HEADER HYDROLASE/HYDROLASE INHIBITOR 13-MAY-13 4KP6
TITLE CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 4B (PDE4B) IN COMPLEX
TITLE 2 WITH A [1,3,5]TRIAZINE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: DPDE4, PDE32;
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: DPDE4, PDE4B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PDE4 INHIBITOR, PHOSPHODIESTERASE, TRIAZINE, NEUTROPHILIA, COPD,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GEWALD,C.GRUNWALD,U.EGERLAND
REVDAT 4 28-FEB-24 4KP6 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4KP6 1 REMARK
REVDAT 2 17-JUL-13 4KP6 1 JRNL
REVDAT 1 10-JUL-13 4KP6 0
JRNL AUTH R.GEWALD,C.GRUNWALD,U.EGERLAND
JRNL TITL DISCOVERY OF TRIAZINES AS POTENT, SELECTIVE AND ORALLY
JRNL TITL 2 ACTIVE PDE4 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 4308 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23806553
JRNL DOI 10.1016/J.BMCL.2013.05.099
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 47008
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1529
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2364
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2621
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.93000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.534
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2826 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1892 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3806 ; 1.359 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4620 ; 1.283 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 339 ; 5.030 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;33.677 ;24.926
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 494 ;11.602 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;15.360 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3095 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 544 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 111 ; 0.157 ; 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): 17 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 65 ; 0.267 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.363 ; 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): 1665 ; 1.481 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 662 ; 0.491 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2714 ; 2.382 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1161 ; 3.808 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1091 ; 5.726 ; 6.000
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 162 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): -38.5940 80.1010 135.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0991 T22: 0.0979
REMARK 3 T33: 0.2145 T12: 0.0246
REMARK 3 T13: 0.0140 T23: 0.0706
REMARK 3 L TENSOR
REMARK 3 L11: 1.6334 L22: 5.8412
REMARK 3 L33: 4.9323 L12: -1.9226
REMARK 3 L13: 0.7158 L23: 1.4650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.1088 S13: -0.2619
REMARK 3 S21: 0.2197 S22: 0.0452 S23: -0.3025
REMARK 3 S31: 0.5631 S32: 0.2494 S33: -0.0588
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 191 A 279
REMARK 3 ORIGIN FOR THE GROUP (A): -50.8680 87.9600 132.7450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0188 T22: 0.0122
REMARK 3 T33: 0.0160 T12: -0.0008
REMARK 3 T13: -0.0002 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.6652 L22: 1.2323
REMARK 3 L33: 1.3407 L12: 0.1349
