data_25048 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and Development: Spin Labels to Structure ; _BMRB_accession_number 25048 _BMRB_flat_file_name bmr25048.str _Entry_type original _Submission_date 2014-06-26 _Accession_date 2014-06-26 _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 Zhao Yingchu . . 2 Marcink Thomas . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 205 "13C chemical shifts" 502 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-02-09 original author . stop_ _Original_release_date 2015-02-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Transient collagen triple helix binding to a key metalloproteinase in invasion and development' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25651059 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhao Yingchu . . 2 Marcink Thomas C. . 3 'Sanganna Gari' R. R. . 4 Marsh B. P. . 5 King G. M. . 6 Stawikowska R. . . 7 Fields Gregg B. . 8 VanDoren Steven R. . stop_ _Journal_abbreviation Structure _Journal_volume 23 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 257 _Page_last 269 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Transient Collagen Triple Helix Binding to a Key Metalloproteinase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Hemopexin-like_(HPX) $Hemopexin-like_(HPX) THP_L_and_M_chain $THP_L_and_M_chain THP_T_chain $THP_T_chain 4-HYDROXYPROLINE $entity_HYP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hemopexin-like_(HPX) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hemopexin-like_(HPX) _Molecular_mass 23131.535 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 196 _Mol_residue_sequence ; PNICDGNFDTVAMLRGEMFV FKERWFWRVRNNQVMDGYPM PIGQFWRGLPASINTAYERK DGKFVFFKGDKHWVFDEASL EPGYPKHIKELGRGLPTDKI DAALFWMPNGKTYFFRGNKY YRFNEELRAVDSEYPKNIKV WEGIPESPRGSFMGSDEVFT YFYKGNKYWKFNNQKLKVEP GYPKSALRDWMGCPSG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 316 PRO 2 317 ASN 3 318 ILE 4 319 CYS 5 320 ASP 6 321 GLY 7 322 ASN 8 323 PHE 9 324 ASP 10 325 THR 11 326 VAL 12 327 ALA 13 328 MET 14 329 LEU 15 330 ARG 16 331 GLY 17 332 GLU 18 333 MET 19 334 PHE 20 335 VAL 21 336 PHE 22 337 LYS 23 338 GLU 24 339 ARG 25 340 TRP 26 341 PHE 27 342 TRP 28 343 ARG 29 344 VAL 30 345 ARG 31 346 ASN 32 347 ASN 33 348 GLN 34 349 VAL 35 350 MET 36 351 ASP 37 352 GLY 38 353 TYR 39 354 PRO 40 355 MET 41 356 PRO 42 357 ILE 43 358 GLY 44 359 GLN 45 360 PHE 46 361 TRP 47 362 ARG 48 363 GLY 49 364 LEU 50 365 PRO 51 366 ALA 52 367 SER 53 368 ILE 54 369 ASN 55 370 THR 56 371 ALA 57 372 TYR 58 373 GLU 59 374 ARG 60 375 LYS 61 376 ASP 62 377 GLY 63 378 LYS 64 379 PHE 65 380 VAL 66 381 PHE 67 382 PHE 68 383 LYS 69 384 GLY 70 385 ASP 71 386 LYS 72 387 HIS 73 388 TRP 74 389 VAL 75 390 PHE 76 391 ASP 77 392 GLU 78 393 ALA 79 394 SER 80 395 LEU 81 396 GLU 82 397 PRO 83 398 GLY 84 399 TYR 85 400 PRO 86 401 LYS 87 402 HIS 88 403 ILE 89 404 LYS 90 405 GLU 91 406 LEU 92 407 GLY 93 408 ARG 94 409 GLY 95 410 LEU 96 411 PRO 97 412 THR 98 413 ASP 99 414 LYS 100 415 ILE 101 416 ASP 102 417 ALA 103 418 ALA 104 419 LEU 105 420 PHE 106 421 TRP 107 422 MET 108 423 PRO 109 424 ASN 110 425 GLY 111 426 LYS 112 427 THR 113 428 TYR 114 429 PHE 115 430 PHE 116 431 ARG 117 432 GLY 118 433 ASN 119 434 LYS 120 435 TYR 121 436 TYR 122 437 ARG 123 438 PHE 124 439 ASN 125 440 GLU 126 441 GLU 127 442 LEU 128 443 ARG 129 444 ALA 130 445 VAL 131 446 ASP 132 447 SER 133 448 GLU 134 449 TYR 135 450 PRO 136 451 LYS 137 452 ASN 138 453 ILE 139 454 LYS 140 455 VAL 141 456 TRP 142 457 GLU 143 458 GLY 144 459 ILE 145 460 PRO 146 461 GLU 147 462 SER 148 463 PRO 149 464 ARG 150 465 GLY 151 466 SER 152 467 PHE 153 468 MET 154 469 GLY 155 470 SER 156 471 ASP 157 472 GLU 158 473 VAL 159 474 PHE 160 475 THR 161 476 TYR 162 477 PHE 163 478 TYR 164 479 LYS 165 480 GLY 166 481 ASN 167 482 LYS 168 483 TYR 169 484 TRP 170 485 LYS 171 486 PHE 172 487 ASN 173 488 ASN 174 489 GLN 175 490 LYS 176 491 LEU 177 492 LYS 178 493 VAL 179 494 GLU 180 495 PRO 181 496 GLY 182 497 TYR 183 498 PRO 184 499 LYS 185 500 SER 186 501 ALA 187 502 LEU 188 503 ARG 189 504 ASP 190 505 TRP 191 506 MET 192 507 GLY 193 508 CYS 194 509 PRO 195 510 SER 196 511 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 2MQS "Transient Collagen Triple Helix Binding To A Key Metalloproteinase In Invasion And Development: Spin Labels To Structure" 99.49 196 100.00 100.00 2.06e-140 PDB 3C7X "Hemopexin-Like Domain Of Matrix Metalloproteinase 14" 100.00 196 100.00 100.00 3.04e-141 DBJ BAA05519 "membrane-type matrix metalloproteinase [Homo sapiens]" 100.00 582 99.49 100.00 8.18e-139 DBJ BAA36551 "Membrane-type matrix metalloproteinase-1 [Capra hircus]" 99.49 582 97.44 98.97 1.20e-135 DBJ BAC40377 "unnamed protein product [Mus musculus]" 100.00 582 99.49 99.49 8.26e-139 DBJ BAE23719 "unnamed protein product [Mus musculus]" 100.00 582 99.49 99.49 8.26e-139 DBJ BAE29158 "unnamed protein product [Mus musculus]" 100.00 582 99.49 99.49 8.26e-139 EMBL CAA58519 "MT-MMP [Homo sapiens]" 100.00 582 100.00 100.00 2.04e-139 EMBL CAA58521 "MT-MMP [Rattus norvegicus]" 100.00 582 99.49 99.49 1.16e-138 