data_5497 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C resonance assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD ; _BMRB_accession_number 5497 _BMRB_flat_file_name bmr5497.str _Entry_type original _Submission_date 2002-08-08 _Accession_date 2002-08-08 _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 Bushell Mark . . 2 Ferguson Stuart J. . 3 Redfield Christina . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 581 "13C chemical shifts" 469 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-23 original author . stop_ _Original_release_date 2002-12-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bushell K. 'Mark W.' . 2 Ferguson Stuart J. . 3 Redfield Christina . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 359 _Page_last 360 _Year 2002 _Details . loop_ _Keyword DsbD DipZ 'thiol-disulfide reductase' 'electron transfer' periplasm 'thioredoxin fold' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Gordon EH, Page MD, Willis AC, Ferguson SI Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. MolMicrobiol. 2000 Mar:35(6):1360-74 ; _Citation_title 'Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10760137 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gordon E.H. H. . 2 Page M.D. D. . 3 Willis A.C. C. . 4 Ferguson S.J. J. . stop_ _Journal_abbreviation 'Mol. Microbiol.' _Journal_name_full 'Molecular microbiology' _Journal_volume 35 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1360 _Page_last 1374 _Year 2000 _Details ; DipZ is a bacterial cytoplasmic membrane protein that transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment. Topological analysis using gene fusions between the Escherichia coli dipZ and either E. coli phoA or lacZ shows that DipZ has a highly hydrophobic central domain comprising eight transmembrane alpha-helices plus periplasmic globular N-terminal and C-terminal domains. The previously assigned translational start codon for the E. coli DipZ was shown to be incorrect and the protein to be larger than previously thought. The experimentally determined translational start position indicates that an additional alpha-helix at the N-terminus acts as a cleavable signal peptide so that the N-terminus of the mature protein is located in the periplasm. The newly assigned 5' end of the dipZ gene was shown to be preceded by a functional ribosome-binding site. The hydrophobic central domain and both of the periplasmic globular domains each have a pair of highly conserved cysteine residues, and it was shown by site directed mutagenesis that all six conserved cysteine residues contribute to DipZ function. ; save_ ################################## # Molecular system description # ################################## save_system_DsbD_C-terminal_domain _Saveframe_category molecular_system _Mol_system_name 'DsbD C-terminal domain' _Abbreviation_common 'DsbD C-terminal domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DsbD C-terminal domain' $DsbD_C_terminal_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'thiol-disulfide reductase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DsbD_C_terminal_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli DsbD C-terminal domain' _Abbreviation_common 'DsbD C-terminal domain' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; The first 9 residues and the last 13 residues are from the expression vector. Residues 10-147 correspond to residues 409 to 546 of the E. coli DsbD sequence. ; ############################## # Polymer residue sequence # ############################## _Residue_count 160 _Mol_residue_sequence ; MDIGINSDPVRPLQDWAFGA THTAQTQTHLNFTQIKTVDE LNQALVEAKGKPVMLDLYAD WCVACKEFEKYTFSDPQVQK ALADTVLLQANVTANDAQDV ALLKHLNVLGLPTILFFDGQ GQEHPQARVTGFMDAETFSA HLRDRQPKLAAALEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASP 3 3 ILE 4 4 GLY 5 5 ILE 6 6 ASN 7 7 SER 8 8 ASP 9 9 PRO 10 409 VAL 11 410 ARG 12 411 PRO 13 412 LEU 14 413 GLN 15 414 ASP 16 415 TRP 17 416 ALA 18 417 PHE 19 418 GLY 20 419 ALA 21 420 THR 22 421 HIS 23 422 THR 24 423 ALA 25 424 GLN 26 425 THR 27 426 GLN 28 427 THR 29 428 HIS 30 429 LEU 31 430 ASN 32 431 PHE 33 432 THR 34 433 GLN 35 434 ILE 36 435 LYS 37 436 THR 38 437 VAL 39 438 ASP 40 439 GLU 41 440 LEU 42 441 ASN 43 442 GLN 44 443 ALA 45 444 LEU 46 445 VAL 47 446 GLU 48 447 ALA 49 448 LYS 50 449 GLY 51 450 LYS 52 451 PRO 53 452 VAL 54 453 MET 55 454 LEU 56 455 ASP 57 456 LEU 58 457 TYR 59 458 ALA 60 459 ASP 61 460 TRP 62 461 CYS 63 462 VAL 64 463 ALA 65 464 CYS 66 465 LYS 67 466 GLU 68 467 PHE 69 468 GLU 70 469 LYS 71 470 TYR 72 471 THR 73 472 PHE 74 473 SER 75 474 ASP 76 475 PRO 77 476 GLN 78 477 VAL 79 478 GLN 80 479 LYS 81 480 ALA 82 481 LEU 83 482 ALA 84 483 ASP 85 484 THR 86 485 VAL 87 486 LEU 88 487 LEU 89 488 GLN 90 489 ALA 91 490 ASN 92 491 VAL 93 492 THR 94 493 ALA 95 494 ASN 96 495 ASP 97 496 ALA 98 497 GLN 99 498 ASP 100 499 VAL 101 500 ALA 102 501 LEU 103 502 LEU 104 503 LYS 105 504 HIS 106 505 LEU 107 506 ASN 108 507 VAL 109 508 LEU 110 509 GLY 111 510 LEU 112 511 PRO 113 512 THR 114 513 ILE 115 514 LEU 116 515 PHE 117 516 PHE 118 517 ASP 119 518 GLY 120 519 GLN 121 520 GLY 122 521 GLN 123 522 GLU 124 523 HIS 125 524 PRO 126 525 GLN 127 526 ALA 128 527 ARG 129 528 VAL 130 529 THR 131 530 GLY 132 531 PHE 133 532 MET 134 533 ASP 135 534 ALA 136 535 GLU 137 536 THR 138 537 PHE 139 538 SER 140 539 ALA 141 540 HIS 142 541 LEU 143 542 ARG 144 543 ASP 145 544 ARG 146 545 GLN 147 546 PRO 148 148 LYS 149 149 LEU 150 150 ALA 151 151 ALA 152 152 ALA 153 153 LEU 154 154 GLU 155 155 HIS 156 156 HIS 157 157 HIS 158 158 HIS 159 159 HIS 160 160 HIS 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 PDB 1UC7 "Crystal Structure Of Dsbdgamma" 78.13 125 100.00 100.00 5.34e-85 PDB 4IP1 "C-terminal Domain Of The Thiol:disulfide Interchange Protein Dsbd, Q488k Mutant" 77.50 132 98.39 99.19 9.29e-83 PDB 4IP6 "C-terminal