HEADER HYDROLASE/HYDROLASE INHIBITOR 09-JUL-13 4LM0
TITLE CRYSTAL STRUCTURE OF PDE10A2 WITH FRAGMENT ZT448
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 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 439-779;
COMPND 6 EC: 3.1.4.17, 3.1.4.35;
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: PDE10A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS FRAGMENT SCREENING, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SRIDHAR,J.BADGER,C.LOGAN,B.CHIE-LEON,V.NIENABER
REVDAT 3 20-SEP-23 4LM0 1 REMARK SEQADV LINK
REVDAT 2 26-MAR-14 4LM0 1 JRNL
REVDAT 1 26-FEB-14 4LM0 0
JRNL AUTH M.I.RECHT,V.SRIDHAR,J.BADGER,P.Y.BOUNAUD,C.LOGAN,
JRNL AUTH 2 B.CHIE-LEON,V.NIENABER,F.E.TORRES
JRNL TITL IDENTIFICATION AND OPTIMIZATION OF PDE10A INHIBITORS USING
JRNL TITL 2 FRAGMENT-BASED SCREENING BY NANOCALORIMETRY AND X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY.
JRNL REF J BIOMOL SCREEN V. 19 497 2014
JRNL REFN ISSN 1087-0571
JRNL PMID 24375910
JRNL DOI 10.1177/1087057113516493
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 72469
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3835
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4728
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5245
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -0.12000
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): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.570
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5446 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7381 ; 1.373 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 655 ; 5.157 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;35.401 ;24.040
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 960 ;13.429 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 819 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4082 ; 0.008 ; 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): 3278 ; 1.115 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5323 ; 1.839 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2168 ; 2.334 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2058 ; 3.697 ; 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 : 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: NULL
REMARK 4
REMARK 4 4LM0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080797.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76392
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2OUR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 4450, 0.2M CALCIUM
REMARK 280 ACETATE,50MM BME, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 25.29900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.84350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.02050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.84350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.29900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.02050
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, 3
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A 445
REMARK 465 SER A 776
REMARK 465 SER A 777
REMARK 465 PRO A 778
REMARK 465 SER A 779
REMARK 465 VAL A 780
REMARK 465 ALA A 781
REMARK 465 GLN A 782
REMARK 465 LYS A 783
REMARK 465 ALA A 784
REMARK 465 ALA A 785
REMARK 465 ALA A 786
REMARK 465 SER A 787
REMARK 465 GLU A 788
REMARK 465 ASP A 789
REMARK 465 GLY B 445
REMARK 465 ALA B 446
REMARK 465 GLY B 447
REMARK 465 ILE B 775
REMARK 465 SER B 776
REMARK 465 SER B 777
REMARK 465 PRO B 778
REMARK 465 SER B 779
REMARK 465 VAL B 780
REMARK 465 ALA B 781
REMARK 465 GLN B 782
REMARK 465 LYS B 783
REMARK 465 ALA B 784
REMARK 465 ALA B 785
REMARK 465 ALA B 786
REMARK 465 SER B 787
