data_6305 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Mainchain proton, carbon and nitrogen chemical shifts for the C-domain of human RanGAP1 ; _BMRB_accession_number 6305 _BMRB_flat_file_name bmr6305.str _Entry_type original _Submission_date 2004-08-27 _Accession_date 2004-08-27 _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 Macauley Matthew S. . 2 Errington Wesley J. . 3 Okon Mark . . 4 Scharpf Manuela . . 5 Mackereth Cameron D. . 6 Schulman Brenda A. . 7 McIntosh Lawrence P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 152 "13C chemical shifts" 459 "15N chemical shifts" 152 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-11-29 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6304 SUMO-1 6306 'Sumoylated RanGAP1' stop_ _Original_release_date 2004-11-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural and Dynamic Independence of Isopeptide-linked RanGAP1 and SUMO-1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15355965 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Macauley Matthew S. . 2 Errington Wesley J. . 3 Okon Mark . . 4 Scharpf Manuela . . 5 Mackereth Cameron D. . 6 Schulman Brenda A. . 7 McIntosh Lawrence P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 279 _Journal_issue 47 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 49131 _Page_last 49137 _Year 2004 _Details . loop_ _Keyword Sumo-1 RanGAP1 stop_ save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name 'RanGAP1 C-domain' _Abbreviation_common 'RanGAP1 C-domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RanGAP1 C-domain' $RanGAP1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'C-domain of Ran GTP-activating protein, site of sumoylation' stop_ _Database_query_date . _Details 'C-domain (residues 420-587) of human RanGAP1' save_ ######################## # Monomeric polymers # ######################## save_RanGAP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RanGAP1 _Abbreviation_common RanGAP1 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Ran-GTP activating protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 172 _Mol_residue_sequence ; GSHMGEPAPVLSSPPPADVS TFLAFPSPEKLLRLGPKSSV LIAQQTDTSDPEKVVSAFLK VSSVFKDEATVTMAVQDAVD ALMQKAFNSSSFNSNTFLTR LLVHMGLLKSEDKVKAIANL YGPLMALNHMVQQDYFPKAL APLLLAFVTKPNSALESCSF ARHSLLQTLYKV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 GLY 2 -3 SER 3 -2 HIS 4 -1 MET 5 420 GLY 6 421 GLU 7 422 PRO 8 423 ALA 9 424 PRO 10 425 VAL 11 426 LEU 12 427 SER 13 428 SER 14 429 PRO 15 430 PRO 16 431 PRO 17 432 ALA 18 433 ASP 19 434 VAL 20 435 SER 21 436 THR 22 437 PHE 23 438 LEU 24 439 ALA 25 440 PHE 26 441 PRO 27 442 SER 28 443 PRO 29 444 GLU 30 445 LYS 31 446 LEU 32 447 LEU 33 448 ARG 34 449 LEU 35 450 GLY 36 451 PRO 37 452 LYS 38 453 SER 39 454 SER 40 455 VAL 41 456 LEU 42 457 ILE 43 458 ALA 44 459 GLN 45 460 GLN 46 461 THR 47 462 ASP 48 463 THR 49 464 SER 50 465 ASP 51 466 PRO 52 467 GLU 53 468 LYS 54 469 VAL 55 470 VAL 56 471 SER 57 472 ALA 58 473 PHE 59 474 LEU 60 475 LYS 61 476 VAL 62 477 SER 63 478 SER 64 479 VAL 65 480 PHE 66 481 LYS 67 482 ASP 68 483 GLU 69 484 ALA 70 485 THR 71 486 VAL 72 487 THR 73 488 MET 74 489 ALA 75 490 VAL 76 491 GLN 77 492 ASP 78 493 ALA 79 494 VAL 80 495 ASP 81 496 ALA 82 497 LEU 83 498 MET 84 499 GLN 85 500 LYS 86 501 ALA 87 502 PHE 88 503 ASN 89 504 SER 90 505 SER 91 506 SER 92 507 PHE 93 508 ASN 94 509 SER 95 510 ASN 96 511 THR 97 512 PHE 98 513 LEU 99 514 THR 100 515 ARG 101 516 LEU 102 517 LEU 103 518 VAL 104 519 HIS 105 520 MET 106 521 GLY 107 522 LEU 108 523 LEU 109 524 LYS 110 525 SER 111 526 GLU 112 527 ASP 113 528 LYS 114 529 VAL 115 530 LYS 116 531 ALA 117 532 ILE 118 533 ALA 119 534 ASN 120 535 LEU 121 536 TYR 122 537 GLY 123 538 PRO 124 539 LEU 125 540 MET 126 541 ALA 127 542 LEU 128 543 ASN 129 544 HIS 130 545 MET 131 546 VAL 132 547 GLN 133 548 GLN 134 549 ASP 135 550 TYR 136 551 PHE 137 552 PRO 138 553 LYS 139 554 ALA 140 555 LEU 141 556 ALA 142 557 PRO 143 558 LEU 144 559 LEU 145 560 LEU 146 561 ALA 147 562 PHE 148 563 VAL 149 564 THR 150 565 LYS 151 566 PRO 152 567 ASN 153 568 SER 154 569 ALA 155 570 LEU 156 571 GLU 157 572 SER 158 573 CYS 159 574 