data_16940 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N assignments for hirugen bound PPACKed thrombin ; _BMRB_accession_number 16940 _BMRB_flat_file_name bmr16940.str _Entry_type new _Submission_date 2010-05-20 _Accession_date 2010-05-20 _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 Lechtenberg Bernhard C. . 2 Johnson Daniel J.D. . 3 Freund Stefan M. . 4 Huntington James A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 253 "13C chemical shifts" 525 "15N chemical shifts" 253 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-12 update BMRB 'Complete entry citation' 2010-07-26 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20660315 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lechtenberg Bernhard C. . 2 Johnson Daniel J.D. . 3 Freund Stefan M.V. . 4 Huntington James A. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 107 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14087 _Page_last 14092 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Thrombin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Thrombin $Thrombin Hirugen $Hirugen PPACK $PPACK Sodium $NA 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_Thrombin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Thrombin _Molecular_mass 33810 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Thrombin is the main protease of the blood coagulation system' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 295 _Mol_residue_sequence ; TFGSGEADCGLRPLFEKKSL EDKTERELLESYIDGRIVEG SDAEIGMSPWQVMLFRKSPQ ELLCGASLISDRWVLTAAHC LLYPPWDKNFTENDLLVRIG KHSRTRYERNIEKISMLEKI YIHPRYNWRENLDRDIALMK LKKPVAFSDYIHPVCLPDRE TAASLLQAGYKGRVTGWGNL KETWTANVGKGQPSVLQVVN LPIVERPVCKDSTRIRITDN MFCAGYKPDEGKRGDACEGD SGGPFVMKSPFNNRWYQMGI VSWGEGCDRDGKYGFYTHVF RLKKWIQKVIDQFGE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 285 THR 2 286 PHE 3 287 GLY 4 288 SER 5 289 GLY 6 290 GLU 7 291 ALA 8 292 ASP 9 293 CYS 10 294 GLY 11 295 LEU 12 296 ARG 13 297 PRO 14 298 LEU 15 299 PHE 16 300 GLU 17 301 LYS 18 302 LYS 19 303 SER 20 304 LEU 21 305 GLU 22 306 ASP 23 307 LYS 24 308 THR 25 309 GLU 26 310 ARG 27 311 GLU 28 312 LEU 29 313 LEU 30 314 GLU 31 315 SER 32 316 TYR 33 317 ILE 34 318 ASP 35 319 GLY 36 320 ARG 37 321 ILE 38 322 VAL 39 323 GLU 40 324 GLY 41 325 SER 42 326 ASP 43 327 ALA 44 328 GLU 45 329 ILE 46 330 GLY 47 331 MET 48 332 SER 49 333 PRO 50 334 TRP 51 335 GLN 52 336 VAL 53 337 MET 54 338 LEU 55 339 PHE 56 340 ARG 57 341 LYS 58 342 SER 59 343 PRO 60 344 GLN 61 345 GLU 62 346 LEU 63 347 LEU 64 348 CYS 65 349 GLY 66 350 ALA 67 351 SER 68 352 LEU 69 353 ILE 70 354 SER 71 355 ASP 72 356 ARG 73 357 TRP 74 358 VAL 75 359 LEU 76 360 THR 77 361 ALA 78 362 ALA 79 363 HIS 80 364 CYS 81 365 LEU 82 366 LEU 83 367 TYR 84 368 PRO 85 369 PRO 86 370 TRP 87 371 ASP 88 372 LYS 89 373 ASN 90 374 PHE 91 375 THR 92 376 GLU 93 377 ASN 94 378 ASP 95 379 LEU 96 380 LEU 97 381 VAL 98 382 ARG 99 383 ILE 100 384 GLY 101 385 LYS 102 386 HIS 103 387 SER 104 388 ARG 105 389 THR 106 390 ARG 107 391 TYR 108 392 GLU 109 393 ARG 110 394 ASN 111 395 ILE 112 396 GLU 113 397 LYS 114 398 ILE 115 399 SER 116 400 MET 117 401 LEU 118 402 GLU 119 403 LYS 120 404 ILE 121 405 TYR 122 406 ILE 123 407 HIS 124 408 PRO 125 409 ARG 126 410 TYR 127 411 ASN 128 412 TRP 129 413 ARG 130 414 GLU 131 415 ASN 132 416 LEU 133 417 ASP 134 418 ARG 135 419 ASP 136 420 ILE 137 421 ALA 138 422 LEU 139 423 MET 140 424 LYS 141 425 LEU 142 426 LYS 143 427 LYS 144 428 PRO 145 429 VAL 146 430 ALA 147 431 PHE 148 432 SER 149 433 ASP 150 434 TYR 151 435 ILE 152 436 HIS 153 437 PRO 154 438 VAL 155 439 CYS 156 440 LEU 157 441 PRO 158 442 ASP 159 443 ARG 160 444 GLU 161 445 THR 162 446 ALA 163 447 ALA 164 448 SER 165 449 LEU 166 450 LEU 167 451 GLN 168 452 ALA 169 453 GLY 170 454 TYR 171 455 LYS 172 456 GLY 173 457 ARG 174 458 VAL 175 459 THR 176 460 GLY 177 461 TRP 178 462 GLY 179 463 ASN 180 464 LEU 181 465 LYS 182 466 GLU 183 467 THR 184 468 TRP 185 469 THR 186 470 ALA 187 471 ASN 188 472 VAL 189 473 GLY 190 474 LYS 191 475 GLY 192 476 GLN 193 477 PRO 194 478 SER 195 479 VAL 196 480 LEU 197 481 GLN 198 482 VAL 199 483 VAL 200 484 ASN 201 485 LEU 202 486 PRO 203 487 ILE 204 488 VAL 205 489 GLU 206 490 ARG 207 491 PRO 208 492 VAL 209 493 CYS 210 494 LYS 211 495 ASP 212 496 SER 213 497 THR 214 498 ARG 215 499 ILE 216 500 ARG 217 501 ILE 218 502 THR 219 503 ASP 220 504 ASN 221 505 MET 222 506 PHE 223 507 CYS 224 508 ALA 225 509 GLY 226 510 TYR 227 511 LYS 228 512 PRO 229 513 ASP 230 514 GLU 231 515 GLY 232 516 LYS 233 517 ARG 234 518 GLY 235 519 ASP 236 520 ALA 237 521 CYS 238 522 GLU 239 523 GLY 240 524 ASP 241 525 SER 242 526 GLY 243 527 GLY 244 528 PRO 245 529 PHE 246 530 VAL 247 531 MET 248 532 LYS 249 533 SER 250 534 PRO 251 535 PHE 252 536 ASN 253 537 ASN 254 538 ARG 255 539 TRP 256 540 TYR 257 541 GLN 258 542 MET 259 543 GLY 260 544 ILE 261 545 VAL 262 546 SER 263 547 TRP 264 548 GLY 265 549 GLU 266 550 GLY 267 551 CYS 268 552 ASP 269 553 ARG 270 554 ASP 271 555 GLY 272 556 LYS 273 557 TYR 274 558 GLY 275 559 PHE 276 560 TYR 277 561 THR 278 562 HIS 279 563 VAL 280 564 PHE 281 565 ARG 282 566 LEU 283 567 LYS 284 568 LYS 285 569 TRP 286 570 ILE 287 571 GLN 288 572 LYS 289 573 VAL 290 574 ILE 291 575 ASP 292 576 GLN 293 577 PHE 294 578 GLY 295 579 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 1A2C "Structure Of Thrombin Inhibited By Aeruginosin298-a From A Blue-green Alga" 87.80 259 100.00 100.00 0.00e+00 PDB 1A3B "Complex Of Human Alpha-Thrombin With The Bifunctional Boronate Inhibitor Borolog1" 87.80 259 100.00 100.00 0.00e+00 PDB 1A3E "Complex Of Human Alpha-Thrombin With The Bifunctional Boronate Inhibitor Borolog2" 87.80 259 100.00 100.00 0.00e+00 PDB 1A46 "Thrombin Complexed With Hirugen And A Beta-Strand Mimetic Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1A4W "Crystal Structures Of Thrombin With Thiazole-Containing Inhibitors: Probes Of The S1' Binding Site" 87.80 259 100.00 100.00 0.00e+00 PDB 1A5G "Human Thrombin Complexed With Novel Synthetic Peptide Mimetic Inhibitor And Hirugen" 87.80 259 100.00 100.00 0.00e+00 PDB 1A61 "Thrombin Complexed With A Beta-Mimetic Thiazole-Containing Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1ABI "Structure Of The Hirulog 3-Thrombin Complex And Nature Of The S' Subsites Of Substrates And Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1ABJ "Structure Of The Hirulog 3-Thrombin Complex And Nature Of The S' Subsites Of Substrates And Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1AD8 "Complex Of Thrombin With And Inhibitor Containing A Novel P1 Moiety" 87.80 259 100.00 100.00 0.00e+00 PDB 1AE8 "Human Alpha-Thrombin Inhibition By Eoc-D-Phe-Pro-Azalys-Onp" 87.80 259 100.00 100.00 0.00e+00 PDB 1AFE "Human Alpha-Thrombin Inhibition By Cbz-Pro-Azalys-Onp" 87.80 259 100.00 100.00 0.00e+00 PDB 1AHT "Crystal Structure Of Human Alpha-Thrombin Complexed With Hirugen And P-Amidinophenylpyruvate At 1.6 Angstroms Resolution" 87.80 259 100.00 100.00 0.00e+00 PDB 1AI8 "Human Alpha-Thrombin Ternary Complex With The Exosite Inhibitor Hirugen And Active Site Inhibitor Phch2oco-D-Dpa-Pro-Borompg" 87.80 259 100.00 100.00 0.00e+00 PDB 1AIX "Human Alpha-Thrombin Ternary Complex With Exosite Inhibitor Hirugen And Active Site Inhibitor Phch2oco-D-Dpa-Pro-Boroval" 87.80 259 100.00 100.00 0.00e+00 PDB 1AWF "Novel Covalent Thrombin Inhibitor From Plant Extract" 87.80 259 100.00 100.00 0.00e+00 PDB 1AWH "Novel Covalent Thrombin Inhibitor From Plant Extract" 87.80 259 100.00 100.00 0.00e+00 PDB 1AY6 "Thrombin Inhibitor From Theonalla, Cyclotheanamide-Based Macrocyclic Tripeptide Motif" 87.80 259 100.00 100.00 0.00e+00 PDB 1B5G "Human Thrombin Complexed With Novel Synthetic Peptide Mimetic Inhibitor And Hirugen" 87.80 259 100.00 100.00 0.00e+00 PDB 1B7X "Structure Of Human Alpha-Thrombin Y225i Mutant Bound To D- Phe-Pro-Arg-Chloromethylketone" 87.80 259 99.61 99.61 0.00e+00 PDB 1BA8 "Thrombin Inhibitor With A Rigid Tripeptidyl Aldehydes" 87.80 259 100.00 100.00 0.00e+00 PDB 1BB0 "Thrombin Inhibitors With Rigid Tripeptidyl Aldehydes" 87.80 259 100.00 100.00 0.00e+00 PDB 1BCU "Alpha-Thrombin Complexed With Hirugen And Proflavin" 87.80 259 100.00 100.00 0.00e+00 PDB 1BMM "Human Alpha-Thrombin Complexed With [s-(R,R)]-4-[(Aminoiminomethyl) Amino]-N-[[1-[3-Hydroxy-2-[(2-Naphthalenylsulfonyl)amino]-1" 87.80 259 100.00 100.00 0.00e+00 PDB 1BMN "Human Alpha-Thrombin Complexed With [s-(R,R)]-1-(Aminoiminomethyl)- N-[[1-[n-[(2-Naphthalenylsulfonyl)-L-Seryl]-Pyrrolidinyl]me" 87.80 259 100.00 100.00 0.00e+00 PDB 1BTH "Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor" 87.80 259 99.23 99.61 0.00e+00 PDB 1C1U "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" 87.80 259 100.00 100.00 0.00e+00 PDB 1C1V "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" 87.80 259 100.00 100.00 0.00e+00 PDB 1C1W "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" 87.80 259 100.00 100.00 0.00e+00 PDB 1C4U "Selective Non Electrophilic Thrombin Inhibitors With Cyclohexyl Moieties." 87.80 259 100.00 100.00 0.00e+00 PDB 1C4V "Selective Non Electrophilic Thrombin Inhibitors With Cyclohexyl Moieties." 