REMARK 465 GLU B 788
REMARK 465 ASP B 789
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 453 OG
REMARK 470 GLU A 454 CG CD OE1 OE2
REMARK 470 LYS A 470 CD CE NZ
REMARK 470 GLU A 506 CD OE1 OE2
REMARK 470 ARG A 521 NE CZ NH1 NH2
REMARK 470 LYS A 577 CD CE NZ
REMARK 470 LYS A 643 CD CE NZ
REMARK 470 GLU A 647 CG CD OE1 OE2
REMARK 470 LYS A 753 CD CE NZ
REMARK 470 THR A 773 OG1 CG2
REMARK 470 ILE A 775 CG1 CG2 CD1
REMARK 470 GLU B 454 CG CD OE1 OE2
REMARK 470 GLU B 504 CG CD OE1 OE2
REMARK 470 ARG B 521 NE CZ NH1 NH2
REMARK 470 SER B 573 OG
REMARK 470 LYS B 577 CG CD CE NZ
REMARK 470 GLU B 606 CD OE1 OE2
REMARK 470 SER B 617 OG
REMARK 470 GLU B 620 CG CD OE1 OE2
REMARK 470 LYS B 643 CD CE NZ
REMARK 470 GLU B 721 CG CD OE1 OE2
REMARK 470 TRP B 774 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 774 CZ3 CH2
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 VAL A 733 -63.07 -126.30
REMARK 500 TYR B 524 -42.12 -130.59
REMARK 500 ASN B 544 28.67 -141.95
REMARK 500 ASP B 579 46.99 39.36
REMARK 500 LEU B 656 23.35 -77.01
REMARK 500 VAL B 733 -60.28 -125.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE FOUR DIVALENT CATIONS ARE REPRESENTED BY NI BUT THIS
REMARK 600 IDENTIFICATION IS SPECULATIVE
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 NI A 901 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 529 NE2
REMARK 620 2 HIS A 563 NE2 93.8
REMARK 620 3 ASP A 564 OD2 89.5 85.3
REMARK 620 4 ASP A 674 OD2 87.1 91.2 174.9
REMARK 620 5 HOH A1010 O 86.9 177.2 97.4 86.2
REMARK 620 6 HOH A1119 O 164.5 101.0 96.5 87.8 78.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 902 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 564 OD1
REMARK 620 2 HOH A1001 O 83.1
REMARK 620 3 HOH A1022 O 164.4 81.7
REMARK 620 4 HOH A1117 O 85.8 89.6 90.4
REMARK 620 5 HOH A1118 O 106.2 170.3 88.8 88.4
REMARK 620 6 HOH A1119 O 97.0 95.4 88.1 174.5 86.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 901 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 529 NE2
REMARK 620 2 HIS B 563 NE2 95.6
REMARK 620 3 ASP B 564 OD2 89.3 88.0
REMARK 620 4 ASP B 674 OD1 80.9 95.1 170.0
REMARK 620 5 HOH B1077 O 166.5 97.6 94.1 94.9
REMARK 620 6 HOH B1079 O 81.9 169.6 81.9 94.5 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 902 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 564 OD1
REMARK 620 2 HOH B1021 O 85.4
REMARK 620 3 HOH B1075 O 157.3 82.7
REMARK 620 4 HOH B1076 O 76.7 83.6 82.8
REMARK 620 5 HOH B1077 O 92.9 174.3 97.1 90.7
REMARK 620 6 HOH B1078 O 106.8 90.4 92.6 172.8 95.3
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 5NI A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LKQ RELATED DB: PDB
REMARK 900 RELATED ID: 4LLJ RELATED DB: PDB
REMARK 900 RELATED ID: 4LLL RELATED DB: PDB
REMARK 900 RELATED ID: 4LLP RELATED DB: PDB
REMARK 900 RELATED ID: 4LLX RELATED DB: PDB
REMARK 900 RELATED ID: 4LM1 RELATED DB: PDB
REMARK 900 RELATED ID: 4LM2 RELATED DB: PDB
REMARK 900 RELATED ID: 4LM3 RELATED DB: PDB
REMARK 900 RELATED ID: 4LM4 RELATED DB: PDB
DBREF 4LM0 A 449 789 UNP Q9Y233 PDE10_HUMAN 439 779
DBREF 4LM0 B 449 789 UNP Q9Y233 PDE10_HUMAN 439 779
SEQADV 4LM0 GLY A 445 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 ALA A 446 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 GLY A 447 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 THR A 448 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 GLY B 445 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 ALA B 446 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 GLY B 447 UNP Q9Y233 EXPRESSION TAG
SEQADV 4LM0 THR B 448 UNP Q9Y233 EXPRESSION TAG
SEQRES 1 A 345 GLY ALA GLY THR SER ILE CYS THR SER GLU GLU TRP GLN
