 4.58 0.0068 1 437 . 55 ASP HB2 H 2.71 0.0068 2 438 . 55 ASP C C 179 0.156 1 439 . 55 ASP CA C 54.91 0.156 1 440 . 55 ASP CB C 38.85 0.156 1 441 . 55 ASP N N 120.12 0.158 1 442 . 56 VAL H H 8.11 0.0068 1 443 . 56 VAL HA H 4.04 0.0068 1 444 . 56 VAL HB H 2.01 0.0068 1 445 . 56 VAL HG1 H 1.13 0.0068 1 446 . 56 VAL C C 177.24 0.156 1 447 . 56 VAL CA C 64.99 0.156 1 448 . 56 VAL CB C 29.58 0.156 1 449 . 56 VAL CG1 C 21.38 0.156 2 450 . 56 VAL N N 123.65 0.158 1 451 . 57 LYS H H 8.1 0.0068 1 452 . 57 LYS HA H 4.28 0.0068 1 453 . 57 LYS HB2 H 1.82 0.0068 2 454 . 57 LYS HG2 H 1.45 0.0068 2 455 . 57 LYS HE2 H 3.18 0.0068 2 456 . 57 LYS C C 177.87 0.156 1 457 . 57 LYS CA C 59.11 0.156 1 458 . 57 LYS CB C 30.09 0.156 1 459 . 57 LYS CG C 24.93 0.156 1 460 . 57 LYS CE C 41 0.156 1 461 . 57 LYS N N 120.02 0.158 1 462 . 58 PHE H H 7.92 0.0068 1 463 . 58 PHE HA H 4.57 0.0068 1 464 . 58 PHE HB2 H 3.17 0.0068 2 465 . 58 PHE C C 176.39 0.156 1 466 . 58 PHE CA C 58.52 0.156 1 467 . 58 PHE CB C 36.95 0.156 1 468 . 58 PHE N N 117.79 0.158 1 469 . 59 ARG H H 8.19 0.0068 1 470 . 59 ARG HA H 4.15 0.0068 1 471 . 59 ARG HB2 H 1.82 0.0068 2 472 . 59 ARG HG2 H 1.68 0.0068 2 473 . 59 ARG HD2 H 3.15 0.0068 2 474 . 59 ARG C C 177.59 0.156 1 475 . 59 ARG CA C 56.42 0.156 1 476 . 59 ARG CB C 28.83 0.156 1 477 . 59 ARG CG C 25.6 0.156 1 478 . 59 ARG CD C 40.83 0.156 1 479 . 59 ARG N N 116.77 0.158 1 480 . 60 ALA H H 7.79 0.0068 1 481 . 60 ALA HA H 4.5 0.0068 1 482 . 60 ALA HB H 1.55 0.0068 1 483 . 60 ALA C C 176.47 0.156 1 484 . 60 ALA CA C 49.6 0.156 1 485 . 60 ALA CB C 20.43 0.156 1 486 . 60 ALA N N 116.45 0.158 1 487 . 61 PHE H H 8.25 0.0068 1 488 . 61 PHE HA H 4.79 0.0068 1 489 . 61 PHE HB2 H 2.73 0.0068 2 490 . 61 PHE C C 177.08 0.156 1 491 . 61 PHE CA C 54.32 0.156 1 492 . 61 PHE CB C 39.61 0.156 1 493 . 61 PHE N N 115.66 0.158 1 494 . 62 GLU H H 8.34 0.0068 1 495 . 62 GLU HA H 3.85 0.0068 1 496 . 62 GLU HB2 H 1.75 0.0068 2 497 . 62 GLU HG2 H 2.41 0.0068 2 498 . 62 GLU C C 177.4 0.156 1 499 . 62 GLU CA C 58.48 0.156 1 500 . 62 GLU CB C 26.88 0.156 1 501 . 62 GLU CG C 32.21 0.156 1 502 . 62 GLU N N 126.39 0.158 1 503 . 63 ASN H H 8.69 0.0068 1 504 . 63 ASN HA H 4.81 0.0068 1 505 . 