data_5878 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N NMR assignment of the region 1463-1617 of mouse p53 Binding Protein 1 (53BP1) ; _BMRB_accession_number 5878 _BMRB_flat_file_name bmr5878.str _Entry_type original _Submission_date 2003-07-22 _Accession_date 2003-07-22 _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 Charier Gaelle . . 2 Alpha-Bazin Beatrice . . 3 Couprie Joel . . 4 Callebaut Isabelle . . 5 Berenguer Frederic . . 6 Quemeneur Eric . . 7 Gilquin Bernard . . 8 Zinn-Justin Sophie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 877 "13C chemical shifts" 676 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 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 the region 1463-1617 of the mouse p53 Binding Protein 1 (53BP1) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14752266 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Charier Gaelle . . 2 Alpha-Bazin Beatrice . . 3 Couprie Joel . . 4 Callebaut Isabelle . . 5 Berenguer Frederic . . 6 Quemeneur Eric . . 7 Gilquin Bernard . . 8 Zinn-Justin Sophie . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 303 _Page_last 304 _Year 2004 _Details . loop_ _Keyword 'DNA Damage' 'double strand break' 'signalling pathway' 'tudor domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_53BP1 _Saveframe_category molecular_system _Mol_system_name 'region 1463-1617 of mouse 53BP1' _Abbreviation_common 53BP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '53BP1 subunit 1' $53BP1_monomer 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_53BP1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'p53 Binding Protein 1' _Abbreviation_common 53BP1 _Molecular_mass 17345 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; DSSSSGNSFVGLRVVAKWSS NGYFYSGKITRDVGAGKYKL LFDDGYECDVLGKDILLCDP IPLDTEVTALSEDEYFSAGV VKGHRKESGELYYSIEKEGQ RKWYKRMAVILSLEQGNRLR EQYGLGPYEAVTPLTKAADI SLDNLVEGKRKRRSN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1463 ASP 2 1464 SER 3 1465 SER 4 1466 SER 5 1467 SER 6 1468 GLY 7 1469 ASN 8 1470 SER 9 1471 PHE 10 1472 VAL 11 1473 GLY 12 1474 LEU 13 1475 ARG 14 1476 VAL 15 1477 VAL 16 1478 ALA 17 1479 LYS 18 1480 TRP 19 1481 SER 20 1482 SER 21 1483 ASN 22 1484 GLY 23 1485 TYR 24 1486 PHE 25 1487 TYR 26 1488 SER 27 1489 GLY 28 1490 LYS 29 1491 ILE 30 1492 THR 31 1493 ARG 32 1494 ASP 33 1495 VAL 34 1496 GLY 35 1497 ALA 36 1498 GLY 37 1499 LYS 38 1500 TYR 39 1501 LYS 40 1502 LEU 41 1503 LEU 42 1504 PHE 43 1505 ASP 44 1506 ASP 45 1507 GLY 46 1508 TYR 47 1509 GLU 48 1510 CYS 49 1511 ASP 50 1512 VAL 51 1513 LEU 52 1514 GLY 53 1515 LYS 54 1516 ASP 55 1517 ILE 56 1518 LEU 57 1519 LEU 58 1520 CYS 59 1521 ASP 60 1522 PRO 61 1523 ILE 62 1524 PRO 63 1525 LEU 64 1526 ASP 65 1527 THR 66 1528 GLU 67 1529 VAL 68 1530 THR 69 1531 ALA 70 1532 LEU 71 1533 SER 72 1534 GLU 73 1535 ASP 74 1536 GLU 75 1537 TYR 76 1538 PHE 77 1539 SER 78 1540 ALA 79 1541 GLY 80 1542 VAL 81 1543 VAL 82 1544 LYS 83 1545 GLY 84 1546 HIS 85 1547 ARG 86 1548 LYS 87 1549 GLU 88 1550 SER 89 1551 GLY 90 1552 GLU 91 1553 LEU 92 1554 TYR 93 1555 TYR 94 1556 SER 95 1557 ILE 96 1558 GLU 97 1559 LYS 98 1560 GLU 99 1561 GLY 100 1562 GLN 101 1563 ARG 102 1564 LYS 103 1565 TRP 104 1566 TYR 105 1567 LYS 106 1568 ARG 107 1569 MET 108 1570 ALA 109 1571 VAL 110 1572 ILE 111 1573 LEU 112 1574 SER 113 1575 LEU 114 1576 GLU 115 1577 GLN 116 1578 GLY 117 1579 ASN 118 1580 ARG 119 1581 LEU 120 1582 ARG 121 1583 GLU 122 1584 GLN 123 1585 TYR 124 1586 GLY 125 1587 LEU 126 1588 GLY 127 1589 PRO 128 1590 TYR 129 1591 GLU 130 1592 ALA 131 1593 VAL 132 1594 THR 133 1595 PRO 134 1596 LEU 135 1597 THR 136 1598 LYS 137 1599 ALA 138 1600 ALA 139 1601 ASP 140 1602 ILE 141 1603 SER 142 1604 LEU 143 1605 ASP 144 1606 ASN 145 1607 LEU 146 1608 VAL 147 1609 GLU 148 1610 GLY 149 1611 LYS 150 1612 ARG 151 1613 LYS 152 1614 ARG 153 1615 ARG 154 1616 SER 155 1617 ASN 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 18579 entity_1 77.42 123 100.00 100.00 1.20e-80 BMRB 25347 entity_1 77.42 123 100.00 100.00 1.20e-80 BMRB 25348 entity_1 77.42 123 100.00 100.00 1.20e-80 PDB 1SSF "Solution Structure Of The Mouse 53bp1 Fragment (Residues 1463-1617)" 100.00 156 100.00 100.00 4.47e-107 PDB 1XNI "Tandem Tudor Domain Of 53bp1" 76.13 118 100.00 100.00 7.09e-79 PDB 2G3R "Crystal Structure Of 53bp1 Tandem Tudor Domains At 1.2 A Resolution" 77.42 123 100.00 100.00 1.20e-80 PDB 2IG0 "Structure Of 53bp1METHYLATED HISTONE PEPTIDE COMPLEX" 77.42 123 100.00 100.00 1.20e-80 PDB 2LVM "Solution Structure Of Human 53bp1 Tandem Tudor Domains In Complex With A Histone H4k20me2 Peptide" 77.42 123 100.00 100.00 1.20e-80 PDB 2MWO "Solution Structure Of 53bp1 Tandem Tudor Domains In Complex With A P53k370me2 Peptide" 77.42 123 100.00 100.00 1.20e-80 PDB 2MWP "Solution Structure Of 53bp1 Tandem Tudor Domains In Complex With A P53k382me2 Peptide" 77.42 123 100.00 100.00 1.20e-80 PDB 3LGF "Crystal Structure Of The 53bp1 Tandem Tudor Domain In Comple P53k370me2" 77.42 125 100.00 100.00 2.20e-80 PDB 3LGL "Crystal Structure Of The 53bp1 Tandem Tudor Domain In Comple P53k382me2" 77.42 125 100.00 100.00 2.20e-80 PDB 3LH0 "Crystal Structure Of The 53bp1 Tandem Tudor Domain In Comple P53k372me2" 77.42 125 100.00 100.00 2.20e-80 PDB 4CRI "Crystal Structure Of 53bp1 Tandem Tudor Domains In Complex With Methylated K810 Rb Peptide" 100.00 176 98.71 99.35 6.17e-106 PDB 4RG2 "Tudor Domain Of Tumor Suppressor P53bp1 With Small Molecule Ligand" 80.00 125 100.00 100.00 6.94e-84 DBJ BAC26637 "unnamed protein product [Mus musculus]" 100.00 714 100.00 100.00 6.63e-103 DBJ BAC29383 "unnamed protein product [Mus musculus]" 100.00 613 100.00 100.00 3.95e-103 DBJ BAE06107 "TP53BP1 variant protein [Homo sapiens]" 100.00 1984 98.71 99.35 1.30e-95 DBJ BAE21103 "unnamed protein product [Mus musculus]" 100.00 689 100.00 100.00 7.77e-103 DBJ BAG10235 "tumor protein p53 binding protein, 1 [synthetic construct]" 100.00 1975 98.71 99.35 1.15e-95 EMBL CAC94013 "53BP1 protein [Mus musculus]" 100.00 1957 100.00 100.00 2.72e-97 EMBL CAD97660 "hypothetical protein [Homo sapiens]" 100.00 1977 98.06 98.71 1.63e-94 GB AAA21596 "p53-binding protein, partial [Homo sapiens]" 100.00 1027 98.71 99.35 2.54e-100 GB AAC62018 "p53 tumor suppressor-binding protein 1 [Homo sapiens]" 100.00 1972 98.71 99.35 1.28e-95 GB AAH35206 "Trp53bp1 protein [Mus musculus]" 100.00 1014 100.00 100.00 1.60e-101 GB AAH79906 "Trp53bp1 protein [Mus musculus]" 100.00 1914 100.00 100.00 2.12e-97 GB AAI12162 "Tumor protein p53 binding protein 1 [Homo sapiens]" 100.00 1972 98.71 99.35 1.28e-95 REF NP_001135451 "tumor suppressor p53-binding protein 1 isoform 2 [Homo sapiens]" 100.00 1975 98.71 99.35 1.15e-95 REF NP_001135452 "tumor suppressor p53-binding protein 1 isoform 1 [Homo sapiens]" 100.00 1977 98.71 99.35 1.29e-95 REF NP_001162434 "tumor suppressor p53-binding protein 1 [Papio anubis]" 100.00 1972 98.71 99.35 8.48e-96 REF NP_001193326 "tumor suppressor p53-binding protein 1 [Bos taurus]" 100.00 1966 98.71 99.35 1.73e-95 REF NP_001277759 "tumor suppressor p53-binding protein 1 isoform b [Mus musculus]" 100.00 1919 100.00 100.00 2.13e-97 SP P70399 "RecName: Full=Tumor suppressor p53-binding protein 1; Short=53BP1; Short=p53-binding protein 1; Short=p53BP1 [Mus musculus]" 100.00 1957 100.00 100.00 3.18e-97 SP Q12888 "RecName: Full=Tumor suppressor p53-binding protein 1; Short=53BP1; Short=p53-binding protein 1; Short=p53BP1 [Homo sapiens]" 100.00 1972 98.71 99.35 1.28e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $53BP1_monomer Mouse 10090 Eukaryota Metazoa Mus musculus nuclear 53BP1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $53BP1_monomer 'recombinant technology' 'E. coli' Escherichia coli 'BL21 Gold DE3' plasmid pDEST15 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 $53BP1_monomer 0.8 mM '[U-95% 13C; U-95% 15N]' Tris-HCl 50 mM . NaCl 150 mM . D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $53BP1_monomer 0.8 mM '[U-95% 13C; U-95% 15N]' Tris-HCl 50 mM . NaCl 150 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $53BP1_monomer 0.7 mM '[U-95% 15N]' Tris-HCl 50 mM . NaCl 150 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.0 loop_ _Task 'data processing' stop_ _Details 'Delaglio et al. (1995), J. Biomol. NMR 6, 277-293.' