HEADER HYDROLASE 22-NOV-04 1Y2E
TITLE CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4D IN COMPLEX WITH 1-(4-
TITLE 2 AMINO-PHENYL)-3,5-DIMETHYL-1H-PYRAZOLE-4-CARBOXYLIC ACID ETHYL ESTER
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, PYRAZOLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.CARD,L.BLASDEL,B.P.ENGLAND,C.ZHANG,Y.SUZUKI,S.GILLETTE,D.FONG,
AUTHOR 2 P.N.IBRAHIM,D.R.ARTIS,G.BOLLAG,M.V.MILBURN,S.-H.KIM,J.SCHLESSINGER,
AUTHOR 3 K.Y.J.ZHANG
REVDAT 4 14-FEB-24 1Y2E 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1Y2E 1 VERSN
REVDAT 2 24-FEB-09 1Y2E 1 VERSN
REVDAT 1 01-MAR-05 1Y2E 0
JRNL AUTH G.L.CARD,L.BLASDEL,B.P.ENGLAND,C.ZHANG,Y.SUZUKI,S.GILLETTE,
JRNL AUTH 2 D.FONG,P.N.IBRAHIM,D.R.ARTIS,G.BOLLAG,M.V.MILBURN,S.-H.KIM,
JRNL AUTH 3 J.SCHLESSINGER,K.Y.J.ZHANG
JRNL TITL A FAMILY OF PHOSPHODIESTERASE INHIBITORS DISCOVERED BY
JRNL TITL 2 COCRYSTALLOGRAPHY AND SCAFFOLD-BASED DRUG DESIGN
JRNL REF NAT.BIOTECHNOL. V. 23 201 2005
JRNL REFN ISSN 1087-0156
JRNL PMID 15685167
JRNL DOI 10.1038/NBT1059
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 44124
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2355
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5237
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.76000
REMARK 3 B22 (A**2) : 3.53000
REMARK 3 B33 (A**2) : -1.77000
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): 0.207
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.377
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5447 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4852 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7372 ; 1.213 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11305 ; 0.843 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 643 ; 2.746 ; 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): 844 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5935 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1025 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1201 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5251 ; 0.220 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2857 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 248 ; 0.141 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.033 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 3 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.293 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.157 ; 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): 3237 ; 0.463 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5281 ; 0.852 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2210 ; 1.433 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2091 ; 2.356 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 86 A 411
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4870 2.0590 15.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.3179 T22: 0.0132
REMARK 3 T33: 0.1798 T12: -0.0186
REMARK 3 T13: 0.0018 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.0288 L22: 0.9825
REMARK 3 L33: 1.8488 L12: 0.2674
REMARK 3 L13: -0.6081 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0951 S12: 0.0855 S13: -0.0379
REMARK 3 S21: -0.0197 S22: 0.0312 S23: 0.0727
REMARK 3 S31: 0.1315 S32: -0.0971 S33: 0.0640
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 292
REMARK 3 RESIDUE RANGE : B 297 B 411
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2710 3.7410 54.2610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2553 T22: 0.0096
REMARK 3 T33: 0.1598 T12: -0.0028
REMARK 3 T13: 0.0213 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.6932 L22: 1.0814
REMARK 3 L33: 1.7987 L12: 0.1412
REMARK 3 L13: -0.1324 L23: -0.4213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: 0.0439 S13: -0.0438
REMARK 3 S21: 0.0134 S22: -0.0102 S23: -0.0792
