HEADER HYDROLASE/HYDROLASE INHIBITOR 04-OCT-12 4HF4
TITLE CRYSTAL STRUCTURE OF PDE10A WITH A BIARYL ETHER INHIBITOR (1-(1-(3-(4-
TITLE 2 (BENZO[D]THIAZOL-2-YLAMINO)PHENOXY)PYRAZIN-2-YL)PIPERIDIN-4-YL)
TITLE 3 ETHANOL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND 3 10A;
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 3.1.4.17, 3.1.4.35;
COMPND 6 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: PDE10A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PDE10A, PHOSPHODIESTERASE 10A, BIARYL ETHERS, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHMAIT,S.JORDAN
REVDAT 1 12-DEC-12 4HF4 0
JRNL AUTH R.M.RZASA,E.HU,S.RUMFELT,N.CHEN,K.L.ANDREWS,S.CHMAIT,
JRNL AUTH 2 J.R.FALSEY,W.ZHONG,A.D.JONES,A.PORTER,S.W.LOUIE,X.ZHAO,
JRNL AUTH 3 J.J.TREANOR,J.R.ALLEN
JRNL TITL DISCOVERY OF SELECTIVE BIARYL ETHERS AS PDE10A INHIBITORS:
JRNL TITL 2 IMPROVEMENT IN POTENCY AND MITIGATION OF PGP-MEDIATED
JRNL TITL 3 EFFLUX.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 7371 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 23149228
JRNL DOI 10.1016/J.BMCL.2012.10.078
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 85049
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4482
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.1460
REMARK 3 BIN FREE R VALUE SET COUNT : 299
REMARK 3 BIN FREE R VALUE : 0.1530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5081
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.001
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5346 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7250 ; 1.066 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 624 ; 4.074 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 247 ;35.191 ;24.049
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 924 ;12.159 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.015 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 795 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3980 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 442 A 759
REMARK 3 RESIDUE RANGE : A 1001 A 1009
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2927 90.5080 29.9806
REMARK 3 T TENSOR
REMARK 3 T11: 0.0425 T22: 0.0162
REMARK 3 T33: 0.0456 T12: -0.0152
REMARK 3 T13: 0.0182 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.9728 L22: 0.4965
REMARK 3 L33: 0.4046 L12: 0.1106
REMARK 3 L13: 0.0423 L23: 0.0903
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: -0.0081 S13: -0.0626
REMARK 3 S21: 0.0463 S22: -0.0167 S23: 0.0098
REMARK 3 S31: 0.0186 S32: -0.0165 S33: 0.0126
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 452 B 759
REMARK 3 RESIDUE RANGE : A 1010 A 1010
REMARK 3 RESIDUE RANGE : B 801 B 809
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1036 58.6113 30.0842
