HEADER BLOOD CLOTTING 19-JUN-02 1M1J
TITLE CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN WITH TWO DIFFERENT
TITLE 2 BOUND LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRINOGEN ALPHA SUBUNIT;
COMPND 3 CHAIN: A, D;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: FIBRINOGEN BETA CHAIN;
COMPND 6 CHAIN: B, E;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: FIBRINOGEN GAMMA CHAIN;
COMPND 9 CHAIN: C, F;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: GLY-PRO-ARG-PRO PEPTIDE;
COMPND 12 CHAIN: G, H;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 5;
COMPND 15 MOLECULE: GLY-HIS-ARG-PRO PEPTIDE;
COMPND 16 CHAIN: I, J;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 8 ORGANISM_COMMON: CHICKEN;
SOURCE 9 ORGANISM_TAXID: 9031;
SOURCE 10 TISSUE: BLOOD;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 13 ORGANISM_COMMON: CHICKEN;
SOURCE 14 ORGANISM_TAXID: 9031;
SOURCE 15 TISSUE: BLOOD;
SOURCE 16 MOL_ID: 4;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 OTHER_DETAILS: THE PEPTIDE IS CHEMICALLY SYNTHESIZED.;
SOURCE 19 MOL_ID: 5;
SOURCE 20 SYNTHETIC: YES;
SOURCE 21 OTHER_DETAILS: THE PEPTIDE IS CHEMICALLY SYNTHESIZED.
KEYWDS COILED COILS, DISULFIDE RINGS, FIBRINOGEN, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.YANG,J.M.KOLLMAN,L.PANDI,R.F.DOOLITTLE
REVDAT 4 29-JUL-20 1M1J 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 1M1J 1 VERSN
REVDAT 2 24-FEB-09 1M1J 1 VERSN
REVDAT 1 26-JUN-02 1M1J 0
SPRSDE 26-JUN-02 1M1J 1JFE
JRNL AUTH Z.YANG,J.M.KOLLMAN,L.PANDI,R.F.DOOLITTLE
JRNL TITL CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN AT 2.7 A
JRNL TITL 2 RESOLUTION
JRNL REF BIOCHEMISTRY V. 40 12515 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11601975
JRNL DOI 10.1021/BI011394P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.YANG,I.MOCHALKIN,L.VEERAPANDIAN,M.RILEY,R.F.DOOLITTLE
REMARK 1 TITL CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN AT 5.5-A
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 97 3907 2000
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.080065697
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.SPRAGGON,S.J.EVERSE,R.F.DOOLITTLE
REMARK 1 TITL CRYSTAL STURCTURES OF FRAGMENT D FROM HUMAN FIBRINOGEN AND
REMARK 1 TITL 2 ITS CROSSLINKED COUNTERPART FROM FIBRIN
REMARK 1 REF NATURE V. 389 455 1997
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/38947
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.J.EVERSE,G.SPRAGGON,L.VEERAPANDIAN,M.RILEY,R.F.DOOLITTLE
REMARK 1 TITL CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN
REMARK 1 TITL 2 WITH TWO DIFFERENT BOUND LIGANDS
REMARK 1 REF BIOCHEMISTRY V. 37 8637 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9804129
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 110727
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5863
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15993
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121776
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: FRAGMENT D FROM STRUCTURE 1FZC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 50.01000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 ASP A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 THR A 5
REMARK 465 THR A 6
REMARK 465 PHE A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 GLU A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 ARG A 15
REMARK 465 GLY A 16
REMARK 465 PRO A 17
REMARK 465 ARG A 18
REMARK 465 ILE A 19
REMARK 465 LEU A 20
REMARK 465 GLU A 21
REMARK 465 ASN A 22
REMARK 465 MET A 23
REMARK 465 HIS A 24
REMARK 465 GLU A 25
REMARK 465 SER A 26
REMARK 465 HIS A 219
REMARK 465 PHE A 220
REMARK 465 LYS A 221
REMARK 465 LEU A 222
REMARK 465 LYS A 223
REMARK 465 PRO A 224
REMARK 465 SER A 225
REMARK 465 PRO A 226
REMARK 465 GLU A 227
REMARK 465 MET A 228
REMARK 465 GLN A 229
REMARK 465 ALA A 230
REMARK 465 MET A 231
REMARK 465 SER A 232
REMARK 465 ALA A 233
REMARK 465 PHE A 234
REMARK 465 ASN A 235
REMARK 465 ASN A 236
REMARK 465 ILE A 237
REMARK 465 LYS A 238
REMARK 465 GLN A 239
REMARK 465 MET A 240
REMARK 465 GLN A 241
REMARK 465 VAL A 242
REMARK 465 VAL A 243
REMARK 465 LEU A 244
REMARK 465 GLU A 245
REMARK 465 ARG A 246
REMARK 465 PRO A 247
REMARK 465 GLU A 248
REMARK 465 THR A 249
REMARK 465 ASP A 250
REMARK 465 HIS A 251
REMARK 465 VAL A 252
REMARK 465 ALA A 253
REMARK 465 GLU A 254
REMARK 465 ALA A 255
REMARK 465 ARG A 256
REMARK 465 GLY A 257
REMARK 465 ASP A 258
REMARK 465 SER A 259
REMARK 465 SER A 260
REMARK 465 PRO A 261
REMARK 465 SER A 262
REMARK 465 HIS A 263
REMARK 465 THR A 264
REMARK 465 GLY A 265
REMARK 465 LYS A 266
REMARK 465 LEU A 267
REMARK 465 ILE A 268
REMARK 465 THR A 269
REMARK 465 SER A 270
REMARK 465 SER A 271
REMARK 465 HIS A 272
REMARK 465 ARG A 273
REMARK 465 ARG A 274
REMARK 465 GLU A 275
REMARK 465 SER A 276
REMARK 465 PRO A 277
REMARK 465 SER A 278
REMARK 465 LEU A 279
REMARK 465 VAL A 280
REMARK 465 ASP A 281
REMARK 465 LYS A 282
REMARK 465 THR A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 ALA A 286
REMARK 465 SER A 287
REMARK 465 SER A 288
REMARK 465 VAL A 289
REMARK 465 HIS A 290
REMARK 465 ARG A 291
REMARK 465 CYS A 292
REMARK 465 THR A 293
REMARK 465 ARG A 294
REMARK 465 THR A 295
REMARK 465 VAL A 296
REMARK 465 THR A 297
REMARK 465 LYS A 298
REMARK 465 LYS A 299
REMARK 465 VAL A 300
REMARK 465 ILE A 301
REMARK 465 SER A 302
REMARK 465 GLY A 303
REMARK 465 PRO A 304
REMARK 465 ASP A 305
REMARK 465 GLY A 306
REMARK 465 PRO A 307
REMARK 465 ARG A 308
REMARK 465 GLU A 309
REMARK 465 GLU A 310
REMARK 465 ILE A 311
REMARK 465 VAL A 312
REMARK 465 GLU A 313
REMARK 465 LYS A 314
REMARK 465 MET A 315
REMARK 465 VAL A 316
REMARK 465 SER A 317
REMARK 465 SER A 318
REMARK 465 ASP A 319
REMARK 465 GLY A 320
REMARK 465 SER A 321
REMARK 465 ASP A 322
REMARK 465 CYS A 323
REMARK 465 SER A 324
REMARK 465 HIS A 325
REMARK 465 LEU A 326