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task 'data analysis' stop_ _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 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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCACOHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACOHA _Sample_label . save_ save_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_(HCA)CO(CA)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label . save_ save_15N_HSQC_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC NOESY' _Sample_label . save_ save_HBHA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HCCH_TOSCY_12 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOSCY' _Sample_label . save_ save_HCCH_COSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _Sample_label . save_ save_13C_HSQC_NOESY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC NOESY' _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 HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACOHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOSCY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.1 0.1 n/a temperature 300 0.2 K 'ionic strength' 0.2 0.05 M stop_ save_ save_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.0 0.1 n/a temperature 300 0.2 K 'ionic strength' 0.2 0.05 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details 'Several residues split in two. The major form is (Segment A) is listed here.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '53BP1 subunit 1' _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 . 5 SER HA H 4.480 0.03 1 2 . 5 SER HB2 H 3.890 0.03 2 3 . 5 SER HB3 H 3.940 0.03 2 4 . 5 SER C C 175.000 0.3 1 5 . 5 SER CA C 58.370 0.3 1 6 . 5 SER CB C 63.450 0.3 1 7 . 6 GLY H H 8.360 0.03 1 8 . 6 GLY HA2 H 3.990 0.03 2 9 . 6 GLY CA C 45.390 0.3 1 10 . 6 GLY N N 110.300 0.3 1 11 . 7 ASN HA H 4.660 0.03 1 12 . 7 ASN HB2 H 2.670 0.03 1 13 . 7 ASN HB3 H 2.670 0.03 1 14 . 7 ASN HD21 H 6.910 0.03 2 15 . 7 ASN HD22 H 7.540 0.03 2 16 . 7 ASN C C 174.890 0.3 1 17 . 7 ASN CA C 53.020 0.3 1 18 . 7 ASN CB C 38.980 0.3 1 19 . 7 ASN ND2 N 112.480 0.3 1 20 . 8 SER H H 8.110 0.03 1 21 . 8 SER HA H 4.380 0.03 1 22 . 8 SER HB2 H 3.670 0.03 2 23 . 8 SER HB3 H 3.760 0.03 2 24 . 8 SER C C 174.540 0.3 1 25 . 8 SER CA C 58.050 0.3 1 26 . 8 SER CB C 63.720 0.3 1 27 . 8 SER N N 115.300 0.3 1 28 . 9 PHE H H 8.710 0.03 1 29 . 9 PHE HA H 4.630 0.03 1 30 . 9 PHE HB2 H 2.690 0.03 2 31 . 9 PHE HB3 H 3.210 0.03 2 32 . 9 PHE HD1 H 7.140 0.03 1 33 . 9 PHE HD2 H 7.140 0.03 1 34 . 9 PHE HE1 H 7.280 0.03 1 35 . 9 PHE HE2 H 7.280 0.03 1 36 . 9 PHE HZ H 7.220 0.03 1 37 . 9 PHE C C 175.090 0.3 1 38 . 9 PHE CA C 57.320 0.3 1 39 . 9 PHE CB C 39.070 0.3 1 40 . 9 PHE CD1 C 131.120 0.3 1 41 . 9 PHE CD2 C 131.120 0.3 1 42 . 9 PHE CE1 C 131.120 0.3 1 43 . 9 PHE CE2 C 131.120 0.3 1 44 . 9 PHE CZ C 128.830 0.3 1 45 . 9 PHE N N 121.300 0.3 1 46 . 10 VAL H H 7.650 0.03 1 47 . 10 VAL HA H 3.250 0.03 1 48 . 10 VAL HB H 1.970 0.03 1 49 . 10 VAL HG1 H 0.850 0.03 1 50 . 10 VAL HG2 H 1.010 0.03 1 51 . 10 VAL C C 176.970 0.3 1 52 . 10 VAL CA C 65.560 0.3 1 53 . 10 VAL CB C 30.750 0.3 1 54 . 10 VAL CG1 C 22.890 0.3 2 55 . 10 VAL CG2 C 21.460 0.3 2 56 . 10 VAL N N 117.940 0.3 1 57 . 11 GLY H H 8.920 0.03 1 58 . 11 GLY HA2 H 3.600 0.03 2 59 . 11 GLY HA3 H 4.400 0.03 2 60 . 11 GLY C C 174.030 0.3 1 61 . 11 GLY CA C 44.460 0.3 1 62 . 11 GLY N N 115.950 0.3 1 63 . 12 LEU H H 7.600 0.03 1 64 . 12 LEU HA H 4.250 0.03 1 65 . 12 LEU HB2 H 1.460 0.03 2 66 . 12 LEU HB3 H 1.730 0.03 2 67 . 12 LEU HG H 1.460 0.03 1 68 . 12 LEU HD1 H 0.560 0.03 1 69 . 12 LEU HD2 H 0.140 0.03 1 70 . 12 LEU C C 176.650 0.3 1 71 . 12 LEU CA C 55.040 0.3 1 72 . 12 LEU CB C 41.560 0.3 1 73 . 12 LEU CG C 26.200 0.3 1 74 . 12 LEU CD1 C 22.950 0.3 2 75 . 12 LEU CD2 C 25.900 0.3 2 76 . 12 LEU N N 119.960 0.3 1 77 . 13 ARG H H 8.250 0.03 1 78 . 13 ARG HB2 H 1.740 0.03 2 79 . 13 ARG HB3 H 1.850 0.03 2 80 . 13 ARG C C 175.230 0.3 1 81 . 13 ARG CA C 56.760 0.3 1 82 . 13 ARG CB C 29.970 0.3 1 83 . 13 ARG N N 120.560 0.3 1 84 . 14 VAL H H 8.330 0.03 1 85 . 14 VAL HA H 4.940 0.03 1 86 . 14 VAL HB H 2.290 0.03 1 87 . 14 VAL HG1 H 0.360 0.03 1 88 . 14 VAL HG2 H 0.660 0.03 1 89 . 14 VAL C C 175.980 0.3 1 90 . 14 VAL CA C 58.280 0.3 1 91 . 14 VAL CB C 36.350 0.3 1 92 . 14 VAL CG1 C 18.200 0.3 2 93 . 14 VAL CG2 C 22.700 0.3 2 94 . 14 VAL N N 110.360 0.3 1 95 . 15 VAL H H 8.590 0.03 1 96 . 15 VAL HA H 5.190 0.03 1 97 . 15 VAL HB H 1.870 0.03 1 98 . 15 VAL HG1 H 0.820 0.03 1 99 . 15 VAL HG2 H 0.840 0.03 1 100 . 15 VAL C C 174.980 0.3 1 101 . 15 VAL CA C 60.760 0.3 1 102 . 15 VAL CB C 33.510 0.3 1 103 . 15 VAL CG1 C 21.150 0.3 1 104 . 15 VAL CG2 C 21.150 0.3 1 105 . 15 VAL N N 114.830 0.3 1 106 . 16 ALA H H 9.930 0.03 1 107 . 16 ALA HA H 5.880 0.03 1 108 . 16 ALA HB H 1.500 0.03 1 109 . 16 ALA C C 174.970 0.3 1 110 . 16 ALA CA C 51.430 0.3 1 111 . 16 ALA CB C 24.900 0.3 1 112 . 16 ALA N N 125.620 0.3 1 113 . 17 LYS H H 8.090 0.03 1 114 . 17 LYS HA H 4.770 0.03 1 115 . 17 LYS HB2 H 0.930 0.03 2 116 . 17 LYS HB3 H 0.460 0.03 2 117 . 17 LYS HE2 H 2.730 0.03 9 118 . 17 LYS HE3 H 2.610 0.03 9 119 . 17 LYS C C 179.000 0.3 1 120 . 17 LYS CA C 54.740 0.3 1 121 . 17 LYS CB C 34.400 0.3 1 122 . 17 LYS CE C 41.700 0.3 9 123 . 17 LYS N N 122.740 0.3 1 124 . 18 TRP HA H 5.000 0.03 1 125 . 18 TRP HB2 H 2.970 0.03 2 126 . 18 TRP HB3 H 3.670 0.03 2 127 . 18 TRP HD1 H 6.450 0.03 1 128 . 18 TRP HE1 H 9.160 0.03 1 129 . 18 TRP HE3 H 7.290 0.03 1 130 . 18 TRP HZ2 H 6.940 0.03 1 131 . 18 TRP HZ3 H 6.740 0.03 1 132 . 18 TRP HH2 H 6.740 0.03 1 133 . 18 TRP C C 175.720 0.3 1 134 . 18 TRP CA C 55.600 0.3 1 135 . 18 TRP CB C 30.900 0.3 1 136 . 18 TRP CD1 C 127.240 0.3 1 137 . 18 TRP CE3 C 121.230 0.3 1 138 . 18 TRP CZ2 C 113.940 0.3 1 139 . 18 TRP CZ3 C 121.230 0.3 1 140 . 18 TRP NE1 N 129.100 0.3 1 141 . 19 SER H H 7.780 0.03 1 142 . 19 SER HA H 4.580 0.03 1 143 . 19 SER HB2 H 3.190 0.03 2 144 . 19 SER HB3 H 3.510 0.03 2 145 . 19 SER CA C 57.060 0.3 1 146 . 19 SER CB C 64.570 0.3 1 147 . 19 SER N N 117.010 0.3 1 148 . 21 ASN HA H 4.780 0.03 1 149 . 21 ASN HB2 H 2.770 0.03 1 150 . 21 ASN HB3 H 2.770 0.03 1 151 . 21 ASN HD21 H 7.390 0.03 2 152 . 21 ASN HD22 H 6.820 0.03 2 153 . 21 ASN C C 175.110 0.3 1 154 . 21 ASN CA C 52.250 0.3 1 155 . 21 ASN CB C 38.500 0.3 1 156 . 21 ASN ND2 N 111.000 0.3 1 157 . 22 GLY H H 7.440 0.03 1 158 . 22 GLY HA2 H 3.600 0.03 2 159 . 22 GLY HA3 H 3.740 0.03 2 160 . 22 GLY C C 170.820 0.3 1 161 . 22 GLY CA C 45.130 0.3 1 162 . 22 GLY N N 107.690 0.3 1 163 . 23 TYR H H 7.270 0.03 1 164 . 23 TYR HA H 4.620 0.03 1 165 . 23 TYR HB2 H 2.250 0.03 2 166 . 23 TYR HB3 H 2.500 0.03 2 167 . 23 TYR HD1 H 6.800 0.03 1 168 . 23 TYR HD2 H 6.800 0.03 1 169 . 23 TYR HE1 H 6.530 0.03 1 170 . 23 TYR HE2 H 6.530 0.03 1 171 . 23 TYR C C 175.000 0.3 1 172 . 23 TYR CA C 56.890 0.3 1 173 . 23 TYR CB C 39.730 0.3 1 174 . 23 TYR CD1 C 132.770 0.3 1 175 . 23 TYR CD2 C 132.770 0.3 1 176 . 23 TYR CE1 C 117.000 0.3 1 177 . 23 TYR CE2 C 117.000 0.3 1 178 . 23 TYR N N 113.650 0.3 1 179 . 24 PHE H H 9.640 0.03 1 180 . 24 PHE HA H 4.580 0.03 1 181 . 24 PHE HB2 H 2.540 0.03 9 182 . 24 PHE HB3 H 3.010 0.03 9 183 . 24 PHE HD1 H 7.160 0.03 1 184 . 24 PHE HD2 H 7.160 0.03 1 185 . 24 PHE HE1 H 7.300 0.03 1 186 . 24 PHE HE2 H 7.300 0.03 1 187 . 24 PHE HZ H 7.250 0.03 1 188 . 24 PHE C C 175.000 0.3 1 189 . 24 PHE CA C 56.760 0.3 1 190 . 24 PHE CB C 39.680 0.3 9 191 . 24 PHE CD1 C 131.100 0.3 1 192 . 24 PHE CD2 C 131.100 0.3 1 193 . 24 PHE CE1 C 131.100 0.3 1 194 . 24 PHE CE2 C 131.100 0.3 1 195 . 24 PHE CZ C 129.400 0.3 1 196 . 24 PHE N N 116.730 0.3 1 197 . 25 TYR H H 9.100 0.03 1 198 . 25 TYR HA H 5.080 0.03 1 199 . 25 TYR HB2 H 3.030 0.03 2 200 . 25 TYR HB3 H 3.450 0.03 2 201 . 25 TYR HD1 H 7.160 0.03 1 202 . 25 TYR HD2 H 7.160 0.03 1 203 . 25 TYR HE1 H 6.570 0.03 1 204 . 25 TYR HE2 H 6.570 0.03 1 205 . 25 TYR C C 176.380 0.3 1 206 . 25 TYR CA C 56.520 0.3 1 207 . 25 TYR CB C 43.650 0.3 1 208 . 25 TYR CD1 C 134.200 0.3 1 209 . 