Domain Of The Thiol:disulfide Interchange Protein Dsbd, Q488a Mutant" 77.50 132 98.39 98.39 2.48e-82 DBJ BAB38540 "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" 86.25 565 100.00 100.00 7.95e-92 DBJ BAE78138 "fused thiol:disulfide interchange protein [Escherichia coli str. K-12 substr. W3110]" 86.25 565 100.00 100.00 1.03e-91 DBJ BAG66862 "fused thiol:disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O111:H-]" 86.25 565 100.00 100.00 7.54e-92 DBJ BAG79959 "thiol:disulfide interchange protein [Escherichia coli SE11]" 86.25 565 100.00 100.00 8.04e-92 DBJ BAI28440 "fused thiol: disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O26:H11 str. 11368]" 86.25 565 99.28 99.28 4.23e-91 EMBL CAA54781 "disulphide isomerase like protein [Escherichia coli K-12]" 86.25 489 100.00 100.00 4.76e-93 EMBL CAA85375 "inner membrane copper tolerance protein [Escherichia coli str. K-12 substr. W3110]" 86.25 489 100.00 100.00 4.76e-93 EMBL CAP78654 "Thiol:disulfide interchange protein dsbD [Escherichia coli LF82]" 86.25 565 100.00 100.00 7.07e-92 EMBL CAQ34485 "DsbD[reduced] [Escherichia coli BL21(DE3)]" 86.25 565 100.00 100.00 8.48e-92 EMBL CAR01112 "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli IAI1]" 86.25 565 100.00 100.00 7.54e-92 GB AAA97035 "cycZ [Escherichia coli str. K-12 substr. MG1655]" 86.25 565 100.00 100.00 1.03e-91 GB AAC77096 "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" 86.25 565 100.00 100.00 1.03e-91 GB AAG59335 "thiol:disulfide interchange protein; copper tolerance [Escherichia coli O157:H7 str. EDL933]" 86.25 565 100.00 100.00 7.95e-92 GB AAL50628 "DsbD [Shigella flexneri 2a]" 58.13 94 100.00 100.00 1.02e-60 GB AAN45708 "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" 86.25 565 100.00 100.00 8.12e-92 REF NP_290769 "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. EDL933]" 86.25 565 100.00 100.00 7.95e-92 REF NP_313144 "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" 86.25 565 100.00 100.00 7.95e-92 REF NP_418559 "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" 86.25 565 100.00 100.00 1.03e-91 REF NP_710001 "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" 86.25 565 100.00 100.00 8.12e-92 REF NP_757066 "thiol:disulfide interchange protein [Escherichia coli CFT073]" 86.25 565 99.28 100.00 2.70e-91 SP P36655 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=C-type cytochrome biogenesis protein CycZ; AltName: Full=" 86.25 565 100.00 100.00 1.03e-91 SP P58162 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 86.25 565 100.00 100.00 7.95e-92 SP Q0SXE3 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 86.25 565 100.00 100.00 7.54e-92 SP Q0T9Q5 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 86.25 565 99.28 99.28 5.77e-91 SP Q1R3C4 "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" 86.25 565 99.28 99.28 5.77e-91 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction _Gene_mnemonic $DsbD_C_terminal_domain 'E. coli' 562 Bacteria . Escherichia coli K12 periplasm DsbD 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 $DsbD_C_terminal_domain 'recombinant technology' 'E. coli' Escherichia coli JM109(DE3) plasmid pET22b(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbD_C_terminal_domain 1.5 mM '[U-99% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbD_C_terminal_domain 1.5 mM '[U-95% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer 'home built' _Model . _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer 'home built' _Model . _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_The_home-built_spectrometers_are_equipped_with_Oxford_Instruments_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'The home-built spectrometers are equipped with Oxford Instruments' _Sample_label . save_ save_Company_magnets,_Omega_software_and_digital_control_equipment_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'Company magnets, Omega software and digital control equipment' _Sample_label . save_ save_(Bruker),_home-built_triple_resonance_pulsed_field_gradient_probe_3 _Saveframe_category NMR_applied_experiment _Experiment_name '(Bruker), home-built triple resonance pulsed field gradient probe' _Sample_label . save_ save_heads_and_home-built_linear_amplifiers._4 _Saveframe_category NMR_applied_experiment _Experiment_name 'heads and home-built linear amplifiers.' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details ; Sample was in the oxidised state throughout the course of the data collection. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 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 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 ; ALA 458 and MET 532 have very upfield shifted H resonances. ; loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'DsbD C-terminal domain' _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 . 25 GLN C C 175.341 0.1 1 2 . 26 THR H H 8.250 0.01 1 3 . 26 THR HA H 4.32 0.01 1 4 . 26 THR HB H 4.23 0.01 1 5 . 26 THR HG2 H 1.18 0.01 1 6 . 26 THR C C 173.702 0.1 1 7 . 26 THR CA C 61.43 0.1 1 8 . 26 THR CB C 69.10 0.1 1 9 . 26 THR CG2 C 21.10 0.1 1 10 . 26 THR N N 115.364 0.1 1 11 . 27 GLN H H 8.457 0.01 1 12 . 27 GLN HA H 4.44 0.01 1 13 . 27 GLN HB2 H 2.10 0.01 2 14 . 27 GLN HB3 H 1.99 0.01 2 15 . 27 GLN HG2 H 2.34 0.01 2 16 . 27 GLN C C 175.226 0.1 1 17 . 27 GLN CA C 55.22 0.1 1 18 . 27 GLN CB C 29.08 0.1 1 19 . 27 GLN CG C 33.26 0.1 1 20 . 27 GLN N N 123.325 0.1 1 21 . 28 THR H H 8.260 0.01 1 22 . 28 THR HA H 4.32 0.01 1 23 . 28 THR HB H 4.23 0.01 1 24 . 28 THR HG2 H 1.13 0.01 1 25 . 28 THR C C 173.149 0.1 1 26 . 28 THR CA C 61.00 0.1 1 27 . 28 THR CB C 69.28 0.1 1 28 . 28 THR CG2 C 20.99 0.1 1 29 . 28 THR N N 115.846 0.1 1 30 . 29 HIS H H 8.270 0.01 1 31 . 29 HIS HA H 4.71 0.01 1 32 . 29 HIS HB2 H 3.06 0.01 2 33 . 29 HIS HB3 H 3.21 0.01 2 34 . 29 HIS C C 173.803 0.1 1 35 . 29 HIS CA C 54.45 0.1 1 36 . 29 HIS CB C 30.15 0.1 1 37 . 