REMARK 465 GLN A 327
REMARK 465 GLY A 328
REMARK 465 GLY A 329
REMARK 465 ARG A 330
REMARK 465 GLU A 331
REMARK 465 GLY A 332
REMARK 465 SER A 333
REMARK 465 THR A 334
REMARK 465 TYR A 335
REMARK 465 HIS A 336
REMARK 465 PHE A 337
REMARK 465 SER A 338
REMARK 465 GLY A 339
REMARK 465 THR A 340
REMARK 465 GLY A 341
REMARK 465 ASP A 342
REMARK 465 PHE A 343
REMARK 465 HIS A 344
REMARK 465 LYS A 345
REMARK 465 LEU A 346
REMARK 465 ASP A 347
REMARK 465 ARG A 348
REMARK 465 LEU A 349
REMARK 465 LEU A 350
REMARK 465 PRO A 351
REMARK 465 ASP A 352
REMARK 465 LEU A 353
REMARK 465 GLU A 354
REMARK 465 SER A 355
REMARK 465 PHE A 356
REMARK 465 PHE A 357
REMARK 465 THR A 358
REMARK 465 HIS A 359
REMARK 465 ASP A 360
REMARK 465 SER A 361
REMARK 465 VAL A 362
REMARK 465 SER A 363
REMARK 465 THR A 364
REMARK 465 SER A 365
REMARK 465 SER A 366
REMARK 465 ARG A 367
REMARK 465 HIS A 368
REMARK 465 SER A 369
REMARK 465 ILE A 370
REMARK 465 GLY A 371
REMARK 465 SER A 372
REMARK 465 SER A 373
REMARK 465 THR A 374
REMARK 465 SER A 375
REMARK 465 SER A 376
REMARK 465 HIS A 377
REMARK 465 VAL A 378
REMARK 465 THR A 379
REMARK 465 GLY A 380
REMARK 465 ALA A 381
REMARK 465 GLY A 382
REMARK 465 SER A 383
REMARK 465 SER A 384
REMARK 465 HIS A 385
REMARK 465 LEU A 386
REMARK 465 GLY A 387
REMARK 465 THR A 388
REMARK 465 GLY A 389
REMARK 465 GLY A 390
REMARK 465 LYS A 391
REMARK 465 ASP A 392
REMARK 465 LYS A 393
REMARK 465 PHE A 394
REMARK 465 THR A 395
REMARK 465 ASP A 396
REMARK 465 LEU A 397
REMARK 465 GLY A 398
REMARK 465 GLU A 399
REMARK 465 GLU A 400
REMARK 465 GLU A 401
REMARK 465 GLU A 402
REMARK 465 ASP A 403
REMARK 465 ASP A 404
REMARK 465 PHE A 405
REMARK 465 GLY A 406
REMARK 465 GLY A 407
REMARK 465 LEU A 408
REMARK 465 GLN A 409
REMARK 465 PRO A 410
REMARK 465 SER A 411
REMARK 465 GLY A 412
REMARK 465 PHE A 413
REMARK 465 ALA A 414
REMARK 465 ALA A 415
REMARK 465 GLY A 416
REMARK 465 SER A 417
REMARK 465 ALA A 418
REMARK 465 SER A 419
REMARK 465 HIS A 420
REMARK 465 SER A 421
REMARK 465 LYS A 422
REMARK 465 THR A 423
REMARK 465 VAL A 424
REMARK 465 LEU A 425
REMARK 465 THR A 426
REMARK 465 SER A 427
REMARK 465 SER A 428
REMARK 465 SER A 429
REMARK 465 SER A 430
REMARK 465 SER A 431
REMARK 465 PHE A 432
REMARK 465 ASN A 433
REMARK 465 LYS A 434
REMARK 465 GLY A 435
REMARK 465 GLY A 436
REMARK 465 SER A 437
REMARK 465 THR A 438
REMARK 465 PHE A 439
REMARK 465 GLU A 440
REMARK 465 THR A 441
REMARK 465 LYS A 442
REMARK 465 SER A 443
REMARK 465 LEU A 444
REMARK 465 LYS A 445
REMARK 465 THR A 446
REMARK 465 ARG A 447
REMARK 465 GLU A 448
REMARK 465 THR A 449
REMARK 465 SER A 450
REMARK 465 GLU A 451
REMARK 465 GLN A 452
REMARK 465 LEU A 453
REMARK 465 GLY A 454
REMARK 465 GLY A 455
REMARK 465 VAL A 456
REMARK 465 GLN A 457
REMARK 465 HIS A 458
REMARK 465 ASP A 459
REMARK 465 GLN A 460
REMARK 465 SER A 461
REMARK 465 ALA A 462
REMARK 465 GLU A 463
REMARK 465 ASP A 464
REMARK 465 THR A 465
REMARK 465 PRO A 466
REMARK 465 ASP A 467
REMARK 465 PHE A 468
REMARK 465 LYS A 469
REMARK 465 ALA A 470
REMARK 465 ARG A 471
REMARK 465 SER A 472
REMARK 465 PHE A 473
REMARK 465 ARG A 474
REMARK 465 PRO A 475
REMARK 465 ALA A 476
REMARK 465 ALA A 477
REMARK 465 MET A 478
REMARK 465 SER A 479
REMARK 465 THR A 480
REMARK 465 ARG A 481
REMARK 465 ARG A 482
REMARK 465 SER A 483
REMARK 465 TYR A 484
REMARK 465 ASN A 485
REMARK 465 GLY A 486
REMARK 465 LYS A 487
REMARK 465 GLY A 488
REMARK 465 THR A 489
REMARK 465 GLN A 490
REMARK 465 LYS A 491
REMARK 465 GLN B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 GLU B 5
REMARK 465 TYR B 6
REMARK 465 ASP B 7
REMARK 465 ASN B 8
REMARK 465 GLU B 9
REMARK 465 GLU B 10
REMARK 465 ASP B 11
REMARK 465 SER B 12
REMARK 465 PRO B 13
REMARK 465 GLN B 14
REMARK 465 ILE B 15
REMARK 465 ASP B 16
REMARK 465 ALA B 17
REMARK 465 ARG B 18
REMARK 465 ALA B 19
REMARK 465 HIS B 20
REMARK 465 ARG B 21
REMARK 465 PRO B 22
REMARK 465 LEU B 23
REMARK 465 ASP B 24
REMARK 465 LYS B 25
REMARK 465 ARG B 26
REMARK 465 GLN B 27
REMARK 465 GLU B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 PRO B 31
REMARK 465 THR B 32
REMARK 465 LEU B 33
REMARK 465 ARG B 34
REMARK 465 PRO B 35
REMARK 465 VAL B 36
REMARK 465 ALA B 37
REMARK 465 PRO B 38
REMARK 465 PRO B 39
REMARK 465 ILE B 40
REMARK 465 SER B 41
REMARK 465 GLY B 42
REMARK 465 THR B 43
REMARK 465 GLY B 44
REMARK 465 TYR B 45
REMARK 465 GLN B 46
REMARK 465 PRO B 47
REMARK 465 ARG B 48
REMARK 465 PRO B 49
REMARK 465 PRO B 50
REMARK 465 LYS B 51
REMARK 465 GLN B 52
REMARK 465 ASP B 53
REMARK 465 LYS B 54
REMARK 465 GLN B 55
REMARK 465 ALA B 56
REMARK 465 MET B 57
REMARK 465 LYS B 58
REMARK 465 LYS B 59
REMARK 465 GLY B 60
REMARK 465 PRO B 61
REMARK 465 ILE B 62
REMARK 465 TYR C 1
REMARK 465 ILE C 2
REMARK 465 ALA C 3
REMARK 465 ILE C 394
REMARK 465 ASP C 395
REMARK 465 GLY C 396
REMARK 465 GLN C 397
REMARK 465 GLN C 398
REMARK 465 HIS C 399
REMARK 465 SER C 400
REMARK 465 GLY C 401
REMARK 465 GLY C 402
REMARK 465 LEU C 403
REMARK 465 LYS C 404
REMARK 465 GLN C 405
REMARK 465 VAL C 406
REMARK 465 GLY C 407
REMARK 465 ASP C 408
REMARK 465 SER C 409
REMARK 465 GLN D 1
REMARK 465 ASP D 2
REMARK 465 GLY D 3
REMARK 465 LYS D 4
REMARK 465 THR D 5
REMARK 465 THR D 6
REMARK 465 PHE D 7
REMARK 465 GLU D 8
REMARK 465 LYS D 9
REMARK 465 GLU D 10
REMARK 465 GLY D 11
REMARK 465 GLY D 12
REMARK 465 GLY D 13
REMARK 465 GLY D 14
REMARK 465 ARG D 15
REMARK 465 GLY D 16
REMARK 465 PRO D 17
REMARK 465 ARG D 18
REMARK 465 ILE D 19
REMARK 465 LEU D 20
REMARK 465 GLU D 21
REMARK 465 ASN D 22
REMARK 465 MET D 23
REMARK 465 HIS D 24
REMARK 465 GLU D 25
REMARK 465 SER D 26
REMARK 465 LYS D 221
REMARK 465 LEU D 222
REMARK 465 LYS D 223
REMARK 465 PRO D 224
REMARK 465 SER D 225
REMARK 465 PRO D 226
REMARK 465 GLU D 227
REMARK 465 MET D 228
REMARK 465 GLN D 229
REMARK 465 ALA D 230
REMARK 465 MET D 231
REMARK 465 SER D 232
REMARK 465 ALA D 233