63 ASN HB2 H 2.74 0.0068 2 506 . 63 ASN HD21 H 6.885 0.0068 2 507 . 63 ASN HD22 H 7.562 0.0068 2 508 . 63 ASN C C 174.04 0.156 1 509 . 63 ASN CA C 50.57 0.156 1 510 . 63 ASN CB C 36.29 0.156 1 511 . 63 ASN N N 114.04 0.158 1 512 . 63 ASN ND2 N 111.8 0.158 1 513 . 64 VAL H H 7.08 0.0068 1 514 . 64 VAL HA H 4.16 0.0068 1 515 . 64 VAL HB H 2.15 0.0068 1 516 . 64 VAL HG1 H 0.98 0.0068 2 517 . 64 VAL CA C 59.17 0.156 1 518 . 64 VAL CB C 28.79 0.156 1 519 . 64 VAL CG1 C 19 0.156 2 520 . 64 VAL N N 119.69 0.158 1 521 . 66 HIS H H 7.469 0.0068 1 522 . 66 HIS C C 174.39 0.156 1 523 . 66 HIS N N 116.2 0.158 1 524 . 67 ARG H H 6.96 0.0068 1 525 . 67 ARG HA H 4.125 0.0068 1 526 . 67 ARG HB2 H 2.132 0.0068 2 527 . 67 ARG HG2 H 1.678 0.0068 2 528 . 67 ARG HD2 H 3.237 0.0068 2 529 . 67 ARG C C 174.86 0.156 1 530 . 67 ARG CA C 50.5 0.156 1 531 . 67 ARG CB C 27.6 0.156 1 532 . 67 ARG CG C 24.5 0.156 1 533 . 67 ARG CD C 41.2 0.156 1 534 . 67 ARG N N 119.3 0.158 1 535 . 68 THR H H 8.72 0.0068 1 536 . 68 THR HA H 4.28 0.0068 1 537 . 68 THR HB H 4.24 0.0068 1 538 . 68 THR HG2 H 1.29 0.0068 1 539 . 68 THR C C 176.18 0.156 1 540 . 68 THR CA C 58.23 0.156 1 541 . 68 THR CB C 69.65 0.156 1 542 . 68 THR CG2 C 18.83 0.156 2 543 . 68 THR N N 115.07 0.158 1 544 . 69 TYR H H 8.93 0.0068 1 545 . 69 TYR HA H 4.53 0.0068 1 546 . 69 TYR HB2 H 3.01 0.0068 2 547 . 69 TYR C C 176.19 0.156 1 548 . 69 TYR CA C 58.8 0.156 1 549 . 69 TYR CB C 35.37 0.156 1 550 . 69 TYR N N 118.03 0.158 1 551 . 70 VAL H H 6.39 0.0068 1 552 . 70 VAL HA H 4.2 0.0068 1 553 . 70 VAL HB H 2.08 0.0068 1 554 . 70 VAL HG1 H 0.91 0.0068 2 555 . 70 VAL C C 176.95 0.156 1 556 . 70 VAL CA C 62.34 0.156 1 557 . 70 VAL CB C 29.74 0.156 1 558 . 70 VAL CG1 C 18.59 0.156 2 559 . 70 VAL N N 120.09 0.158 1 560 . 71 ASP H H 7.29 0.0068 1 561 . 71 ASP HA H 4.61 0.0068 1 562 . 71 ASP HB2 H 2.72 0.0068 2 563 . 71 ASP C C 179.45 0.156 1 564 . 71 ASP CA C 54.91 0.156 1 565 . 71 ASP CB C 39.87 0.156 1 566 . 71 ASP N N 120.37 0.158 1 567 . 72 LEU H H 7.6 0.0068 1 568 . 72 LEU HA H 4.21 0.0068 1 569 . 72 LEU HB2 H 1.82 0.0068 2 570 . 72 LEU HD1 H 0.81 0.0068 2 571 . 72 LEU C C 180.44 0.156 1 572 . 72 LEU CA C 55.5 0.156 1 573 . 