HEADER HYDROLASE 06-OCT-04 1XOM
TITLE CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4D IN COMPLEX WITH
TITLE 2 CILOMILAST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4D;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4D;
COMPND 5 SYNONYM: DPDE3, PDE43;
COMPND 6 EC: 3.1.4.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDE4D;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON PLUS(RIL);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PHOSPHODIESTERASE, PDE, PDE4D, CILOMILAST, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.CARD,B.P.ENGLAND,Y.SUZUKI,D.FONG,B.POWELL,B.LEE,C.LUU,
AUTHOR 2 M.TABRIZIZAD,S.GILLETTE,P.N.IBRAHIM,D.R.ARTIS,G.BOLLAG,M.V.MILBURN,
AUTHOR 3 S.-H.KIM,J.SCHLESSINGER,K.Y.J.ZHANG
REVDAT 3 14-FEB-24 1XOM 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1XOM 1 VERSN
REVDAT 1 14-DEC-04 1XOM 0
JRNL AUTH G.L.CARD,B.P.ENGLAND,Y.SUZUKI,D.FONG,B.POWELL,B.LEE,C.LUU,
JRNL AUTH 2 M.TABRIZIZAD,S.GILLETTE,P.N.IBRAHIM,D.R.ARTIS,G.BOLLAG,
JRNL AUTH 3 M.V.MILBURN,S.-H.KIM,J.SCHLESSINGER,K.Y.J.ZHANG
JRNL TITL STRUCTURAL BASIS FOR THE ACTIVITY OF DRUGS THAT INHIBIT
JRNL TITL 2 PHOSPHODIESTERASES.
JRNL REF STRUCTURE V. 12 2233 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15576036
JRNL DOI 10.1016/J.STR.2004.10.004
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.25
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 107956
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5683
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 413
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 596
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.43000
REMARK 3 B33 (A**2) : 0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.244
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5559 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4951 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7516 ; 1.093 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11562 ; 0.782 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 644 ; 2.667 ; 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): 865 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5952 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1028 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1338 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5739 ; 0.219 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2928 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 463 ; 0.117 ; 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): 8 ; 0.088 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 51 ; 0.293 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.113 ; 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): 3246 ; 0.475 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5307 ; 0.939 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2313 ; 1.515 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2209 ; 2.516 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 293
REMARK 3 RESIDUE RANGE : A 297 A 411
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1980 3.5540 54.1190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.2048
REMARK 3 T33: 0.0475 T12: -0.0063