REMARK 465 PHE D 234
REMARK 465 ASN D 235
REMARK 465 ASN D 236
REMARK 465 ILE D 237
REMARK 465 LYS D 238
REMARK 465 GLN D 239
REMARK 465 MET D 240
REMARK 465 GLN D 241
REMARK 465 VAL D 242
REMARK 465 VAL D 243
REMARK 465 LEU D 244
REMARK 465 GLU D 245
REMARK 465 ARG D 246
REMARK 465 PRO D 247
REMARK 465 GLU D 248
REMARK 465 THR D 249
REMARK 465 ASP D 250
REMARK 465 HIS D 251
REMARK 465 VAL D 252
REMARK 465 ALA D 253
REMARK 465 GLU D 254
REMARK 465 ALA D 255
REMARK 465 ARG D 256
REMARK 465 GLY D 257
REMARK 465 ASP D 258
REMARK 465 SER D 259
REMARK 465 SER D 260
REMARK 465 PRO D 261
REMARK 465 SER D 262
REMARK 465 HIS D 263
REMARK 465 THR D 264
REMARK 465 GLY D 265
REMARK 465 LYS D 266
REMARK 465 LEU D 267
REMARK 465 ILE D 268
REMARK 465 THR D 269
REMARK 465 SER D 270
REMARK 465 SER D 271
REMARK 465 HIS D 272
REMARK 465 ARG D 273
REMARK 465 ARG D 274
REMARK 465 GLU D 275
REMARK 465 SER D 276
REMARK 465 PRO D 277
REMARK 465 SER D 278
REMARK 465 LEU D 279
REMARK 465 VAL D 280
REMARK 465 ASP D 281
REMARK 465 LYS D 282
REMARK 465 THR D 283
REMARK 465 SER D 284
REMARK 465 SER D 285
REMARK 465 ALA D 286
REMARK 465 SER D 287
REMARK 465 SER D 288
REMARK 465 VAL D 289
REMARK 465 HIS D 290
REMARK 465 ARG D 291
REMARK 465 CYS D 292
REMARK 465 THR D 293
REMARK 465 ARG D 294
REMARK 465 THR D 295
REMARK 465 VAL D 296
REMARK 465 THR D 297
REMARK 465 LYS D 298
REMARK 465 LYS D 299
REMARK 465 VAL D 300
REMARK 465 ILE D 301
REMARK 465 SER D 302
REMARK 465 GLY D 303
REMARK 465 PRO D 304
REMARK 465 ASP D 305
REMARK 465 GLY D 306
REMARK 465 PRO D 307
REMARK 465 ARG D 308
REMARK 465 GLU D 309
REMARK 465 GLU D 310
REMARK 465 ILE D 311
REMARK 465 VAL D 312
REMARK 465 GLU D 313
REMARK 465 LYS D 314
REMARK 465 MET D 315
REMARK 465 VAL D 316
REMARK 465 SER D 317
REMARK 465 SER D 318
REMARK 465 ASP D 319
REMARK 465 GLY D 320
REMARK 465 SER D 321
REMARK 465 ASP D 322
REMARK 465 CYS D 323
REMARK 465 SER D 324
REMARK 465 HIS D 325
REMARK 465 LEU D 326
REMARK 465 GLN D 327
REMARK 465 GLY D 328
REMARK 465 GLY D 329
REMARK 465 ARG D 330
REMARK 465 GLU D 331
REMARK 465 GLY D 332
REMARK 465 SER D 333
REMARK 465 THR D 334
REMARK 465 TYR D 335
REMARK 465 HIS D 336
REMARK 465 PHE D 337
REMARK 465 SER D 338
REMARK 465 GLY D 339
REMARK 465 THR D 340
REMARK 465 GLY D 341
REMARK 465 ASP D 342
REMARK 465 PHE D 343
REMARK 465 HIS D 344
REMARK 465 LYS D 345
REMARK 465 LEU D 346
REMARK 465 ASP D 347
REMARK 465 ARG D 348
REMARK 465 LEU D 349
REMARK 465 LEU D 350
REMARK 465 PRO D 351
REMARK 465 ASP D 352
REMARK 465 LEU D 353
REMARK 465 GLU D 354
REMARK 465 SER D 355
REMARK 465 PHE D 356
REMARK 465 PHE D 357
REMARK 465 THR D 358
REMARK 465 HIS D 359
REMARK 465 ASP D 360
REMARK 465 SER D 361
REMARK 465 VAL D 362
REMARK 465 SER D 363
REMARK 465 THR D 364
REMARK 465 SER D 365
REMARK 465 SER D 366
REMARK 465 ARG D 367
REMARK 465 HIS D 368
REMARK 465 SER D 369
REMARK 465 ILE D 370
REMARK 465 GLY D 371
REMARK 465 SER D 372
REMARK 465 SER D 373
REMARK 465 THR D 374
REMARK 465 SER D 375
REMARK 465 SER D 376
REMARK 465 HIS D 377
REMARK 465 VAL D 378
REMARK 465 THR D 379
REMARK 465 GLY D 380
REMARK 465 ALA D 381
REMARK 465 GLY D 382
REMARK 465 SER D 383
REMARK 465 SER D 384
REMARK 465 HIS D 385
REMARK 465 LEU D 386
REMARK 465 GLY D 387
REMARK 465 THR D 388
REMARK 465 GLY D 389
REMARK 465 GLY D 390
REMARK 465 LYS D 391
REMARK 465 ASP D 392
REMARK 465 LYS D 393
REMARK 465 PHE D 394
REMARK 465 THR D 395
REMARK 465 ASP D 396
REMARK 465 LEU D 397
REMARK 465 GLY D 398
REMARK 465 GLU D 399
REMARK 465 GLU D 400
REMARK 465 GLU D 401
REMARK 465 GLU D 402
REMARK 465 ASP D 403
REMARK 465 ASP D 404
REMARK 465 PHE D 405
REMARK 465 GLY D 406
REMARK 465 GLY D 407
REMARK 465 LEU D 408
REMARK 465 GLN D 409
REMARK 465 PRO D 410
REMARK 465 SER D 411
REMARK 465 GLY D 412
REMARK 465 PHE D 413
REMARK 465 ALA D 414
REMARK 465 ALA D 415
REMARK 465 GLY D 416
REMARK 465 SER D 417
REMARK 465 ALA D 418
REMARK 465 SER D 419
REMARK 465 HIS D 420
REMARK 465 SER D 421
REMARK 465 LYS D 422
REMARK 465 THR D 423
REMARK 465 VAL D 424
REMARK 465 LEU D 425
REMARK 465 THR D 426
REMARK 465 SER D 427
REMARK 465 SER D 428
REMARK 465 SER D 429
REMARK 465 SER D 430
REMARK 465 SER D 431
REMARK 465 PHE D 432
REMARK 465 ASN D 433
REMARK 465 LYS D 434
REMARK 465 GLY D 435
REMARK 465 GLY D 436
REMARK 465 SER D 437
REMARK 465 THR D 438
REMARK 465 PHE D 439
REMARK 465 GLU D 440
REMARK 465 THR D 441
REMARK 465 LYS D 442
REMARK 465 SER D 443
REMARK 465 LEU D 444
REMARK 465 LYS D 445
REMARK 465 THR D 446
REMARK 465 ARG D 447
REMARK 465 GLU D 448
REMARK 465 THR D 449
REMARK 465 SER D 450
REMARK 465 GLU D 451
REMARK 465 GLN D 452
REMARK 465 LEU D 453
REMARK 465 GLY D 454
REMARK 465 GLY D 455
REMARK 465 VAL D 456
REMARK 465 GLN D 457
REMARK 465 HIS D 458
REMARK 465 ASP D 459
REMARK 465 GLN D 460
REMARK 465 SER D 461
REMARK 465 ALA D 462
REMARK 465 GLU D 463
REMARK 465 ASP D 464
REMARK 465 THR D 465
REMARK 465 PRO D 466
REMARK 465 ASP D 467
REMARK 465 PHE D 468
REMARK 465 LYS D 469
REMARK 465 ALA D 470
REMARK 465 ARG D 471
REMARK 465 SER D 472
REMARK 465 PHE D 473
REMARK 465 ARG D 474
REMARK 465 PRO D 475
REMARK 465 ALA D 476
REMARK 465 ALA D 477
REMARK 465 MET D 478
REMARK 465 SER D 479
REMARK 465 THR D 480
REMARK 465 ARG D 481
REMARK 465 ARG D 482
REMARK 465 SER D 483
REMARK 465 TYR D 484
REMARK 465 ASN D 485
REMARK 465 GLY D 486
REMARK 465 LYS D 487
REMARK 465 GLY D 488
REMARK 465 THR D 489
REMARK 465 GLN D 490
REMARK 465 LYS D 491
REMARK 465 GLN E 1
REMARK 465 ALA E 2
REMARK 465 SER E 3
REMARK 465 VAL E 4
REMARK 465 GLU E 5
REMARK 465 TYR E 6
REMARK 465 ASP E 7
REMARK 465 ASN E 8
REMARK 465 GLU E 9
REMARK 465 GLU E 10
REMARK 465 ASP E 11
REMARK 465 SER E 12
REMARK 465 PRO E 13
REMARK 465 GLN E 14
REMARK 465 ILE E 15
REMARK 465 ASP E 16
REMARK 465 ALA E 17
REMARK 465 ARG E 18
REMARK 465 ALA E 19
REMARK 465 HIS E 20
REMARK 465 ARG E 21
REMARK 465 PRO E 22
