HEADER HYDROLASE 04-FEB-02 1KY9
TITLE CRYSTAL STRUCTURE OF DEGP (HTRA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE DO;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DEGP, HTRA;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DEGP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN QUALITY CONTROL, SERINE PROTEASE, TRYPSIN, CHAPERONE, PDZ,
KEYWDS 2 ATP-INDEPENDENT, TEMPERATURE-REGULATED, PERIPLASM, CAGE-FORMING
KEYWDS 3 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KROJER,M.GARRIDO-FRANCO,R.HUBER,M.EHRMANN,T.CLAUSEN
REVDAT 4 27-OCT-21 1KY9 1 SEQADV LINK
REVDAT 3 24-FEB-09 1KY9 1 VERSN
REVDAT 2 01-APR-03 1KY9 1 JRNL
REVDAT 1 03-APR-02 1KY9 0
JRNL AUTH T.KROJER,M.GARRIDO-FRANCO,R.HUBER,M.EHRMANN,T.CLAUSEN
JRNL TITL CRYSTAL STRUCTURE OF DEGP (HTRA) REVEALS A NEW
JRNL TITL 2 PROTEASE-CHAPERONE MACHINE.
JRNL REF NATURE V. 416 455 2002
JRNL REFN ISSN 0028-0836
JRNL PMID 11919638
JRNL DOI 10.1038/416455A
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.80
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 47131
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) : 0.218
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2338
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 : 5200
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 82.00
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 1KY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9500, 0.9795, 0.9797
REMARK 200 MONOCHROMATOR : SI111 OR SI311 CRYSTALS, LN2
REMARK 200 COOLED
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 : 48312
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL, PEG 2000 MME, TRIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.83350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 116.83350
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 116.83350
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 116.83350
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 116.83350
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 116.83350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: HEXAMERS OF MOLECULE A AND B ARE ENTIRELY FORMED BY CRYSTAL
REMARK 300 SYMMETRY.
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 121.37400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 60.68700
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 105.11297
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 60.68700
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 105.11297
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 116.83350
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 121.37400
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 116.83350
REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 116.83350
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 ALA A 9
REMARK 465 GLN A 10
REMARK 465 ASP A 52
REMARK 465 ASP A 53
REMARK 465 SER A 54
REMARK 465 PRO A 55