25 TYR CD2 C 134.200 0.3 1 210 . 25 TYR CE1 C 117.600 0.3 1 211 . 25 TYR CE2 C 117.600 0.3 1 212 . 25 TYR N N 119.780 0.3 1 213 . 26 SER H H 9.560 0.03 1 214 . 26 SER HA H 4.960 0.03 1 215 . 26 SER HB2 H 4.160 0.03 2 216 . 26 SER HB3 H 4.420 0.03 2 217 . 26 SER C C 175.900 0.3 1 218 . 26 SER CA C 59.130 0.3 1 219 . 26 SER CB C 63.600 0.3 9 220 . 26 SER N N 115.600 0.3 1 221 . 27 GLY H H 8.540 0.03 1 222 . 27 GLY HA2 H 4.480 0.03 1 223 . 27 GLY HA3 H 3.650 0.03 1 224 . 27 GLY C C 170.410 0.3 1 225 . 27 GLY CA C 46.710 0.3 1 226 . 27 GLY N N 111.320 0.3 1 227 . 28 LYS H H 8.230 0.03 1 228 . 28 LYS HA H 5.280 0.03 1 229 . 28 LYS HB2 H 1.500 0.03 2 230 . 28 LYS HB3 H 1.450 0.03 2 231 . 28 LYS HG2 H 1.200 0.03 1 232 . 28 LYS HG3 H 1.200 0.03 1 233 . 28 LYS HD2 H 1.550 0.03 1 234 . 28 LYS HD3 H 1.550 0.03 1 235 . 28 LYS HE2 H 2.820 0.03 1 236 . 28 LYS HE3 H 2.820 0.03 1 237 . 28 LYS C C 174.890 0.3 1 238 . 28 LYS CA C 54.230 0.3 1 239 . 28 LYS CB C 36.500 0.3 1 240 . 28 LYS CG C 24.500 0.3 1 241 . 28 LYS CD C 29.300 0.3 1 242 . 28 LYS CE C 41.200 0.3 1 243 . 28 LYS N N 119.440 0.3 1 244 . 29 ILE H H 8.250 0.03 1 245 . 29 ILE HA H 4.370 0.03 9 246 . 29 ILE C C 175.930 0.3 1 247 . 29 ILE CA C 62.300 0.3 1 248 . 29 ILE CB C 32.910 0.3 1 249 . 29 ILE N N 122.680 0.3 1 250 . 30 THR H H 8.260 0.03 1 251 . 30 THR HA H 4.630 0.03 1 252 . 30 THR HB H 4.220 0.03 1 253 . 30 THR HG2 H 1.220 0.03 1 254 . 30 THR C C 172.500 0.3 1 255 . 30 THR CA C 59.630 0.3 1 256 . 30 THR CB C 69.570 0.3 1 257 . 30 THR CG2 C 21.000 0.3 1 258 . 30 THR N N 120.270 0.3 1 259 . 31 ARG H H 7.640 0.03 1 260 . 31 ARG HA H 4.410 0.03 1 261 . 31 ARG HB2 H 1.620 0.03 2 262 . 31 ARG HB3 H 1.840 0.03 2 263 . 31 ARG HG2 H 1.480 0.03 2 264 . 31 ARG HD2 H 3.110 0.03 2 265 . 31 ARG C C 173.550 0.3 1 266 . 31 ARG CA C 56.640 0.3 1 267 . 31 ARG CB C 34.330 0.3 1 268 . 31 ARG CG C 27.200 0.3 1 269 . 31 ARG CD C 43.600 0.3 1 270 . 31 ARG N N 119.100 0.3 1 271 . 32 ASP H H 9.010 0.03 1 272 . 32 ASP HA H 4.680 0.03 1 273 . 32 ASP HB2 H 2.960 0.03 2 274 . 32 ASP HB3 H 2.530 0.03 2 275 . 32 ASP C C 176.250 0.3 1 276 . 32 ASP CA C 53.520 0.3 1 277 . 32 ASP CB C 40.690 0.3 1 278 . 32 ASP N N 125.790 0.3 1 279 . 33 VAL H H 7.430 0.03 1 280 . 33 VAL HA H 4.100 0.03 1 281 . 33 VAL HB H 2.040 0.03 1 282 . 33 VAL HG1 H 0.620 0.03 1 283 . 33 VAL HG2 H 0.820 0.03 1 284 . 33 VAL C C 175.690 0.3 1 285 . 33 VAL CA C 62.100 0.3 1 286 . 33 VAL CB C 31.200 0.3 1 287 . 33 VAL CG1 C 20.400 0.3 2 288 . 33 VAL CG2 C 21.900 0.3 2 289 . 33 VAL N N 120.530 0.3 1 290 . 34 GLY H H 7.890 0.03 1 291 . 34 GLY HA2 H 4.270 0.03 2 292 . 34 GLY HA3 H 3.700 0.03 2 293 . 34 GLY C C 173.640 0.3 1 294 . 34 GLY CA C 44.300 0.3 1 295 . 34 GLY N N 110.400 0.3 1 296 . 35 ALA H H 8.610 0.03 1 297 . 35 ALA HA H 3.890 0.03 1 298 . 35 ALA HB H 1.320 0.03 1 299 . 35 ALA C C 177.160 0.3 1 300 . 35 ALA CA C 52.640 0.3 1 301 . 35 ALA CB C 16.680 0.3 1 302 . 35 ALA N N 119.930 0.3 1 303 . 36 GLY H H 8.290 0.03 1 304 . 36 GLY HA2 H 3.630 0.03 2 305 . 36 GLY HA3 H 4.090 0.03 2 306 . 36 GLY C C 173.160 0.3 1 307 . 36 GLY CA C 45.720 0.3 1 308 . 36 GLY N N 104.800 0.3 1 309 . 37 LYS H H 7.370 0.03 1 310 . 37 LYS HA H 4.920 0.03 1 311 . 37 LYS HB2 H 1.410 0.03 2 312 . 37 LYS HB3 H 1.620 0.03 2 313 . 37 LYS HG2 H 1.320 0.03 2 314 . 37 LYS HG3 H 1.150 0.03 2 315 . 37 LYS HD2 H 1.560 0.03 1 316 . 37 LYS HD3 H 1.560 0.03 1 317 . 37 LYS HE2 H 2.820 0.03 2 318 . 37 LYS HE3 H 2.880 0.03 2 319 . 37 LYS C C 174.100 0.3 1 320 . 37 LYS CA C 55.230 0.3 1 321 . 37 LYS CB C 35.360 0.3 1 322 . 37 LYS CG C 25.600 0.3 1 323 . 37 LYS CD C 29.300 0.3 1 324 . 37 LYS N N 119.360 0.3 1 325 . 38 TYR H H 8.840 0.03 1 326 . 38 TYR HA H 4.790 0.03 1 327 . 38 TYR HB2 H 2.370 0.03 2 328 . 38 TYR HB3 H 2.940 0.03 2 329 . 38 TYR HD1 H 6.860 0.03 1 330 . 38 TYR HD2 H 6.860 0.03 1 331 . 38 TYR HE1 H 6.610 0.03 1 332 . 38 TYR HE2 H 6.610 0.03 1 333 . 38 TYR C C 173.660 0.3 1 334 . 38 TYR CA C 57.290 0.3 1 335 . 38 TYR CB C 42.150 0.3 1 336 . 38 TYR CD1 C 132.770 0.3 1 337 . 38 TYR CD2 C 132.770 0.3 1 338 . 38 TYR CE1 C 117.470 0.3 1 339 . 38 TYR CE2 C 117.470 0.3 1 340 . 38 TYR N N 119.330 0.3 1 341 . 39 LYS H H 9.060 0.03 1 342 . 39 LYS HA H 4.840 0.03 1 343 . 39 LYS HB2 H 1.490 0.03 2 344 . 39 LYS HB3 H 1.700 0.03 2 345 . 39 LYS HG2 H 1.240 0.03 1 346 . 39 LYS HG3 H 1.240 0.03 1 347 . 39 LYS HD2 H 1.370 0.03 2 348 . 39 LYS HD3 H 1.600 0.03 2 349 . 39 LYS HE2 H 2.690 0.03 2 350 . 39 LYS HE3 H 2.860 0.03 2 351 . 39 LYS C C 174.060 0.3 1 352 . 39 LYS CA C 56.030 0.3 1 353 . 39 LYS CB C 32.500 0.3 1 354 . 39 LYS CG C 23.600 0.3 1 355 . 39 LYS CD C 27.700 0.3 1 356 . 39 LYS CE C 40.160 0.3 1 357 . 39 LYS N N 123.620 0.3 1 358 . 40 LEU H H 9.090 0.03 1 359 . 40 LEU HA H 4.760 0.03 1 360 . 40 LEU HB2 H 1.010 0.03 2 361 . 40 LEU HB3 H 1.420 0.03 2 362 . 40 LEU HG H 1.270 0.03 1 363 . 40 LEU HD1 H 0.410 0.03 1 364 . 40 LEU HD2 H 0.180 0.03 1 365 . 40 LEU C C 174.950 0.3 1 366 . 40 LEU CA C 52.030 0.3 1 367 . 40 LEU CB C 44.700 0.3 1 368 . 40 LEU CG C 28.500 0.3 1 369 . 40 LEU CD1 C 24.500 0.3 2 370 . 40 LEU CD2 C 25.300 0.3 2 371 . 40 LEU N N 131.950 0.3 1 372 . 41 LEU H H 8.450 0.03 1 373 . 41 LEU HA H 4.800 0.03 1 374 . 41 LEU HB2 H 1.400 0.03 2 375 . 41 LEU HB3 H 1.620 0.03 2 376 . 41 LEU HG H 0.840 0.03 1 377 . 41 LEU C C 177.220 0.3 1 378 . 41 LEU CA C 53.300 0.3 1 379 . 41 LEU CB C 43.780 0.3 1 380 . 41 LEU CG C 23.200 0.3 1 381 . 41 LEU N N 121.410 0.3 1 382 . 42 PHE H H 9.710 0.03 1 383 . 42 PHE HA H 4.830 0.03 1 384 . 42 PHE HB2 H 3.370 0.03 2 385 . 42 PHE HB3 H 3.500 0.03 2 386 . 42 PHE HD1 H 7.340 0.03 1 387 . 42 PHE HD2 H 7.340 0.03 1 388 . 42 PHE HE1 H 7.600 0.03 1 389 . 42 PHE HE2 H 7.600 0.03 1 390 . 42 PHE HZ H 7.090 0.03 1 391 . 42 PHE C C 178.120 0.3 1 392 . 42 PHE CA C 59.950 0.3 1 393 . 42 PHE CB C 39.670 0.3 1 394 . 42 PHE CD1 C 132.060 0.3 1 395 . 42 PHE CD2 C 132.060 0.3 1 396 . 42 PHE CE1 C 132.060 0.3 1 397 . 42 PHE CE2 C 132.060 0.3 1 398 . 42 PHE CZ C 128.770 0.3 1 399 . 42 PHE N N 128.810 0.3 1 400 . 43 ASP H H 8.790 0.03 1 401 . 43 ASP HA H 4.560 0.03 1 402 . 43 ASP HB2 H 2.980 0.03 2 403 . 43 ASP HB3 H 2.940 0.03 2 404 . 43 ASP C C 176.080 0.3 1 405 . 43 ASP CA C 57.430 0.3 1 406 . 43 ASP CB C 40.160 0.3 1 407 . 43 ASP N N 122.040 0.3 1 408 . 44 ASP H H 8.390 0.03 1 409 . 44 ASP HA H 4.570 0.03 1 410 . 44 ASP HB2 H 2.990 0.03 2 411 . 44 ASP HB3 H 2.640 0.03 2 412 . 44 ASP C C 176.890 0.3 1 413 . 44 ASP CA C 53.820 0.3 1 414 . 44 ASP CB C 40.280 0.3 1 415 . 44 ASP N N 116.730 0.3 1 416 . 45 GLY H H 8.430 0.03 1 417 . 45 GLY HA2 H 3.610 0.03 2 418 . 45 GLY HA3 H 4.390 0.03 2 419 . 45 GLY C C 173.590 0.3 1 420 . 45 GLY CA C 44.900 0.3 1 421 . 45 GLY N N 108.540 0.3 1 422 . 46 TYR H H 7.800 0.03 1 423 . 46 TYR HA H 4.490 0.03 1 424 . 46 TYR HB2 H 2.780 0.03 2 425 . 46 TYR HB3 H 2.910 0.03 2 426 . 46 TYR HD1 H 6.570 0.03 1 427 . 46 TYR HD2 H 6.570 0.03 1 428 . 46 TYR HE1 H 6.130 0.03 1 429 . 46 TYR HE2 H 6.130 0.03 1 430 . 46 TYR C C 173.110 0.3 1 431 . 46 TYR CA C 57.820 0.3 1 432 . 46 TYR CB C 38.800 0.3 1 433 . 46 TYR CD1 C 132.100 0.3 1 434 . 46 TYR CD2 C 132.100 0.3 1 435 . 46 TYR CE1 C 117.700 0.3 1 436 . 46 TYR CE2 C 117.700 0.3 1 437 . 46 TYR N N 122.310 0.3 1 438 . 47 GLU H H 7.510 0.03 1 439 . 47 GLU HA H 5.620 0.03 1 440 . 47 GLU HB2 H 1.760 0.03 2 441 . 47 GLU HB3 H 1.820 0.03 2 442 . 47 GLU HG2 H 1.920 0.03 2 443 . 47 GLU HG3 H 2.110 0.03 2 444 . 47 GLU C C 174.970 0.3 1 445 . 47 GLU CA C 53.840 0.3 1 446 . 47 GLU CB C 33.560 0.3 1 447 . 47 GLU CG C 37.200 0.3 1 448 . 47 GLU N N 126.210 0.3 1 449 . 48 CYS H H 8.490 0.03 1 450 . 48 CYS HA H 4.620 0.03 1 451 . 48 CYS HB2 H 2.630 0.03 2 452 . 48 CYS HB3 H 2.900 0.03 2 453 . 48 CYS C C 171.370 0.3 1 454 . 48 CYS CA C 56.730 0.3 1 455 . 48 CYS CB C 30.250 0.3 1 456 . 48 CYS N N 118.650 0.3 1 457 . 49 ASP H H 8.410 0.03 1 458 . 49 ASP HA H 5.560 0.03 1 459 . 49 ASP HB2 H 2.190 0.03 2 460 . 49 ASP HB3 H 2.590 0.03 2 461 . 49 ASP C C 176.400 0.3 1 462 . 49 ASP CA C 53.560 0.3 1 463 . 49 ASP CB C 40.910 0.3 1 464 . 49 ASP N N 121.690 0.3 1 465 . 50 VAL H H 9.600 0.03 1 466 . 50 VAL HA H 4.560 0.03 1 467 . 50 VAL HB H 2.040 0.03 1 468 . 