HEADER OXIDOREDUCTASE 09-JAN-01 1HWL
TITLE COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH
TITLE 2 ROSUVASTATIN (FORMALLY KNOWN AS ZD4522)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HMG-COA REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC PORTION;
COMPND 5 SYNONYM: 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE,
COMPND 6 HYDROXYMETHYLGLUTARYL-COA REDUCTASE;
COMPND 7 EC: 1.1.1.34;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HMGCR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-CS
KEYWDS PROTEIN-INHIBITOR COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.ISTVAN,J.DEISENHOFER
REVDAT 4 09-AUG-23 1HWL 1 REMARK
REVDAT 3 27-OCT-21 1HWL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1HWL 1 VERSN
REVDAT 1 11-MAY-01 1HWL 0
JRNL AUTH E.S.ISTVAN,J.DEISENHOFER
JRNL TITL STRUCTURAL MECHANISM FOR STATIN INHIBITION OF HMG-COA
JRNL TITL 2 REDUCTASE.
JRNL REF SCIENCE V. 292 1160 2001
JRNL REFN ISSN 0036-8075
JRNL PMID 11349148
JRNL DOI 10.1126/SCIENCE.1059344
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2376841.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 101733
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) : 0.219
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15422
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 329
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11764
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 213
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.33000
REMARK 3 B22 (A**2) : -4.08000
REMARK 3 B33 (A**2) : 2.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 13.25000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.35
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.087
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.350
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.700 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.650 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 32.16
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; 250
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 5
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : ADP_PAR:ADP.PARAM
REMARK 3 PARAMETER FILE 5 : FBI_PAR:FBI.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : ADP_PAR:ADP.TOP
REMARK 3 TOPOLOGY FILE 5 : FBI_PAR:FBI.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NCS-RESTRAINTS WERE USED
REMARK 4
REMARK 4 1HWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-00; 02-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 130.0; 123.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; CHESS
REMARK 200 BEAMLINE : 5.0.1; F1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1; 0.942
REMARK 200 MONOCHROMATOR : NULL; HORIZONTALLY BENT SI (111)
REMARK 200 OPTICS : NULL; MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DQA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE, GLYCEROL,
REMARK 280 DTT, HEPES, MICROSEEDING, PH 7.5 AT 294 K, MICROSEEDING
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 86.25600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -183.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A 422
REMARK 465 ALA A 423
REMARK 465 MET A 424
REMARK 465 ALA A 425
REMARK 465 SER A 426
REMARK 465 SER A 427
REMARK 465 VAL A 428
REMARK 465 LEU A 429
REMARK 465 VAL A 430
REMARK 465 THR A 431
REMARK 465 GLN A 432
REMARK 465 GLU A 433
REMARK 465 PRO A 434
REMARK 465 GLU A 435
REMARK 465 ILE A 436
REMARK 465 GLU A 437
REMARK 465 LEU A 438
REMARK 465 PRO A 439
REMARK 465 ARG A 440
REMARK 465 GLU A 441
REMARK 465 LEU A 449
REMARK 465 GLN A 450
REMARK 465 ILE A 451
REMARK 465 LEU A 452
REMARK 465 GLY A 453
REMARK 465 ASN A 454
REMARK 465 ALA A 455
REMARK 465 GLU A 456
REMARK 465 LYS A 457
REMARK 465 GLY A 458
