HEADER OXIDOREDUCTASE 24-MAY-07 2Q1L
TITLE DESIGN AND SYNTHESIS OF PYRROLE-BASED, HEPATOSELECTIVE HMG-COA
TITLE 2 REDUCTASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 441-875);
COMPND 5 SYNONYM: HMG-COA REDUCTASE;
COMPND 6 EC: 1.1.1.34;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: BL21 STAR
KEYWDS OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH, STATIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAVLOVSKY,J.A.PFEFFERKORN,M.S.HARRIS,B.C.FINZEL
REVDAT 7 21-FEB-24 2Q1L 1 REMARK
REVDAT 6 20-OCT-21 2Q1L 1 REMARK SEQADV
REVDAT 5 18-OCT-17 2Q1L 1 REMARK
REVDAT 4 29-FEB-12 2Q1L 1
REVDAT 3 15-FEB-12 2Q1L 1 AUTHOR VERSN
REVDAT 2 24-FEB-09 2Q1L 1 VERSN
REVDAT 1 17-JUL-07 2Q1L 0
JRNL AUTH J.A.PFEFFERKORN,Y.SONG,K.L.SUN,S.R.MILLER,B.K.TRIVEDI,
JRNL AUTH 2 C.CHOI,R.J.SORENSON,L.D.BRATTON,P.C.UNANGST,S.D.LARSEN,
JRNL AUTH 3 T.J.POEL,X.M.CHENG,C.LEE,N.ERASGA,B.AUERBACH,V.ASKEW,
JRNL AUTH 4 L.DILLON,J.C.HANSELMAN,Z.LIN,G.LU,A.ROBERTSON,K.OLSEN,
JRNL AUTH 5 T.MERTZ,C.SEKERKE,A.PAVLOVSKY,M.S.HARRIS,G.BAINBRIDGE,
JRNL AUTH 6 N.CASPERS,H.CHEN,M.EBERSTADT
JRNL TITL DESIGN AND SYNTHESIS OF HEPATOSELECTIVE, PYRROLE-BASED
JRNL TITL 2 HMG-COA REDUCTASE INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 4538 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17574412
JRNL DOI 10.1016/J.BMCL.2007.05.096
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.7
REMARK 3 NUMBER OF REFLECTIONS : 77536
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 + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4291
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4418
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 223
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11889
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 485
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.40000
REMARK 3 B22 (A**2) : 1.18000
REMARK 3 B33 (A**2) : -0.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.85000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.313
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.250
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12238 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 11341 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16545 ; 1.177 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26395 ; 0.749 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1595 ; 5.426 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1900 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13685 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2295 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2607 ; 0.178 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 13390 ; 0.215 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 7248 ; 0.079 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 496 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.129 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.185 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.026 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7919 ; 0.432 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12650 ; 0.818 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4319 ; 1.049 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3895 ; 1.857 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2Q1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000043034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79035
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28300
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 88.47900
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 300 REMARK: THIS ENTRY CONTAINS A BIOLOGICAL UNIT OF FOUR POLYPEPTIDE
REMARK 300 CHAINS (A,B,C,D)
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: 27870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 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 HIS A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
REMARK 465 HIS A 440
REMARK 465 GLU A 441
REMARK 465 PRO A 442
REMARK 465 ARG A 443
REMARK 465 PRO A 444
REMARK 465 ASN A 445
REMARK 465 GLU A 446
REMARK 465 GLU A 447
REMARK 465 CYS A 448
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 LYS A 474