50 VAL HG1 H 1.270 0.03 1 469 . 50 VAL HG2 H 1.070 0.03 1 470 . 50 VAL C C 174.950 0.3 1 471 . 50 VAL CA C 60.790 0.3 1 472 . 50 VAL CB C 36.080 0.3 1 473 . 50 VAL CG1 C 22.600 0.3 1 474 . 50 VAL CG2 C 22.600 0.3 1 475 . 50 VAL N N 122.470 0.3 1 476 . 51 LEU H H 9.000 0.03 1 477 . 51 LEU HA H 4.730 0.03 1 478 . 51 LEU HB2 H 1.750 0.03 2 479 . 51 LEU HB3 H 1.860 0.03 2 480 . 51 LEU HG H 1.860 0.03 1 481 . 51 LEU HD1 H 0.960 0.03 1 482 . 51 LEU HD2 H 1.010 0.03 1 483 . 51 LEU C C 179.070 0.3 1 484 . 51 LEU CA C 55.090 0.3 1 485 . 51 LEU CB C 42.960 0.3 1 486 . 51 LEU CG C 27.300 0.3 1 487 . 51 LEU CD1 C 23.600 0.3 2 488 . 51 LEU CD2 C 25.500 0.3 2 489 . 51 LEU N N 125.120 0.3 1 490 . 52 GLY H H 9.000 0.03 1 491 . 52 GLY HA2 H 3.780 0.03 2 492 . 52 GLY HA3 H 4.170 0.03 2 493 . 52 GLY C C 175.010 0.3 1 494 . 52 GLY CA C 48.110 0.3 1 495 . 52 GLY N N 108.480 0.3 1 496 . 53 LYS H H 7.930 0.03 1 497 . 53 LYS HA H 4.310 0.03 1 498 . 53 LYS HB2 H 1.750 0.03 2 499 . 53 LYS HB3 H 1.830 0.03 2 500 . 53 LYS HD2 H 1.630 0.03 1 501 . 53 LYS HD3 H 1.630 0.03 1 502 . 53 LYS HE2 H 3.150 0.03 1 503 . 53 LYS HE3 H 3.150 0.03 1 504 . 53 LYS C C 175.900 0.3 1 505 . 53 LYS CA C 57.700 0.3 1 506 . 53 LYS CB C 31.460 0.3 1 507 . 53 LYS CD C 27.200 0.3 1 508 . 53 LYS CE C 43.600 0.3 1 509 . 53 LYS N N 115.040 0.3 1 510 . 54 ASP H H 8.140 0.03 1 511 . 54 ASP HA H 5.050 0.03 1 512 . 54 ASP HB2 H 2.870 0.03 2 513 . 54 ASP HB3 H 3.380 0.03 2 514 . 54 ASP C C 173.270 0.3 1 515 . 54 ASP CA C 54.310 0.3 1 516 . 54 ASP CB C 42.100 0.3 1 517 . 54 ASP N N 120.780 0.3 1 518 . 55 ILE H H 7.550 0.03 1 519 . 55 ILE HA H 4.460 0.03 1 520 . 55 ILE HB H 1.870 0.03 1 521 . 55 ILE HD1 H 0.650 0.03 1 522 . 55 ILE C C 174.210 0.3 1 523 . 55 ILE CA C 61.640 0.3 1 524 . 55 ILE CB C 40.080 0.3 1 525 . 55 ILE CD1 C 18.500 0.3 1 526 . 55 ILE N N 117.690 0.3 1 527 . 56 LEU H H 9.160 0.03 1 528 . 56 LEU HA H 4.790 0.03 1 529 . 56 LEU HB2 H 1.010 0.03 2 530 . 56 LEU HB3 H 1.960 0.03 2 531 . 56 LEU C C 176.880 0.3 1 532 . 56 LEU CA C 52.660 0.3 1 533 . 56 LEU CB C 43.600 0.3 1 534 . 56 LEU N N 124.350 0.3 1 535 . 57 LEU H H 9.360 0.03 1 536 . 57 LEU HA H 4.420 0.03 1 537 . 57 LEU HB2 H 1.870 0.03 2 538 . 57 LEU HB3 H 1.640 0.03 2 539 . 57 LEU HG H 1.540 0.03 1 540 . 57 LEU HD1 H 0.680 0.03 1 541 . 57 LEU HD2 H 0.770 0.03 1 542 . 57 LEU C C 175.610 0.3 1 543 . 57 LEU CA C 53.890 0.3 1 544 . 57 LEU CB C 40.300 0.3 1 545 . 57 LEU CG C 26.800 0.3 1 546 . 57 LEU CD1 C 24.200 0.3 2 547 . 57 LEU CD2 C 25.500 0.3 2 548 . 57 LEU N N 126.090 0.3 1 549 . 58 CYS H H 7.410 0.03 1 550 . 58 CYS HA H 4.240 0.03 1 551 . 58 CYS HB2 H 1.830 0.03 2 552 . 58 CYS HB3 H 2.180 0.03 2 553 . 58 CYS C C 172.410 0.3 1 554 . 58 CYS CA C 55.400 0.3 1 555 . 58 CYS CB C 28.420 0.3 1 556 . 58 CYS N N 118.350 0.3 1 557 . 59 ASP H H 8.110 0.03 1 558 . 59 ASP HA H 4.480 0.03 1 559 . 59 ASP HB2 H 2.590 0.03 9 560 . 59 ASP HB3 H 2.850 0.03 9 561 . 59 ASP C C 177.560 0.3 1 562 . 59 ASP CA C 55.490 0.3 1 563 . 59 ASP CB C 42.050 0.3 9 564 . 59 ASP N N 121.700 0.3 1 565 . 60 PRO HA H 4.610 0.03 1 566 . 60 PRO HB2 H 1.780 0.03 2 567 . 60 PRO HB3 H 1.940 0.03 2 568 . 60 PRO HG2 H 1.090 0.03 1 569 . 60 PRO HG3 H 1.090 0.03 1 570 . 60 PRO HD2 H 3.270 0.03 1 571 . 60 PRO HD3 H 3.270 0.03 1 572 . 60 PRO C C 175.760 0.3 1 573 . 60 PRO CA C 62.690 0.3 1 574 . 60 PRO CB C 34.910 0.3 1 575 . 60 PRO CG C 24.000 0.3 1 576 . 60 PRO CD C 49.500 0.3 1 577 . 61 ILE H H 8.980 0.03 1 578 . 61 ILE HA H 3.850 0.03 1 579 . 61 ILE HB H 1.550 0.03 1 580 . 61 ILE HG12 H 0.500 0.03 1 581 . 61 ILE HG13 H 0.500 0.03 1 582 . 61 ILE HG2 H 0.790 0.03 1 583 . 61 ILE HD1 H 0.660 0.03 1 584 . 61 ILE C C 174.400 0.3 1 585 . 61 ILE CA C 60.980 0.3 1 586 . 61 ILE CB C 38.500 0.3 1 587 . 61 ILE CG2 C 17.800 0.3 1 588 . 61 ILE CD1 C 18.500 0.3 1 589 . 61 ILE N N 121.810 0.3 1 590 . 62 PRO HA H 4.470 0.03 1 591 . 62 PRO HB2 H 1.910 0.03 2 592 . 62 PRO HB3 H 2.390 0.03 2 593 . 62 PRO HG2 H 1.800 0.03 2 594 . 62 PRO HG3 H 1.910 0.03 2 595 . 62 PRO HD2 H 3.510 0.03 2 596 . 62 PRO HD3 H 3.570 0.03 2 597 . 62 PRO C C 177.980 0.3 1 598 . 62 PRO CA C 62.690 0.3 1 599 . 62 PRO CB C 32.930 0.3 1 600 . 62 PRO CG C 24.700 0.3 1 601 . 62 PRO CD C 50.000 0.3 1 602 . 63 LEU H H 8.450 0.03 1 603 . 63 LEU HA H 3.710 0.03 1 604 . 63 LEU HB2 H 1.460 0.03 2 605 . 63 LEU HB3 H 1.670 0.03 2 606 . 63 LEU HG H 1.720 0.03 1 607 . 63 LEU HD1 H 0.620 0.03 1 608 . 63 LEU HD2 H 0.910 0.03 1 609 . 63 LEU C C 176.370 0.3 1 610 . 63 LEU CA C 56.340 0.3 1 611 . 63 LEU CB C 42.260 0.3 1 612 . 63 LEU CG C 27.000 0.3 1 613 . 63 LEU CD1 C 23.100 0.3 2 614 . 63 LEU CD2 C 25.000 0.3 2 615 . 63 LEU N N 119.880 0.3 1 616 . 64 ASP H H 9.350 0.03 1 617 . 64 ASP HA H 4.210 0.03 1 618 . 64 ASP HB2 H 2.850 0.03 2 619 . 64 ASP HB3 H 2.960 0.03 2 620 . 64 ASP C C 174.990 0.3 1 621 . 64 ASP CA C 56.480 0.3 1 622 . 64 ASP CB C 37.810 0.3 1 623 . 64 ASP N N 115.230 0.3 1 624 . 65 THR H H 7.290 0.03 1 625 . 65 THR HA H 4.130 0.03 1 626 . 65 THR HB H 3.620 0.03 1 627 . 65 THR HG2 H 1.070 0.03 1 628 . 65 THR C C 173.600 0.3 1 629 . 65 THR CA C 63.430 0.3 1 630 . 65 THR CB C 69.280 0.3 1 631 . 65 THR CG2 C 22.500 0.3 1 632 . 65 THR N N 115.420 0.3 1 633 . 66 GLU H H 8.580 0.03 1 634 . 66 GLU HA H 4.740 0.03 1 635 . 66 GLU HB2 H 1.960 0.03 1 636 . 66 GLU HB3 H 1.960 0.03 1 637 . 66 GLU HG2 H 2.200 0.03 2 638 . 66 GLU HG3 H 2.290 0.03 2 639 . 66 GLU C C 174.530 0.3 1 640 . 66 GLU CA C 56.530 0.3 1 641 . 66 GLU CB C 30.000 0.3 1 642 . 66 GLU CG C 36.700 0.3 1 643 . 66 GLU N N 128.080 0.3 1 644 . 67 VAL H H 8.800 0.03 1 645 . 67 VAL HA H 4.670 0.03 1 646 . 67 VAL HB H 2.060 0.03 1 647 . 67 VAL HG1 H 0.300 0.03 1 648 . 67 VAL HG2 H 0.460 0.03 1 649 . 67 VAL C C 174.530 0.3 1 650 . 67 VAL CA C 58.580 0.3 1 651 . 67 VAL CB C 34.940 0.3 1 652 . 67 VAL CG1 C 18.100 0.3 2 653 . 67 VAL CG2 C 22.000 0.3 2 654 . 67 VAL N N 117.570 0.3 1 655 . 68 THR H H 8.840 0.03 1 656 . 68 THR HA H 4.690 0.03 1 657 . 68 THR HB H 3.810 0.03 1 658 . 68 THR HG2 H 0.920 0.03 1 659 . 68 THR C C 170.790 0.3 1 660 . 68 THR CA C 62.700 0.3 1 661 . 68 THR CB C 71.530 0.3 1 662 . 68 THR CG2 C 21.000 0.3 1 663 . 68 THR N N 117.280 0.3 1 664 . 69 ALA H H 8.750 0.03 1 665 . 69 ALA HA H 4.980 0.03 1 666 . 69 ALA HB H 0.410 0.03 1 667 . 69 ALA C C 176.240 0.3 1 668 . 69 ALA CA C 49.770 0.3 1 669 . 69 ALA CB C 19.840 0.3 1 670 . 69 ALA N N 128.070 0.3 1 671 . 70 LEU H H 8.960 0.03 1 672 . 70 LEU HA H 4.610 0.03 1 673 . 70 LEU HB2 H 1.470 0.03 2 674 . 70 LEU HB3 H 1.570 0.03 2 675 . 70 LEU HG H 1.360 0.03 1 676 . 70 LEU HD1 H 0.520 0.03 1 677 . 70 LEU HD2 H 0.560 0.03 1 678 . 70 LEU C C 176.220 0.3 1 679 . 70 LEU CA C 54.350 0.3 1 680 . 70 LEU CB C 43.070 0.3 1 681 . 70 LEU CG C 27.000 0.3 1 682 . 70 LEU CD1 C 24.200 0.3 1 683 . 70 LEU CD2 C 24.200 0.3 1 684 . 70 LEU N N 125.060 0.3 1 685 . 71 SER H H 8.460 0.03 1 686 . 71 SER HA H 4.780 0.03 1 687 . 71 SER HB2 H 4.000 0.03 2 688 . 71 SER HB3 H 4.150 0.03 2 689 . 71 SER C C 174.550 0.3 1 690 . 71 SER CA C 57.180 0.3 1 691 . 71 SER CB C 64.900 0.3 1 692 . 71 SER N N 117.740 0.3 1 693 . 72 GLU HA H 4.040 0.03 1 694 . 72 GLU HB2 H 2.030 0.03 1 695 . 72 GLU HB3 H 2.030 0.03 1 696 . 72 GLU HG2 H 2.100 0.03 2 697 . 72 GLU HG3 H 2.130 0.03 2 698 . 72 GLU C C 174.690 0.3 1 699 . 72 GLU CA C 56.760 0.3 1 700 . 72 GLU CB C 29.630 0.3 1 701 . 72 GLU CG C 36.400 0.3 1 702 . 73 ASP H H 7.890 0.03 1 703 . 73 ASP HA H 4.660 0.03 1 704 . 73 ASP HB2 H 2.920 0.03 9 705 . 73 ASP HB3 H 2.820 0.03 9 706 . 73 ASP C C 175.020 0.3 1 707 . 73 ASP CA C 57.550 0.3 1 708 . 73 ASP CB C 38.630 0.3 1 709 . 73 ASP N N 119.550 0.3 1 710 . 74 GLU HA H 4.150 0.03 1 711 . 74 GLU HB2 H 2.060 0.03 2 712 . 74 GLU HB3 H 2.120 0.03 2 713 . 74 GLU HG2 H 2.360 0.03 1 714 . 74 GLU HG3 H 2.360 0.03 1 715 . 74 GLU C C 176.140 0.3 1 716 . 74 GLU CA C 58.510 0.3 1 717 . 74 GLU CB C 29.510 0.3 1 718 . 74 GLU CG C 36.100 0.3 1 719 . 75 TYR H H 8.290 0.03 1 720 . 75 TYR HA H 4.550 0.03 1 721 . 75 TYR HB2 H 2.730 0.03 1 722 . 75 TYR HB3 H 2.730 0.03 1 723 . 75 TYR HD1 H 7.050 0.03 1 724 . 75 TYR HD2 H 7.050 0.03 1 725 . 75 TYR HE1 H 6.780 0.03 1 726 . 75 TYR HE2 H 6.780 0.03 1 727 . 