87.80 259 100.00 100.00 0.00e+00 PDB 1C4Y "Selective Non-Electrophilic Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1C5L "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" 87.80 259 100.00 100.00 0.00e+00 PDB 1C5N "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" 87.80 259 100.00 100.00 0.00e+00 PDB 1C5O "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" 87.80 259 100.00 100.00 0.00e+00 PDB 1CA8 "Thrombin Inhibitors With Rigid Tripeptidyl Aldehydes" 87.80 259 100.00 100.00 0.00e+00 PDB 1D3D "Crystal Structure Of Human Alpha Thrombin In Complex With Benzothiophene Inhibitor 4" 87.12 257 100.00 100.00 0.00e+00 PDB 1D3P "Crystal Structure Of Human Aplha-Thrombin In Complex With Benzo[b]thiophene Inhibitor 3" 87.80 259 100.00 100.00 0.00e+00 PDB 1D3Q "Crystal Structure Of Human Alpha Thrombin In Complex With Benzo[b]thiophene Inhibitor 2" 87.80 259 100.00 100.00 0.00e+00 PDB 1D3T "Crystal Structure Of Human Alpha Thrombin In Complex With Benzo[b]thiophene Inhibitor 1" 87.80 259 100.00 100.00 0.00e+00 PDB 1D4P "Crystal Structure Of Human Alpha Thrombin In Complex With 5- Amidinoindole-4-benzylpiperidine Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1D6W "Structure Of Thrombin Complexed With Selective Non-Electrophilic Inhibitors Having Cyclohexyl Moieties At P1" 97.29 287 100.00 100.00 0.00e+00 PDB 1D9I "Structure Of Thrombin Complexed With Selective Non-Electophilic Inhibitors Having Cyclohexyl Moieties At P1" 97.63 288 100.00 100.00 0.00e+00 PDB 1DE7 "Interaction Of Factor Xiii Activation Peptide With Alpha-Thrombin: Crystal Structure Of The Enzyme-Substrate Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1DIT "Complex Of A Divalent Inhibitor With Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1DM4 "Ser195ala Mutant Of Human Thrombin Complexed With Fibrinopeptide A (7- 16)" 88.14 260 99.62 100.00 0.00e+00 PDB 1DOJ "Crystal Structure Of Human Alpha-ThrombinRwj-51438 Complex At 1.7 A" 100.00 295 100.00 100.00 0.00e+00 PDB 1DWB "Crystallographic Analysis At 3.0-angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-directed Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1DWC "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1DWD "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1DWE "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1DX5 "Crystal Structure Of The Thrombin-Thrombomodulin Complex" 87.80 259 99.61 99.61 0.00e+00 PDB 1E0F "Crystal Structure Of The Human Alpha-Thrombin-Haemadin Complex: An Exosite Ii-Binding Inhibitor" 87.80 259 99.61 99.61 0.00e+00 PDB 1EB1 "Complex Structure Of Human Thrombin With N-Methyl-Arginine Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 1EOJ "Design Of P1' And P3' Residues Of Trivalent Thrombin Inhibitors And Their Crystal Structures" 97.97 289 99.65 99.65 0.00e+00 PDB 1EOL "Design Of P1' And P3' Residues Of Trivalent Thrombin Inhibitors And Their Crystal Structures" 97.97 289 99.65 99.65 0.00e+00 PDB 1FPC "Active Site Mimetic Inhibition Of Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1FPH "The Interaction Of Thrombin With Fibrinogen: A Structural Basis For Its Specificity" 87.80 259 100.00 100.00 0.00e+00 PDB 1G30 "Thrombin Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1G32 "Thrombin Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1G37 "Crystal Structure Of Human Alpha-thrombin Complexed With Bch-10556 And Exosite-directed Peptide" 97.29 287 100.00 100.00 0.00e+00 PDB 1GHV "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" 87.12 257 100.00 100.00 0.00e+00 PDB 1GHW "A Novel Serine Protease Inhibition Motif Involving A Multi-centered Short Hydrogen Bonding Network At The Active Site" 87.12 257 100.00 100.00 0.00e+00 PDB 1GHX "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" 87.12 257 100.00 100.00 0.00e+00 PDB 1GHY "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" 87.12 257 100.00 100.00 0.00e+00 PDB 1GJ4 "Selectivity At S1, H2o Displacement, Upa, Tpa, Ser190/ala190 Protease, Structure-based Drug Design" 87.46 258 100.00 100.00 0.00e+00 PDB 1GJ5 "Selectivity At S1, H2o Displacement, Upa, Tpa, Ser190ALA190 PROTEASE, Structure-Based Drug Design" 87.46 258 100.00 100.00 0.00e+00 PDB 1H8D "X-Ray Structure Of The Human Alpha-Thrombin Complex With A Tripeptide Phosphonate Inhibitor" 87.46 260 97.29 97.29 0.00e+00 PDB 1H8I "X-Ray Crystal Structure Of Human Alpha-Thrombin With A Tripeptide Phosphonate Inhibitor" 87.80 253 97.68 97.68 0.00e+00 PDB 1HAG "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" 100.00 295 100.00 100.00 0.00e+00 PDB 1HAH "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" 87.80 259 100.00 100.00 0.00e+00 PDB 1HAI "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" 87.80 259 100.00 100.00 0.00e+00 PDB 1HAO "Complex Of Human Alpha-thrombin With A 15mer Oligonucleotide Ggttggtgtggttgg (based On Nmr Model Of Dna)" 87.80 259 100.00 100.00 0.00e+00 PDB 1HAP "Complex Of Human Alpha-Thrombin With A 15mer Oligonucleotide Ggttggtgtggttgg (Based On X-Ray Model Of Dna)" 87.80 259 100.00 100.00 0.00e+00 PDB 1HBT "Human Alpha-Thrombin Complexed With A Peptidyl Pyridinium Methyl Ketone Containing Bivalent Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1HDT "Structure Of A Retro-Binding Peptide Inhibitor Complexed With Human Alpha-Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1HGT "Structure Of The Hirugen And Hirulog 1 Complexes Of Alpha- Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1HLT "The Structure Of A Nonadecapeptide Of The Fifth Egf Domain Of Thrombomodulin Complexed With Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1HUT "The Structure Of Alpha-Thrombin Inhibited By A 15-Mer Single-Stranded Dna Aptamer" 87.80 259 100.00 100.00 0.00e+00 PDB 1HXE "Serine Protease" 87.80 259 100.00 100.00 0.00e+00 PDB 1HXF "Human Thrombin Complex With Hirudin Variant" 87.80 259 100.00 100.00 0.00e+00 PDB 1IHS "Crystal Structure Of The Complex Of Human Alpha-thrombin And Non- Hydrolyzable Bifunctional Inhibitors, Hirutonin-2 And Hiruton" 87.80 259 100.00 100.00 0.00e+00 PDB 1IHT "Crystal Structure Of The Complex Of Human Alpha-Thrombin And Non- Hydrolyzable Bifunctional Inhibitors, Hirutonin-2 And Hiruton" 87.80 259 100.00 100.00 0.00e+00 PDB 1JMO "Crystal Structure Of The Heparin Cofactor Ii-S195a Thrombin Complex" 88.14 260 99.62 100.00 0.00e+00 PDB 1JOU "Crystal Structure Of Native S195a Thrombin With An Unoccupied Active Site" 87.80 259 99.61 100.00 0.00e+00 PDB 1JWT "Crystal Structure Of Thrombin In Complex With A Novel Bicyclic Lactam Inhibitor" 100.00 305 100.00 100.00 0.00e+00 PDB 1K21 "Human Thrombin-Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1K22 "Human Thrombin-inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1KTS "Thrombin Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1KTT "Thrombin Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1LHC "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boroarg-Oh" 87.80 259 100.00 100.00 0.00e+00 PDB 1LHD "Human Alpha-thrombin Complexed With Ac-(d)phe-pro-borolys-oh" 87.80 259 100.00 100.00 0.00e+00 PDB 1LHE "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boro-N- Butyl-Amidino-Glycine-Oh" 87.80 259 100.00 100.00 0.00e+00 PDB 1LHF "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boro- Homolys-Oh" 87.80 259 100.00 100.00 0.00e+00 PDB 1LHG "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro- Boroornithine-Oh" 87.80 259 100.00 100.00 0.00e+00 PDB 1MH0 "Crystal Structure Of The Anticoagulant Slow Form Of Thrombin" 97.29 287 99.65 99.65 0.00e+00 PDB 1MU6 "Crystal Structure Of Thrombin In Complex With L-378,622" 87.80 259 100.00 100.00 0.00e+00 PDB 1MU8 Thrombin-Hirugen_l-378,650 87.80 259 100.00 100.00 0.00e+00 PDB 1MUE Thrombin-Hirugen-L405,426 87.80 259 100.00 100.00 0.00e+00 PDB 1NM6 "Thrombin In Complex With Selective Macrocyclic Inhibitor At 1.8a" 97.29 287 100.00 100.00 0.00e+00 PDB 1NO9 "Design Of Weakly Basic Thrombin Inhibitors Incorporating Novel P1 Binding Functions: Molecular And X-Ray Crystallographic Studi" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRN "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRO "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRP "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRQ "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRR "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NRS "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" 87.80 259 100.00 100.00 0.00e+00 PDB 1NT1 "Thrombin In Complex With Selective Macrocyclic Inhibitor" 97.29 287 100.00 100.00 0.00e+00 PDB 1NU7 "Staphylocoagulase-Thrombin Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1NU9 "Staphylocoagulase-prethrombin-2 Complex" 98.64 291 100.00 100.00 0.00e+00 PDB 1NY2 "Human Alpha Thrombin Inhibited By Rppgf And Hirugen" 87.80 259 100.00 100.00 0.00e+00 PDB 1NZQ "D-Phe-Pro-Arg-Type Thrombin Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1O0D "Human Thrombin Complexed With A D-Phe-Pro-Arg-Type Inhibitor And A C- Terminal Hirudin Derived Exo-Site Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1O2G "Elaborate Manifold Of Short Hydrogen Bond Arrays Mediating Binding Of Active Site-Directed Serine Protease Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1O5G "Dissecting And Designing Inhibitor Selectivity Determinants At The S1 Site Using An Artificial Ala190 Protease (Ala190 Upa)" 87.80 259 100.00 100.00 0.00e+00 PDB 1OOK "Crystal Structure Of The Complex Of Platelet Receptor Gpib-alpha And Human Alpha-thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1OYT "Complex Of Recombinant Human Thrombin With A Designed Fluorinated Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1P8V "Crystal Structure Of The Complex Of Platelet Receptor Gpib-alpha And Alpha-thrombin At 2.6a" 87.80 259 100.00 100.00 0.00e+00 PDB 1PPB "The Refined 1.9 Angstroms Crystal Structure Of Human Alpha-Thrombin: Interaction With D-Phe-Pro-Arg Chloromethylketone And Sign" 87.80 259 100.00 100.00 0.00e+00 PDB 1QBV "Crystal Structure Of Thrombin Complexed With An Guanidine-Mimetic Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1QHR "Novel Covalent Active Site Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1QJ1 "Novel Covalent Active Site Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1QJ6 "Novel Covalent Active Site Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1QJ7 "Novel Covalent Active Site Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1QUR "Human Alpha-Thrombin In Complex With Bivalent, Benzamidine-Based Synthetic Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 1RD3 "2.5a Structure Of Anticoagulant Thrombin Variant E217k" 87.80 259 99.61 100.00 0.00e+00 PDB 1SB1 "Novel Non-Covalent Thrombin Inhibitors Incorporating P1 4,5,6,7- Tetrahydrobenzothiazole Arginine Side Chain Mimetics" 87.46 258 100.00 100.00 0.00e+00 PDB 1SFQ "Fast Form Of Thrombin Mutant R(77a)a Bound To Ppack" 87.80 259 99.61 99.61 0.00e+00 PDB 1SG8 "Crystal Structure Of The Procoagulant Fast Form Of Thrombin" 87.80 259 99.61 99.61 0.00e+00 PDB 1SGI "Crystal Structure Of The Anticoagulant Slow Form Of Thrombin" 87.80 259 99.61 99.61 0.00e+00 PDB 1SHH "Slow Form Of Thrombin Bound With Ppack" 87.80 259 99.61 99.61 0.00e+00 PDB 1SL3 "Crystal Structue Of Thrombin In Complex With A Potent P1 Heterocycle- Aryl Based Inhibitor" 97.29 287 100.00 100.00 0.00e+00 PDB 1SR5 "Antithrombin-anhydrothrombin-heparin Ternary Complex Structure" 87.80 259 100.00 100.00 0.00e+00 PDB 1T4U "Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1T4V "Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 1TA2 "Crystal Structure Of Thrombin In Complex With Compound 1" 97.29 287 100.00 100.00 0.00e+00 PDB 1TA6 "Crystal Structure Of Thrombin In Complex With Compound 14b" 97.29 287 100.00 100.00 0.00e+00 PDB 1TB6 "2.5a Crystal Structure Of The Antithrombin-Thrombin-Heparin Ternary Complex" 87.80 259 99.61 100.00 0.00e+00 PDB 1TBZ "Human Thrombin With Active Site N-Methyl-D Phenylalanyl-N-[5- (Aminoiminomethyl)amino]-1-{{benzothiazolyl)carbonyl] Butyl]-L- P" 87.80 259 100.00 100.00 0.00e+00 PDB 1THP "Structure Of Human Alpha-Thrombin Y225p Mutant Bound To D-Phe-Pro-Arg- Chloromethylketone" 87.80 259 99.61 99.61 0.00e+00 PDB 1THR "Structures Of Thrombin Complexes With A Designed And A Natural Exosite Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1THS "Structures Of Thrombin Complexes With A Designed And A Natural Exosite Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 1TMB "Molecular Basis For The Inhibition Of Human Alpha-thrombin By The Macrocyclic Peptide Cyclotheonamide A" 87.80 259 100.00 100.00 0.00e+00 PDB 1TMT "Changes In Interactions In Complexes Of Hirudin Derivatives And Human Alpha-Thrombin Due To Different Crystal Forms" 87.80 259 100.00 100.00 0.00e+00 PDB 1TMU "Changes In Interactions In Complexes Of Hirudin Derivatives And Human Alpha-Thrombin Due To Different Crystal Forms" 87.80 259 100.00 100.00 0.00e+00 PDB 1TOM "Alpha-Thrombin Complexed With Hirugen" 87.80 259 100.00 100.00 0.00e+00 PDB 1TQ0 "Crystal Structure Of The Potent Anticoagulant Thrombin Mutant W215aE217A IN FREE FORM" 87.12 257 99.22 99.22 0.00e+00 PDB 1TQ7 "Crystal Structure Of The Anticoagulant Thrombin Mutant W215aE217A Bound To Ppack" 87.12 257 99.22 99.22 0.00e+00 PDB 1TWX "Crystal Structure Of The Thrombin Mutant D221a/d222k" 87.80 259 99.23 99.23 0.00e+00 PDB 1UMA "Alpha-Thrombin (Hirugen) Complexed With Na-(N,N-Dimethylcarbamoyl)- Alpha-Azalysine" 87.80 259 100.00 100.00 0.00e+00 PDB 1UVS "Bovine Thrombin--Bm51.1011 Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 1VR1 "Specifity For Plasminogen Activator Inhibitor-1" 88.47 261 96.93 97.32 0.00e+00 PDB 1W7G "Alpha-Thrombin Complex With Sulfated Hirudin (Residues 54-65) And L- Arginine Template Inhibitor Cs107" 87.80 259 100.00 100.00 0.00e+00 PDB 1WAY "Active Site Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 1WBG "Active Site Thrombin Inhibitors" 87.80 259 99.23 99.23 0.00e+00 PDB 1XM1 "Nonbasic Thrombin Inhibitor Complex" 100.00 295 100.00 100.00 0.00e+00 PDB 1XMN "Crystal Structure Of Thrombin Bound To Heparin" 87.80 259 100.00 100.00 0.00e+00 PDB 1YPE "Thrombin Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 1YPG "Thrombin Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 1YPJ "Thrombin Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 1YPK "Thrombin Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 1YPL "X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue Ra-1008" 87.12 257 100.00 100.00 0.00e+00 PDB 1YPM "X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue Ra-1014" 87.12 257 100.00 100.00 0.00e+00 PDB 1Z71 "Thrombin And P2 Pyridine N-oxide Inhibitor Complex Structure" 97.29 287 100.00 100.00 0.00e+00 PDB 1Z8I "Crystal Structure Of The Thrombin Mutant G193a Bound To Ppack" 87.80 259 99.61 99.61 0.00e+00 PDB 1Z8J "Crystal Structure Of The Thrombin Mutant G193p Bound To Ppack" 87.80 259 99.61 99.61 0.00e+00 PDB 1ZGI "Thrombin In Complex With An Oxazolopyridine Inhibitor 21" 97.29 287 100.00 100.00 0.00e+00 PDB 1ZGV "Thrombin In Complex With An Oxazolopyridine Inhibitor 2" 97.29 287 100.00 100.00 0.00e+00 PDB 1ZRB "Thrombin In Complex With An Azafluorenyl Inhibitor 23b" 97.29 287 100.00 100.00 0.00e+00 PDB 2A0Q "Structure Of Thrombin In 400 Mm Potassium Chloride" 87.12 257 99.61 99.61 0.00e+00 PDB 2A2X "Orally Active Thrombin Inhibitors In Complex With Thrombin Inh12" 87.80 259 100.00 100.00 0.00e+00 PDB 2A45 'Crystal Structure Of The Complex Between Thrombin And The Central "e" Region Of Fibrin' 87.80 259 100.00 100.00 0.00e+00 PDB 2AFQ "1.9 Angstrom Crytal Structure Of Wild-Type Human Thrombin In The Sodium Free State" 87.80 259 100.00 100.00 0.00e+00 PDB 2ANK "Orally Active Thrombin Inhibitors In Complex With Thrombin And An Exosite Decapeptide" 87.80 259 100.00 100.00 0.00e+00 PDB 2ANM "Ternary Complex Of An Orally Active Thrombin Inhibitor With Human Thrombin And A C-Terminal Hirudin Derived Exo-Sit Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 2B5T "2.1 Angstrom Structure Of A Nonproductive Complex Between Antithrombin, Synthetic Heparin Mimetic Sr123781 And Two S195a Thromb" 87.80 259 99.61 100.00 0.00e+00 PDB 2BDY "Thrombin In Complex With Inhibitor" 97.97 289 100.00 100.00 0.00e+00 PDB 2BVR "Human Thrombin Complexed With Fragment-based Small Molecules Occupying The S1 Pocket" 87.80 252 97.30 97.30 0.00e+00 PDB 2BVS "Human Thrombin Complexed With Fragment-Based Small Molecules Occupying The S1 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2BVX "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-P2-Linker" 87.80 259 100.00 100.00 0.00e+00 PDB 2BXT "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-p2-linker" 87.80 259 100.00 100.00 0.00e+00 PDB 2BXU "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-p2-linker" 87.80 259 100.00 100.00 0.00e+00 PDB 2C8W "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2C8X "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2C8Y "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2C8Z "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2C90 "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2C93 "Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2CF8 "Complex Of Recombinant Human Thrombin With A Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 2CF9 "Complex Of Recombinant Human Thrombin With A Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 2CN0 "Complex Of Recombinant Human Thrombin With A Designed Inhibitor" 87.12 257 100.00 100.00 0.00e+00 PDB 2FEQ "Orally Active Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2FES "Orally Active Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2GDE "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 2GP9 "Crystal Structure Of The Slow Form Of Thrombin In A Self- Inhibited Conformation" 87.80 259 99.61 100.00 0.00e+00 PDB 2H9T "Crystal Structure Of Human Alpha-Thrombin In Complex With Suramin" 87.80 259 100.00 100.00 0.00e+00 PDB 2HGT "Structure Of The Hirugen And Hirulog 1 Complexes Of Alpha-Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 2HPP "Structures Of The Noncovalent Complexes Of Human And Bovine Prothrombin Fragment 2 With Human Ppack-Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 2HPQ "Structures Of The Noncovalent Complexes Of Human And Bovine Prothrombin Fragment 2 With Human Ppack-thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 2HWL "Crystal Structure Of Thrombin In Complex With Fibrinogen Gamma' Peptide" 87.80 259 99.61 99.61 0.00e+00 PDB 2JH0 "Human Thrombin Hirugen Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 2JH5 "Human Thrombin Hirugen Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 2JH6 "Human Thrombin Hirugen Inhibitor Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 2OD3 "Human Thrombin Chimera With Human Residues 184a, 186, 186a, 186b, 186c And 222 Replaced By Murine Thrombin Equivalents" 87.80 259 97.68 98.84 0.00e+00 PDB 2PGB "Inhibitor-Free Human Thrombin Mutant C191a-C220a" 87.80 259 99.23 99.23 0.00e+00 PDB 2PGQ "Human Thrombin Mutant C191a-c220a In Complex With The Inhibitor Ppack" 87.80 259 99.23 99.23 0.00e+00 PDB 2PW8 "Crystal Structure Of Sulfo-Hirudin Complexed To Thrombin" 87.46 258 100.00 100.00 0.00e+00 PDB 2R2M "2-(2-chloro-6-fluorophenyl)acetamides As Potent Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 2THF "Structure Of Human Alpha-thrombin Y225f Mutant Bound To D-phe-pro-arg- Chloromethylketone" 87.80 259 99.61 100.00 0.00e+00 PDB 2UUF "Thrombin-hirugen Binary Complex At 1.26a Resolution" 87.80 259 100.00 100.00 0.00e+00 PDB 2UUJ "Thrombin-hirugen-gw473178 Ternary Complex At 1.32a Resolution" 87.80 259 100.00 100.00 0.00e+00 PDB 2UUK "Thrombin-hirugen-gw420128 Ternary Complex At 1.39a Resolution" 87.80 259 100.00 100.00 0.00e+00 PDB 2V3H "Thrombin With 3-cycle No F" 87.12 257 100.00 100.00 0.00e+00 PDB 2V3O "Thrombin With 3-cycle With F" 87.12 257 100.00 100.00 0.00e+00 PDB 2ZC9 "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZDA "Exploring Thrombin S1 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZDV "Exploring Thrombin S1 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZF0 "Exploring Thrombin S1 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZFF "Exploring Thrombin S1-pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZFP "Thrombin Inibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZFQ "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZFR "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZG0 "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZGB "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZGX "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZHE "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZHF "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZHQ "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZHW "Exploring Thrombin S3 Pocket" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZI2 "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZIQ "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZNK "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 2ZO3 "Bisphenylic Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 3B23 "Crystal Structure Of Thrombin-Variegin Complex: Insights Of A Novel Mechanism Of Inhibition And Design Of Tunable Thrombin Inhi" 87.80 259 100.00 100.00 0.00e+00 PDB 3B9F "1.6 A Structure Of The Pci-Thrombin-Heparin Complex" 87.80 259 99.61 100.00 0.00e+00 PDB 3BEF "Crystal Structure Of Thrombin Bound To The Extracellular Fragment Of Par1" 87.80 259 99.61 100.00 0.00e+00 PDB 3BEI "Crystal Structure Of The Slow Form Of Thrombin In A Self_inhibited Conformation" 87.80 259 99.61 100.00 0.00e+00 PDB 3BF6 "Thrombin:suramin Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 3BIU "Human Thrombin-In Complex With Ub-Thr10" 87.12 257 100.00 100.00 