REMARK 465 ALA A 459
REMARK 465 LYS A 460
REMARK 465 HIS A 861
REMARK 465 LEU A 862
REMARK 465 VAL A 863
REMARK 465 LYS A 864
REMARK 465 SER A 865
REMARK 465 HIS A 866
REMARK 465 MET A 867
REMARK 465 ILE A 868
REMARK 465 HIS A 869
REMARK 465 ASN A 870
REMARK 465 ARG A 871
REMARK 465 SER A 872
REMARK 465 LYS A 873
REMARK 465 ILE A 874
REMARK 465 ASN A 875
REMARK 465 LEU A 876
REMARK 465 GLN A 877
REMARK 465 ASP A 878
REMARK 465 LEU A 879
REMARK 465 GLN A 880
REMARK 465 GLY A 881
REMARK 465 ALA A 882
REMARK 465 CYS A 883
REMARK 465 THR A 884
REMARK 465 LYS A 885
REMARK 465 LYS A 886
REMARK 465 THR A 887
REMARK 465 ALA A 888
REMARK 465 GLY B 422
REMARK 465 ALA B 423
REMARK 465 MET B 424
REMARK 465 ALA B 425
REMARK 465 SER B 426
REMARK 465 SER B 427
REMARK 465 VAL B 428
REMARK 465 LEU B 429
REMARK 465 VAL B 430
REMARK 465 THR B 431
REMARK 465 GLN B 432
REMARK 465 GLU B 433
REMARK 465 PRO B 434
REMARK 465 GLU B 435
REMARK 465 ILE B 436
REMARK 465 GLU B 437
REMARK 465 LEU B 438
REMARK 465 PRO B 439
REMARK 465 ARG B 440
REMARK 465 GLU B 441
REMARK 465 PRO B 442
REMARK 465 ARG B 443
REMARK 465 PRO B 444
REMARK 465 ASN B 445
REMARK 465 GLU B 446
REMARK 465 GLU B 447
REMARK 465 CYS B 448
REMARK 465 LEU B 449
REMARK 465 GLN B 450
REMARK 465 ILE B 451
REMARK 465 LEU B 452
REMARK 465 GLY B 453
REMARK 465 ASN B 454
REMARK 465 ALA B 455
REMARK 465 GLU B 456
REMARK 465 LYS B 457
REMARK 465 GLY B 458
REMARK 465 ALA B 459
REMARK 465 LYS B 460
REMARK 465 PHE B 461
REMARK 465 LEU B 462
REMARK 465 HIS B 861
REMARK 465 LEU B 862
REMARK 465 VAL B 863
REMARK 465 LYS B 864
REMARK 465 SER B 865
REMARK 465 HIS B 866
REMARK 465 MET B 867
REMARK 465 ILE B 868
REMARK 465 HIS B 869
REMARK 465 ASN B 870
REMARK 465 ARG B 871
REMARK 465 SER B 872
REMARK 465 LYS B 873
REMARK 465 ILE B 874
REMARK 465 ASN B 875
REMARK 465 LEU B 876
REMARK 465 GLN B 877
REMARK 465 ASP B 878
REMARK 465 LEU B 879
REMARK 465 GLN B 880
REMARK 465 GLY B 881
REMARK 465 ALA B 882
REMARK 465 CYS B 883
REMARK 465 THR B 884
REMARK 465 LYS B 885
REMARK 465 LYS B 886
REMARK 465 THR B 887
REMARK 465 ALA B 888
REMARK 465 GLY C 422
REMARK 465 ALA C 423
REMARK 465 MET C 424
REMARK 465 ALA C 425
REMARK 465 SER C 426
REMARK 465 SER C 427
REMARK 465 VAL C 428
REMARK 465 LEU C 429
REMARK 465 VAL C 430
REMARK 465 THR C 431
REMARK 465 GLN C 432
REMARK 465 GLU C 433
REMARK 465 PRO C 434
REMARK 465 GLU C 435
REMARK 465 ILE C 436
REMARK 465 GLU C 437
REMARK 465 LEU C 438
REMARK 465 PRO C 439
REMARK 465 ARG C 440
REMARK 465 GLU C 441
REMARK 465 PRO C 442
REMARK 465 ARG C 443
REMARK 465 PRO C 444
REMARK 465 ASN C 445
REMARK 465 GLU C 446
REMARK 465 GLU C 447
REMARK 465 CYS C 448
REMARK 465 LEU C 449
REMARK 465 GLN C 450
REMARK 465 ILE C 451
REMARK 465 LEU C 452
REMARK 465 GLY C 453
REMARK 465 ASN C 454
REMARK 465 ALA C 455
REMARK 465 GLU C 456
REMARK 465 LYS C 457
REMARK 465 GLY C 458
REMARK 465 ALA C 459
REMARK 465 LYS C 460
REMARK 465 PHE C 461
REMARK 465 LEU C 462
REMARK 465 HIS C 861
REMARK 465 LEU C 862
REMARK 465 VAL C 863
REMARK 465 LYS C 864
REMARK 465 SER C 865
REMARK 465 HIS C 866
REMARK 465 MET C 867
REMARK 465 ILE C 868
REMARK 465 HIS C 869
REMARK 465 ASN C 870
REMARK 465 ARG C 871
REMARK 465 SER C 872
REMARK 465 LYS C 873
REMARK 465 ILE C 874
REMARK 465 ASN C 875
REMARK 465 LEU C 876
REMARK 465 GLN C 877
REMARK 465 ASP C 878
REMARK 465 LEU C 879
REMARK 465 GLN C 880
REMARK 465 GLY C 881
REMARK 465 ALA C 882
REMARK 465 CYS C 883
REMARK 465 THR C 884
REMARK 465 LYS C 885
REMARK 465 LYS C 886
REMARK 465 THR C 887
REMARK 465 ALA C 888
REMARK 465 GLY D 422
REMARK 465 ALA D 423
REMARK 465 MET D 424
REMARK 465 ALA D 425
REMARK 465 SER D 426
REMARK 465 SER D 427
REMARK 465 VAL D 428
REMARK 465 LEU D 429
REMARK 465 VAL D 430
REMARK 465 THR D 431