REMARK 3 T TENSOR
REMARK 3 T11: 0.0288 T22: 0.0621
REMARK 3 T33: 0.0312 T12: -0.0213
REMARK 3 T13: 0.0169 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.7099 L22: 0.9818
REMARK 3 L33: 0.3376 L12: 0.1661
REMARK 3 L13: 0.0835 L23: 0.0449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0563 S13: -0.0341
REMARK 3 S21: -0.0538 S22: 0.0080 S23: -0.0325
REMARK 3 S31: -0.0116 S32: 0.0110 S33: -0.0079
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4HF4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB075387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0001
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89599
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 9.2.10
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.1M MES
REMARK 280 MONOHYDRATE, 10% V/V 1,4-DIOXANE, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z+1/2
REMARK 290 15555 -X,Y+1/2,-Z+1/2
REMARK 290 16555 X,-Y+1/2,-Z+1/2
REMARK 290 17555 Z,X+1/2,Y+1/2
REMARK 290 18555 Z,-X+1/2,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y+1/2
REMARK 290 20555 -Z,X+1/2,-Y+1/2
REMARK 290 21555 Y,Z+1/2,X+1/2
REMARK 290 22555 -Y,Z+1/2,-X+1/2
REMARK 290 23555 Y,-Z+1/2,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X+1/2
REMARK 290 25555 X+1/2,Y,Z+1/2
REMARK 290 26555 -X+1/2,-Y,Z+1/2
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X,Y+1/2
REMARK 290 30555 Z+1/2,-X,-Y+1/2
REMARK 290 31555 -Z+1/2,-X,Y+1/2
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y+1/2,Z,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z,-X+1/2
REMARK 290 36555 -Y+1/2,-Z,X+1/2
REMARK 290 37555 X+1/2,Y+1/2,Z
REMARK 290 38555 -X+1/2,-Y+1/2,Z
REMARK 290 39555 -X+1/2,Y+1/2,-Z
REMARK 290 40555 X+1/2,-Y+1/2,-Z
REMARK 290 41555 Z+1/2,X+1/2,Y
REMARK 290 42555 Z+1/2,-X+1/2,-Y
REMARK 290 43555 -Z+1/2,-X+1/2,Y
REMARK 290 44555 -Z+1/2,X+1/2,-Y
REMARK 290 45555 Y+1/2,Z+1/2,X
REMARK 290 46555 -Y+1/2,Z+1/2,-X
REMARK 290 47555 Y+1/2,-Z+1/2,-X
REMARK 290 48555 -Y+1/2,-Z+1/2,X
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 126.43950
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 126.43950
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 126.43950
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 126.43950
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 126.43950
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -261.0 KCAL/MOL
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 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 126.43950
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 126.43950
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 126.43950
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 126.43950
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -264.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1183 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1308 LIES ON A SPECIAL POSITION.