REMARK 3 T13: 0.0180 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.2083 L22: 0.2944
REMARK 3 L33: 1.2254 L12: 0.1165
REMARK 3 L13: -0.2785 L23: -0.1010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: -0.1262 S13: -0.0038
REMARK 3 S21: 0.1397 S22: -0.0617 S23: 0.0036
REMARK 3 S31: -0.0126 S32: 0.3618 S33: 0.0533
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 88 B 293
REMARK 3 RESIDUE RANGE : B 297 B 411
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4790 2.1320 15.4960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2086 T22: 0.1956
REMARK 3 T33: 0.1254 T12: -0.0219
REMARK 3 T13: 0.0032 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.5322 L22: 0.5442
REMARK 3 L33: 1.0935 L12: 0.2688
REMARK 3 L13: -0.4403 L23: -0.1321
REMARK 3 S TENSOR
REMARK 3 S11: -0.0735 S12: 0.0535 S13: 0.0171
REMARK 3 S21: -0.0214 S22: 0.0299 S23: 0.0607
REMARK 3 S31: 0.0818 S32: -0.0562 S33: 0.0437
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 1XOM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
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 : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : ELVES
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107956
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 81.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.26100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, ETHYLENE GLYCOL, ISOPROPANOL,
REMARK 280 GLYCEROL AND DTT, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 30.24300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.09300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.48300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.09300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.24300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.48300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS ONE MONOMER.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 65
REMARK 465 GLY A 66
REMARK 465 SER A 67
REMARK 465 SER A 68
REMARK 465 HIS A 69
REMARK 465 HIS A 70
REMARK 465 HIS A 71
REMARK 465 HIS A 72
REMARK 465 HIS A 73
REMARK 465 HIS A 74
REMARK 465 SER A 75
REMARK 465 SER A 76
REMARK 465 GLY A 77
REMARK 465 LEU A 78
REMARK 465 VAL A 79
REMARK 465 PRO A 80
REMARK 465 ARG A 81
REMARK 465 GLY A 82
REMARK 465 SER A 83
REMARK 465 HIS A 84
REMARK 465 MET A 85
REMARK 465 GLN A 412
REMARK 465 SER A 413
REMARK 465 MET B 65
REMARK 465 GLY B 66
REMARK 465 SER B 67
REMARK 465 SER B 68
REMARK 465 HIS B 69
REMARK 465 HIS B 70
REMARK 465 HIS B 71
REMARK 465 HIS B 72
REMARK 465 HIS B 73
REMARK 465 HIS B 74
REMARK 465 SER B 75
REMARK 465 SER B 76
REMARK 465 GLY B 77
REMARK 465 LEU B 78
REMARK 465 VAL B 79
REMARK 465 PRO B 80
REMARK 465 ARG B 81
REMARK 465 GLY B 82
REMARK 465 SER B 83
REMARK 465 HIS B 84
REMARK 465 MET B 85
REMARK 465 THR B 86
REMARK 465 GLU B 87
REMARK 465 SER B 294
REMARK 465 SER B 295
REMARK 465 GLY B 296
REMARK 465 GLN B 412
REMARK 465 SER B 413
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 87 CG CD OE1 OE2
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 OG SER A 226 O HOH A 1020 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU A 87 O HOH A 1133 4455 1.24
