HEADER OXIDOREDUCTASE 26-FEB-08 3CDB
TITLE THERMODYNAMIC AND STRUCTURE GUIDED DESIGN OF STATIN HMG-COA REDUCTASE
TITLE 2 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 GENE: HMGCR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 STAR
KEYWDS OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH, STATIN,
KEYWDS 2 ALTERNATIVE SPLICING, ENDOPLASMIC RETICULUM, GLYCOPROTEIN, LIPID
KEYWDS 3 SYNTHESIS, MEMBRANE, PEROXISOME, POLYMORPHISM, STEROID BIOSYNTHESIS,
KEYWDS 4 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAVLOVSKY,R.W.SARVER,M.S.HARRIS,B.C.FINZEL
REVDAT 6 21-FEB-24 3CDB 1 REMARK
REVDAT 5 20-OCT-21 3CDB 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3CDB 1 REMARK
REVDAT 3 24-FEB-09 3CDB 1 VERSN
REVDAT 2 12-AUG-08 3CDB 1 JRNL
REVDAT 1 17-JUN-08 3CDB 0
JRNL AUTH R.W.SARVER,E.BILLS,G.BOLTON,L.D.BRATTON,N.L.CASPERS,
JRNL AUTH 2 J.B.DUNBAR,M.S.HARRIS,R.H.HUTCHINGS,R.M.KENNEDY,S.D.LARSEN,
JRNL AUTH 3 A.PAVLOVSKY,J.A.PFEFFERKORN,G.BAINBRIDGE
JRNL TITL THERMODYNAMIC AND STRUCTURE GUIDED DESIGN OF STATIN BASED
JRNL TITL 2 INHIBITORS OF 3-HYDROXY-3-METHYLGLUTARYL COENZYME A
JRNL TITL 3 REDUCTASE.
JRNL REF J.MED.CHEM. V. 51 3804 2008
JRNL REFN ISSN 0022-2623
JRNL PMID 18540668
JRNL DOI 10.1021/JM7015057
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 68649
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3496
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3254
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 175
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12283
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 184
REMARK 3 SOLVENT ATOMS : 633
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.80000
REMARK 3 B22 (A**2) : -1.29000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.491
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.257
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12668 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 11714 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17138 ; 1.153 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27282 ; 0.887 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1647 ; 5.448 ; 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): 1960 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14154 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2368 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2726 ; 0.171 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 13926 ; 0.206 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 7608 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 651 ; 0.145 ; 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): 19 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 60 ; 0.171 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.174 ; 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): 8170 ; 0.340 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13062 ; 0.648 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4498 ; 0.852 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4076 ; 1.567 ; 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 3CDB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68943
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.32400
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 15-20 MG/ML, LIGAND
REMARK 280 (SATURATED),PEG 4000, MGCL2 0.2M, TRIS-HCL PH8 0.1M, 7-10 DAYS,
REMARK 280 PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 86.74200
