HEADER TRANSFERASE 27-MAR-15 4UI6
TITLE CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH TA-47
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT, RESIDUES 946-1113;
COMPND 5 SYNONYM: TANK2, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,
COMPND 6 ARTD6, POLY [ADP-RIBOSE] POLYMERASE 5B, TNKS-2, TRF1-INTERACTING
COMPND 7 ANKYRIN-RELATED ADP-RIBOSE POLYMERASE 2, TANKYRASE II,
COMPND 8 TANKYRASE-LIKE PROTEIN, TANKYRASE-RELATED PROTEIN;
COMPND 9 EC: 2.4.2.30;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: TANKYRASE-2;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: C-TERMINAL FRAGMENT, RESIDUES 1115-1162;
COMPND 15 SYNONYM: TANK2, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,
COMPND 16 ARTD6, POLY [ADP-RIBOSE] POLYMERASE 5B, TNKS-2, TRF1-INTERACTING
COMPND 17 ANKYRIN-RELATED ADP-RIBOSE POLYMERASE 2, TANKYRASE II,
COMPND 18 TANKYRASE-LIKE PROTEIN, TANKYRASE-RELATED PROTEIN;
COMPND 19 EC: 2.4.2.30;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSFERASE, PROTEIN-LIGAND COMPLEX, DIPHTHERIA TOXIN LIKE FOLD,
KEYWDS 2 ADP- RIBOSYLATION, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HAIKARAINEN,L.LEHTIO
REVDAT 2 25-MAY-16 4UI6 1 JRNL
REVDAT 1 13-APR-16 4UI6 0
JRNL AUTH A.NATHUBHAI,T.HAIKARAINEN,P.C.HAYWARD,S.MUNOZ-DESCALZO,
JRNL AUTH 2 A.S.THOMPSON,M.D.LLOYD,L.LEHTIO,M.D.THREADGILL
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF 2-ARYLQUINAZOLIN-4-ONES
JRNL TITL 2 AS HIGHLY SELECTIVE AND POTENT INHIBITORS OF THE
JRNL TITL 3 TANKYRASES.
JRNL REF EUR.J.MED.CHEM. V. 118 316 2016
JRNL REFN ISSN 0223-5234
JRNL PMID 27163581
JRNL DOI 10.1016/J.EJMECH.2016.04.041
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 29.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.63
REMARK 3 NUMBER OF REFLECTIONS : 47456
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) : 0.15534
REMARK 3 R VALUE (WORKING SET) : 0.15371
REMARK 3 FREE R VALUE : 0.18555
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2498
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) : 1.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.847
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3450
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.231
REMARK 3 BIN FREE R VALUE SET COUNT : 181
REMARK 3 BIN FREE R VALUE : 0.288
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3383
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 423
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.743
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26
REMARK 3 B22 (A**2) : -0.68
REMARK 3 B33 (A**2) : 0.94
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.003
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3553 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3257 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4802 ; 1.446 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7476 ; 0.787 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 428 ; 6.068 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;31.734 ;22.896
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;11.767 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;16.713 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 482 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4066 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 925 ; 0.001 ; 0.020
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4UI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-15.
REMARK 100 THE PDBE ID CODE IS EBI-63480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92000
REMARK 200 MONOCHROMATOR : SINGLE BOUNCE
REMARK 200 OPTICS : TOROIDAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.8
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.70
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) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.1
REMARK 200 R MERGE FOR SHELL (I) : 0.76
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 0.1 M TRIS HCL,
REMARK 280 22% PEG3350, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.72000
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 59.72000
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 1.000000 0.000000 0.000000 45.73500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.17500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.73500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.17500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.72000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.73500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.17500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.72000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.73500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.17500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 A3117 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B3102 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C3012 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 MET A 923
REMARK 465 HIS A 924
REMARK 465 HIS A 925
REMARK 465 HIS A 926
REMARK 465 HIS A 927
REMARK 465 HIS A 928
REMARK 465 HIS A 929
REMARK 465 SER A 930
REMARK 465 SER A 931