EMBL CAA62432 "MT-MMP protein [Homo sapiens]" 100.00 582 99.49 99.49 1.47e-138 EMBL CAA62897 "membrane-type metalloproteinase [Rattus norvegicus]" 100.00 582 99.49 99.49 9.21e-139 EMBL CAA88372 "membrane-type matrix metalloproteinase 1 [Homo sapiens]" 100.00 582 100.00 100.00 2.48e-139 GB AAA83770 "membrane-type matrix metalloproteinase-1 [Homo sapiens]" 100.00 582 100.00 100.00 2.48e-139 GB AAB41500 "membrane type 1 metalloproteinase [Oryctolagus cuniculus]" 100.00 582 97.45 98.47 2.47e-136 GB AAB51753 "membrane-type matrix metalloproteinase 1 [Mus musculus]" 100.00 582 99.49 99.49 1.00e-138 GB AAB86602 "matrix metalloproteinase-14 [Mus musculus]" 100.00 581 97.96 97.96 6.72e-134 GB AAD13803 "membane-type 1 metalloproteinase precursor, partial [Oryctolagus cuniculus]" 100.00 572 98.98 100.00 1.50e-138 REF NP_001076262 "matrix metalloproteinase-14 precursor [Oryctolagus cuniculus]" 100.00 582 97.45 98.47 2.47e-136 REF NP_001124793 "matrix metalloproteinase-14 precursor [Pongo abelii]" 100.00 582 98.98 99.49 3.81e-138 REF NP_001159653 "matrix metalloproteinase-14 precursor [Ovis aries]" 99.49 582 97.95 98.97 2.61e-136 REF NP_001233698 "matrix metalloproteinase-14 precursor [Cricetulus griseus]" 100.00 582 98.47 98.98 8.46e-137 REF NP_001253739 "matrix metalloproteinase-14 precursor [Macaca mulatta]" 100.00 582 100.00 100.00 2.43e-139 SP P50281 "RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; AltName: Full=MMP-X1; AltName: Full=Membrane-type matrix metalloprotei" 100.00 582 100.00 100.00 2.48e-139 SP P53690 "RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; AltName: Full=MMP-X1; AltName: Full=MT-MMP; AltName: Full=Membrane-typ" 100.00 582 99.49 99.49 8.26e-139 SP Q10739 "RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; AltName: Full=Membrane-type matrix metalloproteinase 1; Short=MT-MMP 1" 100.00 582 99.49 99.49 9.21e-139 SP Q5RES1 "RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; Flags: Precursor" 100.00 582 98.98 99.49 3.81e-138 SP Q95220 "RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; AltName: Full=Membrane-type matrix metalloproteinase 1; Short=MT-MMP 1" 100.00 582 97.45 98.47 2.47e-136 TPG DAA25704 "TPA: matrix metalloproteinase-14 precursor [Bos taurus]" 99.49 582 97.95 98.97 2.61e-136 stop_ save_ save_THP_L_and_M_chain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common THP_L_and_M_chain _Molecular_mass 3293.611 _Mol_thiol_state 'not present' _Details . _Residue_count 36 _Mol_residue_sequence ; GPPGPPGPPGPQGIAGQRGV VGLPGPPGPPGPPGPP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 PRO 3 3 HYP 4 4 GLY 5 5 PRO 6 6 HYP 7 7 GLY 8 8 PRO 9 9 HYP 10 10 GLY 11 11 PRO 12 12 GLN 13 13 GLY 14 14 ILE 15 15 ALA 16 16 GLY 17 17 GLN 18 18 ARG 19 19 GLY 20 20 VAL 21 21 VAL 22 22 GLY 23 23 LEU 24 24 HYP 25 25 GLY 26 26 PRO 27 27 HYP 28 28 GLY 29 29 PRO 30 30 HYP 31 31 GLY 32 32 PRO 33 33 HYP 34 34 GLY 35 35 PRO 36 36 HYP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_THP_T_chain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common THP_T_chain _Molecular_mass 3026.327 _Mol_thiol_state 'not present' _Details . _Residue_count 33 _Mol_residue_sequence ; GPPGPPGPPGPQGIAGQRGV VGLPGPPGPPGPP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 PRO 3 3 HYP 4 4 GLY 5 5 PRO 6 6 HYP 7 7 GLY 8 8 PRO 9 9 HYP 10 10 GLY 11 11 PRO 12 12 GLN 13 13 GLY 14 14 ILE 15 15 ALA 16 16 GLY 17 17 GLN 18 18 ARG 19 19 GLY 20 20 VAL 21 21 VAL 22 22 GLY 23 23 LEU 24 24 HYP 25 25 GLY 26 26 PRO 27 27 HYP 28 28 GLY 29 29 PRO 30 30 HYP 31 31 GLY 32 32 PRO 33 33 HYP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_HYP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 4-HYDROXYPROLINE _BMRB_code HYP _PDB_code HYP _Standard_residue_derivative . _Molecular_mass 131.130 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OD1 OD1 O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG HG H . 0 . ? HD22 HD22 H . 0 . ? HD23 HD23 H . 0 . ? HD1 HD1 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG OD1 ? ? SING CG HG ? ? SING CD HD22 ? ? SING CD HD23 ? ? SING OD1 HD1 ? ? SING OXT HXT ? ? stop_ save_ ############# # Ligands # ############# save_HYP _Saveframe_category ligand _Mol_type non-polymer _Name_common 4-HYDROXYPROLINE _Molecular_mass 131.130 _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hemopexin-like_(HPX) human 9606 Eukaryota Metazoa Homo sapiens $THP_L_and_M_chain human 9606 Eukaryota Metazoa Homo sapiens $THP_T_chain human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Hemopexin-like_(HPX) 'recombinant technology' . . . . pET-27b(+) $THP_L_and_M_chain 'chemical synthesis' . . . . . $THP_T_chain 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Hemopexin_domain_of_MT1-MMP _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Hemopexin-like_(HPX) . mM 0.2 0.4 '[U-13C; U-15N; U-2H]' 'Sodium acetate' 10 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' 'Sodium azide' 1 mM . . 'natural abundance' H2O 93 % . . 'natural abundance' D2O 7 % . . 