REMARK 3 L13: -0.1960 L23: -0.3697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.1095 S13: -0.0353
REMARK 3 S21: 0.1033 S22: 0.0025 S23: 0.0227
REMARK 3 S31: 0.0668 S32: -0.0230 S33: 0.0166
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 280 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): -58.1780 90.1940 107.7730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0719 T22: 0.0640
REMARK 3 T33: 0.0492 T12: -0.0297
REMARK 3 T13: -0.0016 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 3.5799 L22: 4.3785
REMARK 3 L33: 3.2899 L12: -2.9021
REMARK 3 L13: -1.2093 L23: 0.9520
REMARK 3 S TENSOR
REMARK 3 S11: -0.0543 S12: 0.2740 S13: -0.1997
REMARK 3 S21: -0.2611 S22: -0.0013 S23: 0.1114
REMARK 3 S31: -0.0529 S32: -0.0011 S33: 0.0556
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 301 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): -44.8720 95.4230 121.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0524 T22: 0.0234
REMARK 3 T33: 0.0311 T12: 0.0008
REMARK 3 T13: -0.0165 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 2.2778 L22: 0.6871
REMARK 3 L33: 1.0360 L12: 0.2119
REMARK 3 L13: -0.3784 L23: -0.1551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: 0.0978 S13: 0.0549
REMARK 3 S21: -0.0646 S22: -0.0016 S23: -0.0210
REMARK 3 S31: -0.0551 S32: 0.0179 S33: 0.0274
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 4KP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : FIXED-EXIT LN2 COOLED DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : RH COATED MERIDIONALLY FOCUSSING
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48537
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 57.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 41.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ETHYLENE GLYCOLE, PEG1K, PH 5.9, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.52400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.66600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.66600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 171.78600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.66600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.66600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.26200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.66600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.66600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 171.78600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.66600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.66600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.26200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 114.52400
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 148
REMARK 465 ALA A 149
REMARK 465 MET A 150
REMARK 465 GLY A 151
REMARK 465 SER A 152
REMARK 465 ILE A 153
REMARK 465 SER A 154
REMARK 465 ARG A 155
REMARK 465 PHE A 156
REMARK 465 GLY A 157
REMARK 465 VAL A 158
REMARK 465 ASN A 159
REMARK 465 THR A 160
REMARK 465 GLU A 161
REMARK 465 GLN A 486
REMARK 465 SER A 487
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 163 CG CD OE1 OE2
REMARK 480 LYS A 168 CD CE NZ
REMARK 480 GLN A 284 CD OE1 NE2
REMARK 480 GLU A 318 CG CD OE1 OE2
REMARK 480 MET A 351 CE
REMARK 480 LYS A 365 CD CE NZ
REMARK 480 SER A 368 OG
REMARK 480 SER A 369 OG
REMARK 480 TYR A 377 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 GLU A 423 CD OE1 OE2
REMARK 480 GLU A 427 CG CD OE1 OE2
REMARK 480 LYS A 441 NZ