REMARK 465 GLN D 432
REMARK 465 GLU D 433
REMARK 465 PRO D 434
REMARK 465 GLU D 435
REMARK 465 ILE D 436
REMARK 465 GLU D 437
REMARK 465 LEU D 438
REMARK 465 PRO D 439
REMARK 465 ARG D 440
REMARK 465 GLU D 441
REMARK 465 PRO D 442
REMARK 465 ARG D 443
REMARK 465 PRO D 444
REMARK 465 ASN D 445
REMARK 465 GLU D 446
REMARK 465 GLU D 447
REMARK 465 CYS D 448
REMARK 465 LEU D 449
REMARK 465 GLN D 450
REMARK 465 ILE D 451
REMARK 465 LEU D 452
REMARK 465 GLY D 453
REMARK 465 ASN D 454
REMARK 465 ALA D 455
REMARK 465 GLU D 456
REMARK 465 LYS D 457
REMARK 465 GLY D 458
REMARK 465 ALA D 459
REMARK 465 LYS D 460
REMARK 465 PHE D 461
REMARK 465 LEU D 462
REMARK 465 SER D 463
REMARK 465 ASP D 464
REMARK 465 ALA D 465
REMARK 465 GLU D 466
REMARK 465 ILE D 467
REMARK 465 ILE D 468
REMARK 465 GLN D 469
REMARK 465 LEU D 470
REMARK 465 VAL D 471
REMARK 465 ASN D 472
REMARK 465 ALA D 473
REMARK 465 LYS D 474
REMARK 465 HIS D 475
REMARK 465 ILE D 476
REMARK 465 PRO D 477
REMARK 465 ALA D 478
REMARK 465 HIS D 861
REMARK 465 LEU D 862
REMARK 465 VAL D 863
REMARK 465 LYS D 864
REMARK 465 SER D 865
REMARK 465 HIS D 866
REMARK 465 MET D 867
REMARK 465 ILE D 868
REMARK 465 HIS D 869
REMARK 465 ASN D 870
REMARK 465 ARG D 871
REMARK 465 SER D 872
REMARK 465 LYS D 873
REMARK 465 ILE D 874
REMARK 465 ASN D 875
REMARK 465 LEU D 876
REMARK 465 GLN D 877
REMARK 465 ASP D 878
REMARK 465 LEU D 879
REMARK 465 GLN D 880
REMARK 465 GLY D 881
REMARK 465 ALA D 882
REMARK 465 CYS D 883
REMARK 465 THR D 884
REMARK 465 LYS D 885
REMARK 465 LYS D 886
REMARK 465 THR D 887
REMARK 465 ALA D 888
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 LEU A 462 -145.18 -124.38
REMARK 500 THR A 483 46.22 -104.47
REMARK 500 LEU A 484 -6.44 -162.11
REMARK 500 GLU A 486 -72.81 -50.44
REMARK 500 TYR A 514 -20.83 -161.59
REMARK 500 ALA A 525 -44.97 -148.63
REMARK 500 CYS A 561 -8.84 79.17
REMARK 500 SER A 651 40.49 -153.25
REMARK 500 LYS A 735 -62.24 -105.15
REMARK 500 LEU A 737 -66.75 -105.16
REMARK 500 TYR A 749 54.47 -94.24
REMARK 500 HIS A 752 43.03 -157.69
REMARK 500 ASN B 472 23.45 -70.28
REMARK 500 ALA B 478 -39.76 -39.50
REMARK 500 THR B 483 37.15 -84.14
REMARK 500 LEU B 484 -57.38 -167.60
REMARK 500 GLU B 486 7.02 -65.50
REMARK 500 TYR B 514 -20.83 -162.10
REMARK 500 ALA B 525 -44.49 -149.17
REMARK 500 CYS B 561 -8.10 78.21
REMARK 500 ALA B 629 92.25 -69.55
REMARK 500 GLN B 632 -158.84 -91.83
REMARK 500 LYS B 633 151.39 -44.04
REMARK 500 SER B 651 41.38 -153.98
REMARK 500 LYS B 735 -61.65 -103.53
REMARK 500 LEU B 737 -66.54 -106.33
REMARK 500 TYR B 749 55.54 -94.31
REMARK 500 HIS B 752 43.18 -159.10
REMARK 500 SER B 799 57.90 -143.75
REMARK 500 ASN B 830 88.22 -150.56
REMARK 500 ASP C 464 -72.46 -39.89
REMARK 500 LEU C 484 -75.84 -70.09
REMARK 500 ILE C 485 -178.25 -60.99
REMARK 500 GLU C 486 -63.18 -103.20
REMARK 500 TYR C 514 -21.06 -161.93
REMARK 500 ALA C 525 -44.34 -149.10
REMARK 500 CYS C 561 -8.20 78.47
REMARK 500 GLN C 632 -70.07 -71.99
REMARK 500 SER C 651 40.44 -152.76
REMARK 500 LYS C 735 -63.88 -104.37
REMARK 500 LEU C 737 -65.46 -106.11
REMARK 500 TYR C 749 56.48 -93.06
REMARK 500 HIS C 752 41.58 -159.11
REMARK 500 SER C 799 59.39 -145.02
REMARK 500 LEU D 484 -73.63 -119.62
REMARK 500 GLU D 486 -71.50 -81.74
REMARK 500 GLU D 505 79.70 -155.14
REMARK 500 TYR D 514 -21.30 -162.81
REMARK 500 ALA D 525 -44.43 -149.71
REMARK 500 CYS D 561 -8.40 79.27
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBI B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBI A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBI D 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBI C 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQ8 RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX WITH HMG
REMARK 900 AND COA