'natural abundance' stop_ save_ save_THP _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $THP_L_and_M_chain . mM 0.3 1.4 'natural abundance' 'Sodium acetate' 10 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' 'Sodium azide' 1 mM . . 'natural abundance' H2O 93 % . . 'natural abundance' D2O 7 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC_aromatic_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_2D_1H-13C_HSQC_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HN(COCA)CB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ save_3D_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $Hemopexin_domain_of_MT1-MMP save_ ####################### # Sample conditions # ####################### save_free_state_HPX_domain _Saveframe_category sample_conditions _Details 'used for NMR peak assignments' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 310 . K pH 5 . pH pressure 1 . atm 'ionic strength' 10 . mM stop_ save_ save_THP+HPX_domain_complex _Saveframe_category sample_conditions _Details 'Used for titrations and measuring intermolecular PREs' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 292 6 K pH 5.0 . pH pressure 1 . atm 'ionic strength' 10 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $SPARKY stop_ loop_ _Experiment_label '2D 1H-13C HSQC aromatic' '2D 1H-13C HSQC aliphatic' '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(COCA)CB' '3D 1H-15N NOESY' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $Hemopexin_domain_of_MT1-MMP stop_ _Sample_conditions_label $free_state_HPX_domain _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Hemopexin-like_(HPX) _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 1 318 3 ILE HD1 H -0.26 0.04 1 2 318 3 ILE CD1 C 13.83 0.30 1 3 319 4 CYS H H 7.84 0.04 1 4 319 4 CYS C C 172.45 0.30 1 5 319 4 CYS CA C 54.12 0.30 1 6 319 4 CYS CB C 35.79 0.30 1 7 319 4 CYS N N 116.28 0.40 1 8 320 5 ASP H H 7.60 0.04 1 9 320 5 ASP C C 175.40 0.30 1 10 320 5 ASP CA C 54.34 0.30 1 11 320 5 ASP CB C 38.85 0.30 1 12 320 5 ASP N N 119.49 0.40 1 13 321 6 GLY H H 7.40 0.04 1 14 321 6 GLY C C 170.01 0.30 1 15 321 6 GLY CA C 44.33 0.30 1 16 321 6 GLY N N 104.34 0.40 1 17 322 7 ASN H H 9.68 0.04 1 18 322 7 ASN C C 171.64 0.30 1 19 322 7 ASN CA C 52.38 0.30 1 20 322 7 ASN CB C 34.92 0.30 1 21 322 7 ASN N N 116.48 0.40 1 22 323 8 PHE H H 5.83 0.04 1 23 323 8 PHE C C 174.21 0.30 1 24 323 8 PHE CA C 55.38 0.30 1 25 323 8 PHE CB C 36.62 0.30 1 26 323 8 PHE N N 115.35 0.40 1 27 324 9 ASP H H 9.65 0.04 1 28 324 9 ASP C C 173.68 0.30 1 29 324 9 ASP CA C 57.14 0.30 1 30 324 9 ASP CB C 40.69 0.30 1 31 324 9 ASP N N 123.02 0.40 1 32 325 10 THR H H 7.51 0.04 1 33 325 10 THR C C 168.58 0.30 1 34 325 10 THR CA C 60.90 0.30 1 35 325 10 THR CB C 65.93 0.30 1 36 325 10 THR N N 105.52 0.40 1 37 326 11 VAL H H 7.59 0.04 1 38 326 11 VAL HG1 H 0.77 0.04 1 39 326 11 VAL HG2 H 0.36 0.04 1 40 326 11 VAL C C 170.54 0.30 1 41 326 11 VAL CA C 60.76 0.30 1 42 326 11 VAL CB C 34.42 0.30 1 43 326 11 VAL CG1 C 20.93 0.30 1 44 326 11 VAL CG2 C 20.75 0.30 1 45 326 11 VAL N N 123.99 0.40 1 46 327 12 ALA H H 9.32 0.04 1 47 327 12 ALA C C 171.89 0.30 1 48 327 12 ALA CA C 48.79 0.30 1 49 327 12 ALA CB C 22.63 0.30 1 50 327 12 ALA N N 127.50 0.40 1 51 328 13 MET H H 7.59 0.04 1 52 328 13 MET C C 172.02 0.30 1 53 328 13 MET CA C 51.98 0.30 1 54 328 13 MET N N 120.34 0.40 1 55 329 14 LEU H H 8.81 0.04 1 56 329 14 LEU HD1 H -0.33 0.04 1 57 329 14 LEU HD2 H 0.19 0.04 1 58 329 14 LEU C C 173.05 0.30 1 59 329 14 LEU CA C 52.43 0.30 1 60 329 14 LEU CB C 39.49 0.30 1 61 329 14 LEU CD1 C 23.55 0.30 1 62 329 14 LEU CD2 C 21.72 0.30 1 63 329 14 LEU N N 125.31 0.40 1 64 330 15 ARG H H 9.49 0.04 1 65 330 15 ARG HE H 7.53 0.04 1 66 330 15 ARG C C 174.17 0.30 1 67 330 15 ARG CA C 55.09 0.30 1 68 330 15 ARG N N 128.67 0.40 1 69 330 15 ARG NE N 85.71 0.40 1 70 331 16 GLY H H 8.53 0.04 1 71 331 16 GLY C C 170.60 0.30 1 72 331 16 GLY CA C 44.71 0.30 1 73 331 16 GLY N N 103.73 0.40 1 74 332 17 GLU H H 7.55 0.04 1 75 332 17 GLU C C 170.50 0.30 1 76 332 17 GLU CA C 53.02 0.30 1 77 332 17 GLU CB C 31.00 0.30 1 78 332 17 GLU N N 120.62 0.40 1 79 333 18 MET H H 8.11 0.04 1 80 333 18 MET C C 171.33 0.30 1 81 333 18 MET CA C 54.80 0.30 1 82 333 18 MET CB C 32.08 0.30 1 83 333 18 MET N N 123.04 0.40 1 84 334 19 PHE H H 8.96 0.04 1 85 334 19 PHE C C 171.16 0.30 1 86 334 19 PHE CA C 55.14 0.30 1 87 334 19 PHE CB C 42.14 0.30 1 88 334 19 PHE N N 125.98 0.40 1 89 335 20 VAL H H 8.60 0.04 1 90 335 20 VAL HG1 H -0.14 0.04 1 91 335 20 VAL HG2 H 0.49 0.04 1 92 335 20 VAL C C 172.13 0.30 1 93 335 20 VAL CA C 60.11 0.30 1 94 335 20 VAL CB C 32.79 0.30 1 95 335 20 VAL CG1 C 20.03 0.30 1 96 335 20 VAL CG2 C 20.23 0.30 1 97 335 20 VAL N N 122.77 0.40 1 98 336 21 PHE H H 8.35 0.04 1 99 336 21 PHE C C 173.71 0.30 1 100 336 21 PHE CA C 56.60 0.30 1 101 336 21 PHE CB C 40.36 0.30 1 102 336 21 PHE N N 124.47 0.40 1 103 337 22 LYS H H 9.62 0.04 1 104 337 22 LYS C C 171.00 0.30 1 105 337 22 LYS CA C 56.80 0.30 1 106 337 22 LYS CB C 35.58 0.30 1 107 337 22 LYS N N 124.82 0.40 1 108 338 23 GLU H H 10.39 0.04 1 109 338 23 GLU C C 174.45 0.30 1 110 338 23 GLU CA C 58.23 0.30 1 111 338 23 GLU CB C 25.61 