72 LEU CB C 37.41 0.156 1 574 . 72 LEU CD1 C 19.37 0.156 2 575 . 72 LEU N N 118.12 0.158 1 576 . 73 LYS H H 7.37 0.0068 1 577 . 73 LYS HA H 4.32 0.0068 1 578 . 73 LYS HB2 H 1.8 0.0068 2 579 . 73 LYS HE2 H 3.09 0.0068 2 580 . 73 LYS C C 178.52 0.156 1 581 . 73 LYS CA C 57.85 0.156 1 582 . 73 LYS CB C 29.65 0.156 1 583 . 73 LYS CE C 40.83 0.156 1 584 . 73 LYS N N 120.63 0.158 1 585 . 74 ASP H H 8.11 0.0068 1 586 . 74 ASP HA H 4.21 0.0068 1 587 . 74 ASP HB2 H 2.57 0.0068 2 588 . 74 ASP C C 178.95 0.156 1 589 . 74 ASP CA C 55.8 0.156 1 590 . 74 ASP CB C 39.49 0.156 1 591 . 74 ASP N N 118.57 0.158 1 592 . 75 LYS H H 7.98 0.0068 1 593 . 75 LYS HA H 4.28 0.0068 1 594 . 75 LYS HB2 H 1.92 0.0068 2 595 . 75 LYS HG2 H 1.6 0.0068 2 596 . 75 LYS HE2 H 3.14 0.0068 2 597 . 75 LYS C C 178.52 0.156 1 598 . 75 LYS CA C 54.25 0.156 1 599 . 75 LYS CB C 28.85 0.156 1 600 . 75 LYS CG C 23.49 0.156 1 601 . 75 LYS CE C 40.83 0.156 1 602 . 75 LYS N N 120.87 0.158 1 603 . 76 TRP H H 8.4 0.0068 1 604 . 76 TRP HA H 4.29 0.0068 1 605 . 76 TRP HB2 H 3.18 0.0068 2 606 . 76 TRP C C 176.7 0.156 1 607 . 76 TRP CA C 58.57 0.156 1 608 . 76 TRP CB C 28.41 0.156 1 609 . 76 TRP N N 121.04 0.158 1 610 . 76 TRP NE1 N 131.4 0.158 2 611 . 77 LYS H H 7.77 0.0068 1 612 . 77 LYS HA H 4.15 0.0068 1 613 . 77 LYS HB2 H 1.77 0.0068 2 614 . 77 LYS HG2 H 1.52 0.0068 2 615 . 77 LYS HE2 H 3.18 0.0068 2 616 . 77 LYS C C 180.21 0.156 1 617 . 77 LYS CA C 58.03 0.156 1 618 . 77 LYS CB C 29.73 0.156 1 619 . 77 LYS CG C 23.59 0.156 1 620 . 77 LYS CE C 40.93 0.156 1 621 . 77 LYS N N 116.08 0.158 1 622 . 78 THR H H 7.92 0.0068 1 623 . 78 THR HA H 4.29 0.0068 1 624 . 78 THR HB H 4.25 0.0068 1 625 . 78 THR C C 177.33 0.156 1 626 . 78 THR CA C 63.84 0.156 1 627 . 78 THR CB C 66.25 0.156 1 628 . 78 THR CG2 C 18.02 0.156 2 629 . 78 THR N N 114.06 0.158 1 630 . 79 LEU H H 8.47 0.0068 1 631 . 79 LEU HA H 4.17 0.0068 1 632 . 79 LEU HB2 H 1.59 0.0068 2 633 . 79 LEU HD1 H 0.89 0.0068 2 634 . 79 LEU C C 178.04 0.156 1 635 . 79 LEU CA C 56 0.156 1 636 . 79 LEU CB C 39.82 0.156 1 637 . 79 LEU CD1 C 20.02 0.156 2 638 . 79 LEU N N 126.87 0.158 1 639 . 80 VAL H H 8.12 0.0068 1 640 . 80 VAL HA H 3.89 0.0068 1 641 . 