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 THR B 442
REMARK 465 SER B 443
REMARK 465 GLU B 444
REMARK 465 GLU B 445
REMARK 465 TRP B 446
REMARK 465 GLN B 447
REMARK 465 GLY B 448
REMARK 465 LEU B 449
REMARK 465 MET B 450
REMARK 465 GLN B 451
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 514 -51.49 -123.84
REMARK 500 ASP A 569 47.75 72.64
REMARK 500 TYR B 514 -51.72 -122.99
REMARK 500 ASN B 534 34.33 -140.34
REMARK 500 ASP B 569 46.26 70.63
REMARK 500 VAL B 723 -61.37 -120.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1292 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH B1098 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH B1126 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B1143 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH B1181 DISTANCE = 6.93 ANGSTROMS
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 B 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 910 O
REMARK 620 2 ASP B 554 OD1 94.2
REMARK 620 3 HOH B 969 O 95.2 83.2
REMARK 620 4 HOH B 972 O 93.0 167.5 86.0
REMARK 620 5 HOH B 951 O 89.8 104.6 170.4 85.6
REMARK 620 6 HOH B 949 O 175.0 89.6 88.5 83.9 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1220 O
REMARK 620 2 HOH A1185 O 95.4
REMARK 620 3 ASP A 554 OD1 93.8 85.0
REMARK 620 4 HOH A1107 O 89.1 170.2 103.3
REMARK 620 5 HOH A1190 O 91.5 87.0 170.9 84.2
REMARK 620 6 HOH A1166 O 174.3 89.3 89.8 85.7 85.6
REMARK 620 N 1 2 3 4 5
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 HOH A1220 O
REMARK 620 2 ASP A 554 OD2 91.0
REMARK 620 3 HIS A 553 NE2 96.2 87.4
REMARK 620 4 ASP A 664 OD1 92.6 175.2 89.0
REMARK 620 5 HOH A1103 O 81.3 98.2 174.0 85.6
REMARK 620 6 HIS A 519 NE2 169.7 90.8 94.0 86.2 88.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 664 OD1
REMARK 620 2 ASP B 554 OD2 174.9
REMARK 620 3 HOH B 910 O 91.7 88.8
REMARK 620 4 HIS B 553 NE2 88.3 86.6 97.5
REMARK 620 5 HIS B 519 NE2 92.5 87.8 170.1 91.6
REMARK 620 6 HOH B 909 O 86.8 98.3 81.0 174.8 90.3
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 ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15H A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15H B 810
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DDL RELATED DB: PDB
REMARK 900 RELATED ID: 4HEU RELATED DB: PDB
DBREF 4HF4 A 442 759 UNP Q9Y233 PDE10_HUMAN 442 759
DBREF 4HF4 B 442 759 UNP Q9Y233 PDE10_HUMAN 442 759
SEQRES 1 A 318 THR SER GLU GLU TRP GLN GLY LEU MET GLN PHE THR LEU
SEQRES 2 A 318 PRO VAL ARG LEU CYS LYS GLU ILE GLU LEU PHE HIS PHE
SEQRES 3 A 318 ASP ILE GLY PRO PHE GLU ASN MET TRP PRO GLY ILE PHE
SEQRES 4 A 318 VAL TYR MET VAL HIS ARG SER CYS GLY THR SER CYS PHE
SEQRES 5 A 318 GLU LEU GLU LYS LEU CYS ARG PHE ILE MET SER VAL LYS