0.30 1 112 338 23 GLU N N 132.80 0.40 1 113 339 24 ARG H H 8.26 0.04 1 114 339 24 ARG C C 172.21 0.30 1 115 339 24 ARG CA C 55.35 0.30 1 116 339 24 ARG CB C 28.51 0.30 1 117 339 24 ARG N N 123.48 0.40 1 118 340 25 TRP H H 8.62 0.04 1 119 340 25 TRP C C 171.35 0.30 1 120 340 25 TRP CA C 56.50 0.30 1 121 340 25 TRP CB C 32.00 0.30 1 122 340 25 TRP N N 123.87 0.40 1 123 341 26 PHE H H 8.97 0.04 1 124 341 26 PHE C C 169.60 0.30 1 125 341 26 PHE CA C 54.89 0.30 1 126 341 26 PHE CB C 41.49 0.30 1 127 341 26 PHE N N 115.80 0.40 1 128 342 27 TRP H H 9.27 0.04 1 129 342 27 TRP C C 171.16 0.30 1 130 342 27 TRP CA C 56.05 0.30 1 131 342 27 TRP CB C 33.32 0.30 1 132 342 27 TRP N N 116.89 0.40 1 133 343 28 ARG HE H 6.83 0.04 1 134 343 28 ARG NE N 84.80 0.40 1 135 344 29 VAL H H 7.65 0.04 1 136 344 29 VAL HG1 H 0.58 0.04 1 137 344 29 VAL HG2 H 0.41 0.04 1 138 344 29 VAL C C 171.57 0.30 1 139 344 29 VAL CA C 58.35 0.30 1 140 344 29 VAL CB C 33.17 0.30 1 141 344 29 VAL CG1 C 20.99 0.30 1 142 344 29 VAL CG2 C 20.15 0.30 1 143 344 29 VAL N N 120.27 0.40 1 144 345 30 ARG H H 8.44 0.04 1 145 345 30 ARG HE H 7.29 0.04 1 146 345 30 ARG C C 173.02 0.30 1 147 345 30 ARG CA C 54.76 0.30 1 148 345 30 ARG CB C 32.12 0.30 1 149 345 30 ARG N N 123.68 0.40 1 150 345 30 ARG NE N 85.76 0.40 1 151 346 31 ASN H H 9.38 0.04 1 152 346 31 ASN CA C 53.29 0.30 1 153 346 31 ASN N N 124.33 0.40 1 154 347 32 ASN H H 8.75 0.04 1 155 347 32 ASN C C 170.83 0.30 1 156 347 32 ASN CA C 51.92 0.30 1 157 347 32 ASN CB C 36.40 0.30 1 158 347 32 ASN N N 112.72 0.40 1 159 348 33 GLN H H 7.05 0.04 1 160 348 33 GLN C C 171.87 0.30 1 161 348 33 GLN CA C 52.95 0.30 1 162 348 33 GLN CB C 31.01 0.30 1 163 348 33 GLN N N 113.94 0.40 1 164 349 34 VAL H H 8.54 0.04 1 165 349 34 VAL HG1 H 1.29 0.04 1 166 349 34 VAL HG2 H 0.96 0.04 1 167 349 34 VAL C C 174.38 0.30 1 168 349 34 VAL CA C 62.16 0.30 1 169 349 34 VAL CB C 30.66 0.30 1 170 349 34 VAL CG1 C 23.24 0.30 1 171 349 34 VAL CG2 C 23.05 0.30 1 172 349 34 VAL N N 124.27 0.40 1 173 350 35 MET H H 8.01 0.04 1 174 350 35 MET C C 173.04 0.30 1 175 350 35 MET CA C 55.40 0.30 1 176 350 35 MET CB C 32.37 0.30 1 177 350 35 MET N N 128.17 0.40 1 178 351 36 ASP H H 8.35 0.04 1 179 351 36 ASP C C 174.27 0.30 1 180 351 36 ASP CA C 55.06 0.30 1 181 351 36 ASP CB C 39.61 0.30 1 182 351 36 ASP N N 121.54 0.40 1 183 352 37 GLY H H 8.43 0.04 1 184 352 37 GLY C C 169.81 0.30 1 185 352 37 GLY CA C 43.46 0.30 1 186 352 37 GLY N N 110.48 0.40 1 187 353 38 TYR H H 7.14 0.04 1 188 353 38 TYR C C 170.54 0.30 1 189 353 38 TYR CA C 55.88 0.30 1 190 353 38 TYR CB C 36.45 0.30 1 191 353 38 TYR N N 116.59 0.40 1 192 355 40 MET H H 8.32 0.04 1 193 355 40 MET C C 169.77 0.30 1 194 355 40 MET CA C 51.79 0.30 1 195 355 40 MET CB C 34.58 0.30 1 196 355 40 MET N N 119.69 0.40 1 197 357 42 ILE H H 9.00 0.04 1 198 357 42 ILE HD1 H 1.23 0.04 1 199 357 42 ILE C C 175.58 0.30 1 200 357 42 ILE CA C 64.98 0.30 1 201 357 42 ILE CB C 38.69 0.30 1 202 357 42 ILE CD1 C 15.21 0.30 1 203 357 42 ILE N N 128.41 0.40 1 204 358 43 GLY H H 8.62 0.04 1 205 358 43 GLY C C 172.13 0.30 1 206 358 43 GLY CA C 44.49 0.30 1 207 358 43 GLY N N 103.62 0.40 1 208 359 44 GLN H H 7.32 0.04 1 209 359 44 GLN C C 172.42 0.30 1 210 359 44 GLN CA C 55.16 0.30 1 211 359 44 GLN CB C 27.94 0.30 1 212 359 44 GLN N N 116.90 0.40 1 213 362 47 ARG H H 6.93 0.04 1 214 362 47 ARG C C 173.93 0.30 1 215 362 47 ARG CA C 58.71 0.30 1 216 362 47 ARG CB C 28.12 0.30 1 217 362 47 ARG N N 123.33 0.40 1 218 363 48 GLY H H 8.56 0.04 1 219 363 48 GLY C C 172.32 0.30 1 220 363 48 GLY CA C 43.44 0.30 1 221 363 48 GLY N N 113.28 0.40 1 222 364 49 LEU H H 7.63 0.04 1 223 364 49 LEU HD2 H 0.94 0.04 1 224 364 49 LEU CA C 55.55 0.30 1 225 364 49 LEU CB C 39.72 0.30 1 226 364 49 LEU CD2 C 26.62 0.30 1 227 364 49 LEU N N 120.39 0.40 1 228 366 51 ALA H H 7.00 0.04 1 229 366 51 ALA C C 174.68 0.30 1 230 366 51 ALA CA C 49.61 0.30 1 231 366 51 ALA CB C 19.06 0.30 1 232 366 51 ALA N N 112.73 0.40 1 233 367 52 SER H H 8.09 0.04 1 234 367 52 SER C C 173.03 0.30 1 235 367 52 SER CA C 57.11 0.30 1 236 367 52 SER CB C 59.20 0.30 1 237 367 52 SER N N 112.05 0.40 1 238 368 53 ILE H H 7.60 0.04 1 239 368 53 ILE HD1 H -0.06 0.04 1 240 368 53 ILE C C 172.11 0.30 1 241 368 53 ILE CA C 60.51 0.30 1 242 368 53 ILE CB C 37.59 0.30 1 243 368 53 ILE CD1 C 13.99 0.30 1 244 368 53 ILE N N 114.47 0.40 1 245 369 54 ASN H H 9.19 0.04 1 246 369 54 ASN CA C 54.01 0.30 1 247 369 54 ASN CB C 40.45 0.30 1 248 369 54 ASN N N 114.34 0.40 1 249 370 55 THR H H 7.47 0.04 1 250 370 55 THR C C 167.90 0.30 1 251 370 55 THR CA C 61.13 0.30 1 252 370 55 THR CB C 67.52 0.30 1 253 370 55 THR N N 109.29 0.40 1 254 371 56 ALA H H 8.67 0.04 1 255 371 56 ALA C C 172.74 0.30 1 256 371 56 ALA CA C 49.92 0.30 1 257 371 56 ALA CB C 22.42 0.30 1 258 371 56 ALA N N 126.30 0.40 1 259 372 57 TYR H H 8.85 0.04 1 260 372 57 TYR C C 167.96 0.30 1 261 372 57 TYR CA C 55.36 0.30 1 262 372 57 TYR CB C 39.45 0.30 1 263 372 57 TYR N N 117.07 0.40 1 264 373 58 GLU H H 8.40 0.04 1 265 373 58 GLU C C 172.14 0.30 1 266 373 58 GLU CA C 53.00 0.30 1 