0.00e+00 PDB 3BIV "Human Thrombin-In Complex With Ub-Thr11" 87.12 257 100.00 100.00 0.00e+00 PDB 3BV9 "Structure Of Thrombin Bound To The Inhibitor Fm19" 87.80 259 99.61 99.61 0.00e+00 PDB 3C1K "Crystal Structure Of Thrombin In Complex With Inhibitor 15" 97.29 287 100.00 100.00 0.00e+00 PDB 3C27 "Cyanofluorophenylacetamides As Orally Efficacious Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 3D49 "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 3DA9 "Crystal Structure Of Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 3DD2 "Crystal Structure Of An Rna Aptamer Bound To Human Thrombin" 87.46 258 100.00 100.00 0.00e+00 PDB 3DHK "Bisphenylic Thrombin Inhibitors" 87.80 259 100.00 100.00 0.00e+00 PDB 3DT0 "Understanding Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 3DUX "Understanding Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 3E6P "Crystal Structure Of Human Meizothrombin Desf1" 87.80 259 100.00 100.00 0.00e+00 PDB 3EE0 "Crystal Structure Of The W215aE217A MUTANT OF HUMAN Thrombin (Space Group P2(1)2(1)2(1))" 87.80 259 99.23 99.23 0.00e+00 PDB 3EGK "Knoble Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 3EQ0 "Thrombin Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 3F68 "Thrombin Inhibition" 87.80 259 100.00 100.00 0.00e+00 PDB 3GIS "Crystal Structure Of Na-Free Thrombin In Complex With Thrombomodulin" 87.80 259 99.61 100.00 0.00e+00 PDB 3HAT "Active Site Mimetic Inhibition Of Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 3HKJ "Crystal Structure Of Human Thrombin Mutant W215aE217A IN COMPLEX WITH The Extracellular Fragment Of Human Par1" 87.80 259 99.23 99.23 0.00e+00 PDB 3HTC "The Structure Of A Complex Of Recombinant Hirudin And Human Alpha-Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 3JZ1 "Crystal Structure Of Human Thrombin Mutant N143p In E:na+ Form" 87.80 259 99.61 99.61 0.00e+00 PDB 3JZ2 "Crystal Structure Of Human Thrombin Mutant N143p In E Form" 87.80 259 99.61 99.61 0.00e+00 PDB 3K65 "Crystal Structure Of Prethombin-2/fragment-2 Complex" 100.00 308 99.66 100.00 0.00e+00 PDB 3LDX "Discovery And Clinical Evaluation Of Rwj-671818, A Thrombin Inhibitor With An Oxyguanidine P1 Motif" 87.80 259 100.00 100.00 0.00e+00 PDB 3LU9 "Crystal Structure Of Human Thrombin Mutant S195a In Complex Extracellular Fragment Of Human Par1" 87.80 259 99.61 100.00 0.00e+00 PDB 3NXP "Crystal Structure Of Human Prethrombin-1" 100.00 424 100.00 100.00 0.00e+00 PDB 3P17 "Thrombin Inhibition By Pyridin Derivatives" 87.80 259 100.00 100.00 0.00e+00 PDB 3P6Z "Structural Basis Of Thrombin Mediated Factor V Activation: Essential Role Of The Hirudin-Like Sequence Glu666-Glu672 For Proces" 87.80 259 100.00 100.00 0.00e+00 PDB 3P70 "Structural Basis Of Thrombin-Mediated Factor V Activation: Essential Role Of The Hirudin-Like Sequence Glu666-Glu672 For Proces" 87.80 259 100.00 100.00 0.00e+00 PDB 3PMH "Mechanism Of Sulfotyrosine-Mediated Glycoprotein Ib Interaction With Two Distinct Alpha-Thrombin Sites" 87.80 259 100.00 100.00 0.00e+00 PDB 3QDZ "Crystal Structure Of The Human Thrombin Mutant D102n In Complex With The Extracellular Fragment Of Human Par4." 87.80 259 99.61 100.00 0.00e+00 PDB 3QGN "The Allosteric E-E Equilibrium Is A Key Property Of The Trypsin Fold" 87.80 259 99.61 99.61 0.00e+00 PDB 3QLP "X-Ray Structure Of The Complex Between Human Alpha Thrombin And A Modified Thrombin Binding Aptamer (Mtba)" 87.80 259 100.00 100.00 0.00e+00 PDB 3QTO "Thrombin Inhibition By Pyridin Derivatives" 87.80 259 100.00 100.00 0.00e+00 PDB 3QTV "Thrombin Inhibition By Pyridin Derivatives" 87.80 259 100.00 100.00 0.00e+00 PDB 3QWC "Thrombin Inhibition By Pyridin Derivatives" 87.80 259 100.00 100.00 0.00e+00 PDB 3QX5 "Thrombin Inhibition By Pyridin Derivatives" 87.80 259 100.00 100.00 0.00e+00 PDB 3R3G "Structure Of Human Thrombin With Residues 145-150 Of Murine Thrombin" 87.80 259 97.68 98.84 0.00e+00 PDB 3RLW "Human Thrombin In Complex With Mi328" 87.80 259 100.00 100.00 0.00e+00 PDB 3RLY "Human Thrombin In Complex With Mi329" 87.80 259 100.00 100.00 0.00e+00 PDB 3RM0 "Human Thrombin In Complex With Mi354" 87.80 259 100.00 100.00 0.00e+00 PDB 3RM2 "Human Thrombin In Complex With Mi003" 87.80 259 100.00 100.00 0.00e+00 PDB 3RML "Human Thrombin In Complex With Mi331" 87.80 259 100.00 100.00 0.00e+00 PDB 3RMM "Human Thrombin In Complex With Mi332" 87.80 259 100.00 100.00 0.00e+00 PDB 3RMN "Human Thrombin In Complex With Mi341" 87.80 259 100.00 100.00 0.00e+00 PDB 3RMO "Human Thrombin In Complex With Mi004" 87.80 259 100.00 100.00 0.00e+00 PDB 3S7H "Structure Of Thrombin Mutant Y225p In The E Form" 87.80 259 99.61 99.61 0.00e+00 PDB 3S7K "Structure Of Thrombin Mutant Y225p In The E Form" 87.80 259 99.61 99.61 0.00e+00 PDB 3SHA "Human Thrombin In Complex With Ubthr97" 87.80 259 100.00 100.00 0.00e+00 PDB 3SHC "Human Thrombin In Complex With Ubthr101" 87.80 259 100.00 100.00 0.00e+00 PDB 3SI3 "Human Thrombin In Complex With Ubthr103" 87.80 259 100.00 100.00 0.00e+00 PDB 3SI4 "Human Thrombin In Complex With Ubthr104" 87.80 259 100.00 100.00 0.00e+00 PDB 3SQE "Crystal Structure Of Prethrombin-2 Mutant S195a In The Alternative Form" 98.31 290 99.66 100.00 0.00e+00 PDB 3SQH "Crystal Structure Of Prethrombin-2 Mutant S195a In The The Open Form" 98.31 290 99.66 100.00 0.00e+00 PDB 3SV2 "Human Thrombin In Complex With Ubthr105" 87.80 259 100.00 100.00 0.00e+00 PDB 3T5F "Human Thrombin In Complex With Mi340" 87.80 259 100.00 100.00 0.00e+00 PDB 3TU7 "Human Alpha-Thrombin Complexed With N-(Methylsulfonyl)-D-Phenylalanyl- N-((1-Carbamimidoyl-4-Piperidinyl)methyl)-L-Prolinamide " 87.80 259 100.00 100.00 0.00e+00 PDB 3U69 "Unliganded Wild-Type Human Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 3U8O "Human Thrombin Complexed With D-phe-pro-d-arg-d-thr" 87.80 259 100.00 100.00 0.00e+00 PDB 3U8R "Human Thrombin Complexed With D-phe-pro-d-arg-ile" 87.80 259 100.00 100.00 0.00e+00 PDB 3U8T "Human Thrombin Complexed With D-phe-pro-d-arg-cys" 87.80 259 100.00 100.00 0.00e+00 PDB 3U98 "Human Thrombin In Complex With Mi001" 87.80 259 100.00 100.00 0.00e+00 PDB 3U9A "Human Thrombin In Complex With Mi330" 87.80 259 100.00 100.00 0.00e+00 PDB 3UTU "High Affinity Inhibitor Of Human Thrombin" 87.80 259 100.00 100.00 0.00e+00 PDB 3UWJ "Human Thrombin In Complex With Mi353" 87.80 259 100.00 100.00 0.00e+00 PDB 3VXE "Human Alpha-thrombin-bivalirudin Complex At Pd5.0" 87.80 259 100.00 100.00 0.00e+00 PDB 3VXF "X/n Joint Refinement Of Human Alpha-thrombin-bivalirudin Complex Pd5" 87.46 259 100.00 100.00 0.00e+00 PDB 4AX9 "Human Thrombin Complexed With Napsagatran, Ro0466240" 87.12 257 100.00 100.00 0.00e+00 PDB 4AYV "Human Thrombin - Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 4AYY "Human Thrombin - Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 4AZ2 "Human Thrombin - Inhibitor Complex" 87.12 257 100.00 100.00 0.00e+00 PDB 4BAH "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BAK "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BAM "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BAN "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BAO "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BAQ "Thrombin In Complex With Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4BOH "Madanins (merops I53) Are Cleaved By Thrombin And Factor Xa" 87.80 259 100.00 100.00 0.00e+00 PDB 4CH2 "Low-salt Crystal Structure Of A Thrombin-gpibalpha Peptide Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 4CH8 "High-salt Crystal Structure Of A Thrombin-gpibalpha Peptide Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 4DIH "X-Ray Structure Of The Complex Between Human Alpha Thrombin And Thrombin Binding Aptamer In The Presence Of Sodium Ions" 87.80 259 100.00 100.00 0.00e+00 PDB 4DII "X-Ray Structure Of The Complex Between Human Alpha Thrombin And Thrombin Binding Aptamer In The Presence Of Potassium Ions" 87.80 259 100.00 100.00 0.00e+00 PDB 4DT7 "Crystal Structure Of Thrombin Bound To The Activation Domain Qedqvdprlidgkmtrrgds Of Protein C" 87.80 259 99.61 100.00 0.00e+00 PDB 4DY7 "Crystal Structures Of Protease Nexin-1 In Complex With S195a Thrombin" 87.80 259 99.61 100.00 0.00e+00 PDB 4E05 "Anophelin From The Malaria Vector Inhibits Thrombin Through A Novel Reverse-Binding Mechanism" 87.80 259 100.00 100.00 0.00e+00 PDB 4E06 "Anophelin From The Malaria Vector Inhibits Thrombin Through A Novel Reverse-Binding Mechanism" 87.80 259 100.00 100.00 0.00e+00 PDB 4E7R "Thrombin In Complex With 3-Amidinophenylalanine Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4H6S "Crystal Structure Of Thrombin Mutant E14ea/d14la/e18a/s195a" 87.80 259 99.23 99.61 0.00e+00 PDB 4H6T "Crystal Structure Of Prethrombin-2 Mutant E14ea/d14la/e18a/s195a" 100.00 306 98.64 98.98 0.00e+00 PDB 4HFP "Structure Of Thrombin Mutant S195a Bound To The Active Site Inhibitor Argatroban" 87.80 259 99.61 100.00 0.00e+00 PDB 4HTC "The Refined Structure Of The Hirudin-Thrombin Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 4HZH "Structure Of Recombinant Gla-domainless Prothrombin Mutant S525a" 100.00 533 99.66 100.00 0.00e+00 PDB 4I7Y "Crystal Structure Of Human Alpha Thrombin In Complex With A 27-mer Aptamer Bound To Exosite Ii" 87.80 259 100.00 100.00 0.00e+00 PDB 4LOY "Crystal Structure Analysis Of Thrombin In Complex With Compound D57, 5-chlorothiophene-2-carboxylic Acid [(s)-2-[2-methyl-3-(2-" 87.12 257 100.00 100.00 0.00e+00 PDB 4LXB "Crystal Structure Analysis Of Thrombin In Complex With Compound D58" 87.80 259 100.00 100.00 0.00e+00 PDB 4LZ1 "X-ray Structure Of The Complex Between Human Thrombin And The Tba Deletion Mutant Lacking Thymine 12 Nucleobase" 87.80 259 100.00 100.00 0.00e+00 PDB 4LZ4 "X-ray Structure Of The Complex Between Human Thrombin And The Tba Deletion Mutant Lacking Thymine 3 Nucleobase" 87.80 259 100.00 100.00 0.00e+00 PDB 4MLF "Crystal Structure For The Complex Of Thrombin Mutant D102n And Hirudin" 87.80 259 99.61 100.00 0.00e+00 PDB 4N3L "Crystal Structure Of Thrombin In Complex With A Novel Glucose- Conjugated Potent Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4NZE "Crystal Structure Of Thrombin In Complex With A Novel Tetra-o-acetyl- Glucopyranoside-conjugated Potent Inhibitor" 87.80 259 100.00 100.00 0.00e+00 PDB 4NZQ "Crystal Structure Of Ca2+-free Prothrombin Deletion Mutant Residues 