HEADER TRANSFERASE 11-MAR-15 4YO4
TITLE CRYSTAL STRUCTURE OF DAPK1 CATALYTIC DOMAIN IN COMPLEX WITH THE HINGE
TITLE 2 BINDING FRAGMENT PHTHALAZINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEIN KINASE DOMAIN (UNP RESIDUES 2-285);
COMPND 5 SYNONYM: DAP KINASE 1;
COMPND 6 EC: 2.7.11.1;
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: DAPK1, DAPK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.L.GRUM-TOKARS,S.M.ROY,G.MINASOV,W.F.ANDERSON,D.M.WATTERSON
REVDAT 5 27-SEP-23 4YO4 1 REMARK
REVDAT 4 18-DEC-19 4YO4 1 REMARK
REVDAT 3 22-NOV-17 4YO4 1 REMARK
REVDAT 2 06-SEP-17 4YO4 1 SOURCE REMARK
REVDAT 1 06-MAY-15 4YO4 0
JRNL AUTH V.L.GRUM-TOKARS,G.MINASOV,S.M.ROY,W.F.ANDERSON,D.M.WATTERSON
JRNL TITL CRYSTAL STRUCTURE OF DAPK1 CATALYTIC DOMAIN IN COMPLEX WITH
JRNL TITL 2 HINGE BINDING FRAGMENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.M.WATTERSON,V.L.GRUM-TOKARS,S.M.ROY,J.P.SCHAVOCKY,
REMARK 1 AUTH 2 B.D.BRADARIC,A.D.BACHSTETTER,B.XING,E.DIMAYUGA,F.SAEED,
REMARK 1 AUTH 3 H.ZHANG,A.STANISZEWSKI,J.C.PELLETIER,G.MINASOV,W.F.ANDERSON,
REMARK 1 AUTH 4 O.ARANCIO,L.J.VAN ELDIK
REMARK 1 TITL DEVELOPMENT OF NOVEL IN VIVO CHEMICAL PROBES TO ADDRESS CNS
REMARK 1 TITL 2 PROTEIN KINASE INVOLVEMENT IN SYNAPTIC DYSFUNCTION.
REMARK 1 REF PLOS ONE V. 8 66226 2013
REMARK 1 REFN ESSN 1932-6203
REMARK 1 PMID 23840427
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.K.MCNAMARA,J.S.BRUNZELLE,J.P.SCHAVOCKY,D.M.WATTERSON,
REMARK 1 AUTH 2 V.GRUM-TOKARS
REMARK 1 TITL SITE-DIRECTED MUTAGENESIS OF THE GLYCINE-RICH LOOP OF DEATH
REMARK 1 TITL 2 ASSOCIATED PROTEIN KINASE (DAPK) IDENTIFIES IT AS A KEY
REMARK 1 TITL 3 STRUCTURE FOR CATALYTIC ACTIVITY.