267 373 58 GLU CB C 30.02 0.30 1 268 373 58 GLU N N 122.65 0.40 1 269 374 59 ARG H H 7.91 0.04 1 270 374 59 ARG C C 174.59 0.30 1 271 374 59 ARG CA C 53.66 0.30 1 272 374 59 ARG CB C 29.90 0.30 1 273 374 59 ARG N N 123.91 0.40 1 274 375 60 LYS H H 8.07 0.04 1 275 375 60 LYS C C 174.37 0.30 1 276 375 60 LYS CA C 58.77 0.30 1 277 375 60 LYS CB C 30.34 0.30 1 278 375 60 LYS N N 121.67 0.40 1 279 376 61 ASP H H 7.62 0.04 1 280 376 61 ASP C C 174.31 0.30 1 281 376 61 ASP CA C 52.21 0.30 1 282 376 61 ASP CB C 38.19 0.30 1 283 376 61 ASP N N 114.87 0.40 1 284 377 62 GLY H H 7.92 0.04 1 285 377 62 GLY C C 171.70 0.30 1 286 377 62 GLY CA C 43.56 0.30 1 287 377 62 GLY N N 109.05 0.40 1 288 378 63 LYS H H 7.34 0.04 1 289 378 63 LYS C C 172.10 0.30 1 290 378 63 LYS CA C 55.82 0.30 1 291 378 63 LYS CB C 30.13 0.30 1 292 378 63 LYS N N 119.44 0.40 1 293 379 64 PHE H H 8.50 0.04 1 294 379 64 PHE C C 171.75 0.30 1 295 379 64 PHE CA C 51.66 0.30 1 296 379 64 PHE CB C 38.84 0.30 1 297 379 64 PHE N N 119.23 0.40 1 298 380 65 VAL H H 8.74 0.04 1 299 380 65 VAL HG1 H 0.61 0.04 1 300 380 65 VAL HG2 H 0.65 0.04 1 301 380 65 VAL C C 171.66 0.30 1 302 380 65 VAL CA C 59.30 0.30 1 303 380 65 VAL CB C 30.94 0.30 1 304 380 65 VAL CG1 C 22.57 0.30 1 305 380 65 VAL CG2 C 20.75 0.30 1 306 380 65 VAL N N 123.08 0.40 1 307 381 66 PHE H H 8.71 0.04 1 308 381 66 PHE C C 172.77 0.30 1 309 381 66 PHE CA C 55.06 0.30 1 310 381 66 PHE CB C 42.87 0.30 1 311 381 66 PHE N N 122.01 0.40 1 312 382 67 PHE H H 8.78 0.04 1 313 382 67 PHE C C 173.30 0.30 1 314 382 67 PHE CA C 56.28 0.30 1 315 382 67 PHE CB C 40.68 0.30 1 316 382 67 PHE N N 119.14 0.40 1 317 383 68 LYS H H 8.84 0.04 1 318 383 68 LYS C C 173.40 0.30 1 319 383 68 LYS CA C 56.60 0.30 1 320 383 68 LYS CB C 33.86 0.30 1 321 383 68 LYS N N 121.98 0.40 1 322 384 69 GLY H H 9.09 0.04 1 323 384 69 GLY C C 170.47 0.30 1 324 384 69 GLY CA C 46.33 0.30 1 325 384 69 GLY N N 121.23 0.40 1 326 385 70 ASP H H 7.96 0.04 1 327 385 70 ASP C C 172.72 0.30 1 328 385 70 ASP CA C 52.12 0.30 1 329 385 70 ASP CB C 37.90 0.30 1 330 385 70 ASP N N 123.94 0.40 1 331 386 71 LYS H H 7.78 0.04 1 332 386 71 LYS C C 172.13 0.30 1 333 386 71 LYS CA C 53.24 0.30 1 334 386 71 LYS CB C 36.03 0.30 1 335 386 71 LYS N N 118.02 0.40 1 336 387 72 HIS H H 8.18 0.04 1 337 387 72 HIS C C 169.23 0.30 1 338 387 72 HIS CA C 53.27 0.30 1 339 387 72 HIS CB C 30.88 0.30 1 340 387 72 HIS N N 112.46 0.40 1 341 388 73 TRP H H 9.16 0.04 1 342 388 73 TRP C C 170.61 0.30 1 343 388 73 TRP CA C 58.10 0.30 1 344 388 73 TRP CB C 34.21 0.30 1 345 388 73 TRP N N 121.17 0.40 1 346 389 74 VAL HG1 H 0.56 0.04 1 347 389 74 VAL HG2 H 0.61 0.04 1 348 389 74 VAL CA C 59.63 0.30 1 349 389 74 VAL CB C 31.78 0.30 1 350 389 74 VAL CG1 C 21.66 0.30 1 351 389 74 VAL CG2 C 22.25 0.30 1 352 391 76 ASP H H 8.54 0.04 1 353 391 76 ASP C C 173.46 0.30 1 354 391 76 ASP CA C 51.08 0.30 1 355 391 76 ASP CB C 39.89 0.30 1 356 391 76 ASP N N 121.31 0.40 1 357 392 77 GLU H H 8.50 0.04 1 358 392 77 GLU CA C 58.22 0.30 1 359 392 77 GLU N N 124.54 0.40 1 360 394 79 SER H H 8.21 0.04 1 361 394 79 SER C C 170.92 0.30 1 362 394 79 SER CA C 56.68 0.30 1 363 394 79 SER CB C 62.78 0.30 1 364 394 79 SER N N 116.21 0.40 1 365 395 80 LEU H H 8.64 0.04 1 366 395 80 LEU HD1 H 0.47 0.04 1 367 395 80 LEU HD2 H 0.49 0.04 1 368 395 80 LEU C C 173.97 0.30 1 369 395 80 LEU CA C 54.17 0.30 1 370 395 80 LEU CB C 39.54 0.30 1 371 395 80 LEU CD1 C 24.11 0.30 1 372 395 80 LEU CD2 C 24.91 0.30 1 373 395 80 LEU N N 133.51 0.40 1 374 396 81 GLU H H 8.33 0.04 1 375 396 81 GLU C C 171.36 0.30 1 376 396 81 GLU CA C 54.10 0.30 1 377 396 81 GLU CB C 28.12 0.30 1 378 396 81 GLU N N 130.33 0.40 1 379 398 83 GLY H H 8.54 0.04 1 380 398 83 GLY CA C 44.04 0.30 1 381 398 83 GLY N N 109.70 0.40 1 382 399 84 TYR H H 7.29 0.04 1 383 399 84 TYR C C 170.50 0.30 1 384 399 84 TYR CA C 55.97 0.30 1 385 399 84 TYR CB C 36.75 0.30 1 386 399 84 TYR N N 117.16 0.40 1 387 401 86 LYS H H 7.50 0.04 1 388 401 86 LYS C C 173.16 0.30 1 389 401 86 LYS CA C 53.05 0.30 1 390 401 86 LYS CB C 36.60 0.30 1 391 401 86 LYS N N 116.01 0.40 1 392 402 87 HIS H H 9.09 0.04 1 393 402 87 HIS C C 175.96 0.30 1 394 402 87 HIS CA C 56.81 0.30 1 395 402 87 HIS CB C 29.70 0.30 1 396 402 87 HIS N N 125.67 0.40 1 397 403 88 ILE H H 8.36 0.04 1 398 403 88 ILE HD1 H 0.57 0.04 1 399 403 88 ILE C C 175.50 0.30 1 400 403 88 ILE CA C 64.82 0.30 1 401 403 88 ILE CB C 36.37 0.30 1 402 403 88 ILE CD1 C 13.14 0.30 1 403 403 88 ILE N N 125.46 0.40 1 404 405 90 GLU H H 8.01 0.04 1 405 405 90 GLU C C 175.53 0.30 1 406 405 90 GLU CA C 55.55 0.30 1 407 405 90 GLU CB C 27.77 0.30 1 408 405 90 GLU N N 115.94 0.40 1 409 406 91 LEU H H 7.79 0.04 1 410 406 91 LEU HD1 H 1.24 0.04 1 411 406 91 LEU C C 173.99 0.30 1 412 406 91 LEU CA C 56.46 0.30 1 413 406 91 LEU CB C 40.45 0.30 1 414 406 91 LEU CD1 C 24.77 0.30 1 415 406 91 LEU N N 122.37 0.40 1 416 407 92 GLY H H 6.57 0.04 1 417 407 92 GLY C C 168.37 0.30 1 418 407 92 GLY CA C 43.71 0.30 1 419 407 92 GLY N N 100.42 0.40 1 420 408 93 ARG H H 8.00 0.04 1 421 408 93 ARG C C 174.32 0.30 1 422 408 93 