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: 25450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -171.0 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 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 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 ALA C 455
REMARK 465 GLU C 456
REMARK 465 LYS C 457
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 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 C 771 OG SER C 775 2.15
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 ASP B 623 CB - CG - OD2 ANGL. DEV. = 5.8 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 LYS A 457 -82.81 -104.26
REMARK 500 ALA A 473 41.85 103.99
REMARK 500 LYS A 474 -179.64 59.04
REMARK 500 HIS A 475 -50.10 101.33
REMARK 500 ALA A 478 -49.42 164.07
REMARK 500 TYR A 514 -25.07 -153.10
REMARK 500 CYS A 561 -8.06 82.33
REMARK 500 SER A 651 38.41 -157.70
REMARK 500 ALA A 710 148.98 179.50
REMARK 500 LYS A 735 -66.51 -96.76
REMARK 500 LEU A 737 -63.38 -102.03
REMARK 500 TYR A 749 53.38 -94.34
REMARK 500 HIS A 752 42.45 -157.33
REMARK 500 SER A 799 53.33 -143.44
REMARK 500 LYS B 457 -94.66 -125.52
REMARK 500 TYR B 514 -24.05 -142.92
REMARK 500 ALA B 525 -44.05 -156.00
REMARK 500 SER B 649 148.29 -170.25
REMARK 500 SER B 651 33.21 -146.61
REMARK 500 LYS B 735 -64.43 -95.37
REMARK 500 LEU B 737 -65.21 -98.01
REMARK 500 TYR B 749 57.67 -94.24
REMARK 500 HIS B 752 42.52 -153.84
REMARK 500 SER B 799 51.05 -147.88
REMARK 500 LYS C 474 47.53 -90.24
REMARK 500 TYR C 514 -21.03 -143.92
REMARK 500 ALA C 525 -24.18 -149.85
REMARK 500 SER C 651 27.32 -146.60
REMARK 500 LYS C 735 -65.55 -99.54
REMARK 500 LEU C 737 -68.72 -104.05
REMARK 500 TYR C 749 56.93 -95.53
REMARK 500 HIS C 752 39.84 -159.52
REMARK 500 SER C 799 52.34 -141.48
REMARK 500 ALA D 473 42.57 -94.73
REMARK 500 TYR D 514 -29.66 -166.66
REMARK 500 ALA D 525 -45.68 -154.82
REMARK 500 CYS D 561 -4.47 67.52
REMARK 500 SER D 651 41.36 -156.34
REMARK 500 LYS D 735 -65.95 -100.24
REMARK 500 TYR D 749 57.99 -94.71
REMARK 500 HIS D 752 42.44 -158.42
REMARK 500 SER D 799 52.35 -143.12
REMARK 500 ASN D 830 80.43 -150.67
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 9HI A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9HI A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9HI D 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9HI C 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CCT RELATED DB: PDB
REMARK 900 RELATED ID: 3CCW RELATED DB: PDB
REMARK 900 RELATED ID: 3CCZ RELATED DB: PDB
REMARK 900 RELATED ID: 3CD0 RELATED DB: PDB
REMARK 900 RELATED ID: 3CD5 RELATED DB: PDB
REMARK 900 RELATED ID: 3CD7 RELATED DB: PDB
REMARK 900 RELATED ID: 3CDA RELATED DB: PDB
DBREF 3CDB A 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 3CDB B 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 3CDB C 441 875 UNP P04035 HMDH_HUMAN 441 875
DBREF 3CDB D 441 875 UNP P04035 HMDH_HUMAN 441 875
SEQADV 3CDB HIS A 435 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS A 436 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS A 437 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS A 438 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS A 439 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS A 440 UNP P04035 EXPRESSION TAG
SEQADV 3CDB ILE A 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 3CDB HIS B 435 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS B 436 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS B 437 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS B 438 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS B 439 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS B 440 UNP P04035 EXPRESSION TAG