REMARK 465 HIS A 475
REMARK 465 ILE A 476
REMARK 465 PRO A 477
REMARK 465 ALA A 478
REMARK 465 TYR A 479
REMARK 465 LYS A 480
REMARK 465 LEU A 481
REMARK 465 GLU A 482
REMARK 465 THR A 483
REMARK 465 LEU A 484
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 HIS B 435
REMARK 465 HIS B 436
REMARK 465 HIS B 437
REMARK 465 HIS B 438
REMARK 465 HIS B 439
REMARK 465 HIS 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 GLU B 486
REMARK 465 THR B 487
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 HIS C 435
REMARK 465 HIS C 436
REMARK 465 HIS C 437
REMARK 465 HIS C 438
REMARK 465 HIS C 439
REMARK 465 HIS C 440
REMARK 465 GLU C 441
REMARK 465 PRO C 442
REMARK 465 ARG C 443
REMARK 465 LYS C 457
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 HIS D 435
REMARK 465 HIS D 436
REMARK 465 HIS D 437
REMARK 465 HIS D 438
REMARK 465 HIS D 439
REMARK 465 HIS 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 ILE D 476
REMARK 465 PRO D 477
REMARK 465 ALA D 478
REMARK 465 TYR D 479
REMARK 465 LYS D 480
REMARK 465 LEU D 481
REMARK 465 GLU D 482
REMARK 465 THR D 483
REMARK 465 GLY D 860
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 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 OD1 ASN A 771 OG SER A 775 2.10
REMARK 500 OD1 ASN C 771 OG SER C 775 2.17
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 TYR A 514 -23.86 -144.92
REMARK 500 ALA A 525 -48.57 -158.24
REMARK 500 CYS A 561 -5.84 72.27
REMARK 500 SER A 651 42.91 -155.38
REMARK 500 LEU A 737 -60.41 -106.65
REMARK 500 TYR A 749 54.78 -94.87
REMARK 500 HIS A 752 41.66 -156.96
REMARK 500 SER A 799 52.39 -141.69
REMARK 500 ASN A 830 81.62 -155.72
REMARK 500 ALA B 478 -77.10 -64.63
REMARK 500 LYS B 480 41.80 -100.64
REMARK 500 TYR B 514 -34.82 -159.38
REMARK 500 ALA B 525 -51.10 -162.28
REMARK 500 CYS B 561 -3.64 71.41
REMARK 500 SER B 651 32.23 -147.10
REMARK 500 LEU B 737 -64.08 -102.18
REMARK 500 TYR B 749 57.35 -96.62
REMARK 500 HIS B 752 43.44 -157.10
REMARK 500 SER B 799 51.75 -142.52
REMARK 500 ASN B 830 79.31 -150.58
REMARK 500 ASN C 445 -53.59 173.44
REMARK 500 LYS C 474 43.49 -88.22
REMARK 500 TYR C 514 -29.16 -149.39
REMARK 500 ALA C 525 -44.41 -145.45
REMARK 500 CYS C 561 -11.60 82.99
REMARK 500 ARG C 630 82.61 -162.10
REMARK 500 SER C 651 42.67 -155.64
REMARK 500 LYS C 735 -62.88 -94.61
REMARK 500 LEU C 737 -62.37 -102.56
REMARK 500 TYR C 749 54.97 -94.73
REMARK 500 HIS C 752 48.85 -152.42
REMARK 500 ALA C 859 -70.32 -75.77
REMARK 500 TYR D 514 -27.70 -158.62
REMARK 500 ALA D 525 -54.09 -146.62
REMARK 500 CYS D 561 -15.33 86.36
REMARK 500 SER D 651 44.02 -151.60
REMARK 500 LYS D 735 -67.71 -95.19
REMARK 500 LEU D 737 -63.73 -103.41
REMARK 500 TYR D 749 56.63 -92.54
REMARK 500 HIS D 752 42.92 -163.35
REMARK 500 SER D 799 51.58 -143.75
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 882 A 876
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 882 A 877
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 882 D 876
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 882 C 876
DBREF 2Q1L A 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 2Q1L B 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 2Q1L C 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 2Q1L D 441 875 UNP P04035 HMDH_HUMAN 441 875
SEQADV 2Q1L HIS A 435 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS A 436 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS A 437 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS A 438 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS A 439 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS A 440 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L ILE A 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 2Q1L HIS B 435 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS B 436 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS B 437 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS B 438 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS B 439 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS B 440 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L ILE B 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 2Q1L HIS C 435 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS C 