REMARK 500 CD GLU A 87 O HOH A 1133 4455 1.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 87 CB GLU A 87 CG -0.177
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 GLU A 87 CA - CB - CG ANGL. DEV. = 17.8 DEGREES
REMARK 500 ASP A 151 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 151 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 266 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 376 -57.75 -125.03
REMARK 500 ASP B 225 13.15 59.99
REMARK 500 ASN B 302 138.24 -177.84
REMARK 500 ILE B 376 -58.75 -123.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 HOH 1003-1008 ARE ASSOCIATED WITH CHAIN A.
REMARK 600 HOH 2003-2008 ARE ASSOCIATED WITH CHAIN B.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 164 NE2
REMARK 620 2 HIS A 200 NE2 96.4
REMARK 620 3 ASP A 201 OD2 89.3 87.0
REMARK 620 4 ASP A 318 OD1 90.0 89.0 175.9
REMARK 620 5 HOH A1007 O 167.6 95.7 89.0 92.5
REMARK 620 6 HOH A1008 O 87.7 174.2 97.1 87.0 80.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 201 OD1
REMARK 620 2 HOH A1003 O 87.2
REMARK 620 3 HOH A1004 O 85.0 91.5
REMARK 620 4 HOH A1005 O 169.0 88.3 85.1
REMARK 620 5 HOH A1006 O 99.1 87.0 175.5 90.7
REMARK 620 6 HOH A1007 O 91.1 172.2 96.0 94.7 85.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 164 NE2
REMARK 620 2 HIS B 200 NE2 95.3
REMARK 620 3 ASP B 201 OD2 90.8 86.9
REMARK 620 4 ASP B 318 OD1 89.3 89.0 175.8
REMARK 620 5 HOH B2007 O 171.5 93.1 88.2 92.4
REMARK 620 6 HOH B2008 O 87.7 174.3 98.0 86.2 84.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 201 OD1
REMARK 620 2 HOH B2003 O 88.8
REMARK 620 3 HOH B2004 O 85.2 93.0
REMARK 620 4 HOH B2005 O 168.6 86.7 84.6
REMARK 620 5 HOH B2006 O 98.7 84.3 175.2 91.3
REMARK 620 6 HOH B2007 O 89.5 174.3 92.3 96.0 90.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 715
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 716
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 717
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 718
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 719
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 720
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 721
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XLX RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH CILOMILAST
REMARK 900 RELATED ID: 1XLZ RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH FILAMINAST
REMARK 900 RELATED ID: 1XM4 RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH PICLAMILAST
REMARK 900 RELATED ID: 1XM6 RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH (R)-MESOPRAM
REMARK 900 RELATED ID: 1XMU RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH ROFLUMILAST
REMARK 900 RELATED ID: 1XMY RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH (R)-ROLIPRAM
REMARK 900 RELATED ID: 1XN0 RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH (R,S)-ROLIPRAM
REMARK 900 RELATED ID: 1XON RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH PICLAMILAST
REMARK 900 RELATED ID: 1XOQ RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH ROFLUMILAST
REMARK 900 RELATED ID: 1XOR RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH ZARDAVERINE
