HEADER HYDROLASE 21-OCT-15 5EDH
TITLE HUMAN PDE10A, 8-ETHYL-5-METHYL-2-[2-(2-METHYL-5-PYRROLIDIN-1-YL-1,2,4-
TITLE 2 TRIAZOL-3-YL)ETHYL]-[1,2,4]TRIAZOLO[1,5-C]PYRIMIDINE, 2.03A, H3,
TITLE 3 RFREE=22.7%
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND 3 10A;
COMPND 4 CHAIN: A, B, C, D;
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PHOSPHODIESTERASE, PDE10, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.JOSEPH,M.G.RUDOLPH
REVDAT 2 25-MAY-16 5EDH 1 JRNL
REVDAT 1 09-MAR-16 5EDH 0
JRNL AUTH B.KUHN,W.GUBA,J.HERT,D.BANNER,C.BISSANTZ,S.CECCARELLI,
JRNL AUTH 2 W.HAAP,M.KORNER,A.KUGLSTATTER,C.LERNER,P.MATTEI,W.NEIDHART,
JRNL AUTH 3 E.PINARD,M.G.RUDOLPH,T.SCHULZ-GASCH,T.WOLTERING,M.STAHL
JRNL TITL A REAL-WORLD PERSPECTIVE ON MOLECULAR DESIGN.
JRNL REF J.MED.CHEM. V. 59 4087 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26878596
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01875
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 95000
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10163
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 526
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : 1.20000
REMARK 3 B12 (A**2) : -0.37000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.759
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5EDH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103725
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 43.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.170
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.05
REMARK 200 R MERGE FOR SHELL (I) : 0.74200
REMARK 200 R SYM FOR SHELL (I) : 0.74200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES-NAOH PH 7.5, 30%
REMARK 280 PEG550MME, 50MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 67.70050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.08690
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.44500
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 67.70050
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 39.08690
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 78.44500
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 67.70050
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 39.08690
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.44500
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.17380
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 156.89000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 78.17380
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 156.89000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 78.17380
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 156.89000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ALA A 456
REMARK 465 ALA A 457
REMARK 465 GLY A 458
REMARK 465 ALA A 771
REMARK 465 ALA B 456
REMARK 465 ALA C 456
REMARK 465 ALA C 457
REMARK 465 ALA C 771
REMARK 465 GLU D 769
REMARK 465 GLU D 770
REMARK 465 ALA D 771
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 B 1031 O HOH B 1040 2.09
REMARK 500 O HOH B 1026 O HOH C 1036 2.10
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 498 -47.33 -132.32
REMARK 500 TYR A 524 -53.47 -121.71
REMARK 500 ASP A 579 46.73 71.78
REMARK 500 VAL A 733 -62.10 -124.61