SEQRES 2 A 345 GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS
SEQRES 3 A 345 GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU
SEQRES 4 A 345 ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG
SEQRES 5 A 345 SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS
SEQRES 6 A 345 ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL
SEQRES 7 A 345 PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS
SEQRES 8 A 345 CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE
SEQRES 9 A 345 THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU
SEQRES 10 A 345 CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR
SEQRES 11 A 345 LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER
SEQRES 12 A 345 THR SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL
SEQRES 13 A 345 SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR
SEQRES 14 A 345 LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE
SEQRES 15 A 345 ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE
SEQRES 16 A 345 GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY
SEQRES 17 A 345 SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL
SEQRES 18 A 345 ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL
SEQRES 19 A 345 THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP
SEQRES 20 A 345 ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS
SEQRES 21 A 345 LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP
SEQRES 22 A 345 LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR
SEQRES 23 A 345 ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN
SEQRES 24 A 345 ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG
SEQRES 25 A 345 ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU
SEQRES 26 A 345 GLU THR ALA THR TRP ILE SER SER PRO SER VAL ALA GLN
SEQRES 27 A 345 LYS ALA ALA ALA SER GLU ASP
SEQRES 1 B 345 GLY ALA GLY THR SER ILE CYS THR SER GLU GLU TRP GLN
SEQRES 2 B 345 GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS
SEQRES 3 B 345 GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU
SEQRES 4 B 345 ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG
SEQRES 5 B 345 SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS
SEQRES 6 B 345 ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL
SEQRES 7 B 345 PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS
SEQRES 8 B 345 CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE
SEQRES 9 B 345 THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU
SEQRES 10 B 345 CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR
SEQRES 11 B 345 LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER
SEQRES 12 B 345 THR SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL
SEQRES 13 B 345 SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR
SEQRES 14 B 345 LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE
SEQRES 15 B 345 ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE
SEQRES 16 B 345 GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY
SEQRES 17 B 345 SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL
SEQRES 18 B 345 ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL
SEQRES 19 B 345 THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP
SEQRES 20 B 345 ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS
SEQRES 21 B 345 LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP
SEQRES 22 B 345 LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR
SEQRES 23 B 345 ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN
SEQRES 24 B 345 ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG
SEQRES 25 B 345 ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU
SEQRES 26 B 345 GLU THR ALA THR TRP ILE SER SER PRO SER VAL ALA GLN