REMARK 900 RELATED ID: 1XOS RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH SILDENAFIL
REMARK 900 RELATED ID: 1XOT RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH VARDENAFIL
REMARK 900 RELATED ID: 1XOZ RELATED DB: PDB
REMARK 900 PDE5A IN COMPLEX WITH TADALAFIL
REMARK 900 RELATED ID: 1XP0 RELATED DB: PDB
REMARK 900 PDE5A IN COMPLEX WITH VARDENAFIL
DBREF 1XOM A 86 413 UNP Q08499 PDE4D_HUMAN 388 715
DBREF 1XOM B 86 413 UNP Q08499 PDE4D_HUMAN 388 715
SEQADV 1XOM MET A 65 UNP Q08499 INITIATING METHIONINE
SEQADV 1XOM GLY A 66 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER A 67 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER A 68 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM HIS A 69 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS A 70 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS A 71 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS A 72 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS A 73 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS A 74 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM SER A 75 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER A 76 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM GLY A 77 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM LEU A 78 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM VAL A 79 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM PRO A 80 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM ARG A 81 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM GLY A 82 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER A 83 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM HIS A 84 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM MET A 85 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM MET B 65 UNP Q08499 INITIATING METHIONINE
SEQADV 1XOM GLY B 66 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER B 67 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER B 68 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM HIS B 69 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS B 70 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS B 71 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS B 72 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS B 73 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM HIS B 74 UNP Q08499 EXPRESSION TAG
SEQADV 1XOM SER B 75 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER B 76 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM GLY B 77 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM LEU B 78 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM VAL B 79 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM PRO B 80 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM ARG B 81 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM GLY B 82 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM SER B 83 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM HIS B 84 UNP Q08499 CLONING ARTIFACT
SEQADV 1XOM MET B 85 UNP Q08499 CLONING ARTIFACT
SEQRES 1 A 349 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 349 LEU VAL PRO ARG GLY SER HIS MET THR GLU GLN GLU ASP
SEQRES 3 A 349 VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN LYS TRP GLY
