HEADER TRANSFERASE 03-JUL-14 4TXC
TITLE CRYSTAL STRUCTURE OF DAPK1 KINASE DOMAIN IN COMPLEX WITH A SMALL
TITLE 2 MOLECULE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DAP KINASE 1;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DAPK1, DAPK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS PROTEIN-LIGAND COMPLEX, KINASE, SMALL-MOLECULE, CATALYTIC DOMAIN,
KEYWDS 2 PROTEIN KINASE, PROTEIN BINDING, PROTEIN KINASE INHIBITORS,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.SORRELL,T.KROJER,T.S.WILBEK,T.SKOVGAARD,J.BERTHELSEN,S.DIXON-
AUTHOR 2 CLARKE,R.CHALK,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 3 K.STROMGAARD,S.KNAPP
REVDAT 6 20-DEC-23 4TXC 1 REMARK
REVDAT 5 24-JAN-18 4TXC 1 AUTHOR
REVDAT 4 11-FEB-15 4TXC 1 REMARK
REVDAT 3 14-JAN-15 4TXC 1 JRNL
REVDAT 2 19-NOV-14 4TXC 1 JRNL
REVDAT 1 23-JUL-14 4TXC 0
JRNL AUTH T.S.WILBEK,T.SKOVGAARD,F.J.SORRELL,S.KNAPP,J.BERTHELSEN,
JRNL AUTH 2 K.STRMGAARD
JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF A SMALL-MOLECULE
JRNL TITL 2 INHIBITOR OF DEATH-ASSOCIATED PROTEIN KINASE 1.
JRNL REF CHEMBIOCHEM V. 16 59 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 25382253
JRNL DOI 10.1002/CBIC.201402512
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1682)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 31654
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 1559
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.4712 - 4.3369 0.99 2897 158 0.1702 0.1933
REMARK 3 2 4.3369 - 3.4431 1.00 2791 145 0.1628 0.2025
REMARK 3 3 3.4431 - 3.0081 0.99 2742 141 0.1834 0.2045
REMARK 3 4 3.0081 - 2.7332 1.00 2759 130 0.1776 0.2344
REMARK 3 5 2.7332 - 2.5374 1.00 2712 143 0.1912 0.2450
REMARK 3 6 2.5374 - 2.3878 1.00 2717 136 0.1895 0.2314
REMARK 3 7 2.3878 - 2.2682 1.00 2717 143 0.1831 0.2273
REMARK 3 8 2.2682 - 2.1695 0.99 2677 136 0.1852 0.2148
REMARK 3 9 2.1695 - 2.0860 1.00 2688 131 0.1926 0.2303
REMARK 3 10 2.0860 - 2.0140 1.00 2689 172 0.2078 0.2528
REMARK 3 11 2.0140 - 1.9510 1.00 2706 124 0.2257 0.2528
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2311
REMARK 3 ANGLE : 1.016 3117
REMARK 3 CHIRALITY : 0.046 343
REMARK 3 PLANARITY : 0.005 399
REMARK 3 DIHEDRAL : 12.836 854
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31708
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.951
REMARK 200 RESOLUTION RANGE LOW (A) : 36.465
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: 2YAK, 3EH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 10% ETHYLENE GLYCOL, 0.1M
REMARK 280 HEPES PH 7.0, 0.2M SODIUM CHLORIDE, 293K, USING PREVIOUSLY
REMARK 280 FROZEN PROTEIN, PH 7.5, VAPOR DIFFUSION, SITTING DROP
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 24.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.06000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.06000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.64500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 17.0 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 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 3 CG1 CG2