75 TYR C C 174.980 0.3 1 728 . 75 TYR CA C 54.220 0.3 1 729 . 75 TYR CB C 40.360 0.3 1 730 . 75 TYR CD1 C 133.470 0.3 1 731 . 75 TYR CD2 C 133.470 0.3 1 732 . 75 TYR CE1 C 117.700 0.3 1 733 . 75 TYR CE2 C 117.700 0.3 1 734 . 75 TYR N N 116.030 0.3 1 735 . 76 PHE H H 7.930 0.03 1 736 . 76 PHE HA H 4.050 0.03 1 737 . 76 PHE HB2 H 2.910 0.03 1 738 . 76 PHE HB3 H 2.910 0.03 1 739 . 76 PHE HD1 H 6.960 0.03 1 740 . 76 PHE HD2 H 6.960 0.03 1 741 . 76 PHE HE1 H 7.080 0.03 1 742 . 76 PHE HE2 H 7.080 0.03 1 743 . 76 PHE HZ H 7.160 0.03 1 744 . 76 PHE C C 175.130 0.3 1 745 . 76 PHE CA C 56.710 0.3 1 746 . 76 PHE CB C 40.240 0.3 1 747 . 76 PHE CD1 C 131.120 0.3 1 748 . 76 PHE CD2 C 131.120 0.3 1 749 . 76 PHE CE1 C 131.120 0.3 1 750 . 76 PHE CE2 C 131.120 0.3 1 751 . 76 PHE CZ C 129.470 0.3 1 752 . 76 PHE N N 115.530 0.3 1 753 . 77 SER H H 8.440 0.03 1 754 . 77 SER HA H 4.680 0.03 1 755 . 77 SER HB2 H 3.810 0.03 2 756 . 77 SER HB3 H 3.870 0.03 2 757 . 77 SER C C 172.820 0.3 1 758 . 77 SER CA C 57.490 0.3 1 759 . 77 SER CB C 64.650 0.3 1 760 . 77 SER N N 115.390 0.3 1 761 . 78 ALA H H 8.520 0.03 1 762 . 78 ALA HA H 5.160 0.03 1 763 . 78 ALA HB H 1.310 0.03 1 764 . 78 ALA C C 177.400 0.3 1 765 . 78 ALA CA C 51.570 0.3 1 766 . 78 ALA CB C 19.700 0.3 1 767 . 78 ALA N N 126.600 0.3 1 768 . 79 GLY H H 8.370 0.03 1 769 . 79 GLY HA2 H 4.370 0.03 2 770 . 79 GLY HA3 H 3.570 0.03 2 771 . 79 GLY C C 171.100 0.3 1 772 . 79 GLY CA C 44.990 0.3 1 773 . 79 GLY N N 106.080 0.3 1 774 . 80 VAL H H 8.260 0.03 1 775 . 80 VAL HA H 4.920 0.03 1 776 . 80 VAL HB H 1.740 0.03 1 777 . 80 VAL HG1 H 0.770 0.03 1 778 . 80 VAL HG2 H 0.880 0.03 1 779 . 80 VAL C C 176.240 0.3 1 780 . 80 VAL CA C 60.210 0.3 1 781 . 80 VAL CB C 35.700 0.3 1 782 . 80 VAL CG1 C 21.500 0.3 1 783 . 80 VAL CG2 C 21.500 0.3 1 784 . 80 VAL N N 117.530 0.3 1 785 . 81 VAL H H 8.400 0.03 1 786 . 81 VAL HA H 3.960 0.03 1 787 . 81 VAL HB H 2.190 0.03 1 788 . 81 VAL HG1 H 1.010 0.03 1 789 . 81 VAL HG2 H 0.770 0.03 1 790 . 81 VAL C C 176.420 0.3 1 791 . 81 VAL CA C 64.400 0.3 1 792 . 81 VAL CB C 32.400 0.3 1 793 . 81 VAL CG1 C 22.600 0.3 2 794 . 81 VAL CG2 C 22.800 0.3 2 795 . 81 VAL N N 125.820 0.3 1 796 . 82 LYS H H 9.470 0.03 1 797 . 82 LYS HA H 4.730 0.03 1 798 . 82 LYS HB2 H 1.900 0.03 2 799 . 82 LYS HB3 H 1.180 0.03 2 800 . 82 LYS C C 175.770 0.3 1 801 . 82 LYS CA C 52.940 0.3 1 802 . 82 LYS CB C 33.900 0.3 1 803 . 82 LYS N N 126.350 0.3 1 804 . 83 GLY H H 7.460 0.03 1 805 . 83 GLY HA2 H 4.060 0.03 1 806 . 83 GLY HA3 H 4.060 0.03 1 807 . 83 GLY C C 170.480 0.3 1 808 . 83 GLY CA C 45.520 0.3 1 809 . 83 GLY N N 106.650 0.3 1 810 . 84 HIS H H 8.590 0.03 1 811 . 84 HIS HA H 5.770 0.03 1 812 . 84 HIS HB2 H 2.890 0.03 2 813 . 84 HIS HB3 H 3.030 0.03 2 814 . 84 HIS HD2 H 7.100 0.03 1 815 . 84 HIS HE1 H 7.600 0.03 1 816 . 84 HIS C C 174.530 0.3 1 817 . 84 HIS CA C 55.620 0.3 1 818 . 84 HIS CB C 35.230 0.3 1 819 . 84 HIS CD2 C 117.940 0.3 1 820 . 84 HIS CE1 C 137.700 0.3 1 821 . 84 HIS N N 117.310 0.3 1 822 . 85 ARG H H 9.170 0.03 1 823 . 85 ARG HA H 4.660 0.03 1 824 . 85 ARG HB2 H 1.400 0.03 2 825 . 85 ARG HB3 H 1.580 0.03 2 826 . 85 ARG HG2 H 1.100 0.03 2 827 . 85 ARG HG3 H 0.970 0.03 2 828 . 85 ARG HD2 H 2.330 0.03 2 829 . 85 ARG HD3 H 1.920 0.03 2 830 . 85 ARG C C 173.090 0.3 1 831 . 85 ARG CA C 55.650 0.3 1 832 . 85 ARG CB C 33.620 0.3 1 833 . 85 ARG CG C 26.600 0.3 1 834 . 85 ARG CD C 42.700 0.3 1 835 . 85 ARG N N 120.540 0.3 1 836 . 86 LYS H H 8.710 0.03 1 837 . 86 LYS HA H 5.290 0.03 1 838 . 86 LYS HB2 H 1.640 0.03 2 839 . 86 LYS HB3 H 1.590 0.03 2 840 . 86 LYS HG2 H 1.190 0.03 2 841 . 86 LYS HG3 H 1.320 0.03 2 842 . 86 LYS HD2 H 1.570 0.03 1 843 . 86 LYS HD3 H 1.570 0.03 1 844 . 86 LYS HE2 H 2.810 0.03 1 845 . 86 LYS HE3 H 2.810 0.03 1 846 . 86 LYS C C 175.920 0.3 1 847 . 86 LYS CA C 54.860 0.3 1 848 . 86 LYS CB C 34.110 0.3 1 849 . 86 LYS CG C 25.400 0.3 1 850 . 86 LYS CD C 29.100 0.3 1 851 . 86 LYS CE C 42.100 0.3 9 852 . 86 LYS N N 124.020 0.3 1 853 . 87 GLU H H 8.780 0.03 1 854 . 87 GLU HA H 4.530 0.03 1 855 . 87 GLU HB2 H 1.930 0.03 2 856 . 87 GLU HB3 H 1.750 0.03 2 857 . 87 GLU HG2 H 2.040 0.03 1 858 . 87 GLU HG3 H 2.040 0.03 1 859 . 87 GLU C C 175.880 0.3 1 860 . 87 GLU CA C 55.460 0.3 1 861 . 87 GLU CB C 32.140 0.3 1 862 . 87 GLU CG C 35.700 0.3 1 863 . 87 GLU N N 123.650 0.3 1 864 . 89 GLY HA2 H 3.660 0.03 2 865 . 89 GLY HA3 H 4.170 0.03 2 866 . 89 GLY CA C 45.140 0.3 1 867 . 90 GLU H H 7.950 0.03 1 868 . 90 GLU HA H 4.600 0.03 1 869 . 90 GLU HB2 H 2.010 0.03 2 870 . 90 GLU HB3 H 1.970 0.03 2 871 . 90 GLU HG2 H 2.040 0.03 1 872 . 90 GLU HG3 H 2.040 0.03 1 873 . 90 GLU C C 174.050 0.3 1 874 . 90 GLU CA C 54.350 0.3 1 875 . 90 GLU CB C 32.160 0.3 1 876 . 90 GLU CG C 36.000 0.3 1 877 . 90 GLU N N 121.320 0.3 1 878 . 91 LEU H H 8.390 0.03 1 879 . 91 LEU HA H 4.870 0.03 1 880 . 91 LEU HB2 H 1.510 0.03 2 881 . 91 LEU HB3 H 1.350 0.03 2 882 . 91 LEU HG H 1.130 0.03 1 883 . 91 LEU HD1 H 0.490 0.03 1 884 . 91 LEU HD2 H 0.660 0.03 1 885 . 91 LEU C C 174.160 0.3 1 886 . 91 LEU CA C 54.500 0.3 1 887 . 91 LEU CB C 44.100 0.3 1 888 . 91 LEU CG C 27.100 0.3 1 889 . 91 LEU CD1 C 24.300 0.3 2 890 . 91 LEU CD2 C 26.600 0.3 2 891 . 91 LEU N N 125.600 0.3 1 892 . 92 TYR H H 9.290 0.03 1 893 . 92 TYR HA H 5.270 0.03 1 894 . 92 TYR HB2 H 2.710 0.03 2 895 . 92 TYR HB3 H 2.960 0.03 2 896 . 92 TYR HD1 H 6.890 0.03 1 897 . 92 TYR HD2 H 6.890 0.03 1 898 . 92 TYR HE1 H 6.740 0.03 1 899 . 92 TYR HE2 H 6.740 0.03 1 900 . 92 TYR C C 174.960 0.3 1 901 . 92 TYR CA C 56.020 0.3 1 902 . 92 TYR CB C 42.330 0.3 1 903 . 92 TYR CD1 C 132.980 0.3 1 904 . 92 TYR CD2 C 132.980 0.3 1 905 . 92 TYR CE1 C 118.260 0.3 1 906 . 92 TYR CE2 C 118.260 0.3 1 907 . 92 TYR N N 123.200 0.3 1 908 . 93 TYR H H 9.890 0.03 1 909 . 93 TYR HA H 5.220 0.03 1 910 . 93 TYR HB2 H 2.850 0.03 1 911 . 93 TYR HB3 H 2.850 0.03 1 912 . 93 TYR HD1 H 7.200 0.03 1 913 . 93 TYR HD2 H 7.200 0.03 1 914 . 93 TYR HE1 H 6.810 0.03 1 915 . 93 TYR HE2 H 6.810 0.03 1 916 . 93 TYR C C 175.320 0.3 1 917 . 93 TYR CA C 57.450 0.3 1 918 . 93 TYR CB C 42.900 0.3 1 919 . 93 TYR CD1 C 133.470 0.3 1 920 . 93 TYR CD2 C 133.470 0.3 1 921 . 93 TYR CE1 C 117.800 0.3 1 922 . 93 TYR CE2 C 117.800 0.3 1 923 . 93 TYR N N 118.040 0.3 1 924 . 94 SER H H 8.330 0.03 1 925 . 94 SER HA H 4.110 0.03 1 926 . 94 SER HB2 H 1.500 0.03 2 927 . 94 SER HB3 H 2.680 0.03 2 928 . 94 SER C C 174.050 0.3 1 929 . 94 SER CA C 55.690 0.3 1 930 . 94 SER CB C 60.500 0.3 1 931 . 94 SER N N 119.720 0.3 1 932 . 95 ILE H H 8.980 0.03 1 933 . 95 ILE HA H 4.650 0.03 1 934 . 95 ILE HB H 2.000 0.03 1 935 . 95 ILE HG12 H 1.010 0.03 2 936 . 95 ILE HG13 H 1.170 0.03 2 937 . 95 ILE HG2 H 0.390 0.03 1 938 . 95 ILE HD1 H 0.390 0.03 1 939 . 95 ILE C C 175.010 0.3 1 940 . 95 ILE CA C 57.780 0.3 1 941 . 95 ILE CB C 38.110 0.3 1 942 . 95 ILE CG1 C 27.300 0.3 1 943 . 95 ILE CG2 C 16.700 0.3 1 944 . 95 ILE CD1 C 13.100 0.3 1 945 . 95 ILE N N 129.040 0.3 1 946 . 96 GLU H H 9.370 0.03 1 947 . 96 GLU HA H 5.030 0.03 1 948 . 96 GLU HB2 H 1.600 0.03 2 949 . 96 GLU HB3 H 1.920 0.03 2 950 . 96 GLU C C 175.110 0.3 1 951 . 96 GLU CA C 54.580 0.3 1 952 . 96 GLU CB C 33.600 0.3 1 953 . 96 GLU N N 129.470 0.3 1 954 . 97 LYS H H 8.870 0.03 1 955 . 97 LYS HA H 4.580 0.03 1 956 . 97 LYS HB2 H 1.860 0.03 2 957 . 97 LYS HB3 H 1.900 0.03 2 958 . 97 LYS HG2 H 1.340 0.03 2 959 . 97 LYS HG3 H 1.470 0.03 2 960 . 97 LYS HD2 H 1.630 0.03 1 961 . 97 LYS HD3 H 1.630 0.03 1 962 . 97 LYS HE2 H 2.910 0.03 1 963 . 97 LYS HE3 H 2.910 0.03 1 964 . 97 LYS C C 175.390 0.3 1 965 . 97 LYS CA C 56.200 0.3 1 966 . 97 LYS CB C 34.910 0.3 1 967 . 97 LYS CG C 24.600 0.3 1 968 . 97 LYS N N 127.850 0.3 1 969 . 98 GLU H H 9.630 0.03 1 970 . 98 GLU HA H 3.890 0.03 1 971 . 98 GLU HB2 H 2.010 0.03 2 972 . 98 GLU HB3 H 2.260 0.03 2 973 . 98 GLU HG2 H 2.260 0.03 1 974 . 98 GLU HG3 H 2.260 0.03 1 975 . 98 GLU C C 176.420 0.3 1 976 . 98 GLU CA C 57.080 0.3 1 977 . 98 GLU CB C 27.160 0.3 1 978 . 98 GLU CG C 36.400 0.3 1 979 . 98 GLU N N 126.130 0.3 1 980 . 99 GLY H H 8.670 0.03 1 981 . 99 GLY HA2 H 3.570 0.03 2 982 . 99 GLY HA3 H 4.100 0.03 2 983 . 99 GLY C C 173.470 0.3 1 984 . 99 GLY CA C 45.580 0.3 1 985 . 99 GLY N N 103.500 0.3 1 986 . 