SER 160 575 PHE 161 576 ALA 162 577 ARG 163 578 HIS 164 579 SER 165 580 LEU 166 581 LEU 167 582 GLN 168 583 THR 169 584 LEU 170 585 TYR 171 586 LYS 172 587 VAL 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 6306 Sumoylated_RanGAP1 100.00 172 99.42 99.42 7.50e-118 PDB 1Z5S "Crystal Structure Of A Complex Between Ubc9, Sumo-1, Rangap1 And Nup358RANBP2" 98.84 172 98.24 98.82 4.21e-114 PDB 2GRN "Crystal Structure Of Human Rangap1-Ubc9" 97.67 170 99.40 99.40 3.85e-114 PDB 2GRO "Crystal Structure Of Human Rangap1-Ubc9-N85q" 97.67 170 99.40 99.40 3.85e-114 PDB 2GRP "Crystal Structure Of Human Rangap1-Ubc9-Y87a" 97.67 170 99.40 99.40 3.85e-114 PDB 2GRQ "Crystal Structure Of Human Rangap1-Ubc9-D127a" 97.67 170 99.40 99.40 3.85e-114 PDB 2GRR "Crystal Structure Of Human Rangap1-Ubc9-D127s" 97.67 170 99.40 99.40 3.85e-114 PDB 2IO2 "Crystal Structure Of Human Senp2 In Complex With Rangap1-sumo-1" 98.84 172 97.65 98.24 1.27e-112 PDB 2IO3 "Crystal Structure Of Human Senp2 In Complex With Rangap1- Sumo-2" 98.84 172 97.65 98.24 1.27e-112 PDB 2IY0 "Senp1 (Mutant) Sumo1 Rangap" 90.70 156 99.36 99.36 6.06e-105 PDB 3UIN "Complex Between Human Rangap1-sumo2, Ubc9 And The Ir1 Domain From Ranbp2" 97.67 171 99.40 99.40 3.31e-114 PDB 3UIO "Complex Between Human Rangap1-sumo2, Ubc9 And The Ir1 Domain From Ranbp2 Containing Ir2 Motif Ii" 97.67 171 99.40 99.40 3.31e-114 PDB 3UIP "Complex Between Human Rangap1-sumo1, Ubc9 And The Ir1 Domain From Ranbp2 Containing Ir2 Motif Ii" 97.67 171 99.40 99.40 3.31e-114 DBJ BAB47464 "KIAA1835 protein [Homo sapiens]" 98.84 623 98.24 98.82 7.54e-111 DBJ BAG10161 "Ran GTPase-activating protein 1 [synthetic construct]" 98.84 587 98.24 98.82 6.31e-112 DBJ BAG63578 "unnamed protein product [Homo sapiens]" 98.84 532 98.24 98.82 1.16e-111 DBJ BAG64552 "unnamed protein product [Homo sapiens]" 98.84 373 98.24 98.82 6.63e-114 EMBL CAA57714 "RanGAP1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 EMBL CAG30443 "RANGAP1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 EMBL CAK54588 "RANGAP1 [synthetic construct]" 98.84 587 98.24 98.82 6.31e-112 EMBL CAK54887 "RANGAP1 [synthetic construct]" 98.84 587 98.24 98.82 6.31e-112 GB AAH04990 "Unknown (protein for IMAGE:2905857), partial [Homo sapiens]" 98.84 213 98.24 98.82 4.03e-115 GB AAH14044 "Ran GTPase activating protein 1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 GB AAH41396 "RANGAP1 protein [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 GB AIC55014 "RANGAP1, partial [synthetic construct]" 98.84 587 98.24 98.82 6.31e-112 GB EAW60420 "Ran GTPase activating protein 1, isoform CRA_a [Homo sapiens]" 98.26 669 98.22 98.82 3.70e-109 REF NP_001265580 "ran GTPase-activating protein 1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 REF NP_002874 "ran GTPase-activating protein 1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 REF XP_005261752 "PREDICTED: ran GTPase-activating protein 1 isoform X1 [Homo sapiens]" 98.84 642 98.24 98.82 3.47e-110 REF XP_005261753 "PREDICTED: ran GTPase-activating protein 1 isoform X2 [Homo sapiens]" 98.84 628 98.24 98.82 5.59e-111 REF XP_006724352 "PREDICTED: ran GTPase-activating protein 1 isoform X3 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 SP P46060 "RecName: Full=Ran GTPase-activating protein 1; Short=RanGAP1 [Homo sapiens]" 98.84 587 98.24 98.82 6.31e-112 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RanGAP1 Human 9606 Eukaryota Animalia Homo sapian stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $RanGAP1 'recombinant technology' 'E. coli' Escherichia coli BL21 pET28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RanGAP1 . mM . KCl 100 mM . KPhos 10 mM . DTT 2 mM . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe _Version . _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_15N-editted_NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-editted NOESY-HSQC' _Sample_label . save_ save_15N-editted_TOCSY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-editted TOCSY-HSQC' _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 HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-editted NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-editted TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 pH temperature 303 0 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 external direct cylindrical 'outside sample' parallel 1.0 DSS C 13 'methyl carbon' ppm 0 external direct cylindrical 'outside sample' parallel . DSS N 15 nitrogen ppm 0 external indirect cylindrical 'outside sample' parallel 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RanGAP1 C-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 -1 4 MET C C 176.4 0.1 1 2 -1 4 MET CA C 55.68 0.3 1 3 -1 4 MET CB C 32.61 0.3 1 4 420 5 GLY N N 110.22 0.1 1 5 420 5 GLY H H 8.34 0.02 1 6 420 5 GLY C C 173.65 0.1 1 7 420 5 GLY CA C 45.09 0.3 1 8 421 6 GLU N N 121.81 0.1 1 9 421 6 GLU H H 8.16 0.02 1 10 421 6 GLU CA C 54.31 0.3 1 11 421 6 GLU CB C 29.87 0.3 1 12 422 7 PRO CA C 62.95 0.3 1 13 422 7 PRO CB C 32.06 0.3 1 14 423 8 ALA N N 125.65 0.1 1 15 423 8 ALA H H 8.3 0.02 1 16 423 8 ALA CA C 50.35 0.3 1 17 423 8 ALA CB C 18.17 0.3 1 18 424 9 PRO C C 176.72 0.1 1 19 424 9 PRO CA C 62.95 0.3 1 20 424 9 PRO CB C 32.06 0.3 1 21 425 10 VAL N N 120.89 0.1 1 22 425 10 VAL H H 8.21 0.02 1 23 425 10 VAL C C 176.19 0.1 1 24 425 10 VAL CA C 62.4 0.3 1 25 425 10 VAL CB C 32.62 0.3 1 26 426 11 LEU N N 126.53 0.1 1 27 426 11 LEU H H 8.34 0.02 1 28 426 11 LEU C C 177.13 0.1 1 29 426 11 LEU CA C 54.89 0.3 1 30 426 11 LEU CB C 42.5 0.3 1 31 427 12 SER N N 116.81 0.1 1 32 427 12 SER H H 8.24 0.02 1 33 427 12 SER C C 174.04 0.1 1 34 427 12 SER CA C 58.11 0.3 1 35 427 12 SER CB C 63.88 0.3 1 36 428 13 SER N N 118.64 0.1 1 37 428 13 SER H H 8.22 0.02 1 38 428 13 SER CA C 56.42 0.3 1 39 428 13 SER CB C 63.41 0.3 1 40 431 16 PRO C C 177.43 0.1 1 41 431 16 PRO CA C 63.5 0.3 1 42 431 16 PRO CB C 32.06 0.3 1 43 432 17 ALA N N 123.33 0.1 1 44 432 17 ALA H H 8.37 0.02 1 45 432 17 ALA C C 177.82 0.1 1 46 432 17 ALA CA C 53.14 0.3 1 47 432 17 ALA CB C 19.18 0.3 1 48 433 18 ASP N N 119.07 0.1 1 49 433 18 ASP H H 8.15 0.02 1 50 433 18 ASP C C 178.25 0.1 1 51 433 18 ASP CA C 54.85 0.3 1 52 433 18 ASP CB C 41.06 0.3 1 53 434 19 VAL N N 122.71 0.1 1 54 434 19 VAL H H 8.34 0.02 1 55 434 19 VAL CA C 65.85 0.3 1 56 434 19 VAL CB C 31.6 0.3 1 57 435 20 SER N N 116.55 0.1 1 58 435 20 SER H H 8.26 0.02 1 59 435 20 SER C C 177.38 0.1 1 60 435 20 SER CA C 62.21 0.3 1 61 436 21 THR N N 118.26 0.1 1 62 436 21 THR H H 8.22 0.02 1 63 436 21 THR C C 175.99 0.1 1 64 436 21 THR CA C 66.06 0.3 1 65 436 21 THR CB C 68.2 0.3 1 66 437 22 PHE N N 122.25 0.1 1 67 437 22 PHE H H 7.62 0.02 1 68 437 22 PHE C C 174.01 0.1 1 69 437 22 PHE CA C 61.66 0.3 1 70 437 22 PHE CB C 38.51 0.3 1 71 438 23 LEU N N 114.76 0.1 1 72 438 23 LEU H H 7.84 0.02 1 73 438 23 LEU C C 177.87 0.1 1 74 438 23 LEU CA C 57.02 0.3 1 75 438 23 LEU CB C 41.46 0.3 1 76 439 24 ALA N N 119.33 0.1 1 77 439 24 ALA H H 7.51 0.02 1 78 439 24 ALA C C 178.06 0.1 1 79 439 24 ALA CA C 54.32 0.3 1 80 439 24 ALA CB C 19.36 0.3 1 81 440 25 PHE N N 114.8 0.1 1 82 440 25 PHE H H 7.35 0.02 1 83 440 25 PHE CA C 54.58 0.3 1 84 440 25 PHE CB C 39.69 0.3 1 85 441 26 PRO CA C 64.88 0.3 1 86 441 26 PRO CB C 32.52 0.3 1 87 442 27 SER N N 114.53 0.1 1 88 442 27 SER H H 7.17 0.02 1 89 442 27 SER CA C 56.42 0.3 1 90 442 27 SER CB C 63.96 0.3 1 91 443 28 PRO C C 177.59 0.1 1 92 443 28 PRO CA C 65.98 0.3 1 93 443 28 PRO CB C 31.41 0.3 1 94 444 29 GLU N N 116.46 0.1 1 95 444 29 GLU H H 8.77 0.02 1 96 444 29 GLU C C 179.43 0.1 1 97 444 29 GLU CA C 60.45 0.3 1 98 444 29 GLU CB C 28.59 0.3 1 99 445 30 LYS N N 117.75 0.1 1 100 445 30 LYS H H 7.77 0.02 1 101 445 30 LYS C C 178.6 0.1 1 102 445 30 LYS CA C 59.63 0.3 1 103 445 30 LYS CB C 34.97 0.3 1 104 446 31 LEU N N 119.66 0.1 1 105 446 31 LEU H H 7.62 0.02 1 106 446 31 LEU CA C 57.39 0.3 1 107 446 31 LEU CB C 40.86 0.3 1 108 447 32 LEU N N 118.39 0.1 1 109 447 32 LEU H H 7.97 0.02 1 110 447 32 LEU C C 180.6 0.1 1 111 447 32 LEU CA C 57.43 0.3 1 112 447 32 LEU CB C 40.79 0.3 1 113 448 33 ARG N N 118.59 0.1 1 114 448 33 ARG H H 7.84 0.02 1 115 448 33 ARG C C 177.32 0.1 1 116 448 33 ARG CA C 57.72 0.3 1 117 448 33 ARG CB C 30.27 0.3 1 118 449 34 LEU N N 118.14 0.1 1 119 449 34 LEU H H 7.3 0.02 1 120 