ARG CA C 55.36 0.30 1 423 408 93 ARG CB C 30.23 0.30 1 424 408 93 ARG N N 119.88 0.40 1 425 409 94 GLY H H 8.47 0.04 1 426 409 94 GLY C C 171.48 0.30 1 427 409 94 GLY CA C 44.66 0.30 1 428 409 94 GLY N N 110.18 0.40 1 429 410 95 LEU H H 7.37 0.04 1 430 410 95 LEU HD1 H -0.09 0.04 1 431 410 95 LEU HD2 H 0.05 0.04 1 432 410 95 LEU C C 171.46 0.30 1 433 410 95 LEU CA C 51.35 0.30 1 434 410 95 LEU CB C 39.05 0.30 1 435 410 95 LEU CD1 C 25.46 0.30 1 436 410 95 LEU CD2 C 23.48 0.30 1 437 410 95 LEU N N 120.26 0.40 1 438 412 97 THR H H 8.02 0.04 1 439 412 97 THR C C 171.37 0.30 1 440 412 97 THR CA C 60.43 0.30 1 441 412 97 THR CB C 68.45 0.30 1 442 412 97 THR N N 107.35 0.40 1 443 413 98 ASP H H 8.55 0.04 1 444 413 98 ASP C C 171.65 0.30 1 445 413 98 ASP CA C 53.64 0.30 1 446 413 98 ASP CB C 39.17 0.30 1 447 413 98 ASP N N 119.01 0.40 1 448 414 99 LYS H H 7.76 0.04 1 449 414 99 LYS C C 169.41 0.30 1 450 414 99 LYS CA C 54.20 0.30 1 451 414 99 LYS CB C 31.61 0.30 1 452 414 99 LYS N N 116.84 0.40 1 453 415 100 ILE H H 8.99 0.04 1 454 415 100 ILE HD1 H -0.26 0.04 1 455 415 100 ILE C C 172.08 0.30 1 456 415 100 ILE CA C 58.06 0.30 1 457 415 100 ILE CB C 38.03 0.30 1 458 415 100 ILE CD1 C 10.54 0.30 1 459 415 100 ILE N N 118.47 0.40 1 460 416 101 ASP H H 8.00 0.04 1 461 416 101 ASP C C 172.09 0.30 1 462 416 101 ASP CA C 56.18 0.30 1 463 416 101 ASP CB C 40.36 0.30 1 464 416 101 ASP N N 122.45 0.40 1 465 417 102 ALA H H 7.37 0.04 1 466 417 102 ALA C C 171.87 0.30 1 467 417 102 ALA CA C 50.32 0.30 1 468 417 102 ALA CB C 19.10 0.30 1 469 417 102 ALA N N 113.15 0.40 1 470 418 103 ALA H H 8.00 0.04 1 471 418 103 ALA C C 171.25 0.30 1 472 418 103 ALA CA C 49.99 0.30 1 473 418 103 ALA CB C 21.57 0.30 1 474 418 103 ALA N N 124.68 0.40 1 475 419 104 LEU H H 8.77 0.04 1 476 419 104 LEU HD1 H 1.07 0.04 1 477 419 104 LEU C C 171.53 0.30 1 478 419 104 LEU CA C 52.16 0.30 1 479 419 104 LEU CB C 44.41 0.30 1 480 419 104 LEU CD1 C 22.98 0.30 1 481 419 104 LEU N N 123.84 0.40 1 482 420 105 PHE H H 8.97 0.04 1 483 420 105 PHE C C 171.11 0.30 1 484 420 105 PHE CA C 57.14 0.30 1 485 420 105 PHE CB C 38.02 0.30 1 486 420 105 PHE N N 128.49 0.40 1 487 421 106 TRP H H 8.98 0.04 1 488 421 106 TRP C C 170.62 0.30 1 489 421 106 TRP CA C 54.45 0.30 1 490 421 106 TRP CB C 27.92 0.30 1 491 421 106 TRP N N 134.40 0.40 1 492 422 107 MET H H 6.99 0.04 1 493 422 107 MET C C 171.89 0.30 1 494 422 107 MET CA C 58.44 0.30 1 495 422 107 MET CB C 29.01 0.30 1 496 422 107 MET N N 124.64 0.40 1 497 424 109 ASN H H 6.97 0.04 1 498 424 109 ASN C C 173.66 0.30 1 499 424 109 ASN CA C 50.51 0.30 1 500 424 109 ASN CB C 38.14 0.30 1 501 424 109 ASN N N 108.18 0.40 1 502 425 110 GLY H H 8.19 0.04 1 503 425 110 GLY C C 171.71 0.30 1 504 425 110 GLY CA C 45.65 0.30 1 505 425 110 GLY N N 109.25 0.40 1 506 426 111 LYS H H 7.86 0.04 1 507 426 111 LYS C C 170.68 0.30 1 508 426 111 LYS CA C 53.91 0.30 1 509 426 111 LYS CB C 32.10 0.30 1 510 426 111 LYS N N 121.41 0.40 1 511 427 112 THR H H 7.97 0.04 1 512 427 112 THR C C 170.69 0.30 1 513 427 112 THR CA C 60.17 0.30 1 514 427 112 THR CB C 69.72 0.30 1 515 427 112 THR N N 115.76 0.40 1 516 428 113 TYR H H 9.40 0.04 1 517 428 113 TYR C C 171.45 0.30 1 518 428 113 TYR CA C 54.82 0.30 1 519 428 113 TYR CB C 39.57 0.30 1 520 428 113 TYR N N 124.42 0.40 1 521 429 114 PHE H H 8.55 0.04 1 522 429 114 PHE C C 172.38 0.30 1 523 429 114 PHE CA C 53.64 0.30 1 524 429 114 PHE CB C 40.24 0.30 1 525 429 114 PHE N N 119.01 0.40 1 526 430 115 PHE H H 9.26 0.04 1 527 430 115 PHE C C 172.42 0.30 1 528 430 115 PHE CA C 56.28 0.30 1 529 430 115 PHE CB C 39.40 0.30 1 530 430 115 PHE N N 122.00 0.40 1 531 431 116 ARG H H 8.91 0.04 1 532 431 116 ARG C C 173.08 0.30 1 533 431 116 ARG CA C 53.92 0.30 1 534 431 116 ARG CB C 30.37 0.30 1 535 431 116 ARG N N 123.29 0.40 1 536 432 117 GLY H H 9.93 0.04 1 537 432 117 GLY C C 171.98 0.30 1 538 432 117 GLY CA C 46.49 0.30 1 539 432 117 GLY N N 121.86 0.40 1 540 433 118 ASN H H 8.44 0.04 1 541 433 118 ASN C C 172.05 0.30 1 542 433 118 ASN CA C 50.73 0.30 1 543 433 118 ASN CB C 36.35 0.30 1 544 433 118 ASN N N 127.00 0.40 1 545 434 119 LYS H H 8.32 0.04 1 546 434 119 LYS C C 172.35 0.30 1 547 434 119 LYS CA C 53.66 0.30 1 548 434 119 LYS CB C 36.44 0.30 1 549 434 119 LYS N N 119.69 0.40 1 550 435 120 TYR H H 8.84 0.04 1 551 435 120 TYR C C 169.69 0.30 1 552 435 120 TYR CA C 54.85 0.30 1 553 435 120 TYR CB C 41.04 0.30 1 554 435 120 TYR N N 116.08 0.40 1 555 436 121 TYR H H 9.20 0.04 1 556 436 121 TYR C C 170.72 0.30 1 557 436 121 TYR CA C 56.30 0.30 1 558 436 121 TYR CB C 39.60 0.30 1 559 436 121 TYR N N 118.38 0.40 1 560 437 122 ARG H H 5.28 0.04 1 561 437 122 ARG C C 169.60 0.30 1 562 437 122 ARG CA C 54.20 0.30 1 563 437 122 ARG CB C 29.87 0.30 1 564 437 122 ARG N N 124.50 0.40 1 565 438 123 PHE H H 9.48 0.04 1 566 438 123 PHE C C 169.50 0.30 1 567 438 123 PHE CA C 56.25 0.30 1 568 438 123 PHE CB C 41.90 0.30 1 569 438 123 PHE N N 130.10 0.40 1 570 439 124 ASN H H 7.61 0.04 1 571 439 124 ASN C C 172.65 0.30 1 572 439 124 ASN CA C 50.68 0.30 1 573 439 124 ASN CB C 37.91 0.30 