436 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS C 437 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS C 438 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS C 439 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS C 440 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L ILE C 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 2Q1L HIS D 435 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS D 436 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS D 437 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS D 438 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS D 439 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L HIS D 440 UNP P04035 EXPRESSION TAG
SEQADV 2Q1L ILE D 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQRES 1 A 441 HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU
SEQRES 2 A 441 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 3 A 441 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 4 A 441 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 5 A 441 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 6 A 441 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 7 A 441 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 8 A 441 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 9 A 441 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 10 A 441 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 11 A 441 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 12 A 441 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 13 A 441 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 14 A 441 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 15 A 441 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 16 A 441 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 17 A 441 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 18 A 441 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 19 A 441 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 20 A 441 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 21 A 441 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 22 A 441 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 23 A 441 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 24 A 441 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 25 A 441 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 26 A 441 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 27 A 441 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 28 A 441 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 29 A 441 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 30 A 441 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 31 A 441 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 32 A 441 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 33 A 441 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 34 A 441 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN
SEQRES 1 B 441 HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU
SEQRES 2 B 441 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 3 B 441 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 4 B 441 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 5 B 441 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 6 B 441 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 7 B 441 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 8 B 441 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 9 B 441 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 10 B 441 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 11 B 441 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 12 B 441 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 13 B 441 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 14 B 441 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 15 B 441 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 16 B 441 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 17 B 441 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 18 B 441 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 19 B 441 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 20 B 441 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 