29 HIS N N 120.008 0.1 1 38 . 30 LEU H H 8.475 0.01 1 39 . 30 LEU HA H 4.04 0.01 1 40 . 30 LEU HB2 H 1.21 0.01 2 41 . 30 LEU HB3 H 0.62 0.01 2 42 . 30 LEU HG H 1.58 0.01 1 43 . 30 LEU HD1 H 0.34 0.01 2 44 . 30 LEU HD2 H 0.62 0.01 2 45 . 30 LEU C C 175.598 0.1 1 46 . 30 LEU CA C 53.84 0.1 1 47 . 30 LEU CB C 41.03 0.1 1 48 . 30 LEU CG C 25.94 0.1 1 49 . 30 LEU CD1 C 25.40 0.1 2 50 . 30 LEU CD2 C 22.85 0.1 2 51 . 30 LEU N N 122.169 0.1 1 52 . 31 ASN H H 8.422 0.01 1 53 . 31 ASN HA H 4.80 0.01 1 54 . 31 ASN HB2 H 2.72 0.01 2 55 . 31 ASN HB3 H 2.56 0.01 2 56 . 31 ASN HD21 H 7.459 0.01 2 57 . 31 ASN HD22 H 6.762 0.01 2 58 . 31 ASN C C 173.377 0.1 1 59 . 31 ASN CA C 51.54 0.1 1 60 . 31 ASN CB C 37.57 0.1 1 61 . 31 ASN CG C 176.405 0.1 1 62 . 31 ASN N N 122.063 0.1 1 63 . 31 ASN ND2 N 113.075 0.1 1 64 . 32 PHE H H 8.165 0.01 1 65 . 32 PHE HA H 4.29 0.01 1 66 . 32 PHE HB2 H 2.47 0.01 1 67 . 32 PHE HB3 H 2.47 0.01 1 68 . 32 PHE C C 176.557 0.1 1 69 . 32 PHE CA C 57.38 0.1 1 70 . 32 PHE CB C 40.98 0.1 1 71 . 32 PHE N N 121.703 0.1 1 72 . 33 THR H H 8.804 0.01 1 73 . 33 THR HA H 4.38 0.01 1 74 . 33 THR HB H 4.13 0.01 1 75 . 33 THR C C 172.874 0.1 1 76 . 33 THR CA C 62.51 0.1 1 77 . 33 THR CB C 68.91 0.1 1 78 . 33 THR N N 122.127 0.1 1 79 . 34 GLN H H 8.809 0.01 1 80 . 34 GLN HA H 5.00 0.01 1 81 . 34 GLN HB2 H 2.06 0.01 2 82 . 34 GLN HB3 H 1.94 0.01 2 83 . 34 GLN HG2 H 2.36 0.01 2 84 . 34 GLN C C 175.618 0.1 1 85 . 34 GLN CA C 54.67 0.1 1 86 . 34 GLN CB C 28.67 0.1 1 87 . 34 GLN CG C 33.24 0.1 1 88 . 34 GLN N N 127.939 0.1 1 89 . 35 ILE H H 8.619 0.01 1 90 . 35 ILE HA H 4.55 0.01 1 91 . 35 ILE HB H 1.71 0.01 1 92 . 35 ILE HG12 H 0.89 0.01 2 93 . 35 ILE HG13 H 1.23 0.01 2 94 . 35 ILE HG2 H 0.75 0.01 1 95 . 35 ILE HD1 H 0.66 0.01 1 96 . 35 ILE C C 173.995 0.1 1 97 . 35 ILE CA C 58.12 0.1 1 98 . 35 ILE CB C 41.73 0.1 1 99 . 35 ILE CG1 C 25.64 0.1 1 100 . 35 ILE CG2 C 18.82 0.1 1 101 . 35 ILE CD1 C 14.16 0.1 1 102 . 35 ILE N N 119.244 0.1 1 103 . 36 LYS H H 9.104 0.01 1 104 . 36 LYS HA H 4.81 0.01 1 105 . 36 LYS HB2 H 2.21 0.01 2 106 . 36 LYS HB3 H 1.73 0.01 2 107 . 36 LYS C C 174.108 0.1 1 108 . 36 LYS CA C 54.99 0.1 1 109 . 36 LYS CB C 34.63 0.1 1 110 . 36 LYS N N 122.720 0.1 1 111 . 37 THR H H 6.909 0.01 1 112 . 37 THR HA H 5.24 0.01 1 113 . 37 THR HB H 4.65 0.01 1 114 . 37 THR C C 175.245 0.1 1 115 . 37 THR CA C 57.22 0.1 1 116 . 37 THR CB C 72.66 0.1 1 117 . 37 THR N N 102.723 0.1 1 118 . 38 VAL H H 8.349 0.01 1 119 . 38 VAL HA H 3.17 0.01 1 120 . 38 VAL HB H 1.78 0.01 1 121 . 38 VAL HG1 H 0.82 0.01 2 122 . 38 VAL HG2 H 0.24 0.01 2 123 . 38 VAL C C 176.443 0.1 1 124 . 38 VAL CA C 65.68 0.1 1 125 . 38 VAL CB C 31.34 0.1 1 126 . 38 VAL CG1 C 22.68 0.1 2 127 . 38 VAL CG2 C 19.36 0.1 2 128 . 38 VAL N N 120.368 0.1 1 129 . 39 ASP H H 7.937 0.01 1 130 . 39 ASP HA H 4.35 0.01 1 131 . 39 ASP HB2 H 2.49 0.01 2 132 . 39 ASP HB3 H 2.58 0.01 2 133 . 39 ASP C C 178.606 0.1 1 134 . 39 ASP CA C 56.76 0.1 1 135 . 39 ASP CB C 39.61 0.1 1 136 . 39 ASP N N 117.791 0.1 1 137 . 40 GLU H H 7.974 0.01 1 138 . 40 GLU HA H 3.95 0.01 1 139 . 40 GLU HB2 H 2.00 0.01 2 140 . 40 GLU HB3 H 2.28 0.01 2 141 . 40 GLU HG2 H 2.41 0.01 2 142 . 40 GLU HG3 H 2.28 0.01 2 143 . 40 GLU C C 179.333 0.1 1 144 . 40 GLU CA C 58.84 0.1 1 145 . 40 GLU CB C 29.44 0.1 1 146 . 40 GLU CG C 36.49 0.1 1 147 . 40 GLU N N 120.982 0.1 1 148 . 41 LEU H H 8.267 0.01 1 149 . 41 LEU HA H 3.86 0.01 1 150 . 41 LEU HB2 H 2.17 0.01 2 151 . 41 LEU HB3 H 1.21 0.01 2 152 . 41 LEU HG H 1.38 0.01 1 153 . 41 LEU HD1 H 0.90 0.01 2 154 . 41 LEU HD2 H 0.57 0.01 2 155 . 41 LEU C C 176.430 0.1 1 156 . 41 LEU CA C 57.63 0.1 1 157 . 41 LEU CB C 39.66 0.1 1 158 . 41 LEU CG C 26.68 0.1 1 159 . 41 LEU CD1 C 26.88 0.1 2 160 . 41 LEU CD2 C 22.33 0.1 2 161 . 41 LEU N N 123.258 0.1 1 162 . 42 ASN H H 8.400 0.01 1 163 . 42 ASN HA H 4.36 0.01 1 164 . 42 ASN HB2 H 2.85 0.01 2 165 . 42 ASN HB3 H 2.74 0.01 2 166 . 42 ASN HD21 H 7.675 0.01 2 167 . 42 ASN HD22 H 6.396 0.01 2 168 . 42 ASN C C 177.787 0.1 1 169 . 42 ASN CA C 55.55 0.1 1 170 . 42 ASN CB C 36.70 0.1 1 171 . 42 ASN N N 117.153 0.1 1 172 . 42 ASN ND2 N 111.547 0.1 1 173 . 43 GLN H H 8.051 0.01 1 174 . 43 GLN HA H 4.03 0.01 1 175 . 43 GLN HB2 H 2.00 0.01 2 176 . 43 GLN HB3 H 2.12 0.01 2 177 . 43 GLN HG2 H 2.40 0.01 2 178 . 43 GLN C C 176.995 0.1 1 179 . 43 GLN CA C 57.88 0.1 1 180 . 43 GLN CB C 27.27 0.1 1 181 . 43 GLN CG C 32.58 0.1 1 182 . 43 GLN N N 120.327 0.1 1 183 . 44 ALA H H 8.104 0.01 1 184 . 44 ALA HA H 4.06 0.01 1 185 . 44 ALA HB H 1.39 0.01 1 186 . 44 ALA C C 180.361 0.1 1 187 . 44 ALA CA C 54.35 0.1 1 188 . 44 ALA CB C 17.75 0.1 1 189 . 44 ALA N N 123.333 0.1 1 190 . 45 LEU H H 8.257 0.01 1 191 . 45 LEU HA H 3.87 0.01 1 192 . 45 LEU HB2 H 1.92 0.01 2 193 . 45 LEU HB3 H 1.24 0.01 2 194 . 45 LEU HG H 1.49 0.01 1 195 . 45 LEU HD1 H 0.48 0.01 2 196 . 45 LEU HD2 H 0.07 0.01 2 197 . 45 LEU C C 179.420 0.1 1 198 . 45 LEU CA C 57.23 0.1 1 199 . 45 LEU CB C 40.44 0.1 1 200 . 45 LEU CG C 25.75 0.1 1 201 . 45 LEU CD1 C 24.66 0.1 2 202 . 45 LEU CD2 C 21.13 0.1 2 203 . 45 LEU N N 118.005 0.1 1 204 . 46 VAL H H 7.713 0.01 1 205 . 46 VAL HA H 3.66 0.01 1 206 . 46 VAL HB H 2.26 0.01 1 207 . 46 VAL HG1 H 1.06 0.01 2 208 . 46 VAL HG2 H 0.93 0.01 2 209 . 46 VAL C C 179.243 0.1 1 210 . 46 VAL CA C 65.91 0.1 1 211 . 46 VAL CB C 30.83 0.1 1 212 . 46 VAL CG1 C 22.23 0.1 2 213 . 46 VAL CG2 C 20.60 0.1 2 214 . 46 VAL N N 121.529 0.1 1 215 . 47 GLU H H 7.849 0.01 1 216 . 47 GLU HA H 4.04 0.01 1 217 . 47 GLU HB2 H 2.12 0.01 2 218 . 47 GLU HB3 H 2.02 0.01 2 219 . 47 GLU HG2 H 2.49 0.01 2 220 . 47 GLU HG3 H 2.30 0.01 2 221 . 47 GLU C C 176.601 0.1 1 222 . 47 GLU CA C 57.68 0.1 1 223 . 47 GLU CB C 28.60 0.1 1 224 . 47 GLU CG C 35.94 0.1 1 225 . 47 GLU N N 119.543 0.1 1 226 . 48 ALA H H 7.622 0.01 1 227 . 48 ALA HA H 4.34 0.01 1 228 . 48 ALA HB H 1.41 0.01 1 229 . 48 ALA C C 175.232 0.1 1 230 . 48 ALA CA C 51.73 0.1 1 231 . 