REMARK 465 PHE A 56
REMARK 465 CYS A 57
REMARK 465 GLN A 58
REMARK 465 GLU A 59
REMARK 465 GLY A 60
REMARK 465 SER A 61
REMARK 465 PRO A 62
REMARK 465 PHE A 63
REMARK 465 GLN A 64
REMARK 465 SER A 65
REMARK 465 SER A 66
REMARK 465 PRO A 67
REMARK 465 PHE A 68
REMARK 465 CYS A 69
REMARK 465 GLN A 70
REMARK 465 GLY A 71
REMARK 465 GLY A 72
REMARK 465 GLN A 73
REMARK 465 GLY A 74
REMARK 465 GLY A 75
REMARK 465 ASN A 76
REMARK 465 GLY A 77
REMARK 465 GLY A 78
REMARK 465 LEU A 190
REMARK 465 ASN A 191
REMARK 465 ALA A 192
REMARK 465 GLU A 193
REMARK 465 ASN A 194
REMARK 465 LEU A 354
REMARK 465 GLN A 355
REMARK 465 GLN A 356
REMARK 465 SER A 357
REMARK 465 SER A 358
REMARK 465 GLN A 359
REMARK 465 ASN A 360
REMARK 465 GLN A 361
REMARK 465 VAL A 362
REMARK 465 ASP A 363
REMARK 465 SER A 364
REMARK 465 SER A 365
REMARK 465 SER A 366
REMARK 465 ILE A 367
REMARK 465 PHE A 368
REMARK 465 ASN A 369
REMARK 465 GLY A 370
REMARK 465 ILE A 371
REMARK 465 GLU A 372
REMARK 465 GLY A 373
REMARK 465 ALA A 374
REMARK 465 GLU A 375
REMARK 465 MSE A 376
REMARK 465 SER A 377
REMARK 465 ASN A 378
REMARK 465 LYS A 379
REMARK 465 GLY A 380
REMARK 465 LYS A 381
REMARK 465 ASP A 382
REMARK 465 GLN A 383
REMARK 465 GLY A 384
REMARK 465 VAL A 385
REMARK 465 VAL A 386
REMARK 465 VAL A 387
REMARK 465 ASN A 388
REMARK 465 ASN A 389
REMARK 465 VAL A 390
REMARK 465 LYS A 391
REMARK 465 THR A 392
REMARK 465 GLY A 393
REMARK 465 THR A 394
REMARK 465 PRO A 395
REMARK 465 ALA A 396
REMARK 465 ALA A 397
REMARK 465 GLN A 398
REMARK 465 ILE A 399
REMARK 465 GLY A 400
REMARK 465 LEU A 401
REMARK 465 LYS A 402
REMARK 465 LYS A 403
REMARK 465 GLY A 404
REMARK 465 ASP A 405
REMARK 465 VAL A 406
REMARK 465 ILE A 407
REMARK 465 ILE A 408
REMARK 465 GLY A 409
REMARK 465 ALA A 410
REMARK 465 ASN A 411
REMARK 465 GLN A 412
REMARK 465 GLN A 413
REMARK 465 ALA A 414
REMARK 465 VAL A 415
REMARK 465 LYS A 416
REMARK 465 ASN A 417
REMARK 465 ILE A 418
REMARK 465 ALA A 419
REMARK 465 GLU A 420
REMARK 465 LEU A 421
REMARK 465 ARG A 422
REMARK 465 LYS A 423
REMARK 465 VAL A 424
REMARK 465 LEU A 425
REMARK 465 ASP A 426
REMARK 465 SER A 427
REMARK 465 LYS A 428
REMARK 465 PRO A 429
REMARK 465 SER A 430
REMARK 465 VAL A 431
REMARK 465 LEU A 432
REMARK 465 ALA A 433
REMARK 465 LEU A 434
REMARK 465 ASN A 435
REMARK 465 ILE A 436
REMARK 465 GLN A 437
REMARK 465 ARG A 438
REMARK 465 GLY A 439
REMARK 465 ASP A 440
REMARK 465 SER A 441
REMARK 465 THR A 442
REMARK 465 ILE A 443
REMARK 465 TYR A 444
REMARK 465 LEU A 445
REMARK 465 LEU A 446
REMARK 465 MSE A 447
REMARK 465 GLN A 448
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 THR B 8
REMARK 465 ALA B 9
REMARK 465 GLN B 10
REMARK 465 ASP B 52
REMARK 465 ASP B 53
REMARK 465 SER B 54
REMARK 465 PRO B 55
REMARK 465 PHE B 56
REMARK 465 CYS B 57
REMARK 465 GLN B 58
REMARK 465 GLU B 59
REMARK 465 GLY B 60
REMARK 465 SER B 61
REMARK 465 PRO B 62
REMARK 465 PHE B 63