21 B 441 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 22 B 441 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 23 B 441 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 24 B 441 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 25 B 441 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 26 B 441 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 27 B 441 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 28 B 441 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 29 B 441 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 30 B 441 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 31 B 441 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 32 B 441 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 33 B 441 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 34 B 441 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN
SEQRES 1 C 441 HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU
SEQRES 2 C 441 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 3 C 441 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 4 C 441 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 5 C 441 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 6 C 441 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 7 C 441 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 8 C 441 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 9 C 441 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 10 C 441 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 11 C 441 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 12 C 441 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 13 C 441 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 14 C 441 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 15 C 441 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 16 C 441 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 17 C 441 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 18 C 441 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 19 C 441 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 20 C 441 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 21 C 441 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 22 C 441 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 23 C 441 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 24 C 441 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 25 C 441 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 26 C 441 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 27 C 441 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 28 C 441 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 29 C 441 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 30 C 441 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 31 C 441 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 32 C 441 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 33 C 441 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 34 C 441 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN
SEQRES 1 D 441 HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU
SEQRES 2 D 441 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 3 D 441 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 4 D 441 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 5 D 441 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 6 D 441 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 7 D 441 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 8 D 441 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 9 D 441 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 10 D 441 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 11 D 441 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 12 D 441 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 13 D 441 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 14 D 441 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 15 D 441 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 16 D 441 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 17 D 441 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 18 D 441 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 19 D 441 