REMARK 1 REF BIOCHIM. BIOPHYS. ACTA V.1813 1068 2011
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 21126544
REMARK 1 DOI 10.1016/J.BBAMCR.2010.11.011
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 32532
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1731
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2447
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : 1.49000
REMARK 3 B33 (A**2) : -0.74000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2483 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2371 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3368 ; 1.481 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5485 ; 3.520 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 305 ; 4.180 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;32.182 ;24.839
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 457 ;11.218 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;10.816 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 365 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2836 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 566 ; 0.012 ; 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): 1191 ; 1.551 ; 1.431
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1189 ; 1.535 ; 1.426
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1505 ; 2.365 ; 2.129
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1506 ; 2.364 ; 2.133
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1292 ; 2.482 ; 1.791
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1293 ; 2.481 ; 1.792
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1864 ; 3.921 ; 2.549
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2978 ; 6.358 ;13.002
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2886 ; 6.241 ;12.442
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8240 -2.9280 2.3320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0774 T22: 0.0042
REMARK 3 T33: 0.0941 T12: 0.0065
REMARK 3 T13: -0.0103 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.6866 L22: 1.3688
REMARK 3 L33: 1.5852 L12: 1.0935
REMARK 3 L13: 0.6601 L23: 1.3431
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: -0.0182 S13: -0.1297
REMARK 3 S21: 0.1129 S22: 0.0013 S23: -0.1389
REMARK 3 S31: 0.1488 S32: 0.0006 S33: -0.0645
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 50 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6850 8.2290 10.0070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 0.0489
REMARK 3 T33: 0.0564 T12: 0.0023
REMARK 3 T13: -0.0018 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.4625 L22: 0.4406
REMARK 3 L33: 0.4637 L12: -0.2465
REMARK 3 L13: -0.4610 L23: 0.2662
REMARK 3 S TENSOR
REMARK 3 S11: -0.0074 S12: -0.0652 S13: 0.0161
REMARK 3 S21: -0.0384 S22: 0.0262 S23: -0.0349
REMARK 3 S31: 0.0159 S32: 0.0600 S33: -0.0189
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 167 A 239
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0300 6.1980 19.5040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0762 T22: 0.0262
REMARK 3 T33: 0.0708 T12: -0.0033
REMARK 3 T13: -0.0104 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1797 L22: 0.4714
REMARK 3 L33: 0.5264 L12: 0.1346
REMARK 3 L13: -0.0249 L23: 0.0255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: 0.0125 S13: -0.0320
REMARK 3 S21: 0.0073 S22: 0.0365 S23: 0.0046
REMARK 3 S31: 0.0192 S32: 0.0043 S33: -0.0607
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 240 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4270 17.3500 21.7240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0775 T22: 0.0189
REMARK 3 T33: 0.0693 T12: 0.0045
REMARK 3 T13: 0.0037 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.2096 L22: 0.6587
REMARK 3 L33: 0.7961 L12: 0.2576
REMARK 3 L13: 0.1545 L23: -0.0762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: -0.0247 S13: 0.0216
REMARK 3 S21: 0.0247 S22: -0.0419 S23: 0.0132
REMARK 3 S31: -0.0480 S32: -0.0466 S33: 0.0183
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 4YO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-13
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 : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34446
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.53800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1JKS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M HEPES,
REMARK 280 1.6 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 23.50200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.26850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.26150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.26850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.50200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.26150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 278
REMARK 465 ASP A 279
REMARK 465 THR A 280
REMARK 465 GLN A 281
REMARK 465 GLN A 282
REMARK 465 ALA A 283
