HEADER HYDROLASE 12-DEC-06 2O8H
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF RAT PHOSPHODIESTERASE 10A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHODIESTERASE-10A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PDE10A2;
COMPND 6 EC: 3.1.4.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PDE10A, PDE10A;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PHOSPHODIESTERASE 10A; ZN-BINDING SITE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PANDIT,E.S.MARR
REVDAT 7 03-APR-24 2O8H 1 REMARK
REVDAT 6 27-DEC-23 2O8H 1 REMARK SEQADV LINK
REVDAT 5 18-OCT-17 2O8H 1 REMARK
REVDAT 4 24-FEB-09 2O8H 1 VERSN
REVDAT 3 27-FEB-07 2O8H 1 JRNL
REVDAT 2 13-FEB-07 2O8H 1 JRNL
REVDAT 1 09-JAN-07 2O8H 0
JRNL AUTH T.A.CHAPPIE,J.M.HUMPHREY,M.P.ALLEN,K.G.ESTEP,C.B.FOX,
JRNL AUTH 2 L.A.LEBEL,S.LIRAS,E.S.MARR,F.S.MENNITI,J.PANDIT,C.J.SCHMIDT,
JRNL AUTH 3 M.TU,R.D.WILLIAMS,F.V.YANG
JRNL TITL DISCOVERY OF A SERIES OF
JRNL TITL 2 6,7-DIMETHOXY-4-PYRROLIDYLQUINAZOLINE PDE10A INHIBITORS
JRNL REF J.MED.CHEM. V. 50 182 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17228859
JRNL DOI 10.1021/JM060653B
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 37822
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2905
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1437
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3850
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.4290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2491
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.27000
REMARK 3 B22 (A**2) : -2.27000
REMARK 3 B33 (A**2) : 3.40000
REMARK 3 B12 (A**2) : -1.13000
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): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.541
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2590 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2312 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3511 ; 1.476 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5384 ; 0.896 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 5.391 ; 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): 380 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2834 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 532 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 765 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2802 ; 0.245 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1393 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 194 ; 0.233 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.162 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.129 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.210 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.254 ; 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): 1532 ; 0.742 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2481 ; 1.312 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1058 ; 2.071 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1030 ; 3.245 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37865
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67500
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: AMORE
REMARK 200 STARTING MODEL: HOMOLOGY MODEL OF PDE10A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 60.31100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.82057
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.38100
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 60.31100
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 34.82057
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.38100
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 60.31100
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 34.82057
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.38100
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.64114
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 54.76200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.64114