REMARK 480 PRO A 485 CA C O CB CG CD
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 SER A 301 55.82 38.64
REMARK 500 ASP A 375 -78.09 -39.36
REMARK 500 LEU A 393 30.23 -99.12
REMARK 500 ILE A 450 -59.95 -125.33
REMARK 500
REMARK 500 REMARK: NULL
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 A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 238 NE2
REMARK 620 2 HIS A 274 NE2 98.0
REMARK 620 3 ASP A 275 OD2 87.8 87.2
REMARK 620 4 ASP A 392 OD1 92.5 89.2 176.4
REMARK 620 5 HOH A 711 O 87.1 174.7 94.2 89.4
REMARK 620 6 HOH A 712 O 166.1 95.3 88.8 91.7 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 275 OD1
REMARK 620 2 HOH A 612 O 84.8
REMARK 620 3 HOH A 613 O 87.7 91.6
REMARK 620 4 HOH A 709 O 170.6 87.8 86.7
REMARK 620 5 HOH A 712 O 93.8 94.4 173.9 92.5
REMARK 620 6 HOH A 726 O 96.3 178.8 89.0 91.1 85.0
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 1S1 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 522
DBREF 4KP6 A 152 487 UNP Q07343 PDE4B_HUMAN 324 659
SEQADV 4KP6 GLY A 148 UNP Q07343 EXPRESSION TAG
SEQADV 4KP6 ALA A 149 UNP Q07343 EXPRESSION TAG
SEQADV 4KP6 MET A 150 UNP Q07343 EXPRESSION TAG
SEQADV 4KP6 GLY A 151 UNP Q07343 EXPRESSION TAG
SEQRES 1 A 340 GLY ALA MET GLY SER ILE SER ARG PHE GLY VAL ASN THR
SEQRES 2 A 340 GLU ASN GLU ASP HIS LEU ALA LYS GLU LEU GLU ASP LEU
SEQRES 3 A 340 ASN LYS TRP GLY LEU ASN ILE PHE ASN VAL ALA GLY TYR
SEQRES 4 A 340 SER HIS ASN ARG PRO LEU THR CYS ILE MET TYR ALA ILE
SEQRES 5 A 340 PHE GLN GLU ARG ASP LEU LEU LYS THR PHE ARG ILE SER
SEQRES 6 A 340 SER ASP THR PHE ILE THR TYR MET MET THR LEU GLU ASP
SEQRES 7 A 340 HIS TYR HIS SER ASP VAL ALA TYR HIS ASN SER LEU HIS
SEQRES 8 A 340 ALA ALA ASP VAL ALA GLN SER THR HIS VAL LEU LEU SER
SEQRES 9 A 340 THR PRO ALA LEU ASP ALA VAL PHE THR ASP LEU GLU ILE
SEQRES 10 A 340 LEU ALA ALA ILE PHE ALA ALA ALA ILE HIS ASP VAL ASP
SEQRES 11 A 340 HIS PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN
SEQRES 12 A 340 SER GLU LEU ALA LEU MET TYR ASN ASP GLU SER VAL LEU
SEQRES 13 A 340 GLU ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN
SEQRES 14 A 340 GLU GLU HIS CYS ASP ILE PHE MET ASN LEU THR LYS LYS
SEQRES 15 A 340 GLN ARG GLN THR LEU ARG LYS MET VAL ILE ASP MET VAL
SEQRES 16 A 340 LEU ALA THR ASP MET SER LYS HIS MET SER LEU LEU ALA
SEQRES 17 A 340 ASP LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER
SEQRES 18 A 340 SER GLY VAL LEU LEU LEU ASP ASN TYR THR ASP ARG ILE
SEQRES 19 A 340 GLN VAL LEU ARG ASN MET VAL HIS CYS ALA ASP LEU SER
SEQRES 20 A 340 ASN PRO THR LYS SER LEU GLU LEU TYR ARG GLN TRP THR
SEQRES 21 A 340 ASP ARG ILE MET GLU GLU PHE PHE GLN GLN GLY ASP LYS
SEQRES 22 A 340 GLU ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP
SEQRES 23 A 340 LYS HIS THR ALA SER VAL GLU LYS SER GLN VAL GLY PHE
SEQRES 24 A 340 ILE ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA
SEQRES 25 A 340 ASP LEU VAL GLN PRO ASP ALA GLN ASP ILE LEU ASP THR
SEQRES 26 A 340 LEU GLU ASP ASN ARG ASN TRP TYR GLN SER MET ILE PRO
SEQRES 27 A 340 GLN SER
HET 1S1 A 501 21
HET MG A 502 1
HET ZN A 503 1
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 5
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 4
HET EDO A 514 4
HET EDO A 515 4
HET EDO A 516 4
HET EDO A 517 4
HET EDO A 518 4
HET EDO A 519 4
HET EDO A 520 4
HET EDO A 521 4
HET EDO A 522 4
HETNAM 1S1 2-ETHYL-2-{[4-(METHYLAMINO)-6-(1H-1,2,4-TRIAZOL-1-YL)-