449 34 LEU CA C 56.46 0.3 1 121 449 34 LEU CB C 42.88 0.3 1 122 450 35 GLY N N 105.55 0.1 1 123 450 35 GLY H H 7.41 0.02 1 124 450 35 GLY CA C 45.31 0.3 1 125 451 36 PRO C C 178.31 0.1 1 126 451 36 PRO CA C 64.6 0.3 1 127 451 36 PRO CB C 32.24 0.3 1 128 452 37 LYS N N 117.95 0.1 1 129 452 37 LYS H H 8.81 0.02 1 130 452 37 LYS C C 176.62 0.1 1 131 452 37 LYS CA C 55.36 0.3 1 132 452 37 LYS CB C 31.17 0.3 1 133 453 38 SER N N 115.65 0.1 1 134 453 38 SER H H 7.93 0.02 1 135 453 38 SER C C 175.2 0.1 1 136 453 38 SER CA C 61.37 0.3 1 137 453 38 SER CB C 63.08 0.3 1 138 454 39 SER N N 115.43 0.1 1 139 454 39 SER H H 7.79 0.02 1 140 454 39 SER C C 175.4 0.1 1 141 454 39 SER CA C 61.26 0.3 1 142 455 40 VAL N N 120.95 0.1 1 143 455 40 VAL H H 6.99 0.02 1 144 455 40 VAL C C 178.09 0.1 1 145 455 40 VAL CA C 65.1 0.3 1 146 455 40 VAL CB C 32 0.3 1 147 456 41 LEU N N 119.96 0.1 1 148 456 41 LEU H H 7.97 0.02 1 149 456 41 LEU C C 179.7 0.1 1 150 456 41 LEU CA C 57.9 0.3 1 151 456 41 LEU CB C 42.01 0.3 1 152 457 42 ILE N N 118.46 0.1 1 153 457 42 ILE H H 8.12 0.02 1 154 457 42 ILE C C 178.16 0.1 1 155 457 42 ILE CA C 65.66 0.3 1 156 457 42 ILE CB C 37.92 0.3 1 157 458 43 ALA N N 122.27 0.1 1 158 458 43 ALA H H 7.58 0.02 1 159 458 43 ALA C C 179.57 0.1 1 160 458 43 ALA CA C 55.85 0.3 1 161 458 43 ALA CB C 17.5 0.3 1 162 459 44 GLN N N 115.74 0.1 1 163 459 44 GLN H H 8.5 0.02 1 164 459 44 GLN C C 177.45 0.1 1 165 459 44 GLN CA C 58.43 0.3 1 166 459 44 GLN CB C 28.92 0.3 1 167 460 45 GLN N N 114.82 0.1 1 168 460 45 GLN H H 7.4 0.02 1 169 460 45 GLN C C 175.43 0.1 1 170 460 45 GLN CA C 55.62 0.3 1 171 460 45 GLN CB C 28.97 0.3 1 172 461 46 THR N N 117.02 0.1 1 173 461 46 THR H H 7.32 0.02 1 174 461 46 THR C C 172.65 0.1 1 175 461 46 THR CA C 62.74 0.3 1 176 461 46 THR CB C 69.56 0.3 1 177 462 47 ASP N N 125.96 0.1 1 178 462 47 ASP H H 8.5 0.02 1 179 462 47 ASP C C 175.36 0.1 1 180 462 47 ASP CA C 53.1 0.3 1 181 462 47 ASP CB C 39.62 0.3 1 182 463 48 THR N N 113.6 0.1 1 183 463 48 THR H H 7.61 0.02 1 184 463 48 THR C C 173.43 0.1 1 185 463 48 THR CA C 61.62 0.3 1 186 463 48 THR CB C 67.3 0.3 1 187 464 49 SER N N 114.08 0.1 1 188 464 49 SER H H 8.17 0.02 1 189 464 49 SER C C 173.55 0.1 1 190 464 49 SER CA C 59.64 0.3 1 191 464 49 SER CB C 64.04 0.3 1 192 465 50 ASP N N 121.23 0.1 1 193 465 50 ASP H H 7.21 0.02 1 194 465 50 ASP CA C 50.09 0.3 1 195 465 50 ASP CB C 43.55 0.3 1 196 466 51 PRO C C 177.45 0.1 1 197 466 51 PRO CA C 65.98 0.3 1 198 466 51 PRO CB C 32.33 0.3 1 199 467 52 GLU N N 117.37 0.1 1 200 467 52 GLU H H 8.15 0.02 1 201 467 52 GLU C C 179.89 0.1 1 202 467 52 GLU CA C 59.28 0.3 1 203 467 52 GLU CB C 29.86 0.3 1 204 468 53 LYS N N 118.48 0.1 1 205 468 53 LYS H H 7.53 0.02 1 206 468 53 LYS C C 180.28 0.1 1 207 468 53 LYS CA C 58.81 0.3 1 208 468 53 LYS CB C 32.07 0.3 1 209 469 54 VAL N N 121.16 0.1 1 210 469 54 VAL H H 7.85 0.02 1 211 469 54 VAL C C 177.43 0.1 1 212 469 54 VAL CA C 67.07 0.3 1 213 469 54 VAL CB C 31.68 0.3 1 214 470 55 VAL N N 120.83 0.1 1 215 470 55 VAL H H 8.63 0.02 1 216 470 55 VAL C C 177.15 0.1 1 217 470 55 VAL CA C 68.05 0.3 1 218 470 55 VAL CB C 31.52 0.3 1 219 471 56 SER N N 111.79 0.1 1 220 471 56 SER H H 7.76 0.02 1 221 471 56 SER C C 176.8 0.1 1 222 471 56 SER CA C 61.43 0.3 1 223 471 56 SER CB C 63.01 0.3 1 224 472 57 ALA N N 121.61 0.1 1 225 472 57 ALA H H 7.83 0.02 1 226 472 57 ALA C C 178.52 0.1 1 227 472 57 ALA CA C 55.79 0.3 1 228 472 57 ALA CB C 19.04 0.3 1 229 473 58 PHE N N 118.32 0.1 1 230 473 58 PHE H H 8.96 0.02 1 231 473 58 PHE C C 178.82 0.1 1 232 473 58 PHE CA C 62.2 0.3 1 233 473 58 PHE CB C 39.48 0.3 1 234 474 59 LEU N N 121.24 0.1 1 235 474 59 LEU H H 8.88 0.02 1 236 474 59 LEU C C 179.47 0.1 1 237 474 59 LEU CA C 57.71 0.3 1 238 474 59 LEU CB C 40.87 0.3 1 239 475 60 LYS N N 121.03 0.1 1 240 475 60 LYS H H 8.35 0.02 1 241 475 60 LYS C C 179.81 0.1 1 242 475 60 LYS CA C 60.02 0.3 1 243 475 60 LYS CB C 32.94 0.3 1 244 476 61 VAL N N 117.11 0.1 1 245 476 61 VAL H H 8.36 0.02 1 246 476 61 VAL C C 176.48 0.1 1 247 476 61 VAL CA C 66.91 0.3 1 248 476 61 VAL CB C 32.35 0.3 1 249 477 62 SER N N 115.79 0.1 1 250 477 62 SER H H 8.08 0.02 1 251 