48 ALA CB C 19.02 0.1 1 232 . 48 ALA N N 121.806 0.1 1 233 . 49 LYS H H 7.030 0.01 1 234 . 49 LYS HA H 4.09 0.01 1 235 . 49 LYS HB2 H 1.87 0.01 2 236 . 49 LYS HB3 H 1.82 0.01 2 237 . 49 LYS HG2 H 1.44 0.01 2 238 . 49 LYS HG3 H 1.57 0.01 2 239 . 49 LYS HD2 H 1.74 0.01 2 240 . 49 LYS HE2 H 3.02 0.01 2 241 . 49 LYS C C 176.864 0.1 1 242 . 49 LYS CA C 57.81 0.1 1 243 . 49 LYS CB C 31.07 0.1 1 244 . 49 LYS CG C 23.75 0.1 1 245 . 49 LYS CD C 28.50 0.1 1 246 . 49 LYS N N 118.084 0.1 1 247 . 50 GLY H H 9.144 0.01 1 248 . 50 GLY HA2 H 4.38 0.01 2 249 . 50 GLY HA3 H 3.75 0.01 2 250 . 50 GLY C C 173.347 0.1 1 251 . 50 GLY CA C 44.39 0.1 1 252 . 50 GLY N N 113.250 0.1 1 253 . 51 LYS H H 8.457 0.01 1 254 . 51 LYS HA H 4.83 0.01 1 255 . 51 LYS HB2 H 1.94 0.01 2 256 . 51 LYS HB3 H 1.79 0.01 2 257 . 51 LYS HG2 H 1.42 0.01 2 258 . 51 LYS HD2 H 1.65 0.01 2 259 . 51 LYS HD3 H 1.57 0.01 2 260 . 51 LYS HE2 H 2.94 0.01 1 261 . 51 LYS HE3 H 2.94 0.01 1 262 . 51 LYS CA C 53.13 0.1 1 263 . 51 LYS CB C 32.56 0.1 1 264 . 51 LYS CG C 24.50 0.1 1 265 . 51 LYS CD C 28.94 0.1 1 266 . 51 LYS N N 123.325 0.1 1 267 . 52 PRO HA H 4.52 0.01 1 268 . 52 PRO HB2 H 2.34 0.01 2 269 . 52 PRO HB3 H 2.07 0.01 2 270 . 52 PRO HG2 H 2.14 0.01 2 271 . 52 PRO HG3 H 1.84 0.01 2 272 . 52 PRO HD2 H 3.78 0.01 2 273 . 52 PRO HD3 H 3.88 0.01 2 274 . 52 PRO C C 174.690 0.1 1 275 . 52 PRO CA C 61.68 0.1 1 276 . 52 PRO CB C 31.49 0.1 1 277 . 52 PRO CG C 26.90 0.1 1 278 . 52 PRO CD C 49.38 0.1 1 279 . 53 VAL H H 8.067 0.01 1 280 . 53 VAL HA H 5.09 0.01 1 281 . 53 VAL HB H 1.80 0.01 1 282 . 53 VAL HG1 H 0.83 0.01 2 283 . 53 VAL HG2 H 0.65 0.01 2 284 . 53 VAL C C 174.380 0.1 1 285 . 53 VAL CA C 59.72 0.1 1 286 . 53 VAL CB C 35.91 0.1 1 287 . 53 VAL CG1 C 20.93 0.1 2 288 . 53 VAL CG2 C 20.77 0.1 2 289 . 53 VAL N N 119.112 0.1 1 290 . 54 MET H H 9.166 0.01 1 291 . 54 MET HA H 5.10 0.01 1 292 . 54 MET HB2 H 2.08 0.01 2 293 . 54 MET HB3 H 1.57 0.01 2 294 . 54 MET HG2 H 1.79 0.01 2 295 . 54 MET HG3 H 1.55 0.01 2 296 . 54 MET C C 171.770 0.1 1 297 . 54 MET CA C 53.39 0.1 1 298 . 54 MET CB C 37.85 0.1 1 299 . 54 MET CG C 33.12 0.1 1 300 . 54 MET N N 130.404 0.1 1 301 . 55 LEU H H 9.186 0.01 1 302 . 55 LEU HA H 5.27 0.01 1 303 . 55 LEU HB2 H 1.92 0.01 2 304 . 55 LEU HB3 H 1.09 0.01 2 305 . 55 LEU HG H 1.35 0.01 1 306 . 55 LEU HD1 H 0.89 0.01 2 307 . 55 LEU HD2 H 0.64 0.01 2 308 . 55 LEU C C 172.274 0.1 1 309 . 55 LEU CA C 51.84 0.1 1 310 . 55 LEU CB C 45.07 0.1 1 311 . 55 LEU CG C 27.13 0.1 1 312 . 55 LEU CD1 C 27.56 0.1 2 313 . 55 LEU CD2 C 23.12 0.1 2 314 . 55 LEU N N 128.732 0.1 1 315 . 56 ASP H H 8.926 0.01 1 316 . 56 ASP HA H 4.89 0.01 1 317 . 56 ASP HB2 H 2.23 0.01 2 318 . 56 ASP HB3 H 2.07 0.01 2 319 . 56 ASP C C 172.879 0.1 1 320 . 56 ASP CA C 52.93 0.1 1 321 . 56 ASP CB C 44.06 0.1 1 322 . 56 ASP N N 126.403 0.1 1 323 . 57 LEU H H 7.292 0.01 1 324 . 57 LEU HA H 4.87 0.01 1 325 . 57 LEU HB2 H 0.97 0.01 2 326 . 57 LEU HB3 H 2.06 0.01 2 327 . 57 LEU HG H 1.62 0.01 1 328 . 57 LEU HD1 H 0.71 0.01 2 329 . 57 LEU HD2 H 0.83 0.01 2 330 . 57 LEU C C 172.470 0.1 1 331 . 57 LEU CA C 53.15 0.1 1 332 . 57 LEU CB C 41.78 0.1 1 333 . 57 LEU CG C 26.44 0.1 1 334 . 57 LEU CD1 C 23.90 0.1 2 335 . 57 LEU CD2 C 27.35 0.1 2 336 . 57 LEU N N 125.412 0.1 1 337 . 58 TYR H H 8.746 0.01 1 338 . 58 TYR HA H 4.27 0.01 1 339 . 58 TYR HB2 H 2.82 0.01 2 340 . 58 TYR HB3 H 2.40 0.01 2 341 . 58 TYR C C 172.399 0.1 1 342 . 58 TYR CA C 56.99 0.1 1 343 . 58 TYR CB C 41.04 0.1 1 344 . 58 TYR N N 124.111 0.1 1 345 . 59 ALA H H 4.884 0.01 1 346 . 59 ALA HA H 3.73 0.01 1 347 . 59 ALA HB H -0.55 0.01 1 348 . 59 ALA C C 176.982 0.1 1 349 . 59 ALA CA C 50.29 0.1 1 350 . 59 ALA CB C 20.79 0.1 1 351 . 59 ALA N N 121.142 0.1 1 352 . 60 ASP H H 8.431 0.01 1 353 . 60 ASP HA H 4.16 0.01 1 354 . 60 ASP HB2 H 2.70 0.01 2 355 . 60 ASP HB3 H 2.52 0.01 2 356 . 60 ASP C C 174.852 0.1 1 357 . 60 ASP CA C 56.17 0.1 1 358 . 60 ASP CB C 40.58 0.1 1 359 . 60 ASP N N 120.183 0.1 1 360 . 61 TRP H H 5.957 0.01 1 361 . 61 TRP HA H 4.55 0.01 1 362 . 61 TRP HB2 H 3.68 0.01 2 363 . 61 TRP HB3 H 3.17 0.01 2 364 . 61 TRP HE1 H 10.754 0.01 1 365 . 61 TRP C C 174.878 0.1 1 366 . 61 TRP CA C 52.35 0.1 1 367 . 61 TRP CB C 27.91 0.1 1 368 . 61 TRP N N 109.621 0.1 1 369 . 61 TRP NE1 N 132.359 0.1 1 370 . 62 CYS H H 6.916 0.01 1 371 . 62 CYS HA H 4.78 0.01 1 372 . 62 CYS HB2 H 2.94 0.01 1 373 . 62 CYS HB3 H 2.94 0.01 1 374 . 62 CYS C C 172.694 0.1 1 375 . 62 CYS CA C 52.06 0.1 1 376 . 62 CYS CB C 42.32 0.1 1 377 . 62 CYS N N 121.691 0.1 1 378 . 63 VAL H H 8.675 0.01 1 379 . 63 VAL HA H 3.60 0.01 1 380 . 63 VAL HB H 2.06 0.01 1 381 . 63 VAL HG1 H 0.91 0.01 2 382 . 63 VAL HG2 H 1.09 0.01 2 383 . 63 VAL C C 178.750 0.1 1 384 . 63 VAL CA C 66.74 0.1 1 385 . 63 VAL CB C 30.93 0.1 1 386 . 63 VAL CG1 C 20.20 0.1 2 387 . 63 VAL CG2 C 21.87 0.1 2 388 . 63 VAL N N 133.583 0.1 1 389 . 64 ALA H H 9.316 0.01 1 390 . 64 ALA HA H 4.29 0.01 1 391 . 64 ALA HB H 1.50 0.01 1 392 . 64 ALA C C 178.750 0.1 1 393 . 64 ALA CA C 53.87 0.1 1 394 . 64 ALA CB C 18.50 0.1 1 395 . 64 ALA N N 121.680 0.1 1 396 . 65 CYS H H 8.516 0.01 1 397 . 65 CYS HA H 4.93 0.01 1 398 . 65 CYS HB2 H 3.81 0.01 2 399 . 65 CYS HB3 H 3.30 0.01 2 400 . 65 CYS C C 176.399 0.1 1 401 . 65 CYS CA C 63.06 0.1 1 402 . 65 CYS CB C 32.27 0.1 1 403 . 65 CYS N N 113.974 0.1 1 404 . 66 LYS H H 7.617 0.01 1 405 . 66 LYS HA H 4.20 0.01 1 406 . 66 LYS C C 178.787 0.1 1 407 . 66 LYS CA C 58.74 0.1 1 408 . 66 LYS CB C 30.90 0.1 1 409 . 66 LYS N N 121.395 0.1 1 410 . 67 GLU H H 8.024 0.01 1 411 . 67 GLU HA H 3.93 0.01 1 412 . 67 GLU HB2 H 1.43 0.01 2 413 . 67 GLU HB3 H 1.89 0.01 2 414 . 67 GLU HG2 H 2.23 0.01 2 415 . 67 GLU C C 178.583 0.1 1 416 . 67 GLU CA C 59.08 0.1 1 417 . 67 GLU CB C 28.43 0.1 1 418 . 67 GLU CG C 36.06 0.1 1 419 . 67 GLU N N 121.592 0.1 1 420 . 68 PHE H H 8.545 0.01 1 421 . 68 PHE HA H 4.06 0.01 1 422 . 68 PHE HB2 H 3.13 0.01 2 423 . 