SEQRES 27 B 345 LYS ALA ALA ALA SER GLU ASP
HET 5NI A 900 12
HET NI A 901 1
HET NI A 902 1
HET NI B 901 1
HET NI B 902 1
HETNAM 5NI 5-NITROINDAZOLE
HETNAM NI NICKEL (II) ION
FORMUL 3 5NI C7 H5 N3 O2
FORMUL 4 NI 4(NI 2+)
FORMUL 8 HOH *375(H2 O)
HELIX 1 1 THR A 452 PHE A 462 1 11
HELIX 2 2 PRO A 465 GLU A 473 1 9
HELIX 3 3 ILE A 479 ASN A 484 5 6
HELIX 4 4 MET A 485 GLY A 499 1 15
HELIX 5 5 GLU A 504 ASN A 518 1 15
HELIX 6 6 ASN A 526 ASN A 544 1 19
HELIX 7 7 HIS A 545 PHE A 548 5 4
HELIX 8 8 THR A 549 HIS A 563 1 15
HELIX 9 9 SER A 571 PHE A 578 1 8
HELIX 10 10 HIS A 580 TYR A 586 1 7
HELIX 11 11 SER A 589 GLN A 604 1 16
HELIX 12 12 SER A 615 THR A 633 1 19
HELIX 13 13 ASP A 634 THR A 651 1 18
HELIX 14 14 ASN A 658 LEU A 675 1 18
HELIX 15 15 CYS A 676 LYS A 680 5 5
HELIX 16 16 LEU A 681 LEU A 706 1 26
HELIX 17 17 ILE A 711 ASP A 720 5 10
HELIX 18 18 GLU A 721 VAL A 733 1 13
HELIX 19 19 VAL A 733 LEU A 745 1 13
HELIX 20 20 THR A 748 ARG A 767 1 20
HELIX 21 21 THR B 452 GLN B 461 1 10
HELIX 22 22 PRO B 465 CYS B 469 5 5
HELIX 23 23 LYS B 470 LEU B 474 5 5
HELIX 24 24 ILE B 479 ASN B 484 5 6
HELIX 25 25 MET B 485 GLY B 499 1 15
HELIX 26 26 GLU B 504 ASN B 518 1 15
HELIX 27 27 ASN B 526 ASN B 543 1 18
HELIX 28 28 ASN B 544 PHE B 548 5 5
HELIX 29 29 THR B 549 HIS B 563 1 15
HELIX 30 30 SER B 571 PHE B 578 1 8
HELIX 31 31 HIS B 580 TYR B 586 1 7
HELIX 32 32 SER B 589 GLN B 604 1 16
HELIX 33 33 SER B 615 THR B 633 1 19
HELIX 34 34 ASP B 634 THR B 651 1 18
HELIX 35 35 ASN B 658 LEU B 675 1 18
HELIX 36 36 CYS B 676 LYS B 680 5 5
HELIX 37 37 LEU B 681 LYS B 686 1 6
HELIX 38 38 LEU B 687 ALA B 689 5 3
HELIX 39 39 ASN B 690 ILE B 692 5 3
HELIX 40 40 TYR B 693 LEU B 706 1 14
HELIX 41 41 ILE B 711 ASP B 715 5 5
HELIX 42 42 GLU B 721 VAL B 733 1 13
HELIX 43 43 VAL B 733 LEU B 745 1 13
HELIX 44 44 THR B 748 ARG B 767 1 20
LINK NE2 HIS A 529 NI NI A 901 1555 1555 2.21
LINK NE2 HIS A 563 NI NI A 901 1555 1555 2.19
LINK OD2 ASP A 564 NI NI A 901 1555 1555 2.15
LINK OD1 ASP A 564 NI NI A 902 1555 1555 2.19
LINK OD2 ASP A 674 NI NI A 901 1555 1555 2.11
LINK NI NI A 901 O HOH A1010 1555 1555 2.38
LINK NI NI A 901 O HOH A1119 1555 1555 2.07
LINK NI NI A 902 O HOH A1001 1555 1555 2.28
LINK NI NI A 902 O HOH A1022 1555 1555 2.36
LINK NI NI A 902 O HOH A1117 1555 1555 2.25
LINK NI NI A 902 O HOH A1118 1555 1555 2.25
LINK NI NI A 902 O HOH A1119 1555 1555 2.25
LINK NE2 HIS B 529 NI NI B 901 1555 1555 2.29
LINK NE2 HIS B 563 NI NI B 901 1555 1555 2.23
LINK OD2 ASP B 564 NI NI B 901 1555 1555 2.40
LINK OD1 ASP B 564 NI NI B 902 1555 1555 2.27
LINK OD1 ASP B 674 NI NI B 901 1555 1555 2.17
LINK NI NI B 901 O HOH B1077 1555 1555 1.96
LINK NI NI B 901 O HOH B1079 1555 1555 2.02
LINK NI NI B 902 O HOH B1021 1555 1555 2.33
LINK NI NI B 902 O HOH B1075 1555 1555 2.35
LINK NI NI B 902 O HOH B1076 1555 1555 2.24
LINK NI NI B 902 O HOH B1077 1555 1555 2.08
LINK NI NI B 902 O HOH B1078 1555 1555 2.09
SITE 1 AC1 6 LEU A 635 PHE A 696 GLN A 726 PHE A 729
SITE 2 AC1 6 LEU B 706 ILE B 708
SITE 1 AC2 6 HIS A 529 HIS A 563 ASP A 564 ASP A 674
SITE 2 AC2 6 HOH A1010 HOH A1119
SITE 1 AC3 6 ASP A 564 HOH A1001 HOH A1022 HOH A1117
SITE 2 AC3 6 HOH A1118 HOH A1119
SITE 1 AC4 7 HIS B 529 HIS B 563 ASP B 564 ASP B 674
SITE 2 AC4 7 NI B 902 HOH B1077 HOH B1079
SITE 1 AC5 7 ASP B 564 NI B 901 HOH B1021 HOH B1075
SITE 2 AC5 7 HOH B1076 HOH B1077 HOH B1078
CRYST1 50.598 82.041 155.687 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 0.019764 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012189 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006423 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