SEQADV 3CDB ILE B 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 3CDB HIS C 435 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS C 436 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS C 437 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS C 438 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS C 439 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS C 440 UNP P04035 EXPRESSION TAG
SEQADV 3CDB ILE C 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 3CDB HIS D 435 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS D 436 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS D 437 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS D 438 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS D 439 UNP P04035 EXPRESSION TAG
SEQADV 3CDB HIS D 440 UNP P04035 EXPRESSION TAG
SEQADV 3CDB 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 9HI A 1 46
HET 9HI A 2 46
HET 9HI C 4 46
HET 9HI D 3 46
HETNAM 9HI (3R,5R)-7-{3-[(4-CARBAMOYLPHENYL)SULFAMOYL]-4,5-BIS(4-
HETNAM 2 9HI FLUOROPHENYL)-2-(1-METHYLETHYL)-1H-PYRROL-1-YL}-3,5-
HETNAM 3 9HI DIHYDROXYHEPTANOIC ACID
FORMUL 5 9HI 4(C33 H35 F2 N3 O7 S)
FORMUL 9 HOH *633(H2 O)
HELIX 1 1 PRO A 444 ASN A 454 1 11
HELIX 2 2 GLY A 458 LEU A 462 5 5
HELIX 3 3 SER A 463 ASN A 472 1 10
HELIX 4 4 LYS A 480 ILE A 485 1 6
HELIX 5 5 THR A 487 LEU A 503 1 17
HELIX 6 6 SER A 507 LEU A 512 5 6
HELIX 7 7 ASN A 518 VAL A 522 5 5
HELIX 8 8 CYS A 561 LEU A 575 1 15
HELIX 9 9 ARG A 598 THR A 611 1 14
HELIX 10 10 THR A 611 SER A 624 1 14
HELIX 11 11 GLY A 656 PHE A 675 1 20
HELIX 12 12 ALA A 694 GLY A 701 1 8
HELIX 13 13 PRO A 713 VAL A 720 1 8
HELIX 14 14 THR A 724 LEU A 737 1 14
HELIX 15 15 LEU A 737 ALA A 743 1 7
HELIX 16 16 HIS A 752 CYS A 764 1 13
HELIX 17 17 ASP A 767 ALA A 769 5 3
HELIX 18 18 GLN A 770 SER A 775 1 6
HELIX 19 19 GLY A 806 ASN A 810 5 5
HELIX 20 20 LEU A 811 GLY A 822 1 12
HELIX 21 21 GLY A 832 GLY A 860 1 29
HELIX 22 22 PRO B 444 ASN B 454 1 11
HELIX 23 23 GLY B 458 LEU B 462 5 5
HELIX 24 24 SER B 463 ALA B 473 1 11
HELIX 25 25 PRO B 477 TYR B 479 5 3
HELIX 26 26 LYS B 480 ILE B 485 1 6
HELIX 27 27 THR B 487 LEU B 503 1 17
HELIX 28 28 ASN B 518 VAL B 522 5 5
HELIX 29 29 CYS B 561 GLY B 576 1 16
HELIX 30 30 ARG B 598 THR B 611 1 14
HELIX 31 31 THR B 611 SER B 624 1 14
HELIX 32 32 GLY B 656 PHE B 675 1 20
HELIX 33 33 ALA B 694 GLY B 701 1 8
HELIX 34 34 PRO B 713 VAL B 720 1 8
HELIX 35 35 THR B 724 LEU B 737 1 14
HELIX 36 36 LEU B 737 GLY B 744 1 8
HELIX 37 37 HIS B 752 CYS B 764 1 13
HELIX 38 38 ASP B 767 ALA B 769 5 3
HELIX 39 39 GLN B 770 SER B 775 1 6
HELIX 40 40 GLY B 806 ASN B 810 5 5
HELIX 41 41 LEU B 811 LEU B 821 1 11
HELIX 42 42 GLY B 832 GLY B 860 1 29
HELIX 43 43 PRO C 444 GLY C 453 1 10
HELIX 44 44 GLY C 458 LEU C 462 5 5
HELIX 45 45 SER C 463 ALA C 473 1 11
HELIX 46 46 PRO C 477 TYR C 479 5 3
HELIX 47 47 LYS C 480 ILE C 485 1 6
HELIX 48 48 THR C 487 LEU C 503 1 17
HELIX 49 49 SER C 507 LEU C 512 5 6
HELIX 50 50 CYS C 561 LEU C 575 1 15
HELIX 51 51 ARG C 598 THR C 611 1 14
HELIX 52 52 THR C 611 SER C 624 1 14
HELIX 53 53 GLY C 656 PHE C 675 1 20
HELIX 54 54 ALA C 694 GLY C 701 1 8
HELIX 55 55 PRO C 713 VAL C 720 1 8
HELIX 56 56 THR C 724 LEU C 737 1 14
HELIX 57 57 LEU C 737 ALA C 743 1 7
HELIX 58 58 HIS C 752 CYS C 764 1 13
HELIX 59 59 ASP C 767 ALA C 769 5 3
HELIX 60 60 GLN C 770 SER C 775 1 6
HELIX 61 61 GLY C 806 ASN C 810 5 5