80 VAL HB H 2.37 0.0068 1 642 . 80 VAL HG1 H 1 0.0068 2 643 . 80 VAL C C 178.73 0.156 1 644 . 80 VAL CA C 64.68 0.156 1 645 . 80 VAL CB C 29.6 0.156 1 646 . 80 VAL CG1 C 20.93 0.156 2 647 . 80 VAL N N 120 0.158 1 648 . 81 HIS H H 7.7 0.0068 1 649 . 81 HIS HA H 4.66 0.0068 1 650 . 81 HIS HB2 H 3.14 0.0068 2 651 . 81 HIS C C 177.7 0.156 1 652 . 81 HIS CA C 57.96 0.156 1 653 . 81 HIS CB C 27.57 0.156 1 654 . 81 HIS N N 119.2 0.158 1 655 . 82 THR H H 8.53 0.0068 1 656 . 82 THR HA H 4.22 0.0068 1 657 . 82 THR HB H 4.17 0.0068 1 658 . 82 THR HG2 H 0.84 0.0068 1 659 . 82 THR C C 175.08 0.156 1 660 . 82 THR CA C 64.81 0.156 1 661 . 82 THR CB C 66.51 0.156 1 662 . 82 THR CG2 C 18.9 0.156 2 663 . 82 THR N N 116.19 0.158 1 664 . 83 ALA H H 8.53 0.0068 1 665 . 83 ALA HA H 3.93 0.0068 1 666 . 83 ALA HB H 1.37 0.0068 1 667 . 83 ALA C C 177.92 0.156 1 668 . 83 ALA CA C 52.08 0.156 1 669 . 83 ALA CB C 16.47 0.156 1 670 . 83 ALA N N 119.95 0.158 1 671 . 84 SER H H 7.58 0.0068 1 672 . 84 SER HA H 4.39 0.0068 1 673 . 84 SER HB2 H 3.94 0.0068 2 674 . 84 SER C C 173.49 0.156 1 675 . 84 SER CA C 57.57 0.156 1 676 . 84 SER CB C 61.95 0.156 1 677 . 84 SER N N 111.06 0.158 1 678 . 85 ILE H H 7.18 0.0068 1 679 . 85 ILE HA H 4.45 0.0068 1 680 . 85 ILE HB H 1.96 0.0068 1 681 . 85 ILE HG12 H 0.76 0.0068 2 682 . 85 ILE HD1 H 0.66 0.0068 1 683 . 85 ILE C C 174.86 0.156 1 684 . 85 ILE CA C 57.28 0.156 1 685 . 85 ILE CB C 37.26 0.156 1 686 . 85 ILE CD1 C 14.71 0.156 2 687 . 85 ILE N N 118.44 0.158 1 688 . 86 ALA H H 8.18 0.0068 1 689 . 86 ALA HA H 4.45 0.0068 1 690 . 86 ALA HB H 1.42 0.0068 1 691 . 86 ALA CA C 48.75 0.156 1 692 . 86 ALA CB C 15.33 0.156 1 693 . 86 ALA N N 125.57 0.158 1 694 . 87 PRO HA H 4.4 0.0068 1 695 . 87 PRO HB2 H 2.25 0.0068 2 696 . 87 PRO HG2 H 2 0.0068 2 697 . 87 PRO HD2 H 3.84 0.0068 2 698 . 87 PRO C C 179.16 0.156 1 699 . 87 PRO CA C 64.19 0.156 1 700 . 87 PRO CB C 30.09 0.156 1 701 . 87 PRO CG C 25.59 0.156 1 702 . 87 PRO CD C 48.49 0.156 1 703 . 88 GLN H H 8.81 0.0068 1 704 . 88 GLN HA H 4.17 0.0068 1 705 . 88 GLN HB2 H 2.09 0.0068 2 706 . 88 GLN HG2 H 2.48 0.0068 2 707 . 88 GLN C C 176.79 0.156 1 708 . 88 GLN CA C 56.07 0.156 1 709 . 88 GLN CB C 25.75 0.156 1 710 . 