HETNAM 2 1S1 1,3,5-TRIAZIN-2-YL]AMINO}BUTANENITRILE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 1S1 C12 H17 N9
FORMUL 3 MG MG 2+
FORMUL 4 ZN ZN 2+
FORMUL 5 EDO 19(C2 H6 O2)
FORMUL 24 HOH *151(H2 O)
HELIX 1 1 ASN A 162 GLU A 171 1 10
HELIX 2 2 ASN A 179 SER A 187 1 9
HELIX 3 3 ARG A 190 ARG A 203 1 14
HELIX 4 4 ASP A 204 PHE A 209 1 6
HELIX 5 5 SER A 212 HIS A 226 1 15
HELIX 6 6 ASN A 235 SER A 251 1 17
HELIX 7 7 THR A 252 ASP A 256 5 5
HELIX 8 8 THR A 260 HIS A 274 1 15
HELIX 9 9 SER A 282 THR A 289 1 8
HELIX 10 10 SER A 291 TYR A 297 1 7
HELIX 11 11 SER A 301 LEU A 315 1 15
HELIX 12 12 THR A 327 ALA A 344 1 18
HELIX 13 13 THR A 345 SER A 348 5 4
HELIX 14 14 LYS A 349 THR A 363 1 15
HELIX 15 15 ASN A 376 LEU A 393 1 18
HELIX 16 16 SER A 394 LYS A 398 5 5
HELIX 17 17 SER A 399 ARG A 424 1 26
HELIX 18 18 SER A 438 ILE A 450 1 13
HELIX 19 19 ILE A 450 VAL A 462 1 13
HELIX 20 20 ALA A 466 MET A 483 1 18
LINK NE2 HIS A 238 ZN ZN A 503 1555 1555 2.14
LINK NE2 HIS A 274 ZN ZN A 503 1555 1555 2.15
LINK OD1 ASP A 275 MG MG A 502 1555 1555 2.10
LINK OD2 ASP A 275 ZN ZN A 503 1555 1555 2.11
LINK OD1 ASP A 392 ZN ZN A 503 1555 1555 2.13
LINK MG MG A 502 O HOH A 612 1555 1555 2.06
LINK MG MG A 502 O HOH A 613 1555 1555 2.09
LINK MG MG A 502 O HOH A 709 1555 1555 2.15
LINK MG MG A 502 O HOH A 712 1555 1555 2.01
LINK MG MG A 502 O HOH A 726 1555 1555 2.14
LINK ZN ZN A 503 O HOH A 711 1555 1555 2.24
LINK ZN ZN A 503 O HOH A 712 1555 1555 2.22
CISPEP 1 GLN A 463 PRO A 464 0 4.41
SITE 1 AC1 11 HIS A 234 MET A 347 ASN A 395 THR A 407
SITE 2 AC1 11 ILE A 410 MET A 431 SER A 442 GLN A 443
SITE 3 AC1 11 PHE A 446 HOH A 635 HOH A 646
SITE 1 AC2 6 ASP A 275 HOH A 612 HOH A 613 HOH A 709
SITE 2 AC2 6 HOH A 712 HOH A 726
SITE 1 AC3 6 HIS A 238 HIS A 274 ASP A 275 ASP A 392
SITE 2 AC3 6 HOH A 711 HOH A 712
SITE 1 AC4 6 THR A 208 PHE A 209 ASN A 325 LEU A 326
SITE 2 AC4 6 GLN A 330 EDO A 521
SITE 1 AC5 10 ARG A 210 ILE A 211 SER A 212 THR A 215
SITE 2 AC5 10 ASP A 321 ILE A 322 MET A 324 ASN A 325
SITE 3 AC5 10 EDO A 514 HOH A 605
SITE 1 AC6 7 ASN A 283 ASP A 299 SER A 301 VAL A 302
SITE 2 AC6 7 ASP A 346 SER A 348 EDO A 522
SITE 1 AC7 8 GLY A 177 LEU A 178 ILE A 180 ASP A 241
SITE 2 AC7 8 LYS A 398 LEU A 402 TRP A 406 HOH A 611
SITE 1 AC8 4 SER A 251 PRO A 253 ASP A 256 HOH A 669
SITE 1 AC9 4 LEU A 249 THR A 252 TRP A 458 ASP A 465
SITE 1 BC1 3 ASP A 340 LYS A 349 ARG A 385
SITE 1 BC2 3 TYR A 297 HIS A 306 ALA A 309
SITE 1 BC3 7 HIS A 234 GLY A 280 GLU A 413 PHE A 414
SITE 2 BC3 7 GLN A 417 EDO A 518 HOH A 625
SITE 1 BC4 3 SER A 212 HOH A 647 HOH A 671
SITE 1 BC5 5 SER A 212 ASP A 214 THR A 215 HIS A 319
SITE 2 BC5 5 EDO A 505
SITE 1 BC6 3 ARG A 331 ARG A 335 EDO A 516
SITE 1 BC7 5 ASP A 321 ARG A 331 ARG A 335 EDO A 515
SITE 2 BC7 5 HOH A 653
SITE 1 BC8 4 ASN A 174 GLU A 202 HIS A 247 SER A 251
SITE 1 BC9 6 SER A 282 PRO A 430 CYS A 432 EDO A 512
SITE 2 BC9 6 HOH A 693 HOH A 710
SITE 1 CC1 5 LEU A 250 LEU A 255 ALA A 257 VAL A 258
SITE 2 CC1 5 PHE A 259
SITE 1 CC2 7 ARG A 203 ASP A 204 LEU A 205 THR A 208
SITE 2 CC2 7 ASP A 261 ILE A 264 HOH A 609
SITE 1 CC3 5 THR A 208 ASP A 261 GLN A 330 EDO A 504
SITE 2 CC3 5 HOH A 746
SITE 1 CC4 4 GLU A 300 ASP A 346 LYS A 349 EDO A 506
CRYST1 53.332 53.332 229.048 90.00 90.00 90.00 P 43 21 2 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 0.018750 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018750 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