REMARK 465 LEU A 284
REMARK 465 SER A 285
REMARK 465 SER A 286
REMARK 465 ALA A 287
REMARK 465 TRP A 288
REMARK 465 SER A 289
REMARK 465 HIS A 290
REMARK 465 PRO A 291
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 ASP A 139 37.93 -142.54
REMARK 500 ASP A 161 79.27 62.87
REMARK 500 ILE A 168 78.55 -114.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 628 DISTANCE = 6.41 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4FT A 307
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YPD RELATED DB: PDB
DBREF 4YO4 A 2 285 UNP P53355 DAPK1_HUMAN 2 285
SEQADV 4YO4 SER A 286 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 ALA A 287 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 TRP A 288 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 SER A 289 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 HIS A 290 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 PRO A 291 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 GLN A 292 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 PHE A 293 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 GLU A 294 UNP P53355 EXPRESSION TAG
SEQADV 4YO4 LYS A 295 UNP P53355 EXPRESSION TAG
SEQRES 1 A 294 THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR ASP
SEQRES 2 A 294 THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL VAL
SEQRES 3 A 294 LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR ALA
SEQRES 4 A 294 ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER ARG
SEQRES 5 A 294 ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL SER
SEQRES 6 A 294 ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR LEU
SEQRES 7 A 294 HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU ILE
SEQRES 8 A 294 LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE LEU
SEQRES 9 A 294 ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR GLU
SEQRES 10 A 294 PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU HIS
SEQRES 11 A 294 SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU ASN
SEQRES 12 A 294 ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG ILE
SEQRES 13 A 294 LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP PHE
SEQRES 14 A 294 GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU PHE
SEQRES 15 A 294 VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY LEU
SEQRES 16 A 294 GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR ILE
SEQRES 17 A 294 LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR LYS
SEQRES 18 A 294 GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR GLU
SEQRES 19 A 294 PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU ALA
SEQRES 20 A 294 LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO LYS
SEQRES 21 A 294 LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO TRP
SEQRES 22 A 294 ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER SER ALA
SEQRES 23 A 294 TRP SER HIS PRO GLN PHE GLU LYS
HET CL A 301 1
HET CL A 302 2
HET CL A 303 2
HET CL A 304 2
HET ACT A 305 4
HET SO4 A 306 5
HET 4FT A 307 10
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM 4FT PHTHALAZINE
FORMUL 2 CL 4(CL 1-)
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 SO4 O4 S 2-
FORMUL 8 4FT C8 H6 N2
FORMUL 9 HOH *228(H2 O)
HELIX 1 AA1 ASN A 8 ASP A 11 5 4
HELIX 2 AA2 SER A 57 ILE A 71 1 15
HELIX 3 AA3 GLU A 100 LYS A 108 1 9
HELIX 4 AA4 THR A 112 LEU A 133 1 22
HELIX 5 AA5 LYS A 141 GLU A 143 5 3
HELIX 6 AA6 THR A 180 VAL A 184 5 5
HELIX 7 AA7 ALA A 185 ASN A 190 1 6
HELIX 8 AA8 LEU A 196 GLY A 213 1 18
HELIX 9 AA9 THR A 221 VAL A 232 1 12
HELIX 10 AB1 GLU A 237 SER A 242 1 6
HELIX 11 AB2 SER A 245 ARG A 254 1 10
HELIX 12 AB3 ASP A 259 ARG A 263 5 5
HELIX 13 AB4 THR A 265 HIS A 272 1 8
SHEET 1 AA1 5 TYR A 13 SER A 21 0
SHEET 2 AA1 5 ALA A 25 GLU A 32 -1 O LYS A 29 N GLU A 17
SHEET 3 AA1 5 GLN A 38 LYS A 45 -1 O ALA A 41 N LYS A 28
SHEET 4 AA1 5 ASP A 88 GLU A 94 -1 O LEU A 93 N ALA A 40
SHEET 5 AA1 5 LEU A 79 GLU A 84 -1 N HIS A 80 O ILE A 92
SHEET 1 AA2 2 ILE A 135 ALA A 136 0
SHEET 2 AA2 2 HIS A 166 LYS A 167 -1 O HIS A 166 N ALA A 136
SHEET 1 AA3 2 ILE A 145 LEU A 147 0
SHEET 2 AA3 2 ILE A 157 ILE A 159 -1 O LYS A 158 N MET A 146
SITE 1 AC1 1 ARG A 63
SITE 1 AC2 5 LYS A 42 LEU A 93 ASP A 161 4FT A 307
SITE 2 AC2 5 HOH A 487
SITE 1 AC3 6 GLY A 22 GLN A 23 PHE A 24 ALA A 25
SITE 2 AC3 6 HOH A 614 HOH A 620
SITE 1 AC4 3 ASP A 14 THR A 15 PHE A 174
SITE 1 AC5 7 HIS A 80 HIS A 131 SER A 132 ILE A 266
SITE 2 AC5 7 GLN A 267 HOH A 439 HOH A 535
SITE 1 AC6 5 LYS A 86 PHE A 236 LYS A 249 ARG A 253
SITE 2 AC6 5 HOH A 470
SITE 1 AC7 6 ALA A 40 GLU A 94 VAL A 96 MET A 146
SITE 2 AC7 6 CL A 302 HOH A 464
CRYST1 47.004 62.523 88.537 90.00 90.00 90.00 P 21 21 21 4
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 0.021275 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015994 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011295 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