REMARK 3 S31: -0.0117 S32: 0.0561 S33: -0.0055
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 1Y2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000031029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : 44124
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.17300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 (%): 50.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
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 30.44000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.13250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.13250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.44000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.72100
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 THR B 293
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 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 A 140 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 266 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 359 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 151 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 156 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 201 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 386 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 ASP A 225 -2.81 66.26
REMARK 500 SER A 227 54.80 35.02
REMARK 500 ASN A 362 50.41 -142.88
REMARK 500 ASN B 161 -169.71 -129.01
REMARK 500 SER B 227 56.60 36.55
REMARK 500 ILE B 376 -58.78 -120.66
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 90.8
REMARK 620 3 ASP A 201 OD2 85.5 86.5
REMARK 620 4 ASP A 318 OD1 88.5 84.9 169.4
REMARK 620 5 HOH A1009 O 174.0 94.4 97.8 89.0
REMARK 620 6 HOH A1010 O 85.4 171.3 101.0 87.1 89.0
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 A1005 O 82.2
REMARK 620 3 HOH A1006 O 84.4 89.4
REMARK 620 4 HOH A1007 O 164.5 88.7 83.0
REMARK 620 5 HOH A1008 O 97.2 81.9 170.8 93.8
REMARK 620 6 HOH A1009 O 100.0 172.2 98.3 90.8 90.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 164 NE2
REMARK 620 2 HIS B 200 NE2 92.7
REMARK 620 3 ASP B 201 OD1 85.4 78.0
REMARK 620 4 ASP B 318 OD1 86.6 92.8 167.5
REMARK 620 5 HOH B2007 O 168.1 94.3 86.7 102.6
REMARK 620 6 HOH B2008 O 83.9 175.6 104.4 84.2 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 201 OD2
REMARK 620 2 HOH B2003 O 89.7
REMARK 620 3 HOH B2004 O 81.4 96.0
REMARK 620 4 HOH B2005 O 164.8 83.9 85.5
REMARK 620 5 HOH B2006 O 102.7 87.2 174.9 90.8
REMARK 620 6 HOH B2007 O 94.0 169.8 93.9 94.6 82.7
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5DE A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5DE B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 433
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 434
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 444
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y2B RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH 3,5-DIMETHYL-1H-PYRAZOLE-4-CARBOXYLIC ACID
REMARK 900 ETHYL ESTER
REMARK 900 RELATED ID: 1Y2C RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH 3,5-DIMETHYL-1-PHENYL-1H-PYRAZOLE-4-
REMARK 900 CARBOXYLIC ACID ETHYL ESTER
REMARK 900 RELATED ID: 1Y2D RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH 1-(4-METHOXY-PHENYL)-3,5-DIMETHYL-1H-PYRAZOLE-
REMARK 900 4-CARBOXYLIC ACID ETHYL ESTER
REMARK 900 RELATED ID: 1Y2H RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH 1-(2-CHLORO-PHENYL)-3,5-DIMETHYL-1H-PYRAZOLE-
REMARK 900 4-CARBOXYLIC ACID ETHYL ESTER
REMARK 900 RELATED ID: 1Y2J RELATED DB: PDB
REMARK 900 PDE4B IN COMPLEX WITH 3,5-DIMETHYL-1-(3-NITRO-PHENYL)-1H-PYRAZOLE-4-
REMARK 900 CARBOXYLIC ACID ETHYL ESTER
REMARK 900 RELATED ID: 1Y2K RELATED DB: PDB
REMARK 900 PDE4D IN COMPLEX WITH 3,5-DIMETHYL-1-(3-NITRO-PHENYL)-1H-PYRAZOLE-4-
REMARK 900 CARBOXYLIC ACID ETHYL ESTER
DBREF 1Y2E A 86 413 UNP Q08499 PDE4D_HUMAN 388 715