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 54.76200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.64114
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 54.76200
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 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 MET A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 HIS A 427
REMARK 465 HIS A 428
REMARK 465 HIS A 429
REMARK 465 SER A 430
REMARK 465 SER A 431
REMARK 465 GLY A 432
REMARK 465 LEU A 433
REMARK 465 VAL A 434
REMARK 465 PRO A 435
REMARK 465 ARG A 436
REMARK 465 GLY A 437
REMARK 465 SER A 438
REMARK 465 ALA A 439
REMARK 465 MET A 440
REMARK 465 GLY A 441
REMARK 465 THR A 442
REMARK 465 SER A 443
REMARK 465 GLU A 444
REMARK 465 GLU A 445
REMARK 465 TRP A 446
REMARK 465 GLN A 447
REMARK 465 GLY A 448
REMARK 465 LEU A 449
REMARK 465 MET A 450
REMARK 465 HIS A 451
REMARK 465 PHE A 452
REMARK 465 ASN A 453
REMARK 465 THR A 761
REMARK 465 ALA A 762
REMARK 465 MET A 763
REMARK 465 TRP A 764
REMARK 465 ILE A 765
REMARK 465 SER A 766
REMARK 465 GLY A 767
REMARK 465 PRO A 768
REMARK 465 ALA A 769
REMARK 465 THR A 770
REMARK 465 SER A 771
REMARK 465 LYS A 772
REMARK 465 SER A 773
REMARK 465 THR A 774
REMARK 465 SER A 775
REMARK 465 GLU A 776
REMARK 465 LYS A 777
REMARK 465 PRO A 778
REMARK 465 THR A 779
REMARK 465 ARG A 780
REMARK 465 LYS A 781
REMARK 465 VAL A 782
REMARK 465 ASP A 783
REMARK 465 ASP A 784
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 307 O HOH A 309 1.75
REMARK 500 OE1 GLN A 588 O HOH A 306 2.03
REMARK 500 O HOH A 143 O HOH A 293 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 468 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 540 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 653 CB - CG - OD2 ANGL. DEV. = 5.9 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 CYS A 488 -61.93 -100.31
REMARK 500 TYR A 514 -53.76 -122.87
REMARK 500 ASN A 516 -168.75 -118.43
REMARK 500 ILE A 530 36.73 -91.05
REMARK 500 LEU A 531 -48.63 -136.36
REMARK 500 THR A 603 0.33 -69.00
REMARK 500 VAL A 723 -61.23 -126.05
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 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 126 O
REMARK 620 2 HOH A 159 O 81.9
REMARK 620 3 HOH A 260 O 81.9 89.5
REMARK 620 4 HOH A 308 O 156.8 96.6 121.3
REMARK 620 5 ASP A 554 OD1 93.9 172.6 96.0 84.8
REMARK 620 N 1 2 3 4
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 A 308 O
REMARK 620 2 HIS A 519 NE2 151.8
REMARK 620 3 HIS A 553 NE2 99.7 108.4
REMARK 620 4 ASP A 554 OD2 87.2 94.0 82.5
REMARK 620 5 ASP A 664 OD1 89.9 89.5 95.9 176.5
REMARK 620 N 1 2 3 4
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 227 A 999
DBREF 2O8H A 442 784 UNP Q9QYJ6 Q9QYJ6_RAT 452 794
SEQADV 2O8H MET A 423 UNP Q9QYJ6 INITIATING METHIONINE
SEQADV 2O8H HIS A 424 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H HIS A 425 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H HIS A 426 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H HIS A 427 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H HIS A 428 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H HIS A 429 UNP Q9QYJ6 EXPRESSION TAG
SEQADV 2O8H SER A 430 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H SER A 431 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H GLY A 432 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H LEU A 433 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H VAL A 434 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H PRO A 435 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H ARG A 436 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H GLY A 437 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H SER A 438 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H ALA A 439 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H MET A 440 UNP Q9QYJ6 CLONING ARTIFACT
SEQADV 2O8H GLY A 441 UNP Q9QYJ6 CLONING ARTIFACT
SEQRES 1 A 362 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 362 ARG GLY SER ALA MET GLY THR SER GLU GLU TRP GLN GLY