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 20 D 441 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 21 D 441 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 22 D 441 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 23 D 441 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 24 D 441 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 25 D 441 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 26 D 441 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 27 D 441 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 28 D 441 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 29 D 441 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 30 D 441 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 31 D 441 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 32 D 441 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 33 D 441 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 34 D 441 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN
HET 882 A 876 42
HET 882 A 877 42
HET 882 C 876 42
HET 882 D 876 42
HETNAM 882 (3R,5R)-7-[5-(ANILINOCARBONYL)-3,4-BIS(4-FLUOROPHENYL)-
HETNAM 2 882 1-ISOPROPYL-1H-PYRROL-2-YL]-3,5-DIHYDROXYHEPTANOIC
HETNAM 3 882 ACID
FORMUL 5 882 4(C33 H34 F2 N2 O5)
FORMUL 9 HOH *485(H2 O)
HELIX 1 1 SER A 463 ALA A 473 1 11
HELIX 2 2 THR A 487 LEU A 503 1 17
HELIX 3 3 SER A 507 LEU A 512 5 6
HELIX 4 4 ASN A 518 VAL A 522 5 5
HELIX 5 5 CYS A 561 GLY A 576 1 16
HELIX 6 6 ARG A 598 THR A 611 1 14
HELIX 7 7 THR A 611 SER A 624 1 14
HELIX 8 8 GLY A 656 PHE A 675 1 20
HELIX 9 9 ALA A 694 GLY A 701 1 8
HELIX 10 10 PRO A 713 VAL A 720 1 8
HELIX 11 11 THR A 724 LEU A 737 1 14
HELIX 12 12 LEU A 737 ALA A 743 1 7
HELIX 13 13 HIS A 752 CYS A 764 1 13
HELIX 14 14 ASP A 767 ALA A 769 5 3
HELIX 15 15 GLN A 770 SER A 775 1 6
HELIX 16 16 GLY A 806 ASN A 810 5 5
HELIX 17 17 LEU A 811 LEU A 821 1 11
HELIX 18 18 GLY A 832 GLY A 860 1 29
HELIX 19 19 SER B 463 ALA B 473 1 11
HELIX 20 20 HIS B 488 LYS B 501 1 14
HELIX 21 21 CYS B 561 GLY B 576 1 16
HELIX 22 22 ARG B 598 THR B 611 1 14
HELIX 23 23 THR B 611 SER B 624 1 14
HELIX 24 24 GLY B 656 PHE B 675 1 20
HELIX 25 25 ALA B 694 GLY B 701 1 8
HELIX 26 26 PRO B 713 VAL B 720 1 8
HELIX 27 27 THR B 724 LEU B 737 1 14
HELIX 28 28 LEU B 737 ALA B 743 1 7
HELIX 29 29 HIS B 752 CYS B 764 1 13
HELIX 30 30 ASP B 767 ALA B 769 5 3
HELIX 31 31 GLN B 770 SER B 775 1 6
HELIX 32 32 GLY B 806 ASN B 810 5 5
HELIX 33 33 LEU B 811 LEU B 821 1 11
HELIX 34 34 GLY B 832 GLY B 860 1 29
HELIX 35 35 ASN C 445 ASN C 454 1 10
HELIX 36 36 GLY C 458 LEU C 462 5 5
HELIX 37 37 SER C 463 ALA C 473 1 11
HELIX 38 38 PRO C 477 TYR C 479 5 3
HELIX 39 39 LYS C 480 ILE C 485 1 6
HELIX 40 40 THR C 487 LYS C 502 1 16
HELIX 41 41 ASN C 518 VAL C 522 5 5
HELIX 42 42 CYS C 561 GLY C 576 1 16
HELIX 43 43 ARG C 598 THR C 611 1 14
HELIX 44 44 THR C 611 SER C 624 1 14
HELIX 45 45 GLY C 656 PHE C 675 1 20
HELIX 46 46 ALA C 694 GLY C 701 1 8
HELIX 47 47 PRO C 713 VAL C 720 1 8
HELIX 48 48 THR C 724 LEU C 737 1 14
HELIX 49 49 LEU C 737 ALA C 743 1 7
HELIX 50 50 HIS C 752 CYS C 764 1 13
HELIX 51 51 ASP C 767 ALA C 769 5 3
HELIX 52 52 GLN C 770 SER C 775 1 6
HELIX 53 53 GLY C 806 ASN C 810 5 5
HELIX 54 54 LEU C 811 LEU C 821 1 11
HELIX 55 55 GLY C 832 GLY C 860 1 29
HELIX 56 56 GLY D 458 LEU D 462 5 5
HELIX 57 57 SER D 463 ALA D 473 1 11
HELIX 58 58 THR D 487 LYS D 501 1 15
HELIX 59 59 ASN D 518 VAL D 522 5 5
HELIX 60 60 CYS D 561 GLY D 576 1 16
HELIX 61 61 ARG D 598 THR D 611 1 14
HELIX 62 62 THR D 611 SER D 624 1 14
HELIX 63 63 GLY D 656 PHE D 675 1 20
HELIX 64 64 ALA D 694 GLY D 701 1 8
HELIX 65 65 PRO D 713 VAL D 720 1 8
HELIX 66 66 THR D 724 LEU D 737 1 14
HELIX 67 67 LEU D 737 ALA D 743 1 7
HELIX 68 68 HIS D 752 CYS D 764 1 13
HELIX 69 69 ASP D 767 ALA D 769 5 3
HELIX 70 70 GLN D 770 SER D 775 1 6
HELIX 71 71 GLY D 806 ASN D 810 5 5
HELIX 72 72 LEU D 811 LEU D 821 1 11
HELIX 73 73 GLY D 832 ALA D 859 1 28
SHEET 1 A 4 LYS A 549 ALA A 556 0
SHEET 2 A 4 VAL A 530 LEU A 546 -1 N LEU A 546 O LYS A 549
SHEET 3 A 4 VAL B 530 LEU B 546 -1 O VAL B 538 N ILE A 531
SHEET 4 A 4 LYS B 549 ALA B 556 -1 O PHE B 551 N LEU B 544
SHEET 1 B 4 HIS A 635 ALA A 639 0
SHEET 2 B 4 ASN A 642 SER A 649 -1 O TYR A 644 N SER A 637