SEQRES 6 A 318 LYS ASN TYR ARG ARG VAL PRO TYR HIS ASN TRP LYS HIS
SEQRES 7 A 318 ALA VAL THR VAL ALA HIS CYS MET TYR ALA ILE LEU GLN
SEQRES 8 A 318 ASN ASN HIS THR LEU PHE THR ASP LEU GLU ARG LYS GLY
SEQRES 9 A 318 LEU LEU ILE ALA CYS LEU CYS HIS ASP LEU ASP HIS ARG
SEQRES 10 A 318 GLY PHE SER ASN SER TYR LEU GLN LYS PHE ASP HIS PRO
SEQRES 11 A 318 LEU ALA ALA LEU TYR SER THR SER THR MET GLU GLN HIS
SEQRES 12 A 318 HIS PHE SER GLN THR VAL SER ILE LEU GLN LEU GLU GLY
SEQRES 13 A 318 HIS ASN ILE PHE SER THR LEU SER SER SER GLU TYR GLU
SEQRES 14 A 318 GLN VAL LEU GLU ILE ILE ARG LYS ALA ILE ILE ALA THR
SEQRES 15 A 318 ASP LEU ALA LEU TYR PHE GLY ASN ARG LYS GLN LEU GLU
SEQRES 16 A 318 GLU MET TYR GLN THR GLY SER LEU ASN LEU ASN ASN GLN
SEQRES 17 A 318 SER HIS ARG ASP ARG VAL ILE GLY LEU MET MET THR ALA
SEQRES 18 A 318 CYS ASP LEU CYS SER VAL THR LYS LEU TRP PRO VAL THR
SEQRES 19 A 318 LYS LEU THR ALA ASN ASP ILE TYR ALA GLU PHE TRP ALA
SEQRES 20 A 318 GLU GLY ASP GLU MET LYS LYS LEU GLY ILE GLN PRO ILE
SEQRES 21 A 318 PRO MET MET ASP ARG ASP LYS LYS ASP GLU VAL PRO GLN
SEQRES 22 A 318 GLY GLN LEU GLY PHE TYR ASN ALA VAL ALA ILE PRO CYS
SEQRES 23 A 318 TYR THR THR LEU THR GLN ILE LEU PRO PRO THR GLU PRO
SEQRES 24 A 318 LEU LEU LYS ALA CYS ARG ASP ASN LEU SER GLN TRP GLU
SEQRES 25 A 318 LYS VAL ILE ARG GLY GLU
SEQRES 1 B 318 THR SER GLU GLU TRP GLN GLY LEU MET GLN PHE THR LEU
SEQRES 2 B 318 PRO VAL ARG LEU CYS LYS GLU ILE GLU LEU PHE HIS PHE
SEQRES 3 B 318 ASP ILE GLY PRO PHE GLU ASN MET TRP PRO GLY ILE PHE
SEQRES 4 B 318 VAL TYR MET VAL HIS ARG SER CYS GLY THR SER CYS PHE
SEQRES 5 B 318 GLU LEU GLU LYS LEU CYS ARG PHE ILE MET SER VAL LYS
SEQRES 6 B 318 LYS ASN TYR ARG ARG VAL PRO TYR HIS ASN TRP LYS HIS
SEQRES 7 B 318 ALA VAL THR VAL ALA HIS CYS MET TYR ALA ILE LEU GLN
SEQRES 8 B 318 ASN ASN HIS THR LEU PHE THR ASP LEU GLU ARG LYS GLY
SEQRES 9 B 318 LEU LEU ILE ALA CYS LEU CYS HIS ASP LEU ASP HIS ARG
SEQRES 10 B 318 GLY PHE SER ASN SER TYR LEU GLN LYS PHE ASP HIS PRO
SEQRES 11 B 318 LEU ALA ALA LEU TYR SER THR SER THR MET GLU GLN HIS
SEQRES 12 B 318 HIS PHE SER GLN THR VAL SER ILE LEU GLN LEU GLU GLY
SEQRES 13 B 318 HIS ASN ILE PHE SER THR LEU SER SER SER GLU TYR GLU
SEQRES 14 B 318 GLN VAL LEU GLU ILE ILE ARG LYS ALA ILE ILE ALA THR
SEQRES 15 B 318 ASP LEU ALA LEU TYR PHE GLY ASN ARG LYS GLN LEU GLU
SEQRES 16 B 318 GLU MET TYR GLN THR GLY SER LEU ASN LEU ASN ASN GLN
SEQRES 17 B 318 SER HIS ARG ASP ARG VAL ILE GLY LEU MET MET THR ALA
SEQRES 18 B 318 CYS ASP LEU CYS SER VAL THR LYS LEU TRP PRO VAL THR
SEQRES 19 B 318 LYS LEU THR ALA ASN ASP ILE TYR ALA GLU PHE TRP ALA
SEQRES 20 B 318 GLU GLY ASP GLU MET LYS LYS LEU GLY ILE GLN PRO ILE
SEQRES 21 B 318 PRO MET MET ASP ARG ASP LYS LYS ASP GLU VAL PRO GLN