REMARK 900 RELATED ID: 1DQ9 RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX WITH HMG-COA
REMARK 900 RELATED ID: 1DQA RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX WITH HMG,
REMARK 900 COA, AND NADP+
REMARK 900 RELATED ID: 1HW8 RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH COMPACTIN
REMARK 900 RELATED ID: 1HW9 RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH SIMVASTATIN
REMARK 900 RELATED ID: 1HWI RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH FLUVASTATIN
REMARK 900 RELATED ID: 1HWJ RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH CERIVASTATIN
REMARK 900 RELATED ID: 1HWK RELATED DB: PDB
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX WITH
REMARK 900 ATORVASTATIN
DBREF 1HWL A 426 888 UNP P04035 HMDH_HUMAN 426 888
DBREF 1HWL B 426 888 UNP P04035 HMDH_HUMAN 426 888
DBREF 1HWL C 426 888 UNP P04035 HMDH_HUMAN 426 888
DBREF 1HWL D 426 888 UNP P04035 HMDH_HUMAN 426 888
SEQADV 1HWL GLY A 422 UNP P04035 INSERTION
SEQADV 1HWL ALA A 423 UNP P04035 INSERTION
SEQADV 1HWL MET A 424 UNP P04035 INSERTION
SEQADV 1HWL ALA A 425 UNP P04035 INSERTION
SEQADV 1HWL ILE A 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1HWL GLY B 422 UNP P04035 INSERTION
SEQADV 1HWL ALA B 423 UNP P04035 INSERTION
SEQADV 1HWL MET B 424 UNP P04035 INSERTION
SEQADV 1HWL ALA B 425 UNP P04035 INSERTION
SEQADV 1HWL ILE B 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1HWL GLY C 422 UNP P04035 INSERTION
SEQADV 1HWL ALA C 423 UNP P04035 INSERTION
SEQADV 1HWL MET C 424 UNP P04035 INSERTION
SEQADV 1HWL ALA C 425 UNP P04035 INSERTION
SEQADV 1HWL ILE C 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1HWL GLY D 422 UNP P04035 INSERTION
SEQADV 1HWL ALA D 423 UNP P04035 INSERTION
SEQADV 1HWL MET D 424 UNP P04035 INSERTION
SEQADV 1HWL ALA D 425 UNP P04035 INSERTION
SEQADV 1HWL ILE D 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQRES 1 A 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 A 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 A 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 A 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 A 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 A 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 A 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 A 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 A 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 A 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 A 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 A 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 A 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 A 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 A 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 A 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 A 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 A 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 A 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 A 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 A 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 A 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 A 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 A 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 A 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 A 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 A 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 A 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 A 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 A 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 A 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 A 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 A 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 