SHEET 3 B 4 VAL A 593 ARG A 595 -1 N VAL A 594 O LEU A 643
SHEET 4 B 4 GLN A 679 ALA A 682 -1 O GLN A 679 N ARG A 595
SHEET 1 C 7 HIS A 635 ALA A 639 0
SHEET 2 C 7 ASN A 642 SER A 649 -1 O TYR A 644 N SER A 637
SHEET 3 C 7 SER A 580 ARG A 590 -1 N ARG A 590 O PHE A 647
SHEET 4 C 7 GLY A 703 ILE A 712 -1 O SER A 705 N LEU A 584
SHEET 5 C 7 ASP A 790 ILE A 800 -1 O MET A 797 N VAL A 706
SHEET 6 C 7 CYS A 777 SER A 784 -1 N GLU A 782 O TYR A 792
SHEET 7 C 7 GLY A 748 TYR A 749 1 N TYR A 749 O THR A 779
SHEET 1 D 4 HIS B 635 ALA B 639 0
SHEET 2 D 4 ASN B 642 SER B 649 -1 O ARG B 646 N HIS B 635
SHEET 3 D 4 VAL B 593 ARG B 595 -1 N VAL B 594 O LEU B 643
SHEET 4 D 4 GLN B 679 ALA B 682 -1 O GLN B 679 N ARG B 595
SHEET 1 E 7 HIS B 635 ALA B 639 0
SHEET 2 E 7 ASN B 642 SER B 649 -1 O ARG B 646 N HIS B 635
SHEET 3 E 7 SER B 580 ARG B 590 -1 N ARG B 590 O PHE B 647
SHEET 4 E 7 GLY B 703 ILE B 712 -1 O SER B 705 N LEU B 584
SHEET 5 E 7 ASP B 790 ILE B 800 -1 O ILE B 800 N LYS B 704
SHEET 6 E 7 CYS B 777 SER B 784 -1 N GLU B 782 O TYR B 792
SHEET 7 E 7 GLY B 748 TYR B 749 1 N TYR B 749 O THR B 779
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 O VAL D 538 N ILE C 531
SHEET 4 F 4 LYS D 549 ALA D 556 -1 O PHE D 551 N LEU D 544
SHEET 1 G 4 HIS C 635 ALA C 639 0
SHEET 2 G 4 ASN C 642 SER C 649 -1 O ARG C 646 N HIS C 635
SHEET 3 G 4 VAL C 593 ARG C 595 -1 N VAL C 594 O LEU C 643
SHEET 4 G 4 GLN C 679 ALA C 682 -1 O GLN C 679 N ARG C 595
SHEET 1 H 7 HIS C 635 ALA C 639 0
SHEET 2 H 7 ASN C 642 SER C 649 -1 O ARG C 646 N HIS C 635
SHEET 3 H 7 SER C 580 ARG C 590 -1 N ARG C 590 O PHE C 647
SHEET 4 H 7 GLY C 703 ILE C 712 -1 O SER C 705 N LEU C 584
SHEET 5 H 7 ASP C 790 ILE C 800 -1 O ILE C 800 N LYS C 704
SHEET 6 H 7 CYS C 777 SER C 784 -1 N GLU C 782 O TYR C 792
SHEET 7 H 7 GLY C 748 TYR C 749 1 N TYR C 749 O THR C 779
SHEET 1 I 4 HIS D 635 ALA D 639 0
SHEET 2 I 4 ASN D 642 SER D 649 -1 O TYR D 644 N SER D 637
SHEET 3 I 4 VAL D 593 ARG D 595 -1 N VAL D 594 O LEU D 643
SHEET 4 I 4 GLN D 679 ALA D 682 -1 O GLN D 679 N ARG D 595
SHEET 1 J 7 HIS D 635 ALA D 639 0
SHEET 2 J 7 ASN D 642 SER D 649 -1 O TYR D 644 N SER D 637
SHEET 3 J 7 SER D 580 ARG D 590 -1 N ARG D 590 O PHE D 647
SHEET 4 J 7 GLY D 703 ILE D 712 -1 O SER D 705 N LEU D 584
SHEET 5 J 7 ASP D 790 ILE D 800 -1 O MET D 797 N VAL D 706
SHEET 6 J 7 CYS D 777 SER D 784 -1 N GLU D 782 O TYR D 792
SHEET 7 J 7 GLY D 748 TYR D 749 1 N TYR D 749 O THR D 779
CISPEP 1 GLY A 542 PRO A 543 0 3.70
CISPEP 2 CYS A 688 THR A 689 0 -10.04
CISPEP 3 GLY B 542 PRO B 543 0 0.59
CISPEP 4 CYS B 688 THR B 689 0 -14.17
CISPEP 5 GLY C 542 PRO C 543 0 1.40
CISPEP 6 CYS C 688 THR C 689 0 -8.20
CISPEP 7 GLY D 542 PRO D 543 0 -2.61
CISPEP 8 CYS D 688 THR D 689 0 -14.87
SITE 1 AC1 21 GLU A 559 CYS A 561 LEU A 562 SER A 565
SITE 2 AC1 21 ARG A 568 LYS A 735 ALA A 751 HIS A 752
SITE 3 AC1 21 ASN A 755 LEU A 853 ALA A 856 HIS A 861
SITE 4 AC1 21 HOH A 910 ARG B 590 MET B 657 SER B 661
SITE 5 AC1 21 VAL B 683 SER B 684 ASP B 690 LYS B 691
SITE 6 AC1 21 LYS B 692
SITE 1 AC2 23 ARG A 590 SER A 661 VAL A 683 SER A 684
SITE 2 AC2 23 ASN A 686 ASP A 690 LYS A 691 LYS A 692
SITE 3 AC2 23 HOH A 881 HOH A 999 GLU B 559 GLY B 560
SITE 4 AC2 23 CYS B 561 LEU B 562 SER B 565 LYS B 735
SITE 5 AC2 23 ALA B 751 HIS B 752 ASN B 755 LEU B 853
SITE 6 AC2 23 ALA B 856 LEU B 857 GLY B 860
SITE 1 AC3 21 GLU C 559 CYS C 561 LEU C 562 SER C 565
SITE 2 AC3 21 LYS C 735 ALA C 751 HIS C 752 ASN C 755
SITE 3 AC3 21 LEU C 853 ALA C 856 GLY C 860 ARG D 590
SITE 4 AC3 21 MET D 657 SER D 661 VAL D 683 SER D 684
SITE 5 AC3 21 ASN D 686 ASP D 690 LYS D 691 LYS D 692
SITE 6 AC3 21 HOH D 892
SITE 1 AC4 21 ARG C 590 SER C 661 VAL C 683 SER C 684
SITE 2 AC4 21 ASN C 686 ASP C 690 LYS C 691 LYS C 692
SITE 3 AC4 21 HOH C 880 GLU D 559 CYS D 561 LEU D 562
SITE 4 AC4 21 SER D 565 ARG D 568 LYS D 735 ALA D 751
SITE 5 AC4 21 HIS D 752 ASN D 755 SER D 852 LEU D 853
SITE 6 AC4 21 ALA D 856
CRYST1 74.732 176.958 76.735 90.00 118.83 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 0.013381 0.000000 0.007366 0.00000
SCALE2 0.000000 0.005651 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014876 0.00000
(ATOM LINES ARE NOT SHOWN.)
END