68 PHE HB3 H 1.90 0.01 2 424 . 68 PHE C C 178.624 0.1 1 425 . 68 PHE CA C 62.27 0.1 1 426 . 68 PHE CB C 38.37 0.1 1 427 . 68 PHE N N 121.006 0.1 1 428 . 69 GLU H H 7.368 0.01 1 429 . 69 GLU HA H 4.03 0.01 1 430 . 69 GLU HB2 H 2.26 0.01 2 431 . 69 GLU HG2 H 2.40 0.01 2 432 . 69 GLU C C 176.403 0.1 1 433 . 69 GLU CA C 58.99 0.1 1 434 . 69 GLU CB C 28.76 0.1 1 435 . 69 GLU CG C 34.70 0.1 1 436 . 69 GLU N N 118.228 0.1 1 437 . 70 LYS H H 7.742 0.01 1 438 . 70 LYS HA H 3.95 0.01 1 439 . 70 LYS HB2 H 1.39 0.01 2 440 . 70 LYS HB3 H 1.07 0.01 2 441 . 70 LYS HG2 H 1.08 0.01 2 442 . 70 LYS HG3 H 0.64 0.01 2 443 . 70 LYS HD2 H 1.39 0.01 2 444 . 70 LYS HD3 H 1.48 0.01 2 445 . 70 LYS HE2 H 2.77 0.01 1 446 . 70 LYS HE3 H 2.77 0.01 1 447 . 70 LYS C C 178.782 0.1 1 448 . 70 LYS CA C 58.29 0.1 1 449 . 70 LYS CB C 32.97 0.1 1 450 . 70 LYS CG C 24.10 0.1 1 451 . 70 LYS CD C 28.86 0.1 1 452 . 70 LYS CE C 41.35 0.1 1 453 . 70 LYS N N 116.394 0.1 1 454 . 71 TYR H H 8.485 0.01 1 455 . 71 TYR HA H 4.94 0.01 1 456 . 71 TYR HB2 H 3.43 0.01 2 457 . 71 TYR HB3 H 2.95 0.01 2 458 . 71 TYR C C 175.973 0.1 1 459 . 71 TYR CA C 58.14 0.1 1 460 . 71 TYR CB C 39.34 0.1 1 461 . 71 TYR N N 115.584 0.1 1 462 . 72 THR H H 7.719 0.01 1 463 . 72 THR HA H 4.38 0.01 1 464 . 72 THR HB H 4.12 0.01 1 465 . 72 THR C C 174.551 0.1 1 466 . 72 THR CA C 66.24 0.1 1 467 . 72 THR CB C 67.82 0.1 1 468 . 72 THR N N 117.821 0.1 1 469 . 73 PHE H H 8.931 0.01 1 470 . 73 PHE HA H 4.64 0.01 1 471 . 73 PHE HB2 H 3.56 0.01 2 472 . 73 PHE HB3 H 3.31 0.01 2 473 . 73 PHE C C 174.370 0.1 1 474 . 73 PHE CA C 55.30 0.1 1 475 . 73 PHE CB C 36.67 0.1 1 476 . 73 PHE N N 119.117 0.1 1 477 . 74 SER H H 7.071 0.01 1 478 . 74 SER HA H 4.26 0.01 1 479 . 74 SER HB2 H 4.02 0.01 2 480 . 74 SER HB3 H 3.80 0.01 2 481 . 74 SER C C 172.986 0.1 1 482 . 74 SER CA C 56.71 0.1 1 483 . 74 SER CB C 63.69 0.1 1 484 . 74 SER N N 107.859 0.1 1 485 . 75 ASP H H 7.392 0.01 1 486 . 75 ASP HA H 4.98 0.01 1 487 . 75 ASP HB2 H 3.06 0.01 2 488 . 75 ASP HB3 H 2.69 0.01 2 489 . 75 ASP CA C 51.61 0.1 1 490 . 75 ASP CB C 44.41 0.1 1 491 . 75 ASP N N 125.886 0.1 1 492 . 76 PRO HA H 4.25 0.01 1 493 . 76 PRO HB2 H 2.00 0.01 2 494 . 76 PRO HB3 H 2.41 0.01 2 495 . 76 PRO HG2 H 2.11 0.01 2 496 . 76 PRO HG3 H 2.15 0.01 2 497 . 76 PRO HD2 H 4.10 0.01 2 498 . 76 PRO HD3 H 3.89 0.01 2 499 . 76 PRO C C 178.559 0.1 1 500 . 76 PRO CA C 64.62 0.1 1 501 . 76 PRO CB C 31.72 0.1 1 502 . 76 PRO CG C 27.02 0.1 1 503 . 76 PRO CD C 50.70 0.1 1 504 . 77 GLN H H 8.642 0.01 1 505 . 77 GLN HA H 4.20 0.01 1 506 . 77 GLN HB2 H 2.29 0.01 2 507 . 77 GLN HB3 H 2.17 0.01 2 508 . 77 GLN HG2 H 2.47 0.01 2 509 . 77 GLN C C 179.135 0.1 1 510 . 77 GLN CA C 58.27 0.1 1 511 . 77 GLN CB C 27.37 0.1 1 512 . 77 GLN CG C 33.76 0.1 1 513 . 77 GLN N N 119.082 0.1 1 514 . 78 VAL H H 8.011 0.01 1 515 . 78 VAL HA H 3.59 0.01 1 516 . 78 VAL HB H 2.75 0.01 1 517 . 78 VAL HG1 H 1.22 0.01 2 518 . 78 VAL HG2 H 1.44 0.01 2 519 . 78 VAL C C 176.551 0.1 1 520 . 78 VAL CA C 65.78 0.1 1 521 . 78 VAL CB C 31.48 0.1 1 522 . 78 VAL CG1 C 21.95 0.1 2 523 . 78 VAL CG2 C 24.10 0.1 2 524 . 78 VAL N N 124.556 0.1 1 525 . 79 GLN H H 7.938 0.01 1 526 . 79 GLN HA H 3.74 0.01 1 527 . 79 GLN HB2 H 1.99 0.01 2 528 . 79 GLN HG2 H 2.20 0.01 2 529 . 79 GLN HG3 H 2.58 0.01 2 530 . 79 GLN C C 178.824 0.1 1 531 . 79 GLN CA C 59.12 0.1 1 532 . 79 GLN CB C 26.78 0.1 1 533 . 79 GLN CG C 33.11 0.1 1 534 . 79 GLN N N 116.622 0.1 1 535 . 80 LYS H H 7.898 0.01 1 536 . 80 LYS HA H 4.06 0.01 1 537 . 80 LYS HB2 H 1.90 0.01 2 538 . 80 LYS HG2 H 1.55 0.01 2 539 . 80 LYS HG3 H 1.45 0.01 2 540 . 80 LYS HD2 H 1.68 0.01 2 541 . 80 LYS HE2 H 2.97 0.01 2 542 . 80 LYS C C 178.780 0.1 1 543 . 80 LYS CA C 58.55 0.1 1 544 . 80 LYS CB C 31.67 0.1 1 545 . 80 LYS CG C 24.45 0.1 1 546 . 80 LYS CD C 28.62 0.1 1 547 . 80 LYS N N 119.273 0.1 1 548 . 81 ALA H H 7.827 0.01 1 549 . 81 ALA HA H 4.17 0.01 1 550 . 81 ALA HB H 1.55 0.01 1 551 . 81 ALA C C 178.873 0.1 1 552 . 81 ALA CA C 53.87 0.1 1 553 . 81 ALA CB C 18.23 0.1 1 554 . 81 ALA N N 122.586 0.1 1 555 . 82 LEU H H 7.493 0.01 1 556 . 82 LEU HA H 4.40 0.01 1 557 . 82 LEU HB2 H 1.68 0.01 2 558 . 82 LEU HB3 H 1.85 0.01 2 559 . 82 LEU HG H 1.78 0.01 1 560 . 82 LEU HD1 H 0.87 0.01 2 561 . 82 LEU HD2 H 1.03 0.01 2 562 . 82 LEU C C 176.659 0.1 1 563 . 82 LEU CA C 53.96 0.1 1 564 . 82 LEU CB C 41.83 0.1 1 565 . 82 LEU CG C 26.10 0.1 1 566 . 82 LEU CD1 C 26.38 0.1 2 567 . 82 LEU CD2 C 22.63 0.1 2 568 . 82 LEU N N 117.612 0.1 1 569 . 83 ALA H H 7.333 0.01 1 570 . 83 ALA HA H 4.07 0.01 1 571 . 83 ALA HB H 1.50 0.01 1 572 . 83 ALA C C 177.090 0.1 1 573 . 83 ALA CA C 54.84 0.1 1 574 . 83 ALA CB C 18.47 0.1 1 575 . 83 ALA N N 122.679 0.1 1 576 . 84 ASP H H 8.158 0.01 1 577 . 84 ASP HA H 4.81 0.01 1 578 . 84 ASP HB2 H 2.84 0.01 2 579 . 84 ASP HB3 H 2.61 0.01 2 580 . 84 ASP C C 174.182 0.1 1 581 . 84 ASP CA C 53.07 0.1 1 582 . 84 ASP CB C 40.56 0.1 1 583 . 84 ASP N N 116.498 0.1 1 584 . 85 THR H H 7.638 0.01 1 585 . 85 THR HA H 4.32 0.01 1 586 . 85 THR HB H 3.99 0.01 1 587 . 85 THR C C 172.674 0.1 1 588 . 85 THR CA C 61.96 0.1 1 589 . 85 THR CB C 69.95 0.1 1 590 . 85 THR N N 117.595 0.1 1 591 . 86 VAL H H 9.049 0.01 1 592 . 86 VAL HA H 3.84 0.01 1 593 . 86 VAL HB H 2.10 0.01 1 594 . 86 VAL HG1 H 0.87 0.01 2 595 . 86 VAL HG2 H 1.00 0.01 2 596 . 86 VAL C C 173.746 0.1 1 597 . 86 VAL CA C 63.35 0.1 1 598 . 86 VAL CB C 31.04 0.1 1 599 . 86 VAL CG1 C 19.64 0.1 2 600 . 86 VAL CG2 C 21.46 0.1 2 601 . 86 VAL N N 129.198 0.1 1 602 . 87 LEU H H 8.312 0.01 1 603 . 87 LEU HA H 4.92 0.01 1 604 . 87 LEU HB2 H 1.74 0.01 2 605 . 87 LEU HB3 H 0.87 0.01 2 606 . 87 LEU HG H 1.73 0.01 1 607 . 87 LEU HD1 H 0.41 0.01 2 608 . 87 LEU HD2 H 0.65 0.01 2 609 . 87 LEU C C 174.777 0.1 1 610 . 87 LEU CA C 53.20 0.1 1 611 . 87 LEU CB C 41.16 0.1 1 612 . 87 LEU CG C 25.23 0.1 1 613 . 87 LEU CD1 C 26.72 0.1 2 614 . 87 LEU CD2 C 24.30 0.1 2 615 . 