1 574 439 124 ASN N N 125.96 0.40 1 575 440 125 GLU H H 8.87 0.04 1 576 440 125 GLU C C 175.54 0.30 1 577 440 125 GLU CA C 57.76 0.30 1 578 440 125 GLU CB C 28.32 0.30 1 579 440 125 GLU N N 125.77 0.40 1 580 441 126 GLU H H 8.17 0.04 1 581 441 126 GLU C C 175.52 0.30 1 582 441 126 GLU CA C 58.29 0.30 1 583 441 126 GLU CB C 27.54 0.30 1 584 441 126 GLU N N 119.29 0.40 1 585 442 127 LEU H H 7.24 0.04 1 586 442 127 LEU HD1 H 0.92 0.04 1 587 442 127 LEU HD2 H 0.84 0.04 1 588 442 127 LEU C C 173.76 0.30 1 589 442 127 LEU CA C 53.19 0.30 1 590 442 127 LEU CB C 40.41 0.30 1 591 442 127 LEU CD1 C 24.91 0.30 1 592 442 127 LEU CD2 C 22.21 0.30 1 593 442 127 LEU N N 117.23 0.40 1 594 443 128 ARG H H 7.64 0.04 1 595 443 128 ARG C C 172.31 0.30 1 596 443 128 ARG CA C 55.52 0.30 1 597 443 128 ARG CB C 24.64 0.30 1 598 443 128 ARG N N 115.94 0.40 1 599 444 129 ALA H H 6.94 0.04 1 600 444 129 ALA C C 173.97 0.30 1 601 444 129 ALA CA C 50.19 0.30 1 602 444 129 ALA CB C 20.88 0.30 1 603 444 129 ALA N N 118.71 0.40 1 604 445 130 VAL H H 8.19 0.04 1 605 445 130 VAL C C 172.77 0.30 1 606 445 130 VAL CA C 61.80 0.30 1 607 445 130 VAL CB C 31.49 0.30 1 608 445 130 VAL N N 124.05 0.40 1 609 446 131 ASP H H 8.26 0.04 1 610 446 131 ASP C C 174.23 0.30 1 611 446 131 ASP CA C 54.17 0.30 1 612 446 131 ASP CB C 40.64 0.30 1 613 446 131 ASP N N 128.65 0.40 1 614 447 132 SER H H 8.40 0.04 1 615 447 132 SER CA C 59.65 0.30 1 616 447 132 SER CB C 62.22 0.30 1 617 447 132 SER N N 115.55 0.40 1 618 448 133 GLU H H 8.69 0.04 1 619 448 133 GLU C C 171.32 0.30 1 620 448 133 GLU CA C 56.74 0.30 1 621 448 133 GLU CB C 25.82 0.30 1 622 448 133 GLU N N 116.07 0.40 1 623 449 134 TYR H H 7.45 0.04 1 624 449 134 TYR C C 170.40 0.30 1 625 449 134 TYR CA C 55.96 0.30 1 626 449 134 TYR CB C 36.93 0.30 1 627 449 134 TYR N N 116.07 0.40 1 628 451 136 LYS H H 7.61 0.04 1 629 451 136 LYS C C 171.49 0.30 1 630 451 136 LYS CA C 53.42 0.30 1 631 451 136 LYS CB C 35.48 0.30 1 632 451 136 LYS N N 118.50 0.40 1 633 452 137 ASN H H 8.48 0.04 1 634 452 137 ASN C C 173.91 0.30 1 635 452 137 ASN CA C 52.78 0.30 1 636 452 137 ASN CB C 38.88 0.30 1 637 452 137 ASN N N 120.06 0.40 1 638 453 138 ILE H H 8.39 0.04 1 639 453 138 ILE HD1 H 0.76 0.04 1 640 453 138 ILE C C 173.17 0.30 1 641 453 138 ILE CA C 63.06 0.30 1 642 453 138 ILE CB C 38.93 0.30 1 643 453 138 ILE CD1 C 14.62 0.30 1 644 453 138 ILE N N 124.00 0.40 1 645 454 139 LYS H H 8.69 0.04 1 646 454 139 LYS C C 174.40 0.30 1 647 454 139 LYS CA C 57.37 0.30 1 648 454 139 LYS CB C 30.07 0.30 1 649 454 139 LYS N N 123.47 0.40 1 650 455 140 VAL H H 7.44 0.04 1 651 455 140 VAL HG1 H 1.24 0.04 1 652 455 140 VAL HG2 H 0.78 0.04 1 653 455 140 VAL CA C 64.62 0.30 1 654 455 140 VAL CB C 31.28 0.30 1 655 455 140 VAL CG1 C 22.29 0.30 1 656 455 140 VAL CG2 C 20.86 0.30 1 657 455 140 VAL N N 118.87 0.40 1 658 458 143 GLY H H 8.57 0.04 1 659 458 143 GLY C C 171.66 0.30 1 660 458 143 GLY CA C 43.32 0.30 1 661 458 143 GLY N N 113.44 0.40 1 662 459 144 ILE H H 7.92 0.04 1 663 459 144 ILE HD1 H -0.25 0.04 1 664 459 144 ILE C C 171.64 0.30 1 665 459 144 ILE CA C 50.85 0.30 1 666 459 144 ILE CB C 40.94 0.30 1 667 459 144 ILE CD1 C 12.16 0.30 1 668 459 144 ILE N N 125.29 0.40 1 669 461 146 GLU H H 7.31 0.04 1 670 461 146 GLU C C 173.42 0.30 1 671 461 146 GLU CA C 54.49 0.30 1 672 461 146 GLU CB C 28.31 0.30 1 673 461 146 GLU N N 112.78 0.40 1 674 462 147 SER H H 8.43 0.04 1 675 462 147 SER C C 173.44 0.30 1 676 462 147 SER CA C 57.14 0.30 1 677 462 147 SER CB C 61.25 0.30 1 678 462 147 SER N N 112.08 0.40 1 679 464 149 ARG H H 8.11 0.04 1 680 464 149 ARG C C 175.58 0.30 1 681 464 149 ARG CA C 53.89 0.30 1 682 464 149 ARG CB C 30.16 0.30 1 683 464 149 ARG N N 112.60 0.40 1 684 465 150 GLY H H 7.83 0.04 1 685 465 150 GLY C C 169.37 0.30 1 686 465 150 GLY CA C 44.46 0.30 1 687 465 150 GLY N N 107.33 0.40 1 688 466 151 SER H H 9.37 0.04 1 689 466 151 SER C C 170.80 0.30 1 690 466 151 SER CA C 55.03 0.30 1 691 466 151 SER CB C 63.42 0.30 1 692 466 151 SER N N 118.47 0.40 1 693 467 152 PHE H H 8.05 0.04 1 694 467 152 PHE C C 170.94 0.30 1 695 467 152 PHE CA C 54.91 0.30 1 696 467 152 PHE CB C 38.56 0.30 1 697 467 152 PHE N N 119.37 0.40 1 698 468 153 MET H H 9.29 0.04 1 699 468 153 MET C C 174.34 0.30 1 700 468 153 MET CA C 54.89 0.30 1 701 468 153 MET CB C 33.42 0.30 1 702 468 153 MET N N 121.00 0.40 1 703 469 154 GLY H H 8.89 0.04 1 704 469 154 GLY C C 172.27 0.30 1 705 469 154 GLY CA C 44.08 0.30 1 706 469 154 GLY N N 109.25 0.40 1 707 471 156 ASP H H 7.85 0.04 1 708 471 156 ASP C C 173.54 0.30 1 709 471 156 ASP CA C 52.33 0.30 1 710 471 156 ASP CB C 40.22 0.30 1 711 471 156 ASP N N 119.27 0.40 1 712 473 158 VAL H H 8.16 0.04 1 713 473 158 VAL HG1 H 0.09 0.04 1 714 473 158 VAL HG2 H 0.75 0.04 1 715 473 158 VAL C C 172.15 0.30 1 716 473 158 VAL CA C 64.39 0.30 1 717 473 158 VAL CB C 30.34 0.30 1 718 473 158 VAL CG1 C 20.90 0.30 1 719 473 158 VAL CG2 C 22.32 0.30 1 720 473 158 VAL N N 123.70 0.40 1 721 474 159 PHE H H 7.70 0.04 1 722 474 159 PHE C C 173.07 0.30 1 723 474 159 PHE CA C 55.17 0.30 1 724 474 159 PHE CB