146-167" 100.00 557 100.00 100.00 0.00e+00 PDB 4O03 "Crystal Structure Of Ca2+ Bound Prothrombin Deletion Mutant Residues 146-167" 100.00 557 100.00 100.00 0.00e+00 PDB 4RKJ "Crystal Structure Of Thrombin Mutant S195t (free Form)" 87.80 259 99.61 100.00 0.00e+00 PDB 4RKO "Crystal Structure Of Thrombin Mutant S195t Bound With Ppack" 87.80 259 99.61 100.00 0.00e+00 PDB 4RN6 "Structure Of Prethrombin-2 Mutant S195a Bound To The Active Site Inhibitor Argatroban" 98.31 290 99.66 100.00 0.00e+00 PDB 4THN "The Crystal Structure Of Alpha-Thrombin-Hirunorm Iv Complex Reveals A Novel Specificity Site Recognition Mode." 87.80 259 100.00 100.00 0.00e+00 PDB 4UD9 "Thrombin In Complex With 5-chlorothiophene-2-carboxamide" 87.80 259 100.00 100.00 0.00e+00 PDB 4UDW "Thrombin In Complex With 1-(2r)-2-amino-3-phenyl-propanoyl- N-(2,5dichlorophenyl)methylpyrrolidine-2-carboxamide" 87.46 258 100.00 100.00 0.00e+00 PDB 4UE7 "Thrombin In Complex With 1-amidinopiperidine" 87.46 258 100.00 100.00 0.00e+00 PDB 4UEH "Thrombin In Complex With Benzamidine" 87.46 258 100.00 100.00 0.00e+00 PDB 4YES "Thrombin In Complex With (s)-(4-chloro-2-((1-(5-methyl-1h-pyrrole-2- Carbonyl)pyrrolidine-2-carboxamido)methyl)phenyl)methanami" 87.80 259 100.00 100.00 0.00e+00 PDB 5AF9 "Thrombin In Complex With 4-methoxy-n-(2-pyridinyl)benzamide" 87.46 258 100.00 100.00 0.00e+00 PDB 5AFY "Thrombin In Complex With 3-chloro-benzamide" 87.46 258 100.00 100.00 0.00e+00 PDB 5AFZ "Thrombin In Complex With (2r)-2-(benzylsulfonylamino)-n-(2-((4-carbamimidoylphenyl)methylamino)-2-oxo-propyl)-3-phenyl- Propana" 87.46 258 100.00 100.00 0.00e+00 PDB 5AHG "Thrombin In Complex With ((4-chlorophenyl)sulfamoyl)) Diemethylamine" 87.46 258 100.00 100.00 0.00e+00 PDB 5GDS "Hirunorms Are True Hirudin Mimetics. The Crystal Structure Of Human Alpha-Thrombin:hirunorm V Complex" 87.80 259 100.00 100.00 0.00e+00 PDB 7KME "Crystal Structure Of Human Alpha-Thrombin Inhibited With Sel2711." 87.80 259 100.00 100.00 0.00e+00 PDB 8KME "Crystal Structure Of Human Alpha-thrombin Inhibited With Sel2770." 87.80 259 100.00 100.00 0.00e+00 DBJ BAD96495 "coagulation factor II precursor variant [Homo sapiens]" 100.00 622 99.66 99.66 0.00e+00 DBJ BAD96497 "coagulation factor II precursor variant [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 DBJ BAG35804 "unnamed protein product [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 DBJ BAG56844 "unnamed protein product [Homo sapiens]" 100.00 471 100.00 100.00 0.00e+00 DBJ BAG64719 "unnamed protein product [Homo sapiens]" 100.00 605 100.00 100.00 0.00e+00 EMBL CAA23842 "unnamed protein product [Homo sapiens]" 100.00 615 100.00 100.00 0.00e+00 EMBL CAH93129 "hypothetical protein [Pongo abelii]" 100.00 623 98.98 99.32 0.00e+00 EMBL CAJ01369 "prothrombin [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 GB AAC63054 "prothrombin [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 GB AAH51332 "Coagulation factor II (thrombin) [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 GB AAL77436 "coagulation factor II (thrombin) [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 GB AAR08142 "prothrombin [Homo sapiens]" 100.00 295 99.32 99.32 0.00e+00 GB AAR08143 "prothrombin B-chain [Homo sapiens]" 87.80 259 99.23 99.23 0.00e+00 REF NP_000497 "prothrombin isoform 1 preproprotein [Homo sapiens]" 100.00 622 100.00 100.00 0.00e+00 REF NP_001126851 "prothrombin precursor [Pongo abelii]" 100.00 623 98.98 99.32 0.00e+00 REF NP_001298186 "prothrombin isoform 2 [Homo sapiens]" 100.00 606 100.00 100.00 0.00e+00 REF XP_001165233 "PREDICTED: prothrombin isoform X1 [Pan troglodytes]" 100.00 622 100.00 100.00 0.00e+00 REF XP_003815248 "PREDICTED: prothrombin [Pan paniscus]" 100.00 622 100.00 100.00 0.00e+00 SP P00734 "RecName: Full=Prothrombin; AltName: Full=Coagulation factor II; Contains: RecName: Full=Activation peptide fragment 1; Contains" 100.00 622 100.00 100.00 0.00e+00 SP Q5R537 "RecName: Full=Prothrombin; AltName: Full=Coagulation factor II; Contains: RecName: Full=Activation peptide fragment 1; Contains" 100.00 623 98.98 99.32 0.00e+00 stop_ save_ save_Hirugen _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hirugen _Molecular_mass 1468 _Mol_thiol_state 'not present' _Details . _Residue_count 12 _Mol_residue_sequence GDFEEIPEEYLQ loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 PHE 4 GLU 5 GLU 6 ILE 7 PRO 8 GLU 9 GLU 10 TYR 11 LEU 12 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_PPACK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PPACK _Molecular_mass . _Mol_thiol_state 'not present' _Details Inhibitor _Residue_count 4 _Mol_residue_sequence FPRX loop_ _Residue_seq_code _Residue_label 1 PHE 2 PRO 3 ARG 4 CHM stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_CHM _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 1,3-DICHLORO-PROPAN-2-ONE _BMRB_code . _PDB_code CHM _Standard_residue_derivative . _Molecular_mass 126.969 _Mol_paramagnetic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 13:27:26 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? O O O . 0 . ? CL1 CL1 CL . 0 . ? CL3 CL3 CL . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H31 H31 H . 0 . ? H32 H32 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 C1 C2 ? ? SING C1 CL1 ? ? SING C1 H11 ? ? SING C1 H12 ? ? SING C2 C3 ? ? DOUB C2 O ? ? SING C3 CL3 ? ? SING C3 H31 ? ? SING C3 H32 ? ? stop_ save_ ############# # Ligands # ############# save_NA _Saveframe_category ligand _Mol_type non-polymer _Name_common "NA (SODIUM ION)" _BMRB_code . _PDB_code NA _Molecular_mass 22.990 _Mol_charge 1 _Mol_paramagnetic no _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 15:20:12 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons NA NA NA . 1 . ? stop_ _Mol_thiol_state 'not present' _Sequence_homology_query_date . save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name Thrombin 241 SER HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Thrombin 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 _Details $Thrombin 'recombinant technology' . . . . pET23a 'Expressed as prethrombin-2 in inclusion bodies and refolded.' $Hirugen 'obtained from a vendor' . . . . . . $PPACK 'obtained from a vendor' . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Thrombin 100 uM '[U-13C; U-15N; U-2H]' $Hirugen 110 uM 'natural abundance' $PPACK 100 uM 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_TROSY_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_1 save_ save_3D_HN(CA)NNH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)NNH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 310 . K pH 7.4 . pH pressure 1 . atm 'ionic strength' 150 . 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 water H 1 protons ppm 4.75 internal direct . . . 1 water C 13 protons ppm 4.75 internal indirect . . . 0.25144953 water N 15 protons ppm 4.75 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HN(CO)CACB' '3D TROSY HNCACB' '3D TROSY HNCA' '3D HN(CA)NNH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Thrombin _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 1 292 8 ASP CA C 50.46 0.30 1 2 292 8 ASP CB C 37.77 0.30 1 3 293 9 CYS H H 7.78 0.05 1 4 293 9 CYS CA C 52.17 0.30 1 5 293 9 CYS CB C 39.56 0.30 1 6 293 9 CYS N N 117.65 0.30 1 7 294 10 GLY H H 9.14 0.05 1 8 294 10 GLY CA C 45.32 0.30 1 9 294 10 GLY N N 104.65 0.30 1 10 295 11 LEU H H 7.33 0.05 1 11 295 11 LEU CA C 50.12 0.30 1 12 295 11 LEU CB C 39.89 0.30 1 13 295 11 LEU N N 120.23 0.30 1 14 296 12 ARG H H 8.64 0.05 1 15 296 12 ARG CA C 51.69 0.30 1 16 296 12 ARG CB C 26.58 0.30 1 17 296 12 ARG N N 120.65 0.30 1 18 297 13 PRO CA C 62.33 0.30 1 19 297 13 PRO CB C 30.41 0.30 1 20 298 14 LEU H H 7.75 0.05 1 21 298 14 LEU CA C 51.49 0.30 1 22 298 14 LEU CB C 37.39 0.30 1 23 298 14 LEU N N 109.83 0.30 1 24 299 15 PHE H H 7.07 0.05 1 25 299 15 PHE CA C 56.23 0.30 1 26 299 15 PHE CB C 36.82 0.30 1 27 299 15 PHE N N 113.57 0.30 1 28 300 16 GLU H H 9.01 0.05 1 29 300 16 GLU CA C 60.41 0.30 1 30 300 16 GLU CB C 25.86 0.30 1 31 300 16 GLU N N 125.88 0.30 1 32 301 17 LYS H H 7.76 0.05 1 33 301 17 LYS CA C 55.91 0.30 1 34 301 17 LYS CB C 27.80 0.30 1 35 301 17 LYS N N 113.83 0.30 1 36 302 18 LYS H H 7.22 0.05 1 37 302 18 LYS CA C 52.27 0.30 1 38 302 18 LYS CB C 29.89 0.30 1 39 302 18 LYS N N 117.02 0.30 1 40 303 19 SER H H 7.68 0.05 1 41 303 19 SER CA C 56.25 0.30 1 42 303 19 SER CB C 61.77 0.30 1 43 303 19 SER N N 112.52 0.30 1 44 304 20 LEU H H 7.84 0.05 1 45 304 20 LEU CA C 50.34 0.30 1 46 304 20 LEU CB C 41.30 0.30 1 47 304 20 LEU N N 120.49 0.30 1 48 305 21 GLU H H 8.36 0.05 1 49 305 21 GLU CA C 51.89 0.30 1 50 305 21 GLU CB C 28.92 0.30 1 51 305 21 GLU N N 121.99 0.30 1 52 306 22 ASP H H 9.70 0.05 1 53 306 22 ASP CA C 50.58 0.30 1 54 306 22 ASP CB C 37.68 0.30 1 55 306 22 ASP N N 125.37 0.30 1 56 307 23 LYS H H 9.97 0.05 1 57 307 23 LYS CA C 56.73 0.30 1 58 307 23 LYS CB C 29.90 0.30 1 59 307 23 LYS N N 117.58 0.30 1 60 308 24 THR H H 8.09 0.05 1 61 308 24 THR CA C 58.14 0.30 1 62 308 24 THR CB C 67.05 0.30 1 63 308 24 THR N N 104.28 0.30 1 64 309 25 GLU H H 8.04 0.05 1 65 309 25 GLU CA C 57.27 0.30 1 66 309 25 GLU CB C 26.34 0.30 1 67 309 25 GLU N N 123.41 0.30 1 68 310 26 ARG H H 8.87 0.05 1 69 310 26 ARG CA C 56.21 0.30 1 70 310 26 ARG CB C 25.23 0.30 1 71 310 26 ARG N N 122.65 0.30 1 72 311 27 GLU H H 7.55 0.05 1 73 311 27 GLU CA C 55.51 0.30 1 74 311 27 GLU CB C 25.71 0.30 1 75 311 27 GLU N N 118.67 0.30 1 76 312 28 LEU H H 7.09 0.05 1 77 312 28 LEU CA C 54.91 0.30 1 78 312 28 LEU CB C 39.29 0.30 1 79 312 28 LEU N N 117.77 0.30 1 80 313 29 LEU H H 7.15 0.05 1 81 313 29 LEU CA C 54.55 0.30 1 82 313 29 LEU CB C 37.41 0.30 1 83 313 29 LEU N N 120.35 0.30 1 84 314 30 GLU H H 8.34 0.05 1 85 314 30 GLU CA C 55.16 0.30 1 86 314 30 GLU CB C 25.84 0.30 1 87 314 30 GLU N N 116.95 0.30 1 88 315 31 SER H H 7.20 0.05 1 89 315 31 SER CA C 56.99 0.30 1 90 315 31 SER CB C 60.49 0.30 1 91 315 31 SER N N 114.85 0.30 1 92 316 32 TYR H H 6.59 0.05 1 93 316 32 TYR CA C 50.67 0.30 1 94 316 32 TYR CB C 35.27 0.30 1 95 316 32 TYR N N 121.67 0.30 1 96 317 33 ILE H H 7.10 0.05 1 97 317 33 ILE CA C 58.60 0.30 1 98 317 33 ILE CB C 35.72 0.30 1 99 317 33 ILE N N 118.40 0.30 1 100 318 34 ASP H H 8.06 0.05 1 101 318 34 ASP CA C 52.03 0.30 1 102 318 34 ASP CB C 37.69 0.30 1 103 318 34 ASP N N 128.04 0.30 