SEQRES 3 A 362 LEU MET HIS PHE ASN LEU PRO ALA ARG ILE CYS ARG ASP
SEQRES 4 A 362 ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU ASN
SEQRES 5 A 362 MET TRP PRO GLY ILE PHE VAL TYR MET ILE HIS ARG SER
SEQRES 6 A 362 CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS ARG
SEQRES 7 A 362 PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL PRO
SEQRES 8 A 362 TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS CYS
SEQRES 9 A 362 MET TYR ALA ILE LEU GLN ASN ASN ASN GLY LEU PHE THR
SEQRES 10 A 362 ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU CYS
SEQRES 11 A 362 HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR LEU
SEQRES 12 A 362 GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER THR
SEQRES 13 A 362 SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL SER
SEQRES 14 A 362 ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR LEU
SEQRES 15 A 362 SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE ARG
SEQRES 16 A 362 LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE GLY
SEQRES 17 A 362 ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY SER
SEQRES 18 A 362 LEU ASN LEU HIS ASN GLN SER HIS ARG ASP ARG VAL ILE
SEQRES 19 A 362 GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL THR
SEQRES 20 A 362 LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP ILE
SEQRES 21 A 362 TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS LYS
SEQRES 22 A 362 LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP LYS
SEQRES 23 A 362 ARG ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR ASN
SEQRES 24 A 362 ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN ILE
SEQRES 25 A 362 LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG ASP
SEQRES 26 A 362 ASN LEU ASN GLN TRP GLU LYS VAL ILE ARG GLY GLU GLU
SEQRES 27 A 362 THR ALA MET TRP ILE SER GLY PRO ALA THR SER LYS SER
SEQRES 28 A 362 THR SER GLU LYS PRO THR ARG LYS VAL ASP ASP
HET ZN A1001 1
HET MG A1002 1
HET 227 A 999 34
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM 227 6,7-DIMETHOXY-4-{8-[(4-METHYLPIPERAZIN-1-YL)SULFONYL]-
HETNAM 2 227 3,4-DIHYDROISOQUINOLIN-2(1H)-YL}QUINAZOLINE
FORMUL 2 ZN ZN 2+
FORMUL 3 MG MG 2+
FORMUL 4 227 C24 H29 N5 O4 S
FORMUL 5 HOH *312(H2 O)
HELIX 1 1 PRO A 455 ILE A 462 1 8
HELIX 2 2 PHE A 472 ASN A 474 5 3
HELIX 3 3 MET A 475 CYS A 488 1 14
HELIX 4 4 GLU A 494 ASN A 508 1 15
HELIX 5 5 ASN A 516 ASN A 533 1 18
HELIX 6 6 THR A 539 HIS A 553 1 15
HELIX 7 7 SER A 561 ASP A 569 1 9
HELIX 8 8 HIS A 570 TYR A 576 1 7
HELIX 9 9 SER A 579 LEU A 595 1 17
HELIX 10 10 SER A 605 THR A 623 1 19
HELIX 11 11 ASP A 624 THR A 641 1 18
HELIX 12 12 ASN A 648 LEU A 665 1 18
HELIX 13 13 CYS A 666 LYS A 670 5 5
HELIX 14 14 LEU A 671 LYS A 695 1 25
HELIX 15 15 ILE A 701 ASP A 710 5 10
HELIX 16 16 GLU A 711 VAL A 723 1 13
HELIX 17 17 VAL A 723 LEU A 735 1 13
HELIX 18 18 THR A 738 ARG A 757 1 20
LINK O HOH A 126 MG MG A1002 1555 1555 2.78
LINK O HOH A 159 MG MG A1002 1555 1555 2.36
LINK O HOH A 260 MG MG A1002 1555 1555 1.97
LINK O HOH A 308 ZN ZN A1001 1555 1555 1.72
LINK O HOH A 308 MG MG A1002 1555 1555 2.42
LINK NE2 HIS A 519 ZN ZN A1001 1555 1555 1.96
LINK NE2 HIS A 553 ZN ZN A1001 1555 1555 2.14
LINK OD2 ASP A 554 ZN ZN A1001 1555 1555 2.05
LINK OD1 ASP A 554 MG MG A1002 1555 1555 1.93
LINK OD1 ASP A 664 ZN ZN A1001 1555 1555 2.17
SITE 1 AC1 5 HOH A 308 HIS A 519 HIS A 553 ASP A 554
SITE 2 AC1 5 ASP A 664
SITE 1 AC2 5 HOH A 126 HOH A 159 HOH A 260 HOH A 308
SITE 2 AC2 5 ASP A 554
SITE 1 AC3 13 HOH A 34 HOH A 39 HOH A 78 HOH A 186
SITE 2 AC3 13 LEU A 625 PHE A 629 VAL A 668 TYR A 683
SITE 3 AC3 13 PHE A 686 MET A 703 GLN A 716 PHE A 719
SITE 4 AC3 13 VAL A 723
CRYST1 120.622 120.622 82.143 90.00 90.00 120.00 H 3 9
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 0.008290 0.004786 0.000000 0.00000
SCALE2 0.000000 0.009573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012174 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