88 GLN CG C 31.49 0.156 1 711 . 88 GLN N N 114.4 0.158 1 712 . 89 GLN H H 8.05 0.0068 1 713 . 89 GLN HA H 4.26 0.0068 1 714 . 89 GLN HB2 H 2.07 0.0068 2 715 . 89 GLN HG2 H 2.41 0.0068 2 716 . 89 GLN C C 175.89 0.156 1 717 . 89 GLN CA C 53.27 0.156 1 718 . 89 GLN CB C 27.99 0.156 1 719 . 89 GLN CG C 32.24 0.156 1 720 . 89 GLN N N 116.78 0.158 1 721 . 90 ARG H H 7.29 0.0068 1 722 . 90 ARG HA H 4.16 0.0068 1 723 . 90 ARG HB2 H 1.89 0.0068 2 724 . 90 ARG HG2 H 1.55 0.0068 2 725 . 90 ARG HD2 H 3.18 0.0068 2 726 . 90 ARG C C 180.39 0.156 1 727 . 90 ARG CA C 55.23 0.156 1 728 . 90 ARG CB C 28.44 0.156 1 729 . 90 ARG CG C 25.5 0.156 1 730 . 90 ARG CD C 41.83 0.156 1 731 . 90 ARG N N 120.16 0.158 1 732 . 91 ARG H H 8.52 0.0068 1 733 . 91 ARG HA H 4.64 0.0068 1 734 . 91 ARG HB2 H 1.95 0.0068 2 735 . 91 ARG HG2 H 1.71 0.0068 2 736 . 91 ARG HD2 H 3.26 0.0068 2 737 . 91 ARG C C 176.71 0.156 1 738 . 91 ARG CA C 53.3 0.156 1 739 . 91 ARG CB C 30.6 0.156 1 740 . 91 ARG CG C 24.71 0.156 1 741 . 91 ARG CD C 41.24 0.156 1 742 . 91 ARG N N 122.48 0.158 1 743 . 92 GLY H H 8.51 0.0068 1 744 . 92 GLY HA2 H 3.81 0.0068 2 745 . 92 GLY C C 173.72 0.156 1 746 . 92 GLY CA C 42.09 0.156 1 747 . 92 GLY N N 109.51 0.158 1 748 . 93 ALA H H 8.37 0.0068 1 749 . 93 ALA HA H 4.48 0.0068 1 750 . 93 ALA HB H 1.34 0.0068 1 751 . 93 ALA CA C 49.69 0.156 1 752 . 93 ALA CB C 15.3 0.156 1 753 . 93 ALA N N 125.14 0.158 1 754 . 94 PRO HA H 4.33 0.0068 1 755 . 94 PRO HB2 H 2.14 0.0068 2 756 . 94 PRO HG2 H 1.95 0.0068 2 757 . 94 PRO HD2 H 3.58 0.0068 2 758 . 94 PRO C C 176.69 0.156 1 759 . 94 PRO CA C 61.11 0.156 1 760 . 94 PRO CB C 29.88 0.156 1 761 . 94 PRO CG C 25.59 0.156 1 762 . 94 PRO CD C 48.48 0.156 1 763 . 95 VAL H H 8.15 0.0068 1 764 . 95 VAL HA H 4.3 0.0068 1 765 . 95 VAL HB H 1.78 0.0068 1 766 . 95 VAL HG1 H 0.88 0.0068 2 767 . 95 VAL CA C 56.96 0.156 1 768 . 95 VAL CB C 32.45 0.156 1 769 . 95 VAL CG1 C 18.59 0.156 2 770 . 95 VAL N N 123 0.158 1 771 . 96 PRO HA H 4.44 0.0068 1 772 . 96 PRO HB2 H 2.14 0.0068 2 773 . 96 PRO HG2 H 1.92 0.0068 2 774 . 96 PRO HD2 H 3.81 0.0068 2 775 . 96 PRO C C 177.88 0.156 1 776 . 96 PRO CA C 60.97 0.156 1 777 . 96 PRO CB C 30.72 0.156 1 778 . 