87 LEU N N 128.731 0.1 1 616 . 88 LEU H H 9.372 0.01 1 617 . 88 LEU HA H 5.62 0.01 1 618 . 88 LEU HB2 H 1.76 0.01 2 619 . 88 LEU HB3 H 1.15 0.01 2 620 . 88 LEU HG H 1.50 0.01 1 621 . 88 LEU HD1 H 0.51 0.01 2 622 . 88 LEU HD2 H 0.72 0.01 2 623 . 88 LEU C C 174.588 0.1 1 624 . 88 LEU CA C 51.76 0.1 1 625 . 88 LEU CB C 46.07 0.1 1 626 . 88 LEU CG C 26.33 0.1 1 627 . 88 LEU CD1 C 21.73 0.1 2 628 . 88 LEU CD2 C 26.51 0.1 2 629 . 88 LEU N N 125.347 0.1 1 630 . 89 GLN H H 8.645 0.01 1 631 . 89 GLN HA H 5.36 0.01 1 632 . 89 GLN HB2 H 1.57 0.01 2 633 . 89 GLN HB3 H 1.01 0.01 2 634 . 89 GLN HG2 H 1.93 0.01 2 635 . 89 GLN HG3 H 1.57 0.01 2 636 . 89 GLN C C 171.873 0.1 1 637 . 89 GLN CA C 53.38 0.1 1 638 . 89 GLN CB C 33.76 0.1 1 639 . 89 GLN CG C 34.34 0.1 1 640 . 89 GLN N N 122.462 0.1 1 641 . 90 ALA H H 8.102 0.01 1 642 . 90 ALA HA H 5.17 0.01 1 643 . 90 ALA HB H 1.19 0.01 1 644 . 90 ALA C C 174.215 0.1 1 645 . 90 ALA CA C 49.78 0.1 1 646 . 90 ALA CB C 21.41 0.1 1 647 . 90 ALA N N 127.594 0.1 1 648 . 91 ASN H H 9.502 0.01 1 649 . 91 ASN HA H 5.23 0.01 1 650 . 91 ASN HB2 H 3.20 0.01 2 651 . 91 ASN HB3 H 2.73 0.01 2 652 . 91 ASN C C 175.783 0.1 1 653 . 91 ASN CA C 50.41 0.1 1 654 . 91 ASN CB C 37.27 0.1 1 655 . 91 ASN N N 122.139 0.1 1 656 . 92 VAL H H 8.669 0.01 1 657 . 92 VAL HA H 4.63 0.01 1 658 . 92 VAL HB H 2.64 0.01 1 659 . 92 VAL HG1 H 0.76 0.01 2 660 . 92 VAL HG2 H 0.90 0.01 2 661 . 92 VAL C C 175.967 0.1 1 662 . 92 VAL CA C 59.80 0.1 1 663 . 92 VAL CB C 29.68 0.1 1 664 . 92 VAL CG1 C 19.30 0.1 2 665 . 92 VAL CG2 C 20.01 0.1 2 666 . 92 VAL N N 115.721 0.1 1 667 . 93 THR H H 7.891 0.01 1 668 . 93 THR HA H 3.64 0.01 1 669 . 93 THR HB H 4.00 0.01 1 670 . 93 THR C C 174.674 0.1 1 671 . 93 THR CA C 67.11 0.1 1 672 . 93 THR CB C 69.50 0.1 1 673 . 93 THR N N 117.723 0.1 1 674 . 94 ALA H H 8.982 0.01 1 675 . 94 ALA HA H 4.15 0.01 1 676 . 94 ALA HB H 1.46 0.01 1 677 . 94 ALA C C 176.566 0.1 1 678 . 94 ALA CA C 53.37 0.1 1 679 . 94 ALA CB C 18.06 0.1 1 680 . 94 ALA N N 120.821 0.1 1 681 . 95 ASN H H 8.259 0.01 1 682 . 95 ASN HA H 4.32 0.01 1 683 . 95 ASN HB2 H 3.26 0.01 2 684 . 95 ASN HB3 H 2.53 0.01 2 685 . 95 ASN HD21 H 7.377 0.01 2 686 . 95 ASN HD22 H 6.227 0.01 2 687 . 95 ASN C C 173.985 0.1 1 688 . 95 ASN CA C 53.84 0.1 1 689 . 95 ASN CB C 38.02 0.1 1 690 . 95 ASN CG C 177.132 0.1 1 691 . 95 ASN N N 119.406 0.1 1 692 . 95 ASN ND2 N 110.875 0.1 1 693 . 96 ASP H H 8.993 0.01 1 694 . 96 ASP HA H 4.56 0.01 1 695 . 96 ASP HB2 H 3.25 0.01 2 696 . 96 ASP HB3 H 2.51 0.01 2 697 . 96 ASP C C 174.828 0.1 1 698 . 96 ASP CA C 52.59 0.1 1 699 . 96 ASP CB C 40.64 0.1 1 700 . 96 ASP N N 118.455 0.1 1 701 . 97 ALA H H 8.339 0.01 1 702 . 97 ALA HA H 4.02 0.01 1 703 . 97 ALA HB H 1.44 0.01 1 704 . 97 ALA C C 181.155 0.1 1 705 . 97 ALA CA C 55.12 0.1 1 706 . 97 ALA CB C 17.93 0.1 1 707 . 97 ALA N N 117.505 0.1 1 708 . 98 GLN H H 8.000 0.01 1 709 . 98 GLN HA H 4.20 0.01 1 710 . 98 GLN C C 177.562 0.1 1 711 . 98 GLN CA C 58.41 0.1 1 712 . 98 GLN CB C 27.63 0.1 1 713 . 98 GLN N N 118.444 0.1 1 714 . 99 ASP H H 8.639 0.01 1 715 . 99 ASP HA H 4.34 0.01 1 716 . 99 ASP HB2 H 3.18 0.01 2 717 . 99 ASP HB3 H 2.56 0.01 2 718 . 99 ASP C C 177.410 0.1 1 719 . 99 ASP CA C 56.85 0.1 1 720 . 99 ASP CB C 39.82 0.1 1 721 . 99 ASP N N 125.062 0.1 1 722 . 100 VAL H H 8.747 0.01 1 723 . 100 VAL HA H 3.56 0.01 1 724 . 100 VAL HB H 1.98 0.01 1 725 . 100 VAL HG1 H 0.94 0.01 1 726 . 100 VAL HG2 H 0.94 0.01 1 727 . 100 VAL C C 178.142 0.1 1 728 . 100 VAL CA C 65.72 0.1 1 729 . 100 VAL CB C 31.47 0.1 1 730 . 100 VAL CG1 C 20.43 0.1 2 731 . 100 VAL CG2 C 22.30 0.1 2 732 . 100 VAL N N 118.351 0.1 1 733 . 101 ALA H H 7.591 0.01 1 734 . 101 ALA HA H 4.17 0.01 1 735 . 101 ALA HB H 1.56 0.01 1 736 . 101 ALA C C 180.006 0.1 1 737 . 101 ALA CA C 54.55 0.1 1 738 . 101 ALA CB C 17.50 0.1 1 739 . 101 ALA N N 121.634 0.1 1 740 . 102 LEU H H 8.091 0.01 1 741 . 102 LEU HA H 4.02 0.01 1 742 . 102 LEU HB2 H 1.49 0.01 2 743 . 102 LEU HB3 H 2.21 0.01 2 744 . 102 LEU HG H 1.38 0.01 1 745 . 102 LEU HD1 H 0.67 0.01 2 746 . 102 LEU HD2 H 0.61 0.01 2 747 . 102 LEU C C 178.896 0.1 1 748 . 102 LEU CA C 57.83 0.1 1 749 . 102 LEU CB C 40.76 0.1 1 750 . 102 LEU CG C 26.60 0.1 1 751 . 102 LEU CD1 C 23.35 0.1 2 752 . 102 LEU CD2 C 25.59 0.1 2 753 . 102 LEU N N 122.907 0.1 1 754 . 103 LEU H H 8.389 0.01 1 755 . 103 LEU HA H 3.81 0.01 1 756 . 103 LEU HB2 H 1.55 0.01 2 757 . 103 LEU HB3 H 1.98 0.01 2 758 . 103 LEU HG H 1.99 0.01 1 759 . 103 LEU HD1 H 0.78 0.01 2 760 . 103 LEU HD2 H 0.92 0.01 2 761 . 103 LEU C C 177.240 0.1 1 762 . 103 LEU CA C 58.03 0.1 1 763 . 103 LEU CB C 40.27 0.1 1 764 . 103 LEU CG C 26.41 0.1 1 765 . 103 LEU CD1 C 22.82 0.1 2 766 . 103 LEU CD2 C 24.72 0.1 2 767 . 103 LEU N N 118.738 0.1 1 768 . 104 LYS H H 8.389 0.01 1 769 . 104 LYS HA H 4.22 0.01 1 770 . 104 LYS HB2 H 1.92 0.01 2 771 . 104 LYS HE2 H 2.96 0.01 2 772 . 104 LYS C C 179.845 0.1 1 773 . 104 LYS CA C 58.40 0.1 1 774 . 104 LYS CB C 31.83 0.1 1 775 . 104 LYS N N 118.738 0.1 1 776 . 105 HIS H H 8.294 0.01 1 777 . 105 HIS HA H 4.26 0.01 1 778 . 105 HIS HB2 H 3.38 0.01 2 779 . 105 HIS HB3 H 3.26 0.01 2 780 . 105 HIS C C 176.067 0.1 1 781 . 105 HIS CA C 58.97 0.1 1 782 . 105 HIS CB C 30.76 0.1 1 783 . 105 HIS N N 121.880 0.1 1 784 . 106 LEU H H 7.533 0.01 1 785 . 106 LEU HA H 4.13 0.01 1 786 . 106 LEU HB2 H 1.58 0.01 2 787 . 106 LEU HG H 1.93 0.01 1 788 . 106 LEU HD1 H 0.80 0.01 2 789 . 106 LEU HD2 H 0.90 0.01 2 790 . 106 LEU C C 174.982 0.1 1 791 . 106 LEU CA C 53.39 0.1 1 792 . 106 LEU CB C 42.71 0.1 1 793 . 106 LEU CG C 25.81 0.1 1 794 . 106 LEU CD1 C 26.22 0.1 2 795 . 106 LEU CD2 C 20.75 0.1 2 796 . 106 LEU N N 114.339 0.1 1 797 . 107 ASN H H 8.000 0.01 1 798 . 107 ASN HA H 4.30 0.01 1 799 . 107 ASN HB2 H 3.14 0.01 2 800 . 107 ASN HB3 H 2.65 0.01 2 801 . 107 ASN HD21 H 7.498 0.01 2 802 . 107 ASN HD22 H 6.674 0.01 2 803 . 107 ASN C C 173.566 0.1 1 804 . 107 ASN CA C 53.49 0.1 1 805 . 