HEADER TRANSFERASE 09-JUN-15 5BXO
TITLE HUMAN TANKYRASE-2 IN COMPLEX WITH MACROCYCLISED EXTENDED PEPTIDE
TITLE 2 CP4N2M3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 488-649;
COMPND 5 SYNONYM: TANK2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,ARTD6,
COMPND 6 POLY [ADP-RIBOSE] POLYMERASE 5B,TNKS-2,TRF1-INTERACTING ANKYRIN-
COMPND 7 RELATED ADP-RIBOSE POLYMERASE 2,TANKYRASE II,TANKYRASE-LIKE PROTEIN,
COMPND 8 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 SYNONYM: TANK2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,ARTD6,
COMPND 15 POLY [ADP-RIBOSE] POLYMERASE 5B,TNKS-2,TRF1-INTERACTING ANKYRIN-
COMPND 16 RELATED ADP-RIBOSE POLYMERASE 2,TANKYRASE II,TANKYRASE-LIKE PROTEIN,
COMPND 17 TANKYRASE-RELATED PROTEIN;
COMPND 18 EC: 2.4.2.30;
COMPND 19 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: TNKS2, PARP5B, TANK2, TNKL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGST;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS STAPLED PEPTIDE, PROTEIN-PROTEIN INTERACTION, ANKYRIN-REPEAT DOMAIN,
KEYWDS 2 TANKYRASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XU,G.FISCHER,M.HYVONEN,L.ITZHAKI
REVDAT 3 29-MAR-23 5BXO 1 JRNL REMARK
REVDAT 2 13-SEP-17 5BXO 1 REMARK
REVDAT 1 29-JUN-16 5BXO 0
JRNL AUTH W.XU,Y.H.LAU,G.FISCHER,Y.S.TAN,A.CHATTOPADHYAY,
JRNL AUTH 2 M.DE LA ROCHE,M.HYVONEN,C.VERMA,D.R.SPRING,L.S.ITZHAKI
JRNL TITL MACROCYCLIZED EXTENDED PEPTIDES: INHIBITING THE
JRNL TITL 2 SUBSTRATE-RECOGNITION DOMAIN OF TANKYRASE.
JRNL REF J.AM.CHEM.SOC. V. 139 2245 2017
JRNL REFN ESSN 1520-5126
JRNL PMID 28084734
JRNL DOI 10.1021/JACS.6B10234
REMARK 2
REMARK 2 RESOLUTION. 1.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 56016
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2934
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) : 1.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3990
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2583
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : -0.19000
REMARK 3 B13 (A**2) : -0.09000
REMARK 3 B23 (A**2) : 0.49000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.157
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2964 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2835 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4023 ; 1.577 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6538 ; 1.230 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 395 ; 5.402 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;28.412 ;24.809
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 507 ;14.524 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;14.365 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3587 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 658 ; 0.005 ; 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): 1509 ; 1.247 ; 1.446
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1510 ; 1.246 ; 1.446
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1916 ; 1.976 ; 2.151
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1917 ; 1.976 ; 2.151
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1455 ; 1.798 ; 1.701
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1456 ; 1.797 ; 1.704
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2105 ; 2.749 ; 2.459
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3680 ; 5.196 ;12.677