100 GLN H H 7.840 0.03 1 987 . 100 GLN HA H 4.700 0.03 1 988 . 100 GLN HB2 H 1.990 0.03 2 989 . 100 GLN HB3 H 2.140 0.03 2 990 . 100 GLN HG2 H 2.270 0.03 2 991 . 100 GLN HG3 H 2.360 0.03 2 992 . 100 GLN HE21 H 7.570 0.03 2 993 . 100 GLN HE22 H 6.880 0.03 2 994 . 100 GLN C C 174.510 0.3 1 995 . 100 GLN CA C 54.020 0.3 1 996 . 100 GLN CB C 31.480 0.3 1 997 . 100 GLN CG C 33.500 0.3 1 998 . 100 GLN N N 119.080 0.3 1 999 . 100 GLN NE2 N 112.020 0.3 1 1000 . 101 ARG H H 8.690 0.03 1 1001 . 101 ARG HA H 5.180 0.03 1 1002 . 101 ARG HB2 H 1.320 0.03 2 1003 . 101 ARG HB3 H 1.420 0.03 2 1004 . 101 ARG HG2 H 1.020 0.03 2 1005 . 101 ARG HG3 H 1.500 0.03 2 1006 . 101 ARG HD2 H 2.750 0.03 1 1007 . 101 ARG HD3 H 2.750 0.03 1 1008 . 101 ARG C C 175.080 0.3 1 1009 . 101 ARG CA C 54.950 0.3 1 1010 . 101 ARG CB C 31.660 0.3 1 1011 . 101 ARG CG C 27.500 0.3 1 1012 . 101 ARG CD C 43.200 0.3 1 1013 . 101 ARG N N 121.880 0.3 1 1014 . 102 LYS H H 8.060 0.03 1 1015 . 102 LYS HA H 4.380 0.03 1 1016 . 102 LYS HB2 H 1.660 0.03 1 1017 . 102 LYS HB3 H 1.660 0.03 1 1018 . 102 LYS HG2 H 1.220 0.03 2 1019 . 102 LYS HG3 H 1.360 0.03 2 1020 . 102 LYS HD2 H 1.580 0.03 1 1021 . 102 LYS HD3 H 1.580 0.03 1 1022 . 102 LYS HE2 H 2.840 0.03 1 1023 . 102 LYS HE3 H 2.840 0.03 1 1024 . 102 LYS C C 174.560 0.3 1 1025 . 102 LYS CA C 54.810 0.3 1 1026 . 102 LYS CB C 37.000 0.3 1 1027 . 102 LYS CG C 25.600 0.3 1 1028 . 102 LYS CD C 29.300 0.3 1 1029 . 102 LYS CE C 41.800 0.3 1 1030 . 102 LYS N N 122.190 0.3 1 1031 . 103 TRP H H 8.420 0.03 1 1032 . 103 TRP HA H 5.560 0.03 1 1033 . 103 TRP HB2 H 2.920 0.03 2 1034 . 103 TRP HB3 H 3.070 0.03 2 1035 . 103 TRP HD1 H 7.330 0.03 1 1036 . 103 TRP HE1 H 10.250 0.03 1 1037 . 103 TRP HE3 H 7.290 0.03 1 1038 . 103 TRP HZ2 H 7.020 0.03 1 1039 . 103 TRP HZ3 H 6.740 0.03 1 1040 . 103 TRP HH2 H 7.500 0.03 1 1041 . 103 TRP C C 176.870 0.3 1 1042 . 103 TRP CA C 56.200 0.3 1 1043 . 103 TRP CB C 30.600 0.3 1 1044 . 103 TRP CD1 C 128.530 0.3 1 1045 . 103 TRP CE3 C 120.060 0.3 1 1046 . 103 TRP CZ2 C 124.060 0.3 1 1047 . 103 TRP CZ3 C 124.060 0.3 1 1048 . 103 TRP CH2 C 115.230 0.3 1 1049 . 103 TRP N N 120.760 0.3 1 1050 . 103 TRP NE1 N 130.200 0.3 1 1051 . 104 TYR H H 10.000 0.03 1 1052 . 104 TYR HA H 4.970 0.03 1 1053 . 104 TYR HB2 H 2.690 0.03 2 1054 . 104 TYR HB3 H 3.090 0.03 2 1055 . 104 TYR HD1 H 7.190 0.03 1 1056 . 104 TYR HD2 H 7.190 0.03 1 1057 . 104 TYR HE1 H 6.620 0.03 1 1058 . 104 TYR HE2 H 6.620 0.03 1 1059 . 104 TYR C C 175.450 0.3 1 1060 . 104 TYR CA C 57.040 0.3 1 1061 . 104 TYR CB C 42.670 0.3 1 1062 . 104 TYR CD1 C 133.900 0.3 1 1063 . 104 TYR CD2 C 133.900 0.3 1 1064 . 104 TYR CE1 C 117.930 0.3 1 1065 . 104 TYR CE2 C 117.930 0.3 1 1066 . 104 TYR N N 121.890 0.3 1 1067 . 105 LYS H H 9.110 0.03 1 1068 . 105 LYS HA H 3.990 0.03 1 1069 . 105 LYS HB2 H 1.790 0.03 2 1070 . 105 LYS HB3 H 1.940 0.03 2 1071 . 105 LYS C C 177.000 0.3 1 1072 . 105 LYS CA C 56.940 0.3 1 1073 . 105 LYS CB C 33.260 0.3 1 1074 . 105 LYS N N 122.230 0.3 1 1075 . 106 ARG H H 7.940 0.03 1 1076 . 106 ARG HA H 4.030 0.03 1 1077 . 106 ARG HB2 H 1.970 0.03 2 1078 . 106 ARG HB3 H 2.140 0.03 2 1079 . 106 ARG C C 178.890 0.3 1 1080 . 106 ARG CA C 61.020 0.3 1 1081 . 106 ARG CB C 31.670 0.3 1 1082 . 106 ARG N N 120.470 0.3 1 1083 . 107 MET H H 8.820 0.03 1 1084 . 107 MET HA H 4.580 0.03 1 1085 . 107 MET HB2 H 2.220 0.03 2 1086 . 107 MET HB3 H 2.400 0.03 2 1087 . 107 MET HG2 H 2.570 0.03 2 1088 . 107 MET HG3 H 2.690 0.03 2 1089 . 107 MET C C 175.320 0.3 1 1090 . 107 MET CA C 57.820 0.3 1 1091 . 107 MET CB C 32.460 0.3 1 1092 . 107 MET CG C 31.200 0.3 1 1093 . 107 MET N N 113.280 0.3 1 1094 . 108 ALA H H 8.160 0.03 1 1095 . 108 ALA HA H 4.580 0.03 1 1096 . 108 ALA HB H 1.930 0.03 1 1097 . 108 ALA C C 174.350 0.3 1 1098 . 108 ALA CA C 51.840 0.3 1 1099 . 108 ALA CB C 19.650 0.3 1 1100 . 108 ALA N N 121.890 0.3 1 1101 . 109 VAL H H 7.480 0.03 1 1102 . 109 VAL HA H 4.370 0.03 1 1103 . 109 VAL HB H 1.960 0.03 1 1104 . 109 VAL HG1 H 0.220 0.03 1 1105 . 109 VAL HG2 H 0.690 0.03 1 1106 . 109 VAL C C 174.510 0.3 1 1107 . 109 VAL CA C 62.730 0.3 1 1108 . 109 VAL CB C 31.800 0.3 1 1109 . 109 VAL CG1 C 21.100 0.3 2 1110 . 109 VAL CG2 C 22.300 0.3 2 1111 . 109 VAL N N 118.520 0.3 1 1112 . 110 ILE H H 8.99 0.03 1 1113 . 110 ILE HA H 4.84 0.03 1 1114 . 110 ILE HB H 1.71 0.03 1 1115 . 110 ILE HG12 H 0.63 0.03 2 1116 . 110 ILE HG13 H 0.78 0.03 2 1117 . 110 ILE HG2 H 0.63 0.03 1 1118 . 110 ILE HD1 H 0 0.03 1 1119 . 110 ILE C C 173.9 0.3 1 1120 . 110 ILE CA C 58.52 0.3 1 1121 . 110 ILE CB C 41.5 0.3 1 1122 . 110 ILE CG1 C 27.4 0.3 1 1123 . 110 ILE CG2 C 18.4 0.3 1 1124 . 110 ILE CD1 C 14 0.3 1 1125 . 110 ILE N N 123.77 0.3 1 1126 . 111 LEU H H 8.250 0.03 1 1127 . 111 LEU HA H 5.350 0.03 1 1128 . 111 LEU HB2 H 1.430 0.03 2 1129 . 111 LEU HB3 H 1.530 0.03 2 1130 . 111 LEU HG H 1.430 0.03 1 1131 . 111 LEU HD1 H 0.480 0.03 1 1132 . 111 LEU HD2 H 0.680 0.03 1 1133 . 111 LEU C C 176.510 0.3 1 1134 . 111 LEU CA C 52.980 0.3 1 1135 . 111 LEU CB C 44.040 0.3 1 1136 . 111 LEU CG C 27.200 0.3 1 1137 . 111 LEU CD1 C 26.800 0.3 2 1138 . 111 LEU CD2 C 26.300 0.3 2 1139 . 111 LEU N N 115.860 0.3 1 1140 . 112 SER H H 9.030 0.03 1 1141 . 112 SER HA H 3.810 0.03 1 1142 . 112 SER HB2 H 4.060 0.03 1 1143 . 112 SER HB3 H 4.060 0.03 1 1144 . 112 SER C C 173.570 0.3 1 1145 . 112 SER CA C 57.050 0.3 1 1146 . 112 SER CB C 62.400 0.3 1 1147 . 112 SER N N 118.750 0.3 1 1148 . 113 LEU H H 8.200 0.03 1 1149 . 113 LEU HA H 4.180 0.03 1 1150 . 113 LEU HB2 H 1.600 0.03 1 1151 . 113 LEU HB3 H 1.630 0.03 1 1152 . 113 LEU HG H 1.560 0.03 1 1153 . 113 LEU HD1 H 0.970 0.03 2 1154 . 113 LEU HD2 H 0.870 0.03 2 1155 . 113 LEU C C 178.720 0.3 1 1156 . 113 LEU CA C 58.940 0.3 1 1157 . 113 LEU CB C 41.160 0.3 1 1158 . 113 LEU CG C 27.000 0.3 1 1159 . 113 LEU CD1 C 24.100 0.3 2 1160 . 113 LEU CD2 C 25.100 0.3 2 1161 . 113 LEU N N 121.820 0.3 1 1162 . 114 GLU H H 8.400 0.03 1 1163 . 114 GLU HA H 4.000 0.03 1 1164 . 114 GLU HB2 H 1.850 0.03 2 1165 . 114 GLU HB3 H 1.970 0.03 2 1166 . 114 GLU HG2 H 2.250 0.03 1 1167 . 114 GLU HG3 H 2.250 0.03 1 1168 . 114 GLU C C 179.380 0.3 1 1169 . 114 GLU CA C 59.530 0.3 1 1170 . 114 GLU CB C 29.280 0.3 1 1171 . 114 GLU CG C 36.400 0.3 1 1172 . 114 GLU N N 116.110 0.3 1 1173 . 115 GLN H H 7.590 0.03 1 1174 . 115 GLN HA H 3.920 0.03 1 1175 . 115 GLN HB2 H 2.000 0.03 2 1176 . 115 GLN HB3 H 2.270 0.03 2 1177 . 115 GLN HE21 H 5.560 0.03 5 1178 . 115 GLN HE22 H 8.350 0.03 5 1179 . 115 GLN C C 179.720 0.3 1 1180 . 115 GLN CA C 57.900 0.3 1 1181 . 115 GLN CB C 27.520 0.3 1 1182 . 115 GLN N N 117.930 0.3 1 1183 . 115 GLN NE2 N 109.030 0.3 5 1184 . 116 GLY H H 9.170 0.03 1 1185 . 116 GLY HA2 H 2.860 0.03 2 1186 . 116 GLY HA3 H 3.250 0.03 2 1187 . 116 GLY C C 175.900 0.3 1 1188 . 116 GLY CA C 46.380 0.3 1 1189 . 116 GLY N N 106.600 0.3 1 1190 . 117 ASN H H 8.560 0.03 1 1191 . 117 ASN HA H 4.480 0.03 1 1192 . 117 ASN HB2 H 2.840 0.03 2 1193 . 117 ASN HB3 H 3.010 0.03 2 1194 . 117 ASN HD21 H 6.750 0.03 2 1195 . 117 ASN HD22 H 7.650 0.03 2 1196 . 117 ASN C C 178.480 0.3 1 1197 . 117 ASN CA C 55.540 0.3 1 1198 . 117 ASN CB C 37.290 0.3 1 1199 . 117 ASN N N 120.150 0.3 1 1200 . 117 ASN ND2 N 110.150 0.3 1 1201 . 118 ARG H H 7.270 0.03 1 1202 . 118 ARG HA H 4.200 0.03 1 1203 . 118 ARG HB2 H 1.890 0.03 2 1204 . 118 ARG HB3 H 1.980 0.03 2 1205 . 118 ARG HG2 H 1.740 0.03 2 1206 . 118 ARG HG3 H 1.930 0.03 2 1207 . 118 ARG HD2 H 3.260 0.03 1 1208 . 118 ARG HD3 H 3.260 0.03 1 1209 . 118 ARG C C 177.010 0.3 1 1210 . 118 ARG CA C 58.440 0.3 1 1211 . 118 ARG CB C 29.930 0.3 1 1212 . 118 ARG CG C 27.400 0.3 1 1213 . 118 ARG CD C 43.500 0.3 1 1214 . 118 ARG N N 116.870 0.3 1 1215 . 119 LEU H H 7.340 0.03 1 1216 . 119 LEU HA H 4.650 0.03 1 1217 . 119 LEU HB2 H 1.710 0.03 2 1218 . 119 LEU HB3 H 1.790 0.03 2 1219 . 119 LEU HG H 1.710 0.03 1 1220 . 119 LEU HD1 H 0.730 0.03 1 1221 . 119 LEU HD2 H 0.840 0.03 1 1222 . 119 LEU C C 177.350 0.3 1 1223 . 119 LEU CA C 54.930 0.3 1 1224 . 119 LEU CB C 43.600 0.3 1 1225 . 119 LEU CG C 27.400 0.3 1 1226 . 119 LEU CD1 C 26.100 0.3 2 1227 . 119 LEU CD2 C 23.100 0.3 2 1228 . 119 LEU N N 116.980 0.3 1 1229 . 