107 ASN CB C 36.33 0.1 1 806 . 107 ASN CG C 177.416 0.1 1 807 . 107 ASN N N 118.444 0.1 1 808 . 107 ASN ND2 N 112.408 0.1 1 809 . 108 VAL H H 8.100 0.01 1 810 . 108 VAL HA H 3.91 0.01 1 811 . 108 VAL HB H 1.88 0.01 1 812 . 108 VAL HG1 H 0.88 0.01 1 813 . 108 VAL HG2 H 0.88 0.01 1 814 . 108 VAL C C 175.087 0.1 1 815 . 108 VAL CA C 62.05 0.1 1 816 . 108 VAL CB C 32.23 0.1 1 817 . 108 VAL CG1 C 22.37 0.1 2 818 . 108 VAL CG2 C 21.03 0.1 2 819 . 108 VAL N N 119.709 0.1 1 820 . 109 LEU H H 8.633 0.01 1 821 . 109 LEU HA H 4.43 0.01 1 822 . 109 LEU HB2 H 1.64 0.01 2 823 . 109 LEU HG H 1.59 0.01 1 824 . 109 LEU HD1 H 0.79 0.01 2 825 . 109 LEU HD2 H 0.90 0.01 2 826 . 109 LEU C C 176.217 0.1 1 827 . 109 LEU CA C 54.66 0.1 1 828 . 109 LEU CB C 41.88 0.1 1 829 . 109 LEU CG C 26.65 0.1 1 830 . 109 LEU CD1 C 22.18 0.1 2 831 . 109 LEU CD2 C 24.31 0.1 2 832 . 109 LEU N N 128.878 0.1 1 833 . 110 GLY H H 7.361 0.01 1 834 . 110 GLY HA2 H 4.09 0.01 2 835 . 110 GLY HA3 H 3.95 0.01 2 836 . 110 GLY C C 169.246 0.1 1 837 . 110 GLY CA C 44.22 0.1 1 838 . 110 GLY N N 107.387 0.1 1 839 . 111 LEU H H 8.694 0.01 1 840 . 111 LEU HA H 4.48 0.01 1 841 . 111 LEU HB2 H 1.50 0.01 2 842 . 111 LEU HB3 H 1.59 0.01 2 843 . 111 LEU HG H 1.60 0.01 1 844 . 111 LEU HD1 H 0.54 0.01 1 845 . 111 LEU HD2 H 0.54 0.01 1 846 . 111 LEU CA C 51.92 0.1 1 847 . 111 LEU CB C 42.40 0.1 1 848 . 111 LEU CG C 28.78 0.1 1 849 . 111 LEU CD1 C 24.59 0.1 1 850 . 111 LEU CD2 C 24.59 0.1 1 851 . 111 LEU N N 120.927 0.1 1 852 . 112 PRO HA H 4.39 0.01 1 853 . 112 PRO HB2 H 2.65 0.01 2 854 . 112 PRO HB3 H 1.85 0.01 2 855 . 112 PRO HG2 H 1.68 0.01 2 856 . 112 PRO HG3 H 1.72 0.01 2 857 . 112 PRO HD2 H 3.47 0.01 2 858 . 112 PRO HD3 H 3.79 0.01 2 859 . 112 PRO C C 175.288 0.1 1 860 . 112 PRO CA C 61.92 0.1 1 861 . 112 PRO CB C 34.69 0.1 1 862 . 112 PRO CG C 23.72 0.1 1 863 . 112 PRO CD C 50.37 0.1 1 864 . 113 THR H H 8.389 0.01 1 865 . 113 THR HA H 5.16 0.01 1 866 . 113 THR HB H 3.91 0.01 1 867 . 113 THR C C 169.875 0.1 1 868 . 113 THR CA C 63.99 0.1 1 869 . 113 THR CB C 72.93 0.1 1 870 . 113 THR N N 118.738 0.1 1 871 . 114 ILE H H 8.750 0.01 1 872 . 114 ILE HA H 4.82 0.01 1 873 . 114 ILE HB H 1.67 0.01 1 874 . 114 ILE HG12 H 1.37 0.01 2 875 . 114 ILE HG13 H 1.23 0.01 2 876 . 114 ILE HG2 H 0.71 0.01 1 877 . 114 ILE HD1 H 0.17 0.01 1 878 . 114 ILE C C 174.259 0.1 1 879 . 114 ILE CA C 59.82 0.1 1 880 . 114 ILE CB C 39.74 0.1 1 881 . 114 ILE CG1 C 26.91 0.1 1 882 . 114 ILE CG2 C 18.48 0.1 1 883 . 114 ILE CD1 C 13.86 0.1 1 884 . 114 ILE N N 126.471 0.1 1 885 . 115 LEU H H 8.739 0.01 1 886 . 115 LEU HA H 4.90 0.01 1 887 . 115 LEU HB2 H 1.29 0.01 2 888 . 115 LEU HB3 H 1.45 0.01 2 889 . 115 LEU HG H 1.45 0.01 1 890 . 115 LEU HD1 H 0.85 0.01 2 891 . 115 LEU HD2 H 0.78 0.01 2 892 . 115 LEU C C 174.351 0.1 1 893 . 115 LEU CA C 53.82 0.1 1 894 . 115 LEU CB C 44.96 0.1 1 895 . 115 LEU CG C 28.90 0.1 1 896 . 115 LEU CD1 C 27.15 0.1 2 897 . 115 LEU CD2 C 27.45 0.1 2 898 . 115 LEU N N 125.518 0.1 1 899 . 116 PHE H H 9.963 0.01 1 900 . 116 PHE HA H 5.30 0.01 1 901 . 116 PHE HB2 H 3.15 0.01 2 902 . 116 PHE HB3 H 2.51 0.01 2 903 . 116 PHE C C 173.359 0.1 1 904 . 116 PHE CA C 56.50 0.1 1 905 . 116 PHE CB C 41.91 0.1 1 906 . 116 PHE N N 118.726 0.1 1 907 . 117 PHE H H 9.332 0.01 1 908 . 117 PHE HA H 5.38 0.01 1 909 . 117 PHE HB2 H 2.89 0.01 2 910 . 117 PHE HB3 H 2.64 0.01 2 911 . 117 PHE C C 175.856 0.1 1 912 . 117 PHE CA C 54.38 0.1 1 913 . 117 PHE CB C 40.76 0.1 1 914 . 117 PHE N N 120.081 0.1 1 915 . 118 ASP H H 8.655 0.01 1 916 . 118 ASP HA H 4.66 0.01 1 917 . 118 ASP HB2 H 3.36 0.01 2 918 . 118 ASP HB3 H 2.55 0.01 2 919 . 118 ASP C C 176.864 0.1 1 920 . 118 ASP CA C 51.50 0.1 1 921 . 118 ASP CB C 41.67 0.1 1 922 . 118 ASP N N 121.144 0.1 1 923 . 119 GLY H H 8.544 0.01 1 924 . 119 GLY HA2 H 4.17 0.01 2 925 . 119 GLY HA3 H 3.54 0.01 2 926 . 119 GLY C C 174.219 0.1 1 927 . 119 GLY CA C 45.72 0.1 1 928 . 119 GLY N N 104.367 0.1 1 929 . 120 GLN H H 8.539 0.01 1 930 . 120 GLN HA H 4.60 0.01 1 931 . 120 GLN HB2 H 2.17 0.01 2 932 . 120 GLN HG2 H 2.35 0.01 2 933 . 120 GLN C C 175.806 0.1 1 934 . 120 GLN CA C 54.57 0.1 1 935 . 120 GLN CB C 28.44 0.1 1 936 . 120 GLN CG C 34.02 0.1 1 937 . 120 GLN N N 118.703 0.1 1 938 . 121 GLY H H 8.365 0.01 1 939 . 121 GLY HA2 H 4.17 0.01 2 940 . 121 GLY HA3 H 3.54 0.01 2 941 . 121 GLY C C 172.636 0.1 1 942 . 121 GLY CA C 45.77 0.1 1 943 . 121 GLY N N 110.054 0.1 1 944 . 122 GLN H H 8.317 0.01 1 945 . 122 GLN HA H 4.59 0.01 1 946 . 122 GLN HG2 H 2.23 0.01 2 947 . 122 GLN HG3 H 2.33 0.01 2 948 . 122 GLN C C 175.482 0.1 1 949 . 122 GLN CA C 53.66 0.1 1 950 . 122 GLN CB C 28.83 0.1 1 951 . 122 GLN CG C 33.05 0.1 1 952 . 122 GLN N N 120.164 0.1 1 953 . 123 GLU H H 9.122 0.01 1 954 . 123 GLU HA H 4.10 0.01 1 955 . 123 GLU HG2 H 1.74 0.01 2 956 . 123 GLU HG3 H 1.62 0.01 2 957 . 123 GLU C C 176.710 0.1 1 958 . 123 GLU CA C 56.14 0.1 1 959 . 123 GLU CG C 35.50 0.1 1 960 . 123 GLU N N 128.752 0.1 1 961 . 124 HIS H H 8.274 0.01 1 962 . 124 HIS HA H 5.18 0.01 1 963 . 124 HIS HB2 H 3.06 0.01 2 964 . 124 HIS HB3 H 2.86 0.01 2 965 . 124 HIS CA C 52.93 0.1 1 966 . 124 HIS CB C 30.54 0.1 1 967 . 124 HIS N N 126.187 0.1 1 968 . 125 PRO HA H 4.51 0.01 1 969 . 125 PRO HB2 H 2.00 0.01 2 970 . 125 PRO HB3 H 2.36 0.01 2 971 . 125 PRO HG2 H 2.00 0.01 2 972 . 125 PRO HD2 H 3.90 0.01 2 973 . 125 PRO HD3 H 3.73 0.01 2 974 . 125 PRO C C 178.158 0.1 1 975 . 125 PRO CA C 64.34 0.1 1 976 . 125 PRO CB C 31.01 0.1 1 977 . 125 PRO CG C 26.78 0.1 1 978 . 125 PRO CD C 51.17 0.1 1 979 . 126 GLN H H 9.285 0.01 1 980 . 126 GLN HA H 4.28 0.01 1 981 . 126 GLN HB2 H 2.07 0.01 2 982 . 126 GLN HB3 H 2.16 0.01 2 983 . 126 GLN HG2 H 2.52 0.01 2 984 . 126 GLN HG3 H 2.45 0.01 2 985 . 126 GLN C C 175.730 0.1 1 986 . 126 GLN CA C 57.20 0.1 1 987 . 126 GLN CB C 26.76 0.1 1 988 . 126 GLN CG C 33.39 0.1 1 989 . 126 GLN N N 118.708 0.1 1 990 . 127 ALA H H 8.175 0.01 1 991 . 