REMARK 465 LEU E 23
REMARK 465 ASP E 24
REMARK 465 LYS E 25
REMARK 465 ARG E 26
REMARK 465 GLN E 27
REMARK 465 GLU E 28
REMARK 465 ALA E 29
REMARK 465 ALA E 30
REMARK 465 PRO E 31
REMARK 465 THR E 32
REMARK 465 LEU E 33
REMARK 465 ARG E 34
REMARK 465 PRO E 35
REMARK 465 VAL E 36
REMARK 465 ALA E 37
REMARK 465 PRO E 38
REMARK 465 PRO E 39
REMARK 465 ILE E 40
REMARK 465 SER E 41
REMARK 465 GLY E 42
REMARK 465 THR E 43
REMARK 465 GLY E 44
REMARK 465 TYR E 45
REMARK 465 GLN E 46
REMARK 465 PRO E 47
REMARK 465 ARG E 48
REMARK 465 PRO E 49
REMARK 465 PRO E 50
REMARK 465 LYS E 51
REMARK 465 GLN E 52
REMARK 465 ASP E 53
REMARK 465 LYS E 54
REMARK 465 GLN E 55
REMARK 465 ALA E 56
REMARK 465 MET E 57
REMARK 465 LYS E 58
REMARK 465 LYS E 59
REMARK 465 GLY E 60
REMARK 465 PRO E 61
REMARK 465 ILE E 62
REMARK 465 ASP E 464
REMARK 465 TYR F 1
REMARK 465 ILE F 2
REMARK 465 ALA F 3
REMARK 465 THR F 4
REMARK 465 ILE F 394
REMARK 465 ASP F 395
REMARK 465 GLY F 396
REMARK 465 GLN F 397
REMARK 465 GLN F 398
REMARK 465 HIS F 399
REMARK 465 SER F 400
REMARK 465 GLY F 401
REMARK 465 GLY F 402
REMARK 465 LEU F 403
REMARK 465 LYS F 404
REMARK 465 GLN F 405
REMARK 465 VAL F 406
REMARK 465 GLY F 407
REMARK 465 ASP F 408
REMARK 465 SER F 409
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG C 197 O GLY C 346 2.16
REMARK 500 NH2 ARG F 197 O GLY F 346 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG C 338 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 ARG F 338 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 28 -56.49 -178.57
REMARK 500 TRP A 34 156.94 -46.09
REMARK 500 CYS A 37 162.64 -49.09
REMARK 500 SER A 48 171.58 -49.94
REMARK 500 ASP A 57 -64.00 -90.73
REMARK 500 LYS A 80 32.67 -78.88
REMARK 500 VAL A 87 3.34 -55.61
REMARK 500 ILE A 88 -58.02 -120.07
REMARK 500 VAL A 89 -19.08 -47.99
REMARK 500 SER A 165 -32.33 -133.04
REMARK 500 LYS A 176 -3.67 -55.73
REMARK 500 THR A 187 -13.15 -49.98
REMARK 500 PRO A 196 173.55 -48.55
REMARK 500 LEU A 203 -105.07 5.67
REMARK 500 SER A 204 126.04 -27.33
REMARK 500 LEU A 206 151.49 -46.89
REMARK 500 LYS A 207 74.69 40.34
REMARK 500 PRO A 210 -91.33 -45.25
REMARK 500 LEU A 211 -108.11 172.47
REMARK 500 ASP A 213 -70.08 -82.90
REMARK 500 SER A 214 42.56 -86.95
REMARK 500 PRO A 217 39.80 -79.54
REMARK 500 PRO B 65 -97.03 -60.88
REMARK 500 ASP B 66 118.90 79.66
REMARK 500 ALA B 67 148.03 -173.35
REMARK 500 PRO B 73 3.61 -59.37
REMARK 500 ASP B 75 -30.90 -35.03
REMARK 500 PRO B 82 138.15 -38.01
REMARK 500 THR B 83 -178.37 -69.63
REMARK 500 LEU B 92 -34.57 -39.95
REMARK 500 SER B 145 -29.54 -38.00
REMARK 500 ASN B 164 -69.30 -139.44
REMARK 500 SER B 205 78.31 -106.51
REMARK 500 GLU B 228 -174.37 -171.47
REMARK 500 ASP B 250 65.30 36.06
REMARK 500 GLN B 261 -12.15 -165.78
REMARK 500 ASP B 262 3.99 -159.24
REMARK 500 LYS B 287 172.78 -57.68
REMARK 500 SER B 347 -176.70 178.35
REMARK 500 LYS B 350 124.21 -175.74
REMARK 500 ASN B 355 83.96 -65.33
REMARK 500 ASN B 386 15.50 -141.87
REMARK 500 ASN B 409 -114.50 -112.14
REMARK 500 ARG B 410 43.37 -92.00
REMARK 500 CYS B 411 -107.31 95.62
REMARK 500 ASN B 443 0.98 -52.77
REMARK 500 TRP B 448 38.80 -95.47
REMARK 500 PRO B 463 95.77 -59.06
REMARK 500 LEU C 11 -115.86 -89.56
REMARK 500 ASP C 12 103.58 98.17
REMARK 500
REMARK 500 THIS ENTRY HAS 163 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 385 OD1
REMARK 620 2 ASP B 385 OD2 48.2
REMARK 620 3 ASP B 387 OD1 110.6 67.8
REMARK 620 4 TRP B 389 O 145.9 149.0 82.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 318 OD1
REMARK 620 2 ASP C 318 OD2 51.9
REMARK 620 3 ASP C 320 OD1 71.8 102.6
REMARK 620 4 PHE C 322 O 147.4 150.7 77.9
REMARK 620 5 GLY C 324 O 120.5 76.6 96.4 74.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 385 OD2
REMARK 620 2 ASP E 385 OD1 50.3
REMARK 620 3 ASP E 387 OD2 57.0 95.9
REMARK 620 4 ASP E 387 OD1 73.8 124.0 41.8
REMARK 620 5 TRP E 389 O 163.3 146.4 111.5 89.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 318 OD1
REMARK 620 2 ASP F 318 OD2 50.2
REMARK 620 3 ASP F 320 OD1 66.9 97.9
REMARK 620 4 PHE F 322 O 144.8 154.2 80.8
REMARK 620 5 GLY F 324 O 120.4 78.4 97.9 76.3
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EI3 RELATED DB: PDB
REMARK 900 LOW RESOLUTION NATIVE CHICKEN FIBRINOGEN
REMARK 900 RELATED ID: 1FZC RELATED DB: PDB
REMARK 900 FRAGMENT DD FROM HUMAN FIBRIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO THE AUTHORS, THE PUBLISHED
REMARK 999 SEQUENCE OF CHICKEN FIBRINOGEN IS INCORRECT.
REMARK 999 IN THE ALPHA CHAIN, RESIDUE 49 IS GLY, NOT
REMARK 999 CYS. IN THE BETA CHAIN, RESIDUE 1 GENETICALLY
REMARK 999 MUST BE A GLN. IN THE GAMMA CHAIN, RESIDUE 286
REMARK 999 IS ALA, NOT ARG.
REMARK 999 CHAINS G AND H MIMIC A16-A19 OF THE FIBRIN
REMARK 999 SEQUENCE WITH PRO REPLACING ILE A19 OF THE
REMARK 999 FIBRIN SEQUENCE.
REMARK 999 CHAINS I AND J MIMIC B19-B22 OF THE FIBRIN
REMARK 999 SEQUENCE, WITH GLY REPLACING ALA B19 OF THE
REMARK 999 FIBRIN SEQUENCE.
DBREF 1M1J A 1 491 UNP P14448 FIBA_CHICK 19 509
DBREF 1M1J B 2 464 UNP Q02020 FIBB_CHICK 1 463
DBREF 1M1J C 1 409 UNP O93568 O93568_CHICK 27 435
DBREF 1M1J D 1 491 UNP P14448 FIBA_CHICK 19 509
DBREF 1M1J E 2 464 UNP Q02020 FIBB_CHICK 1 463
DBREF 1M1J F 1 409 UNP O93568 O93568_CHICK 27 435
DBREF 1M1J G 1 4 PDB 1M1J 1M1J 1 4
DBREF 1M1J H 1 4 PDB 1M1J 1M1J 1 4
DBREF 1M1J I 1 4 PDB 1M1J 1M1J 1 4
DBREF 1M1J J 1 4 PDB 1M1J 1M1J 1 4
SEQADV 1M1J GLY A 49 UNP P14448 CYS 67 SEE REMARK 999
SEQADV 1M1J GLN B 1 UNP Q02020 SEE REMARK 999
SEQADV 1M1J ALA C 286 UNP O93568 ARG 312 SEE REMARK 999
SEQADV 1M1J GLY D 49 UNP P14448 CYS 67 SEE REMARK 999
SEQADV 1M1J GLN E 1 UNP Q02020 SEE REMARK 999
SEQADV 1M1J ALA F 286 UNP O93568 ARG 312 SEE REMARK 999
SEQRES 1 A 491 GLN ASP GLY LYS THR THR PHE GLU LYS GLU GLY GLY GLY
SEQRES 2 A 491 GLY ARG GLY PRO ARG ILE LEU GLU ASN MET HIS GLU SER
SEQRES 3 A 491 SER CYS LYS TYR GLU LYS ASN TRP PRO ILE CYS VAL ASP