SEQRES 4 A 349 LEU HIS VAL PHE ARG ILE ALA GLU LEU SER GLY ASN ARG
SEQRES 5 A 349 PRO LEU THR VAL ILE MET HIS THR ILE PHE GLN GLU ARG
SEQRES 6 A 349 ASP LEU LEU LYS THR PHE LYS ILE PRO VAL ASP THR LEU
SEQRES 7 A 349 ILE THR TYR LEU MET THR LEU GLU ASP HIS TYR HIS ALA
SEQRES 8 A 349 ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA ALA ASP VAL
SEQRES 9 A 349 VAL GLN SER THR HIS VAL LEU LEU SER THR PRO ALA LEU
SEQRES 10 A 349 GLU ALA VAL PHE THR ASP LEU GLU ILE LEU ALA ALA ILE
SEQRES 11 A 349 PHE ALA SER ALA ILE HIS ASP VAL ASP HIS PRO GLY VAL
SEQRES 12 A 349 SER ASN GLN PHE LEU ILE ASN THR ASN SER GLU LEU ALA
SEQRES 13 A 349 LEU MET TYR ASN ASP SER SER VAL LEU GLU ASN HIS HIS
SEQRES 14 A 349 LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU GLU ASN CYS
SEQRES 15 A 349 ASP ILE PHE GLN ASN LEU THR LYS LYS GLN ARG GLN SER
SEQRES 16 A 349 LEU ARG LYS MET VAL ILE ASP ILE VAL LEU ALA THR ASP
SEQRES 17 A 349 MET SER LYS HIS MET ASN LEU LEU ALA ASP LEU LYS THR
SEQRES 18 A 349 MET VAL GLU THR LYS LYS VAL THR SER SER GLY VAL LEU
SEQRES 19 A 349 LEU LEU ASP ASN TYR SER ASP ARG ILE GLN VAL LEU GLN
SEQRES 20 A 349 ASN MET VAL HIS CYS ALA ASP LEU SER ASN PRO THR LYS
SEQRES 21 A 349 PRO LEU GLN LEU TYR ARG GLN TRP THR ASP ARG ILE MET
SEQRES 22 A 349 GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU ARG GLU ARG
SEQRES 23 A 349 GLY MET GLU ILE SER PRO MET CYS ASP LYS HIS ASN ALA
SEQRES 24 A 349 SER VAL GLU LYS SER GLN VAL GLY PHE ILE ASP TYR ILE
SEQRES 25 A 349 VAL HIS PRO LEU TRP GLU THR TRP ALA ASP LEU VAL HIS
SEQRES 26 A 349 PRO ASP ALA GLN ASP ILE LEU ASP THR LEU GLU ASP ASN
SEQRES 27 A 349 ARG GLU TRP TYR GLN SER THR ILE PRO GLN SER
SEQRES 1 B 349 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 349 LEU VAL PRO ARG GLY SER HIS MET THR GLU GLN GLU ASP
SEQRES 3 B 349 VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN LYS TRP GLY
SEQRES 4 B 349 LEU HIS VAL PHE ARG ILE ALA GLU LEU SER GLY ASN ARG
SEQRES 5 B 349 PRO LEU THR VAL ILE MET HIS THR ILE PHE GLN GLU ARG
SEQRES 6 B 349 ASP LEU LEU LYS THR PHE LYS ILE PRO VAL ASP THR LEU
SEQRES 7 B 349 ILE THR TYR LEU MET THR LEU GLU ASP HIS TYR HIS ALA
SEQRES 8 B 349 ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA ALA ASP VAL
SEQRES 9 B 349 VAL GLN SER THR HIS VAL LEU LEU SER THR PRO ALA LEU
SEQRES 10 B 349 GLU ALA VAL PHE THR ASP LEU GLU ILE LEU ALA ALA ILE
SEQRES 11 B 349 PHE ALA SER ALA ILE HIS ASP VAL ASP HIS PRO GLY VAL
SEQRES 12 B 349 SER ASN GLN PHE LEU ILE ASN THR ASN SER GLU LEU ALA
SEQRES 13 B 349 LEU MET TYR ASN ASP SER SER VAL LEU GLU ASN HIS HIS
SEQRES 14 B 349 LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU GLU ASN CYS
SEQRES 15 B 349 ASP ILE PHE GLN ASN LEU THR LYS LYS GLN ARG GLN SER
SEQRES 16 B 349 LEU ARG LYS MET VAL ILE ASP ILE VAL LEU ALA THR ASP
SEQRES 17 B 349 MET SER LYS HIS MET ASN LEU LEU ALA ASP LEU LYS THR
SEQRES 18 B 349 MET VAL GLU THR LYS LYS VAL THR SER SER GLY VAL LEU
SEQRES 19 B 349 LEU LEU ASP ASN TYR SER ASP ARG ILE GLN VAL LEU GLN
SEQRES 20 B 349 ASN MET VAL HIS CYS ALA ASP LEU SER ASN PRO THR LYS
SEQRES 21 B 349 PRO LEU GLN LEU TYR ARG GLN TRP THR ASP ARG ILE MET