C 41.09 0.30 1 725 474 159 PHE N N 115.61 0.40 1 726 475 160 THR H H 9.23 0.04 1 727 475 160 THR C C 169.60 0.30 1 728 475 160 THR CA C 61.74 0.30 1 729 475 160 THR CB C 69.93 0.30 1 730 475 160 THR N N 119.16 0.40 1 731 476 161 TYR H H 9.09 0.04 1 732 476 161 TYR C C 171.71 0.30 1 733 476 161 TYR CA C 55.92 0.30 1 734 476 161 TYR CB C 39.57 0.30 1 735 476 161 TYR N N 124.65 0.40 1 736 477 162 PHE H H 8.56 0.04 1 737 477 162 PHE C C 172.14 0.30 1 738 477 162 PHE CA C 55.44 0.30 1 739 477 162 PHE CB C 41.91 0.30 1 740 477 162 PHE N N 116.51 0.40 1 741 478 163 TYR H H 8.90 0.04 1 742 478 163 TYR C C 171.56 0.30 1 743 478 163 TYR CA C 55.64 0.30 1 744 478 163 TYR CB C 41.64 0.30 1 745 478 163 TYR N N 121.90 0.40 1 746 479 164 LYS H H 8.02 0.04 1 747 479 164 LYS C C 174.00 0.30 1 748 479 164 LYS CA C 57.78 0.30 1 749 479 164 LYS CB C 34.96 0.30 1 750 479 164 LYS N N 127.12 0.40 1 751 482 167 LYS H H 8.13 0.04 1 752 482 167 LYS C C 170.59 0.30 1 753 482 167 LYS CA C 54.31 0.30 1 754 482 167 LYS CB C 35.71 0.30 1 755 482 167 LYS N N 123.81 0.40 1 756 483 168 TYR H H 8.39 0.04 1 757 483 168 TYR C C 169.81 0.30 1 758 483 168 TYR CA C 54.79 0.30 1 759 483 168 TYR CB C 41.92 0.30 1 760 483 168 TYR N N 113.72 0.40 1 761 484 169 TRP H H 9.39 0.04 1 762 484 169 TRP C C 170.69 0.30 1 763 484 169 TRP CA C 57.99 0.30 1 764 484 169 TRP CB C 33.89 0.30 1 765 484 169 TRP N N 120.77 0.40 1 766 486 171 PHE H H 9.77 0.04 1 767 486 171 PHE C C 170.40 0.30 1 768 486 171 PHE CA C 57.12 0.30 1 769 486 171 PHE CB C 40.99 0.30 1 770 486 171 PHE N N 130.52 0.40 1 771 487 172 ASN H H 7.99 0.04 1 772 487 172 ASN C C 171.72 0.30 1 773 487 172 ASN CA C 51.96 0.30 1 774 487 172 ASN CB C 38.33 0.30 1 775 487 172 ASN N N 127.35 0.40 1 776 488 173 ASN H H 8.79 0.04 1 777 488 173 ASN C C 172.67 0.30 1 778 488 173 ASN CA C 54.58 0.30 1 779 488 173 ASN CB C 37.51 0.30 1 780 488 173 ASN N N 125.31 0.40 1 781 489 174 GLN H H 8.35 0.04 1 782 489 174 GLN C C 174.93 0.30 1 783 489 174 GLN CA C 56.59 0.30 1 784 489 174 GLN CB C 26.95 0.30 1 785 489 174 GLN N N 118.25 0.40 1 786 490 175 LYS H H 7.40 0.04 1 787 490 175 LYS C C 172.56 0.30 1 788 490 175 LYS CA C 55.20 0.30 1 789 490 175 LYS CB C 32.19 0.30 1 790 490 175 LYS N N 117.08 0.40 1 791 491 176 LEU H H 7.72 0.04 1 792 491 176 LEU HD1 H 0.74 0.04 1 793 491 176 LEU C C 172.10 0.30 1 794 491 176 LEU CA C 54.41 0.30 1 795 491 176 LEU CB C 36.11 0.30 1 796 491 176 LEU CD1 C 23.18 0.30 1 797 491 176 LEU N N 116.33 0.40 1 798 492 177 LYS H H 6.28 0.04 1 799 492 177 LYS C C 174.00 0.30 1 800 492 177 LYS CA C 53.92 0.30 1 801 492 177 LYS CB C 35.05 0.30 1 802 492 177 LYS N N 112.21 0.40 1 803 493 178 VAL H H 8.14 0.04 1 804 493 178 VAL HG1 H 1.41 0.04 1 805 493 178 VAL HG2 H 1.43 0.04 1 806 493 178 VAL C C 172.77 0.30 1 807 493 178 VAL CA C 62.62 0.30 1 808 493 178 VAL CB C 31.04 0.30 1 809 493 178 VAL CG1 C 24.50 0.30 1 810 493 178 VAL CG2 C 22.72 0.30 1 811 493 178 VAL N N 124.29 0.40 1 812 494 179 GLU H H 8.20 0.04 1 813 494 179 GLU C C 171.24 0.30 1 814 494 179 GLU CA C 53.90 0.30 1 815 494 179 GLU CB C 29.46 0.30 1 816 494 179 GLU N N 127.40 0.40 1 817 496 181 GLY H H 8.38 0.04 1 818 496 181 GLY C C 170.34 0.30 1 819 496 181 GLY CA C 43.79 0.30 1 820 496 181 GLY N N 110.17 0.40 1 821 497 182 TYR H H 7.10 0.04 1 822 497 182 TYR C C 170.68 0.30 1 823 497 182 TYR CA C 55.88 0.30 1 824 497 182 TYR CB C 37.07 0.30 1 825 497 182 TYR N N 116.70 0.40 1 826 499 184 LYS H H 7.32 0.04 1 827 499 184 LYS C C 172.16 0.30 1 828 499 184 LYS CA C 53.45 0.30 1 829 499 184 LYS CB C 35.36 0.30 1 830 499 184 LYS N N 118.55 0.40 1 831 501 186 ALA H H 8.91 0.04 1 832 501 186 ALA C C 176.62 0.30 1 833 501 186 ALA CA C 52.77 0.30 1 834 501 186 ALA CB C 16.73 0.30 1 835 501 186 ALA N N 132.31 0.40 1 836 502 187 LEU H H 7.09 0.04 1 837 502 187 LEU HD2 H 0.93 0.04 1 838 502 187 LEU C C 174.59 0.30 1 839 502 187 LEU CA C 56.52 0.30 1 840 502 187 LEU CB C 38.50 0.30 1 841 502 187 LEU CD2 C 23.58 0.30 1 842 502 187 LEU N N 116.37 0.40 1 843 503 188 ARG H H 7.33 0.04 1 844 503 188 ARG C C 175.44 0.30 1 845 503 188 ARG CA C 56.35 0.30 1 846 503 188 ARG CB C 29.27 0.30 1 847 503 188 ARG N N 117.39 0.40 1 848 504 189 ASP H H 7.15 0.04 1 849 504 189 ASP C C 174.19 0.30 1 850 504 189 ASP CA C 55.03 0.30 1 851 504 189 ASP CB C 38.49 0.30 1 852 504 189 ASP N N 115.00 0.40 1 853 505 190 TRP H H 7.62 0.04 1 854 505 190 TRP C C 174.20 0.30 1 855 505 190 TRP CA C 53.97 0.30 1 856 505 190 TRP CB C 29.67 0.30 1 857 505 190 TRP N N 116.27 0.40 1 858 506 191 MET H H 6.43 0.04 1 859 506 191 MET C C 172.98 0.30 1 860 506 191 MET CA C 52.64 0.30 1 861 506 191 MET CB C 29.63 0.30 1 862 506 191 MET N N 109.46 0.40 1 863 507 192 GLY H H 7.87 0.04 1 864 507 192 GLY C C 173.36 0.30 1 865 507 192 GLY CA C 45.63 0.30 1 866 507 192 GLY N N 106.19 0.40 1 867 508 193 CYS H H 7.79 0.04 1 868 508 193 CYS C C 170.15 0.30 1 869 508 193 CYS CA C 53.99 0.30 1 870 508 193 CYS CB C 39.27 0.30 1 871 508 193 CYS N N 119.50 0.40 1 872 511 196 GLY H H 6.82 0.04 1 873 511 196 GLY CA C 42.27 0.30 1 874 511 196 GLY N N 120.40 0.40 1 stop_ save_