SEQRES 22 B 318 GLY GLN LEU GLY PHE TYR ASN ALA VAL ALA ILE PRO CYS
SEQRES 23 B 318 TYR THR THR LEU THR GLN ILE LEU PRO PRO THR GLU PRO
SEQRES 24 B 318 LEU LEU LYS ALA CYS ARG ASP ASN LEU SER GLN TRP GLU
SEQRES 25 B 318 LYS VAL ILE ARG GLY GLU
HET ZN A1001 1
HET ZN A1002 1
HET SO4 A1003 5
HET SO4 A1004 5
HET SO4 A1005 5
HET SO4 A1006 5
HET SO4 A1007 5
HET SO4 A1008 5
HET SO4 A1009 5
HET SO4 A1010 5
HET GOL A1011 6
HET 15H A1012 32
HET ZN B 801 1
HET ZN B 802 1
HET SO4 B 803 5
HET SO4 B 804 5
HET SO4 B 805 5
HET SO4 B 806 5
HET SO4 B 807 5
HET SO4 B 808 5
HET SO4 B 809 5
HET 15H B 810 32
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM 15H (1S)-1-(1-{3-[4-(1,3-BENZOTHIAZOL-2-YLAMINO)
HETNAM 2 15H PHENOXY]PYRAZIN-2-YL}PIPERIDIN-4-YL)ETHANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 SO4 15(O4 S 2-)
FORMUL 13 GOL C3 H8 O3
FORMUL 14 15H 2(C24 H25 N5 O2 S)
FORMUL 25 HOH *515(H2 O)
HELIX 1 1 THR A 442 MET A 450 1 9
HELIX 2 2 PRO A 455 ILE A 462 1 8
HELIX 3 3 PHE A 472 ASN A 474 5 3
HELIX 4 4 MET A 475 CYS A 488 1 14
HELIX 5 5 GLU A 494 ASN A 508 1 15
HELIX 6 6 ASN A 516 ASN A 534 1 19
HELIX 7 7 THR A 539 HIS A 553 1 15
HELIX 8 8 SER A 561 ASP A 569 1 9
HELIX 9 9 HIS A 570 TYR A 576 1 7
HELIX 10 10 SER A 579 GLN A 594 1 16
HELIX 11 11 SER A 605 THR A 623 1 19
HELIX 12 12 ASP A 624 GLY A 642 1 19
HELIX 13 13 ASN A 648 LEU A 665 1 18
HELIX 14 14 CYS A 666 LYS A 670 5 5
HELIX 15 15 LEU A 671 LEU A 696 1 26
HELIX 16 16 ILE A 701 ASP A 710 5 10
HELIX 17 17 GLU A 711 VAL A 723 1 13
HELIX 18 18 VAL A 723 LEU A 735 1 13
HELIX 19 19 THR A 738 GLY A 758 1 21
HELIX 20 20 PRO B 455 ILE B 462 1 8
HELIX 21 21 PHE B 472 ASN B 474 5 3
HELIX 22 22 MET B 475 CYS B 488 1 14
HELIX 23 23 GLU B 494 ASN B 508 1 15
HELIX 24 24 ASN B 516 ASN B 534 1 19
HELIX 25 25 HIS B 535 PHE B 538 5 4
HELIX 26 26 THR B 539 HIS B 553 1 15
HELIX 27 27 SER B 561 ASP B 569 1 9
HELIX 28 28 HIS B 570 TYR B 576 1 7
HELIX 29 29 SER B 579 GLN B 594 1 16
HELIX 30 30 SER B 605 ALA B 622 1 18
HELIX 31 31 ASP B 624 THR B 641 1 18
HELIX 32 32 ASN B 648 LEU B 665 1 18
HELIX 33 33 CYS B 666 LYS B 670 5 5
HELIX 34 34 LEU B 671 LEU B 696 1 26
HELIX 35 35 ILE B 701 ASP B 710 5 10
HELIX 36 36 GLU B 711 VAL B 723 1 13
HELIX 37 37 VAL B 723 LEU B 735 1 13
HELIX 38 38 THR B 738 GLY B 758 1 21
SSBOND 1 CYS A 488 CYS A 492 1555 1555 2.03
SSBOND 2 CYS B 488 CYS B 492 1555 1555 2.04
LINK ZN ZN B 802 O HOH B 910 1555 1555 1.96
LINK ZN ZN A1002 O HOH A1220 1555 1555 1.99
LINK ZN ZN A1001 O HOH A1220 1555 1555 2.06
LINK ZN ZN A1002 O HOH A1185 1555 1555 2.09
LINK OD2 ASP A 554 ZN ZN A1001 1555 1555 2.11
LINK OD1 ASP B 664 ZN ZN B 801 1555 1555 2.11
LINK OD2 ASP B 554 ZN ZN B 801 1555 1555 2.12
LINK ZN ZN B 801 O HOH B 910 1555 1555 2.13
LINK OD1 ASP A 554 ZN ZN A1002 1555 1555 2.13