HELIX 62 62 LEU C 811 LEU C 821 1 11
HELIX 63 63 GLY C 832 GLY C 860 1 29
HELIX 64 64 SER D 463 ALA D 473 1 11
HELIX 65 65 THR D 487 LYS D 501 1 15
HELIX 66 66 GLU D 505 LEU D 512 5 8
HELIX 67 67 ASN D 518 VAL D 522 5 5
HELIX 68 68 CYS D 561 GLY D 576 1 16
HELIX 69 69 ARG D 598 GLU D 610 1 13
HELIX 70 70 THR D 611 SER D 624 1 14
HELIX 71 71 GLY D 656 PHE D 675 1 20
HELIX 72 72 ALA D 694 GLY D 701 1 8
HELIX 73 73 PRO D 713 VAL D 720 1 8
HELIX 74 74 THR D 724 LEU D 737 1 14
HELIX 75 75 LEU D 737 ALA D 743 1 7
HELIX 76 76 HIS D 752 CYS D 764 1 13
HELIX 77 77 ASP D 767 ALA D 769 5 3
HELIX 78 78 GLN D 770 SER D 775 1 6
HELIX 79 79 GLY D 806 ASN D 810 5 5
HELIX 80 80 LEU D 811 LEU D 821 1 11
HELIX 81 81 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 LEU A 544 O PHE A 551
SHEET 3 A 4 VAL B 530 LEU B 546 -1 O ILE B 531 N VAL A 538
SHEET 4 A 4 LYS B 549 ALA B 556 -1 O PHE B 551 N LEU B 544
SHEET 1 B 4 ARG A 630 LEU A 631 0
SHEET 2 B 4 ASN A 642 ARG A 650 -1 O ARG A 650 N ARG A 630
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 ARG A 650 -1 O ARG A 646 N HIS A 635
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 TYR B 644 N SER B 637
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 TYR B 644 N SER B 637
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 MET B 797 N VAL B 706
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 LEU C 544 O PHE C 551
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 MET D 555 N GLY D 539
SHEET 1 G 4 HIS C 635 ALA C 639 0
SHEET 2 G 4 ASN C 642 SER C 649 -1 O TYR C 644 N SER C 637
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 TYR C 644 N SER C 637
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 MET C 797 N VAL C 706
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 ARG D 630 LEU D 631 0
SHEET 2 I 4 ASN D 642 ARG D 650 -1 O ARG D 650 N ARG D 630
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 ARG D 650 -1 O ARG D 646 N HIS D 635
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 ILE D 800 N LYS D 704
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 -4.18
CISPEP 2 CYS A 688 THR A 689 0 -7.60
CISPEP 3 GLY B 542 PRO B 543 0 -1.31
CISPEP 4 CYS B 688 THR B 689 0 -4.27
CISPEP 5 GLY C 542 PRO C 543 0 0.62
CISPEP 6 CYS C 688 THR C 689 0 -12.42
CISPEP 7 GLY D 542 PRO D 543 0 -0.19
CISPEP 8 CYS D 688 THR D 689 0 -10.18
SITE 1 AC1 18 GLU A 559 GLY A 560 SER A 565 LYS A 735
SITE 2 AC1 18 ALA A 751 ASN A 755 LEU A 853 ALA A 856
SITE 3 AC1 18 LEU A 857 HIS A 861 HOH A 906 ARG B 590
SITE 4 AC1 18 ASN B 658 SER B 684 ASN B 686 ASP B 690
SITE 5 AC1 18 LYS B 691 LYS B 692
SITE 1 AC2 17 ARG A 590 SER A 684 ASP A 690 LYS A 691
SITE 2 AC2 17 LYS A 692 HOH A 878 HOH A 951 GLU B 559
SITE 3 AC2 17 GLY B 560 SER B 565 LYS B 735 ALA B 751
SITE 4 AC2 17 HIS B 752 ASN B 755 ALA B 856 GLY B 860
SITE 5 AC2 17 HIS B 861
SITE 1 AC3 19 GLU C 559 GLY C 560 CYS C 561 SER C 565
SITE 2 AC3 19 LYS C 735 ALA C 751 ASN C 755 LEU C 853
SITE 3 AC3 19 ALA C 856 GLY C 860 HIS C 861 ARG D 590
SITE 4 AC3 19 MET D 657 SER D 684 ASP D 690 LYS D 691
SITE 5 AC3 19 LYS D 692 HOH D 891 HOH D 928
SITE 1 AC4 15 ARG C 590 ASN C 658 SER C 684 ASP C 690
SITE 2 AC4 15 LYS C 691 LYS C 692 HOH C 879 GLU D 559
SITE 3 AC4 15 GLY D 560 CYS D 561 LYS D 735 ALA D 751
SITE 4 AC4 15 ASN D 755 ALA D 856 HIS D 861
CRYST1 73.575 173.484 75.990 90.00 118.68 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 0.013592 0.000000 0.007435 0.00000
SCALE2 0.000000 0.005764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