REMARK 500 TYR B 524 -54.10 -122.43
REMARK 500 VAL B 733 -62.52 -125.98
REMARK 500 PRO C 465 156.16 -47.29
REMARK 500 TYR C 524 -55.43 -124.35
REMARK 500 VAL C 733 -65.00 -121.60
REMARK 500 ARG C 767 33.15 -93.82
REMARK 500 TYR D 524 -51.48 -120.16
REMARK 500 ASP D 579 42.70 75.57
REMARK 500 VAL D 733 -61.99 -132.91
REMARK 500 ARG D 767 -91.06 -107.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 529 NE2
REMARK 620 2 HIS A 563 NE2 96.7
REMARK 620 3 ASP A 564 OD2 87.5 91.5
REMARK 620 4 ASP A 674 OD1 92.4 93.4 175.1
REMARK 620 5 HOH A 962 O 92.4 166.0 99.6 75.5
REMARK 620 6 HOH A 966 O 155.3 107.6 87.7 90.4 64.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 564 OD1
REMARK 620 2 HOH A 999 O 108.0
REMARK 620 3 HOH A 919 O 161.2 88.7
REMARK 620 4 HOH A 972 O 90.6 83.2 82.9
REMARK 620 5 HOH A 966 O 92.3 87.2 97.1 170.4
REMARK 620 6 HOH A 908 O 76.6 171.6 85.8 89.8 99.7
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 HIS B 529 NE2
REMARK 620 2 HIS B 563 NE2 96.6
REMARK 620 3 ASP B 564 OD2 90.4 86.1
REMARK 620 4 ASP B 674 OD1 84.4 93.2 174.6
REMARK 620 5 HOH B 975 O 161.3 101.3 85.3 100.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 564 OD1
REMARK 620 2 HOH B 975 O 91.6
REMARK 620 3 HOH B1004 O 106.2 86.1
REMARK 620 4 HOH B 927 O 164.8 90.5 88.9
REMARK 620 5 HOH B 951 O 83.3 93.6 170.5 81.6
REMARK 620 6 HOH B 960 O 92.2 175.9 91.4 86.2 88.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 529 NE2
REMARK 620 2 HIS C 563 NE2 98.0
REMARK 620 3 ASP C 564 OD2 89.7 88.9
REMARK 620 4 ASP C 674 OD1 88.3 91.2 178.0
REMARK 620 5 HOH C 941 O 92.5 165.9 100.6 79.7
REMARK 620 6 HOH C 954 O 154.9 106.6 85.7 96.2 64.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 564 OD1
REMARK 620 2 HOH C1001 O 98.4
REMARK 620 3 HOH C 954 O 91.8 81.8
REMARK 620 4 HOH C 935 O 173.1 87.9 91.9
REMARK 620 5 HOH C 983 O 89.5 83.0 164.7 88.4
REMARK 620 6 HOH C 943 O 84.6 175.6 101.4 88.9 93.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 529 NE2
REMARK 620 2 HIS D 563 NE2 91.1
REMARK 620 3 ASP D 564 OD2 85.4 87.2
REMARK 620 4 ASP D 674 OD1 86.5 92.4 171.9
REMARK 620 5 HOH D 914 O 94.6 171.9 98.8 82.4
REMARK 620 6 HOH D 923 O 159.7 108.6 90.5 97.3 66.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 564 OD1
REMARK 620 2 HOH D 905 O 159.8
REMARK 620 3 HOH D 941 O 94.5 82.8
REMARK 620 4 HOH D 903 O 80.2 79.7 88.9
REMARK 620 5 HOH D 923 O 88.8 93.6 176.3 90.1
REMARK 620 6 HOH D 935 O 104.2 96.0 93.8 174.7 87.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5MF A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5MF B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5MF C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5MF D 803
DBREF 5EDH A 458 770 UNP Q9Y233 PDE10_HUMAN 448 760
DBREF 5EDH B 458 770 UNP Q9Y233 PDE10_HUMAN 448 760
DBREF 5EDH C 458 770 UNP Q9Y233 PDE10_HUMAN 448 760
DBREF 5EDH D 458 770 UNP Q9Y233 PDE10_HUMAN 448 760
SEQADV 5EDH ALA A 456 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA A 457 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA A 771 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA B 456 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA B 457 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA B 771 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA C 456 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA C 457 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA C 771 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA D 456 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA D 457 UNP Q9Y233 EXPRESSION TAG