REMARK 465 GLN B 64
REMARK 465 SER B 65
REMARK 465 SER B 66
REMARK 465 PRO B 67
REMARK 465 PHE B 68
REMARK 465 CYS B 69
REMARK 465 GLN B 70
REMARK 465 GLY B 71
REMARK 465 GLY B 72
REMARK 465 GLN B 73
REMARK 465 GLY B 74
REMARK 465 GLY B 75
REMARK 465 ASN B 76
REMARK 465 GLY B 77
REMARK 465 GLY B 78
REMARK 465 SER B 188
REMARK 465 GLY B 189
REMARK 465 LEU B 190
REMARK 465 ASN B 191
REMARK 465 ALA B 192
REMARK 465 GLU B 193
REMARK 465 ASN B 194
REMARK 465 TYR B 195
REMARK 465 GLY B 370
REMARK 465 ILE B 371
REMARK 465 GLU B 372
REMARK 465 GLY B 373
REMARK 465 ALA B 374
REMARK 465 MSE B 447
REMARK 465 GLN B 448
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 C ALA B 230 CD PRO B 231 1.68
REMARK 500 NH2 ARG B 121 O LYS B 145 2.03
REMARK 500 O VAL A 160 O VAL A 182 2.12
REMARK 500 CG MSE A 127 O HOH A 490 2.14
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 PRO A 231 C - N - CA ANGL. DEV. = 24.6 DEGREES
REMARK 500 PRO A 231 C - N - CD ANGL. DEV. = -21.4 DEGREES
REMARK 500 LEU B 87 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 PRO B 231 C - N - CA ANGL. DEV. = 60.1 DEGREES
REMARK 500 PRO B 231 C - N - CD ANGL. DEV. = -53.7 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 PHE A 46 11.89 -69.53
REMARK 500 ARG A 187 -74.30 -155.51
REMARK 500 GLU A 196 66.29 -107.06
REMARK 500 ASN A 197 -175.01 -50.65
REMARK 500 ALA A 210 105.96 -49.35
REMARK 500 PRO A 231 9.26 -56.23
REMARK 500 GLU A 264 95.79 -44.48
REMARK 500 ILE A 267 -72.62 179.00
REMARK 500 MSE A 268 100.95 157.54
REMARK 500 GLU A 271 156.20 -27.90
REMARK 500 ASN A 273 -6.41 96.06
REMARK 500 SER A 274 -167.52 -77.61
REMARK 500 GLU A 275 -70.73 -56.93
REMARK 500 MSE A 280 -155.42 -85.46
REMARK 500 LYS A 281 -97.97 -22.81
REMARK 500 ALA A 284 40.41 100.94
REMARK 500 GLN A 285 -153.68 -57.27
REMARK 500 ARG A 286 86.40 69.87
REMARK 500 VAL A 293 -11.26 -163.46
REMARK 500 PRO A 295 -18.96 -49.96
REMARK 500 ALA A 299 -33.13 -130.41
REMARK 500 ALA A 306 151.44 -46.44
REMARK 500 ASP A 308 167.21 -35.66
REMARK 500 VAL A 309 84.74 -151.97
REMARK 500 THR A 311 27.64 -148.37
REMARK 500 LEU A 313 69.61 -153.91
REMARK 500 ASN A 314 30.89 81.00
REMARK 500 SER A 319 -85.62 -59.37
REMARK 500 VAL A 333 152.78 -40.96
REMARK 500 ARG A 343 26.94 170.15
REMARK 500 ASP A 344 57.06 70.01
REMARK 500 LYS A 346 116.28 -179.06
REMARK 500 GLN A 347 103.31 -160.39
REMARK 500 LEU A 352 126.47 -37.24
REMARK 500 PRO B 43 -173.83 -67.22
REMARK 500 PHE B 50 -165.47 -61.91
REMARK 500 ASN B 143 54.49 70.69
REMARK 500 LEU B 173 4.06 -52.64
REMARK 500 LEU B 185 59.17 -108.22
REMARK 500 ASN B 197 56.98 -60.78
REMARK 500 ALA B 204 -138.27 -120.04
REMARK 500 ALA B 210 99.52 -45.06
REMARK 500 ILE B 228 34.81 -95.32
REMARK 500 PRO B 231 40.29 75.81
REMARK 500 TYR B 257 -26.48 -150.54
REMARK 500 THR B 270 -149.53 -154.19
REMARK 500 SER B 274 152.25 -40.41
REMARK 500 ALA B 279 -9.56 -59.53
REMARK 500 LYS B 281 98.68 39.97