REMARK 465 GLY A 932
REMARK 465 VAL A 933
REMARK 465 ASP A 934
REMARK 465 LEU A 935
REMARK 465 GLY A 936
REMARK 465 THR A 937
REMARK 465 GLU A 938
REMARK 465 ASN A 939
REMARK 465 LEU A 940
REMARK 465 TYR A 941
REMARK 465 PHE A 942
REMARK 465 GLN A 943
REMARK 465 SER A 944
REMARK 465 MET A 945
REMARK 465 LEU A 946
REMARK 465 ASN A 947
REMARK 465 THR A 948
REMARK 465 SER A 949
REMARK 465 GLY A 950
REMARK 465 SER A 951
REMARK 465 MET A 1113
REMARK 465 MET B 923
REMARK 465 HIS B 924
REMARK 465 HIS B 925
REMARK 465 HIS B 926
REMARK 465 HIS B 927
REMARK 465 HIS B 928
REMARK 465 HIS B 929
REMARK 465 SER B 930
REMARK 465 SER B 931
REMARK 465 GLY B 932
REMARK 465 VAL B 933
REMARK 465 ASP B 934
REMARK 465 LEU B 935
REMARK 465 GLY B 936
REMARK 465 THR B 937
REMARK 465 GLU B 938
REMARK 465 ASN B 939
REMARK 465 LEU B 940
REMARK 465 TYR B 941
REMARK 465 PHE B 942
REMARK 465 GLN B 943
REMARK 465 SER B 944
REMARK 465 MET B 945
REMARK 465 LEU B 946
REMARK 465 ASN B 947
REMARK 465 THR B 948
REMARK 465 SER B 949
REMARK 465 GLY B 950
REMARK 465 SER B 951
REMARK 465 GLY C 1162
REMARK 465 GLY D 1162
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 ND1 HIS A 1084 ZN ZN A 2116 2.18
REMARK 500 ND1 HIS B 1084 ZN ZN B 2116 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 C1 GOL C 2162 O2 GOL C 2162 3455 1.14
REMARK 500 O1 GOL C 2162 O2 GOL C 2162 3455 1.90
REMARK 500 C2 GOL C 2162 O2 GOL C 2162 3455 0.55
REMARK 500 C2 GOL C 2162 C2 GOL C 2162 3455 0.98
REMARK 500 C2 GOL C 2162 C3 GOL C 2162 3455 2.03
REMARK 500 O2 GOL C 2162 O2 GOL C 2162 3455 1.86
REMARK 500 O2 GOL C 2162 C3 GOL C 2162 3455 1.48
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 ASN A1020 56.45 -145.53
REMARK 500 VAL C1131 -61.89 -134.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ECZ B2114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ECZ A2113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B2115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A2116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B2116
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2117
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UFY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-13
REMARK 900 RELATED ID: 4UHG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-21
REMARK 900 RELATED ID: 4UI3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-26
REMARK 900 RELATED ID: 4UI4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-29
REMARK 900 RELATED ID: 4UI5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-41
REMARK 900 RELATED ID: 4UI7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-49
REMARK 900 RELATED ID: 4UI8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH
REMARK 900 TA-55
DBREF 4UI6 A 946 1113 UNP Q9H2K2 TNKS2_HUMAN 946 1113
DBREF 4UI6 B 946 1113 UNP Q9H2K2 TNKS2_HUMAN 946 1113
DBREF 4UI6 C 1115 1162 UNP Q9H2K2 TNKS2_HUMAN 1115 1162
DBREF 4UI6 D 1115 1162 UNP Q9H2K2 TNKS2_HUMAN 1115 1162
SEQADV 4UI6 MET A 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS A 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER A 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER A 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLY A 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 VAL A 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 ASP A 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 LEU A 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLY A 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 THR A 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLU A 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 ASN A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 LEU A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 TYR A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 PHE A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLN A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 MET A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 MET B 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 HIS B 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER B 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER B 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLY B 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 VAL B 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 ASP B 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 LEU B 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLY B 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 THR B 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLU B 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 ASN B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 LEU B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 TYR B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 PHE B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 GLN B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 SER B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4UI6 MET B 945 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 A 191 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 A 191 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 A 191 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 A 191 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 A 191 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 A 191 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 A 191 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 A 191 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 A 191 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 A 191 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 A 191 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 A 191 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 A 191 LYS SER PHE LEU GLN PHE SER ALA MET