SEQRES 4 A 491 ASP ASP TRP GLY THR LYS CYS PRO SER GLY CYS ARG MET
SEQRES 5 A 491 GLN GLY ILE ILE ASP ASP THR ASP GLN ASN TYR SER GLN
SEQRES 6 A 491 ARG ILE ASP ASN ILE ARG GLN GLN LEU ALA ASP SER GLN
SEQRES 7 A 491 ASN LYS TYR LYS THR SER ASN ARG VAL ILE VAL GLU THR
SEQRES 8 A 491 ILE ASN ILE LEU LYS PRO GLY LEU GLU GLY ALA GLN GLN
SEQRES 9 A 491 LEU ASP GLU ASN TYR GLY HIS VAL SER THR GLU LEU ARG
SEQRES 10 A 491 ARG ARG ILE VAL THR LEU LYS GLN ARG VAL ALA THR GLN
SEQRES 11 A 491 VAL ASN ARG ILE LYS ALA LEU GLN ASN SER ILE GLN GLU
SEQRES 12 A 491 GLN VAL VAL GLU MET LYS ARG LEU GLU VAL ASP ILE ASP
SEQRES 13 A 491 ILE LYS ILE ARG ALA CYS LYS GLY SER CYS ALA ARG SER
SEQRES 14 A 491 PHE ASP TYR GLN VAL ASP LYS GLU GLY TYR ASP ASN ILE
SEQRES 15 A 491 GLN LYS HIS LEU THR GLN ALA SER SER ILE ASP MET HIS
SEQRES 16 A 491 PRO ASP PHE GLN THR THR THR LEU SER THR LEU LYS MET
SEQRES 17 A 491 ARG PRO LEU LYS ASP SER ASN VAL PRO GLU HIS PHE LYS
SEQRES 18 A 491 LEU LYS PRO SER PRO GLU MET GLN ALA MET SER ALA PHE
SEQRES 19 A 491 ASN ASN ILE LYS GLN MET GLN VAL VAL LEU GLU ARG PRO
SEQRES 20 A 491 GLU THR ASP HIS VAL ALA GLU ALA ARG GLY ASP SER SER
SEQRES 21 A 491 PRO SER HIS THR GLY LYS LEU ILE THR SER SER HIS ARG
SEQRES 22 A 491 ARG GLU SER PRO SER LEU VAL ASP LYS THR SER SER ALA
SEQRES 23 A 491 SER SER VAL HIS ARG CYS THR ARG THR VAL THR LYS LYS
SEQRES 24 A 491 VAL ILE SER GLY PRO ASP GLY PRO ARG GLU GLU ILE VAL
SEQRES 25 A 491 GLU LYS MET VAL SER SER ASP GLY SER ASP CYS SER HIS
SEQRES 26 A 491 LEU GLN GLY GLY ARG GLU GLY SER THR TYR HIS PHE SER
SEQRES 27 A 491 GLY THR GLY ASP PHE HIS LYS LEU ASP ARG LEU LEU PRO
SEQRES 28 A 491 ASP LEU GLU SER PHE PHE THR HIS ASP SER VAL SER THR
SEQRES 29 A 491 SER SER ARG HIS SER ILE GLY SER SER THR SER SER HIS
SEQRES 30 A 491 VAL THR GLY ALA GLY SER SER HIS LEU GLY THR GLY GLY
SEQRES 31 A 491 LYS ASP LYS PHE THR ASP LEU GLY GLU GLU GLU GLU ASP
SEQRES 32 A 491 ASP PHE GLY GLY LEU GLN PRO SER GLY PHE ALA ALA GLY
SEQRES 33 A 491 SER ALA SER HIS SER LYS THR VAL LEU THR SER SER SER
SEQRES 34 A 491 SER SER PHE ASN LYS GLY GLY SER THR PHE GLU THR LYS
SEQRES 35 A 491 SER LEU LYS THR ARG GLU THR SER GLU GLN LEU GLY GLY
SEQRES 36 A 491 VAL GLN HIS ASP GLN SER ALA GLU ASP THR PRO ASP PHE
SEQRES 37 A 491 LYS ALA ARG SER PHE ARG PRO ALA ALA MET SER THR ARG
SEQRES 38 A 491 ARG SER TYR ASN GLY LYS GLY THR GLN LYS
SEQRES 1 B 464 GLN ALA SER VAL GLU TYR ASP ASN GLU GLU ASP SER PRO
SEQRES 2 B 464 GLN ILE ASP ALA ARG ALA HIS ARG PRO LEU ASP LYS ARG
SEQRES 3 B 464 GLN GLU ALA ALA PRO THR LEU ARG PRO VAL ALA PRO PRO
SEQRES 4 B 464 ILE SER GLY THR GLY TYR GLN PRO ARG PRO PRO LYS GLN
SEQRES 5 B 464 ASP LYS GLN ALA MET LYS LYS GLY PRO ILE ILE TYR PRO
SEQRES 6 B 464 ASP ALA GLY GLY CYS LYS HIS PRO LEU ASP GLU LEU GLY
SEQRES 7 B 464 VAL LEU CYS PRO THR GLY CYS GLU LEU GLN THR THR LEU
SEQRES 8 B 464 LEU LYS GLN GLU LYS THR VAL LYS PRO VAL LEU ARG ASP
SEQRES 9 B 464 LEU LYS ASP ARG VAL ALA LYS PHE SER ASP THR SER THR
SEQRES 10 B 464 THR MET TYR GLN TYR VAL ASN MET ILE ASP ASN LYS LEU
SEQRES 11 B 464 VAL LYS THR GLN LYS GLN ARG LYS ASP ASN ASP ILE ILE
SEQRES 12 B 464 LEU SER GLU TYR ASN THR GLU MET GLU LEU HIS TYR ASN
SEQRES 13 B 464 TYR ILE LYS ASP ASN LEU ASP ASN ASN ILE PRO SER SER
SEQRES 14 B 464 LEU ARG VAL LEU ARG ALA VAL ILE ASP SER LEU HIS LYS
SEQRES 15 B 464 LYS ILE GLN LYS LEU GLU ASN ALA ILE ALA THR GLN THR
SEQRES 16 B 464 ASP TYR CYS ARG SER PRO CYS VAL ALA SER CYS ASN ILE
SEQRES 17 B 464 PRO VAL VAL SER GLY ARG GLU CYS GLU ASP ILE TYR ARG
SEQRES 18 B 464 LYS GLY GLY GLU THR SER GLU MET TYR ILE ILE GLN PRO
SEQRES 19 B 464 ASP PRO PHE THR THR PRO TYR ARG VAL TYR CYS ASP MET
SEQRES 20 B 464 GLU THR ASP ASN GLY GLY TRP THR LEU ILE GLN ASN ARG
SEQRES 21 B 464 GLN ASP GLY SER VAL ASN PHE GLY ARG ALA TRP ASP GLU
SEQRES 22 B 464 TYR LYS ARG GLY PHE GLY ASN ILE ALA LYS SER GLY GLY
SEQRES 23 B 464 LYS LYS TYR CYS ASP THR PRO GLY GLU TYR TRP LEU GLY
SEQRES 24 B 464 ASN ASP LYS ILE SER GLN LEU THR LYS ILE GLY PRO THR
SEQRES 25 B 464 LYS VAL LEU ILE GLU MET GLU ASP TRP ASN GLY ASP LYS
SEQRES 26 B 464 VAL SER ALA LEU TYR GLY GLY PHE THR ILE HIS ASN GLU
SEQRES 27 B 464 GLY ASN LYS TYR GLN LEU SER VAL SER ASN TYR LYS GLY
SEQRES 28 B 464 ASN ALA GLY ASN ALA LEU MET GLU GLY ALA SER GLN LEU
SEQRES 29 B 464 TYR GLY GLU ASN ARG THR MET THR ILE HIS ASN GLY MET
SEQRES 30 B 464 TYR PHE SER THR TYR ASP ARG ASP ASN ASP GLY TRP LEU
SEQRES 31 B 464 THR THR ASP PRO ARG LYS GLN CYS SER LYS GLU ASP GLY
SEQRES 32 B 464 GLY GLY TRP TRP TYR ASN ARG CYS HIS ALA ALA ASN PRO
SEQRES 33 B 464 ASN GLY ARG TYR TYR TRP GLY GLY THR TYR SER TRP ASP
SEQRES 34 B 464 MET ALA LYS HIS GLY THR ASP ASP GLY ILE VAL TRP MET
SEQRES 35 B 464 ASN TRP LYS GLY SER TRP TYR SER MET LYS LYS MET SER
SEQRES 36 B 464 MET LYS ILE LYS PRO TYR PHE PRO ASP
SEQRES 1 C 409 TYR ILE ALA THR ARG GLU ASN CYS CYS ILE LEU ASP GLU
SEQRES 2 C 409 ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA
SEQRES 3 C 409 ASP PHE PHE ASN LYS TYR ARG LEU THR THR ASP GLY GLU
SEQRES 4 C 409 LEU LEU GLU ILE GLU GLY LEU LEU GLN GLN ALA THR ASN
SEQRES 5 C 409 SER THR GLY SER ILE GLU TYR LEU ILE GLN HIS ILE LYS
SEQRES 6 C 409 THR ILE TYR PRO SER GLU LYS GLN THR LEU PRO GLN SER
SEQRES 7 C 409 ILE GLU GLN LEU THR GLN LYS SER LYS LYS ILE ILE GLU
SEQRES 8 C 409 GLU ILE ILE ARG TYR GLU ASN THR ILE LEU ALA HIS GLU
SEQRES 9 C 409 ASN THR ILE GLN GLN LEU THR ASP MET HIS ILE MET ASN
SEQRES 10 C 409 SER ASN LYS ILE THR GLN LEU LYS GLN LYS ILE ALA GLN
SEQRES 11 C 409 LEU GLU SER HIS CYS GLN GLU PRO CYS LYS ASP THR ALA
SEQRES 12 C 409 GLU ILE GLN GLU THR THR GLY ARG ASP CYS GLN ASP ILE
SEQRES 13 C 409 ALA ASN LYS GLY ALA ARG LYS SER GLY LEU TYR PHE ILE
SEQRES 14 C 409 LYS PRO GLN LYS ALA LYS GLN SER PHE LEU VAL TYR CYS
SEQRES 15 C 409 GLU ILE ASP THR TYR GLY ASN GLY TRP THR VAL LEU GLN
SEQRES 16 C 409 ARG ARG LEU ASP GLY SER GLU ASP PHE ARG ARG ASN TRP