SEQRES 22 B 349 GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU ARG GLU ARG
SEQRES 23 B 349 GLY MET GLU ILE SER PRO MET CYS ASP LYS HIS ASN ALA
SEQRES 24 B 349 SER VAL GLU LYS SER GLN VAL GLY PHE ILE ASP TYR ILE
SEQRES 25 B 349 VAL HIS PRO LEU TRP GLU THR TRP ALA ASP LEU VAL HIS
SEQRES 26 B 349 PRO ASP ALA GLN ASP ILE LEU ASP THR LEU GLU ASP ASN
SEQRES 27 B 349 ARG GLU TRP TYR GLN SER THR ILE PRO GLN SER
HET ZN A1001 1
HET MG A1002 1
HET CIO A 603 50
HET EDO A 702 4
HET EDO A 703 4
HET EDO A 704 4
HET EDO A 707 4
HET EDO A 712 4
HET EDO A 715 4
HET EDO A 716 4
HET EDO A 719 4
HET EDO A 720 4
HET ZN B2001 1
HET MG B2002 1
HET CIO B 601 50
HET EDO B 701 4
HET EDO B 705 4
HET EDO B 706 4
HET EDO B 709 4
HET EDO B 710 4
HET EDO B 711 4
HET EDO B 713 4
HET EDO B 714 4
HET EDO B 717 4
HET EDO B 718 4
HET EDO B 721 4
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM CIO CILOMILAST
HETNAM EDO 1,2-ETHANEDIOL
HETSYN CIO CIS-4-CYANO-4-[3-(CYCLOPENTYLOXY)-4-
HETSYN 2 CIO METHOXYPHENYL]CYCLOHEXANECARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 CIO 2(C20 H25 N O4)
FORMUL 6 EDO 20(C2 H6 O2)
FORMUL 29 HOH *596(H2 O)
HELIX 1 22 THR A 86 GLU A 97 1 12
HELIX 2 23 HIS A 105 SER A 113 1 9
HELIX 3 24 ARG A 116 ARG A 129 1 14
HELIX 4 25 ASP A 130 PHE A 135 1 6
HELIX 5 26 PRO A 138 HIS A 152 1 15
HELIX 6 27 ASN A 161 SER A 177 1 17
HELIX 7 28 THR A 178 GLU A 182 5 5
HELIX 8 29 THR A 186 HIS A 200 1 15
HELIX 9 30 SER A 208 THR A 215 1 8
HELIX 10 31 SER A 217 ASN A 224 1 8
HELIX 11 32 SER A 227 LEU A 240 1 14
HELIX 12 33 LEU A 241 GLU A 243 5 3
HELIX 13 34 THR A 253 ALA A 270 1 18
HELIX 14 35 THR A 271 SER A 274 5 4
HELIX 15 36 LYS A 275 THR A 289 1 15
HELIX 16 37 ASN A 302 LEU A 319 1 18
HELIX 17 38 SER A 320 LYS A 324 5 5
HELIX 18 39 PRO A 325 ARG A 350 1 26
HELIX 19 40 SER A 364 ILE A 376 1 13
HELIX 20 41 ILE A 376 VAL A 388 1 13
HELIX 21 42 ALA A 392 THR A 409 1 18
HELIX 22 1 GLN B 88 GLU B 97 1 10
HELIX 23 2 HIS B 105 SER B 113 1 9
HELIX 24 3 ARG B 116 ARG B 129 1 14
HELIX 25 4 ASP B 130 PHE B 135 1 6
HELIX 26 5 PRO B 138 HIS B 152 1 15
HELIX 27 6 ASN B 161 SER B 177 1 17
HELIX 28 7 THR B 178 GLU B 182 5 5
HELIX 29 8 THR B 186 HIS B 200 1 15
HELIX 30 9 SER B 208 THR B 215 1 8
HELIX 31 10 SER B 217 ASN B 224 1 8
HELIX 32 11 SER B 227 LEU B 240 1 14
HELIX 33 12 LEU B 241 GLU B 243 5 3
HELIX 34 13 THR B 253 ALA B 270 1 18
HELIX 35 14 THR B 271 SER B 274 5 4
HELIX 36 15 LYS B 275 THR B 289 1 15
HELIX 37 16 ASN B 302 LEU B 319 1 18
HELIX 38 17 SER B 320 LYS B 324 5 5
HELIX 39 18 PRO B 325 ARG B 350 1 26
HELIX 40 19 SER B 364 ILE B 376 1 13
HELIX 41 20 ILE B 376 VAL B 388 1 13
HELIX 42 21 ALA B 392 ILE B 410 1 19
LINK NE2 HIS A 164 ZN ZN A1001 1555 1555 2.15
LINK NE2 HIS A 200 ZN ZN A1001 1555 1555 2.15
LINK OD2 ASP A 201 ZN ZN A1001 1555 1555 2.08
LINK OD1 ASP A 201 MG MG A1002 1555 1555 2.19
LINK OD1 ASP A 318 ZN ZN A1001 1555 1555 2.16
LINK ZN ZN A1001 O HOH A1007 1555 1555 2.14
LINK ZN ZN A1001 O HOH A1008 1555 1555 2.21
LINK MG MG A1002 O HOH A1003 1555 1555 2.19
LINK MG MG A1002 O HOH A1004 1555 1555 2.15
LINK MG MG A1002 O HOH A1005 1555 1555 2.21
LINK MG MG A1002 O HOH A1006 1555 1555 2.17
LINK MG MG A1002 O HOH A1007 1555 1555 2.11