1 104 319 35 GLY H H 8.30 0.05 1 105 319 35 GLY CA C 42.87 0.30 1 106 319 35 GLY N N 110.55 0.30 1 107 320 36 ARG H H 7.73 0.05 1 108 320 36 ARG CA C 54.52 0.30 1 109 320 36 ARG CB C 27.77 0.30 1 110 320 36 ARG N N 126.13 0.30 1 111 321 37 ILE CA C 54.26 0.30 1 112 321 37 ILE CB C 33.74 0.30 1 113 322 38 VAL H H 9.08 0.05 1 114 322 38 VAL CA C 57.64 0.30 1 115 322 38 VAL CB C 30.18 0.30 1 116 322 38 VAL N N 130.67 0.30 1 117 323 39 GLU H H 9.26 0.05 1 118 323 39 GLU CA C 54.58 0.30 1 119 323 39 GLU CB C 26.21 0.30 1 120 323 39 GLU N N 120.69 0.30 1 121 324 40 GLY H H 7.90 0.05 1 122 324 40 GLY CA C 41.23 0.30 1 123 324 40 GLY N N 106.22 0.30 1 124 325 41 SER H H 8.44 0.05 1 125 325 41 SER CA C 53.52 0.30 1 126 325 41 SER CB C 63.09 0.30 1 127 325 41 SER N N 112.94 0.30 1 128 326 42 ASP H H 8.37 0.05 1 129 326 42 ASP CA C 51.95 0.30 1 130 326 42 ASP CB C 36.92 0.30 1 131 326 42 ASP N N 121.23 0.30 1 132 327 43 ALA H H 8.86 0.05 1 133 327 43 ALA CA C 48.84 0.30 1 134 327 43 ALA CB C 15.50 0.30 1 135 327 43 ALA N N 125.81 0.30 1 136 328 44 GLU H H 7.23 0.05 1 137 328 44 GLU CA C 53.21 0.30 1 138 328 44 GLU CB C 28.85 0.30 1 139 328 44 GLU N N 121.01 0.30 1 140 329 45 ILE H H 8.56 0.05 1 141 329 45 ILE CA C 59.53 0.30 1 142 329 45 ILE CB C 32.87 0.30 1 143 329 45 ILE N N 125.26 0.30 1 144 330 46 GLY H H 9.08 0.05 1 145 330 46 GLY CA C 42.63 0.30 1 146 330 46 GLY N N 113.47 0.30 1 147 331 47 MET H H 7.61 0.05 1 148 331 47 MET CA C 54.08 0.30 1 149 331 47 MET CB C 30.91 0.30 1 150 331 47 MET N N 117.60 0.30 1 151 332 48 SER H H 8.89 0.05 1 152 332 48 SER CA C 54.23 0.30 1 153 332 48 SER CB C 59.60 0.30 1 154 332 48 SER N N 115.35 0.30 1 155 333 49 PRO CA C 62.49 0.30 1 156 333 49 PRO CB C 30.06 0.30 1 157 334 50 TRP H H 5.80 0.05 1 158 334 50 TRP CA C 51.39 0.30 1 159 334 50 TRP CB C 24.80 0.30 1 160 334 50 TRP N N 117.93 0.30 1 161 335 51 GLN H H 8.19 0.05 1 162 335 51 GLN CA C 54.92 0.30 1 163 335 51 GLN CB C 23.45 0.30 1 164 335 51 GLN N N 125.37 0.30 1 165 336 52 VAL H H 8.77 0.05 1 166 336 52 VAL CA C 58.53 0.30 1 167 336 52 VAL CB C 31.55 0.30 1 168 336 52 VAL N N 131.18 0.30 1 169 337 53 MET H H 8.95 0.05 1 170 337 53 MET CA C 52.20 0.30 1 171 337 53 MET CB C 33.43 0.30 1 172 337 53 MET N N 126.63 0.30 1 173 338 54 LEU H H 8.91 0.05 1 174 338 54 LEU CA C 52.11 0.30 1 175 338 54 LEU CB C 38.69 0.30 1 176 338 54 LEU N N 128.75 0.30 1 177 339 55 PHE H H 9.03 0.05 1 178 339 55 PHE CA C 53.48 0.30 1 179 339 55 PHE CB C 41.53 0.30 1 180 339 55 PHE N N 131.87 0.30 1 181 340 56 ARG H H 8.37 0.05 1 182 340 56 ARG CA C 53.37 0.30 1 183 340 56 ARG CB C 28.78 0.30 1 184 340 56 ARG N N 130.10 0.30 1 185 341 57 LYS H H 7.21 0.05 1 186 341 57 LYS CA C 56.96 0.30 1 187 341 57 LYS CB C 30.10 0.30 1 188 341 57 LYS N N 120.39 0.30 1 189 342 58 SER H H 7.71 0.05 1 190 342 58 SER CA C 51.94 0.30 1 191 342 58 SER CB C 60.99 0.30 1 192 342 58 SER N N 110.46 0.30 1 193 343 59 PRO CA C 59.86 0.30 1 194 343 59 PRO CB C 30.65 0.30 1 195 344 60 GLN H H 7.88 0.05 1 196 344 60 GLN CA C 53.30 0.30 1 197 344 60 GLN CB C 24.49 0.30 1 198 344 60 GLN N N 116.81 0.30 1 199 345 61 GLU H H 6.15 0.05 1 200 345 61 GLU CA C 51.74 0.30 1 201 345 61 GLU CB C 29.56 0.30 1 202 345 61 GLU N N 120.24 0.30 1 203 346 62 LEU H H 7.85 0.05 1 204 346 62 LEU CA C 53.41 0.30 1 205 346 62 LEU CB C 38.86 0.30 1 206 346 62 LEU N N 124.89 0.30 1 207 347 63 LEU H H 8.35 0.05 1 208 347 63 LEU CA C 52.62 0.30 1 209 347 63 LEU CB C 40.68 0.30 1 210 347 63 LEU N N 125.27 0.30 1 211 348 64 CYS H H 7.71 0.05 1 212 348 64 CYS CA C 52.87 0.30 1 213 348 64 CYS CB C 51.62 0.30 1 214 348 64 CYS N N 116.20 0.30 1 215 349 65 GLY H H 8.89 0.05 1 216 349 65 GLY CA C 44.07 0.30 1 217 349 65 GLY N N 106.62 0.30 1 218 350 66 ALA H H 7.97 0.05 1 219 350 66 ALA CA C 48.47 0.30 1 220 350 66 ALA CB C 17.40 0.30 1 221 350 66 ALA N N 117.39 0.30 1 222 351 67 SER H H 9.77 0.05 1 223 351 67 SER CA C 53.10 0.30 1 224 351 67 SER CB C 63.16 0.30 1 225 351 67 SER N N 114.86 0.30 1 226 352 68 LEU H H 9.36 0.05 1 227 352 68 LEU CA C 51.99 0.30 1 228 352 68 LEU CB C 41.38 0.30 1 229 352 68 LEU N N 126.70 0.30 1 230 353 69 ILE H H 8.08 0.05 1 231 353 69 ILE CA C 58.49 0.30 1 232 353 69 ILE CB C 35.83 0.30 1 233 353 69 ILE N N 118.32 0.30 1 234 354 70 SER H H 8.43 0.05 1 235 354 70 SER CA C 54.62 0.30 1 236 354 70 SER CB C 60.52 0.30 1 237 354 70 SER N N 116.96 0.30 1 238 355 71 ASP H H 8.91 0.05 1 239 355 71 ASP CA C 52.96 0.30 1 240 355 71 ASP CB C 36.69 0.30 1 241 355 71 ASP N N 115.83 0.30 1 242 356 72 ARG H H 7.79 0.05 1 243 356 72 ARG CA C 51.38 0.30 1 244 356 72 ARG CB C 29.53 0.30 1 245 356 72 ARG N N 114.31 0.30 1 246 357 73 TRP H H 7.19 0.05 1 247 357 73 TRP CA C 53.84 0.30 1 248 357 73 TRP CB C 29.50 0.30 1 249 357 73 TRP N N 118.34 0.30 1 250 358 74 VAL H H 9.12 0.05 1 251 358 74 VAL CA C 56.63 0.30 1 252 358 74 VAL CB C 32.25 0.30 1 253 358 74 VAL N N 121.09 0.30 1 254 359 75 LEU H H 9.56 0.05 1 255 359 75 LEU CA C 50.77 0.30 1 256 359 75 LEU CB C 42.78 0.30 1 257 359 75 LEU N N 129.92 0.30 1 258 360 76 THR H H 9.19 0.05 1 259 360 76 THR CA C 57.78 0.30 1 260 360 76 THR CB C 67.07 0.30 1 261 360 76 THR N N 120.87 0.30 1 262 361 77 ALA H H 8.02 0.05 1 263 361 77 ALA CA C 47.60 0.30 1 264 361 77 ALA CB C 15.51 0.30 1 265 361 77 ALA N N 123.33 0.30 1 266 362 78 ALA H H 6.47 0.05 1 267 362 78 ALA CA C 53.07 0.30 1 268 362 78 ALA CB C 12.87 0.30 1 269 362 78 ALA N N 127.79 0.30 1 270 363 79 HIS H H 10.46 0.05 1 271 363 79 HIS CA C 55.63 0.30 1 272 363 79 HIS CB C 27.05 0.30 1 273 363 79 HIS N N 116.50 0.30 1 274 364 80 CYS H H 6.85 0.05 1 275 364 80 CYS CA C 56.61 0.30 1 276 364 80 CYS CB C 41.00 0.30 1 277 364 80 CYS N N 116.63 0.30 1 278 365 81 LEU H H 7.38 0.05 1 279 365 81 LEU CA C 52.16 0.30 1 280 365 81 LEU CB C 39.46 0.30 1 281 365 81 LEU N N 116.68 0.30 1 282 366 82 LEU H H 8.10 0.05 1 283 366 82 LEU CA C 50.84 0.30 1 284 366 82 LEU CB C 40.39 0.30 1 285 366 82 LEU N N 119.80 0.30 1 286 367 83 TYR H H 9.21 0.05 1 287 367 83 TYR CA C 55.30 0.30 1 288 367 83 TYR CB C 33.94 0.30 1 289 367 83 TYR N N 125.83 0.30 1 290 369 85 PRO CA C 62.80 0.30 1 291 369 85 PRO CB C 26.91 0.30 1 292 370 86 TRP H H 7.02 0.05 1 293 370 86 TRP CA C 50.09 0.30 1 294 370 86 TRP CB C 27.31 0.30 1 295 370 86 TRP N N 113.50 0.30 1 296 371 87 ASP H H 8.58 0.05 1 297 371 87 ASP CA C 52.43 0.30 1 298 371 87 ASP CB C 36.29 0.30 1 299 371 87 ASP N N 119.30 0.30 1 300 372 88 LYS H H 6.71 0.05 1 301 372 88 LYS CA C 51.23 0.30 1 302 372 88 LYS CB C 28.68 0.30 1 303 372 88 LYS N N 115.85 0.30 1 304 373 89 ASN CA C 49.86 0.30 1 305 373 89 ASN CB C 34.78 0.30 1 306 374 90 PHE H H 8.63 0.05 1 307 374 90 PHE CA C 55.26 0.30 1 308 374 90 PHE CB C 38.19 0.30 1 309 374 90 PHE N N 122.39 0.30 1 310 375 91 THR H H 9.19 0.05 1 311 375 91 THR CA C 57.00 0.30 1 312 375 91 THR CB C 68.96 0.30 1 313 375 91 THR N N 111.76 0.30 1 314 376 92 GLU H H 10.18 0.05 1 315 376 92 GLU CA C 58.20 0.30 1 316 376 92 GLU CB C 24.74 0.30 1 317 376 92 GLU N N 119.20 0.30 1 318 377 93 ASN H H 8.01 0.05 1 319 377 93 ASN CA C 51.40 0.30 1 320 377 93 ASN CB C 35.82 0.30 1 321 377 93 ASN N N 113.89 0.30 1 322 378 94 ASP H H 7.82 0.05 1 323 378 94 ASP CA C 53.16 0.30 1 324 378 94 ASP CB C 40.83 0.30 1 325 378 94 ASP N N 116.13 0.30 1 326 379 95 LEU H H 6.96 0.05 1 327 379 95 LEU CA C 51.17 0.30 1 328 379 95 LEU CB C 43.23 0.30 1 329 379 95 LEU N N 117.20 0.30 1 330 380 96 LEU H H 8.97 0.05 1 331 380 96 LEU CA C 50.45 0.30 1 332 380 96 LEU CB C 43.20 0.30 1 333 380 96 LEU N N 117.81 0.30 1 334 381 97 VAL H H 8.27 0.05 1 335 381 97 VAL CA C 56.60 0.30 1 336 381 97 VAL CB C 29.88 0.30 1 337 381 97 VAL N N 114.35 0.30 1 338 382 98 ARG H H 8.71 0.05 1 339 382 98 ARG CA C 52.06 0.30 1 340 382 98 ARG CB C 28.69 0.30 1 341 382 98 ARG N N 120.95 0.30 1 342 383 99 ILE H H 9.83 0.05 1 343 383 99 ILE CA C 59.63 0.30 1 344 383 99 ILE CB C 37.00 0.30 1 345 383 99 ILE N N 130.55 0.30 1 346 384 100 GLY H H 8.81 0.05 1 347 384 100 GLY CA C 43.12 0.30 1 348 384 100 GLY N N 117.10 0.30 1 349 385 101 LYS H H 8.22 0.05 1 350 385 101 LYS CA C 54.85 0.30 1 351 385 101 LYS CB C 28.25 0.30 1 352 385 101 LYS N N 114.17 0.30 1 353 386 102 HIS H H 10.12 0.05 1 354 386 102 HIS CA C 56.98 0.30 1 355 386 102 HIS CB C 31.72 0.30 1 356 386 102 HIS N N 121.03 0.30 1 357 387 103 SER H H 9.64 0.05 1 358 387 103 SER CA C 55.44 0.30 1 359 387 103 SER CB C 60.56 0.30 1 360 387 103 SER N N 117.91 0.30 1 361 388 104 ARG H H 8.19 0.05 1 362 388 104 ARG CA C 56.16 0.30 1 363 388 104 ARG CB C 29.08 0.30 1 364 388 104 ARG N N 124.74 0.30 1 365 389 105 THR H H 7.06 0.05 1 366 389 105 THR CA C 58.82 0.30 1 367 389 105 THR CB C 66.95 0.30 1 368 389 105 THR N N 97.73 0.30 1 369 390 106 ARG H H 7.89 0.05 1 370 390 106 ARG CA C 53.54 0.30 1 371 390 106 ARG CB C 27.23 0.30 1 372 390 106 ARG N N 124.75 0.30 1 373 391 107 TYR H H 9.31 0.05 1 374 391 107 TYR CA C 53.40 0.30 1 375 391 107 TYR CB C 33.06 0.30 1 376 391 107 TYR N N 124.23 0.30 1 377 392 108 GLU H H 9.50 0.05 1 378 392 108 GLU CA C 52.00 0.30 1 379 392 108 GLU CB C 24.63 0.30 1 380 392 108 GLU N N 133.81 0.30 1 381 393 109 ARG H H 6.93 0.05 1 382 393 109 ARG CA C 54.97 0.30 1 383 393 109 ARG CB C 27.12 0.30 1 384 393 109 ARG N N 125.54 0.30 1 385 395 111 ILE H H 7.78 0.05 1 386 395 111 ILE CA C 60.16 0.30 1 387 395 111 ILE CB C 36.50 0.30 1 388 395 111 ILE N N 121.75 0.30 1 389 396 112 GLU H H 8.03 0.05 1 390 396 112 GLU CA C 51.89 0.30 1 391 396 112 GLU CB C 30.08 0.30 1 392 396 112 GLU N N 115.69 0.30 1 393 397 113 LYS H H 9.01 0.05 1 394 397 113 LYS CA C 50.59 0.30 1 395 397 113 LYS CB C 32.28 0.30 1 396 397 113 LYS N N 119.94 0.30 1 397 398 114 ILE H H 8.02 0.05 1 398 398 114 ILE CA C 57.61 0.30 1 399 398 114 ILE CB C 33.92 0.30 1 400 398 114 ILE N N 123.86 0.30 1 401 399 115 SER H H 8.84 0.05 1 402 399 115 SER CA C 54.83 0.30 1 403 399 115 SER CB C 62.84 0.30 1 404 399 115 SER N N 120.51 0.30 1 405 400 116 MET H H 8.63 0.05 1 406 400 116 MET CA C 52.23 0.30 1 407 400 116 MET CB C 30.96 0.30 1 408 400 116 MET N N 122.78 0.30 1 409 401 117 LEU H H 9.34 0.05 1 410 401 117 LEU CA C 51.20 0.30 1 411 401 117 LEU CB C 39.35 0.30 1 412 401 117 LEU N N 122.33 0.30 1 413 402 118 GLU H H 9.21 0.05 1 414 402 118 GLU CA C 54.13 0.30 1 415 402 118 GLU CB C 28.48 0.30 1 416 402 118 GLU N N 122.30 0.30 1 417 403 119 LYS H H 7.09 0.05 1 418 403 119 LYS CA