SEQADV 5EDH ALA D 771 UNP Q9Y233 EXPRESSION TAG
SEQRES 1 A 316 ALA ALA GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU
SEQRES 2 A 316 CYS LYS GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO
SEQRES 3 A 316 PHE GLU ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL
SEQRES 4 A 316 HIS ARG SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS
SEQRES 5 A 316 LEU CME ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG
SEQRES 6 A 316 ARG VAL PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL
SEQRES 7 A 316 ALA HIS CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR
SEQRES 8 A 316 LEU PHE THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA
SEQRES 9 A 316 CYS LEU CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN
SEQRES 10 A 316 SER TYR LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU
SEQRES 11 A 316 TYR SER THR SER THR MET GLU GLN HIS HIS PHE SER GLN
SEQRES 12 A 316 THR VAL SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE
SEQRES 13 A 316 SER THR LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU
SEQRES 14 A 316 ILE ILE ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU
SEQRES 15 A 316 TYR PHE GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN
SEQRES 16 A 316 THR GLY SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP
SEQRES 17 A 316 ARG VAL ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS
SEQRES 18 A 316 SER VAL THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA
SEQRES 19 A 316 ASN ASP ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU
SEQRES 20 A 316 MET LYS LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP
SEQRES 21 A 316 ARG ASP LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY
SEQRES 22 A 316 PHE TYR ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU
SEQRES 23 A 316 THR GLN ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA
SEQRES 24 A 316 CYS ARG ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG
SEQRES 25 A 316 GLY GLU GLU ALA
SEQRES 1 B 316 ALA ALA GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU
SEQRES 2 B 316 CYS LYS GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO
SEQRES 3 B 316 PHE GLU ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL
SEQRES 4 B 316 HIS ARG SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS
SEQRES 5 B 316 LEU CME ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG
SEQRES 6 B 316 ARG VAL PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL
SEQRES 7 B 316 ALA HIS CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR
SEQRES 8 B 316 LEU PHE THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA
SEQRES 9 B 316 CYS LEU CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN
SEQRES 10 B 316 SER TYR LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU
SEQRES 11 B 316 TYR SER THR SER THR MET GLU GLN HIS HIS PHE SER GLN
SEQRES 12 B 316 THR VAL SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE
SEQRES 13 B 316 SER THR LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU
SEQRES 14 B 316 ILE ILE ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU
SEQRES 15 B 316 TYR PHE GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN
SEQRES 16 B 316 THR GLY SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP
SEQRES 17 B 316 ARG VAL ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS
SEQRES 18 B 316 SER VAL THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA
SEQRES 19 B 316 ASN ASP ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU
SEQRES 20 B 316 MET LYS LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP
SEQRES 21 B 316 ARG ASP LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY
SEQRES 22 B 316 PHE TYR ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU
SEQRES 23 B 316 THR GLN ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA
SEQRES 24 B 316 CYS ARG ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG
SEQRES 25 B 316 GLY GLU GLU ALA
SEQRES 1 C 316 ALA ALA GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU
SEQRES 2 C 316 CYS LYS GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO
SEQRES 3 C 316 PHE GLU ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL
SEQRES 4 C 316 HIS ARG SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS
SEQRES 5 C 316 LEU CME ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG
SEQRES 6 C 316 ARG VAL PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL
SEQRES 7 C 316 ALA HIS CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR
SEQRES 8 C 316 LEU PHE THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA
SEQRES 9 C 316 CYS LEU CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN
SEQRES 10 C 316 SER TYR LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU
SEQRES 11 C 316 TYR SER THR SER THR MET GLU GLN HIS HIS PHE SER GLN
SEQRES 12 C 316 THR VAL SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE
SEQRES 13 C 316 SER THR LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU
SEQRES 14 C 316 ILE ILE ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU
SEQRES 15 C 316 TYR PHE GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN
SEQRES 16 C 316 THR GLY SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP
SEQRES 17 C 316 ARG VAL ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS
SEQRES 18 C 316 SER VAL THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA
SEQRES 19 C 316 ASN ASP ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU
SEQRES 20 C 316 MET LYS LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP
SEQRES 21 C 316 ARG ASP LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY
SEQRES 22 C 316 PHE TYR ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU
SEQRES 23 C 316 THR GLN ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA
SEQRES 24 C 316 CYS ARG ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG
SEQRES 25 C 316 GLY GLU GLU ALA
SEQRES 1 D 316 ALA ALA GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU
SEQRES 2 D 316 CYS LYS GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO
SEQRES 3 D 316 PHE GLU ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL
SEQRES 4 D 316 HIS ARG SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS
SEQRES 5 D 316 LEU CME ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG
SEQRES 6 D 316 ARG VAL PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL
SEQRES 7 D 316 ALA HIS CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR
SEQRES 8 D 316 LEU PHE THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA
SEQRES 9 D 316 CYS LEU CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN
SEQRES 10 D 316 SER TYR LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU
SEQRES 11 D 316 TYR SER THR SER THR MET GLU GLN HIS HIS PHE SER GLN
SEQRES 12 D 316 THR VAL SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE
SEQRES 13 D 316 SER THR LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU
SEQRES 14 D 316 ILE ILE ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU
SEQRES 15 D 316 TYR PHE GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN
SEQRES 16 D 316 THR GLY SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP
SEQRES 17 D 316 ARG VAL ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS
SEQRES 18 D 316 SER VAL THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA
SEQRES 19 D 316 ASN ASP ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU
SEQRES 20 D 316 MET LYS LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP
SEQRES 21 D 316 ARG ASP LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY
SEQRES 22 D 316 PHE TYR ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU
SEQRES 23 D 316 THR GLN ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA
SEQRES 24 D 316 CYS ARG ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG
SEQRES 25 D 316 GLY GLU GLU ALA
MODRES 5EDH CME A 509 CYS MODIFIED RESIDUE
MODRES 5EDH CME B 509 CYS MODIFIED RESIDUE
MODRES 5EDH CME C 509 CYS MODIFIED RESIDUE
MODRES 5EDH CME D 509 CYS MODIFIED RESIDUE
HET CME A 509 10
HET CME B 509 10
HET CME C 509 10
HET CME D 509 10
HET ZN A 801 1
HET MG A 802 1
HET 5MF A 803 25
HET ZN B 801 1
HET MG B 802 1
HET 5MF B 803 25
HET ZN C 801 1
HET MG C 802 1
HET 5MF C 803 25
HET ZN D 801 1
HET MG D 802 1
HET 5MF D 803 25
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM 5MF 8-ETHYL-5-METHYL-2-[2-(2-METHYL-5-PYRROLIDIN-1-YL-1,2,
HETNAM 2 5MF 4-TRIAZOL-3-YL)ETHYL]-[1,2,4]TRIAZOLO[1,5-C]PYRIMIDINE
FORMUL 1 CME 4(C5 H11 N O3 S2)
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 MG 4(MG 2+)
FORMUL 7 5MF 4(C17 H24 N8)
FORMUL 17 HOH *526(H2 O)
HELIX 1 AA1 PRO A 465 ILE A 472 1 8
HELIX 2 AA2 PHE A 482 ASN A 484 5 3
HELIX 3 AA3 MET A 485 CYS A 498 1 14
HELIX 4 AA4 GLU A 504 ASN A 518 1 15
HELIX 5 AA5 ASN A 526 ASN A 543 1 18
HELIX 6 AA6 ASN A 544 PHE A 548 5 5
HELIX 7 AA7 THR A 549 HIS A 563 1 15
HELIX 8 AA8 SER A 571 ASP A 579 1 9
HELIX 9 AA9 HIS A 580 TYR A 586 1 7
HELIX 10 AB1 SER A 589 GLN A 604 1 16
HELIX 11 AB2 SER A 615 THR A 633 1 19
HELIX 12 AB3 ASP A 634 ALA A 636 5 3
HELIX 13 AB4 LEU A 637 THR A 651 1 15
HELIX 14 AB5 ASN A 658 LEU A 675 1 18
HELIX 15 AB6 CYS A 676 LYS A 680 5 5
HELIX 16 AB7 LEU A 681 LEU A 706 1 26
HELIX 17 AB8 ILE A 711 ASP A 720 5 10
HELIX 18 AB9 GLU A 721 VAL A 733 1 13
HELIX 19 AC1 VAL A 733 LEU A 745 1 13
HELIX 20 AC2 THR A 748 ARG A 767 1 20
HELIX 21 AC3 PRO B 465 ILE B 472 1 8
HELIX 22 AC4 PHE B 482 ASN B 484 5 3
HELIX 23 AC5 MET B 485 CYS B 498 1 14