477 62 SER C C 176.51 0.1 1 252 477 62 SER CA C 61.87 0.3 1 253 477 62 SER CB C 63.31 0.3 1 254 478 63 SER N N 115.79 0.1 1 255 478 63 SER H H 7.73 0.02 1 256 478 63 SER C C 175.86 0.1 1 257 478 63 SER CA C 61.29 0.3 1 258 478 63 SER CB C 63.03 0.3 1 259 479 64 VAL N N 114.03 0.1 1 260 479 64 VAL H H 7.09 0.02 1 261 479 64 VAL C C 173.47 0.1 1 262 479 64 VAL CA C 59.67 0.3 1 263 479 64 VAL CB C 30.93 0.3 1 264 480 65 PHE N N 118.53 0.1 1 265 480 65 PHE H H 7.37 0.02 1 266 480 65 PHE C C 174.32 0.1 1 267 480 65 PHE CA C 62.08 0.3 1 268 480 65 PHE CB C 40.89 0.3 1 269 481 66 LYS N N 124.79 0.1 1 270 481 66 LYS H H 6.11 0.02 1 271 481 66 LYS C C 173.77 0.1 1 272 481 66 LYS CA C 54.02 0.3 1 273 481 66 LYS CB C 36.53 0.3 1 274 482 67 ASP N N 118.73 0.1 1 275 482 67 ASP H H 8.42 0.02 1 276 482 67 ASP C C 175.67 0.1 1 277 482 67 ASP CA C 54.52 0.3 1 278 482 67 ASP CB C 40.37 0.3 1 279 483 68 GLU N N 121.99 0.1 1 280 483 68 GLU H H 7.61 0.02 1 281 483 68 GLU CA C 56.82 0.3 1 282 483 68 GLU CB C 30.99 0.3 1 283 484 69 ALA N N 128.02 0.1 1 284 484 69 ALA H H 8.62 0.02 1 285 484 69 ALA C C 178.8 0.1 1 286 484 69 ALA CA C 56.7 0.3 1 287 484 69 ALA CB C 19.13 0.3 1 288 485 70 THR N N 110.04 0.1 1 289 485 70 THR H H 8.43 0.02 1 290 485 70 THR C C 177.35 0.1 1 291 485 70 THR CA C 65.9 0.3 1 292 485 70 THR CB C 68.15 0.3 1 293 486 71 VAL N N 122.24 0.1 1 294 486 71 VAL H H 7.41 0.02 1 295 486 71 VAL C C 176.55 0.1 1 296 486 71 VAL CA C 66.22 0.3 1 297 486 71 VAL CB C 32.19 0.3 1 298 487 72 THR N N 120.67 0.1 1 299 487 72 THR H H 8.53 0.02 1 300 487 72 THR C C 178.32 0.1 1 301 487 72 THR CA C 60.47 0.3 1 302 487 72 THR CB C 29.97 0.3 1 303 488 73 MET N N 115.31 0.1 1 304 488 73 MET H H 8.08 0.02 1 305 488 73 MET C C 177.22 0.1 1 306 488 73 MET CA C 58.71 0.3 1 307 488 73 MET CB C 32.45 0.3 1 308 489 74 ALA N N 120.63 3.1 1 309 489 74 ALA H H 7.3 0.02 1 310 489 74 ALA C C 181.35 0.1 1 311 489 74 ALA CA C 54.94 0.3 1 312 489 74 ALA CB C 18.23 0.3 1 313 490 75 VAL N N 119.23 0.1 1 314 490 75 VAL H H 8.61 0.02 1 315 490 75 VAL C C 177.32 0.1 1 316 490 75 VAL CA C 67.22 0.3 1 317 490 75 VAL CB C 31.67 0.3 1 318 491 76 GLN N N 118.66 0.1 1 319 491 76 GLN H H 8.38 0.02 1 320 491 76 GLN C C 177.04 0.1 1 321 491 76 GLN CA C 60.44 0.3 1 322 491 76 GLN CB C 27.27 0.3 1 323 492 77 ASP N N 117.37 0.1 1 324 492 77 ASP H H 8.61 0.02 1 325 492 77 ASP C C 179.38 0.1 1 326 492 77 ASP CA C 57.46 0.3 1 327 492 77 ASP CB C 40.1 0.3 1 328 493 78 ALA N N 123.05 0.1 1 329 493 78 ALA H H 7.67 0.02 1 330 493 78 ALA CA C 55.4 0.3 1 331 493 78 ALA CB C 18.25 0.3 1 332 494 79 VAL N N 119.26 0.1 1 333 494 79 VAL H H 8.64 0.02 1 334 494 79 VAL C C 177.03 0.1 1 335 494 79 VAL CA C 67.5 0.3 1 336 494 79 VAL CB C 31.67 0.3 1 337 495 80 ASP N N 119.06 0.1 1 338 495 80 ASP H H 8.57 0.02 1 339 495 80 ASP C C 177.94 0.1 1 340 495 80 ASP CA C 57.93 0.3 1 341 495 80 ASP CB C 40.04 0.3 1 342 496 81 ALA N N 121.4 0.1 1 343 496 81 ALA H H 8 0.02 1 344 496 81 ALA C C 180.46 0.1 1 345 496 81 ALA CA C 55.16 0.3 1 346 496 81 ALA CB C 19.16 0.3 1 347 497 82 LEU N N 118.45 0.1 1 348 497 82 LEU H H 7.98 0.02 1 349 497 82 LEU C C 177.21 0.1 1 350 497 82 LEU CA C 57.99 0.3 1 351 497 82 LEU CB C 43.04 0.3 1 352 498 83 MET N N 113.72 0.1 1 353 498 83 MET H H 8.69 0.02 1 354 498 83 MET C C 178.94 0.1 1 355 498 83 MET CA C 54.72 0.3 1 356 498 83 MET CB C 28.34 0.3 1 357 499 84 GLN N N 119.78 0.1 1 358 499 84 GLN H H 8.31 0.02 1 359 499 84 GLN C C 178.16 0.1 1 360 499 84 GLN CA C 59.67 0.3 1 361 499 84 GLN CB C 28.41 0.3 1 362 500 85 LYS N N 117.35 0.1 1 363 500 85 LYS H H 6.74 0.02 1 364 500 85 LYS C C 179.13 0.1 1 365 500 85 LYS CA C 59.24 0.3 1 366 500 85 LYS CB C 32.65 0.3 1 367 501 86 ALA N N 121.73 0.1 1 368 501 86 ALA H H 7.88 0.02 1 369 501 86 ALA C C 178.35 0.1 1 370 501 86 ALA CA C 55.34 0.3 1 371 501 86 ALA CB C 17.33 0.3 1 372 502 87 PHE N N 111.76 0.1 1 373 502 87 PHE H H 8.47 0.02 1 374 502 87 PHE C C 177.38 0.1 1 375 502 87 PHE CA C 60.34 0.3 1 376 502 87 PHE CB C 38.14 0.3 1 377 503 88 ASN N N 115.41 0.1 1 378 503 88 ASN H H 7.34 0.02 1 379 503 88 ASN C C 175.23 0.1 1 380 503 88 ASN CA C 53.81 0.3 1 381 503 88 ASN CB C 39.13 0.3 1 