96 PRO CG C 25.59 0.156 1 779 . 96 PRO CD C 48.84 0.156 1 780 . 97 GLN H H 9.06 0.0068 1 781 . 97 GLN HA H 4.37 0.0068 1 782 . 97 GLN HB2 H 2.02 0.0068 2 783 . 97 GLN HG2 H 2.4 0.0068 2 784 . 97 GLN C C 177.04 0.156 1 785 . 97 GLN CA C 56.5 0.156 1 786 . 97 GLN CB C 26.59 0.156 1 787 . 97 GLN CG C 31.34 0.156 1 788 . 97 GLN N N 126.54 0.158 1 789 . 98 GLU H H 9.54 0.0068 1 790 . 98 GLU HA H 4.13 0.0068 1 791 . 98 GLU HB2 H 2.1 0.0068 2 792 . 98 GLU HG2 H 2.42 0.0068 2 793 . 98 GLU C C 179.62 0.156 1 794 . 98 GLU CA C 57 0.156 1 795 . 98 GLU CB C 26.56 0.156 1 796 . 98 GLU CG C 31.66 0.156 1 797 . 98 GLU N N 116.67 0.158 1 798 . 99 LEU H H 7.21 0.0068 1 799 . 99 LEU HA H 4.25 0.0068 1 800 . 99 LEU HB2 H 1.88 0.0068 2 801 . 99 LEU HG H 1.78 0.0068 1 802 . 99 LEU HD1 H 0.97 0.0068 2 803 . 99 LEU C C 178.63 0.156 1 804 . 99 LEU CA C 55.09 0.156 1 805 . 99 LEU CB C 39.68 0.156 1 806 . 99 LEU CG C 25 0.156 1 807 . 99 LEU CD1 C 21.71 0.156 2 808 . 99 LEU N N 117.99 0.158 1 809 . 100 LEU H H 7.42 0.0068 1 810 . 100 LEU HA H 3.81 0.0068 1 811 . 100 LEU HB2 H 2.07 0.0068 2 812 . 100 LEU HD1 H 0.92 0.0068 2 813 . 100 LEU C C 178.95 0.156 1 814 . 100 LEU CA C 55.58 0.156 1 815 . 100 LEU CB C 38 0.156 1 816 . 100 LEU CD1 C 23.96 0.156 2 817 . 100 LEU N N 119.88 0.158 1 818 . 101 ASP H H 8.94 0.0068 1 819 . 101 ASP HA H 4.44 0.0068 1 820 . 101 ASP HB2 H 2.76 0.0068 2 821 . 101 ASP C C 176.2 0.156 1 822 . 101 ASP CA C 55.65 0.156 1 823 . 101 ASP CB C 37.86 0.156 1 824 . 101 ASP N N 119.29 0.158 1 825 . 102 ARG H H 7.06 0.0068 1 826 . 102 ARG HA H 4.3 0.0068 1 827 . 102 ARG HB2 H 1.9 0.0068 2 828 . 102 ARG HD2 H 3.11 0.0068 2 829 . 102 ARG C C 180.07 0.156 1 830 . 102 ARG CA C 56.78 0.156 1 831 . 102 ARG CB C 28.64 0.156 1 832 . 102 ARG CD C 41.17 0.156 1 833 . 102 ARG N N 121.22 0.158 1 834 . 103 VAL H H 8.22 0.0068 1 835 . 103 VAL HA H 4.3 0.0068 1 836 . 103 VAL HB H 2.49 0.0068 1 837 . 103 VAL HG1 H 0.91 0.0068 2 838 . 103 VAL C C 177.46 0.156 1 839 . 103 VAL CA C 64.29 0.156 1 840 . 103 VAL CB C 29.04 0.156 1 841 . 103 VAL CG1 C 20.67 0.156 2 842 . 103 VAL N N 123.36 0.158 1 843 . 104 LEU H H 7.81 0.0068 1 844 . 104 LEU HA H 4.32 0.0068 1 845 . 