C 52.11 0.30 1 419 403 119 LYS CB C 33.39 0.30 1 420 403 119 LYS N N 114.58 0.30 1 421 404 120 ILE H H 8.32 0.05 1 422 404 120 ILE CA C 57.83 0.30 1 423 404 120 ILE CB C 37.32 0.30 1 424 404 120 ILE N N 123.69 0.30 1 425 405 121 TYR H H 9.42 0.05 1 426 405 121 TYR CA C 54.37 0.30 1 427 405 121 TYR CB C 36.86 0.30 1 428 405 121 TYR N N 125.58 0.30 1 429 406 122 ILE H H 8.98 0.05 1 430 406 122 ILE CA C 57.61 0.30 1 431 406 122 ILE CB C 35.60 0.30 1 432 406 122 ILE N N 125.95 0.30 1 433 407 123 HIS H H 6.92 0.05 1 434 407 123 HIS CA C 54.95 0.30 1 435 407 123 HIS CB C 27.34 0.30 1 436 407 123 HIS N N 129.91 0.30 1 437 408 124 PRO CA C 61.54 0.30 1 438 408 124 PRO CB C 29.00 0.30 1 439 409 125 ARG H H 11.21 0.05 1 440 409 125 ARG CA C 51.19 0.30 1 441 409 125 ARG CB C 26.13 0.30 1 442 409 125 ARG N N 121.35 0.30 1 443 410 126 TYR H H 7.54 0.05 1 444 410 126 TYR CA C 53.97 0.30 1 445 410 126 TYR CB C 35.33 0.30 1 446 410 126 TYR N N 124.30 0.30 1 447 411 127 ASN H H 8.77 0.05 1 448 411 127 ASN CA C 47.47 0.30 1 449 411 127 ASN CB C 35.43 0.30 1 450 411 127 ASN N N 131.91 0.30 1 451 412 128 TRP H H 6.37 0.05 1 452 412 128 TRP CA C 53.08 0.30 1 453 412 128 TRP CB C 24.67 0.30 1 454 412 128 TRP N N 118.92 0.30 1 455 413 129 ARG H H 6.87 0.05 1 456 413 129 ARG CA C 55.71 0.30 1 457 413 129 ARG CB C 26.93 0.30 1 458 413 129 ARG N N 120.68 0.30 1 459 414 130 GLU H H 7.14 0.05 1 460 414 130 GLU CA C 54.18 0.30 1 461 414 130 GLU CB C 28.26 0.30 1 462 414 130 GLU N N 115.98 0.30 1 463 415 131 ASN H H 7.22 0.05 1 464 415 131 ASN CA C 49.46 0.30 1 465 415 131 ASN CB C 35.62 0.30 1 466 415 131 ASN N N 113.40 0.30 1 467 416 132 LEU H H 7.72 0.05 1 468 416 132 LEU CA C 52.70 0.30 1 469 416 132 LEU CB C 39.60 0.30 1 470 416 132 LEU N N 110.95 0.30 1 471 417 133 ASP H H 7.14 0.05 1 472 417 133 ASP CA C 52.95 0.30 1 473 417 133 ASP CB C 38.74 0.30 1 474 417 133 ASP N N 116.89 0.30 1 475 418 134 ARG H H 8.70 0.05 1 476 418 134 ARG CA C 54.63 0.30 1 477 418 134 ARG CB C 25.38 0.30 1 478 418 134 ARG N N 119.22 0.30 1 479 419 135 ASP H H 6.89 0.05 1 480 419 135 ASP CA C 50.35 0.30 1 481 419 135 ASP CB C 37.73 0.30 1 482 419 135 ASP N N 114.53 0.30 1 483 420 136 ILE H H 8.31 0.05 1 484 420 136 ILE CA C 57.84 0.30 1 485 420 136 ILE CB C 38.53 0.30 1 486 420 136 ILE N N 126.81 0.30 1 487 421 137 ALA H H 8.29 0.05 1 488 421 137 ALA CA C 47.91 0.30 1 489 421 137 ALA CB C 20.46 0.30 1 490 421 137 ALA N N 127.35 0.30 1 491 422 138 LEU H H 9.49 0.05 1 492 422 138 LEU CA C 50.25 0.30 1 493 422 138 LEU CB C 44.39 0.30 1 494 422 138 LEU N N 121.92 0.30 1 495 423 139 MET H H 9.61 0.05 1 496 423 139 MET CA C 51.27 0.30 1 497 423 139 MET CB C 32.24 0.30 1 498 423 139 MET N N 118.46 0.30 1 499 424 140 LYS H H 8.71 0.05 1 500 424 140 LYS CA C 50.97 0.30 1 501 424 140 LYS CB C 31.18 0.30 1 502 424 140 LYS N N 126.36 0.30 1 503 425 141 LEU H H 8.68 0.05 1 504 425 141 LEU CA C 51.94 0.30 1 505 425 141 LEU CB C 38.58 0.30 1 506 425 141 LEU N N 128.03 0.30 1 507 426 142 LYS H H 8.10 0.05 1 508 426 142 LYS CA C 56.37 0.30 1 509 426 142 LYS CB C 29.81 0.30 1 510 426 142 LYS N N 120.54 0.30 1 511 427 143 LYS H H 7.33 0.05 1 512 427 143 LYS CA C 49.80 0.30 1 513 427 143 LYS CB C 31.02 0.30 1 514 427 143 LYS N N 114.95 0.30 1 515 428 144 PRO CA C 59.26 0.30 1 516 428 144 PRO CB C 28.52 0.30 1 517 429 145 VAL H H 8.70 0.05 1 518 429 145 VAL CA C 56.87 0.30 1 519 429 145 VAL CB C 30.17 0.30 1 520 429 145 VAL N N 122.17 0.30 1 521 430 146 ALA H H 7.87 0.05 1 522 430 146 ALA CA C 48.03 0.30 1 523 430 146 ALA CB C 15.58 0.30 1 524 430 146 ALA N N 127.66 0.30 1 525 431 147 PHE H H 7.81 0.05 1 526 431 147 PHE CA C 51.68 0.30 1 527 431 147 PHE CB C 34.21 0.30 1 528 431 147 PHE N N 122.19 0.30 1 529 432 148 SER H H 9.75 0.05 1 530 432 148 SER CA C 54.34 0.30 1 531 432 148 SER CB C 63.74 0.30 1 532 432 148 SER N N 118.63 0.30 1 533 433 149 ASP H H 8.54 0.05 1 534 433 149 ASP CA C 53.82 0.30 1 535 433 149 ASP CB C 36.19 0.30 1 536 433 149 ASP N N 118.97 0.30 1 537 434 150 TYR H H 7.70 0.05 1 538 434 150 TYR CA C 53.40 0.30 1 539 434 150 TYR CB C 37.26 0.30 1 540 434 150 TYR N N 113.03 0.30 1 541 435 151 ILE H H 6.96 0.05 1 542 435 151 ILE CA C 58.27 0.30 1 543 435 151 ILE CB C 37.25 0.30 1 544 435 151 ILE N N 118.97 0.30 1 545 436 152 HIS H H 7.53 0.05 1 546 436 152 HIS CA C 52.32 0.30 1 547 436 152 HIS CB C 31.84 0.30 1 548 436 152 HIS N N 126.26 0.30 1 549 437 153 PRO CA C 59.73 0.30 1 550 437 153 PRO CB C 28.92 0.30 1 551 438 154 VAL H H 8.08 0.05 1 552 438 154 VAL CA C 57.10 0.30 1 553 438 154 VAL CB C 29.33 0.30 1 554 438 154 VAL N N 122.69 0.30 1 555 439 155 CYS H H 6.79 0.05 1 556 439 155 CYS CA C 50.82 0.30 1 557 439 155 CYS CB C 38.09 0.30 1 558 439 155 CYS N N 119.97 0.30 1 559 440 156 LEU H H 9.11 0.05 1 560 440 156 LEU CA C 48.92 0.30 1 561 440 156 LEU CB C 37.75 0.30 1 562 440 156 LEU N N 122.38 0.30 1 563 441 157 PRO CA C 60.47 0.30 1 564 441 157 PRO CB C 28.61 0.30 1 565 442 158 ASP H H 7.12 0.05 1 566 442 158 ASP CA C 48.75 0.30 1 567 442 158 ASP CB C 39.24 0.30 1 568 442 158 ASP N N 118.20 0.30 1 569 443 159 ARG CA C 56.82 0.30 1 570 443 159 ARG CB C 26.42 0.30 1 571 444 160 GLU H H 8.39 0.05 1 572 444 160 GLU CA C 56.60 0.30 1 573 444 160 GLU CB C 25.36 0.30 1 574 444 160 GLU N N 119.33 0.30 1 575 445 161 THR H H 7.90 0.05 1 576 445 161 THR CA C 64.05 0.30 1 577 445 161 THR CB C 64.53 0.30 1 578 445 161 THR N N 119.20 0.30 1 579 446 162 ALA H H 7.84 0.05 1 580 446 162 ALA CA C 52.37 0.30 1 581 446 162 ALA CB C 13.94 0.30 1 582 446 162 ALA N N 121.77 0.30 1 583 447 163 ALA H H 7.78 0.05 1 584 447 163 ALA CA C 51.42 0.30 1 585 447 163 ALA CB C 14.76 0.30 1 586 447 163 ALA N N 118.49 0.30 1 587 448 164 SER H H 7.54 0.05 1 588 448 164 SER CA C 58.20 0.30 1 589 448 164 SER CB C 60.55 0.30 1 590 448 164 SER N N 110.76 0.30 1 591 449 165 LEU H H 7.55 0.05 1 592 449 165 LEU CA C 52.58 0.30 1 593 449 165 LEU CB C 38.83 0.30 1 594 449 165 LEU N N 116.44 0.30 1 595 450 166 LEU H H 7.23 0.05 1 596 450 166 LEU CA C 50.36 0.30 1 597 450 166 LEU CB C 38.72 0.30 1 598 450 166 LEU N N 118.99 0.30 1 599 451 167 GLN H H 7.29 0.05 1 600 451 167 GLN CA C 50.20 0.30 1 601 451 167 GLN CB C 27.23 0.30 1 602 451 167 GLN N N 123.00 0.30 1 603 452 168 ALA H H 8.18 0.05 1 604 452 168 ALA CA C 50.36 0.30 1 605 452 168 ALA CB C 14.58 0.30 1 606 452 168 ALA N N 123.36 0.30 1 607 453 169 GLY H H 8.96 0.05 1 608 453 169 GLY CA C 42.22 0.30 1 609 453 169 GLY N N 111.31 0.30 1 610 454 170 TYR H H 8.07 0.05 1 611 454 170 TYR CA C 53.30 0.30 1 612 454 170 TYR CB C 33.30 0.30 1 613 454 170 TYR N N 123.87 0.30 1 614 455 171 LYS H H 8.95 0.05 1 615 455 171 LYS CA C 53.08 0.30 1 616 455 171 LYS CB C 33.05 0.30 1 617 455 171 LYS N N 119.77 0.30 1 618 456 172 GLY H H 8.44 0.05 1 619 456 172 GLY CA C 40.95 0.30 1 620 456 172 GLY N N 107.61 0.30 1 621 457 173 ARG H H 8.59 0.05 1 622 457 173 ARG CA C 51.30 0.30 1 623 457 173 ARG CB C 31.62 0.30 1 624 457 173 ARG N N 120.19 0.30 1 625 458 174 VAL H H 9.29 0.05 1 626 458 174 VAL CA C 58.01 0.30 1 627 458 174 VAL CB C 31.47 0.30 1 628 458 174 VAL N N 128.35 0.30 1 629 459 175 THR H H 6.73 0.05 1 630 459 175 THR CA C 53.93 0.30 1 631 459 175 THR CB C 68.73 0.30 1 632 459 175 THR N N 111.84 0.30 1 633 460 176 GLY H H 7.95 0.05 1 634 460 176 GLY CA C 43.83 0.30 1 635 460 176 GLY N N 105.81 0.30 1 636 461 177 TRP H H 9.56 0.05 1 637 461 177 TRP CA C 55.70 0.30 1 638 461 177 TRP CB C 26.21 0.30 1 639 461 177 TRP N N 122.73 0.30 1 640 462 178 GLY H H 8.72 0.05 1 641 462 178 GLY CA C 40.76 0.30 1 642 462 178 GLY N N 107.80 0.30 1 643 463 179 ASN H H 8.20 0.05 1 644 463 179 ASN CA C 51.28 0.30 1 645 463 179 ASN CB C 35.80 0.30 1 646 463 179 ASN N N 116.01 0.30 1 647 464 180 LEU H H 8.26 0.05 1 648 464 180 LEU CA C 52.09 0.30 1 649 464 180 LEU CB C 40.42 0.30 1 650 464 180 LEU N N 120.08 0.30 1 651 465 181 LYS H H 7.50 0.05 1 652 465 181 LYS CA C 51.10 0.30 1 653 465 181 LYS CB C 34.09 0.30 1 654 465 181 LYS N N 113.71 0.30 1 655 466 182 GLU H H 9.07 0.05 1 656 466 182 GLU CA C 56.43 0.30 1 657 466 182 GLU CB C 27.03 0.30 1 658 466 182 GLU N N 121.47 0.30 1 659 467 183 THR H H 7.80 0.05 1 660 467 183 THR CA C 58.09 0.30 1 661 467 183 THR N N 111.65 0.30 1 662 478 194 SER CA C 57.07 0.30 1 663 478 194 SER CB C 60.18 0.30 1 664 479 195 VAL H H 7.55 0.05 1 665 479 195 VAL CA C 55.26 0.30 1 666 479 195 VAL CB C 32.55 0.30 1 667 479 195 VAL N N 113.02 0.30 1 668 480 196 LEU H H 7.09 0.05 1 669 480 196 LEU CA C 53.37 0.30 1 670 480 196 LEU CB C 38.64 0.30 1 671 480 196 LEU N N 122.28 0.30 1 672 481 197 GLN H H 7.15 0.05 1 673 481 197 GLN CA C 49.77 0.30 1 674 481 197 GLN CB C 30.55 0.30 1 675 481 197 GLN N N 122.75 0.30 1 676 482 198 VAL H H 8.97 0.05 1 677 482 198 VAL CA C 56.01 0.30 1 678 482 198 VAL CB C 32.63 0.30 1 679 482 198 VAL N N 118.82 0.30 1 680 483 199 VAL H H 8.72 0.05 1 681 483 199 VAL CA C 57.86 0.30 1 682 483 199 VAL CB C 32.30 0.30 1 683 483 199 VAL N N 126.15 0.30 1 684 484 200 ASN H H 8.59 0.05 1 685 484 200 ASN CA C 48.38 0.30 1 686 484 200 ASN CB C 36.47 0.30 1 687 484 200 ASN N N 126.45 0.30 1 688 485 201 LEU H H 8.95 0.05 1 689 485 201 LEU CA C 48.57 0.30 1 690 485 201 LEU CB C 43.99 0.30 1 691 485 201 LEU N N 121.39 0.30 1 692 486 202 PRO CA C 58.28 0.30 1 693 486 202 PRO CB C 28.10 0.30 1 694 487 203 ILE H H 8.60 0.05 1 695 487 203 ILE CA C 59.80 0.30 1 696 487 203 ILE CB C 33.97 0.30 1 697 487 203 ILE N N 122.37 0.30 1 698 488 204 VAL H H 7.88 0.05 1 699 488 204 VAL CA C 59.12 0.30 1 700 488 204 VAL CB C 30.14 0.30 1 701 488 204 VAL N N 133.56 0.30 1 702 489 205 GLU H H 9.56 0.05 1 703 489 205 GLU CA C 54.27 0.30 1 704 489 205 GLU CB C 26.38 0.30 1 705 489 205 GLU N N 126.33 0.30 1 706 490 206 ARG H H 8.83 0.05 1 707 490 206 ARG CA C 59.12 0.30 1 708 490 206 ARG N N 124.40 0.30 1 709 491 207 PRO CA C 63.24 0.30 1 710 491 207 PRO CB C 27.78 0.30 1 711 492 208 VAL H H 6.73 0.05 1 712 492 208 VAL CA C 62.43 0.30 1 713 492 208 VAL CB C 27.35 0.30 1 714 492 208 VAL N N 117.57 0.30 1 715 493 209 CYS H H 7.67 0.05 1 716 493 209 CYS CA C 54.10 0.30 1 717 493 209 CYS CB C 35.04 0.30 1 718 493 209 CYS N N 118.47 0.30 1 719 494 210 LYS H H 8.68 0.05 1 720 494 210 LYS CA C 56.89 0.30 1 721 494 210 LYS CB C 29.13 0.30 1 722 494 210 LYS N N 121.59 0.30 1 723 495 211 ASP H H 7.74 0.05 1 724 495 211 ASP CA C 53.00 0.30 1 725 495 211 ASP CB C 37.59 