120 ARG H H 7.370 0.03 1 1230 . 120 ARG HA H 3.550 0.03 1 1231 . 120 ARG HB2 H 1.760 0.03 2 1232 . 120 ARG HB3 H 1.890 0.03 2 1233 . 120 ARG C C 178.040 0.3 1 1234 . 120 ARG CA C 60.170 0.3 1 1235 . 120 ARG CB C 30.460 0.3 1 1236 . 120 ARG N N 120.110 0.3 1 1237 . 121 GLU H H 8.640 0.03 1 1238 . 121 GLU HA H 3.850 0.03 1 1239 . 121 GLU HB2 H 1.960 0.03 2 1240 . 121 GLU HG2 H 2.130 0.03 2 1241 . 121 GLU HG3 H 2.190 0.03 2 1242 . 121 GLU C C 177.630 0.3 1 1243 . 121 GLU CA C 59.810 0.3 1 1244 . 121 GLU CB C 28.870 0.3 1 1245 . 121 GLU CG C 36.400 0.3 1 1246 . 121 GLU N N 119.200 0.3 1 1247 . 122 GLN H H 7.870 0.03 1 1248 . 122 GLN HA H 4.090 0.03 1 1249 . 122 GLN HB2 H 1.370 0.03 2 1250 . 122 GLN HB3 H 1.720 0.03 2 1251 . 122 GLN HG2 H 1.620 0.03 2 1252 . 122 GLN HG3 H 1.950 0.03 2 1253 . 122 GLN HE21 H 6.760 0.03 2 1254 . 122 GLN HE22 H 7.290 0.03 2 1255 . 122 GLN C C 177.160 0.3 1 1256 . 122 GLN CA C 57.310 0.3 1 1257 . 122 GLN CB C 29.980 0.3 1 1258 . 122 GLN CG C 33.500 0.3 1 1259 . 122 GLN N N 114.780 0.3 1 1260 . 122 GLN NE2 N 110.760 0.3 1 1261 . 123 TYR H H 8.130 0.03 1 1262 . 123 TYR HA H 4.780 0.03 1 1263 . 123 TYR HB2 H 2.540 0.03 2 1264 . 123 TYR HB3 H 3.120 0.03 2 1265 . 123 TYR HD1 H 7.250 0.03 1 1266 . 123 TYR HD2 H 7.250 0.03 1 1267 . 123 TYR HE1 H 6.830 0.03 1 1268 . 123 TYR HE2 H 6.830 0.03 1 1269 . 123 TYR C C 175.450 0.3 1 1270 . 123 TYR CA C 58.050 0.3 1 1271 . 123 TYR CB C 39.490 0.3 1 1272 . 123 TYR CD1 C 133.470 0.3 1 1273 . 123 TYR CD2 C 133.470 0.3 1 1274 . 123 TYR CE1 C 118.000 0.3 1 1275 . 123 TYR CE2 C 118.000 0.3 1 1276 . 123 TYR N N 112.670 0.3 1 1277 . 124 GLY H H 8.350 0.03 1 1278 . 124 GLY HA2 H 3.960 0.03 2 1279 . 124 GLY HA3 H 4.460 0.03 2 1280 . 124 GLY C C 173.840 0.3 1 1281 . 124 GLY CA C 45.580 0.3 1 1282 . 124 GLY N N 109.260 0.3 1 1283 . 125 LEU H H 8.320 0.03 1 1284 . 125 LEU HA H 4.170 0.03 1 1285 . 125 LEU HB2 H 1.720 0.03 2 1286 . 125 LEU HB3 H 1.350 0.03 2 1287 . 125 LEU HG H 1.230 0.03 1 1288 . 125 LEU HD1 H 0.260 0.03 1 1289 . 125 LEU HD2 H 0.360 0.03 1 1290 . 125 LEU C C 177.500 0.3 1 1291 . 125 LEU CA C 56.140 0.3 1 1292 . 125 LEU CB C 41.900 0.3 1 1293 . 125 LEU CG C 27.800 0.3 1 1294 . 125 LEU CD1 C 24.200 0.3 2 1295 . 125 LEU CD2 C 25.100 0.3 2 1296 . 125 LEU N N 122.750 0.3 1 1297 . 126 GLY H H 8.040 0.03 1 1298 . 126 GLY HA2 H 3.910 0.03 2 1299 . 126 GLY HA3 H 4.140 0.03 2 1300 . 126 GLY C C 171.100 0.3 1 1301 . 126 GLY CA C 44.840 0.3 1 1302 . 126 GLY N N 108.400 0.3 1 1303 . 127 PRO HA H 4.440 0.03 1 1304 . 127 PRO HB2 H 1.810 0.03 2 1305 . 127 PRO HB3 H 2.220 0.03 2 1306 . 127 PRO HG2 H 1.960 0.03 1 1307 . 127 PRO HG3 H 1.960 0.03 1 1308 . 127 PRO HD2 H 3.600 0.03 1 1309 . 127 PRO HD3 H 3.600 0.03 1 1310 . 127 PRO CA C 63.150 0.3 1 1311 . 127 PRO CB C 31.900 0.3 1 1312 . 127 PRO CG C 27.400 0.3 1 1313 . 127 PRO CD C 50.000 0.3 1 1314 . 128 TYR H H 8.290 0.03 1 1315 . 128 TYR HA H 4.520 0.03 1 1316 . 128 TYR HB2 H 3.010 0.03 2 1317 . 128 TYR HB3 H 3.060 0.03 2 1318 . 128 TYR HD1 H 7.120 0.03 1 1319 . 128 TYR HD2 H 7.120 0.03 1 1320 . 128 TYR HE1 H 6.830 0.03 1 1321 . 128 TYR HE2 H 6.830 0.03 1 1322 . 128 TYR C C 175.390 0.3 1 1323 . 128 TYR CA C 58.170 0.3 1 1324 . 128 TYR CB C 38.820 0.3 1 1325 . 128 TYR CD1 C 133.000 0.3 1 1326 . 128 TYR CD2 C 133.000 0.3 1 1327 . 128 TYR CE1 C 117.940 0.3 1 1328 . 128 TYR CE2 C 117.940 0.3 1 1329 . 128 TYR N N 120.520 0.3 1 1330 . 129 GLU H H 8.070 0.03 1 1331 . 129 GLU HA H 4.220 0.03 1 1332 . 129 GLU HB2 H 1.840 0.03 2 1333 . 129 GLU HB3 H 1.940 0.03 2 1334 . 129 GLU HG2 H 2.160 0.03 1 1335 . 129 GLU HG3 H 2.160 0.03 1 1336 . 129 GLU C C 175.080 0.3 1 1337 . 129 GLU CA C 55.830 0.3 1 1338 . 129 GLU CB C 30.520 0.3 1 1339 . 129 GLU CG C 36.100 0.3 1 1340 . 129 GLU N N 123.220 0.3 1 1341 . 130 ALA H H 8.090 0.03 1 1342 . 130 ALA HA H 4.260 0.03 1 1343 . 130 ALA HB H 1.350 0.03 1 1344 . 130 ALA C C 177.270 0.3 1 1345 . 130 ALA CA C 52.220 0.3 1 1346 . 130 ALA CB C 18.980 0.3 1 1347 . 130 ALA N N 124.810 0.3 1 1348 . 131 VAL H H 8.020 0.03 1 1349 . 131 VAL HA H 4.140 0.03 1 1350 . 131 VAL HB H 2.050 0.03 1 1351 . 131 VAL HG1 H 0.890 0.03 1 1352 . 131 VAL HG2 H 0.920 0.03 1 1353 . 131 VAL C C 175.890 0.3 1 1354 . 131 VAL CA C 62.000 0.3 1 1355 . 131 VAL CB C 32.650 0.3 1 1356 . 131 VAL CG1 C 20.800 0.3 2 1357 . 131 VAL CG2 C 21.100 0.3 2 1358 . 131 VAL N N 118.800 0.3 1 1359 . 132 THR H H 7.840 0.03 1 1360 . 132 THR HA H 4.440 0.03 1 1361 . 132 THR HB H 4.080 0.03 1 1362 . 132 THR HG2 H 1.150 0.03 1 1363 . 132 THR CA C 58.560 0.3 1 1364 . 132 THR CB C 70.120 0.3 1 1365 . 132 THR CG2 C 20.900 0.3 1 1366 . 132 THR N N 116.520 0.3 1 1367 . 133 PRO HA H 4.420 0.03 1 1368 . 133 PRO HB2 H 1.890 0.03 2 1369 . 133 PRO HB3 H 2.300 0.03 2 1370 . 133 PRO HG2 H 1.970 0.03 2 1371 . 133 PRO HG3 H 2.030 0.03 2 1372 . 133 PRO HD2 H 3.720 0.03 2 1373 . 133 PRO HD3 H 3.870 0.03 2 1374 . 133 PRO C C 176.680 0.3 1 1375 . 133 PRO CA C 63.010 0.3 1 1376 . 133 PRO CB C 31.880 0.3 1 1377 . 133 PRO CG C 27.400 0.3 1 1378 . 133 PRO CD C 51.000 0.3 1 1379 . 134 LEU H H 8.270 0.03 1 1380 . 134 LEU HA H 4.340 0.03 1 1381 . 134 LEU HB2 H 1.590 0.03 2 1382 . 134 LEU HB3 H 1.640 0.03 2 1383 . 134 LEU HG H 1.600 0.03 1 1384 . 134 LEU HD1 H 0.900 0.03 1 1385 . 134 LEU HD2 H 0.830 0.03 1 1386 . 134 LEU C C 177.510 0.3 1 1387 . 134 LEU CA C 55.320 0.3 1 1388 . 134 LEU CB C 42.090 0.3 1 1389 . 134 LEU CG C 26.900 0.3 1 1390 . 134 LEU CD1 C 25.000 0.3 2 1391 . 134 LEU CD2 C 23.300 0.3 2 1392 . 134 LEU N N 121.540 0.3 1 1393 . 135 THR H H 8.000 0.03 1 1394 . 135 THR HA H 4.300 0.03 1 1395 . 135 THR HB H 4.180 0.03 1 1396 . 135 THR HG2 H 1.190 0.03 1 1397 . 135 THR C C 174.200 0.3 1 1398 . 135 THR CA C 61.780 0.3 1 1399 . 135 THR CB C 69.700 0.3 1 1400 . 135 THR CG2 C 20.500 0.3 1 1401 . 135 THR N N 114.430 0.3 1 1402 . 136 LYS H H 8.260 0.03 1 1403 . 136 LYS HA H 4.310 0.03 1 1404 . 136 LYS HB2 H 1.740 0.03 2 1405 . 136 LYS HB3 H 1.820 0.03 2 1406 . 136 LYS HG2 H 1.420 0.03 1 1407 . 136 LYS HG3 H 1.420 0.03 1 1408 . 136 LYS HD2 H 1.670 0.03 1 1409 . 136 LYS HD3 H 1.670 0.03 1 1410 . 136 LYS HE2 H 2.970 0.03 1 1411 . 136 LYS HE3 H 2.970 0.03 1 1412 . 136 LYS C C 175.950 0.3 1 1413 . 136 LYS CA C 55.970 0.3 1 1414 . 136 LYS CB C 32.950 0.3 1 1415 . 136 LYS CG C 25.000 0.3 1 1416 . 136 LYS CD C 28.900 0.3 1 1417 . 136 LYS CE C 41.800 0.3 1 1418 . 136 LYS N N 123.450 0.3 1 1419 . 137 ALA H H 8.280 0.03 1 1420 . 137 ALA HA H 4.260 0.03 1 1421 . 137 ALA HB H 1.350 0.03 1 1422 . 137 ALA C C 177.340 0.3 1 1423 . 137 ALA CA C 52.520 0.3 1 1424 . 137 ALA CB C 18.930 0.3 1 1425 . 137 ALA N N 125.320 0.3 1 1426 . 138 ALA H H 8.220 0.03 1 1427 . 138 ALA HA H 4.270 0.03 1 1428 . 138 ALA HB H 1.350 0.03 1 1429 . 138 ALA C C 177.330 0.3 1 1430 . 138 ALA CA C 52.400 0.3 1 1431 . 138 ALA CB C 18.900 0.3 1 1432 . 138 ALA N N 122.470 0.3 1 1433 . 139 ASP H H 8.220 0.03 1 1434 . 139 ASP HA H 4.600 0.03 1 1435 . 139 ASP HB2 H 2.600 0.03 2 1436 . 139 ASP HB3 H 2.700 0.03 2 1437 . 139 ASP C C 176.170 0.3 1 1438 . 139 ASP CA C 54.250 0.3 1 1439 . 139 ASP CB C 40.950 0.3 1 1440 . 139 ASP N N 119.130 0.3 1 1441 . 140 ILE H H 7.960 0.03 1 1442 . 140 ILE HA H 4.210 0.03 1 1443 . 140 ILE HB H 1.910 0.03 1 1444 . 140 ILE HG12 H 1.170 0.03 2 1445 . 140 ILE HG13 H 1.420 0.03 2 1446 . 140 ILE HG2 H 0.870 0.03 1 1447 . 140 ILE HD1 H 0.820 0.03 1 1448 . 140 ILE C C 176.080 0.3 1 1449 . 140 ILE CA C 61.070 0.3 1 1450 . 140 ILE CB C 38.670 0.3 1 1451 . 140 ILE CG1 C 26.900 0.3 1 1452 . 140 ILE CG2 C 17.500 0.3 1 1453 . 140 ILE CD1 C 13.400 0.3 1 1454 . 140 ILE N N 120.080 0.3 1 1455 . 141 SER H H 8.360 0.03 1 1456 . 141 SER HA H 4.450 0.03 1 1457 . 141 SER HB2 H 3.850 0.03 2 1458 . 141 SER HB3 H 3.870 0.03 2 1459 . 141 SER C C 174.690 0.3 1 1460 . 141 SER CA C 58.230 0.3 1 1461 . 141 SER CB C 63.460 0.3 1 1462 . 141 SER N N 119.030 0.3 1 1463 . 142 LEU H H 8.270 0.03 1 1464 . 142 LEU HA H 4.320 0.03 1 1465 . 142 LEU HB2 H 1.590 0.03 2 1466 . 142 LEU HB3 H 1.640 0.03 2 1467 . 142 LEU HG H 1.600 0.03 1 1468 . 142 LEU HD1 H 0.900 0.03 1 1469 . 142 LEU HD2 H 0.830 0.03 1 1470 . 142 LEU C C 177.190 0.3 1 1471 . 142 LEU CA C 55.420 0.3 1 1472 . 