382 504 89 SER N N 115.72 0.1 1 383 504 89 SER H H 7.61 0.02 1 384 504 89 SER CA C 57.63 0.3 1 385 504 89 SER CB C 63.72 0.3 1 386 505 90 SER C C 174.53 0.1 1 387 505 90 SER CA C 63.13 0.3 1 388 505 90 SER CB C 60.74 0.3 1 389 506 91 SER N N 118.21 0.1 1 390 506 91 SER H H 8.32 0.02 1 391 506 91 SER C C 173.92 0.1 1 392 506 91 SER CA C 58.56 0.3 1 393 506 91 SER CB C 63.8 0.3 1 394 507 92 PHE N N 124 0.1 1 395 507 92 PHE H H 7.54 0.02 1 396 507 92 PHE C C 174.22 0.1 1 397 507 92 PHE CA C 58.69 0.3 1 398 507 92 PHE CB C 40.56 0.3 1 399 508 93 ASN N N 126.9 0.1 1 400 508 93 ASN H H 7.55 0.02 1 401 508 93 ASN C C 175.79 0.1 1 402 508 93 ASN CA C 52.16 0.3 1 403 508 93 ASN CB C 38.59 0.3 1 404 509 94 SER N N 122.44 0.1 1 405 509 94 SER H H 8.64 0.02 1 406 509 94 SER C C 175.48 0.1 1 407 509 94 SER CA C 61.65 0.3 1 408 509 94 SER CB C 63.08 0.3 1 409 510 95 ASN N N 121.68 0.1 1 410 510 95 ASN H H 8.19 0.02 1 411 510 95 ASN CA C 57.59 0.3 1 412 510 95 ASN CB C 38.65 0.3 1 413 511 96 THR N N 119.23 0.1 1 414 511 96 THR H H 8.09 0.02 1 415 511 96 THR C C 175.62 0.1 1 416 511 96 THR CA C 66.36 0.3 1 417 511 96 THR CB C 68.16 0.3 1 418 512 97 PHE N N 119.28 0.1 1 419 512 97 PHE H H 7.85 0.02 1 420 512 97 PHE C C 174.43 0.1 1 421 512 97 PHE CA C 61.69 0.3 1 422 512 97 PHE CB C 39.46 0.3 1 423 513 98 LEU N N 118.51 0.1 1 424 513 98 LEU H H 7.99 0.02 1 425 513 98 LEU C C 177.88 0.1 1 426 513 98 LEU CA C 57.8 0.3 1 427 513 98 LEU CB C 41.56 0.3 1 428 514 99 THR N N 113.15 0.1 1 429 514 99 THR H H 8.14 0.02 1 430 514 99 THR C C 175.95 0.1 1 431 514 99 THR CA C 67.2 0.3 1 432 514 99 THR CB C 68.83 0.3 1 433 515 100 ARG N N 117.06 0.1 1 434 515 100 ARG H H 8.31 0.02 1 435 515 100 ARG C C 178.75 0.1 1 436 515 100 ARG CA C 56.05 0.3 1 437 515 100 ARG CB C 27.13 0.3 1 438 516 101 LEU N N 122.91 0.1 1 439 516 101 LEU H H 8.43 0.02 1 440 516 101 LEU C C 178.08 0.1 1 441 516 101 LEU CA C 58.62 0.3 1 442 516 101 LEU CB C 40.81 0.3 1 443 517 102 LEU N N 117.55 0.1 1 444 517 102 LEU H H 7.88 0.02 1 445 517 102 LEU C C 176.53 0.1 1 446 517 102 LEU CA C 58.2 0.3 1 447 517 102 LEU CB C 41.09 0.3 1 448 518 103 VAL N N 121.93 0.1 1 449 518 103 VAL H H 8.18 0.02 1 450 518 103 VAL C C 180.89 0.1 1 451 518 103 VAL CA C 63.12 0.3 1 452 518 103 VAL CB C 31.99 0.3 1 453 519 104 HIS N N 121.26 0.1 1 454 519 104 HIS H H 8.5 0.02 1 455 519 104 HIS C C 176.84 0.1 1 456 519 104 HIS CA C 61.04 0.3 1 457 519 104 HIS CB C 31.5 0.3 1 458 520 105 MET N N 114.38 0.1 1 459 520 105 MET H H 8.07 0.02 1 460 520 105 MET C C 175.04 0.1 1 461 520 105 MET CA C 57.33 0.3 1 462 520 105 MET CB C 35.11 0.3 1 463 521 106 GLY N N 105.71 0.1 1 464 521 106 GLY H H 7.91 0.02 1 465 521 106 GLY C C 174.57 0.1 1 466 521 106 GLY CA C 45.54 0.3 1 467 522 107 LEU N N 117.09 0.3 1 468 522 107 LEU H H 8.05 0.02 1 469 522 107 LEU C C 175.05 0.1 1 470 522 107 LEU CA C 55.05 0.3 1 471 522 107 LEU CB C 42.43 0.3 1 472 523 108 LEU N N 120.36 0.1 1 473 523 108 LEU H H 6.86 0.02 1 474 523 108 LEU C C 174.97 0.1 1 475 523 108 LEU CA C 53.51 0.3 1 476 523 108 LEU CB C 46.11 0.3 1 477 524 109 LYS N N 124.76 0.1 1 478 524 109 LYS H H 8.33 0.02 1 479 524 109 LYS CA C 56.31 0.3 1 480 524 109 LYS CB C 33.24 0.3 1 481 525 110 SER N N 116.92 0.1 1 482 525 110 SER H H 8.24 0.02 1 483 525 110 SER CA C 56.9 0.3 1 484 525 110 SER CB C 65.75 0.3 1 485 526 111 GLU N N 120.96 0.1 1 486 526 111 GLU H H 8.79 0.02 1 487 526 111 GLU C C 176.74 0.1 1 488 526 111 GLU CA C 57.51 0.3 1 489 526 111 GLU CB C 29.76 0.3 1 490 527 112 ASP N N 117.57 0.1 1 491 527 112 ASP H H 8.52 0.02 1 492 527 112 ASP C C 175.35 0.1 1 493 527 112 ASP CA C 53.17 0.3 1 494 527 112 ASP CB C 40.62 0.3 1 495 528 113 LYS N N 120.58 0.1 1 496 528 113 LYS H H 8.18 0.02 1 497 528 113 LYS C C 176.15 0.1 1 498 528 113 LYS CA C 56.43 0.3 1 499 528 113 LYS CB C 31.32 0.3 1 500 529 114 VAL N N 121.89 0.1 1 501 529 114 VAL H H 7.75 0.02 1 502 529 114 VAL C C 175.67 0.1 1 503 529 114 VAL CA C 61.31 0.3 1 504 529 114 VAL CB C 33.78 0.3 1 505 530 115 LYS N N 127.23 0.1 1 506 530 115 LYS H H 8.42 0.02 1 507 530 115 LYS C C 175.37 0.1 1 508 530 115 LYS CA C 55.59 0.3 1 509 530 115 LYS CB C 32.14 0.3 1 510 531 116 