A 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 A 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 A 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 B 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 B 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 B 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 B 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 B 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 B 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 B 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 B 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 B 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 B 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 B 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 B 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 B 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 B 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 B 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 B 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 B 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 B 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 B 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 B 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 B 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 B 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 B 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 B 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 B 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 B 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 B 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 B 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 B 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 B 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 B 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 B 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 B 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 B 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 B 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 B 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 C 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 C 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 C 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 C 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 C 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 C 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 C 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 C 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 C 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 C 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 C 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 C 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 C 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 C 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 C 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 C 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 C 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 C 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 C 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 C 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 C 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 C 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 C 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 C 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 C 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 C 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 C 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 C 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 C 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 C 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 C 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 C 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 C 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 C 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 C 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 C 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 D 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 D 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 D 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 D 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 D 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 D 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 D 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 D 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 D 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 D 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 D 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 D 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 D 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 D 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 D 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 D 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 D 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 D 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 D 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 D 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 D 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 D 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 D 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 D 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 D 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 D 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 D 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 D 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 D 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 D 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 D 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 D 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 D 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 D 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 D 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 D 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
HET ADP A 101 27
HET ADP A 102 27
HET FBI A 2 33
HET FBI B 1 33
HET ADP C 103 27
HET FBI C 4 33
HET FBI D 3 33
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM FBI 7-[4-(4-FLUORO-PHENYL)-6-ISOPROPYL-2-(METHANESULFONYL-
HETNAM 2 FBI METHYL-AMINO)-PYRIMIDIN-5-YL] -3,5-DIHYDROXY-HEPTANOIC
HETNAM 3 FBI ACID
HETSYN FBI ROSUVASTATIN
FORMUL 5 ADP 3(C10 H15 N5 O10 P2)
FORMUL 7 FBI 4(C22 H30 F N3 O6 S)
FORMUL 12 HOH *182(H2 O)
HELIX 1 1 SER A 463 LYS A 474 1 12
HELIX 2 2 PRO A 477 LEU A 484 5 8
HELIX 3 3 THR A 487 LYS A 501 1 15
HELIX 4 4 SER A 507 LEU A 512 5 6
HELIX 5 5 ASN A 518 MET A 523 1 6
HELIX 6 6 CYS A 561 GLY A 576 1 16
HELIX 7 7 ARG A 598 GLU A 610 1 13
HELIX 8 8 THR A 611 SER A 624 1 14
HELIX 9 9 GLY A 656 PHE A 675 1 20
HELIX 10 10 ALA A 694 GLY A 701 1 8
HELIX 11 11 PRO A 713 VAL A 720 1 8
HELIX 12 12 THR A 724 LEU A 737 1 14
HELIX 13 13 LEU A 737 ALA A 743 1 7
HELIX 14 14 HIS A 752 CYS A 764 1 13
HELIX 15 15 ASP A 767 ALA A 769 5 3
HELIX 16 16 GLN A 770 SER A 775 1 6
HELIX 17 17 GLY A 806 ASN A 810 5 5
HELIX 18 18 LEU A 811 LEU A 821 1 11
HELIX 19 19 GLY A 832 GLY A 860 1 29
HELIX 20 20 SER B 463 ASN B 472 1 10
HELIX 21 21 PRO B 477 LEU B 481 5 5
HELIX 22 22 THR B 487 LYS B 501 1 15
HELIX 23 23 SER B 507 LEU B 512 5 6