142 LEU CB C 41.900 0.3 1 1473 . 142 LEU CG C 26.900 0.3 1 1474 . 142 LEU CD1 C 25.000 0.3 2 1475 . 142 LEU CD2 C 23.300 0.3 2 1476 . 142 LEU N N 124.000 0.3 1 1477 . 143 ASP H H 8.180 0.03 1 1478 . 143 ASP HA H 4.520 0.03 1 1479 . 143 ASP HB2 H 2.550 0.03 2 1480 . 143 ASP HB3 H 2.650 0.03 2 1481 . 143 ASP C C 176.090 0.3 1 1482 . 143 ASP CA C 54.790 0.3 1 1483 . 143 ASP CB C 40.910 0.3 1 1484 . 143 ASP N N 119.460 0.3 1 1485 . 144 ASN H H 8.210 0.03 1 1486 . 144 ASN HA H 4.660 0.03 1 1487 . 144 ASN HB2 H 2.810 0.03 2 1488 . 144 ASN HB3 H 2.760 0.03 2 1489 . 144 ASN C C 175.180 0.3 1 1490 . 144 ASN CA C 53.490 0.3 1 1491 . 144 ASN CB C 38.670 0.3 1 1492 . 144 ASN N N 117.730 0.3 1 1493 . 145 LEU H H 8.090 0.03 1 1494 . 145 LEU HA H 4.320 0.03 1 1495 . 145 LEU HB2 H 1.590 0.03 2 1496 . 145 LEU HB3 H 1.640 0.03 2 1497 . 145 LEU HG H 1.600 0.03 1 1498 . 145 LEU HD1 H 0.900 0.03 1 1499 . 145 LEU HD2 H 0.830 0.03 1 1500 . 145 LEU C C 177.500 0.3 1 1501 . 145 LEU CA C 55.490 0.3 1 1502 . 145 LEU CB C 42.080 0.3 1 1503 . 145 LEU CG C 26.900 0.3 1 1504 . 145 LEU CD1 C 25.000 0.3 2 1505 . 145 LEU CD2 C 23.300 0.3 2 1506 . 145 LEU N N 121.470 0.3 1 1507 . 146 VAL H H 8.010 0.03 1 1508 . 146 VAL HA H 4.030 0.03 1 1509 . 146 VAL HB H 2.080 0.03 1 1510 . 146 VAL HG1 H 0.920 0.03 1 1511 . 146 VAL HG2 H 0.920 0.03 1 1512 . 146 VAL C C 176.370 0.3 1 1513 . 146 VAL CA C 62.790 0.3 1 1514 . 146 VAL CB C 32.470 0.3 1 1515 . 146 VAL CG1 C 21.200 0.3 1 1516 . 146 VAL CG2 C 21.200 0.3 1 1517 . 146 VAL N N 119.750 0.3 1 1518 . 147 GLU H H 8.440 0.03 1 1519 . 147 GLU HA H 4.200 0.03 1 1520 . 147 GLU HB2 H 1.980 0.03 2 1521 . 147 GLU HB3 H 2.040 0.03 2 1522 . 147 GLU HG2 H 2.260 0.03 1 1523 . 147 GLU HG3 H 2.260 0.03 1 1524 . 147 GLU C C 177.130 0.3 1 1525 . 147 GLU CA C 57.080 0.3 1 1526 . 147 GLU CB C 29.780 0.3 1 1527 . 147 GLU CG C 36.000 0.3 1 1528 . 147 GLU N N 123.280 0.3 1 1529 . 148 GLY H H 8.340 0.03 1 1530 . 148 GLY HA2 H 3.930 0.03 1 1531 . 148 GLY HA3 H 3.930 0.03 1 1532 . 148 GLY C C 174.290 0.3 1 1533 . 148 GLY CA C 45.670 0.3 1 1534 . 148 GLY N N 108.620 0.3 1 1535 . 149 LYS H H 8.040 0.03 1 1536 . 149 LYS HA H 4.310 0.03 1 1537 . 149 LYS HB2 H 1.740 0.03 2 1538 . 149 LYS HB3 H 1.820 0.03 2 1539 . 149 LYS HG2 H 1.420 0.03 1 1540 . 149 LYS HG3 H 1.420 0.03 1 1541 . 149 LYS HD2 H 1.670 0.03 1 1542 . 149 LYS HD3 H 1.670 0.03 1 1543 . 149 LYS HE2 H 2.970 0.03 1 1544 . 149 LYS HE3 H 2.970 0.03 1 1545 . 149 LYS C C 176.580 0.3 1 1546 . 149 LYS CA C 56.300 0.3 1 1547 . 149 LYS CB C 32.860 0.3 1 1548 . 149 LYS CG C 25.000 0.3 1 1549 . 149 LYS CD C 28.900 0.3 1 1550 . 149 LYS CE C 41.800 0.3 1 1551 . 149 LYS N N 119.950 0.3 1 1552 . 150 ARG H H 8.160 0.03 1 1553 . 150 ARG HA H 4.310 0.03 1 1554 . 150 ARG HB2 H 1.760 0.03 2 1555 . 150 ARG HB3 H 1.820 0.03 2 1556 . 150 ARG HG2 H 1.620 0.03 1 1557 . 150 ARG HG3 H 1.620 0.03 1 1558 . 150 ARG HD2 H 3.170 0.03 1 1559 . 150 ARG HD3 H 3.170 0.03 1 1560 . 150 ARG CA C 56.240 0.3 1 1561 . 150 ARG CB C 30.700 0.3 1 1562 . 150 ARG CG C 27.000 0.3 1 1563 . 150 ARG CD C 42.800 0.3 1 1564 . 150 ARG N N 120.710 0.3 1 1565 . 151 LYS H H 8.240 0.03 1 1566 . 151 LYS HA H 4.300 0.03 1 1567 . 151 LYS HB2 H 1.740 0.03 2 1568 . 151 LYS HB3 H 1.820 0.03 2 1569 . 151 LYS HG2 H 1.420 0.03 1 1570 . 151 LYS HG3 H 1.420 0.03 1 1571 . 151 LYS HD2 H 1.670 0.03 1 1572 . 151 LYS HD3 H 1.670 0.03 1 1573 . 151 LYS HE2 H 2.970 0.03 1 1574 . 151 LYS HE3 H 2.970 0.03 1 1575 . 151 LYS C C 176.240 0.3 1 1576 . 151 LYS CA C 55.980 0.3 1 1577 . 151 LYS CB C 32.870 0.3 1 1578 . 151 LYS CG C 25.000 0.3 1 1579 . 151 LYS CD C 28.900 0.3 1 1580 . 151 LYS CE C 41.800 0.3 1 1581 . 151 LYS N N 122.110 0.3 1 1582 . 152 ARG H H 8.320 0.03 1 1583 . 152 ARG HA H 4.310 0.03 1 1584 . 152 ARG HB2 H 1.760 0.03 2 1585 . 152 ARG HB3 H 1.820 0.03 2 1586 . 152 ARG HG2 H 1.620 0.03 1 1587 . 152 ARG HG3 H 1.620 0.03 1 1588 . 152 ARG HD2 H 3.170 0.03 1 1589 . 152 ARG HD3 H 3.170 0.03 1 1590 . 152 ARG C C 176.090 0.3 1 1591 . 152 ARG CA C 56.060 0.3 1 1592 . 152 ARG CB C 30.750 0.3 1 1593 . 152 ARG CG C 27.000 0.3 1 1594 . 152 ARG CD C 42.800 0.3 1 1595 . 152 ARG N N 122.320 0.3 1 1596 . 153 ARG H H 8.420 0.03 1 1597 . 153 ARG HA H 4.310 0.03 1 1598 . 153 ARG HB2 H 1.760 0.03 2 1599 . 153 ARG HB3 H 1.820 0.03 2 1600 . 153 ARG HG2 H 1.620 0.03 1 1601 . 153 ARG HG3 H 1.620 0.03 1 1602 . 153 ARG HD2 H 3.170 0.03 1 1603 . 153 ARG HD3 H 3.170 0.03 1 1604 . 153 ARG C C 175.930 0.3 1 1605 . 153 ARG CA C 56.100 0.3 1 1606 . 153 ARG CB C 30.760 0.3 1 1607 . 153 ARG CG C 27.000 0.3 1 1608 . 153 ARG CD C 42.800 0.3 1 1609 . 153 ARG N N 122.350 0.3 1 1610 . 154 SER H H 8.380 0.03 1 1611 . 154 SER HA H 4.470 0.03 1 1612 . 154 SER HB2 H 3.860 0.03 1 1613 . 154 SER HB3 H 3.860 0.03 1 1614 . 154 SER C C 173.090 0.3 1 1615 . 154 SER CA C 57.940 0.3 1 1616 . 154 SER CB C 63.770 0.3 1 1617 . 154 SER N N 125.150 0.3 1 1618 . 155 ASN H H 8.070 0.03 1 1619 . 155 ASN HA H 4.460 0.03 1 1620 . 155 ASN HB2 H 2.690 0.03 2 1621 . 155 ASN HB3 H 2.750 0.03 2 1622 . 155 ASN C C 179.570 0.3 1 1623 . 155 ASN CA C 54.780 0.3 1 1624 . 155 ASN CB C 40.000 0.3 1 1625 . 155 ASN N N 125.430 0.3 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details 'Several residues split in two. The minor form (Segment B) is listed here.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '53BP1 subunit 1' _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 . 15 VAL H H 8.600 0.03 1 2 . 15 VAL HA H 5.180 0.03 1 3 . 15 VAL HB H 1.870 0.03 1 4 . 15 VAL C C 174.980 0.3 1 5 . 15 VAL CA C 60.820 0.3 1 6 . 15 VAL N N 115.350 0.3 1 7 . 30 THR H H 8.210 0.03 1 8 . 30 THR HA H 4.630 0.03 1 9 . 30 THR HB H 4.220 0.03 1 10 . 30 THR C C 175.600 0.3 1 11 . 30 THR CA C 59.690 0.3 1 12 . 30 THR N N 120.110 0.3 1 13 . 36 GLY H H 8.340 0.03 1 14 . 36 GLY HA2 H 3.640 0.03 2 15 . 36 GLY HA3 H 4.090 0.03 2 16 . 36 GLY C C 173.160 0.3 1 17 . 36 GLY CA C 45.760 0.3 1 18 . 36 GLY N N 104.920 0.3 1 19 . 38 TYR H H 8.810 0.03 1 20 . 38 TYR N N 119.000 0.3 1 21 . 52 GLY H H 9.090 0.03 1 22 . 52 GLY HA2 H 4.300 0.03 2 23 . 52 GLY HA3 H 3.760 0.03 2 24 . 52 GLY C C 175.900 0.3 1 25 . 52 GLY CA C 48.080 0.3 1 26 . 52 GLY N N 108.770 0.3 1 27 . 53 LYS H H 7.900 0.03 1 28 . 53 LYS HA H 4.050 0.03 1 29 . 53 LYS CA C 57.960 0.3 1 30 . 53 LYS CB C 31.400 0.3 1 31 . 53 LYS N N 115.000 0.3 1 32 . 56 LEU H H 9.200 0.03 1 33 . 56 LEU HA H 4.800 0.03 1 34 . 56 LEU CA C 52.750 0.3 1 35 . 56 LEU N N 124.710 0.3 1 36 . 61 ILE H H 9.530 0.03 1 37 . 61 ILE HA H 4.620 0.03 1 38 . 61 ILE C C 175.330 0.3 1 39 . 61 ILE CA C 61.950 0.3 1 40 . 61 ILE CB C 37.790 0.3 1 41 . 61 ILE N N 120.050 0.3 1 42 . 119 LEU H H 7.370 0.03 1 43 . 119 LEU HA H 4.650 0.03 1 44 . 119 LEU C C 177.330 0.3 1 45 . 119 LEU CA C 54.930 0.3 1 46 . 119 LEU CB C 43.600 0.3 1 47 . 119 LEU N N 117.010 0.3 1 48 . 120 ARG H H 7.340 0.03 1 49 . 120 ARG HA H 3.550 0.03 1 50 . 120 ARG C C 177.830 0.3 1 51 . 120 ARG CA C 60.140 0.3 1 52 . 120 ARG CB C 30.510 0.3 1 53 . 120 ARG N N 120.330 0.3 1 54 . 121 GLU H H 8.610 0.03 1 55 . 121 GLU HA H 3.840 0.03 1 56 . 121 GLU CA C 59.820 0.3 1 57 . 121 GLU CB C 28.810 0.3 1 58 . 121 GLU N N 118.750 0.3 1 59 . 124 GLY H H 8.580 0.03 1 60 . 124 GLY HA2 H 4.170 0.03 1 61 . 124 GLY HA3 H 4.170 0.03 1 62 . 124 GLY C C 174.540 0.3 1 63 . 124 GLY CA C 46.040 0.3 1 64 . 124 GLY N N 110.340 0.3 1 65 . 125 LEU H H 8.400 0.03 1 66 . 125 LEU HA H 4.110 0.03 1 67 . 125 LEU HB2 H 1.850 0.03 2 68 . 125 LEU C C 177.500 0.3 1 69 . 125 LEU CA C 57.130 0.3 1 70 . 125 LEU CB C 41.070 0.3 1 71 . 125 LEU N N 125.270 0.3 1 72 . 126 GLY H H 7.260 0.03 1 73 . 126 GLY HA2 H 2.480 0.03 2 74 . 126 GLY HA3 H 3.650 0.03 2 75 . 126 GLY C C 170.320 0.3 1 76 . 126 GLY CA C 43.990 0.3 1 77 . 126 GLY N N 105.820 0.3 1 78 . 130 ALA H H 8.380 0.03 1 79 . 130 ALA HA H 4.340 0.03 1 80 . 130 ALA HB H 1.380 0.03 1 81 . 130 ALA C C 177.000 0.3 1 82 . 130 ALA CA C 52.320 0.3 1 83 . 130 ALA CB C 18.940 0.3 1 84 . 130 ALA N N 125.230 0.3 1 85 . 131 VAL H H 8.120 0.03 1 86 . 131 VAL HA H 4.160 0.03 1 87 . 131 VAL C C 175.960 0.3 1 88 . 131 VAL CA C 61.990 0.3 1 89 . 131 VAL CB C 32.690 0.3 1 90 . 131 VAL N N 119.230 0.3 1 stop_ save_