LINK OD1 ASP B 554 ZN ZN B 802 1555 1555 2.14
LINK ZN ZN B 802 O HOH B 969 1555 1555 2.14
LINK NE2 HIS B 553 ZN ZN B 801 1555 1555 2.16
LINK ZN ZN A1002 O HOH A1107 1555 1555 2.16
LINK NE2 HIS A 553 ZN ZN A1001 1555 1555 2.16
LINK ZN ZN A1002 O HOH A1190 1555 1555 2.19
LINK OD1 ASP A 664 ZN ZN A1001 1555 1555 2.19
LINK ZN ZN B 802 O HOH B 972 1555 1555 2.20
LINK NE2 HIS B 519 ZN ZN B 801 1555 1555 2.20
LINK ZN ZN A1002 O HOH A1166 1555 1555 2.22
LINK ZN ZN B 802 O HOH B 951 1555 1555 2.24
LINK ZN ZN A1001 O HOH A1103 1555 1555 2.25
LINK ZN ZN B 802 O HOH B 949 1555 1555 2.26
LINK NE2 HIS A 519 ZN ZN A1001 1555 1555 2.26
LINK ZN ZN B 801 O HOH B 909 1555 1555 2.34
SITE 1 AC1 7 HIS A 519 HIS A 553 ASP A 554 ASP A 664
SITE 2 AC1 7 ZN A1002 HOH A1103 HOH A1220
SITE 1 AC2 7 ASP A 554 ZN A1001 HOH A1107 HOH A1166
SITE 2 AC2 7 HOH A1185 HOH A1190 HOH A1220
SITE 1 AC3 6 PHE A 472 GLU A 473 ASN A 474 ARG A 510
SITE 2 AC3 6 ARG A 558 HOH A1296
SITE 1 AC4 5 LYS A 497 GLY A 597 HIS A 598 ASN A 599
SITE 2 AC4 5 HOH A1132
SITE 1 AC5 6 VAL A 512 PRO A 513 ARG A 558 GLY A 559
SITE 2 AC5 6 GLU A 685 ALA A 688
SITE 1 AC6 7 LEU A 537 LEU A 646 ASN A 647 ARG A 652
SITE 2 AC6 7 LEU B 537 ASN B 647 ARG B 652
SITE 1 AC7 2 ARG A 510 ARG A 511
SITE 1 AC8 5 LEU A 575 TYR A 576 SER A 577 THR A 578
SITE 2 AC8 5 GLN A 583
SITE 1 AC9 4 ASN A 508 GLN A 588 SER A 591 ILE A 592
SITE 1 BC1 7 ARG A 486 GLN A 532 HIS A 535 HOH A1211
SITE 2 BC1 7 HOH A1276 THR B 641 GLY B 642
SITE 1 BC2 3 SER A 650 HIS A 651 ARG A 654
SITE 1 BC3 15 TYR A 514 LEU A 665 VAL A 668 ILE A 682
SITE 2 BC3 15 TYR A 683 PHE A 686 PRO A 702 MET A 703
SITE 3 BC3 15 LYS A 708 GLU A 711 GLY A 715 GLN A 716
SITE 4 BC3 15 PHE A 719 HOH A1268 HOH A1290
SITE 1 BC4 7 HIS B 519 HIS B 553 ASP B 554 ASP B 664
SITE 2 BC4 7 ZN B 802 HOH B 909 HOH B 910
SITE 1 BC5 7 ASP B 554 ZN B 801 HOH B 910 HOH B 949
SITE 2 BC5 7 HOH B 951 HOH B 969 HOH B 972
SITE 1 BC6 7 PHE B 472 GLU B 473 ASN B 474 ARG B 510
SITE 2 BC6 7 ARG B 558 HIS B 570 HOH B1055
SITE 1 BC7 3 ARG B 510 ARG B 511 HOH B1176
SITE 1 BC8 6 PRO B 673 GLY B 697 ILE B 698 GLN B 699
SITE 2 BC8 6 HOH B1001 HOH B1169
SITE 1 BC9 6 LYS B 497 GLY B 597 HIS B 598 ASN B 599
SITE 2 BC9 6 HOH B1077 HOH B1078
SITE 1 CC1 4 ASN A 645 THR B 539 ASP B 540 HOH B1122
SITE 1 CC2 4 ASN B 508 GLN B 588 SER B 591 ILE B 592
SITE 1 CC3 6 VAL B 512 PRO B 513 ARG B 558 GLY B 559
SITE 2 CC3 6 GLU B 685 ALA B 688
SITE 1 CC4 16 ASP B 664 LEU B 665 SER B 667 VAL B 668
SITE 2 CC4 16 ILE B 682 TYR B 683 PHE B 686 PRO B 702
SITE 3 CC4 16 MET B 703 LYS B 708 GLU B 711 VAL B 712
SITE 4 CC4 16 GLY B 715 GLN B 716 PHE B 719 HOH B1041
CRYST1 252.879 252.879 252.879 90.00 90.00 90.00 F 2 3 96
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 0.003954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