0.30 1 726 495 211 ASP N N 116.25 0.30 1 727 496 212 SER H H 7.80 0.05 1 728 496 212 SER CA C 57.35 0.30 1 729 496 212 SER CB C 61.91 0.30 1 730 496 212 SER N N 114.01 0.30 1 731 497 213 THR H H 7.54 0.05 1 732 497 213 THR CA C 57.05 0.30 1 733 497 213 THR CB C 66.50 0.30 1 734 497 213 THR N N 118.27 0.30 1 735 498 214 ARG H H 8.73 0.05 1 736 498 214 ARG CA C 52.62 0.30 1 737 498 214 ARG CB C 26.72 0.30 1 738 498 214 ARG N N 124.14 0.30 1 739 499 215 ILE H H 8.14 0.05 1 740 499 215 ILE CA C 58.81 0.30 1 741 499 215 ILE CB C 32.86 0.30 1 742 499 215 ILE N N 126.96 0.30 1 743 500 216 ARG H H 8.13 0.05 1 744 500 216 ARG CA C 53.53 0.30 1 745 500 216 ARG CB C 26.63 0.30 1 746 500 216 ARG N N 127.58 0.30 1 747 501 217 ILE H H 7.70 0.05 1 748 501 217 ILE CA C 57.16 0.30 1 749 501 217 ILE CB C 35.88 0.30 1 750 501 217 ILE N N 123.67 0.30 1 751 502 218 THR H H 7.23 0.05 1 752 502 218 THR CA C 56.13 0.30 1 753 502 218 THR CB C 69.12 0.30 1 754 502 218 THR N N 110.86 0.30 1 755 503 219 ASP CA C 52.82 0.30 1 756 503 219 ASP CB C 36.97 0.30 1 757 504 220 ASN H H 8.08 0.05 1 758 504 220 ASN CA C 51.15 0.30 1 759 504 220 ASN CB C 34.80 0.30 1 760 504 220 ASN N N 112.55 0.30 1 761 505 221 MET H H 8.23 0.05 1 762 505 221 MET CA C 51.77 0.30 1 763 505 221 MET CB C 33.58 0.30 1 764 505 221 MET N N 124.17 0.30 1 765 506 222 PHE H H 8.90 0.05 1 766 506 222 PHE CA C 53.91 0.30 1 767 506 222 PHE CB C 37.72 0.30 1 768 506 222 PHE N N 117.13 0.30 1 769 507 223 CYS H H 8.74 0.05 1 770 507 223 CYS CA C 52.36 0.30 1 771 507 223 CYS CB C 38.52 0.30 1 772 507 223 CYS N N 121.08 0.30 1 773 508 224 ALA H H 8.52 0.05 1 774 508 224 ALA CA C 48.52 0.30 1 775 508 224 ALA CB C 20.41 0.30 1 776 508 224 ALA N N 120.93 0.30 1 777 509 225 GLY H H 8.73 0.05 1 778 509 225 GLY CA C 41.46 0.30 1 779 509 225 GLY N N 110.03 0.30 1 780 510 226 TYR H H 9.52 0.05 1 781 510 226 TYR CA C 56.80 0.30 1 782 510 226 TYR CB C 35.83 0.30 1 783 510 226 TYR N N 118.87 0.30 1 784 511 227 LYS H H 10.01 0.05 1 785 511 227 LYS CA C 52.21 0.30 1 786 511 227 LYS CB C 28.33 0.30 1 787 511 227 LYS N N 124.64 0.30 1 788 512 228 PRO CA C 62.59 0.30 1 789 512 228 PRO CB C 28.48 0.30 1 790 513 229 ASP H H 8.40 0.05 1 791 513 229 ASP CA C 51.50 0.30 1 792 513 229 ASP CB C 36.75 0.30 1 793 513 229 ASP N N 113.67 0.30 1 794 514 230 GLU H H 7.73 0.05 1 795 514 230 GLU CA C 55.05 0.30 1 796 514 230 GLU CB C 27.97 0.30 1 797 514 230 GLU N N 118.06 0.30 1 798 515 231 GLY H H 8.03 0.05 1 799 515 231 GLY CA C 43.67 0.30 1 800 515 231 GLY N N 107.58 0.30 1 801 516 232 LYS H H 6.68 0.05 1 802 516 232 LYS CA C 51.97 0.30 1 803 516 232 LYS CB C 30.79 0.30 1 804 516 232 LYS N N 119.42 0.30 1 805 517 233 ARG H H 7.95 0.05 1 806 517 233 ARG CA C 51.68 0.30 1 807 517 233 ARG CB C 29.10 0.30 1 808 517 233 ARG N N 118.28 0.30 1 809 518 234 GLY H H 8.60 0.05 1 810 518 234 GLY CA C 41.62 0.30 1 811 518 234 GLY N N 107.21 0.30 1 812 519 235 ASP H H 8.25 0.05 1 813 519 235 ASP CA C 50.11 0.30 1 814 519 235 ASP CB C 41.01 0.30 1 815 519 235 ASP N N 117.86 0.30 1 816 520 236 ALA H H 8.80 0.05 1 817 520 236 ALA CA C 49.13 0.30 1 818 520 236 ALA CB C 17.75 0.30 1 819 520 236 ALA N N 124.49 0.30 1 820 521 237 CYS H H 9.55 0.05 1 821 521 237 CYS CA C 51.35 0.30 1 822 521 237 CYS CB C 33.91 0.30 1 823 521 237 CYS N N 115.23 0.30 1 824 522 238 GLU H H 8.14 0.05 1 825 522 238 GLU CA C 57.85 0.30 1 826 522 238 GLU CB C 25.30 0.30 1 827 522 238 GLU N N 123.07 0.30 1 828 525 241 SER CA C 55.74 0.30 1 829 525 241 SER CB C 59.49 0.30 1 830 526 242 GLY H H 8.98 0.05 1 831 526 242 GLY CA C 43.14 0.30 1 832 526 242 GLY N N 110.67 0.30 1 833 527 243 GLY H H 8.07 0.05 1 834 527 243 GLY CA C 41.14 0.30 1 835 527 243 GLY N N 105.11 0.30 1 836 528 244 PRO CA C 60.12 0.30 1 837 528 244 PRO CB C 27.84 0.30 1 838 529 245 PHE H H 7.93 0.05 1 839 529 245 PHE CA C 53.19 0.30 1 840 529 245 PHE CB C 36.95 0.30 1 841 529 245 PHE N N 123.88 0.30 1 842 530 246 VAL H H 9.58 0.05 1 843 530 246 VAL CA C 55.89 0.30 1 844 530 246 VAL CB C 31.84 0.30 1 845 530 246 VAL N N 122.83 0.30 1 846 531 247 MET H H 9.18 0.05 1 847 531 247 MET CA C 52.36 0.30 1 848 531 247 MET CB C 35.86 0.30 1 849 531 247 MET N N 118.55 0.30 1 850 532 248 LYS H H 6.77 0.05 1 851 532 248 LYS CA C 51.35 0.30 1 852 532 248 LYS CB C 28.35 0.30 1 853 532 248 LYS N N 123.29 0.30 1 854 533 249 SER H H 8.85 0.05 1 855 533 249 SER CA C 51.67 0.30 1 856 533 249 SER CB C 61.66 0.30 1 857 533 249 SER N N 120.70 0.30 1 858 534 250 PRO CA C 59.89 0.30 1 859 534 250 PRO CB C 28.08 0.30 1 860 535 251 PHE H H 7.61 0.05 1 861 535 251 PHE CA C 55.44 0.30 1 862 535 251 PHE CB C 35.44 0.30 1 863 535 251 PHE N N 118.52 0.30 1 864 536 252 ASN H H 7.17 0.05 1 865 536 252 ASN CA C 48.95 0.30 1 866 536 252 ASN CB C 35.77 0.30 1 867 536 252 ASN N N 113.30 0.30 1 868 537 253 ASN H H 7.77 0.05 1 869 537 253 ASN CA C 52.16 0.30 1 870 537 253 ASN CB C 35.40 0.30 1 871 537 253 ASN N N 114.20 0.30 1 872 538 254 ARG H H 7.39 0.05 1 873 538 254 ARG CA C 52.14 0.30 1 874 538 254 ARG CB C 29.29 0.30 1 875 538 254 ARG N N 112.84 0.30 1 876 539 255 TRP H H 8.69 0.05 1 877 539 255 TRP CA C 54.02 0.30 1 878 539 255 TRP CB C 27.70 0.30 1 879 539 255 TRP N N 120.62 0.30 1 880 540 256 TYR H H 8.97 0.05 1 881 540 256 TYR CA C 53.42 0.30 1 882 540 256 TYR CB C 40.06 0.30 1 883 540 256 TYR N N 118.44 0.30 1 884 541 257 GLN H H 8.93 0.05 1 885 541 257 GLN CA C 52.88 0.30 1 886 541 257 GLN CB C 23.47 0.30 1 887 541 257 GLN N N 121.67 0.30 1 888 542 258 MET H H 8.42 0.05 1 889 542 258 MET CA C 50.74 0.30 1 890 542 258 MET CB C 28.94 0.30 1 891 542 258 MET N N 121.71 0.30 1 892 543 259 GLY H H 8.88 0.05 1 893 543 259 GLY CA C 42.30 0.30 1 894 543 259 GLY N N 104.77 0.30 1 895 544 260 ILE H H 7.88 0.05 1 896 544 260 ILE CA C 57.54 0.30 1 897 544 260 ILE CB C 38.66 0.30 1 898 544 260 ILE N N 122.29 0.30 1 899 545 261 VAL H H 9.31 0.05 1 900 545 261 VAL CA C 62.77 0.30 1 901 545 261 VAL CB C 28.51 0.30 1 902 545 261 VAL N N 127.29 0.30 1 903 546 262 SER H H 7.57 0.05 1 904 546 262 SER CA C 56.95 0.30 1 905 546 262 SER CB C 60.70 0.30 1 906 546 262 SER N N 122.73 0.30 1 907 547 263 TRP H H 7.91 0.05 1 908 547 263 TRP CA C 53.59 0.30 1 909 547 263 TRP CB C 29.51 0.30 1 910 547 263 TRP N N 114.33 0.30 1 911 548 264 GLY H H 8.88 0.05 1 912 548 264 GLY CA C 42.36 0.30 1 913 548 264 GLY N N 107.18 0.30 1 914 549 265 GLU H H 9.52 0.05 1 915 549 265 GLU CA C 53.50 0.30 1 916 549 265 GLU CB C 27.94 0.30 1 917 549 265 GLU N N 125.27 0.30 1 918 550 266 GLY H H 8.52 0.05 1 919 550 266 GLY CA C 41.23 0.30 1 920 550 266 GLY N N 113.58 0.30 1 921 551 267 CYS H H 9.06 0.05 1 922 551 267 CYS CA C 52.59 0.30 1 923 551 267 CYS CB C 42.48 0.30 1 924 551 267 CYS N N 117.76 0.30 1 925 552 268 ASP H H 10.70 0.05 1 926 552 268 ASP CA C 52.62 0.30 1 927 552 268 ASP CB C 39.92 0.30 1 928 552 268 ASP N N 126.90 0.30 1 929 553 269 ARG H H 8.32 0.05 1 930 553 269 ARG CA C 53.06 0.30 1 931 553 269 ARG CB C 27.43 0.30 1 932 553 269 ARG N N 117.36 0.30 1 933 554 270 ASP H H 8.92 0.05 1 934 554 270 ASP CA C 52.72 0.30 1 935 554 270 ASP CB C 36.81 0.30 1 936 554 270 ASP N N 124.89 0.30 1 937 555 271 GLY H H 9.07 0.05 1 938 555 271 GLY CA C 42.42 0.30 1 939 555 271 GLY N N 112.26 0.30 1 940 556 272 LYS H H 7.01 0.05 1 941 556 272 LYS CA C 52.43 0.30 1 942 556 272 LYS CB C 30.42 0.30 1 943 556 272 LYS N N 116.98 0.30 1 944 557 273 TYR H H 8.99 0.05 1 945 557 273 TYR CA C 54.51 0.30 1 946 557 273 TYR CB C 40.24 0.30 1 947 557 273 TYR N N 118.77 0.30 1 948 558 274 GLY H H 7.62 0.05 1 949 558 274 GLY CA C 42.98 0.30 1 950 558 274 GLY N N 108.84 0.30 1 951 559 275 PHE H H 8.60 0.05 1 952 559 275 PHE CA C 54.93 0.30 1 953 559 275 PHE CB C 36.86 0.30 1 954 559 275 PHE N N 118.71 0.30 1 955 560 276 TYR H H 8.79 0.05 1 956 560 276 TYR CA C 53.20 0.30 1 957 560 276 TYR CB C 37.66 0.30 1 958 560 276 TYR N N 122.65 0.30 1 959 561 277 THR H H 9.18 0.05 1 960 561 277 THR CA C 60.72 0.30 1 961 561 277 THR CB C 65.80 0.30 1 962 561 277 THR N N 120.63 0.30 1 963 562 278 HIS H H 8.50 0.05 1 964 562 278 HIS CA C 53.22 0.30 1 965 562 278 HIS CB C 28.74 0.30 1 966 562 278 HIS N N 130.62 0.30 1 967 563 279 VAL H H 7.76 0.05 1 968 563 279 VAL CA C 65.13 0.30 1 969 563 279 VAL CB C 28.34 0.30 1 970 563 279 VAL N N 126.20 0.30 1 971 564 280 PHE H H 9.85 0.05 1 972 564 280 PHE CA C 59.76 0.30 1 973 564 280 PHE CB C 35.96 0.30 1 974 564 280 PHE N N 118.98 0.30 1 975 565 281 ARG H H 8.31 0.05 1 976 565 281 ARG CA C 55.66 0.30 1 977 565 281 ARG CB C 25.45 0.30 1 978 565 281 ARG N N 119.34 0.30 1 979 566 282 LEU H H 7.31 0.05 1 980 566 282 LEU CA C 50.73 0.30 1 981 566 282 LEU CB C 38.43 0.30 1 982 566 282 LEU N N 119.80 0.30 1 983 567 283 LYS H H 7.62 0.05 1 984 567 283 LYS CA C 56.84 0.30 1 985 567 283 LYS CB C 29.46 0.30 1 986 567 283 LYS N N 123.60 0.30 1 987 568 284 LYS CA C 60.08 0.30 1 988 568 284 LYS CB C 27.91 0.30 1 989 569 285 TRP H H 7.58 0.05 1 990 569 285 TRP CA C 59.27 0.30 1 991 569 285 TRP CB C 24.14 0.30 1 992 569 285 TRP N N 121.04 0.30 1 993 570 286 ILE H H 7.56 0.05 1 994 570 286 ILE CA C 61.63 0.30 1 995 570 286 ILE CB C 35.05 0.30 1 996 570 286 ILE N N 117.59 0.30 1 997 571 287 GLN H H 8.25 0.05 1 998 571 287 GLN CA C 55.02 0.30 1 999 571 287 GLN CB C 25.56 0.30 1 1000 571 287 GLN N N 114.50 0.30 1 1001 572 288 LYS H H 7.36 0.05 1 1002 572 288 LYS CA C 55.91 0.30 1 1003 572 288 LYS CB C 28.32 0.30 1 1004 572 288 LYS N N 119.46 0.30 1 1005 573 289 VAL H H 7.24 0.05 1 1006 573 289 VAL CA C 63.17 0.30 1 1007 573 289 VAL CB C 27.11 0.30 1 1008 573 289 VAL N N 120.39 0.30 1 1009 574 290 ILE H H 7.17 0.05 1 1010 574 290 ILE CA C 61.85 0.30 1 1011 574 290 ILE CB C 33.80 0.30 1 1012 574 290 ILE N N 117.53 0.30 1 1013 575 291 ASP H H 8.07 0.05 1 1014 575 291 ASP CA C 53.41 0.30 1 1015 575 291 ASP CB C 37.49 0.30 1 1016 575 291 ASP N N 119.64 0.30 1 1017 576 292 GLN H H 7.66 0.05 1 1018 576 292 GLN CA C 54.55 0.30 1 1019 576 292 GLN CB C 25.49 0.30 1 1020 576 292 GLN N N 117.97 0.30 1 1021 577 293 PHE H H 8.05 0.05 1 1022 577 293 PHE CA C 55.03 0.30 1 1023 577 293 PHE CB C 35.85 0.30 1 1024 577 293 PHE N N 117.78 0.30 1 1025 578 294 GLY H H 7.99 0.05 1 1026 578 294 GLY CA C 43.18 0.30 1 1027 578 294 GLY N N 110.38 0.30 1 1028 579 295 GLU H H 7.84 0.05 1 1029 579 295 GLU CA C 54.40 0.30 1 1030 579 295 GLU CB C 27.81 0.30 1 1031 579 295 GLU N N 125.93 0.30 1 stop_ save_