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3681 ; 5.195 ;12.691
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 487 645 B 487 645 9517 0.13 0.05
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5BXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210728.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.91731
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59052
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.334
REMARK 200 RESOLUTION RANGE LOW (A) : 53.312
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THIN NEEDLE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE, PH 5.0, 3.2
REMARK 280 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 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 486
REMARK 465 ALA A 647
REMARK 465 ALA A 648
REMARK 465 LEU A 649
REMARK 465 GLY B 486
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 491 OE1 OE2
REMARK 480 GLU A 498 CD OE1 OE2
REMARK 480 LYS A 509 CE NZ
REMARK 480 LYS A 510 CE NZ
REMARK 480 GLN A 547 OE1 NE2
REMARK 480 LYS A 602 NZ
REMARK 480 LYS A 621 NZ
REMARK 480 ASN B 489 CG OD1 ND2
REMARK 480 GLU B 498 CD OE1 OE2
REMARK 480 LYS B 509 NZ
REMARK 480 LYS B 620 CE NZ
REMARK 480 GLU C 8 CD OE1 OE2
REMARK 480 GLU D 8 CD OE1 OE2
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 NH2 ARG B 644 OD2 ASP B 646 2.19
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 OE1 GLN A 613 NH2 ARG A 623 1455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 491 CD GLU A 491 OE1 0.156
REMARK 500 GLU A 491 CD GLU A 491 OE2 -0.299
REMARK 500 LYS A 510 CD LYS A 510 CE -0.165
REMARK 500 GLN A 547 CD GLN A 547 OE1 0.226
REMARK 500 GLN A 547 CD GLN A 547 NE2 -0.220
REMARK 500 LYS A 602 CE LYS A 602 NZ -0.297
REMARK 500 ASN B 489 CB ASN B 489 CG -0.208
REMARK 500 GLU D 8 CG GLU D 8 CD 0.195
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 LYS A 602 CD - CE - NZ ANGL. DEV. = 37.1 DEGREES
REMARK 500 LYS B 509 CD - CE - NZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 GLU D 8 CG - CD - OE1 ANGL. DEV. = -18.1 DEGREES
REMARK 500 GLU D 8 CG - CD - OE2 ANGL. DEV. = 17.0 DEGREES
REMARK 500 GLU D 8 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 GLU D 8 O - C - N ANGL. DEV. = 11.1 DEGREES
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 SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE C 0 and ARG C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU C 8 and NH2 C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU C 8 and NH2 C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4XP C 100 and ALA C
REMARK 800 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4XP C 100 and ALA C
REMARK 800 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE D 0 and ARG D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU D 8 and NH2 D 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU D 8 and NH2 D 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4XP D 100 and ALA D
REMARK 800 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4XP D 100 and ALA D
REMARK 800 3
DBREF 5BXO A 488 649 UNP Q9H2K2 TNKS2_HUMAN 488 649
DBREF 5BXO B 488 649 UNP Q9H2K2 TNKS2_HUMAN 488 649
DBREF 5BXO C 1 8 UNP Q9H2K2 TNKS2_HUMAN 5 12
DBREF 5BXO D 1 8 UNP Q9H2K2 TNKS2_HUMAN 5 12