ALA N N 128.74 0.1 1 511 531 116 ALA H H 8.34 0.02 1 512 531 116 ALA CA C 52.07 0.3 1 513 531 116 ALA CB C 19.42 0.3 1 514 532 117 ILE N N 118.94 0.1 1 515 532 117 ILE H H 8.02 0.02 1 516 532 117 ILE C C 176.82 0.1 1 517 532 117 ILE CA C 61.18 0.3 1 518 532 117 ILE CB C 38.71 0.3 1 519 533 118 ALA N N 124.54 0.1 1 520 533 118 ALA H H 8.16 0.02 1 521 533 118 ALA C C 177.89 0.1 1 522 533 118 ALA CA C 54.03 0.3 1 523 533 118 ALA CB C 19.84 0.3 1 524 534 119 ASN N N 114.88 0.1 1 525 534 119 ASN H H 7.67 0.02 1 526 534 119 ASN C C 175.04 0.1 1 527 534 119 ASN CA C 52.3 0.3 1 528 534 119 ASN CB C 39.59 0.3 1 529 535 120 LEU N N 123.41 0.1 1 530 535 120 LEU H H 8.8 0.02 1 531 535 120 LEU C C 176.2 0.1 1 532 535 120 LEU CA C 55.31 0.3 1 533 535 120 LEU CB C 42.76 0.3 1 534 536 121 TYR N N 122.25 0.1 1 535 536 121 TYR H H 8.21 0.02 1 536 536 121 TYR CA C 63.32 0.3 1 537 536 121 TYR CB C 38.95 0.3 1 538 537 122 GLY N N 104.83 0.1 1 539 537 122 GLY H H 8.89 0.02 1 540 537 122 GLY CA C 48.71 0.3 1 541 538 123 PRO C C 177.96 0.1 1 542 538 123 PRO CA C 66.08 0.3 1 543 538 123 PRO CB C 31.87 0.3 1 544 539 124 LEU N N 115.26 0.1 1 545 539 124 LEU H H 8.27 0.02 1 546 539 124 LEU C C 179.29 0.1 1 547 539 124 LEU CA C 58.44 0.3 1 548 539 124 LEU CB C 42.45 0.3 1 549 540 125 MET N N 118.43 0.1 1 550 540 125 MET H H 8.07 0.02 1 551 540 125 MET C C 180.74 0.1 1 552 540 125 MET CA C 56.19 0.3 1 553 540 125 MET CB C 28.82 0.3 1 554 541 126 ALA N N 124.89 0.1 1 555 541 126 ALA H H 8.91 0.02 1 556 541 126 ALA C C 179.91 0.1 1 557 541 126 ALA CA C 55.33 0.3 1 558 541 126 ALA CB C 19.54 0.3 1 559 542 127 LEU N N 120.87 0.1 1 560 542 127 LEU H H 8.75 0.02 1 561 542 127 LEU C C 176.96 0.1 1 562 542 127 LEU CA C 58.33 0.3 1 563 542 127 LEU CB C 42.67 0.3 1 564 543 128 ASN N N 116.78 0.1 1 565 543 128 ASN H H 8.25 0.02 1 566 543 128 ASN C C 176.42 0.1 1 567 543 128 ASN CA C 57.15 0.3 1 568 543 128 ASN CB C 39 0.3 1 569 544 129 HIS N N 115.21 0.1 1 570 544 129 HIS H H 7.34 0.02 1 571 544 129 HIS C C 177.68 0.1 1 572 544 129 HIS CA C 60.35 0.3 1 573 544 129 HIS CB C 30.45 0.3 1 574 545 130 MET N N 120.03 0.1 1 575 545 130 MET H H 8.53 0.02 1 576 545 130 MET C C 177.59 0.1 1 577 545 130 MET CA C 59.76 0.3 1 578 545 130 MET CB C 35.06 0.3 1 579 546 131 VAL N N 109.84 0.1 1 580 546 131 VAL H H 7.95 0.02 1 581 546 131 VAL C C 174.87 0.1 1 582 546 131 VAL CA C 63.19 0.3 1 583 546 131 VAL CB C 30.67 0.3 1 584 547 132 GLN N N 113.21 0.1 1 585 547 132 GLN H H 6.69 0.02 1 586 547 132 GLN C C 176.44 0.1 1 587 547 132 GLN CA C 55.68 0.3 1 588 547 132 GLN CB C 30.53 0.3 1 589 548 133 GLN N N 117.24 0.1 1 590 548 133 GLN H H 7.41 0.02 1 591 548 133 GLN C C 178.12 0.1 1 592 548 133 GLN CA C 53.51 0.3 1 593 548 133 GLN CB C 29.32 0.3 1 594 549 134 ASP N N 122.1 0.1 1 595 549 134 ASP H H 8.81 0.02 1 596 549 134 ASP C C 176.64 0.1 1 597 549 134 ASP CA C 56.64 0.3 1 598 549 134 ASP CB C 40.22 0.3 1 599 550 135 TYR N N 111.21 0.1 1 600 550 135 TYR H H 6.65 0.02 1 601 550 135 TYR C C 175.2 0.1 1 602 550 135 TYR CA C 56.44 0.3 1 603 550 135 TYR CB C 37.29 0.3 1 604 551 136 PHE N N 125.87 0.1 1 605 551 136 PHE H H 7.04 0.02 1 606 551 136 PHE CA C 56.09 0.3 1 607 551 136 PHE CB C 39.85 0.3 1 608 552 137 PRO CA C 62.31 0.3 1 609 552 137 PRO CB C 30.58 0.3 1 610 553 138 LYS N N 126.57 0.1 1 611 553 138 LYS H H 8.33 0.02 1 612 553 138 LYS C C 179.31 0.1 1 613 553 138 LYS CA C 59.27 0.3 1 614 553 138 LYS CB C 31.6 0.3 1 615 554 139 ALA N N 120.87 0.1 1 616 554 139 ALA H H 8.55 0.02 1 617 554 139 ALA C C 178.86 0.1 1 618 554 139 ALA CA C 54.21 0.3 1 619 554 139 ALA CB C 18.54 0.3 1 620 555 140 LEU N N 114.16 0.1 1 621 555 140 LEU H H 7.72 0.02 1 622 555 140 LEU C C 178.34 0.1 1 623 555 140 LEU CA C 55.41 0.3 1 624 555 140 LEU CB C 42.72 0.3 1 625 556 141 ALA N N 121.79 0.1 1 626 556 141 ALA H H 7.9 0.02 1 627 556 141 ALA CA C 57.43 0.3 1 628 556 141 ALA CB C 16.8 0.3 1 629 557 142 PRO C C 179.28 0.1 1 630 557 142 PRO CA C 65.89 0.3 1 631 557 142 PRO CB C 31.04 0.3 1 632 558 143 LEU N N 118.39 0.1 1 633 558 143 LEU H H 6.94 0.02 1 634 558 143 LEU C C 178.37 0.1 1 635 558 143 LEU CA C 57.66 0.3 1 636 558 143 LEU CB C 41.88 0.3 1 637 559 