DBREF 1Y2E B 86 413 UNP Q08499 PDE4D_HUMAN 388 715
SEQADV 1Y2E MET A 65 UNP Q08499 INITIATING METHIONINE
SEQADV 1Y2E GLY A 66 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER A 67 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER A 68 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E HIS A 69 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS A 70 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS A 71 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS A 72 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS A 73 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS A 74 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E SER A 75 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER A 76 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E GLY A 77 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E LEU A 78 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E VAL A 79 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E PRO A 80 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E ARG A 81 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E GLY A 82 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER A 83 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E HIS A 84 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E MET A 85 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E MET B 65 UNP Q08499 INITIATING METHIONINE
SEQADV 1Y2E GLY B 66 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER B 67 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER B 68 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E HIS B 69 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS B 70 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS B 71 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS B 72 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS B 73 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E HIS B 74 UNP Q08499 EXPRESSION TAG
SEQADV 1Y2E SER B 75 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER B 76 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E GLY B 77 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E LEU B 78 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E VAL B 79 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E PRO B 80 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E ARG B 81 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E GLY B 82 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E SER B 83 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E HIS B 84 UNP Q08499 CLONING ARTIFACT
SEQADV 1Y2E 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 5DE A1003 19
HET EDO A1004 4
HET EDO A 415 4
HET EDO A 416 4
HET EDO A 419 4
HET EDO A 420 4
HET EDO A 422 4
HET EDO A 433 4
HET EDO A 444 4
HET ZN B1001 1
HET MG B1002 1
HET 5DE B1003 19
HET EDO B1004 4
HET EDO B1005 4
HET EDO B1006 4
HET EDO B 417 4
HET EDO B 430 4
HET EDO B 434 4
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM 5DE 1-(4-AMINOPHENYL)-3,5-DIMETHYL-1H-PYRAZOLE-4-CARBOXYLIC
HETNAM 2 5DE ACID ETHYL ESTER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 5DE 2(C14 H17 N3 O2)
FORMUL 6 EDO 14(C2 H6 O2)
FORMUL 23 HOH *271(H2 O)
HELIX 1 1 THR A 86 GLU A 97 1 12
HELIX 2 2 HIS A 105 SER A 113 1 9
HELIX 3 3 ARG A 116 ARG A 129 1 14
HELIX 4 4 ASP A 130 PHE A 135 1 6
HELIX 5 5 PRO A 138 HIS A 152 1 15
HELIX 6 6 ASN A 161 SER A 177 1 17
HELIX 7 7 THR A 178 GLU A 182 5 5
HELIX 8 8 THR A 186 HIS A 200 1 15
HELIX 9 9 SER A 208 THR A 215 1 8
HELIX 10 10 SER A 217 ASN A 224 1 8
HELIX 11 11 SER A 227 LEU A 240 1 14
HELIX 12 12 LEU A 241 GLU A 243 5 3
HELIX 13 13 THR A 253 ALA A 270 1 18
HELIX 14 14 THR A 271 SER A 274 5 4
HELIX 15 15 LYS A 275 THR A 289 1 15
HELIX 16 16 ASN A 302 LEU A 319 1 18
HELIX 17 17 SER A 320 LYS A 324 5 5