REMARK 470 LYS A 29 CE NZ
REMARK 470 LYS A 45 CE NZ
REMARK 470 LYS A 69 CD CE NZ
REMARK 470 LYS A 86 CD CE NZ
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 LYS A 154 CG CD CE NZ
REMARK 470 LYS A 262 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 446 O HOH A 453 1.85
REMARK 500 O HOH A 574 O HOH A 655 1.86
REMARK 500 O HOH A 603 O HOH A 604 1.97
REMARK 500 O HOH A 636 O HOH A 660 2.00
REMARK 500 OE2 GLU A 84 O HOH A 631 2.04
REMARK 500 O HOH A 455 O HOH A 467 2.04
REMARK 500 NH1 ARG A 156 O HOH A 611 2.04
REMARK 500 OE1 GLU A 173 O HOH A 401 2.07
REMARK 500 O HOH A 669 O HOH A 671 2.08
REMARK 500 O HOH A 508 O HOH A 555 2.08
REMARK 500 OE1 GLU A 107 O HOH A 643 2.11
REMARK 500 O HOH A 608 O HOH A 641 2.13
REMARK 500 NH2 ARG A 63 O HOH A 548 2.15
REMARK 500 O HOH A 449 O HOH A 462 2.15
REMARK 500 O HOH A 578 O HOH A 603 2.16
REMARK 500 O HOH A 587 O HOH A 628 2.17
REMARK 500 O HOH A 607 O HOH A 611 2.17
REMARK 500 O HOH A 611 O HOH A 654 2.18
REMARK 500 NZ LYS A 158 O HOH A 543 2.18
REMARK 500 O HOH A 426 O HOH A 468 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 O HOH A 438 O HOH A 458 3845 2.04
REMARK 500 O HOH A 470 O HOH A 579 4575 2.15
REMARK 500 O HOH A 424 O HOH A 464 1455 2.16
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 3 44.97 71.45
REMARK 500 ARG A 48 -46.21 71.94
REMARK 500 ASN A 85 -159.91 -126.69
REMARK 500 ASP A 139 37.19 -146.34
REMARK 500 ASN A 151 47.61 -107.27
REMARK 500 ASP A 161 88.35 59.42
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 38G A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 307
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YAK RELATED DB: PDB
REMARK 900 2YAK CONTAINS SAME PROTEIN COMPLEXED WITH DIFFERENT LIGAND.
REMARK 900 RELATED ID: 4PF4 RELATED DB: PDB
REMARK 900 APO VERSION OF THE SAME PROTEIN
DBREF 4TXC A 1 285 UNP P53355 DAPK1_HUMAN 1 285
SEQADV 4TXC GLY A -18 UNP P53355 EXPRESSION TAG
SEQADV 4TXC SER A -17 UNP P53355 EXPRESSION TAG
SEQADV 4TXC SER A -16 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -15 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -14 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -13 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -12 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -11 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A -10 UNP P53355 EXPRESSION TAG
SEQADV 4TXC SER A -9 UNP P53355 EXPRESSION TAG
SEQADV 4TXC SER A -8 UNP P53355 EXPRESSION TAG
SEQADV 4TXC GLY A -7 UNP P53355 EXPRESSION TAG
SEQADV 4TXC LEU A -6 UNP P53355 EXPRESSION TAG
SEQADV 4TXC VAL A -5 UNP P53355 EXPRESSION TAG
SEQADV 4TXC PRO A -4 UNP P53355 EXPRESSION TAG
SEQADV 4TXC ARG A -3 UNP P53355 EXPRESSION TAG
SEQADV 4TXC GLY A -2 UNP P53355 EXPRESSION TAG
SEQADV 4TXC SER A -1 UNP P53355 EXPRESSION TAG
SEQADV 4TXC HIS A 0 UNP P53355 EXPRESSION TAG
SEQRES 1 A 304 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 304 VAL PRO ARG GLY SER HIS MET THR VAL PHE ARG GLN GLU