REMARK 500 ALA B 284 89.32 49.21
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KY9 A 1 448 UNP P0C0V0 DEGP_ECOLI 27 474
DBREF 1KY9 B 1 448 UNP P0C0V0 DEGP_ECOLI 27 474
SEQADV 1KY9 MSE A 12 UNP P0C0V0 MET 38 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 18 UNP P0C0V0 MET 44 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 23 UNP P0C0V0 MET 49 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 42 UNP P0C0V0 MET 68 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 85 UNP P0C0V0 MET 111 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 127 UNP P0C0V0 MET 153 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 152 UNP P0C0V0 MET 178 MODIFIED RESIDUE
SEQADV 1KY9 ALA A 210 UNP P0C0V0 SER 236 ENGINEERED MUTATION
SEQADV 1KY9 MSE A 246 UNP P0C0V0 MET 272 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 254 UNP P0C0V0 MET 280 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 268 UNP P0C0V0 MET 294 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 280 UNP P0C0V0 MET 306 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 331 UNP P0C0V0 MET 357 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 376 UNP P0C0V0 MET 402 MODIFIED RESIDUE
SEQADV 1KY9 MSE A 447 UNP P0C0V0 MET 473 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 12 UNP P0C0V0 MET 38 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 18 UNP P0C0V0 MET 44 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 23 UNP P0C0V0 MET 49 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 42 UNP P0C0V0 MET 68 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 85 UNP P0C0V0 MET 111 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 127 UNP P0C0V0 MET 153 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 152 UNP P0C0V0 MET 178 MODIFIED RESIDUE
SEQADV 1KY9 ALA B 210 UNP P0C0V0 SER 236 ENGINEERED MUTATION
SEQADV 1KY9 MSE B 246 UNP P0C0V0 MET 272 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 254 UNP P0C0V0 MET 280 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 268 UNP P0C0V0 MET 294 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 280 UNP P0C0V0 MET 306 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 331 UNP P0C0V0 MET 357 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 376 UNP P0C0V0 MET 402 MODIFIED RESIDUE
SEQADV 1KY9 MSE B 447 UNP P0C0V0 MET 473 MODIFIED RESIDUE
SEQRES 1 A 448 ALA GLU THR SER SER ALA THR THR ALA GLN GLN MSE PRO
SEQRES 2 A 448 SER LEU ALA PRO MSE LEU GLU LYS VAL MSE PRO SER VAL
SEQRES 3 A 448 VAL SER ILE ASN VAL GLU GLY SER THR THR VAL ASN THR
SEQRES 4 A 448 PRO ARG MSE PRO ARG ASN PHE GLN GLN PHE PHE GLY ASP
SEQRES 5 A 448 ASP SER PRO PHE CYS GLN GLU GLY SER PRO PHE GLN SER
SEQRES 6 A 448 SER PRO PHE CYS GLN GLY GLY GLN GLY GLY ASN GLY GLY
SEQRES 7 A 448 GLY GLN GLN GLN LYS PHE MSE ALA LEU GLY SER GLY VAL
SEQRES 8 A 448 ILE ILE ASP ALA ASP LYS GLY TYR VAL VAL THR ASN ASN