HELIX 18 18 PRO A 325 GLY A 351 1 27
HELIX 19 19 SER A 364 ILE A 376 1 13
HELIX 20 20 ILE A 376 VAL A 388 1 13
HELIX 21 21 ALA A 392 THR A 409 1 18
HELIX 22 22 GLN B 88 LEU B 96 1 9
HELIX 23 23 GLU B 97 VAL B 99 5 3
HELIX 24 24 HIS B 105 SER B 113 1 9
HELIX 25 25 ARG B 116 ARG B 129 1 14
HELIX 26 26 ASP B 130 PHE B 135 1 6
HELIX 27 27 PRO B 138 HIS B 152 1 15
HELIX 28 28 ASN B 161 SER B 177 1 17
HELIX 29 29 THR B 178 GLU B 182 5 5
HELIX 30 30 THR B 186 HIS B 200 1 15
HELIX 31 31 SER B 208 THR B 215 1 8
HELIX 32 32 SER B 217 TYR B 223 1 7
HELIX 33 33 SER B 227 LEU B 240 1 14
HELIX 34 34 LEU B 241 GLU B 243 5 3
HELIX 35 35 THR B 253 ALA B 270 1 18
HELIX 36 36 THR B 271 SER B 274 5 4
HELIX 37 37 LYS B 275 THR B 289 1 15
HELIX 38 38 ASN B 302 LEU B 319 1 18
HELIX 39 39 SER B 320 LYS B 324 5 5
HELIX 40 40 PRO B 325 ARG B 350 1 26
HELIX 41 41 SER B 364 ILE B 376 1 13
HELIX 42 42 ILE B 376 VAL B 388 1 13
HELIX 43 43 ALA B 392 ILE B 410 1 19
LINK NE2 HIS A 164 ZN ZN A1001 1555 1555 2.22
LINK NE2 HIS A 200 ZN ZN A1001 1555 1555 2.16
LINK OD2 ASP A 201 ZN ZN A1001 1555 1555 2.22
LINK OD1 ASP A 201 MG MG A1002 1555 1555 2.17
LINK OD1 ASP A 318 ZN ZN A1001 1555 1555 2.31
LINK ZN ZN A1001 O HOH A1009 1555 1555 2.15
LINK ZN ZN A1001 O HOH A1010 1555 1555 2.04
LINK MG MG A1002 O HOH A1005 1555 1555 2.24
LINK MG MG A1002 O HOH A1006 1555 1555 2.26
LINK MG MG A1002 O HOH A1007 1555 1555 2.04
LINK MG MG A1002 O HOH A1008 1555 1555 2.23
LINK MG MG A1002 O HOH A1009 1555 1555 2.15
LINK NE2 HIS B 164 ZN ZN B1001 1555 1555 2.28
LINK NE2 HIS B 200 ZN ZN B1001 1555 1555 2.18
LINK OD1 ASP B 201 ZN ZN B1001 1555 1555 2.23
LINK OD2 ASP B 201 MG MG B1002 1555 1555 2.08
LINK OD1 ASP B 318 ZN ZN B1001 1555 1555 2.19
LINK ZN ZN B1001 O HOH B2007 1555 1555 2.08
LINK ZN ZN B1001 O HOH B2008 1555 1555 2.11
LINK MG MG B1002 O HOH B2003 1555 1555 2.09
LINK MG MG B1002 O HOH B2004 1555 1555 2.12
LINK MG MG B1002 O HOH B2005 1555 1555 2.24
LINK MG MG B1002 O HOH B2006 1555 1555 2.13
LINK MG MG B1002 O HOH B2007 1555 1555 1.96
CISPEP 1 HIS A 389 PRO A 390 0 0.18
CISPEP 2 HIS B 389 PRO B 390 0 -1.33
SITE 1 AC1 7 HIS A 164 HIS A 200 ASP A 201 ASP A 318
SITE 2 AC1 7 MG A1002 HOH A1009 HOH A1010
SITE 1 AC2 7 ASP A 201 ZN A1001 HOH A1005 HOH A1006
SITE 2 AC2 7 HOH A1007 HOH A1008 HOH A1009
SITE 1 AC3 7 HIS B 164 HIS B 200 ASP B 201 ASP B 318
SITE 2 AC3 7 MG B1002 HOH B2007 HOH B2008
SITE 1 AC4 7 ASP B 201 ZN B1001 HOH B2003 HOH B2004
SITE 2 AC4 7 HOH B2005 HOH B2006 HOH B2007
SITE 1 AC5 13 TYR A 159 THR A 271 MET A 273 ASP A 318
SITE 2 AC5 13 LEU A 319 ASN A 321 THR A 333 ILE A 336
SITE 3 AC5 13 GLN A 369 PHE A 372 EDO A 444 HOH A1008
SITE 4 AC5 13 HOH A1023
SITE 1 AC6 11 HIS B 160 MET B 273 ASP B 318 LEU B 319
SITE 2 AC6 11 ASN B 321 THR B 333 MET B 357 GLN B 369
SITE 3 AC6 11 PHE B 372 HOH B2006 HOH B2060
SITE 1 AC7 4 PRO A 411 GLU B 366 TYR B 406 HOH B2061
SITE 1 AC8 4 LYS A 262 ILE A 265 ASP A 266 HOH A1026
SITE 1 AC9 2 GLN B 327 HOH B2126
SITE 1 BC1 5 SER B 208 PRO B 356 CYS B 358 HOH B2067
SITE 2 BC1 5 HOH B2143
SITE 1 BC2 4 ASN A 115 ASN A 162 ILE A 163 ARG A 335
SITE 1 BC3 6 LEU A 175 THR A 178 TRP A 384 ASP A 391
SITE 2 BC3 6 ALA A 392 ILE A 395
SITE 1 BC4 3 ARG B 257 ARG B 261 HOH B2090
SITE 1 BC5 5 ALA A 183 GLY B 114 ASN B 115 ARG B 116
SITE 2 BC5 5 HOH B2077
SITE 1 BC6 3 PHE A 238 ARG A 257 ARG A 261
SITE 1 BC7 4 SER A 208 PHE A 340 PRO A 356 HOH A1063
SITE 1 BC8 5 ALA B 158 GLU B 339 ARG B 342 HOH B2019
SITE 2 BC8 5 HOH B2072
SITE 1 BC9 4 HIS A 154 ASP A 203 PRO A 205 HIS A 232
SITE 1 CC1 5 ASN B 115 ALA B 155 ASN B 162 ILE B 163
SITE 2 CC1 5 HOH B2088
SITE 1 CC2 1 5DE A1003
CRYST1 60.880 79.442 164.265 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 0.016426 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006088 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