SEQRES 3 A 304 ASN VAL ASP ASP TYR TYR ASP THR GLY GLU GLU LEU GLY
SEQRES 4 A 304 SER GLY GLN PHE ALA VAL VAL LYS LYS CYS ARG GLU LYS
SEQRES 5 A 304 SER THR GLY LEU GLN TYR ALA ALA LYS PHE ILE LYS LYS
SEQRES 6 A 304 ARG ARG THR LYS SER SER ARG ARG GLY VAL SER ARG GLU
SEQRES 7 A 304 ASP ILE GLU ARG GLU VAL SER ILE LEU LYS GLU ILE GLN
SEQRES 8 A 304 HIS PRO ASN VAL ILE THR LEU HIS GLU VAL TYR GLU ASN
SEQRES 9 A 304 LYS THR ASP VAL ILE LEU ILE LEU GLU LEU VAL ALA GLY
SEQRES 10 A 304 GLY GLU LEU PHE ASP PHE LEU ALA GLU LYS GLU SER LEU
SEQRES 11 A 304 THR GLU GLU GLU ALA THR GLU PHE LEU LYS GLN ILE LEU
SEQRES 12 A 304 ASN GLY VAL TYR TYR LEU HIS SER LEU GLN ILE ALA HIS
SEQRES 13 A 304 PHE ASP LEU LYS PRO GLU ASN ILE MET LEU LEU ASP ARG
SEQRES 14 A 304 ASN VAL PRO LYS PRO ARG ILE LYS ILE ILE ASP PHE GLY
SEQRES 15 A 304 LEU ALA HIS LYS ILE ASP PHE GLY ASN GLU PHE LYS ASN
SEQRES 16 A 304 ILE PHE GLY THR PRO GLU PHE VAL ALA PRO GLU ILE VAL
SEQRES 17 A 304 ASN TYR GLU PRO LEU GLY LEU GLU ALA ASP MET TRP SER
SEQRES 18 A 304 ILE GLY VAL ILE THR TYR ILE LEU LEU SER GLY ALA SER
SEQRES 19 A 304 PRO PHE LEU GLY ASP THR LYS GLN GLU THR LEU ALA ASN
SEQRES 20 A 304 VAL SER ALA VAL ASN TYR GLU PHE GLU ASP GLU TYR PHE
SEQRES 21 A 304 SER ASN THR SER ALA LEU ALA LYS ASP PHE ILE ARG ARG
SEQRES 22 A 304 LEU LEU VAL LYS ASP PRO LYS LYS ARG MET THR ILE GLN
SEQRES 23 A 304 ASP SER LEU GLN HIS PRO TRP ILE LYS PRO LYS ASP THR
SEQRES 24 A 304 GLN GLN ALA LEU SER
HET 38G A 301 32
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HETNAM 38G 4-(3-{3-[(R)-{[2-(DIMETHYLAMINO)ETHYL]AMINO}(HYDROXY)
HETNAM 2 38G METHYL]PHENYL}IMIDAZO[1,2-B]PYRIDAZIN-6-YL)-2-
HETNAM 3 38G METHOXYPHENOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 38G C24 H27 N5 O3
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *275(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 GLU A 107 1 8
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 ALA A 231 1 11
HELIX 10 AB1 GLU A 237 SER A 242 1 6
HELIX 11 AB2 SER A 245 LEU A 256 1 12
HELIX 12 AB3 THR A 265 LEU A 270 1 6
SHEET 1 AA1 5 TYR A 13 SER A 21 0
SHEET 2 AA1 5 ALA A 25 GLU A 32 -1 O VAL A 27 N LEU A 19
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 15 LEU A 19 VAL A 27 ALA A 40 LYS A 42
SITE 2 AC1 15 GLU A 64 ILE A 77 LEU A 93 GLU A 94
SITE 3 AC1 15 VAL A 96 GLU A 143 ASN A 144 MET A 146
SITE 4 AC1 15 ASP A 161 PHE A 162 HOH A 627
SITE 1 AC2 3 PHE A 43 LYS A 45 ASP A 88
SITE 1 AC3 6 PRO A 193 LEU A 194 GLY A 195 GLU A 197
SITE 2 AC3 6 PRO A 260 HOH A 404
SITE 1 AC4 6 ASP A 14 GLY A 16 ARG A 31 GLN A 38
SITE 2 AC4 6 GLU A 173 HOH A 416
SITE 1 AC5 3 TYR A 234 PHE A 236 ARG A 253
SITE 1 AC6 4 PHE A 102 ILE A 209 GLY A 213 EDO A 307
SITE 1 AC7 4 LEU A 211 SER A 212 GLY A 213 EDO A 306
CRYST1 49.900 77.290 110.120 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 0.020040 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009081 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