104 LEU HB2 H 1.64 0.0068 2 846 . 104 LEU HG H 1.64 0.0068 2 847 . 104 LEU HD1 H 0.83 0.0068 2 848 . 104 LEU C C 180.47 0.156 1 849 . 104 LEU CA C 55.9 0.156 1 850 . 104 LEU CB C 39.14 0.156 1 851 . 104 LEU CG C 24.71 0.156 1 852 . 104 LEU CD1 C 20.12 0.156 2 853 . 104 LEU N N 117.45 0.158 1 854 . 105 ALA H H 8.12 0.0068 1 855 . 105 ALA HA H 4.25 0.0068 1 856 . 105 ALA HB H 1.58 0.0068 1 857 . 105 ALA C C 176.16 0.156 1 858 . 105 ALA CA C 53.03 0.156 1 859 . 105 ALA CB C 16.09 0.156 1 860 . 105 ALA N N 121.66 0.158 1 861 . 106 ALA H H 8.51 0.0068 1 862 . 106 ALA HA H 4.2 0.0068 1 863 . 106 ALA HB H 1.52 0.0068 1 864 . 106 ALA C C 179.46 0.156 1 865 . 106 ALA CA C 53.03 0.156 1 866 . 106 ALA CB C 16.09 0.156 1 867 . 106 ALA N N 122.69 0.158 1 868 . 107 GLN H H 8.87 0.0068 1 869 . 107 GLN HA H 4.16 0.0068 1 870 . 107 GLN HB2 H 2.24 0.0068 2 871 . 107 GLN HG2 H 2.55 0.0068 2 872 . 107 GLN C C 178.8 0.156 1 873 . 107 GLN CA C 56.25 0.156 1 874 . 107 GLN CB C 26.9 0.156 1 875 . 107 GLN CG C 35.32 0.156 1 876 . 107 GLN N N 118.19 0.158 1 877 . 108 ALA H H 8.01 0.0068 1 878 . 108 ALA HA H 4.29 0.0068 1 879 . 108 ALA HB H 1.54 0.0068 1 880 . 108 ALA C C 180 0.156 1 881 . 108 ALA CA C 52.78 0.156 1 882 . 108 ALA CB C 16.22 0.156 1 883 . 108 ALA N N 120.27 0.158 1 884 . 109 TYR H H 8.3 0.0068 1 885 . 109 TYR HA H 4.57 0.0068 1 886 . 109 TYR HB2 H 3.16 0.0068 2 887 . 109 TYR C C 177.71 0.156 1 888 . 109 TYR CA C 59.29 0.156 1 889 . 109 TYR CB C 36.67 0.156 1 890 . 109 TYR N N 119.82 0.158 1 891 . 110 TRP H H 8.1 0.0068 1 892 . 110 TRP HA H 4.56 0.0068 1 893 . 110 TRP HB2 H 3.13 0.0068 2 894 . 110 TRP HE1 H 9.44 0.0068 2 895 . 110 TRP C C 176.74 0.156 1 896 . 110 TRP CA C 56.31 0.156 1 897 . 110 TRP CB C 27.5 0.156 1 898 . 110 TRP N N 115.57 0.158 1 899 . 110 TRP NE1 N 128.4 0.158 2 900 . 111 SER H H 7.74 0.0068 1 901 . 111 SER HA H 4.65 0.0068 1 902 . 111 SER HB2 H 4.14 0.0068 2 903 . 111 SER C C 174.7 0.156 1 904 . 111 SER CA C 57.33 0.156 1 905 . 111 SER CB C 62.19 0.156 1 906 . 111 SER N N 115.27 0.158 1 907 . 112 VAL H H 7.72 0.0068 1 908 . 112 VAL HA H 4.21 0.0068 1 909 . 112 VAL HB H 2.05 0.0068 1 910 . 112 VAL HG1 H 0.9 0.0068 2 911 . 112 VAL C C 176.13 0.156 1 912 . 