SEQRES 17 C 409 VAL GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO ASP
SEQRES 18 C 409 ASP THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS
SEQRES 19 C 409 LEU ILE THR THR GLN SER THR LEU PRO TYR ALA LEU ARG
SEQRES 20 C 409 ILE GLU LEU GLU ASP TRP SER GLY LYS LYS GLY THR ALA
SEQRES 21 C 409 ASP TYR ALA VAL PHE LYS VAL GLY THR GLU GLU ASP LYS
SEQRES 22 C 409 TYR ARG LEU THR TYR ALA TYR PHE ILE GLY GLY GLU ALA
SEQRES 23 C 409 GLY ASP ALA PHE ASP GLY PHE ASN PHE GLY ASP ASP PRO
SEQRES 24 C 409 SER ASP LYS SER TYR THR TYR HIS ASN GLY MET ARG PHE
SEQRES 25 C 409 SER THR PHE ASP ASN ASP ASN ASP ASN PHE GLU GLY ASN
SEQRES 26 C 409 CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN ARG
SEQRES 27 C 409 CYS HIS ALA GLY HIS LEU ASN GLY PRO TYR TYR ILE GLY
SEQRES 28 C 409 GLY VAL TYR SER ARG ASP THR GLY THR ASN SER TYR ASP
SEQRES 29 C 409 ASN GLY ILE ILE TRP ALA THR TRP ARG ASP ARG TRP TYR
SEQRES 30 C 409 SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN
SEQRES 31 C 409 ARG LEU SER ILE ASP GLY GLN GLN HIS SER GLY GLY LEU
SEQRES 32 C 409 LYS GLN VAL GLY ASP SER
SEQRES 1 D 491 GLN ASP GLY LYS THR THR PHE GLU LYS GLU GLY GLY GLY
SEQRES 2 D 491 GLY ARG GLY PRO ARG ILE LEU GLU ASN MET HIS GLU SER
SEQRES 3 D 491 SER CYS LYS TYR GLU LYS ASN TRP PRO ILE CYS VAL ASP
SEQRES 4 D 491 ASP ASP TRP GLY THR LYS CYS PRO SER GLY CYS ARG MET
SEQRES 5 D 491 GLN GLY ILE ILE ASP ASP THR ASP GLN ASN TYR SER GLN
SEQRES 6 D 491 ARG ILE ASP ASN ILE ARG GLN GLN LEU ALA ASP SER GLN
SEQRES 7 D 491 ASN LYS TYR LYS THR SER ASN ARG VAL ILE VAL GLU THR
SEQRES 8 D 491 ILE ASN ILE LEU LYS PRO GLY LEU GLU GLY ALA GLN GLN
SEQRES 9 D 491 LEU ASP GLU ASN TYR GLY HIS VAL SER THR GLU LEU ARG
SEQRES 10 D 491 ARG ARG ILE VAL THR LEU LYS GLN ARG VAL ALA THR GLN
SEQRES 11 D 491 VAL ASN ARG ILE LYS ALA LEU GLN ASN SER ILE GLN GLU
SEQRES 12 D 491 GLN VAL VAL GLU MET LYS ARG LEU GLU VAL ASP ILE ASP
SEQRES 13 D 491 ILE LYS ILE ARG ALA CYS LYS GLY SER CYS ALA ARG SER
SEQRES 14 D 491 PHE ASP TYR GLN VAL ASP LYS GLU GLY TYR ASP ASN ILE
SEQRES 15 D 491 GLN LYS HIS LEU THR GLN ALA SER SER ILE ASP MET HIS
SEQRES 16 D 491 PRO ASP PHE GLN THR THR THR LEU SER THR LEU LYS MET
SEQRES 17 D 491 ARG PRO LEU LYS ASP SER ASN VAL PRO GLU HIS PHE LYS
SEQRES 18 D 491 LEU LYS PRO SER PRO GLU MET GLN ALA MET SER ALA PHE
SEQRES 19 D 491 ASN ASN ILE LYS GLN MET GLN VAL VAL LEU GLU ARG PRO
SEQRES 20 D 491 GLU THR ASP HIS VAL ALA GLU ALA ARG GLY ASP SER SER
SEQRES 21 D 491 PRO SER HIS THR GLY LYS LEU ILE THR SER SER HIS ARG
SEQRES 22 D 491 ARG GLU SER PRO SER LEU VAL ASP LYS THR SER SER ALA
SEQRES 23 D 491 SER SER VAL HIS ARG CYS THR ARG THR VAL THR LYS LYS
SEQRES 24 D 491 VAL ILE SER GLY PRO ASP GLY PRO ARG GLU GLU ILE VAL
SEQRES 25 D 491 GLU LYS MET VAL SER SER ASP GLY SER ASP CYS SER HIS
SEQRES 26 D 491 LEU GLN GLY GLY ARG GLU GLY SER THR TYR HIS PHE SER
SEQRES 27 D 491 GLY THR GLY ASP PHE HIS LYS LEU ASP ARG LEU LEU PRO
SEQRES 28 D 491 ASP LEU GLU SER PHE PHE THR HIS ASP SER VAL SER THR
SEQRES 29 D 491 SER SER ARG HIS SER ILE GLY SER SER THR SER SER HIS
SEQRES 30 D 491 VAL THR GLY ALA GLY SER SER HIS LEU GLY THR GLY GLY
SEQRES 31 D 491 LYS ASP LYS PHE THR ASP LEU GLY GLU GLU GLU GLU ASP
SEQRES 32 D 491 ASP PHE GLY GLY LEU GLN PRO SER GLY PHE ALA ALA GLY
SEQRES 33 D 491 SER ALA SER HIS SER LYS THR VAL LEU THR SER SER SER
SEQRES 34 D 491 SER SER PHE ASN LYS GLY GLY SER THR PHE GLU THR LYS
SEQRES 35 D 491 SER LEU LYS THR ARG GLU THR SER GLU GLN LEU GLY GLY
SEQRES 36 D 491 VAL GLN HIS ASP GLN SER ALA GLU ASP THR PRO ASP PHE
SEQRES 37 D 491 LYS ALA ARG SER PHE ARG PRO ALA ALA MET SER THR ARG
SEQRES 38 D 491 ARG SER TYR ASN GLY LYS GLY THR GLN LYS
SEQRES 1 E 464 GLN ALA SER VAL GLU TYR ASP ASN GLU GLU ASP SER PRO
SEQRES 2 E 464 GLN ILE ASP ALA ARG ALA HIS ARG PRO LEU ASP LYS ARG
SEQRES 3 E 464 GLN GLU ALA ALA PRO THR LEU ARG PRO VAL ALA PRO PRO
SEQRES 4 E 464 ILE SER GLY THR GLY TYR GLN PRO ARG PRO PRO LYS GLN
SEQRES 5 E 464 ASP LYS GLN ALA MET LYS LYS GLY PRO ILE ILE TYR PRO
SEQRES 6 E 464 ASP ALA GLY GLY CYS LYS HIS PRO LEU ASP GLU LEU GLY
SEQRES 7 E 464 VAL LEU CYS PRO THR GLY CYS GLU LEU GLN THR THR LEU
SEQRES 8 E 464 LEU LYS GLN GLU LYS THR VAL LYS PRO VAL LEU ARG ASP
SEQRES 9 E 464 LEU LYS ASP ARG VAL ALA LYS PHE SER ASP THR SER THR
SEQRES 10 E 464 THR MET TYR GLN TYR VAL ASN MET ILE ASP ASN LYS LEU
SEQRES 11 E 464 VAL LYS THR GLN LYS GLN ARG LYS ASP ASN ASP ILE ILE
SEQRES 12 E 464 LEU SER GLU TYR ASN THR GLU MET GLU LEU HIS TYR ASN
SEQRES 13 E 464 TYR ILE LYS ASP ASN LEU ASP ASN ASN ILE PRO SER SER
SEQRES 14 E 464 LEU ARG VAL LEU ARG ALA VAL ILE ASP SER LEU HIS LYS
SEQRES 15 E 464 LYS ILE GLN LYS LEU GLU ASN ALA ILE ALA THR GLN THR
SEQRES 16 E 464 ASP TYR CYS ARG SER PRO CYS VAL ALA SER CYS ASN ILE
SEQRES 17 E 464 PRO VAL VAL SER GLY ARG GLU CYS GLU ASP ILE TYR ARG
SEQRES 18 E 464 LYS GLY GLY GLU THR SER GLU MET TYR ILE ILE GLN PRO
SEQRES 19 E 464 ASP PRO PHE THR THR PRO TYR ARG VAL TYR CYS ASP MET
SEQRES 20 E 464 GLU THR ASP ASN GLY GLY TRP THR LEU ILE GLN ASN ARG
SEQRES 21 E 464 GLN ASP GLY SER VAL ASN PHE GLY ARG ALA TRP ASP GLU
SEQRES 22 E 464 TYR LYS ARG GLY PHE GLY ASN ILE ALA LYS SER GLY GLY
SEQRES 23 E 464 LYS LYS TYR CYS ASP THR PRO GLY GLU TYR TRP LEU GLY
SEQRES 24 E 464 ASN ASP LYS ILE SER GLN LEU THR LYS ILE GLY PRO THR
SEQRES 25 E 464 LYS VAL LEU ILE GLU MET GLU ASP TRP ASN GLY ASP LYS
SEQRES 26 E 464 VAL SER ALA LEU TYR GLY GLY PHE THR ILE HIS ASN GLU
SEQRES 27 E 464 GLY ASN LYS TYR GLN LEU SER VAL SER ASN TYR LYS GLY
SEQRES 28 E 464 ASN ALA GLY ASN ALA LEU MET GLU GLY ALA SER GLN LEU
SEQRES 29 E 464 TYR GLY GLU ASN ARG THR MET THR ILE HIS ASN GLY MET
SEQRES 30 E 464 TYR PHE SER THR TYR ASP ARG ASP ASN ASP GLY TRP LEU
SEQRES 31 E 464 THR THR ASP PRO ARG LYS GLN CYS SER LYS GLU ASP GLY
SEQRES 32 E 464 GLY GLY TRP TRP TYR ASN ARG CYS HIS ALA ALA ASN PRO
SEQRES 33 E 464 ASN GLY ARG TYR TYR TRP GLY GLY THR TYR SER TRP ASP