SEQRES 9 A 448 HIS VAL VAL ASP ASN ALA THR VAL ILE LYS VAL GLN LEU
SEQRES 10 A 448 SER ASP GLY ARG LYS PHE ASP ALA LYS MSE VAL GLY LYS
SEQRES 11 A 448 ASP PRO ARG SER ASP ILE ALA LEU ILE GLN ILE GLN ASN
SEQRES 12 A 448 PRO LYS ASN LEU THR ALA ILE LYS MSE ALA ASP SER ASP
SEQRES 13 A 448 ALA LEU ARG VAL GLY ASP TYR THR VAL ALA ILE GLY ASN
SEQRES 14 A 448 PRO PHE GLY LEU GLY GLU THR VAL THR SER GLY ILE VAL
SEQRES 15 A 448 SER ALA LEU GLY ARG SER GLY LEU ASN ALA GLU ASN TYR
SEQRES 16 A 448 GLU ASN PHE ILE GLN THR ASP ALA ALA ILE ASN ARG GLY
SEQRES 17 A 448 ASN ALA GLY GLY ALA LEU VAL ASN LEU ASN GLY GLU LEU
SEQRES 18 A 448 ILE GLY ILE ASN THR ALA ILE LEU ALA PRO ASP GLY GLY
SEQRES 19 A 448 ASN ILE GLY ILE GLY PHE ALA ILE PRO SER ASN MSE VAL
SEQRES 20 A 448 LYS ASN LEU THR SER GLN MSE VAL GLU TYR GLY GLN VAL
SEQRES 21 A 448 LYS ARG GLY GLU LEU GLY ILE MSE GLY THR GLU LEU ASN
SEQRES 22 A 448 SER GLU LEU ALA LYS ALA MSE LYS VAL ASP ALA GLN ARG
SEQRES 23 A 448 GLY ALA PHE VAL SER GLN VAL LEU PRO ASN SER SER ALA
SEQRES 24 A 448 ALA LYS ALA GLY ILE LYS ALA GLY ASP VAL ILE THR SER
SEQRES 25 A 448 LEU ASN GLY LYS PRO ILE SER SER PHE ALA ALA LEU ARG
SEQRES 26 A 448 ALA GLN VAL GLY THR MSE PRO VAL GLY SER LYS LEU THR
SEQRES 27 A 448 LEU GLY LEU LEU ARG ASP GLY LYS GLN VAL ASN VAL ASN
SEQRES 28 A 448 LEU GLU LEU GLN GLN SER SER GLN ASN GLN VAL ASP SER
SEQRES 29 A 448 SER SER ILE PHE ASN GLY ILE GLU GLY ALA GLU MSE SER
SEQRES 30 A 448 ASN LYS GLY LYS ASP GLN GLY VAL VAL VAL ASN ASN VAL
SEQRES 31 A 448 LYS THR GLY THR PRO ALA ALA GLN ILE GLY LEU LYS LYS
SEQRES 32 A 448 GLY ASP VAL ILE ILE GLY ALA ASN GLN GLN ALA VAL LYS
SEQRES 33 A 448 ASN ILE ALA GLU LEU ARG LYS VAL LEU ASP SER LYS PRO
SEQRES 34 A 448 SER VAL LEU ALA LEU ASN ILE GLN ARG GLY ASP SER THR
SEQRES 35 A 448 ILE TYR LEU LEU MSE GLN
SEQRES 1 B 448 ALA GLU THR SER SER ALA THR THR ALA GLN GLN MSE PRO
SEQRES 2 B 448 SER LEU ALA PRO MSE LEU GLU LYS VAL MSE PRO SER VAL
SEQRES 3 B 448 VAL SER ILE ASN VAL GLU GLY SER THR THR VAL ASN THR
SEQRES 4 B 448 PRO ARG MSE PRO ARG ASN PHE GLN GLN PHE PHE GLY ASP
SEQRES 5 B 448 ASP SER PRO PHE CYS GLN GLU GLY SER PRO PHE GLN SER
SEQRES 6 B 448 SER PRO PHE CYS GLN GLY GLY GLN GLY GLY ASN GLY GLY
SEQRES 7 B 448 GLY GLN GLN GLN LYS PHE MSE ALA LEU GLY SER GLY VAL
SEQRES 8 B 448 ILE ILE ASP ALA ASP LYS GLY TYR VAL VAL THR ASN ASN
SEQRES 9 B 448 HIS VAL VAL ASP ASN ALA THR VAL ILE LYS VAL GLN LEU
SEQRES 10 B 448 SER ASP GLY ARG LYS PHE ASP ALA LYS MSE VAL GLY LYS
SEQRES 11 B 448 ASP PRO ARG SER ASP ILE ALA LEU ILE GLN ILE GLN ASN
SEQRES 12 B 448 PRO LYS ASN LEU THR ALA ILE LYS MSE ALA ASP SER ASP
SEQRES 13 B 448 ALA LEU ARG VAL GLY ASP TYR THR VAL ALA ILE GLY ASN
SEQRES 14 B 448 PRO PHE GLY LEU GLY GLU THR VAL THR SER GLY ILE VAL
SEQRES 15 B 448 SER ALA LEU GLY ARG SER GLY LEU ASN ALA GLU ASN TYR
SEQRES 16 B 448 GLU ASN PHE ILE GLN THR ASP ALA ALA ILE ASN ARG GLY