HELIX 24 24 ASN B 518 MET B 523 1 6
HELIX 25 25 CYS B 561 LEU B 575 1 15
HELIX 26 26 ARG B 598 GLU B 610 1 13
HELIX 27 27 THR B 611 SER B 624 1 14
HELIX 28 28 GLY B 656 PHE B 675 1 20
HELIX 29 29 ALA B 694 GLY B 701 1 8
HELIX 30 30 PRO B 713 VAL B 720 1 8
HELIX 31 31 THR B 724 LEU B 737 1 14
HELIX 32 32 LEU B 737 ALA B 743 1 7
HELIX 33 33 HIS B 752 CYS B 764 1 13
HELIX 34 34 ASP B 767 ALA B 769 5 3
HELIX 35 35 GLN B 770 SER B 775 1 6
HELIX 36 36 GLY B 806 ASN B 810 5 5
HELIX 37 37 LEU B 811 LEU B 821 1 11
HELIX 38 38 GLY B 832 GLY B 860 1 29
HELIX 39 39 SER C 463 HIS C 475 1 13
HELIX 40 40 PRO C 477 TYR C 479 5 3
HELIX 41 41 LYS C 480 ILE C 485 1 6
HELIX 42 42 THR C 487 LYS C 501 1 15
HELIX 43 43 SER C 507 LEU C 512 5 6
HELIX 44 44 ASN C 518 MET C 523 1 6
HELIX 45 45 CYS C 561 LEU C 575 1 15
HELIX 46 46 ARG C 598 GLU C 610 1 13
HELIX 47 47 THR C 611 SER C 624 1 14
HELIX 48 48 GLY C 656 PHE C 675 1 20
HELIX 49 49 ALA C 694 GLY C 701 1 8
HELIX 50 50 PRO C 713 VAL C 720 1 8
HELIX 51 51 THR C 724 LEU C 737 1 14
HELIX 52 52 LEU C 737 ALA C 743 1 7
HELIX 53 53 HIS C 752 CYS C 764 1 13
HELIX 54 54 ASP C 767 ALA C 769 5 3
HELIX 55 55 GLN C 770 SER C 775 1 6
HELIX 56 56 GLY C 806 ASN C 810 5 5
HELIX 57 57 LEU C 811 LEU C 821 1 11
HELIX 58 58 GLY C 832 GLY C 860 1 29
HELIX 59 59 LYS D 480 LEU D 484 5 5
HELIX 60 60 THR D 487 LEU D 503 1 17
HELIX 61 61 GLU D 505 LEU D 512 5 8
HELIX 62 62 ASN D 518 MET D 523 1 6
HELIX 63 63 CYS D 561 LEU D 575 1 15
HELIX 64 64 ARG D 598 GLU D 610 1 13
HELIX 65 65 THR D 611 SER D 624 1 14
HELIX 66 66 GLY D 656 PHE D 675 1 20
HELIX 67 67 ALA D 694 GLY D 701 1 8
HELIX 68 68 PRO D 713 VAL D 720 1 8
HELIX 69 69 THR D 724 LEU D 737 1 14
HELIX 70 70 LEU D 737 ALA D 743 1 7
HELIX 71 71 HIS D 752 CYS D 764 1 13
HELIX 72 72 ASP D 767 ALA D 769 5 3
HELIX 73 73 GLN D 770 SER D 775 1 6
HELIX 74 74 GLY D 806 ASN D 810 5 5
HELIX 75 75 LEU D 811 LEU D 821 1 11
HELIX 76 76 GLY D 832 GLY D 860 1 29
SHEET 1 A 4 LYS A 549 ALA A 556 0
SHEET 2 A 4 VAL A 530 LEU A 546 -1 N GLY A 539 O MET A 555
SHEET 3 A 4 VAL B 530 LEU B 546 -1 N ILE B 531 O VAL A 538
SHEET 4 A 4 LYS B 549 ALA B 556 -1 O LYS B 549 N LEU B 546
SHEET 1 B 8 GLY A 748 TYR A 749 0
SHEET 2 B 8 CYS A 777 SER A 784 1 O CYS A 777 N TYR A 749
SHEET 3 B 8 ASP A 790 ILE A 800 -1 O ASP A 790 N SER A 784
SHEET 4 B 8 GLY A 703 ILE A 712 -1 N LYS A 704 O ILE A 800
SHEET 5 B 8 SER A 580 ARG A 590 -1 N SER A 580 O GLU A 709
SHEET 6 B 8 ASN A 642 ARG A 650 -1 N PHE A 647 O ARG A 590
SHEET 7 B 8 VAL A 593 ARG A 595 -1 O VAL A 594 N LEU A 643
SHEET 8 B 8 GLN A 679 ALA A 682 -1 N GLN A 679 O ARG A 595
SHEET 1 C 7 GLY A 748 TYR A 749 0
SHEET 2 C 7 CYS A 777 SER A 784 1 O CYS A 777 N TYR A 749
SHEET 3 C 7 ASP A 790 ILE A 800 -1 O ASP A 790 N SER A 784
SHEET 4 C 7 GLY A 703 ILE A 712 -1 N LYS A 704 O ILE A 800
SHEET 5 C 7 SER A 580 ARG A 590 -1 N SER A 580 O GLU A 709
SHEET 6 C 7 ASN A 642 ARG A 650 -1 N PHE A 647 O ARG A 590
SHEET 7 C 7 ARG A 630 ALA A 639 -1 O ARG A 630 N ARG A 650
SHEET 1 D 8 GLY B 748 TYR B 749 0
SHEET 2 D 8 CYS B 777 SER B 784 1 O CYS B 777 N TYR B 749
SHEET 3 D 8 ASP B 790 ILE B 800 -1 N ASP B 790 O SER B 784
SHEET 4 D 8 GLY B 703 ILE B 712 -1 N LYS B 704 O ILE B 800
SHEET 5 D 8 SER B 580 ARG B 590 -1 N SER B 580 O GLU B 709
SHEET 6 D 8 ASN B 642 ARG B 650 -1 N PHE B 647 O ARG B 590
SHEET 7 D 8 VAL B 593 ARG B 595 -1 O VAL B 594 N LEU B 643
SHEET 8 D 8 GLN B 679 ALA B 682 -1 N GLN B 679 O ARG B 595
SHEET 1 E 7 GLY B 748 TYR B 749 0
SHEET 2 E 7 CYS B 777 SER B 784 1 O CYS B 777 N TYR B 749
SHEET 3 E 7 ASP B 790 ILE B 800 -1 N ASP B 790 O SER B 784
SHEET 4 E 7 GLY B 703 ILE B 712 -1 N LYS B 704 O ILE B 800
SHEET 5 E 7 SER B 580 ARG B 590 -1 N SER B 580 O GLU B 709
SHEET 6 E 7 ASN B 642 ARG B 650 -1 N PHE B 647 O ARG B 590