HELIX 24 AC6 GLU B 504 ASN B 518 1 15
HELIX 25 AC7 ASN B 526 ASN B 544 1 19
HELIX 26 AC8 HIS B 545 PHE B 548 5 4
HELIX 27 AC9 THR B 549 HIS B 563 1 15
HELIX 28 AD1 SER B 571 ASP B 579 1 9
HELIX 29 AD2 HIS B 580 TYR B 586 1 7
HELIX 30 AD3 SER B 589 GLN B 604 1 16
HELIX 31 AD4 SER B 615 THR B 633 1 19
HELIX 32 AD5 ASP B 634 THR B 651 1 18
HELIX 33 AD6 ASN B 658 LEU B 675 1 18
HELIX 34 AD7 CYS B 676 LYS B 680 5 5
HELIX 35 AD8 LEU B 681 LEU B 706 1 26
HELIX 36 AD9 ILE B 711 ASP B 720 5 10
HELIX 37 AE1 GLU B 721 VAL B 733 1 13
HELIX 38 AE2 VAL B 733 LEU B 745 1 13
HELIX 39 AE3 THR B 748 ARG B 767 1 20
HELIX 40 AE4 PRO C 465 ILE C 472 1 8
HELIX 41 AE5 PHE C 482 ASN C 484 5 3
HELIX 42 AE6 MET C 485 CYS C 498 1 14
HELIX 43 AE7 GLU C 504 ASN C 518 1 15
HELIX 44 AE8 ASN C 526 ASN C 543 1 18
HELIX 45 AE9 ASN C 544 PHE C 548 5 5
HELIX 46 AF1 THR C 549 HIS C 563 1 15
HELIX 47 AF2 SER C 571 ASP C 579 1 9
HELIX 48 AF3 HIS C 580 TYR C 586 1 7
HELIX 49 AF4 SER C 589 GLN C 604 1 16
HELIX 50 AF5 SER C 615 THR C 633 1 19
HELIX 51 AF6 ASP C 634 THR C 651 1 18
HELIX 52 AF7 ASN C 658 LEU C 675 1 18
HELIX 53 AF8 CYS C 676 LYS C 680 5 5
HELIX 54 AF9 LEU C 681 LEU C 706 1 26
HELIX 55 AG1 ILE C 711 ASP C 720 5 10
HELIX 56 AG2 GLU C 721 VAL C 733 1 13
HELIX 57 AG3 VAL C 733 LEU C 745 1 13
HELIX 58 AG4 THR C 748 ARG C 767 1 20
HELIX 59 AG5 ALA D 456 MET D 460 5 5
HELIX 60 AG6 PRO D 465 ILE D 472 1 8
HELIX 61 AG7 PHE D 482 ASN D 484 5 3
HELIX 62 AG8 MET D 485 CYS D 498 1 14
HELIX 63 AG9 GLU D 504 TYR D 519 1 16
HELIX 64 AH1 ASN D 526 ASN D 544 1 19
HELIX 65 AH2 HIS D 545 PHE D 548 5 4
HELIX 66 AH3 THR D 549 HIS D 563 1 15
HELIX 67 AH4 SER D 571 ASP D 579 1 9
HELIX 68 AH5 HIS D 580 TYR D 586 1 7
HELIX 69 AH6 SER D 589 GLN D 604 1 16
HELIX 70 AH7 SER D 615 THR D 633 1 19
HELIX 71 AH8 ASP D 634 THR D 651 1 18
HELIX 72 AH9 ASN D 658 LEU D 675 1 18
HELIX 73 AI1 CYS D 676 LYS D 680 5 5
HELIX 74 AI2 LEU D 681 LEU D 706 1 26
HELIX 75 AI3 ILE D 711 ASP D 720 5 10
HELIX 76 AI4 GLU D 721 VAL D 733 1 13
HELIX 77 AI5 VAL D 733 LEU D 745 1 13
HELIX 78 AI6 THR D 748 ARG D 767 1 20
SSBOND 1 CYS A 498 CYS A 502 1555 1555 2.04
SSBOND 2 CYS B 498 CYS B 502 1555 1555 2.05
SSBOND 3 CYS C 498 CYS C 502 1555 1555 2.04
SSBOND 4 CYS D 498 CYS D 502 1555 1555 2.05
LINK C LEU A 508 N CME A 509 1555 1555 1.34
LINK C CME A 509 N ARG A 510 1555 1555 1.33
LINK NE2 HIS A 529 ZN ZN A 801 1555 1555 2.12
LINK NE2 HIS A 563 ZN ZN A 801 1555 1555 2.14
LINK OD1 ASP A 564 MG MG A 802 1555 1555 1.99
LINK OD2 ASP A 564 ZN ZN A 801 1555 1555 2.16
LINK OD1 ASP A 674 ZN ZN A 801 1555 1555 2.22
LINK C LEU B 508 N CME B 509 1555 1555 1.33
LINK C CME B 509 N ARG B 510 1555 1555 1.32
LINK NE2 HIS B 529 ZN ZN B 801 1555 1555 2.23
LINK NE2 HIS B 563 ZN ZN B 801 1555 1555 2.18
LINK OD1 ASP B 564 MG MG B 802 1555 1555 2.12
LINK OD2 ASP B 564 ZN ZN B 801 1555 1555 2.21
LINK OD1 ASP B 674 ZN ZN B 801 1555 1555 2.16
LINK C LEU C 508 N CME C 509 1555 1555 1.33
LINK C CME C 509 N ARG C 510 1555 1555 1.33
LINK NE2 HIS C 529 ZN ZN C 801 1555 1555 2.16
LINK NE2 HIS C 563 ZN ZN C 801 1555 1555 2.20
LINK OD1 ASP C 564 MG MG C 802 1555 1555 2.07
LINK OD2 ASP C 564 ZN ZN C 801 1555 1555 2.21
LINK OD1 ASP C 674 ZN ZN C 801 1555 1555 2.22
LINK C LEU D 508 N CME D 509 1555 1555 1.33
