HEADER TRANSFERASE 28-MAR-09 3GU4
TITLE CRYSTAL STRUCTURE OF DAPKQ23V-AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEIN KINASE DOMAIN;
COMPND 5 SYNONYM: DAP KINASE 1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DAPK, DAPK1, DEATH-ASSOCIATED PROTEIN KINASE 1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PASK-IBA3
KEYWDS GLYCINE-RICH LOOP MUTANT, KINASE-AMPPNP COMPLEX, ALTERNATIVE
KEYWDS 2 SPLICING, ANK REPEAT, APOPTOSIS, ATP-BINDING, CALMODULIN-BINDING,
KEYWDS 3 CYTOPLASM, KINASE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM,
KEYWDS 4 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.K.MCNAMARA,J.S.SCHAVOCKY,D.M.WATTERSON,J.S.BRUNZELLE
REVDAT 3 06-SEP-23 3GU4 1 REMARK
REVDAT 2 13-OCT-21 3GU4 1 REMARK SEQADV
REVDAT 1 09-MAR-10 3GU4 0
JRNL AUTH L.K.MCNAMARA,J.S.SCHAVOCKY,D.M.WATTERSON,J.S.BRUNZELLE
JRNL TITL ENZYMATIC ACTIVITY AND CRYSTALLGORAPHIC ANALYSES OF A
JRNL TITL 2 GLYCINE-RICH LOOP MUTANT OF DAPK
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 54069
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2887
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3863
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 220
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2272
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 338
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.25000
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): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.891
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2573 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3517 ; 1.307 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 5.788 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;37.431 ;24.622
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 472 ;13.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.870 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 388 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1971 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1269 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1809 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 275 ; 0.113 ; 0.200
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): 96 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 58 ; 0.128 ; 0.200
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): 1573 ; 0.754 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2538 ; 1.276 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1106 ; 1.776 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 979 ; 2.728 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3GU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : SINGLE DIAMOND CRYSAL
REMARK 200 OPTICS : BE LENSES
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 : 57021
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JKS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 1.8 M AMMONIUM SULFATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, 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 23.44150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.20600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.21550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.20600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.44150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.21550
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 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 MET A 1
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 LYS A 295
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 GLU A 109 CB - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 SER A 110 N - CA - CB ANGL. DEV. = 13.6 DEGREES
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 VAL A 23 97.45 -62.85
REMARK 500 SER A 110 91.53 -178.99
REMARK 500 ASP A 139 41.14 -144.28
REMARK 500 ASP A 161 79.48 63.74
REMARK 500 ASN A 176 9.77 93.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 175 ASN A 176 31.78
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 ANP A 296
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F5U RELATED DB: PDB
REMARK 900 DAPK-AMPPNP-MG2+
REMARK 900 RELATED ID: 3F5G RELATED DB: PDB
REMARK 900 DAPK-ADP-MG2+
REMARK 900 RELATED ID: 3EHA RELATED DB: PDB
REMARK 900 DAPK-AMPPNP
REMARK 900 RELATED ID: 3EH9 RELATED DB: PDB
REMARK 900 DAPK-ADP
REMARK 900 RELATED ID: 3DGK RELATED DB: PDB
REMARK 900 DAPKQ23K
REMARK 900 RELATED ID: 3DFC RELATED DB: PDB
REMARK 900 DAPKQ23K-AMPPNP
REMARK 900 RELATED ID: 3GU5 RELATED DB: PDB
REMARK 900 DAPKQ23V-AMPPNP-MG2+
REMARK 900 RELATED ID: 3GU6 RELATED DB: PDB
REMARK 900 DAPKQ23V-ADP
REMARK 900 RELATED ID: 3GU7 RELATED DB: PDB
REMARK 900 DAPKQ23V-ADP-MG2+
REMARK 900 RELATED ID: 3GU8 RELATED DB: PDB
REMARK 900 DAPKL93G-N6CYCLOPENTYLADENOSINE
REMARK 900 RELATED ID: 3GUB RELATED DB: PDB
DBREF 3GU4 A 1 285 UNP P53355 DAPK1_HUMAN 1 285
SEQADV 3GU4 VAL A 23 UNP P53355 GLN 23 ENGINEERED MUTATION
SEQADV 3GU4 SER A 286 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 ALA A 287 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 TRP A 288 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 SER A 289 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 HIS A 290 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 PRO A 291 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 GLN A 292 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 PHE A 293 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 GLU A 294 UNP P53355 EXPRESSION TAG
SEQADV 3GU4 LYS A 295 UNP P53355 EXPRESSION TAG
SEQRES 1 A 295 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 A 295 ASP THR GLY GLU GLU LEU GLY SER GLY VAL PHE ALA VAL
SEQRES 3 A 295 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 A 295 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 A 295 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 A 295 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 A 295 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 A 295 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 A 295 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 A 295 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 A 295 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 A 295 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 A 295 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 A 295 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 A 295 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 A 295 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 A 295 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 A 295 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 A 295 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 A 295 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 A 295 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 A 295 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER SER
SEQRES 23 A 295 ALA TRP SER HIS PRO GLN PHE GLU LYS
HET ANP A 296 31
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 HOH *338(H2 O)
HELIX 1 1 ASN A 8 ASP A 11 5 4
HELIX 2 2 SER A 57 ILE A 71 1 15
HELIX 3 3 GLU A 100 GLU A 109 1 10
HELIX 4 4 THR A 112 LEU A 133 1 22
HELIX 5 5 LYS A 141 GLU A 143 5 3
HELIX 6 6 THR A 180 VAL A 184 5 5
HELIX 7 7 ALA A 185 ASN A 190 1 6
HELIX 8 8 LEU A 196 GLY A 213 1 18
HELIX 9 9 THR A 221 ALA A 231 1 11
HELIX 10 10 GLU A 237 SER A 242 1 6
HELIX 11 11 SER A 245 ARG A 254 1 10
HELIX 12 12 ASP A 259 ARG A 263 5 5
HELIX 13 13 THR A 265 HIS A 272 1 8
SHEET 1 A 5 TYR A 13 GLY A 22 0
SHEET 2 A 5 ALA A 25 GLU A 32 -1 O LYS A 29 N GLU A 17
SHEET 3 A 5 GLN A 38 LYS A 45 -1 O PHE A 43 N VAL A 26
SHEET 4 A 5 ASP A 88 GLU A 94 -1 O VAL A 89 N ILE A 44
SHEET 5 A 5 LEU A 79 GLU A 84 -1 N HIS A 80 O ILE A 92
SHEET 1 B 2 ILE A 135 ALA A 136 0
SHEET 2 B 2 HIS A 166 LYS A 167 -1 O HIS A 166 N ALA A 136
SHEET 1 C 2 ILE A 145 LEU A 147 0
SHEET 2 C 2 ILE A 157 ILE A 159 -1 O LYS A 158 N MET A 146
SITE 1 AC1 23 LEU A 19 GLY A 20 SER A 21 GLY A 22
SITE 2 AC1 23 VAL A 23 ALA A 25 VAL A 27 ALA A 40
SITE 3 AC1 23 LYS A 42 ILE A 77 GLU A 94 VAL A 96
SITE 4 AC1 23 GLU A 100 ASP A 139 GLU A 143 MET A 146
SITE 5 AC1 23 ILE A 160 ASP A 161 HOH A 340 HOH A 349
SITE 6 AC1 23 HOH A 466 HOH A 506 HOH A 622
CRYST1 46.883 62.431 88.412 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 0.021330 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011311 0.00000
(ATOM LINES ARE NOT SHOWN.)
END