112 VAL CA C 60.13 0.156 1 913 . 112 VAL CB C 30.11 0.156 1 914 . 112 VAL CG1 C 19.17 0.156 2 915 . 112 VAL N N 120 0.158 1 916 . 113 ASP H H 8.32 0.0068 1 917 . 113 ASP HA H 4.89 0.0068 1 918 . 113 ASP HB2 H 2.73 0.0068 2 919 . 113 ASP C C 176.91 0.156 1 920 . 113 ASP CA C 51.5 0.156 1 921 . 113 ASP CB C 39.49 0.156 1 922 . 113 ASP N N 123.28 0.158 1 923 . 114 SER H H 8.35 0.0068 1 924 . 114 SER HA H 4.33 0.0068 1 925 . 114 SER HB2 H 3.82 0.0068 2 926 . 114 SER C C 175.35 0.156 1 927 . 114 SER CA C 56.63 0.156 1 928 . 114 SER CB C 61.46 0.156 1 929 . 114 SER N N 116.67 0.158 1 930 . 115 SER H H 8.42 0.0068 1 931 . 115 SER HA H 4.3 0.0068 1 932 . 115 SER HB2 H 3.91 0.0068 2 933 . 115 SER C C 175.3 0.156 1 934 . 115 SER CA C 57.8 0.156 1 935 . 115 SER CB C 62.05 0.156 1 936 . 115 SER N N 117.94 0.158 1 937 . 116 GLY H H 8.34 0.0068 1 938 . 116 GLY HA2 H 3.92 0.0068 2 939 . 116 GLY C C 175.03 0.156 1 940 . 116 GLY CA C 43.39 0.156 1 941 . 116 GLY N N 110.43 0.158 1 942 . 117 ARG H H 8.01 0.0068 1 943 . 117 ARG HA H 4.25 0.0068 1 944 . 117 ARG HB2 H 1.79 0.0068 2 945 . 117 ARG HD2 H 3.1 0.0068 2 946 . 117 ARG C C 176 0.156 1 947 . 117 ARG CA C 54.38 0.156 1 948 . 117 ARG CB C 28.76 0.156 1 949 . 117 ARG CD C 41.76 0.156 1 950 . 117 ARG N N 123.87 0.158 1 951 . 118 ILE H H 8.24 0.0068 1 952 . 118 ILE HA H 4.18 0.0068 1 953 . 118 ILE HB H 1.8 0.0068 1 954 . 118 ILE HG12 H 0.84 0.0068 2 955 . 118 ILE HD1 H 0.79 0.0068 1 956 . 118 ILE C C 176.18 0.156 1 957 . 118 ILE CA C 59.31 0.156 1 958 . 118 ILE CB C 36.32 0.156 1 959 . 118 ILE CD1 C 15.81 0.156 2 960 . 118 ILE N N 123.52 0.158 1 961 . 119 VAL H H 8.32 0.0068 1 962 . 119 VAL HA H 4.25 0.0068 1 963 . 119 VAL HB H 2.11 0.0068 1 964 . 119 VAL HG1 H 0.97 0.0068 2 965 . 119 VAL C C 176.2 0.156 1 966 . 119 VAL CA C 60.13 0.156 1 967 . 119 VAL CB C 30.4 0.156 1 968 . 119 VAL CG1 C 18.19 0.156 2 969 . 119 VAL N N 125.59 0.158 1 970 . 120 THR H H 8.226 0.0068 1 971 . 120 THR HA H 4.479 0.0068 1 972 . 120 THR HB H 4.346 0.0068 1 973 . 120 THR HG2 H 1.232 0.0068 1 974 . 120 THR CA C 58.97 0.156 1 975 . 120 THR CB C 67.73 0.156 1 976 . 120 THR CG2 C 18.09 0.156 2 977 . 120 THR N N 118 0.158 1 stop_ save_