LINK C CME D 509 N ARG D 510 1555 1555 1.33
LINK NE2 HIS D 529 ZN ZN D 801 1555 1555 2.26
LINK NE2 HIS D 563 ZN ZN D 801 1555 1555 2.23
LINK OD1 ASP D 564 MG MG D 802 1555 1555 2.10
LINK OD2 ASP D 564 ZN ZN D 801 1555 1555 2.29
LINK OD1 ASP D 674 ZN ZN D 801 1555 1555 2.32
LINK ZN ZN A 801 O HOH A 962 1555 1555 2.52
LINK ZN ZN A 801 O HOH A 966 1555 1555 2.02
LINK MG MG A 802 O HOH A 999 1555 1555 1.98
LINK MG MG A 802 O HOH A 919 1555 1555 2.19
LINK MG MG A 802 O HOH A 972 1555 1555 2.17
LINK MG MG A 802 O HOH A 966 1555 1555 2.07
LINK MG MG A 802 O HOH A 908 1555 1555 2.08
LINK ZN ZN B 801 O HOH B 975 1555 1555 2.17
LINK MG MG B 802 O HOH B 975 1555 1555 1.90
LINK MG MG B 802 O HOH B1004 1555 1555 2.09
LINK MG MG B 802 O HOH B 927 1555 1555 2.09
LINK MG MG B 802 O HOH B 951 1555 1555 1.96
LINK MG MG B 802 O HOH B 960 1555 1555 2.13
LINK ZN ZN C 801 O HOH C 941 1555 1555 2.54
LINK ZN ZN C 801 O HOH C 954 1555 1555 2.11
LINK MG MG C 802 O HOH C1001 1555 1555 2.14
LINK MG MG C 802 O HOH C 954 1555 1555 1.97
LINK MG MG C 802 O HOH C 935 1555 1555 2.14
LINK MG MG C 802 O HOH C 983 1555 1555 2.06
LINK MG MG C 802 O HOH C 943 1555 1555 1.98
LINK ZN ZN D 801 O HOH D 914 1555 1555 2.57
LINK ZN ZN D 801 O HOH D 923 1555 1555 1.94
LINK MG MG D 802 O HOH D 905 1555 1555 2.17
LINK MG MG D 802 O HOH D 941 1555 1555 2.03
LINK MG MG D 802 O HOH D 903 1555 1555 2.26
LINK MG MG D 802 O HOH D 923 1555 1555 2.16
LINK MG MG D 802 O HOH D 935 1555 1555 2.08
SITE 1 AC1 6 HIS A 529 HIS A 563 ASP A 564 ASP A 674
SITE 2 AC1 6 HOH A 962 HOH A 966
SITE 1 AC2 6 ASP A 564 HOH A 908 HOH A 919 HOH A 966
SITE 2 AC2 6 HOH A 972 HOH A 999
SITE 1 AC3 17 LEU A 675 VAL A 678 ILE A 692 TYR A 693
SITE 2 AC3 17 PHE A 696 PRO A 712 MET A 713 LYS A 718
SITE 3 AC3 17 GLU A 721 VAL A 722 GLY A 725 GLN A 726
SITE 4 AC3 17 PHE A 729 HOH A 903 HOH A 983 HOH A1002
SITE 5 AC3 17 HOH A1027
SITE 1 AC4 6 HIS B 529 HIS B 563 ASP B 564 ASP B 674
SITE 2 AC4 6 HOH B 915 HOH B 975
SITE 1 AC5 6 ASP B 564 HOH B 927 HOH B 951 HOH B 960
SITE 2 AC5 6 HOH B 975 HOH B1004
SITE 1 AC6 13 LEU B 675 VAL B 678 ILE B 692 TYR B 693
SITE 2 AC6 13 PHE B 696 MET B 713 LYS B 718 GLY B 725
SITE 3 AC6 13 GLN B 726 PHE B 729 HOH B 924 HOH B1002
SITE 4 AC6 13 HOH B1024
SITE 1 AC7 6 HIS C 529 HIS C 563 ASP C 564 ASP C 674
SITE 2 AC7 6 HOH C 941 HOH C 954
SITE 1 AC8 6 ASP C 564 HOH C 935 HOH C 943 HOH C 954
SITE 2 AC8 6 HOH C 983 HOH C1001
SITE 1 AC9 14 LEU C 635 LEU C 675 VAL C 678 ILE C 692
SITE 2 AC9 14 TYR C 693 PHE C 696 PRO C 712 MET C 713
SITE 3 AC9 14 LYS C 718 GLU C 721 GLY C 725 GLN C 726
SITE 4 AC9 14 PHE C 729 HOH C 902
SITE 1 AD1 6 HIS D 529 HIS D 563 ASP D 564 ASP D 674
SITE 2 AD1 6 HOH D 914 HOH D 923
SITE 1 AD2 6 ASP D 564 HOH D 903 HOH D 905 HOH D 923
SITE 2 AD2 6 HOH D 935 HOH D 941
SITE 1 AD3 12 LEU D 675 ILE D 692 TYR D 693 PHE D 696
SITE 2 AD3 12 MET D 713 LYS D 718 GLU D 721 VAL D 722
SITE 3 AD3 12 GLY D 725 GLN D 726 PHE D 729 HOH D 901
CRYST1 135.401 135.401 235.335 90.00 90.00 120.00 H 3 36
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 0.007385 0.004264 0.000000 0.00000
SCALE2 0.000000 0.008528 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004249 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