SHEET 7 E 7 ARG B 630 ALA B 639 -1 O ARG B 630 N ARG B 650
SHEET 1 F 4 LYS C 549 ALA C 556 0
SHEET 2 F 4 VAL C 530 LEU C 546 -1 N GLY C 539 O MET C 555
SHEET 3 F 4 VAL D 530 LEU D 546 -1 N ILE D 531 O VAL C 538
SHEET 4 F 4 LYS D 549 ALA D 556 -1 O LYS D 549 N LEU D 546
SHEET 1 G 8 GLY C 748 TYR C 749 0
SHEET 2 G 8 CYS C 777 SER C 784 1 O CYS C 777 N TYR C 749
SHEET 3 G 8 ASP C 790 ILE C 800 -1 O ASP C 790 N SER C 784
SHEET 4 G 8 GLY C 703 ILE C 712 -1 N LYS C 704 O ILE C 800
SHEET 5 G 8 SER C 580 ARG C 590 -1 N SER C 580 O GLU C 709
SHEET 6 G 8 ASN C 642 ARG C 650 -1 N PHE C 647 O ARG C 590
SHEET 7 G 8 VAL C 593 ARG C 595 -1 O VAL C 594 N LEU C 643
SHEET 8 G 8 GLN C 679 ALA C 682 -1 N GLN C 679 O ARG C 595
SHEET 1 H 7 GLY C 748 TYR C 749 0
SHEET 2 H 7 CYS C 777 SER C 784 1 O CYS C 777 N TYR C 749
SHEET 3 H 7 ASP C 790 ILE C 800 -1 O ASP C 790 N SER C 784
SHEET 4 H 7 GLY C 703 ILE C 712 -1 N LYS C 704 O ILE C 800
SHEET 5 H 7 SER C 580 ARG C 590 -1 N SER C 580 O GLU C 709
SHEET 6 H 7 ASN C 642 ARG C 650 -1 N PHE C 647 O ARG C 590
SHEET 7 H 7 ARG C 630 ALA C 639 -1 O ARG C 630 N ARG C 650
SHEET 1 I 8 GLY D 748 TYR D 749 0
SHEET 2 I 8 CYS D 777 SER D 784 1 O CYS D 777 N TYR D 749
SHEET 3 I 8 ASP D 790 ILE D 800 -1 O ASP D 790 N SER D 784
SHEET 4 I 8 GLY D 703 ILE D 712 -1 N LYS D 704 O ILE D 800
SHEET 5 I 8 SER D 580 ARG D 590 -1 N SER D 580 O GLU D 709
SHEET 6 I 8 ASN D 642 ARG D 650 -1 N PHE D 647 O ARG D 590
SHEET 7 I 8 VAL D 593 ARG D 595 -1 O VAL D 594 N LEU D 643
SHEET 8 I 8 GLN D 679 ALA D 682 -1 N GLN D 679 O ARG D 595
SHEET 1 J 7 GLY D 748 TYR D 749 0
SHEET 2 J 7 CYS D 777 SER D 784 1 O CYS D 777 N TYR D 749
SHEET 3 J 7 ASP D 790 ILE D 800 -1 O ASP D 790 N SER D 784
SHEET 4 J 7 GLY D 703 ILE D 712 -1 N LYS D 704 O ILE D 800
SHEET 5 J 7 SER D 580 ARG D 590 -1 N SER D 580 O GLU D 709
SHEET 6 J 7 ASN D 642 ARG D 650 -1 N PHE D 647 O ARG D 590
SHEET 7 J 7 ARG D 630 ALA D 639 -1 O ARG D 630 N ARG D 650
CISPEP 1 GLY A 542 PRO A 543 0 0.74
CISPEP 2 CYS A 688 THR A 689 0 -1.35
CISPEP 3 GLY B 542 PRO B 543 0 1.09
CISPEP 4 CYS B 688 THR B 689 0 -0.79
CISPEP 5 GLY C 542 PRO C 543 0 1.11
CISPEP 6 CYS C 688 THR C 689 0 -1.04
CISPEP 7 GLY D 542 PRO D 543 0 0.73
CISPEP 8 CYS D 688 THR D 689 0 -0.75
SITE 1 AC1 6 TYR A 479 GLU A 528 ASN A 529 ALA B 564
SITE 2 AC1 6 ASN B 567 ARG B 568
SITE 1 AC2 7 ALA A 564 ASN A 567 ARG A 568 LYS A 722
SITE 2 AC2 7 TYR B 479 GLU B 528 ASN B 529
SITE 1 AC3 8 TYR C 479 GLU C 528 ASN C 529 HOH C1143
SITE 2 AC3 8 ALA D 564 ASN D 567 ARG D 568 LYS D 722
SITE 1 AC4 18 GLU A 559 GLY A 560 CYS A 561 LEU A 562
SITE 2 AC4 18 SER A 565 LYS A 735 ALA A 751 HIS A 752
SITE 3 AC4 18 ASN A 755 LEU A 853 ALA A 856 ARG B 590
SITE 4 AC4 18 VAL B 683 SER B 684 ASP B 690 LYS B 691
SITE 5 AC4 18 LYS B 692 HOH B1080
SITE 1 AC5 17 ARG A 590 VAL A 683 SER A 684 ASP A 690
SITE 2 AC5 17 LYS A 691 LYS A 692 HOH A1068 GLU B 559
SITE 3 AC5 17 GLY B 560 CYS B 561 LEU B 562 SER B 565
SITE 4 AC5 17 LYS B 735 ALA B 751 ASN B 755 LEU B 853
SITE 5 AC5 17 ALA B 856
SITE 1 AC6 18 GLU C 559 GLY C 560 CYS C 561 LEU C 562
SITE 2 AC6 18 SER C 565 LYS C 735 ALA C 751 ASN C 755
SITE 3 AC6 18 LEU C 853 ALA C 856 ARG D 590 VAL D 683
SITE 4 AC6 18 SER D 684 ASN D 686 ASP D 690 LYS D 691
SITE 5 AC6 18 LYS D 692 HOH D1059
SITE 1 AC7 17 ARG C 590 VAL C 683 SER C 684 ASP C 690
SITE 2 AC7 17 LYS C 691 LYS C 692 HOH C1173 GLU D 559
SITE 3 AC7 17 GLY D 560 CYS D 561 LEU D 562 SER D 565
SITE 4 AC7 17 LYS D 735 ALA D 751 ASN D 755 LEU D 853
SITE 5 AC7 17 ALA D 856
CRYST1 74.432 172.512 79.987 90.00 117.36 90.00 P 1 21 1 8
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 0.013435 0.000000 0.006953 0.00000
SCALE2 0.000000 0.005797 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END