LINK NE2 HIS B 164 ZN ZN B2001 1555 1555 2.17
LINK NE2 HIS B 200 ZN ZN B2001 1555 1555 2.20
LINK OD2 ASP B 201 ZN ZN B2001 1555 1555 2.08
LINK OD1 ASP B 201 MG MG B2002 1555 1555 2.11
LINK OD1 ASP B 318 ZN ZN B2001 1555 1555 2.17
LINK ZN ZN B2001 O HOH B2007 1555 1555 2.11
LINK ZN ZN B2001 O HOH B2008 1555 1555 2.24
LINK MG MG B2002 O HOH B2003 1555 1555 2.17
LINK MG MG B2002 O HOH B2004 1555 1555 2.14
LINK MG MG B2002 O HOH B2005 1555 1555 2.21
LINK MG MG B2002 O HOH B2006 1555 1555 2.13
LINK MG MG B2002 O HOH B2007 1555 1555 2.10
CISPEP 1 HIS A 389 PRO A 390 0 -1.37
CISPEP 2 HIS B 389 PRO B 390 0 -0.19
SITE 1 AC1 6 HIS A 164 HIS A 200 ASP A 201 ASP A 318
SITE 2 AC1 6 HOH A1007 HOH A1008
SITE 1 AC2 7 ASP A 201 CIO A 603 HOH A1003 HOH A1004
SITE 2 AC2 7 HOH A1005 HOH A1006 HOH A1007
SITE 1 AC3 6 HIS B 164 HIS B 200 ASP B 201 ASP B 318
SITE 2 AC3 6 HOH B2007 HOH B2008
SITE 1 AC4 6 ASP B 201 HOH B2003 HOH B2004 HOH B2005
SITE 2 AC4 6 HOH B2006 HOH B2007
SITE 1 AC5 15 HIS B 160 THR B 271 MET B 273 LEU B 319
SITE 2 AC5 15 ASN B 321 ILE B 336 MET B 337 PHE B 340
SITE 3 AC5 15 MET B 357 GLN B 369 PHE B 372 HOH B2005
SITE 4 AC5 15 HOH B2006 HOH B2061 HOH B2072
SITE 1 AC6 18 HIS A 160 THR A 271 MET A 273 ASP A 318
SITE 2 AC6 18 LEU A 319 ASN A 321 ILE A 336 MET A 337
SITE 3 AC6 18 PHE A 340 MET A 357 GLN A 369 PHE A 372
SITE 4 AC6 18 MG A1002 HOH A1005 HOH A1006 HOH A1007
SITE 5 AC6 18 HOH A1044 HOH A1058
SITE 1 AC7 5 PRO A 411 ARG B 330 GLU B 366 TYR B 406
SITE 2 AC7 5 EDO B 713
SITE 1 AC8 4 LYS A 262 ILE A 265 ASP A 266 HOH A1021
SITE 1 AC9 6 THR A 186 GLU A 189 ARG A 306 HOH A1026
SITE 2 AC9 6 HOH A1066 ASP B 151
SITE 1 BC1 5 GLN A 210 HOH A1012 HOH A1033 HOH A1042
SITE 2 BC1 5 HOH A1051
SITE 1 BC2 6 LEU A 326 ARG A 330 EDO B 706 HOH B2014
SITE 2 BC2 6 HOH B2063 HOH B2236
SITE 1 BC3 4 HOH A1069 EDO B 705 HOH B2096 HOH B2269
SITE 1 BC4 8 GLU A 150 ASP A 151 TYR A 153 ALA A 155
SITE 2 BC4 8 ASN A 162 HOH A1067 HOH A1130 GLN B 407
SITE 1 BC5 4 LYS B 255 GLN B 258 SER B 259 HOH B2219
SITE 1 BC6 5 LEU B 92 SER B 113 VAL B 120 HOH B2216
SITE 2 BC6 5 HOH B2283
SITE 1 BC7 6 SER B 208 PHE B 340 GLN B 343 SER B 355
SITE 2 BC7 6 HOH B2188 HOH B2248
SITE 1 BC8 5 SER A 295 GLY A 296 HIS A 389 PRO A 390
SITE 2 BC8 5 ASP A 391
SITE 1 BC9 7 ARG B 330 THR B 333 ASP B 334 VAL B 365
SITE 2 BC9 7 TYR B 406 EDO B 701 HOH B2142
SITE 1 CC1 6 TRP A 405 HOH A1257 ASP B 401 ASN B 402
SITE 2 CC1 6 HOH B2014 HOH B2260
SITE 1 CC2 6 ASN A 115 ALA A 155 ASN A 162 ILE A 163
SITE 2 CC2 6 HOH A1130 HOH A1223
SITE 1 CC3 8 LEU A 175 THR A 178 TRP A 384 VAL A 388
SITE 2 CC3 8 ASP A 391 ALA A 392 ILE A 395 HOH A1100
SITE 1 CC4 9 PHE B 238 LEU B 241 PHE B 249 ARG B 257
SITE 2 CC4 9 LEU B 260 ARG B 261 EDO B 718 HOH B2210
SITE 3 CC4 9 HOH B2233
SITE 1 CC5 4 ARG B 257 GLN B 258 EDO B 717 HOH B2122
SITE 1 CC6 7 ALA A 183 VAL A 184 HOH A1073 ASN B 115
SITE 2 CC6 7 ARG B 116 HOH B2178 HOH B2273
SITE 1 CC7 5 PHE A 238 ARG A 257 ARG A 261 HOH A1152
SITE 2 CC7 5 HOH A1194
SITE 1 CC8 2 HOH B2022 HOH B2183
CRYST1 60.486 78.966 164.186 90.00 90.00 90.00 P 21 21 21 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 0.016533 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