SEQRES 17 B 448 ASN ALA GLY GLY ALA LEU VAL ASN LEU ASN GLY GLU LEU
SEQRES 18 B 448 ILE GLY ILE ASN THR ALA ILE LEU ALA PRO ASP GLY GLY
SEQRES 19 B 448 ASN ILE GLY ILE GLY PHE ALA ILE PRO SER ASN MSE VAL
SEQRES 20 B 448 LYS ASN LEU THR SER GLN MSE VAL GLU TYR GLY GLN VAL
SEQRES 21 B 448 LYS ARG GLY GLU LEU GLY ILE MSE GLY THR GLU LEU ASN
SEQRES 22 B 448 SER GLU LEU ALA LYS ALA MSE LYS VAL ASP ALA GLN ARG
SEQRES 23 B 448 GLY ALA PHE VAL SER GLN VAL LEU PRO ASN SER SER ALA
SEQRES 24 B 448 ALA LYS ALA GLY ILE LYS ALA GLY ASP VAL ILE THR SER
SEQRES 25 B 448 LEU ASN GLY LYS PRO ILE SER SER PHE ALA ALA LEU ARG
SEQRES 26 B 448 ALA GLN VAL GLY THR MSE PRO VAL GLY SER LYS LEU THR
SEQRES 27 B 448 LEU GLY LEU LEU ARG ASP GLY LYS GLN VAL ASN VAL ASN
SEQRES 28 B 448 LEU GLU LEU GLN GLN SER SER GLN ASN GLN VAL ASP SER
SEQRES 29 B 448 SER SER ILE PHE ASN GLY ILE GLU GLY ALA GLU MSE SER
SEQRES 30 B 448 ASN LYS GLY LYS ASP GLN GLY VAL VAL VAL ASN ASN VAL
SEQRES 31 B 448 LYS THR GLY THR PRO ALA ALA GLN ILE GLY LEU LYS LYS
SEQRES 32 B 448 GLY ASP VAL ILE ILE GLY ALA ASN GLN GLN ALA VAL LYS
SEQRES 33 B 448 ASN ILE ALA GLU LEU ARG LYS VAL LEU ASP SER LYS PRO
SEQRES 34 B 448 SER VAL LEU ALA LEU ASN ILE GLN ARG GLY ASP SER THR
SEQRES 35 B 448 ILE TYR LEU LEU MSE GLN
MODRES 1KY9 MSE A 12 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 18 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 23 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 42 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 85 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 127 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 152 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 246 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 254 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 268 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 280 MET SELENOMETHIONINE
MODRES 1KY9 MSE A 331 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 12 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 18 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 23 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 42 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 85 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 127 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 152 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 246 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 254 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 268 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 280 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 331 MET SELENOMETHIONINE
MODRES 1KY9 MSE B 376 MET SELENOMETHIONINE
HET MSE A 12 8
HET MSE A 18 8
HET MSE A 23 8
HET MSE A 42 8
HET MSE A 85 8
HET MSE A 127 8
HET MSE A 152 8
HET MSE A 246 8
HET MSE A 254 8
HET MSE A 268 8
HET MSE A 280 8
HET MSE A 331 8
HET MSE B 12 8
HET MSE B 18 8
HET MSE B 23 8
HET MSE B 42 8