SEQRES 34 E 464 MET ALA LYS HIS GLY THR ASP ASP GLY ILE VAL TRP MET
SEQRES 35 E 464 ASN TRP LYS GLY SER TRP TYR SER MET LYS LYS MET SER
SEQRES 36 E 464 MET LYS ILE LYS PRO TYR PHE PRO ASP
SEQRES 1 F 409 TYR ILE ALA THR ARG GLU ASN CYS CYS ILE LEU ASP GLU
SEQRES 2 F 409 ARG PHE GLY SER TYR CYS PRO THR THR CYS GLY ILE ALA
SEQRES 3 F 409 ASP PHE PHE ASN LYS TYR ARG LEU THR THR ASP GLY GLU
SEQRES 4 F 409 LEU LEU GLU ILE GLU GLY LEU LEU GLN GLN ALA THR ASN
SEQRES 5 F 409 SER THR GLY SER ILE GLU TYR LEU ILE GLN HIS ILE LYS
SEQRES 6 F 409 THR ILE TYR PRO SER GLU LYS GLN THR LEU PRO GLN SER
SEQRES 7 F 409 ILE GLU GLN LEU THR GLN LYS SER LYS LYS ILE ILE GLU
SEQRES 8 F 409 GLU ILE ILE ARG TYR GLU ASN THR ILE LEU ALA HIS GLU
SEQRES 9 F 409 ASN THR ILE GLN GLN LEU THR ASP MET HIS ILE MET ASN
SEQRES 10 F 409 SER ASN LYS ILE THR GLN LEU LYS GLN LYS ILE ALA GLN
SEQRES 11 F 409 LEU GLU SER HIS CYS GLN GLU PRO CYS LYS ASP THR ALA
SEQRES 12 F 409 GLU ILE GLN GLU THR THR GLY ARG ASP CYS GLN ASP ILE
SEQRES 13 F 409 ALA ASN LYS GLY ALA ARG LYS SER GLY LEU TYR PHE ILE
SEQRES 14 F 409 LYS PRO GLN LYS ALA LYS GLN SER PHE LEU VAL TYR CYS
SEQRES 15 F 409 GLU ILE ASP THR TYR GLY ASN GLY TRP THR VAL LEU GLN
SEQRES 16 F 409 ARG ARG LEU ASP GLY SER GLU ASP PHE ARG ARG ASN TRP
SEQRES 17 F 409 VAL GLN TYR LYS GLU GLY PHE GLY HIS LEU SER PRO ASP
SEQRES 18 F 409 ASP THR THR GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS
SEQRES 19 F 409 LEU ILE THR THR GLN SER THR LEU PRO TYR ALA LEU ARG
SEQRES 20 F 409 ILE GLU LEU GLU ASP TRP SER GLY LYS LYS GLY THR ALA
SEQRES 21 F 409 ASP TYR ALA VAL PHE LYS VAL GLY THR GLU GLU ASP LYS
SEQRES 22 F 409 TYR ARG LEU THR TYR ALA TYR PHE ILE GLY GLY GLU ALA
SEQRES 23 F 409 GLY ASP ALA PHE ASP GLY PHE ASN PHE GLY ASP ASP PRO
SEQRES 24 F 409 SER ASP LYS SER TYR THR TYR HIS ASN GLY MET ARG PHE
SEQRES 25 F 409 SER THR PHE ASP ASN ASP ASN ASP ASN PHE GLU GLY ASN
SEQRES 26 F 409 CYS ALA GLU GLN ASP GLY SER GLY TRP TRP MET ASN ARG
SEQRES 27 F 409 CYS HIS ALA GLY HIS LEU ASN GLY PRO TYR TYR ILE GLY
SEQRES 28 F 409 GLY VAL TYR SER ARG ASP THR GLY THR ASN SER TYR ASP
SEQRES 29 F 409 ASN GLY ILE ILE TRP ALA THR TRP ARG ASP ARG TRP TYR
SEQRES 30 F 409 SER MET LYS LYS THR THR MET LYS ILE ILE PRO PHE ASN
SEQRES 31 F 409 ARG LEU SER ILE ASP GLY GLN GLN HIS SER GLY GLY LEU
SEQRES 32 F 409 LYS GLN VAL GLY ASP SER
SEQRES 1 G 4 GLY PRO ARG PRO
SEQRES 1 H 4 GLY PRO ARG PRO
SEQRES 1 I 4 GLY HIS ARG PRO
SEQRES 1 J 4 GLY HIS ARG PRO
HET NDG B 470 15
HET CA B 503 1
HET NDG C 420 15
HET NAG C 421 15
HET CA C 501 1
HET NDG E 570 15
HET CA E 504 1
HET NDG F 520 15
HET NAG F 521 15
HET CA F 502 1
HET NAG I 471 15
HET NDG J 571 15
HETNAM NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 11 NDG 5(C8 H15 N O6)
FORMUL 12 CA 4(CA 2+)
FORMUL 14 NAG 3(C8 H15 N O6)
HELIX 1 1 ARG A 51 LYS A 80 1 30
HELIX 2 2 LYS A 82 ALA A 161 1 80
HELIX 3 3 TYR A 179 SER A 190 1 12
HELIX 4 4 CYS B 85 ASN B 164 1 80
HELIX 5 5 ASN B 164 CYS B 198 1 35
HELIX 6 6 GLU B 215 LYS B 222 1 8
HELIX 7 7 GLU B 248 GLY B 252 5 5
HELIX 8 8 ALA B 270 GLY B 277 1 8
HELIX 9 9 GLY B 299 LYS B 308 1 10
HELIX 10 10 ASN B 337 LYS B 341 5 5
HELIX 11 11 ASN B 355 GLY B 360 1 6
HELIX 12 12 GLY B 366 MET B 371 1 6
HELIX 13 13 GLN B 397 ASP B 402 1 6
HELIX 14 14 SER B 427 ALA B 431 5 5
HELIX 15 15 MET B 442 GLY B 446 1 5
HELIX 16 16 ASP C 12 GLY C 16 5 5
HELIX 17 17 THR C 21 TYR C 68 1 48
HELIX 18 18 SER C 78 TYR C 96 1 19
HELIX 19 19 TYR C 96 SER C 133 1 38
HELIX 20 20 ASP C 152 ASN C 158 1 7
HELIX 21 21 ASN C 207 GLY C 214 1 8
HELIX 22 22 GLY C 229 THR C 238 1 10
HELIX 23 23 ASP C 288 GLY C 292 5 5
HELIX 24 24 SER C 300 THR C 305 5 6
HELIX 25 25 ASN C 325 GLY C 331 1 7
HELIX 26 26 ASN C 390 SER C 393 5 4
HELIX 27 27 ARG D 51 ILE D 55 5 5
HELIX 28 28 LEU D 74 ASN D 79 1 6
HELIX 29 29 TYR D 81 ALA D 161 1 81
HELIX 30 30 GLU D 177 ILE D 192 1 16
HELIX 31 31 THR E 83 THR E 90 1 8
HELIX 32 32 LYS E 99 ARG E 103 5 5
HELIX 33 33 ASP E 114 HIS E 154 1 41
HELIX 34 34 ASN E 156 ASN E 165 1 10
HELIX 35 35 ASN E 165 CYS E 198 1 34
HELIX 36 36 GLU E 215 LYS E 222 1 8
HELIX 37 37 ALA E 270 GLY E 277 1 8
HELIX 38 38 GLY E 299 LYS E 308 1 10
HELIX 39 39 ASN E 337 LYS E 341 5 5
HELIX 40 40 ASN E 355 GLY E 360 1 6
HELIX 41 41 GLY E 366 MET E 371 1 6
HELIX 42 42 GLN E 397 GLY E 403 1 7
HELIX 43 43 MET E 442 GLY E 446 1 5
HELIX 44 44 LEU F 34 GLY F 38 5 5
HELIX 45 45 GLU F 42 GLU F 58 1 17
HELIX 46 46 HIS F 63 TYR F 68 1 6
HELIX 47 47 SER F 78 GLU F 97 1 20
HELIX 48 48 ASN F 98 HIS F 134 1 37
HELIX 49 49 ASP F 152 ASN F 158 1 7
HELIX 50 50 ASN F 207 GLY F 214 1 8
HELIX 51 51 GLY F 229 THR F 238 1 10
HELIX 52 52 ASP F 288 GLY F 292 5 5
HELIX 53 53 SER F 300 THR F 305 5 6
HELIX 54 54 ASN F 325 ASP F 330 1 6
HELIX 55 55 ASN F 390 SER F 393 5 4
SHEET 1 A 3 LYS A 45 CYS A 46 0
SHEET 2 A 3 VAL E 79 PRO E 82 -1 O CYS E 81 N CYS A 46
SHEET 3 A 3 CYS E 70 LYS E 71 -1 N CYS E 70 O LEU E 80
SHEET 1 B 3 CYS B 70 LYS B 71 0
SHEET 2 B 3 VAL B 79 PRO B 82 -1 O LEU B 80 N CYS B 70
SHEET 3 B 3 LYS D 45 CYS D 46 -1 O CYS D 46 N CYS B 81
SHEET 1 C 2 VAL B 203 ALA B 204 0
SHEET 2 C 2 LYS C 140 ASP C 141 1 O LYS C 140 N ALA B 204
SHEET 1 D 8 TYR C 280 GLY C 283 0
SHEET 2 D 8 LYS C 257 ALA C 263 -1 N ALA C 263 O TYR C 280
SHEET 3 D 8 TYR C 244 GLU C 251 -1 N ILE C 248 O ALA C 260
SHEET 4 D 8 LYS C 381 PRO C 388 -1 O LYS C 385 N ARG C 247
SHEET 5 D 8 GLY C 190 ARG C 197 -1 N ARG C 197 O THR C 382
SHEET 6 D 8 PHE C 178 ILE C 184 -1 N GLU C 183 O TRP C 191
SHEET 7 D 8 GLY C 165 ILE C 169 -1 N GLY C 165 O CYS C 182
SHEET 8 D 8 ILE C 145 GLY C 150 1 N GLY C 150 O PHE C 168
SHEET 1 E 8 TYR C 280 GLY C 283 0
SHEET 2 E 8 LYS C 257 ALA C 263 -1 N ALA C 263 O TYR C 280
SHEET 3 E 8 TYR C 244 GLU C 251 -1 N ILE C 248 O ALA C 260
SHEET 4 E 8 LYS C 381 PRO C 388 -1 O LYS C 385 N ARG C 247
SHEET 5 E 8 GLY C 190 ARG C 197 -1 N ARG C 197 O THR C 382