SEQRES 1 C 48 MET ALA HIS SER PRO PRO GLY HIS HIS SER VAL THR GLY
SEQRES 2 C 48 ARG PRO SER VAL ASN GLY LEU ALA LEU ALA GLU TYR VAL
SEQRES 3 C 48 ILE TYR ARG GLY GLU GLN ALA TYR PRO GLU TYR LEU ILE
SEQRES 4 C 48 THR TYR GLN ILE MET ARG PRO GLU GLY
SEQRES 1 B 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 B 191 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 B 191 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 B 191 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 B 191 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 B 191 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 B 191 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 B 191 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 B 191 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 B 191 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 B 191 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 B 191 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 B 191 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 B 191 LYS SER PHE LEU GLN PHE SER ALA MET
SEQRES 1 D 48 MET ALA HIS SER PRO PRO GLY HIS HIS SER VAL THR GLY
SEQRES 2 D 48 ARG PRO SER VAL ASN GLY LEU ALA LEU ALA GLU TYR VAL
SEQRES 3 D 48 ILE TYR ARG GLY GLU GLN ALA TYR PRO GLU TYR LEU ILE
SEQRES 4 D 48 THR TYR GLN ILE MET ARG PRO GLU GLY
HET GOL C2162 6
HET ECZ B2114 23
HET ECZ A2113 23
HET SO4 A2114 5
HET SO4 B2115 5
HET SO4 A2115 5
HET SO4 D2162 5
HET ZN A2116 1
HET ZN B2116 1
HET GOL A2117 6
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM ECZ 8-METHOXY-2-[4-(TRIFLUOROMETHYL)PHENYL]-3,4-
HETNAM 2 ECZ DIHYDROQUINAZOLIN-4-ONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 8 ECZ 2(C16 H11 F3 N2 O2)
FORMUL 9 HOH *423(H2 O)
HELIX 1 1 ASP A 962 THR A 975 1 14
HELIX 2 2 ASN A 1002 GLU A 1019 1 18
HELIX 3 3 PHE A 1035 GLY A 1043 1 9
HELIX 4 4 ASP A 1045 ALA A 1049 5 5
HELIX 5 5 ASN A 1064 GLN A 1070 1 7
HELIX 6 6 GLY A 1074 GLY A 1078 5 5
HELIX 7 7 ASP B 962 THR B 975 1 14
HELIX 8 8 ASN B 1002 ASN B 1020 1 19
HELIX 9 9 PHE B 1035 GLY B 1043 1 9
HELIX 10 10 ASP B 1045 ALA B 1049 5 5
HELIX 11 11 ASN B 1064 GLN B 1070 1 7
HELIX 12 12 GLY B 1074 GLY B 1078 5 5
HELIX 13 13 ARG C 1143 GLU C 1145 5 3
HELIX 14 14 ARG D 1143 GLU D 1145 5 3
SHEET 1 AA 5 ILE A 954 ASP A 957 0
SHEET 2 AA 5 TYR A 992 CYS A1001 -1 O LYS A 999 N ILE A 956
SHEET 3 AA 5 ALA C1147 ILE C1157 -1 O GLU C1150 N VAL A1000
SHEET 4 AA 5 ARG A1094 THR A1102 -1 O ARG A1094 N TYR C1155
SHEET 5 AA 5 GLU A1026 HIS A1031 -1 O ARG A1027 N VAL A1101
SHEET 1 AB 4 ILE A1059 ALA A1062 0
SHEET 2 AB 4 GLU C1138 ILE C1141 -1 O TYR C1139 N PHE A1061
SHEET 3 AB 4 SER C1124 PRO C1129 -1 O VAL C1125 N VAL C1140
SHEET 4 AB 4 SER A1106 SER A1111 1 O PHE A1107 N THR C1126
SHEET 1 BA 5 ILE B 954 ASP B 957 0
SHEET 2 BA 5 TYR B 992 CYS B1001 -1 O LYS B 999 N ILE B 956
SHEET 3 BA 5 ALA D1147 ILE D1157 -1 O GLU D1150 N VAL B1000
SHEET 4 BA 5 ARG B1094 THR B1102 -1 O ARG B1094 N TYR D1155
SHEET 5 BA 5 GLU B1026 HIS B1031 -1 O ARG B1027 N VAL B1101
SHEET 1 BB 4 ILE B1059 ALA B1062 0
SHEET 2 BB 4 GLU D1138 ILE D1141 -1 O TYR D1139 N PHE B1061
SHEET 3 BB 4 SER D1124 PRO D1129 -1 O VAL D1125 N VAL D1140
SHEET 4 BB 4 SER B1106 SER B1111 1 O PHE B1107 N THR D1126
SITE 1 AC1 5 PRO C1129 SER C1130 VAL C1131 ASN C1132
SITE 2 AC1 5 GLY C1133
SITE 1 AC2 13 HIS B1031 GLY B1032 SER B1033 PHE B1035
SITE 2 AC2 13 ALA B1049 TYR B1050 TYR B1060 ALA B1062
SITE 3 AC2 13 LYS B1067 SER B1068 TYR B1071 ILE B1075
SITE 4 AC2 13 GLU D1138
SITE 1 AC3 13 HIS A1031 GLY A1032 PRO A1034 PHE A1035
SITE 2 AC3 13 ALA A1049 TYR A1050 TYR A1060 ALA A1062
SITE 3 AC3 13 LYS A1067 SER A1068 TYR A1071 ILE A1075
SITE 4 AC3 13 GLU C1138
SITE 1 AC4 8 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC4 8 GLN A1070 HOH A3047 HOH A3147 HOH A3205
SITE 1 AC5 6 ARG B 977 HIS B 979 ARG B 980 LYS B1067
SITE 2 AC5 6 GLN B1070 HOH B3045
SITE 1 AC6 6 ASN A 990 ARG A 991 HOH A3064 HOH A3067
SITE 2 AC6 6 PRO C1160 GLU C1161
SITE 1 AC7 6 ASN B 990 ARG B 991 HOH B3059 HOH B3062
SITE 2 AC7 6 PRO D1160 GLU D1161
SITE 1 AC8 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC9 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 BC1 5 ASN A1037 GLN A1095 ARG B 980 ALA B1112
SITE 2 BC1 5 HOH B3044
CRYST1 91.470 98.350 119.440 90.00 90.00 90.00 C 2 2 21 16
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 0.010933 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008372 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