HET MSE B 85 8
HET MSE B 127 8
HET MSE B 152 8
HET MSE B 246 8
HET MSE B 254 8
HET MSE B 268 8
HET MSE B 280 8
HET MSE B 331 8
HET MSE B 376 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 25(C5 H11 N O2 SE)
FORMUL 3 HOH *166(H2 O)
HELIX 1 1 LEU A 15 MSE A 23 1 9
HELIX 2 2 ASN A 104 ASP A 108 1 5
HELIX 3 3 ASP A 154 LEU A 158 5 5
HELIX 4 4 SER A 244 GLY A 258 1 15
HELIX 5 5 SER A 274 ALA A 279 1 6
HELIX 6 6 PHE A 321 VAL A 328 1 8
HELIX 7 7 LEU B 15 MSE B 23 1 9
HELIX 8 8 ASN B 104 ASP B 108 1 5
HELIX 9 9 ASP B 154 LEU B 158 5 5
HELIX 10 10 SER B 244 GLY B 258 1 15
HELIX 11 11 SER B 274 ALA B 279 1 6
HELIX 12 12 SER B 297 GLY B 303 1 7
HELIX 13 13 SER B 320 VAL B 328 1 9
HELIX 14 14 GLY B 329 MSE B 331 5 3
HELIX 15 15 ALA B 396 GLY B 400 5 5
HELIX 16 16 ASN B 417 LEU B 425 1 9
SHEET 1 A 7 VAL A 26 VAL A 37 0
SHEET 2 A 7 GLN A 80 ASP A 94 -1 O PHE A 84 N GLY A 33
SHEET 3 A 7 TYR A 99 ASN A 103 -1 O VAL A 101 N VAL A 91
SHEET 4 A 7 ILE A 136 ILE A 141 -1 O ILE A 139 N VAL A 100
SHEET 5 A 7 LYS A 122 ASP A 131 -1 N GLY A 129 O LEU A 138
SHEET 6 A 7 ALA A 110 LEU A 117 -1 N VAL A 115 O PHE A 123
SHEET 7 A 7 VAL A 26 VAL A 37 -1 N GLU A 32 O VAL A 112
SHEET 1 B 7 TYR A 163 GLY A 168 0
SHEET 2 B 7 THR A 176 LEU A 185 -1 O THR A 178 N ALA A 166
SHEET 3 B 7 ILE A 199 THR A 201 -1 O GLN A 200 N ALA A 184
SHEET 4 B 7 GLY A 239 PRO A 243 -1 O GLY A 239 N THR A 201
SHEET 5 B 7 LEU A 221 THR A 226 -1 N ILE A 224 O ILE A 242
SHEET 6 B 7 ALA A 213 VAL A 215 -1 N LEU A 214 O ILE A 222
SHEET 7 B 7 TYR A 163 GLY A 168 -1 N VAL A 165 O VAL A 215
SHEET 1 C 4 ALA A 288 PHE A 289 0
SHEET 2 C 4 VAL A 309 ILE A 310 -1 O ILE A 310 N ALA A 288
SHEET 3 C 4 THR A 338 LEU A 342 -1 O LEU A 342 N VAL A 309
SHEET 4 C 4 GLN A 347 ASN A 349 -1 O VAL A 348 N LEU A 339
SHEET 1 D 7 VAL B 26 VAL B 37 0
SHEET 2 D 7 GLN B 80 ASP B 94 -1 O ALA B 86 N VAL B 31
SHEET 3 D 7 TYR B 99 ASN B 103 -1 O VAL B 101 N VAL B 91
SHEET 4 D 7 ILE B 136 GLN B 142 -1 O ALA B 137 N THR B 102
SHEET 5 D 7 LYS B 122 ASP B 131 -1 N ASP B 124 O GLN B 142
SHEET 6 D 7 ALA B 110 GLN B 116 -1 N VAL B 115 O PHE B 123
SHEET 7 D 7 VAL B 26 VAL B 37 -1 N ASN B 30 O LYS B 114
SHEET 1 E 7 TYR B 163 GLY B 168 0
SHEET 2 E 7 THR B 176 LEU B 185 -1 O THR B 178 N ALA B 166
SHEET 3 E 7 ILE B 199 THR B 201 -1 O GLN B 200 N ALA B 184
SHEET 4 E 7 GLY B 239 PRO B 243 -1 O ALA B 241 N ILE B 199
SHEET 5 E 7 LEU B 221 THR B 226 -1 N THR B 226 O PHE B 240
SHEET 6 E 7 ALA B 213 VAL B 215 -1 N LEU B 214 O ILE B 222
SHEET 7 E 7 TYR B 163 GLY B 168 -1 N VAL B 165 O VAL B 215
SHEET 1 F 2 GLY B 263 GLU B 264 0
SHEET 2 F 2 GLU B 353 LEU B 354 -1 O GLU B 353 N GLU B 264
SHEET 1 G 3 ILE B 267 THR B 270 0
SHEET 2 G 3 ALA B 288 VAL B 293 -1 O PHE B 289 N THR B 270
SHEET 3 G 3 VAL B 309 ILE B 310 -1 O ILE B 310 N ALA B 288
SHEET 1 H 4 LYS B 316 PRO B 317 0
SHEET 2 H 4 SER B 312 LEU B 313 -1 N LEU B 313 O LYS B 316