SHEET 6 E 8 PHE C 226 TRP C 227 -1 O PHE C 226 N ARG C 196
SHEET 7 E 8 PHE C 215 LEU C 218 -1 N PHE C 215 O TRP C 227
SHEET 8 E 8 ILE B 208 PRO B 209 -1 N ILE B 208 O LEU C 218
SHEET 1 F 7 LEU B 344 GLY B 351 0
SHEET 2 F 7 LYS B 325 ILE B 335 -1 N LEU B 329 O LYS B 350
SHEET 3 F 7 THR B 312 GLU B 319 -1 N ILE B 316 O ALA B 328
SHEET 4 F 7 LYS B 453 PRO B 460 -1 O LYS B 457 N LEU B 315
SHEET 5 F 7 TRP B 254 ARG B 260 -1 N ARG B 260 O MET B 454
SHEET 6 F 7 TYR B 241 ASP B 246 -1 N ASP B 246 O TRP B 254
SHEET 7 F 7 GLU B 228 ILE B 232 -1 N TYR B 230 O VAL B 243
SHEET 1 G 7 LEU B 344 GLY B 351 0
SHEET 2 G 7 LYS B 325 ILE B 335 -1 N LEU B 329 O LYS B 350
SHEET 3 G 7 THR B 312 GLU B 319 -1 N ILE B 316 O ALA B 328
SHEET 4 G 7 LYS B 453 PRO B 460 -1 O LYS B 457 N LEU B 315
SHEET 5 G 7 TRP B 254 ARG B 260 -1 N ARG B 260 O MET B 454
SHEET 6 G 7 TYR B 296 TRP B 297 -1 O TYR B 296 N ASN B 259
SHEET 7 G 7 PHE B 278 GLY B 279 -1 N PHE B 278 O TRP B 297
SHEET 1 H 2 ALA B 282 LYS B 283 0
SHEET 2 H 2 THR B 292 PRO B 293 -1 O THR B 292 N LYS B 283
SHEET 1 I 2 ALA B 414 ASN B 415 0
SHEET 2 I 2 VAL B 440 TRP B 441 -1 O VAL B 440 N ASN B 415
SHEET 1 J 3 TYR C 18 PRO C 20 0
SHEET 2 J 3 GLY F 16 PRO F 20 -1 O CYS F 19 N CYS C 19
SHEET 3 J 3 ILE F 10 ASP F 12 -1 O ASP F 12 N GLY F 16
SHEET 1 K 2 LYS C 266 VAL C 267 0
SHEET 2 K 2 LEU C 276 THR C 277 -1 O THR C 277 N LYS C 266
SHEET 1 L 2 GLY C 342 HIS C 343 0
SHEET 2 L 2 ILE C 368 TRP C 369 -1 O ILE C 368 N HIS C 343
SHEET 1 M 2 VAL E 203 ALA E 204 0
SHEET 2 M 2 LYS F 140 ASP F 141 1 O LYS F 140 N ALA E 204
SHEET 1 N 8 TYR F 280 GLY F 283 0
SHEET 2 N 8 LYS F 257 ALA F 263 -1 N ASP F 261 O ILE F 282
SHEET 3 N 8 TYR F 244 GLU F 251 -1 N LEU F 250 O GLY F 258
SHEET 4 N 8 LYS F 381 PRO F 388 -1 O LYS F 385 N ARG F 247
SHEET 5 N 8 GLY F 190 ARG F 197 -1 N ARG F 197 O THR F 382
SHEET 6 N 8 PHE F 178 ILE F 184 -1 N GLU F 183 O TRP F 191
SHEET 7 N 8 GLY F 165 ILE F 169 -1 N GLY F 165 O CYS F 182
SHEET 8 N 8 ILE F 145 GLY F 150 1 N GLY F 150 O PHE F 168
SHEET 1 O 8 TYR F 280 GLY F 283 0
SHEET 2 O 8 LYS F 257 ALA F 263 -1 N ASP F 261 O ILE F 282
SHEET 3 O 8 TYR F 244 GLU F 251 -1 N LEU F 250 O GLY F 258
SHEET 4 O 8 LYS F 381 PRO F 388 -1 O LYS F 385 N ARG F 247
SHEET 5 O 8 GLY F 190 ARG F 197 -1 N ARG F 197 O THR F 382
SHEET 6 O 8 PHE F 226 TRP F 227 -1 O PHE F 226 N ARG F 196
SHEET 7 O 8 PHE F 215 LEU F 218 -1 N PHE F 215 O TRP F 227
SHEET 8 O 8 ILE E 208 PRO E 209 -1 N ILE E 208 O LEU F 218
SHEET 1 P 7 LEU E 344 GLY E 351 0
SHEET 2 P 7 LYS E 325 ILE E 335 -1 N LEU E 329 O LYS E 350
SHEET 3 P 7 THR E 312 GLU E 319 -1 N ILE E 316 O ALA E 328
SHEET 4 P 7 LYS E 453 PRO E 460 -1 O LYS E 457 N LEU E 315
SHEET 5 P 7 TRP E 254 ARG E 260 -1 N THR E 255 O ILE E 458
SHEET 6 P 7 TYR E 241 ASP E 246 -1 N ASP E 246 O TRP E 254
SHEET 7 P 7 GLU E 228 ILE E 232 -1 N TYR E 230 O VAL E 243
SHEET 1 Q 7 LEU E 344 GLY E 351 0
SHEET 2 Q 7 LYS E 325 ILE E 335 -1 N LEU E 329 O LYS E 350
SHEET 3 Q 7 THR E 312 GLU E 319 -1 N ILE E 316 O ALA E 328
SHEET 4 Q 7 LYS E 453 PRO E 460 -1 O LYS E 457 N LEU E 315
SHEET 5 Q 7 TRP E 254 ARG E 260 -1 N THR E 255 O ILE E 458
SHEET 6 Q 7 TYR E 296 TRP E 297 -1 O TYR E 296 N ASN E 259
SHEET 7 Q 7 PHE E 278 GLY E 279 -1 N PHE E 278 O TRP E 297
SHEET 1 R 2 ALA E 282 LYS E 283 0
SHEET 2 R 2 THR E 292 PRO E 293 -1 O THR E 292 N LYS E 283
SHEET 1 S 2 ALA E 414 ASN E 415 0
SHEET 2 S 2 VAL E 440 TRP E 441 -1 O VAL E 440 N ASN E 415
SHEET 1 T 2 LYS F 266 VAL F 267 0
SHEET 2 T 2 LEU F 276 THR F 277 -1 O THR F 277 N LYS F 266
SHEET 1 U 2 GLY F 342 HIS F 343 0
SHEET 2 U 2 ILE F 368 TRP F 369 -1 O ILE F 368 N HIS F 343
SSBOND 1 CYS A 28 CYS D 28 1555 1555 2.03
SSBOND 2 CYS A 37 CYS E 70 1555 1555 2.03
SSBOND 3 CYS A 46 CYS C 23 1555 1555 2.03
SSBOND 4 CYS A 50 CYS B 81 1555 1555 2.02
SSBOND 5 CYS A 162 CYS C 135 1555 1555 2.03
SSBOND 6 CYS A 166 CYS B 198 1555 1555 2.04
SSBOND 7 CYS B 70 CYS D 37 1555 1555 2.04
SSBOND 8 CYS B 85 CYS C 19 1555 1555 2.03
SSBOND 9 CYS B 202 CYS C 139 1555 1555 2.04
SSBOND 10 CYS B 206 CYS B 290 1555 1555 2.04
SSBOND 11 CYS B 216 CYS B 245 1555 1555 2.04
SSBOND 12 CYS B 398 CYS B 411 1555 1555 2.04
SSBOND 13 CYS C 8 CYS F 9 1555 1555 2.03
SSBOND 14 CYS C 9 CYS F 8 1555 1555 2.03
SSBOND 15 CYS C 153 CYS C 182 1555 1555 2.03
SSBOND 16 CYS C 326 CYS C 339 1555 1555 2.04
SSBOND 17 CYS D 46 CYS F 23 1555 1555 2.02
SSBOND 18 CYS D 50 CYS E 81 1555 1555 2.03
SSBOND 19 CYS D 162 CYS F 135 1555 1555 2.03
SSBOND 20 CYS D 166 CYS E 198 1555 1555 2.04
SSBOND 21 CYS E 85 CYS F 19 1555 1555 2.03
SSBOND 22 CYS E 202 CYS F 139 1555 1555 2.04
SSBOND 23 CYS E 206 CYS E 290 1555 1555 2.04
SSBOND 24 CYS E 216 CYS E 245 1555 1555 2.03
SSBOND 25 CYS E 398 CYS E 411 1555 1555 2.03
SSBOND 26 CYS F 153 CYS F 182 1555 1555 2.03
SSBOND 27 CYS F 326 CYS F 339 1555 1555 2.05
LINK OD1 ASP B 385 CA CA B 503 1555 1555 2.42
LINK OD2 ASP B 385 CA CA B 503 1555 1555 2.86
LINK OD1 ASP B 387 CA CA B 503 1555 1555 2.46
LINK O TRP B 389 CA CA B 503 1555 1555 2.36
LINK OD1 ASP C 318 CA CA C 501 1555 1555 2.58
LINK OD2 ASP C 318 CA CA C 501 1555 1555 2.42
LINK OD1 ASP C 320 CA CA C 501 1555 1555 2.41
LINK O PHE C 322 CA CA C 501 1555 1555 2.22
LINK O GLY C 324 CA CA C 501 1555 1555 2.31
LINK OD2 ASP E 385 CA CA E 504 1555 1555 2.76
LINK OD1 ASP E 385 CA CA E 504 1555 1555 2.38
LINK OD2 ASP E 387 CA CA E 504 1555 1555 3.26
LINK OD1 ASP E 387 CA CA E 504 1555 1555 2.13
LINK O TRP E 389 CA CA E 504 1555 1555 2.39
LINK OD1 ASP F 318 CA CA F 502 1555 1555 2.69
LINK OD2 ASP F 318 CA CA F 502 1555 1555 2.43
LINK OD1 ASP F 320 CA CA F 502 1555 1555 2.40
LINK O PHE F 322 CA CA F 502 1555 1555 2.14
LINK O GLY F 324 CA CA F 502 1555 1555 2.22
CRYST1 114.090 100.020 200.090 90.00 105.79 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008765 0.000000 0.002478 0.00000
SCALE2 0.000000 0.009998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