127 ALA HA H 4.42 0.01 1 992 . 127 ALA HB H 1.41 0.01 1 993 . 127 ALA C C 175.279 0.1 1 994 . 127 ALA CA C 50.38 0.1 1 995 . 127 ALA CB C 19.17 0.1 1 996 . 127 ALA N N 120.406 0.1 1 997 . 128 ARG H H 7.448 0.01 1 998 . 128 ARG HA H 4.94 0.01 1 999 . 128 ARG HB2 H 1.66 0.01 2 1000 . 128 ARG HB3 H 2.03 0.01 2 1001 . 128 ARG HG2 H 1.84 0.01 2 1002 . 128 ARG HG3 H 2.33 0.01 2 1003 . 128 ARG HD2 H 3.19 0.01 2 1004 . 128 ARG HD3 H 3.00 0.01 2 1005 . 128 ARG C C 176.874 0.1 1 1006 . 128 ARG CA C 57.88 0.1 1 1007 . 128 ARG CB C 31.67 0.1 1 1008 . 128 ARG CG C 28.68 0.1 1 1009 . 128 ARG CD C 43.64 0.1 1 1010 . 128 ARG N N 118.617 0.1 1 1011 . 129 VAL H H 8.814 0.01 1 1012 . 129 VAL HA H 4.43 0.01 1 1013 . 129 VAL HB H 2.19 0.01 1 1014 . 129 VAL HG1 H 0.97 0.01 2 1015 . 129 VAL HG2 H 1.41 0.01 2 1016 . 129 VAL C C 176.094 0.1 1 1017 . 129 VAL CA C 61.56 0.1 1 1018 . 129 VAL CB C 33.65 0.1 1 1019 . 129 VAL CG1 C 20.34 0.1 2 1020 . 129 VAL CG2 C 21.93 0.1 2 1021 . 129 VAL N N 125.623 0.1 1 1022 . 130 THR H H 8.887 0.01 1 1023 . 130 THR HA H 5.17 0.01 1 1024 . 130 THR HB H 4.75 0.01 1 1025 . 130 THR C C 173.171 0.1 1 1026 . 130 THR CA C 59.82 0.1 1 1027 . 130 THR CB C 68.65 0.1 1 1028 . 130 THR N N 115.721 0.1 1 1029 . 131 GLY H H 7.456 0.01 1 1030 . 131 GLY HA2 H 4.17 0.01 2 1031 . 131 GLY HA3 H 3.92 0.01 2 1032 . 131 GLY C C 170.329 0.1 1 1033 . 131 GLY CA C 43.65 0.1 1 1034 . 131 GLY N N 108.629 0.1 1 1035 . 132 PHE H H 8.787 0.01 1 1036 . 132 PHE HA H 3.70 0.01 1 1037 . 132 PHE HB2 H 2.90 0.01 2 1038 . 132 PHE HB3 H 2.58 0.01 2 1039 . 132 PHE C C 173.941 0.1 1 1040 . 132 PHE CA C 59.92 0.1 1 1041 . 132 PHE CB C 38.48 0.1 1 1042 . 132 PHE N N 117.518 0.1 1 1043 . 133 MET H H 4.865 0.01 1 1044 . 133 MET HA H 4.12 0.01 1 1045 . 133 MET HB2 H 1.86 0.01 2 1046 . 133 MET HB3 H 1.58 0.01 2 1047 . 133 MET HG2 H 2.71 0.01 2 1048 . 133 MET HG3 H 2.34 0.01 2 1049 . 133 MET C C 171.523 0.1 1 1050 . 133 MET CA C 54.20 0.1 1 1051 . 133 MET CB C 37.64 0.1 1 1052 . 133 MET CG C 32.33 0.1 1 1053 . 133 MET N N 127.224 0.1 1 1054 . 134 ASP H H 7.886 0.01 1 1055 . 134 ASP HA H 3.94 0.01 1 1056 . 134 ASP HB2 H 3.20 0.01 2 1057 . 134 ASP HB3 H 2.63 0.01 2 1058 . 134 ASP C C 173.914 0.1 1 1059 . 134 ASP CA C 51.67 0.1 1 1060 . 134 ASP CB C 39.44 0.1 1 1061 . 134 ASP N N 119.273 0.1 1 1062 . 135 ALA H H 8.705 0.01 1 1063 . 135 ALA HA H 4.08 0.01 1 1064 . 135 ALA HB H 1.67 0.01 1 1065 . 135 ALA C C 179.400 0.1 1 1066 . 135 ALA CA C 56.18 0.1 1 1067 . 135 ALA CB C 18.56 0.1 1 1068 . 135 ALA N N 120.309 0.1 1 1069 . 136 GLU H H 8.593 0.01 1 1070 . 136 GLU HA H 4.01 0.01 1 1071 . 136 GLU HB2 H 2.11 0.01 2 1072 . 136 GLU HB3 H 2.02 0.01 2 1073 . 136 GLU HG2 H 2.32 0.01 2 1074 . 136 GLU C C 178.953 0.1 1 1075 . 136 GLU CA C 59.30 0.1 1 1076 . 136 GLU CB C 29.06 0.1 1 1077 . 136 GLU CG C 35.82 0.1 1 1078 . 136 GLU N N 120.054 0.1 1 1079 . 137 THR H H 8.604 0.01 1 1080 . 137 THR HA H 3.95 0.01 1 1081 . 137 THR HB H 4.06 0.01 1 1082 . 137 THR C C 176.471 0.1 1 1083 . 137 THR CA C 66.25 0.1 1 1084 . 137 THR CB C 67.74 0.1 1 1085 . 137 THR N N 119.752 0.1 1 1086 . 138 PHE H H 9.669 0.01 1 1087 . 138 PHE HA H 4.69 0.01 1 1088 . 138 PHE HB2 H 3.13 0.01 2 1089 . 138 PHE HB3 H 2.84 0.01 2 1090 . 138 PHE C C 176.911 0.1 1 1091 . 138 PHE CA C 60.23 0.1 1 1092 . 138 PHE CB C 39.34 0.1 1 1093 . 138 PHE N N 125.227 0.1 1 1094 . 139 SER H H 8.666 0.01 1 1095 . 139 SER HA H 3.93 0.01 1 1096 . 139 SER HB2 H 4.01 0.01 2 1097 . 139 SER HB3 H 3.79 0.01 2 1098 . 139 SER C C 176.116 0.1 1 1099 . 139 SER CA C 62.71 0.1 1 1100 . 139 SER CB C 61.91 0.1 1 1101 . 139 SER N N 114.955 0.1 1 1102 . 140 ALA H H 7.615 0.01 1 1103 . 140 ALA HA H 3.98 0.01 1 1104 . 140 ALA HB H 1.53 0.01 1 1105 . 140 ALA C C 177.787 0.1 1 1106 . 140 ALA CA C 54.63 0.1 1 1107 . 140 ALA CB C 17.16 0.1 1 1108 . 140 ALA N N 125.403 0.1 1 1109 . 141 HIS H H 8.043 0.01 1 1110 . 141 HIS HA H 4.01 0.01 1 1111 . 141 HIS HB2 H 3.33 0.01 2 1112 . 141 HIS HB3 H 3.03 0.01 2 1113 . 141 HIS C C 177.090 0.1 1 1114 . 141 HIS CA C 59.98 0.1 1 1115 . 141 HIS CB C 30.60 0.1 1 1116 . 141 HIS N N 120.982 0.1 1 1117 . 142 LEU H H 8.185 0.01 1 1118 . 142 LEU HA H 3.47 0.01 1 1119 . 142 LEU HB2 H 1.78 0.01 2 1120 . 142 LEU HB3 H 1.26 0.01 2 1121 . 142 LEU HG H 1.29 0.01 1 1122 . 142 LEU HD1 H 0.63 0.01 2 1123 . 142 LEU HD2 H 0.52 0.01 2 1124 . 142 LEU C C 178.726 0.1 1 1125 . 142 LEU CA C 56.55 0.1 1 1126 . 142 LEU CB C 40.25 0.1 1 1127 . 142 LEU CG C 25.14 0.1 1 1128 . 142 LEU CD1 C 26.26 0.1 2 1129 . 142 LEU CD2 C 22.55 0.1 2 1130 . 142 LEU N N 117.799 0.1 1 1131 . 143 ARG H H 7.736 0.01 1 1132 . 143 ARG HA H 3.86 0.01 1 1133 . 143 ARG HB2 H 1.88 0.01 2 1134 . 143 ARG HG2 H 1.76 0.01 2 1135 . 143 ARG HG3 H 1.45 0.01 2 1136 . 143 ARG HD2 H 3.18 0.01 2 1137 . 143 ARG C C 177.665 0.1 1 1138 . 143 ARG CA C 58.58 0.1 1 1139 . 143 ARG CB C 29.63 0.1 1 1140 . 143 ARG CG C 26.38 0.1 1 1141 . 143 ARG CD C 42.90 0.1 1 1142 . 143 ARG N N 119.241 0.1 1 1143 . 144 ASP H H 7.882 0.01 1 1144 . 144 ASP HA H 4.53 0.01 1 1145 . 144 ASP HB2 H 2.55 0.01 2 1146 . 144 ASP C C 177.229 0.1 1 1147 . 144 ASP CA C 55.64 0.1 1 1148 . 144 ASP CB C 41.32 0.1 1 1149 . 144 ASP N N 116.073 0.1 1 1150 . 145 ARG H H 8.198 0.01 1 1151 . 145 ARG HA H 4.23 0.01 1 1152 . 145 ARG HB2 H 0.96 0.01 2 1153 . 145 ARG HB3 H 1.27 0.01 2 1154 . 145 ARG HG2 H 1.18 0.01 2 1155 . 145 ARG HD2 H 2.83 0.01 2 1156 . 145 ARG HD3 H 2.95 0.01 2 1157 . 145 ARG CA C 54.67 0.1 1 1158 . 145 ARG CB C 30.79 0.1 1 1159 . 145 ARG CD C 42.26 0.1 1 1160 . 145 ARG N N 115.647 0.1 1 1161 . 147 PRO HA H 4.38 0.01 1 1162 . 147 PRO HB2 H 2.28 0.01 2 1163 . 147 PRO HB3 H 1.90 0.01 2 1164 . 147 PRO HG2 H 2.01 0.01 2 1165 . 147 PRO HG3 H 1.99 0.01 2 1166 . 147 PRO HD2 H 3.77 0.01 2 1167 . 147 PRO HD3 H 3.65 0.01 2 1168 . 147 PRO CA C 62.52 0.1 1 1169 . 147 PRO CB C 31.43 0.1 1 1170 . 147 PRO CG C 26.85 0.1 1 1171 . 147 PRO CD C 50.07 0.1 1 stop_ save_