SHEET 3 H 4 LEU B 339 GLY B 340 -1 O GLY B 340 N SER B 312
SHEET 4 H 4 GLN B 347 VAL B 348 -1 O VAL B 348 N LEU B 339
SHEET 1 I 4 GLN B 413 ALA B 414 0
SHEET 2 I 4 VAL B 406 ALA B 410 -1 N ALA B 410 O GLN B 413
SHEET 3 I 4 LEU B 434 GLN B 437 -1 O GLN B 437 N VAL B 406
SHEET 4 I 4 THR B 442 LEU B 445 -1 O LEU B 445 N LEU B 434
LINK C GLN A 11 N MSE A 12 1555 1555 1.33
LINK C MSE A 12 N PRO A 13 1555 1555 1.34
LINK C PRO A 17 N MSE A 18 1555 1555 1.34
LINK C MSE A 18 N LEU A 19 1555 1555 1.32
LINK C VAL A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N PRO A 24 1555 1555 1.34
LINK C ARG A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N PRO A 43 1555 1555 1.35
LINK C PHE A 84 N MSE A 85 1555 1555 1.32
LINK C MSE A 85 N ALA A 86 1555 1555 1.33
LINK C LYS A 126 N MSE A 127 1555 1555 1.31
LINK C MSE A 127 N VAL A 128 1555 1555 1.34
LINK C LYS A 151 N MSE A 152 1555 1555 1.33
LINK C MSE A 152 N ALA A 153 1555 1555 1.32
LINK C ASN A 245 N MSE A 246 1555 1555 1.33
LINK C MSE A 246 N VAL A 247 1555 1555 1.33
LINK C GLN A 253 N MSE A 254 1555 1555 1.33
LINK C MSE A 254 N VAL A 255 1555 1555 1.33
LINK C ILE A 267 N MSE A 268 1555 1555 1.35
LINK C MSE A 268 N GLY A 269 1555 1555 1.31
LINK C ALA A 279 N MSE A 280 1555 1555 1.33
LINK C MSE A 280 N LYS A 281 1555 1555 1.33
LINK C THR A 330 N MSE A 331 1555 1555 1.33
LINK C MSE A 331 N PRO A 332 1555 1555 1.35
LINK C GLN B 11 N MSE B 12 1555 1555 1.33
LINK C MSE B 12 N PRO B 13 1555 1555 1.33
LINK C PRO B 17 N MSE B 18 1555 1555 1.34
LINK C MSE B 18 N LEU B 19 1555 1555 1.33
LINK C VAL B 22 N MSE B 23 1555 1555 1.32
LINK C MSE B 23 N PRO B 24 1555 1555 1.34
LINK C ARG B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N PRO B 43 1555 1555 1.35
LINK C PHE B 84 N MSE B 85 1555 1555 1.32
LINK C MSE B 85 N ALA B 86 1555 1555 1.32
LINK C LYS B 126 N MSE B 127 1555 1555 1.33
LINK C MSE B 127 N VAL B 128 1555 1555 1.31
LINK C LYS B 151 N MSE B 152 1555 1555 1.33
LINK C MSE B 152 N ALA B 153 1555 1555 1.33
LINK C ASN B 245 N MSE B 246 1555 1555 1.33
LINK C MSE B 246 N VAL B 247 1555 1555 1.34
LINK C GLN B 253 N MSE B 254 1555 1555 1.33
LINK C MSE B 254 N VAL B 255 1555 1555 1.34
LINK C ILE B 267 N MSE B 268 1555 1555 1.32
LINK C MSE B 268 N GLY B 269 1555 1555 1.32
LINK C ALA B 279 N MSE B 280 1555 1555 1.33
LINK C MSE B 280 N LYS B 281 1555 1555 1.33
LINK C THR B 330 N MSE B 331 1555 1555 1.33
LINK C MSE B 331 N PRO B 332 1555 1555 1.35
LINK C GLU B 375 N MSE B 376 1555 1555 1.33
LINK C MSE B 376 N SER B 377 1555 1555 1.33
CISPEP 1 MSE A 42 PRO A 43 0 0.06
CISPEP 2 ALA A 230 PRO A 231 0 0.14
CISPEP 3 MSE B 42 PRO B 43 0 -0.13
CRYST1 121.374 121.374 233.667 90.00 90.00 120.00 P 63 2 2 24
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 0.008239 0.004757 0.000000 0.00000
SCALE2 0.000000 0.009514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004280 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