SEQADV 5BXO GLY A 486 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO SER A 487 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO GLY B 486 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO SER B 487 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO ACE C 0 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO GLU C 2 UNP Q9H2K2 CYS 6 CONFLICT
SEQADV 5BXO ASP C 5 UNP Q9H2K2 GLY 9 CONFLICT
SEQADV 5BXO GLU C 8 UNP Q9H2K2 ALA 12 CONFLICT
SEQADV 5BXO NH2 C 9 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO ACE D 0 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5BXO GLU D 2 UNP Q9H2K2 CYS 6 CONFLICT
SEQADV 5BXO ASP D 5 UNP Q9H2K2 GLY 9 CONFLICT
SEQADV 5BXO GLU D 8 UNP Q9H2K2 ALA 12 CONFLICT
SEQADV 5BXO NH2 D 9 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 164 GLY SER GLY ASN SER GLU ALA ASP ARG GLN LEU LEU GLU
SEQRES 2 A 164 ALA ALA LYS ALA GLY ASP VAL GLU THR VAL LYS LYS LEU
SEQRES 3 A 164 CYS THR VAL GLN SER VAL ASN CYS ARG ASP ILE GLU GLY
SEQRES 4 A 164 ARG GLN SER THR PRO LEU HIS PHE ALA ALA GLY TYR ASN
SEQRES 5 A 164 ARG VAL SER VAL VAL GLU TYR LEU LEU GLN HIS GLY ALA
SEQRES 6 A 164 ASP VAL HIS ALA LYS ASP LYS GLY GLY LEU VAL PRO LEU
SEQRES 7 A 164 HIS ASN ALA CYS SER TYR GLY HIS TYR GLU VAL ALA GLU
SEQRES 8 A 164 LEU LEU VAL LYS HIS GLY ALA VAL VAL ASN VAL ALA ASP
SEQRES 9 A 164 LEU TRP LYS PHE THR PRO LEU HIS GLU ALA ALA ALA LYS
SEQRES 10 A 164 GLY LYS TYR GLU ILE CYS LYS LEU LEU LEU GLN HIS GLY
SEQRES 11 A 164 ALA ASP PRO THR LYS LYS ASN ARG ASP GLY ASN THR PRO
SEQRES 12 A 164 LEU ASP LEU VAL LYS ASP GLY ASP THR ASP ILE GLN ASP
SEQRES 13 A 164 LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 1 B 164 GLY SER GLY ASN SER GLU ALA ASP ARG GLN LEU LEU GLU
SEQRES 2 B 164 ALA ALA LYS ALA GLY ASP VAL GLU THR VAL LYS LYS LEU
SEQRES 3 B 164 CYS THR VAL GLN SER VAL ASN CYS ARG ASP ILE GLU GLY
SEQRES 4 B 164 ARG GLN SER THR PRO LEU HIS PHE ALA ALA GLY TYR ASN
SEQRES 5 B 164 ARG VAL SER VAL VAL GLU TYR LEU LEU GLN HIS GLY ALA
SEQRES 6 B 164 ASP VAL HIS ALA LYS ASP LYS GLY GLY LEU VAL PRO LEU
SEQRES 7 B 164 HIS ASN ALA CYS SER TYR GLY HIS TYR GLU VAL ALA GLU
SEQRES 8 B 164 LEU LEU VAL LYS HIS GLY ALA VAL VAL ASN VAL ALA ASP
SEQRES 9 B 164 LEU TRP LYS PHE THR PRO LEU HIS GLU ALA ALA ALA LYS
SEQRES 10 B 164 GLY LYS TYR GLU ILE CYS LYS LEU LEU LEU GLN HIS GLY
SEQRES 11 B 164 ALA ASP PRO THR LYS LYS ASN ARG ASP GLY ASN THR PRO
SEQRES 12 B 164 LEU ASP LEU VAL LYS ASP GLY ASP THR ASP ILE GLN ASP
SEQRES 13 B 164 LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 1 C 10 ACE ARG GLU ALA GLY ASP GLY ALA GLU NH2
SEQRES 1 D 10 ACE ARG GLU ALA GLY ASP GLY ALA GLU NH2
HET ACE C 0 3
HET NH2 C 9 1
HET ACE D 0 3
HET NH2 D 9 1
HET SO4 A 701 5
HET SO4 A 702 5
HET SO4 A 703 5
HET DMS A 704 4
HET SO4 B 701 5
HET SO4 B 702 5
HET SO4 B 703 5
HET DMS B 704 4
HET DMS B 705 4
HET 4XP C 100 15
HET 4XP D 100 15
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 4XP 4,4'-PROPANE-1,3-DIYLBIS(1-METHYL-1H-1,2,3-TRIAZOLE)
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 NH2 2(H2 N)
FORMUL 5 SO4 6(O4 S 2-)
FORMUL 8 DMS 3(C2 H6 O S)
FORMUL 14 4XP 2(C9 H14 N6)
FORMUL 16 HOH *277(H2 O)
HELIX 1 AA1 SER A 487 GLY A 503 1 17
HELIX 2 AA2 ASP A 504 CYS A 512 1 9
HELIX 3 AA3 THR A 528 TYR A 536 1 9
HELIX 4 AA4 ARG A 538 HIS A 548 1 11
HELIX 5 AA5 VAL A 561 TYR A 569 1 9
HELIX 6 AA6 HIS A 571 HIS A 581 1 11
HELIX 7 AA7 THR A 594 GLY A 603 1 10
HELIX 8 AA8 LYS A 604 HIS A 614 1 11
HELIX 9 AA9 THR A 627 VAL A 632 1 6
HELIX 10 AB1 ASP A 636 GLY A 645 1 10