144 LEU N N 117.85 0.1 1 638 559 144 LEU H H 7.67 0.02 1 639 559 144 LEU C C 178.62 0.1 1 640 559 144 LEU CA C 57.92 0.3 1 641 559 144 LEU CB C 42.37 0.3 1 642 560 145 LEU N N 118.98 0.1 1 643 560 145 LEU H H 8.58 0.02 1 644 560 145 LEU C C 178.45 0.1 1 645 560 145 LEU CA C 58.34 0.3 1 646 560 145 LEU CB C 42.2 0.3 1 647 561 146 ALA N N 120.3 0.1 1 648 561 146 ALA H H 7.66 0.02 1 649 561 146 ALA C C 179.31 0.1 1 650 561 146 ALA CA C 54.97 0.3 1 651 561 146 ALA CB C 17.93 0.3 1 652 562 147 PHE N N 113.1 0.1 1 653 562 147 PHE H H 7.56 0.02 1 654 562 147 PHE C C 177.59 0.1 1 655 562 147 PHE CA C 61.39 0.3 1 656 562 147 PHE CB C 40.6 0.3 1 657 563 148 VAL N N 115.43 0.1 1 658 563 148 VAL H H 8.3 0.02 1 659 563 148 VAL C C 175.71 0.1 1 660 563 148 VAL CA C 63.91 0.3 1 661 563 148 VAL CB C 31.82 0.3 1 662 564 149 THR N N 110.75 0.1 1 663 564 149 THR H H 7.59 0.02 1 664 564 149 THR C C 174.74 0.1 1 665 564 149 THR CA C 63.33 0.3 1 666 564 149 THR CB C 69.83 0.3 1 667 565 150 LYS N N 123.14 0.1 1 668 565 150 LYS H H 6.84 0.02 1 669 565 150 LYS CA C 54.72 0.3 1 670 565 150 LYS CB C 32.29 0.3 1 671 568 153 SER C C 176.06 0.1 1 672 568 153 SER CA C 61.67 0.3 1 673 568 153 SER CB C 62.98 0.3 1 674 569 154 ALA N N 125.27 0.1 1 675 569 154 ALA H H 8.44 0.02 1 676 569 154 ALA C C 179.94 0.1 1 677 569 154 ALA CA C 54.86 0.3 1 678 569 154 ALA CB C 18.55 0.3 1 679 570 155 LEU N N 116.49 0.1 1 680 570 155 LEU H H 7.9 0.02 1 681 570 155 LEU C C 178.72 0.1 1 682 570 155 LEU CA C 56.58 0.3 1 683 570 155 LEU CB C 42.36 0.3 1 684 571 156 GLU N N 117.92 0.1 1 685 571 156 GLU H H 7.84 0.02 1 686 571 156 GLU C C 178.5 0.1 1 687 571 156 GLU CA C 58.61 0.3 1 688 571 156 GLU CB C 29.5 0.3 1 689 572 157 SER N N 112.4 0.1 1 690 572 157 SER H H 7.77 0.02 1 691 572 157 SER C C 174.69 0.1 1 692 572 157 SER CA C 60.07 0.3 1 693 572 157 SER CB C 63.47 0.3 1 694 573 158 CYS N N 121.26 0.1 1 695 573 158 CYS H H 7.6 0.02 1 696 573 158 CYS C C 175.34 0.1 1 697 573 158 CYS CA C 56.61 0.3 1 698 573 158 CYS CB C 27.05 0.3 1 699 574 159 SER N N 115.68 0.1 1 700 574 159 SER H H 7.78 0.02 1 701 574 159 SER CA C 61.23 0.3 1 702 575 160 PHE N N 123.71 0.1 1 703 575 160 PHE H H 8.8 0.02 1 704 575 160 PHE CA C 54.96 0.3 1 705 575 160 PHE CB C 42.51 0.3 1 706 576 161 ALA N N 123.8 0.1 1 707 576 161 ALA H H 8.13 0.02 1 708 576 161 ALA C C 178.93 0.1 1 709 576 161 ALA CA C 54.85 0.3 1 710 576 161 ALA CB C 19.72 0.3 1 711 577 162 ARG N N 117.97 0.1 1 712 577 162 ARG H H 8.33 0.02 1 713 577 162 ARG C C 176.98 0.1 1 714 577 162 ARG CA C 60.11 0.3 1 715 577 162 ARG CB C 30.05 0.3 1 716 578 163 HIS N N 117.69 0.1 1 717 578 163 HIS H H 8.49 0.02 1 718 578 163 HIS C C 177.63 0.1 1 719 578 163 HIS CA C 60.22 0.3 1 720 578 163 HIS CB C 30.13 0.3 1 721 579 164 SER N N 114.88 0.1 1 722 579 164 SER H H 8 0.02 1 723 579 164 SER C C 175.28 0.1 1 724 579 164 SER CA C 62.25 0.3 1 725 580 165 LEU N N 121.81 0.1 1 726 580 165 LEU H H 7.62 0.02 1 727 580 165 LEU C C 178.15 0.1 1 728 580 165 LEU CA C 57.03 0.3 1 729 580 165 LEU CB C 41.46 0.3 1 730 581 166 LEU N N 118.67 0.1 1 731 581 166 LEU H H 8.2 0.02 1 732 581 166 LEU C C 177.23 0.1 1 733 581 166 LEU CA C 58.5 0.3 1 734 581 166 LEU CB C 41.45 0.3 1 735 582 167 GLN N N 114.53 0.1 1 736 582 167 GLN H H 7.79 0.02 1 737 582 167 GLN C C 179.35 0.1 1 738 582 167 GLN CA C 58.67 0.3 1 739 582 167 GLN CB C 28.36 0.3 1 740 583 168 THR N N 117.58 0.1 1 741 583 168 THR H H 7.83 0.02 1 742 583 168 THR C C 176.93 0.1 1 743 583 168 THR CA C 65.79 0.3 1 744 583 168 THR CB C 68.19 0.3 1 745 584 169 LEU N N 121.29 0.1 1 746 584 169 LEU H H 8.39 0.02 1 747 584 169 LEU C C 178.8 0.1 1 748 584 169 LEU CA C 57.71 0.3 1 749 584 169 LEU CB C 42.69 0.3 1 750 585 170 TYR N N 116.91 0.1 1 751 585 170 TYR H H 8.11 0.02 1 752 585 170 TYR C C 176.89 0.1 1 753 585 170 TYR CA C 59.14 0.3 1 754 585 170 TYR CB C 38.07 0.3 1 755 586 171 LYS N N 117.84 0.1 1 756 586 171 LYS H H 7.49 0.02 1 757 586 171 LYS C C 176.08 0.1 1 758 586 171 LYS CA C 56.42 0.3 1 759 586 171 LYS CB C 33.41 0.3 1 760 587 172 VAL N N 124.45 0.1 1 761 587 172 VAL H H 7.16 0.02 1 762 587 172 VAL CA C 65.1 0.3 1 763 587 172 VAL CB C 32.37 0.3 1 stop_ save_