HELIX 11 AB2 GLY B 488 GLY B 503 1 16
HELIX 12 AB3 ASP B 504 CYS B 512 1 9
HELIX 13 AB4 THR B 528 TYR B 536 1 9
HELIX 14 AB5 ARG B 538 HIS B 548 1 11
HELIX 15 AB6 VAL B 561 TYR B 569 1 9
HELIX 16 AB7 HIS B 571 HIS B 581 1 11
HELIX 17 AB8 THR B 594 GLY B 603 1 10
HELIX 18 AB9 LYS B 604 HIS B 614 1 11
HELIX 19 AC1 THR B 627 VAL B 632 1 6
HELIX 20 AC2 ASP B 636 GLY B 645 1 10
LINK C ACE C 0 N ARG C 1 1555 1555 1.35
LINK CB ALA C 3 C8 4XP C 100 1555 1555 1.54
LINK CB ALA C 7 C 4XP C 100 1555 1555 1.55
LINK C AGLU C 8 N NH2 C 9 1555 1555 1.32
LINK C BGLU C 8 N NH2 C 9 1555 1555 1.31
LINK C ACE D 0 N ARG D 1 1555 1555 1.35
LINK CB ALA D 3 C8 4XP D 100 1555 1555 1.54
LINK CB ALA D 7 C 4XP D 100 1555 1555 1.56
LINK C AGLU D 8 N NH2 D 9 1555 1555 1.34
LINK C BGLU D 8 N NH2 D 9 1555 1555 1.32
CISPEP 1 SER B 487 GLY B 488 0 17.68
SITE 1 AC1 6 ALA A 601 LYS A 602 LYS A 633 HOH A 809
SITE 2 AC1 6 ASN B 626 HOH B 878
SITE 1 AC2 7 GLU A 576 LYS A 580 LYS A 592 HIS A 614
SITE 2 AC2 7 ARG A 623 HOH A 869 GLN B 613
SITE 1 AC3 8 ARG A 538 VAL A 539 SER A 540 LYS A 557
SITE 2 AC3 8 HOH A 805 HOH A 825 HOH A 856 HOH A 868
SITE 1 AC4 3 CYS A 512 HIS A 548 HIS B 548
SITE 1 AC5 10 LYS A 633 ASP A 634 HOH A 848 GLY B 603
SITE 2 AC5 10 LYS B 604 TYR B 605 GLU B 606 HOH B 811
SITE 3 AC5 10 HOH B 815 HOH B 861
SITE 1 AC6 5 LYS B 592 GLN B 613 HIS B 614 ARG B 623
SITE 2 AC6 5 HOH B 806
SITE 1 AC7 7 ASN B 537 ARG B 538 VAL B 539 SER B 540
SITE 2 AC7 7 LYS B 557 HOH B 802 HOH B 825
SITE 1 AC8 5 TYR B 605 LYS B 609 ASP B 624 GLY B 625
SITE 2 AC8 5 HOH B 827
SITE 1 AC9 3 LYS B 555 ASP B 556 GLY B 559
SITE 1 AD1 9 ASP A 589 TRP A 591 PHE A 593 GLU A 598
SITE 2 AD1 9 HOH A 879 ASP B 634 THR B 637 GLU C 2
SITE 3 AD1 9 HOH C 207
SITE 1 AD2 10 TYR A 569 HIS A 571 LYS A 602 HOH A 837
SITE 2 AD2 10 GLU B 491 ARG B 494 ALA C 7 4XP C 100
SITE 3 AD2 10 HOH C 204 HOH C 206
SITE 1 AD3 10 TYR A 569 HIS A 571 LYS A 602 HOH A 837
SITE 2 AD3 10 GLU B 491 ARG B 494 ALA C 7 4XP C 100
SITE 3 AD3 10 HOH C 204 HOH C 206
SITE 1 AD4 13 ARG A 525 TYR A 569 GLU B 506 THR B 507
SITE 2 AD4 13 GLU B 523 GLU C 2 GLY C 4 GLY C 6
SITE 3 AD4 13 ALA C 7 GLU C 8 NH2 C 9 HOH C 202
SITE 4 AD4 13 HOH C 203
SITE 1 AD5 12 GLY A 535 TYR A 569 HIS A 571 GLU B 506
SITE 2 AD5 12 THR B 507 GLU B 523 ALA C 3 GLY C 6
SITE 3 AD5 12 GLU C 8 NH2 C 9 HOH C 203 HOH C 209
SITE 1 AD6 9 ASP A 634 GLY A 635 THR A 637 ASP B 589
SITE 2 AD6 9 TRP B 591 PHE B 593 GLU B 598 GLU D 2
SITE 3 AD6 9 HOH D 208
SITE 1 AD7 10 ARG A 494 TYR B 569 HIS B 571 LYS B 602
SITE 2 AD7 10 HOH B 829 ALA D 7 4XP D 100 HOH D 201
SITE 3 AD7 10 HOH D 210 HOH D 212
SITE 1 AD8 10 ARG A 494 TYR B 569 HIS B 571 LYS B 602
SITE 2 AD8 10 HOH B 829 ALA D 7 4XP D 100 HOH D 201
SITE 3 AD8 10 HOH D 210 HOH D 212
SITE 1 AD9 12 ARG A 494 GLU A 506 GLU A 523 GLY B 535
SITE 2 AD9 12 TYR B 569 HIS B 571 ALA D 3 GLY D 6
SITE 3 AD9 12 GLU D 8 NH2 D 9 HOH D 205 HOH D 209
SITE 1 AE1 13 ARG A 494 GLU A 506 GLU A 523 ARG B 525
SITE 2 AE1 13 TYR B 569 GLU D 2 GLY D 4 GLY D 6
SITE 3 AE1 13 ALA D 7 GLU D 8 HOH D 203 HOH D 205
SITE 4 AE1 13 HOH D 215
CRYST1 29.823 46.014 54.472 78.45 88.99 72.35 P 1 2
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 0.033531 -0.010666 0.001627 0.00000
SCALE2 0.000000 0.022805 -0.004765 0.00000
SCALE3 0.000000 0.000000 0.018757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
